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(1'S)-7-(1-aminoethyl)-2-(2-methoxyphenyl)pyrazolo[1,5-a] pyrimidine hydrochloride
-
(1'S)-7-(1-aminoethyl)-2-(3-trifluoromethylphenyl)pyrazolo-[1,5-a]pyrimidine hydrochloride
-
(1'S)-7-(1-aminoethyl)-2-benzyl-3-phenylpyrazolo[1,5-a]pyrimidine hydrochloride
-
(1'S)-7-(1-aminoethyl)-2-phenylpyrazolo[1,5-a]pyrimidine hydrochloride
-
(1'S)-7-(1-aminoethyl)pyrazolo[1,5-a]pyrimidine-3-(N-methylcarboxamide) hydrochloride
-
(1'S)-7-(1-aminoethyl)pyrazolo[1,5-a]pyrimidine-3-carboxylate hydrochloride
-
(11R,12R)-14,14-difluoro-34-(methylsulfanyl)-N-(prop-2-yn-1-yl)-11,12,13,14,15,16-hexahydro[11,21:22,31-terphenyl]-12-carboxamide
-
(1R,2R)-5,5-dichloro-2-[4-[4-(methanesulfonyl)phenyl]-1-(2,2,2-trifluoroethyl)-1H-pyrrol-3-yl]-N-(prop-2-yn-1-yl)cyclohexane-1-carboxamide
-
(1R,2R)-5,5-difluoro-2-[4-[4-(methanesulfonyl)phenyl]-1-(2,2,2-trifluoroethyl)-1H-pyrrol-3-yl]-N-(prop-2-yn-1-yl)cyclohexane-1-carboxamide
-
(1R,2R)-N-(1-cyanocyclopropyl)-2-(6-methoxy-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carbonyl)cyclohexane-1-carboxamide
-
(2E,4E)-5-(1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl)-3-methylpenta-2,4-dienoic acid
-
(2R)-N-cyano-4-methyl-2-[4'-(piperazin-1-yl)[1,1'-biphenyl]-3-yl]pentanamide
-
(4-[[(2S)-2-([1-[([1,1'-biphenyl]-3-yl)amino]cyclohexane-1-carbonyl]amino)butyl]amino]phenoxy)acetic acid
-
1,4-anhydro-3,5,6-trideoxy-3-[(1-[4-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]benzamido]cyclohexane-1-carbonyl)amino]-L-erythro-hex-2-ulose
-
1,5-(N-benzyloxycarbonylleucyl)carbohydrazide
-
1,6-dimethyl-1,2-dihydrophenanthro[1,2-b]furan-10,11-dione
-
1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
-
1-(phenoxymethyl)cyclobutyl (3aR,6aS)-6-oxohexahydro-1H-furo[3,2-c]pyrazole-1-carboxylate
-
1-(phenoxymethyl)cyclobutyl (3aS,6aR)-3-oxohexahydro-4H-furo[3,2-b]pyrrole-4-carboxylate
-
1-ethyl-2-[(4-methylpiperazin-1-yl)methyl]-6-[3-(trifluoromethyl)phenyl]-2,3-dihydro-1H-indole-4-carbonitrile
-
1-[(1H-imidazol-4-yl)methyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole
-
13-methyl-2H,10H-[1,3]benzodioxolo[5,6-c][1,3]dioxolo[4,5-i]phenanthridin-13-ium
-
2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-6-[5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl]-2,3-dihydro-4H-1-benzopyran-4-one
-
2-amino-4-bromo-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]benzamide
-
2-cyano-4-(cyclohexylamino)-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-(cyclohexylmethoxy)-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[(cyclohexylmethyl)(methyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[(cyclohexylmethyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-N-(2-phenylethyl)-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-4-[[(4,4-difluorocyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[[(4,4-dimethylcyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-N-(1-methyl-4-phenylpiperidin-4-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-(2-phenylethyl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-(4,5-dimethoxybiphenyl-2-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-[(1-methyl-4-phenylpiperidin-4-yl)methyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-[(1R)-2-pyridin-2-yl-1-(pyrrolidin-1-ylmethyl)ethyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-[5-[(1-methylpiperidin-4-yl)oxy]biphenyl-2-yl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methylene]bis(6-hydroxybenzoic acid)
-
3-[(6-deoxy-L-mannopyranosyl)oxy]-5-hydroxy-2-(4-methoxyphenyl)-8-(3-methylbut-2-en-1-yl)-4-oxo-4H-1-benzopyran-7-yl D-glucopyranoside
-
4'-[(1S)-1-([(2S)-1-[(1-cyanocyclopropyl)amino]-4-fluoro-4-methyl-1-oxopentan-2-yl]amino)-2,2,2-trifluoroethyl][1,1'-biphenyl]-4-sulfonic acid
-
4'-[(1S)-1-([(2S)-1-[(cyanomethyl)amino]-4-methyl-1-oxopentan-2-yl]amino)-2,2,2-trifluoroethyl][1,1'-biphenyl]-4-sulfonic acid
-
4-(cyclohexylamino)-6-(piperazin-1-yl)-1,3,5-triazine-2-carbonitrile
-
4-cycloheptyl-6-[3-(piperidin-1-yl)propyl]pyrimidine-2-carbonitrile
-
4-dihydrotanshinone
potent exosite inhibitor of cathepsin K
4-fluoro-N-prop-2-yn-1-yl-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
-
4-[2-(4-methylpiperazin-1-yl)-4,5-dihydro-1,3-thiazol-4-yl]-N-(1-[[(3S,4R)-2-oxo-4-phenoxyazetidin-3-yl]carbamoyl]cyclohexyl)benzamide
-
5-bromo-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
-
6,8-dihydroxy-3-(3,4,5-trihydroxyphenyl)-2,3-dihydro-1,4-benzodioxin-2-yl 3,4,5-trihydroxybenzoate
-
6-[4-[3-(diethylamino)propoxy]-3-(trifluoromethyl)phenyl]-1-ethyl-2,3-dihydro-1H-indole-4-carbonitrile
-
7-(2,2-dimethylpropyl)-6-[(1,3-dioxo-2,8-diazaspiro[4.5]decan-2-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
benzyl [(5S,13S)-11,15-dimethyl-5-(2-methylpropyl)-3,6,9,12-tetraoxo-1-phenyl-2-oxa-4,7,11-triazahexadecan-13-yl]carbamate
-
Boc-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
-
dibenzyl [(2-oxopropane-1,3-diyl)bis[azanediyl[(2S)-4-methyl-1-oxopentane-1,2-diyl]]]biscarbamate
-
ethyl (4S)-4-[(4-fluoro-N-[2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucyl)amino]-3-oxopiperidine-1-carboxylate
-
kushennol F
shows inhibitory effects on the bone resorption process related to cathepsin K
methyl (3S)-3-[(4-fluoro-N-[2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucyl)amino]-4-oxopyrrolidine-1-carboxylate
-
methyl 5-hydroxy-7,12-dioxo-7,12-dihydrodinaphtho[1,2-b:2',3'-d]furan-6-carboxylate
-
methyl methanethiolsulfonate
-
mPEG-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
conjugate
N'-cyano-N,N',4-trimethyl-2-(4'-(methylsulfonyl)-[1,1'-biphenyl]-3-yl)pentanehydrazide
racemic
N'-cyano-N,N',4-trimethyl-2-(4'-(methylsulfonyl)-[1,1'-biphenyl]-4-yl)pentanehydrazide
racemic
N'-cyano-N,N',4-trimethyl-2-([11,21:24,31-terphenyl]-14-yl)pentanehydrazide
-
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(1-hydroxycyclopropyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(2-hydroxypropan-2-yl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1R)-2,2-difluoro-1-hydroxyethyl][1,1'-biphenyl]-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
-
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1S)-2,2-difluoro-1-hydroxyethyl][1,1'-biphenyl]-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
-
N-(1-ethynylcyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-(3-bromoprop-2-yn-1-yl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-(3-[[(3R)-3-([1,1'-biphenyl]-3-yl)-5-methylhex-1-en-2-yl]amino]-2-oxopropyl)-4-phenoxybenzene-1-sulfonamide
-
N-(4-benzyl-1-methylpiperidin-4-yl)-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-(cyanomethyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-(cyanomethyl)-N2-[(1S)-2,2,2-trifluoro-1-[4'-(piperazin-1-yl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)oxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-benzyl-2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-but-3-yn-2-yl-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-cyano-N2-[4-[4-(piperazin-1-yl)phenyl]thiophen-3-yl]-L-leucinamide
-
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylpropyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-[(1S)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-[(1S)-1-cyclohexyl-3-[(2Z)-2-[(4R)-3,4-dimethyl-1,3-thiazolidin-2-ylidene]hydrazinyl]-2,3-dioxopropyl]cycloheptanecarboxamide
-
N-[(2S)-1-[4-(benzyloxy)anilino]butan-2-yl]-N2-(morpholine-4-carbonyl)-L-leucinamide
-
N-[(2S)-1-[4-(morpholin-4-yl)anilino]butan-2-yl]-N2-[(1S)-2,2,2-trifluoro-1-(4-hydroxyphenyl)ethyl]-L-leucinamide
-
N-[(2S)-4-methyl-1-([2-[4-(2-methylpropoxy)anilino]ethyl]amino)-1-oxopentan-2-yl]-2,3-dihydro-1-benzofuran-2-carboxamide
-
N-[(2S)-4-methyl-1-oxo-1-[(3aS,6aR)-3-oxohexahydro-4H-furo[3,2-b]pyrrol-4-yl]pentan-2-yl]-4-(4-methylpiperazin-1-yl)benzamide
-
N-[(2S)-4-methyl-1-oxo-1-[(3aS,7aR)-3-oxohexahydrofuro[3,2-b]pyridin-4(2H)-yl]pentan-2-yl]-4-(4-methylpiperazin-1-yl)benzamide
-
N-[(2S)-4-methyl-1-oxo-1-[[(4R)-3-oxo-1-(pyridine-2-sulfonyl)azepan-4-yl]amino]pentan-2-yl]-2,3-dihydro-1-benzofuran-2-carboxamide
-
N-[(2S)-4-methyl-1-[(3aS,6S,6aR)-6-methyl-3-oxohexahydro-4H-furo[3,2-b]pyrrol-4-yl]-1-oxopentan-2-yl]-4-[2-(1-methylpiperidin-4-yl)-1,3-thiazol-4-yl]benzamide
-
N-[(2S)-4-methyl-1-[[(4S,7R)-7-methyl-3-oxo-1-(pyridine-2-sulfonyl)azepan-4-yl]amino]-1-oxopentan-2-yl]-2,3-dihydro-1-benzofuran-2-carboxamide
-
N-[(4S)-3-oxo-1-(pyridine-2-sulfonyl)azepan-4-yl]-N2-[2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-(4-propylpiperazin-1-yl)benzamide
-
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]benzamide
-
N2-[(1S)-1-[4'-(1-carbamoylcyclopropyl)[1,1'-biphenyl]-4-yl]-2,2,2-trifluoroethyl]-N-(1-cyanocyclopropyl)-4-fluoro-L-leucinamide
-
N2-[(1S)-1-[4'-(2-amino-2-oxoethyl)[1,1'-biphenyl]-4-yl]-2,2,2-trifluoroethyl]-N-(1-cyanocyclopropyl)-4-fluoro-L-leucinamide
-
N2-[(benzyloxy)carbonyl]-N-[2-oxo-3-[(4-phenoxybenzene-1-sulfonyl)amino]propyl]-L-leucinamide
-
NSC13345
i.e. 2-[(2-carbamoylsulfanylacetyl)-amino]benzoic acid, good selectivity for cathepsin K over related enzymes
Phe-Phe-fluoromethylketone
-
PHPMA-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
conjugate
PHPMA-GG-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
conjugate
S-[2-[2-(dihydroxymethyl)anilino]-2-oxoethyl] carbamothioate
-
SM934-testosterone
inhibits proliferation and metastasis ability of breast cancer cells via inhibiting the expression of cathepsin K followed by the inhibition of Bcl-xL
sodium (2S,3S)-3-[[(2S)-4-methyl-1-(2-methylpropoxy)pentan-2-yl]amino]oxirane-2-carboxylate
-
sophoraflavanone G
shows inhibitory effects on the bone resorption process related to cathepsin K
STPHPMA-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
conjugate
((S)-1-[1-[4(R,S)-((S)-2-benzyloxycarbonylamino-4-methylpentanoylamino)-3-oxoazepan-1-yl]methanoyl]-3-methylbutl)carbamic acid benzyl ester
((S)-1-[[(3R,S)-((S)-2-benzyloxycarbonylamino-4-methylpentanoylamino)-3-oxopiperidin-1-yl]methanoyl]-3-methylbutyl)carbamic acid benzyl ester
-
-
((S)-1-[[(3R,S)-((S)-2-benzyloxycarbonylamino-4-methylpentanoylamino)-4-oxopyrrolidin-1-yl]methanoyl]-3-methylbutyl)carbamic acid benzyl ester
-
-
((S)-1-[[(3R,S)-((S)-2-benzyloxycarbonylmethylamino-4-methylpentanoylamino)-4-oxopyrrolidin-1-yl]methanoyl]-3-methylbutyl)carbamic acid benzyl ester
-
-
(1R)-1-benzyl-2-methylpropyl [(1S)-1-formylpentyl]carbamate
-
-
(1R)-1-benzyl-2-methylpropyl [(1S)-1-[(E)-[(morpholin-4-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
(1R)-N-(cyanomethyl)-5,5-difluoro-2-[4'-(methylsulfanyl)biphenyl-2-yl]cyclohexanecarboxamide
-
-
(1R,2R)-2-[1-benzyl-5-[4-(methylsulfanyl)phenyl]-1H-1,2,3-triazol-4-yl]-N-(cyanomethyl)-5,5-difluorocyclohexanecarboxamide
-
-
(1R,2R)-N-(cyanomethyl)-2-(4-[4-[(difluoromethyl)sulfanyl]phenyl]pyridin-3-yl)-5,5-difluorocyclohexanecarboxamide
-
-
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[1-methyl-4-[4-(methylsulfanyl)phenyl]-1H-pyrazol-3-yl]cyclohexanecarboxamide
-
-
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[2-methyl-4-[4-(methylsulfanyl)phenyl]-1,3-thiazol-5-yl]cyclohexanecarboxamide
-
-
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[2-[4-(methylsulfanyl)phenyl]pyridin-3-yl]cyclohexanecarboxamide
-
-
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[3-[4-(methylsulfanyl)phenyl]-1-oxidopyridin-4-yl]cyclohexanecarboxamide
-
-
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[3-[4-(methylsulfanyl)phenyl]-2-oxo-1,2-dihydropyridin-4-yl]cyclohexanecarboxamide
-
-
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[3-[4-(methylsulfanyl)phenyl]pyridin-4-yl]cyclohexanecarboxamide
-
-
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[4'-(methylsulfanyl)biphenyl-2-yl]cyclohexanecarboxamide
-
-
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[5-[4-(methylsulfanyl)phenyl]-2-oxo-1,2-dihydropyridin-4-yl]cyclohexanecarboxamide
-
-
(1R,2S)-N-(cyanomethyl)-2-[2-[4-(methylsulfanyl)phenyl]ethyl]cyclohexanecarboxamide
-
-
(1S)-1-methyl-2-phenylethyl [(1S)-1-formylpentyl]carbamate
-
-
(1S)-1-methyl-2-phenylethyl [(1S)-1-[(E)-[(morpholin-4-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
(1S)-1-[(5,6-dichloro-1H-benzimidazol-1-yl)methyl]-2,2-dimethylpropyl [(1S)-1-methyl-2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamate
-
-
(1S)-1-[(5,6-dichloro-1H-benzimidazol-1-yl)methyl]-2,2-dimethylpropyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
-
-
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-([[(6-fluoropyridin-2-yl)carbonyl]amino]acetyl)pentyl]carbamate
-
-
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-methyl-2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamate
-
-
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-[oxo(1H-pyrazol-5-ylamino)acetyl]pentyl]carbamate
-
-
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-[[(morpholin-4-ylcarbonyl)amino]acetyl]pentyl]carbamate
-
-
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
-
-
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamate
-
-
(1S)-2,2-dimethyl-1-([4-[4-(trifluoromethyl)phenyl]-1H-imidazol-1-yl]methyl)propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
-
-
(1S)-2,2-dimethyl-1-([4-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
-
-
(1S)-2,2-dimethyl-1-[(3-pyridin-3-yl-1H-pyrazol-1-yl)methyl]propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
-
-
(1S)-2,2-dimethyl-1-[(3-pyridin-4-yl-1H-pyrazol-1-yl)methyl]propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
-
-
(1S)-2,2-dimethyl-1-[[3-(trifluoromethyl)-1H-pyrazol-1-yl]methyl]propyl [(1S)-1-methyl-2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamate
-
-
(1S)-2,2-dimethyl-1-[[3-(trifluoromethyl)-1H-pyrazol-1-yl]methyl]propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
-
-
(2R)-2-[3'-[2-(4-tert-butylpiperazin-1-yl)-1,3-thiazol-4-yl]biphenyl-3-yl]-N-(cyanomethyl)-4-methylpentanamide
-
-
(2R)-3,3-dimethyl-1-(5-phenyl-1,3,4-oxadiazol-2-yl)butan-2-yl [(3S)-1,2-dioxo-1-[[(1S)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(2R)-3,3-dimethyl-1-[2-oxo-3-[4-(trifluoromethyl)phenyl]imidazolidin-1-yl]butan-2-yl [(3S)-1,2-dioxo-1-(1H-pyrazol-5-ylamino)heptan-3-yl]carbamate
-
-
(2R)-3,3-dimethyl-1-[3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]butan-2-yl [(3S)-1,2-dioxo-1-(1H-pyrazol-5-ylamino)heptan-3-yl]carbamate
-
-
(2R)-3,3-dimethyl-1-[4-[4-(trifluoromethyl)phenyl]-1H-imidazol-1-yl]butan-2-yl [(3S)-1,2-dioxo-1-(1,3-thiazol-2-ylamino)heptan-3-yl]carbamate
-
-
(2R)-3,3-dimethyl-1-[4-[4-(trifluoromethyl)phenyl]-1H-imidazol-1-yl]butan-2-yl [(3S)-1,2-dioxo-1-(1H-pyrazol-5-ylamino)heptan-3-yl]carbamate
-
-
(2R)-3,3-dimethyl-1-[4-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]butan-2-yl [(3S)-1,2-dioxo-1-(1H-pyrazol-5-ylamino)heptan-3-yl]carbamate
-
-
(2R)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl)-2-((R)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2R)-N-(cyanomethyl)-2-[3'-(2-[[3-(dimethylamino)pyrrolidin-1-yl]methyl]-1,3-thiazol-4-yl)biphenyl-3-yl]-4-methylpentanamide
-
-
(2R)-N-(cyanomethyl)-4-methyl-2-[3'-[2-(piperazin-1-ylmethyl)-1,3-thiazol-4-yl]biphenyl-3-yl]pentanamide
-
-
(2R)-N-(cyanomethyl)-4-methyl-2-[4'-(1-piperazinyl)-[1,1'-biphenyl]-3-yl]pentanamide
-
IC 50: 3 nM, reversible inhibition
(2R)-N-(cyanomethyl)-4-methyl-2-[4'-(4-methylpiperazin-1-yl)biphenyl-3-yl]pentanamide
-
-
(2S)-1-[5-(4-fluorophenyl)-1,3,4-oxadiazol-2-yl]-3,3-dimethylbutan-2-yl [(3S)-1,2-dioxo-1-[(pyridin-3-ylmethyl)amino]heptan-3-yl]carbamate
-
-
(2S)-1-[5-(4-fluorophenyl)-1,3,4-oxadiazol-2-yl]-3,3-dimethylbutan-2-yl [(3S)-1,2-dioxo-1-[[(1S)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(2S)-2-(biphenyl-2-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methylpentanamide
-
-
(2S)-2-(biphenyl-3-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methylpentanamide
-
-
(2S)-2-(biphenyl-4-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methylpentanamide
-
-
(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
-
-
(2S)-3,3-dimethyl-1-(5-phenyl-1,3,4-oxadiazol-2-yl)butan-2-yl [(3S)-1,2-dioxo-1-[[(1S)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(2S)-3,3-dimethyl-1-[5-[4-(trifluoromethyl)phenyl]-1,3,4-oxadiazol-2-yl]butan-2-yl [(3S)-1,2-dioxo-1-[(2-oxo-1,3-oxazolidin-3-yl)amino]heptan-3-yl]carbamate
-
-
(2S)-3-methyl-1-(5-phenyl-1,3,4-oxadiazol-2-yl)butan-2-yl [(3S)-1,2-dioxo-1-[[(1S)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(2S)-4-fluoro-4-methyl-N-(1-(2-(methylsulfonyl)phenyl)-3-oxopiperidin-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-4-fluoro-4-methyl-N-(1-(methylsulfonyl)-3-oxoazepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-4-fluoro-4-methyl-N-(1-(methylsulfonyl)-4-oxopyrrolidin-3-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)piperidin-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-phenylpiperidin-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-4-fluoro-4-methyl-N-(3-oxoazepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-4-fluoro-4-methyl-N-(4-oxo-1-(pyridin-2-ylsulfonyl)pyrrolidin-3-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-4-fluoro-4-methyl-N-(4-oxopyrrolidin-3-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-N-(1-(benzylsulfonyl)-3-oxoazepan-4-yl)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-N-(1-acetyl-4-oxopyrrolidin-3-yl)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-N-(1-benzoyl-4-oxopyrrolidin-3-yl)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methyl-2-(3-phenoxyphenoxy)pentanamide
-
-
(2S)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methyl-2-(4-phenoxyphenoxy)pentanamide
-
-
(2S)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methyl-2-phenoxypentanamide
-
-
(3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetic acid
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
(3S)-1-(1H-indol-6-ylcarbonyl)-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-(2,2-dimethylpropoxy)-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-(benzylcarbamoyl)-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-(benzylsulfonyl)-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-(biphenyl-4-ylcarbonyl)-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-(dicyclopentylmethoxy)-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-(heptan-4-yloxy)-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-([(2R)-1-[5-(4-fluorophenyl)-1,3,4-oxadiazol-2-yl]-3,3-dimethylbutan-2-yl]oxy)-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(3S)-2-oxopiperidin-3-yl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-([(3S)-1-[(3,5-dimethyl-1,2-oxazol-4-yl)carbonyl]-4,4-dimethylpyrrolidin-3-yl]oxy)-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-benzyl-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-tert-butoxy-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[(thiophen-2-ylmethyl)amino]heptan-3-yl]carbamate
-
-
(3S)-1-tert-butoxy-4,4-dimethylpyrrolidin-3-yl [(3S)-1-(ethylamino)-1,2-dioxoheptan-3-yl]carbamate
-
-
(3S)-1-[(1-benzylcyclobutyl)methoxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-[(2,4-dimethylpentan-3-yl)oxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-[(3,3-dimethylbutan-2-yl)oxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-[[(2R)-3,3-dimethyl-1-[5-[4-(trifluoromethyl)phenyl]-1,3,4-oxadiazol-2-yl]butan-2-yl]oxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-(1H-pyrazol-5-ylamino)heptan-3-yl]carbamate
-
-
(3S)-1-[[(2R)-3,3-dimethyl-1-[5-[4-(trifluoromethyl)phenyl]-1,3,4-oxadiazol-2-yl]butan-2-yl]oxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1S)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-[[(3R)-2,2-dimethyl-6-phenylhexan-3-yl]oxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-[[(3R)-4,4-dimethyl-1-phenylpentan-3-yl]oxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-[[(3S)-1-(1-benzothiophen-2-ylcarbonyl)-4,4-dimethylpyrrolidin-3-yl]oxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-[[(3S)-1-benzoyl-4,4-dimethylpyrrolidin-3-yl]oxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-[[(3S)-4,4-dimethyl-1-phenylpentan-3-yl]oxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-1-[[1-(4-fluorobenzyl)cyclobutyl]methoxy]-4,4-dimethylpyrrolidin-3-yl [(3S)-1,2-dioxo-1-(1H-pyrazol-5-ylamino)heptan-3-yl]carbamate
-
-
(3S)-2-oxo-N-[(1R)-1-phenylethyl]-3-[([[1-(2-phenylethyl)cyclobutyl]oxy]acetyl)amino]heptanamide
-
-
(3S)-2-oxo-N-[(1R)-1-phenylethyl]-3-[([[1-(3-phenylpropyl)cyclobutyl]oxy]acetyl)amino]heptanamide
-
-
(3S)-3-([[(2-methyl-1-phenylpropan-2-yl)oxy]acetyl]amino)-2-oxo-N-[(1R)-1-phenylethyl]heptanamide
-
-
(3S)-4,4-dimethyl-1-(1,2-oxazol-5-ylcarbonyl)pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-(4-phenylbutanoyl)pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-(naphthalen-2-ylcarbonyl)pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-(pentan-3-yloxy)pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-(phenylacetyl)pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-(phenylcarbamoyl)pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-(phenylsulfonyl)pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-(pyridin-3-ylcarbonyl)pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-[(2,2,4,4-tetramethylpentan-3-yl)oxy]pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-[(2-phenylethyl)carbamoyl]pyrrolidin-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
(3S)-4,4-dimethyl-1-[4-(trifluoromethyl)benzoyl]pyrrolidin-3-yl [(3S)-1,2-dioxo-1-(1H-pyrazol-3-ylamino)heptan-3-yl]carbamate
-
-
(S)-N-(1-cyanocyclopropyl)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(S,S)-piperidine-4-carboxylic acid [1-[1-(benzoxazole-2-carbonyl)-3-phenyl-propylcarbamoyl]-3-methyl-butyl]-amide
-
-
1,3-bis(CBZ-Leu-NH)-2-propanone
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([2-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-3-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-4-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(thiophen-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[methyl(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(methylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(phenylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-([[4-([[(dimethylamino)methyl]sulfonyl]amino)phenyl]carbonyl]amino)-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([2-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-fluoro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([4-[(ethylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2,4-dimethyl-1,3-thiazol-5-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-(methylsulfamoyl)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-([[4-(1-methylethyl)-1,3-thiazol-2-yl]sulfonyl]amino)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-sulfamoylphenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methyl-1H-imidazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methylethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2,2,2-trifluoroethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2-methylphenyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methylpyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(5-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[4-methyl-N-(thiophen-3-ylcarbonyl)-L-leucyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(benzylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(butylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(cyclopropylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-chloropyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(3-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(4-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(cyclohexylmethyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1-(3-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
-
-
1-(4-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
-
-
1-(4-cyanophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
-
-
1-(4-cyclohexylphenoxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
-
-
1-(4-ethylphenoxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
-
-
1-(biphenyl-2-ylamino)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
-
-
1-(biphenyl-3-ylamino)-N-[(1R)-2-[(4-methoxyphenyl)amino]-1-methylethyl]cyclohexanecarboxamide
-
-
1-(biphenyl-3-ylamino)-N-[(1S)-1-[[(4-methoxyphenyl)amino]methyl]butyl]cyclohexanecarboxamide
-
-
1-(biphenyl-3-ylamino)-N-[(1S)-1-[[(4-methoxyphenyl)amino]methyl]pentyl]cyclohexanecarboxamide
-
-
1-(biphenyl-3-ylamino)-N-[(1S)-1-[[(4-methoxyphenyl)amino]methyl]propyl]cyclohexanecarboxamide
-
-
1-(biphenyl-3-ylamino)-N-[(1S)-2-[(4-methoxyphenyl)amino]-1-methylethyl]cyclohexanecarboxamide
-
-
1-(biphenyl-3-ylamino)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
-
-
1-(biphenyl-3-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
-
-
1-(biphenyl-4-ylamino)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
-
-
1-(biphenyl-4-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
-
-
1-(N-benzyloxycarbonyl-leucyl)-5-(N-Boc-phenylalanylleucyl)carbohydrazide
-
cathepsin K inhibitor
1-benzylcyclopentyl [(1S)-1-formylpentyl]carbamate
-
-
1-benzylcyclopentyl [(1S)-1-[(E)-[(2,3-dihydro-1H-indol-1-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
1-benzylcyclopentyl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
1-cyano-3-azetidinyl cyclohexylmethyl ether
-
IC 50: 20 nM
1-Isopropyl-2-methylpropyl (1S)-1-cyclohexylmethyl-2,3-dioxo-3-[(thien-2-ylmethyl)-amino]propylcarbamate
-
IC50: 14 nM
1-Isopropyl-2-methylpropyl (1S)-1-isoprpyl-2,3-dioxo-3-[(thien-2-ylmethyl)-amino]propylcarbamate
-
IC50: 47 nM
1-Isopropyl-2-methylpropyl (1S)-1-methyl-2,3-dioxo-3-[(thien-2-ylmethyl)-amino]propylcarbamate
-
IC50: 360 nM
1-Isopropyl-2-methylpropyl (1S)-1-[(isoxazol-3-ylamino)(oxo)acetyl]pentylcarbamate
-
IC50: 5.1 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(1,3,4-thiadiazol-2-ylamino)acetyl]pentylcarbamate
-
IC50: 83 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(1,3-thiazol-2-ylamino)acetyl]pentylcarbamate
-
IC50: 40 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(1H-pyrazol-5-ylamino)acetyl]pentylcarbamate
-
IC50: 0.77 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(isoquinolin-2-ylamino)acetyl]pentylcarbamate
-
IC50: 4.8 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(pyrazin-2-ylamino)acetyl]pentylcarbamate
-
IC50: 52 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(pyridin-2-ylamino)acetyl]pentylcarbamate
-
IC50: 32 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(pyridin-3-ylamino)acetyl]pentylcarbamate
-
IC50: 95 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(quinolin-2-ylamino)acetyl]pentylcarbamate
-
IC50: 250 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(1-phenyl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
-
IC50: 15 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(1-pyridin-2-yl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
-
IC50: 62 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(1-pyridin-4-yl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
-
IC50: 25 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(3-phenyl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
-
IC50: 0.65 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(4-phenyl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
-
IC50: 0.21 nM
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(thien-2-ylmethyl)-amino]acetyl]pentylcarbamate
-
IC50: 9.2 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-cyclobutyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 15 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-cyclohexyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 22 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-cyclopentyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 20 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-ethyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 26 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-isobutyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 39 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-isopropyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 17 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-methyl-1H-pyrazol-3-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 0.41 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-methyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 32 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(3-methyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 0.71 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(4-bromo-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 0.24 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(4-cyano-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 0.91 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(4-fluoro-1H-indazol-3-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 0.26 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[(4-methyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
-
IC50: 0.47 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[[1-(3,3-dimethyl)-1H-pyrazol-5-yl]amino](oxo)acetyl]pentylcarbamate
-
IC50: 62 nM
1-Isopropyl-2-methylpropyl (1S)-1-[[[1-(cyclopropylmethyl)-1H-pyrazol-5-yl]amino](oxo)acetyl]pentylcarbamate
-
IC50: 27 nM
1-Isopropyl-2-methylpropyl (1S)-2,3-dioxo--1-phenyl-3-[(thien-2-ylmethyl)-amino]propylcarbamate
-
IC50: 27 nM
1-Isopropyl-2-methylpropyl (1S)-3-methyl-1-[oxo[(thien-2-ylmethyl)-amino]acetyl]butylcarbamate
-
IC50: 24 nM
1-Isopropyl-2-methylpropyl (1S,2S)-2-methyl-1-[oxo[(thien-2-ylmethyl)-amino]acetyl]butylcarbamate
-
IC50: 87 nM
1-Isopropyl-2-methylpropyl 2,3-dioxo-3-[(thien-2-ylmethyl)-amino]propylcarbamate
-
IC50: 0.012 mM
1-methylethyl (2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazinecarboxylate
-
-
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-(3-methylphenyl)urea
-
-
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-phenylurea
-
-
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-[3-(trifluoromethyl)phenyl]urea
-
-
2,2'-N,N'-bis(benzyloxycarbonyl)-L-leucinylcarbohydrazide
-
-
2-(3-methoxyphenyl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-(3-methylphenyl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-(3-tert-butylphenyl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-(4-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-3-oxoazepan-1-ylsulfonyl)pyridine 1-oxide
-
-
2-(biphenyl-3-yl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-(cyclohexylamino)pyrimidine-4-carbonitrile
-
-
2-(cyclohexylmethyl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-cyano-4-(cyclohexylamino)-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-(cyclohexylamino)-N-[2-(3-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
-
-
2-cyano-4-(cyclohexylamino)-N-[2-(4-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
-
-
2-cyano-4-(cyclohexylamino)-N-[2-(4-pyrrolidin-1-ylphenyl)ethyl]pyrimidine-5-carboxamide
-
-
2-cyano-4-(cyclohexylamino)-N-[2-[4-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[3-[2-(1H-imidazol-1-yl)ethoxy]-4-methoxyphenyl]ethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[3-[2-(1H-imidazol-1-yl)ethoxy]phenyl]ethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[4-[(1-methylpiperidin-4-yl)oxy]phenyl]ethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[4-[(4-methylpiperazin-1-yl)methyl]phenyl]ethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[4-[2-(1H-imidazol-1-yl)ethoxy]phenyl]ethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-(3-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-(4-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-(4-pyrrolidin-1-ylphenyl)ethyl]pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-[3-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-[4-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
-
-
2-cycloheptyl-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-cycloheptyl-3,5-dioxo-4-[3-(piperidin-1-yl)propyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-cycloheptyl-4-[2-(dimethylamino)ethyl]-3,5-dioxo-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-cycloheptyl-4-[3-(morpholin-4-yl)propyl]-3,5-dioxo-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-cyclohexyl-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-cyclopentyl-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-methyl-1-phenylpropan-2-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
2-methylpropyl [(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamate
-
-
2-phenylethyl (4S)-4-[[(4S)-4-([[(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamoyl]oxy)-3,3-dimethylpyrrolidin-1-yl]oxy]-3,3-dimethylpyrrolidine-1-carboxylate
-
-
2-phenylpropan-2-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
2-[3-(hydroxymethyl)phenyl]-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
2-[[2-cyano-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methyl]-N-cyclohexyl-1,3-dioxo-2,8-diazaspiro[4.5]decane-8-carboxamide
-
-
2-[[2-cyano-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methyl]-N-methyl-1,3-dioxo-2,8-diazaspiro[4.5]decane-8-carboxamide
-
-
3,5-dioxo-2-phenyl-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
3,5-dioxo-2-[3-(propan-2-yl)phenyl]-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
3,5-dioxo-4-(2-phenylethyl)-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
3,5-dioxo-4-phenyl-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
3,5-dioxo-4-propyl-2-[4-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
3,5-dioxo-4-[2-(piperidin-1-yl)ethyl]-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
3,5-dioxo-4-[3-(piperidin-1-yl)propyl]-2-[3-(propan-2-yl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
3,5-dioxo-4-[3-(piperidin-1-yl)propyl]-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-2-oxopropylcarbamate
-
-
3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxo-N-(phenylsulfonyl)pyrrolidine-1-carboxamide
-
-
3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxo-N-phenylpyrrolidine-1-carboxamide
-
-
3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxamide
-
-
3-(4-([4'-((1-[(cyanomethyl)carbamoyl]cyclohexyl)carbamoyl)biphenyl-4-yl]oxy)piperidin-1-yl)propanoic acid
-
-
3-(4-[[(2S)-2-([[1-(biphenyl-3-ylamino)cyclohexyl]carbonyl]amino)butyl]amino]phenoxy)propanoic acid
-
-
3-(benzyloxy)-1-cyanoazetidine
-
IC 50: 40 nM
3-(cyclohexylamino)benzonitrile
-
-
3-amino-4-[(tetrahydro-2-furanylmethyl)amino] benzoic acid
-
-
3-benzylpentan-3-yl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
3-bromo-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
3-bromo-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]benzamide
-
moderate inhibition
3-[(benzyloxy)methyl]-1-cyanopyrrolidine
-
IC 50: 100 nM
3-[4-([(2S)-2-[(N-biphenyl-3-yl-L-leucyl)amino]butyl]amino)phenoxy]propanoic acid
-
-
3-[[(2S)-2-[([3-acetyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
3-[[(2S)-2-[[(4-[[(4-aminophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
4'-(4-tert-butylpiperazin-1-yl)-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)biphenyl-4-carboxamide
-
-
4'-(4-tert-butylpiperazin-1-yl)-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]biphenyl-4-carboxamide
-
strong inhibition
4'-[4-(tert-butylamino)piperidin-1-yl]-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)biphenyl-4-carboxamide
-
-
4'-[4-(tert-butylamino)piperidin-1-yl]-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]biphenyl-4-carboxamide
-
strong inhibition
4-(2-[(3R)-3-aminopyrrolidin-1-yl]-1,3-thiazol-4-yl)-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
4-(3,4-dimethylphenyl)-6-propylpyrimidine-2-carbonitrile
-
-
4-(3-cyanophenyl)-6-propylpyrimidine-2-carbonitrile
-
-
4-(3-cyclopentylphenyl)-6-propylpyrimidine-2-carbonitrile
-
-
4-(3-methylphenyl)-6-propylpyrimidine-2-carbonitrile
-
-
4-(3-tert-butylphenyl)-6-propylpyrimidine-2-carbonitrile
-
-
4-(4-acetylpiperazin-1-yl)-5-amino-6-[(2-methylpropyl)amino]pyrimidine-2-carbonitrile
-
-
4-(cyclohexylamino)pyrimidine-2-carbonitrile
-
-
4-(dimethylamino)-N-[1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]benzamide
-
-
4-(trifluoromethoxy)-N-(1-[[(1S)-1-([5-[3-(trifluoromethyl)phenyl]-1,3,4-oxadiazol-2-yl]carbonyl)butyl]carbamoyl]cyclohexyl)benzamide
-
-
4-(trifluoromethoxy)-N-(1-[[(1S)-1-([5-[4-(trifluoromethyl)phenyl]-1,3,4-oxadiazol-2-yl]carbonyl)butyl]carbamoyl]cyclohexyl)benzamide
-
-
4-amino-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
4-amino-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]benzamide
-
moderate inhibition
4-benzyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
4-bromo-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
4-bromo-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]benzamide
-
moderate inhibition
4-butyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
4-cyano-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]benzamide
-
moderate inhibition
4-cycloheptyl-6-propylpyrimidine-2-carbonitrile
-
-
4-cycloheptyl-6-[3-(piperidin-1-yl)propyl]pyrimidine-2-carbonitrile
-
-
4-cyclohexyl-6-propylpyrimidine-2-carbonitrile
-
-
4-cyclooctyl-6-propylpyrimidine-2-carbonitrile
-
-
4-cyclopentyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
4-ethyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
4-fluoro-N-[1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]benzamide
-
-
4-methyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
4-Morpholinecarbonyl-Ala-homophenylalanine-PSI(CH=CH-SO2-Ph)
-
-
4-Morpholinecarbonyl-aminohexanoic acid-homophenylalanine-PSI(CH=CH-SO2-Ph)
-
-
4-Morpholinecarbonyl-Gly-homophenylalanine-PSI(CH=CH-SO2-Ph)
-
-
4-Morpholinecarbonyl-Ile-homophenylalanine-PSI(CH=CH-SO2-Ph)
-
-
4-Morpholinecarbonyl-Leu-homophenylalanine-PSI(CH=CH-SO2-Ph)
-
-
4-Morpholinecarbonyl-Met-homophenylalanine-PSI(CH=CH-SO2-Ph)
-
-
4-Morpholinecarbonyl-methionine dioxide-homophenylalanine-PSI(CH=CH-SO2-Ph)
-
-
4-Morpholinecarbonyl-Phe-homophenylalanine-PSI(CH=CH-SO2-Ph)
-
-
4-Morpholinecarbonyl-Val-homophenylalanine-PSI(CH=CH-SO2-Ph)
-
-
4-phenyl-6-propylpyrimidine-2-carbonitrile
-
-
4-propyl-6-[2-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
-
-
4-propyl-6-[3-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
-
moderate cathepsin K potency
4-propyl-6-[4-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
-
-
4-[(2,2-dimethylpropyl)(4-iodobenzyl)amino]pyrimidine-2-carbonitrile
-
-
4-[(2,2-dimethylpropyl)amino]-5-(3-[4-[(4-methoxyphenyl)sulfonyl]piperazin-1-yl]prop-1-yn-1-yl)pyrimidine-2-carbonitrile
-
-
4-[(2,2-dimethylpropyl)amino]-5-[3-(pyridin-3-yloxy)prop-1-yn-1-yl]pyrimidine-2-carbonitrile
-
-
4-[(2,2-dimethylpropyl)amino]-5-[3-[4-(4-methylpiperazin-1-yl)phenyl]prop-1-yn-1-yl]pyrimidine-2-carbonitrile
-
-
4-[(2,2-dimethylpropyl)[4-(1H-1,2,4-triazol-1-ylmethyl)benzyl]amino]pyrimidine-2-carbonitrile
-
-
4-[(2,2-dimethylpropyl)[4-(3-piperidin-1-ylprop-1-yn-1-yl)benzyl]amino]pyrimidine-2-carbonitrile
-
-
4-[(2,2-dimethylpropyl)[4-[3-(1H-1,2,4-triazol-1-yl)prop-1-yn-1-yl]benzyl]amino]pyrimidine-2-carbonitrile
-
-
4-[(2,2-dimethylpropyl)[4-[3-(4-methylpiperazin-1-yl)prop-1-yn-1-yl]benzyl]amino]pyrimidine-2-carbonitrile
-
-
4-[2-(1,4'-bipiperidin-1'-yl)-1,3-thiazol-4-yl]-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
4-[2-(1,4'-bipiperidin-1'-yl)-1,3-thiazol-4-yl]-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]benzamide
-
strong inhibition
4-[2-(4-tert-butylpiperazin-1-yl)-1,3-thiazol-4-yl]-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
4-[2-(4-tert-butylpiperazin-1-yl)-1,3-thiazol-4-yl]-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]benzamide
-
strong inhibition
4-[2-(dimethylamino)ethyl]-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
4-[2-chloro-3-(trifluoromethyl)phenyl]-6-propylpyrimidine-2-carbonitrile
-
-
4-[2-[(3R)-3-aminopyrrolidin-1-yl]-1,3-thiazol-4-yl]-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]benzamide
-
strong inhibition
4-[3-(dimethylamino)propyl]-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
4-[3-(methylsulfonyl)phenyl]-6-propylpyrimidine-2-carbonitrile
-
-
4-[3-(morpholin-4-yl)propyl]-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
-
-
4-[3-(pentan-3-ylamino)propyl]-6-[3-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
-
-
4-[3-(piperidin-1-yl)propyl]-6-[3-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
-
-
4-[3-(tert-butylamino)propyl]-6-[3-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
-
-
4-[4-chloro-3-(trifluoromethyl)phenyl]-6-propylpyrimidine-2-carbonitrile
-
-
4-[benzyl(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
-
-
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzoic acid
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
4-[[4-[3-(1,4'-bipiperidin-1'-yl)prop-1-yn-1-yl]benzyl](2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
-
-
4-[[4-[3-(4-acetylpiperazin-1-yl)prop-1-yn-1-yl]benzyl](2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
-
-
5-(3-[4-[(3-chloropropyl)sulfonyl]piperazin-1-yl]prop-1-yn-1-yl)-4-[(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
-
-
5-amino-4-(3-hydroxyazetidin-1-yl)-6-[(2-methylpropyl)amino]pyrimidine-2-carbonitrile
-
-
5-amino-4-(bicyclo[2.2.1]hept-2-ylamino)-6-morpholin-4-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-(cyclohexylamino)-6-morpholin-4-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-(cyclopentylamino)-6-morpholin-4-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-morpholin-4-yl-6-(phenylamino)pyrimidine-2-carbonitrile
-
-
5-amino-4-morpholin-4-yl-6-(tetrahydrofuran-3-ylamino)pyrimidine-2-carbonitrile
-
-
5-amino-4-morpholin-4-yl-6-piperidin-1-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-morpholin-4-yl-6-pyrrolidin-1-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-[(1,1-dioxidotetrahydrothiophen-3-yl)amino]-6-[(2-methylpropyl)amino]pyrimidine-2-carbonitrile
-
-
5-amino-4-[(1-methylethyl)amino]-6-morpholin-4-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-[(1-methylpropyl)amino]-6-morpholin-4-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-[(2,2-dimethylpropyl)amino]-6-morpholin-4-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-[(2-methoxyethyl)amino]-6-[(2-methylpropyl)amino]pyrimidine-2-carbonitrile
-
-
5-amino-4-[(2-methylpropyl)amino]-6-morpholin-4-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-[(2-methylpropyl)amino]-6-piperazin-1-ylpyrimidine-2-carbonitrile
-
-
5-amino-4-[(2-methylpropyl)amino]-6-[(tetrazolidin-5-ylmethyl)amino]pyrimidine-2-carbonitrile
-
-
5-bromo-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)thiophene-2-carboxamide
-
-
5-bromo-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]thiophene-2-carboxamide
-
moderate inhibition
5-[3-(1,3-dihydro-2H-isoindol-2-yl)prop-1-yn-1-yl]-4-[(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
-
-
5-[3-(3,4-dihydroisoquinolin-2(1H)-yl)prop-1-yn-1-yl]-4-[(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
-
-
5-[3-(4,5-dichloro-1H-imidazol-1-yl)prop-1-yn-1-yl]-4-[(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(2,2,2-trifluoroethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-(4-chlorobenzyl)-7-(2-cyclooctylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-(4-chlorobenzyl)-7-(2-piperidin-1-ylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(3,3,3-trifluoropropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(3,3-dimethylbutyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(3-cyclohexylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-(4-chlorobenzyl)-7-(4,4,4-trifluorobutyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(4,4-dimethylpentyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-(4-chlorobenzyl)-7-cyclohexyl-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-(4-chlorobenzyl)-7-[2-(piperidin-1-yl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(bromomethyl)-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(cyclohexylamino)-9-[(2S,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]-9H-purine-2-carbonitrile
-
-
6-(cyclohexylamino)-9-[2-(4-methylpiperazin-1-yl)ethyl]-9H-purine-2-carbonitrile
-
-
6-(cyclohexylamino)pyrazine-2-carbonitrile
-
-
6-(cyclohexylamino)pyridine-2-carbonitrile
-
-
6-benzyl-7-(2,2,2-trifluoroethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-benzyl-7-cyclohexyl-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-cyano-2-(3-trifluoromethyl-phenyl)-3,5-dioxo-1,2,4-triazine
-
poor catK potency
6-[(1'-acetyl-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[(4,5-dichloro-1H-imidazol-1-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[(5,5-dimethyl-2,4-dioxo-1,3-oxazolidin-3-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[(8-acetyl-1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[(8-benzyl-1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[4-[(diethylamino)methyl]benzyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(1-acetyl-1,2,3,6-tetrahydropyridin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
6-[[4-(1-acetylpiperidin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
6-[[4-(4-acetyl-1,4-diazepan-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)-2-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)-3-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4,4-difluorocyclohexyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[8-(2,4-dimethoxyphenyl)-1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl]methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethyl-propyl)-6-(1,3-dioxo-2,8-diaza-spiro[4.5]dec-2-ylmethyl)-7H-pyrrolo[2,3-d] pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-(1H-1,2,3-triazol-1-ylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-(1H-imidazol-1-ylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(1'-methyl-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-1,3,8-triazaspiro[4.5]dec-3-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-3-propyl-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-8-propyl-1,3,8-triazaspiro[4.5]dec-3-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(3-methyl-2,4-dioxo-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(5-fluoro-1'-methyl-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(5-fluoro-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(5-methoxy-1'-methyl-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(5-methoxy-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[(pyridin-4-yloxy)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[4-(4-methylpiperazin-1-yl)benzyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[4-(morpholin-4-yl)benzyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[[2-oxo-1'-(propan-2-yl)spiro[indole-3,4'-piperidin]-1(2H)-yl]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[[4-(4-fluorophenyl)piperazin-1-yl]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2,2-dimethylpropyl)-6-[[8-(morpholin-4-ylacetyl)-1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2-cyclohexylethyl)-6-(4-methoxybenzyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-(phenoxymethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(phenylamino)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(pyridin-2-yloxy)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(pyridin-2-ylsulfanyl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[[methyl(phenyl)amino]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
benzofuran-2-carboxylic acid [(S)-3-methyl-1-[2-oxo-3-(pyridin-2-ylsulfonylamino)propylcarbamoyl]butyl]amide
-
-
benzyl (1-[(cyanomethyl)carbamoyl]-2-hydroxypropyl)carbamate
-
-
benzyl (2S)-2-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)-4-methylpentanoate
-
-
benzyl (2S,3R)-1-(cyanomethylamino)-3-hydroxy-1-oxobutan-2-ylcarbamate
-
weak inhibition
benzyl (2S,3S)-1-(cyanomethylamino)-3-methyl-1-oxopentan-2-ylcarbamate
-
weak inhibition
benzyl 1-cyano-3-pyrrolidinylcarbamate
-
IC 50: 40 nM
benzyl [(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamate
-
-
benzyl [(1S)-1-[(cyanomethyl)carbamoyl]-2,2-dimethylpropyl]carbamate
-
weak inhibition
benzyl [(1S)-2-[(cyanomethyl)amino]-1-(naphthalen-2-ylmethyl)-2-oxoethyl]carbamate
benzyl [(2S)-1-{2-[(2-{(2S)-2-[(2-amino-3-phenylpropanoyl)amino]-4-methylpentanoyl}hydrazinyl)carbonyl]hydrazinyl}-4-methyl-1-oxopentan-2-yl]carbamate
-
shows any degree of Cat K selectivity (10fold vs. Cat L and F)
benzyl [1-[(cyanomethyl)carbamoyl]cyclohexyl]carbamate
benzyl [1-[(cyanomethyl)carbamoyl]cyclopentyl]carbamate
-
weak inhibition
Benzyloxycarbonyl-Phe-Ala-CHN2
-
-
Benzyloxycarbonyl-Phe-Phe-CHN2
-
-
biphenyl-4-yl (4S)-4-([[(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamoyl]oxy)-3,3-dimethylpyrrolidine-1-carboxylate
-
-
biphenyl-4-ylmethyl (4S)-4-([[(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamoyl]oxy)-3,3-dimethylpyrrolidine-1-carboxylate
-
-
BML-244
-
has moderate selectivity (more than 30fold), but is a relatively weak inhibitor of human Cat K
Boc-I
-
lysosomotropic, water-soluble polymer selective catK inhibitor. Inhibition of catK greatly reduces melanoma cell invasion through Matrigel basement membrane matrix and increases detection of internalized collagen
Boc-Phe-Leu-NHNH-CO-NHNH-Leu-Z
-
-
carbobenzyloxy-Phe-Phe-CH2F
-
-
cathepsin K propeptide
-
-
-
CatK-selective inhibitor II
-
i.e. Boc-Phe-Leu-NHNH-CO-NHNH-Leu-Z
cystatin
-
different types, expression analysis in various cell types isolated from normal and neoplastic breast tissue, overview
-
dibenzyl [(2-oxopropane-1,3-diyl)bis{imino[(2S)-4-methyl-1-oxopentane-1,2-diyl]}]biscarbamate
-
-
E64
-
i.e. L-3-carboxy-trans-2,3-epoxypropionyl-leucylamido-(4-guanidino)butane, inhibitor-enzyme complex structure 9in presence of different chondroitin 4-sulfate fractions, overview
ethyl 3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxylate
-
-
ethyl 4-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-3-oxoazepane-1-carboxylate
-
-
ethyl 4-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-3-oxopiperidine-1-carboxylate
-
-
Ethyl 5-[((3S)-3[[(isopropyl-2-methylpropoxy)carbonyl]amide]-2-oxoheptanoyl)amino]-1H-pyrazole-4-carboxylate
-
IC50: 1.7 nM
ethyl N-[[(2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazino]carbonyl]-b-alaninate
-
-
ethyl N-[[(2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazino]carbonyl]glycinate
-
-
H-kininogen
-
natural inhibitor of cathepsin K, reversible, tight-binding competitive inhibitor
-
Human squamous cell carcinoma antigen 1
-
i.e. SCCA1
-
K4b
-
potent, reversible, Cat K-selective inhibitor
L-kininogen
-
natural inhibitor of cathepsin K, reversible, tight-binding competitive inhibitor
-
leupeptazin
-
isolated from a liquid culture of soil Streptomyces sp. IS2-4
LHVS
-
a cell-permeable broad spectrum cathepsin inhibitor
methyl 3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxylate
-
-
methyl 5-acetoxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
-
-
methyl 5-hydroxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
-
furanquinone from Paulownia tomentosa stem
methyl 5-methoxy dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
-
-
methyl 5-propoxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
-
-
methyl N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-methioninate
-
-
methyl [[(2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazino]carbonyl]carbamate
-
-
Mu-Leu-Hph-fluoromethylketone
-
highly potent versus Cat K, but is essentially non-selective versus all human cathepsins
MV061194
-
selective, potent reversible cathepsin K inhibitor
N-((S)-4-methyl-1-oxo-1-((S)-3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-ylamino)pentan-2-yl)benzofuran-2-carboxamide
-
-
N-(1-([(cyanomethyl)amino]carbonyl)cyclohexyl)-4-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]benzamide
-
i.e. L-006235 or CRA-013788/L
N-(1-cyano-3-pyrrolidinyl)benzamide
-
IC 50: 370 nM
N-(1-cyano-3-pyrrolidinyl)[1,1'-biphenyl]-4-carboxamide
-
IC 50: 290 nM
N-(1-cyano-3pyrrolidinyl)benzenesulfonamide
-
IC 50: 50 nM
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(1-hydroxycyclopropyl)biphenyl-4-yl]ethyl]-L-leucinamide
-
-
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(2-hydroxypropan-2-yl)biphenyl-4-yl]ethyl]-L-leucinamide
-
-
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4-(4-methyl-4,5-dihydro-1,3-thiazol-2-yl)phenyl]ethyl]-L-leucinamide
-
-
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4-(quinolin-6-yl)phenyl]ethyl]-L-leucinamide
-
-
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4-[5-(1-hydroxycyclopropyl)pyridin-2-yl]phenyl]ethyl]-L-leucinamide
-
-
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4-[6-(methylsulfonyl)pyridin-3-yl]phenyl]ethyl]-L-leucinamide
-
-
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1R)-2,2-difluoro-1-hydroxyethyl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1S)-2,2-difluoro-1-hydroxyethyl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-2-pyridin-4-yl-1,3-thiazole-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-(4-fluoropiperidin-4-yl)biphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-(dimethylamino)biphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-(piperazin-1-ylsulfonyl)biphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-([(2S)-1-methylpyrrolidin-2-yl]methoxy)biphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-([1-(2-hydroxyethyl)piperidin-4-yl]oxy)biphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-([4-(2,2,2-trifluoroethyl)piperazin-1-yl]sulfonyl)biphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-isoxazol-5-ylbiphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-piperazin-1-ylbiphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-[(1-methylpiperidin-3-yl)oxy]biphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-[(1-methylpiperidin-4-yl)oxy]biphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-[methyl(1-methylpyrrolidin-3-yl)amino]biphenyl-4-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-(4-[(1-methylethyl)amino]piperidin-1-yl)-1,3-thiazol-4-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-(4-[methyl(1-methylethyl)amino]piperidin-1-yl)-1,3-thiazol-4-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-morpholin-4-yl-1,3-thiazol-4-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[(4-methylpiperazin-1-yl)amino]-1,3-thiazol-4-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[(4-methylpiperazin-1-yl)methyl]-1,3-thiazol-4-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[3-(dimethylamino)pyrrolidin-1-yl]-1,3-thiazol-4-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[4-(2-methoxyethyl)piperazin-1-yl]-1,3-thiazol-4-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[4-(tetrahydro-2H-pyran-4-yl)piperazin-1-yl]-1,3-thiazol-4-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(4-methylpiperazin-1-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(4-propylpiperazin-1-yl)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(dimethylamino)benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-ethynylbenzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-morpholin-4-ylbenzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[(4-methylpiperazin-1-yl)carbonyl]benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[(4-methylpiperazin-1-yl)sulfonyl]benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(1,4-dimethylpiperidin-4-yl)-1,3-thiazol-4-yl]benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(1-methylpiperidin-4-yl)-1,3-thiazol-4-yl]benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(4-morpholin-4-ylpiperidin-1-yl)-1,3-thiazol-4-yl]benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(morpholin-4-ylmethyl)-1,3-thiazol-4-yl]benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(piperidin-4-yloxy)-1,3-thiazol-4-yl]benzamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)biphenyl-3-carboxamide
-
-
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)biphenyl-4-carboxamide
-
-
N-(1-[[(1S)-1-[[5-(1-methylethyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamoyl]cyclohexyl)-4-(trifluoromethoxy)benzamide
-
-
N-(1-[[(1S)-1-[[5-(3-methoxyphenyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamoyl]cyclohexyl)-4-(trifluoromethoxy)benzamide
-
-
N-(1-[[(1S)-1-[[5-(4-methoxyphenyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamoyl]cyclohexyl)-4-(trifluoromethoxy)benzamide
-
-
N-(2,3-dichlorophenyl)triazolyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
-
IC50: 9 nM
N-(2-chlorophenyl)triazolyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
-
IC50: 6 nM
N-(4-chlorophenyl)-2-methylalanyl-N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-L-leucinamide
-
IC50 is below 1 nM
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)propanamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
N-(5-isopropyl)pyridine-2-carboxyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
-
IC50: less than 3 nM
N-(cyanomethyl)-1-[(3-phenylpropanoyl)amino]cyclohexanecarboxamide
-
-
N-(cyanomethyl)-4-methyl-2-[3'-(2-piperazin-1-yl-1,3-thiazol-4-yl)biphenyl-3-yl]pentanamide
-
-
N-(cyanomethyl)-4-methyl-2-[3'-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]biphenyl-3-yl]pentanamide
-
-
N-(cyanomethyl)-4-methyl-2-[4'-(2-piperazin-1-yl-1,3-thiazol-4-yl)biphenyl-3-yl]pentanamide
-
-
N-(cyanomethyl)-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
-
-
N-4-benzyloxybenzoyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
-
IC50: 6 nM
N-4-isopropylbenzoyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
-
IC50: less than 3 nM
N-4-methoxybenzoyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
-
-
N-4-propylbenzoyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
-
IC50: less than 3 nM
N-benzyl-3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxamide
-
-
N-cyano-tetrahydro-pyridazine compounds
-
-
-
N-[(1-cyano-2-pyrrolidinyl)methyl]benzamide
-
IC 50: 0.013 mM
N-[(1-cyano-2-pyrrolidinyl)methyl]benzenesulfonamide
-
IC 50: 0.012 mM
N-[(1-cyano-3-azetidinyl)methyl]benzamide
-
IC 50: 70 nM
N-[(1-cyano-3-azetidinyl)methyl]benzenesulfonamide
-
IC 50: 20 nM
N-[(1-cyano-3-azetidinyl)methyl]cyclohexanecarboxamide
-
IC 50: 5 nM
N-[(1-cyano-3pyrrolidinyl)methyl]benzenesulfonamide
-
IC 50: 200 nM
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-N2-(piperazin-1-ylcarbonyl)-D-leucinamide
-
i.e. APC3328
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[(2-methyl-1H-imidazol-1-yl)acetyl]-L-leucinamide
-
IC50: 190 nM
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[(4-phenylpiperidin-1-yl)acetyl]-L-leucinamide
-
IC50: 84 nM
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[(4-pyridin-4-ylpiperazin-1-yl)acetyl]-L-leucinamide
-
IC50: 9 nM
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[(5-methyl-1H-imidazol-4-yl)acetyl]-L-leucinamide
-
IC50: 24 nM
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[2-(4-chlorophenoxy)-2-methylpropanoyl]-L-leucinamide
-
IC50 is below 1 nM
N-[(1S)-1-((3-hydroxy-1-[(3-pyridin-2-ylphenyl)acetyl]azepan-4-yl)carbamoyl)-3-methylbutyl]-5-(2-morpholin-4-ylethoxy)-1-benzofuran-2-carboxamide
-
-
N-[(1S)-1-([(1R)-2-(benzyloxy)-1-cyanoethyl]carbamoyl)-3-methylbutyl]-1-methyl-1H-indole-2-carboxamide
-
IC50 is below 1 nM
N-[(1S)-1-([(1R)-2-(benzyloxy)-1-cyanoethyl]carbamoyl)-3-methylbutyl]-1H-indole-2-carboxamide
-
IC50: 430 nM
N-[(1S)-1-([1-(2-hydroxy-2,3-dihydro-1,4-benzodioxin-2-yl)ethenyl]carbamoyl)-3-methylbutyl]-1-benzofuran-2-carboxamide
-
-
N-[(1S)-1-([3-(2-hydroxyphenoxy)-1-methylidene-2-oxopropyl]carbamoyl)-3-methylbutyl]-1-benzofuran-2-carboxamide
-
-
N-[(1S)-1-carbamoyl-3-(methylsulfonyl)propyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
-
-
N-[(1S)-1-carbamoyl-3-phenylpropyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
-
-
N-[(1S)-1-cyano-2-phenylethyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
-
-
N-[(1S)-1-cyano-3-(methylsulfanyl)propyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
-
-
N-[(1S)-1-cyanoethyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
-
-
N-[(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]-2-phenylacetamide
-
-
N-[(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]-3-phenylpropanamide
-
-
N-[(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]-N2-(2,2,2-trifluoroethyl)-L-leucinamide
-
-
N-[(1S)-1-[2-(methylsulfanyl)ethyl]-2-oxopropyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-3-(methylsulfonyl)-L-alaninamide
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-alaninamide
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-methioninamide
-
excellent selectivity against the cathepsins B, L and S
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-methionine
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-phenylalaninamide
-
excellent selectivity against the cathepsins B, L and S
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N,N-dimethyl-L-methioninamide
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N-(2,2,2-trifluoroethyl)-L-methioninamide
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N-(methylsulfonyl)-L-methioninamide
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N-benzyl-L-methioninamide
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N-methyl-L-methioninamide
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-S-methyl-L-cysteinamide
-
-
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucylglycinamide
-
-
N-[(1S)-3-methyl-1-(((4R)-3-oxo-1-[(3-pyridin-2-ylphenyl)acetyl]azepan-4-yl)carbamoyl)butyl]-5-(2-morpholin-4-ylethoxy)-1-benzofuran-2-carboxamide
-
-
N-[(1S)-3-methyl-1-([(1S)-1-methyl-2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamoyl)butyl]-1-benzofuran-2-carboxamide
-
-
N-[(1S)-3-methyl-1-([(4S)-3-oxo-1-[(3-pyridin-2-ylphenyl)acetyl]azepan-4-yl]carbamoyl)butyl]-5-(2-morpholin-4-ylethoxy)-1-benzofuran-2-carboxamide
-
-
N-[1-([(1S)-1-[(5-ethyl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
N-[1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
N-[1-([(1S)-1-[(5-methoxy-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
N-[1-([(1S)-1-[(5-phenyl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
N-[1-([(1S)-1-[(5-tert-butyl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
N-[1-([(1S)-1-[(5-thiophen-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-2-pyridin-4-yl-1,3-thiazole-4-carboxamide
-
moderate inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-(4-fluoropiperidin-4-yl)biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-(dimethylamino)biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-(piperazin-1-ylsulfonyl)biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-isoxazol-5-ylbiphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-piperazin-1-ylbiphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-[(1-methylpiperidin-3-yl)oxy]biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-[(1-methylpiperidin-4-yl)oxy]biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-[methyl(1-methylpyrrolidin-3-yl)amino]biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-[[(2S)-1-methylpyrrolidin-2-yl]methoxy]biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-[[1-(2-hydroxyethyl)piperidin-4-yl]oxy]biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-[[1-(2-methoxyethyl)piperidin-4-yl]oxy]biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4'-[[4-(2,2,2-trifluoroethyl)piperazin-1-yl]sulfonyl]biphenyl-4-carboxamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-(2-morpholin-4-yl-1,3-thiazol-4-yl)benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-(2-[4-[(1-methylethyl)amino]piperidin-1-yl]-1,3-thiazol-4-yl)benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-(2-[4-[methyl(1-methylethyl)amino]piperidin-1-yl]-1,3-thiazol-4-yl)benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-(4-methylpiperazin-1-yl)benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-(4-propylpiperazin-1-yl)benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-morpholin-4-ylbenzamide
-
moderate inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[(4-methylpiperazin-1-yl)carbonyl]benzamide
-
moderate inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[(4-methylpiperazin-1-yl)sulfonyl]benzamide
-
moderate inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-(1-methylpiperidin-4-yl)-1,3-thiazol-4-yl]benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-(4-morpholin-4-ylpiperidin-1-yl)-1,3-thiazol-4-yl]benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-(morpholin-4-ylmethyl)-1,3-thiazol-4-yl]benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-(piperidin-4-yloxy)-1,3-thiazol-4-yl]benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-[(4-methylpiperazin-1-yl)methyl]-1,3-thiazol-4-yl]benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-[3-(dimethylamino)pyrrolidin-1-yl]-1,3-thiazol-4-yl]benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-[4-(tetrahydro-2H-pyran-4-yl)piperazin-1-yl]-1,3-thiazol-4-yl]benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-[methyl(4-methylpiperazin-1-yl)amino]-1,3-thiazol-4-yl]benzamide
-
strong inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]biphenyl-3-carboxamide
-
moderate inhibition
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]biphenyl-4-carboxamide
-
moderate inhibition
N-[2-[(4-methoxyphenyl)amino]ethyl]-1-(phenylamino)cyclohexanecarboxamide
-
-
N-[2-[(4-methoxyphenyl)amino]ethyl]-1-phenoxycyclohexanecarboxamide
-
-
N-[2-[(4-methoxyphenyl)amino]ethyl]-1-[4-(1-methylethyl)phenoxy]cyclohexanecarboxamide
-
-
N2-(3-cyclohexylphenyl)-N-[2-[(4-methoxyphenyl)amino]ethyl]-L-leucinamide
-
-
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
N2-biphenyl-3-yl-N-[(1S)-1-[([4-[2-(1H-tetrazol-5-yl)ethoxy]phenyl]amino)methyl]propyl]-L-leucinamide
-
-
N2-biphenyl-3-yl-N-[(1S)-1-[[(4-methoxyphenyl)amino]methyl]propyl]-L-leucinamide
-
-
N2-biphenyl-3-yl-N-[(1S)-2-[(4-methoxyphenyl)amino]-1-methylethyl]-L-leucinamide
-
-
N2-biphenyl-3-yl-N-[2-[(4-methoxyphenyl)amino]ethyl]-L-leucinamide
-
-
N2-[(1S)-1-[4'-(1-carbamoylcyclopropyl)biphenyl-4-yl]-2,2,2-trifluoroethyl]-N-(1-cyanocyclopropyl)-4-fluoro-L-leucinamide
-
-
N2-[(1S)-1-[4'-[(2S)-1-amino-1-oxopropan-2-yl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-N-(1-cyanocyclopropyl)-4-fluoro-L-leucinamide
-
-
N2-[(1S)-1-[4-[5-(1-carbamoylcyclopropyl)pyridin-2-yl]phenyl]-2,2,2-trifluoroethyl]-N-(1-cyanocyclopropyl)-4-fluoro-L-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-((1S)-1-cyano-2-[4-(trifluoromethyl)phenyl]ethyl)-L-leucinamide
-
IC50: 43 nM
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-2-methylleucinamide
-
weak inhibition
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-4-methyl-L-leucinamide
-
moderate inhibition
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-5,5,5-trifluoro-D-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-5,5,5-trifluoroleucinamide
-
moderate inhibition
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-D-leucinamide
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-L-isoleucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-L-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-L-norleucinamide
N2-[(benzyloxy)carbonyl]-N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-L-leucinamide
-
IC50: 9 nM
N2-[(benzyloxy)carbonyl]-N-[(1R)-2-tert-butoxy-1-cyanoethyl]-L-leucinamide
-
IC50: 240 nM
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-cyano-2-(3-methylphenyl)ethyl]-L-leucinamide
-
IC50: 120 nM
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-cyano-2-(4-methoxyphenyl)ethyl]-L-leucinamide
-
IC50: 63 nM
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-cyano-2-(4-methylphenyl)ethyl]-L-leucinamide
-
IC50: 48 nM
N2-[(benzyloxy)carbonyl]-N-[(1S)-2-(4-tert-butoxyphenyl)-1-cyanoethyl]-L-leucinamide
-
IC50: 398 nM
N2-[(benzyloxy)carbonyl]-N-[2-[(4-methoxyphenyl)amino]ethyl]-L-leucinamide
-
-
N2TY
-
slow-binding inhibitor of cathepsin K
-
naphthalen-2-yl (4S)-4-([[(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamoyl]oxy)-3,3-dimethylpyrrolidine-1-carboxylate
-
-
odanacatib 1
-
i.e. MK-0822, a reversible, non-basic, potent and selective Cat K inhibitor. The nitrile forms a hydrogen bond-stabilized thioimidate intermediate with Cys25. The leucine moiety interacts with the hydrophobic S2 subsite and the biphenyl moiety with the S3 subsite, and the hydrogen bond of the trifluroethylamine amide isostere interact with Gly66. Furthermore, odanacatib does not interact with the prime side of Cat K, binding structure, overview
phenyl (4S)-4-([[(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamoyl]oxy)-3,3-dimethylpyrrolidine-1-carboxylate
-
-
piperidin-2-yl-[2-(trifluoromethyl)-6-[4-(trifluoromethyl)phenyl]pyridin-4-yl] methanol
-
-
piperidine-4-carboxylic acid [3-methyl-1[1-(1-oxa-3-aza-cyclopenta[a]naphthalene-2-carbonyl)-3-phenyl-propylcarbamoyl]-butyl]-amide trifluoroacetate
-
-
piperidine-4-carboxylic acid [3-methyl-1[1-(naphtho[1,2-d]oxazole-2-carbonyl)-3-phenyl-propylcarbamoyl]-butyl]-amide trifluoroacetate
-
-
quinoline-2-carboxylic acid [(S)-1-((3R,S)-4-oxotetrahydrofuran-3ylcarbamoyl)-3-methylbutyl]amide
-
-
relicatib
-
also known as SB-462795, highly potent human cathepsin K inhibitor
S-(1-methylethyl) (2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazinecarbothioate
-
-
SB-357114
-
specific inhibitor
Stefin A
-
slow-binding inhibitor of cathepsin K
-
Stefin B
-
natural inhibitor of cathepsin K, reversible, tight-binding competitive inhibitor
-
Synthetic inhibitors
-
-
-
tert-butyl ([1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]carbamoyl)carbamate
-
-
tert-butyl 3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxylate
-
-
tert-butyl 3-(4-[[(2S)-2-([[1-(biphenyl-3-ylamino)cyclohexyl]carbonyl]amino)butyl]amino]phenoxy)propanoate
-
-
tert-butyl 3-[4-([(2S)-2-[(N-biphenyl-3-yl-L-leucyl)amino]butyl]amino)phenoxy]propanoate
-
-
tert-butyl [(1S)-1-([5-[4-(dimethylamino)phenyl]-1,3,4-oxadiazol-2-yl]carbonyl)butyl]carbamate
-
-
tert-butyl [(1S)-1-formylpentyl]carbamate
-
-
tert-butyl [(1S)-1-[(5-thiophen-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-(4,5-dihydro-1,3-thiazol-2-ylhydrazono)methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-(carbamimidoylhydrazono)methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-(carbamoylhydrazono)methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(2,3-dihydro-1H-indol-1-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(3,4-dihydroisoquinolin-2(1H)-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(3,4-dihydroquinolin-1(2H)-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(3-methylbutanoyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(benzylcarbamoyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(diethylcarbamoyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(dimethylcarbamoyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(dimethylsulfamoyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(ethylcarbamoyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(methylcarbamoyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(morpholin-4-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(phenylcarbamoyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(phenylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(piperidin-1-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(pyrrolidin-1-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(tert-butylcarbamoyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[(trifluoroacetyl)hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[methyl[(2-phenylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[methyl[methyl(2-phenylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[[(1-methylethyl)carbamothioyl]hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[[(1-methylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[[(2-phenylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[[(morpholin-4-ylcarbonyl)oxy]imino]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[(E)-[[methyl(2-phenylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
-
-
tert-butyl [(1S)-1-[[5-(1-methylethyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamate
-
-
tert-butyl [(1S)-1-[[5-(2-methoxyphenyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamate
-
-
tert-butyl [(3S)-1,2-dioxo-1-(phenylamino)heptan-3-yl]carbamate
-
-
tert-butyl [(3S)-1,2-dioxo-1-(propan-2-ylamino)heptan-3-yl]carbamate
-
-
tert-butyl [(3S)-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
tert-butyl [(3S)-1,2-dioxo-1-[[(1S)-1-phenylethyl]amino]heptan-3-yl]carbamate
-
-
tert-butyl [(3S)-1-(benzylamino)-1,2-dioxoheptan-3-yl]carbamate
-
-
tert-butyl [(3S)-1-amino-1,2-dioxoheptan-3-yl]carbamate
-
-
tert-butyl [1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]carbamate
-
-
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E-64
[(S)-1-((3R,S)-1-acetyl-4-oxopyrrolidin-3-ylcarbamoyl)-3-methylbutyl]carbamic acid benzyl ester
-
-
[(S)-1-((3R,S)-4-oxotetrahydrofuran-3-ylcarbamoyl)-3-methylbutyl]carbamic acid benzyl ester
-
-
[(S)-1-((4R,S)-3-oxotetrahydropyran-4-ylcarbamoyl)-3-methylbutyl]carbamic acid benzyl ester
-
-
[1-(2-cyano-tetrahydro-pyridazine-1-carbonyl)-2-methyl-propyl]-carbamic acid benzyl ester
-
inhibits the bone resorptive activity of mature osteoclasts, structure and interaction pattern with cathepsin K, overview
E-64
-
E-64
irreversible inhibitor
E-64
i.e. L-3-carboxy-trans-2,3-epoxypropionylleucylamido-(4-guanidino)butane
E-64
i.e. trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane
((S)-1-[1-[4(R,S)-((S)-2-benzyloxycarbonylamino-4-methylpentanoylamino)-3-oxoazepan-1-yl]methanoyl]-3-methylbutl)carbamic acid benzyl ester
-
the faster eluting diastereomer C34H46N4O7*0.4H2O
((S)-1-[1-[4(R,S)-((S)-2-benzyloxycarbonylamino-4-methylpentanoylamino)-3-oxoazepan-1-yl]methanoyl]-3-methylbutl)carbamic acid benzyl ester
-
the slower eluting diastereomer C34H46N4O7*0.3H2O
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
-
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
-
racemate
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclooctylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(2-cyclooctylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(3-cyclohexylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(3-cyclohexylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
balicatib
-
-
balicatib
-
shows no selectivity in cell-based assays over cathepsins B, L, and S
balicatib
-
high degree of potency and selectivity for purified human Cat K
balicatib
-
potent human cathepsin K inhibitor with a high selectivity against human cathepsins B, L and S (> 4800fold, > 500fold and > 65000fold, respectively)
benzyl [(1S)-2-[(cyanomethyl)amino]-1-(naphthalen-2-ylmethyl)-2-oxoethyl]carbamate
-
-
benzyl [(1S)-2-[(cyanomethyl)amino]-1-(naphthalen-2-ylmethyl)-2-oxoethyl]carbamate
-
weak inhibition
benzyl [1-[(cyanomethyl)carbamoyl]cyclohexyl]carbamate
-
-
benzyl [1-[(cyanomethyl)carbamoyl]cyclohexyl]carbamate
-
moderate inhibition
cystatin C
-
-
-
cystatin C
-
natural inhibitor of cathepsin K, reversible, tight-binding competitive inhibitor
-
E-64
-
-
E-64
-
a cysteine protease inhibitor
L-006235
-
-
L-006235
-
shows no selectivity in cell-based assays over cathepsins B, L, and S
L-873724
-
-
L-873724
-
a cathepsin K inhibitor
L-873724
-
highly selective for cathespin K over other cathepsins, metabolization, overview
L-873724
-
has a greater than 800fold selectivity over other cysteine cathepsins
L-873724
-
high degree of potency and selectivity (more than 100fold) for purified human Cat K
MK-0674
-
-
MK-0674
-
orally bioavailable potent and selective cathepsin K inhibitor
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1R)-2,2-difluoro-1-hydroxyethyl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
-
-
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1R)-2,2-difluoro-1-hydroxyethyl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
-
MIV-701
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-D-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-D-leucinamide
-
weak inhibition
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-L-norleucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-L-norleucinamide
-
moderate inhibition
odanacatib
-
-
odanacatib
-
i.e. MK-0822, a selective cathepsin K inhibitor
odanacatib
-
i.e. MK-0822, development of an enantioselective method for synthesis of the potent cathepsin K inhibitor, via triflate displacement of an alpha-trifluoromethylbenzyl triflate, overview. The key step involves the novel stereospecific SN2 triflate displacement of a chiral alpha-trifluoromethylbenzyl triflate with (S)-gamma-fluoroleucine ethyl ester to generate the required alpha-trifluoromethylbenzyl amino stereocenter
odanacatib
-
formely MK-0822
odanacatib
-
high degree of potency and selectivity for purified human Cat K
odanacatib
-
MK-0822 or MK-822
odanacatib
-
MK-0822, orally active, potent and selective cathepsin K inhibitor
relacatib
-
-
relacatib
-
a Cat K inhibitor in clinical development
relacatib
-
highly potent versus human Cat K, but lacks selectivity versus Cat L, S, and F
additional information
a fluorescence polarization assay is developed to screen 4761 compounds for substrate-specific ectosteric collagenase inhibitors of cathepsin K. A total of 38 compounds are identified that block the collagenase activity without interfering with the hydrolysis of active site substrates such as the synthetic peptide substrate, benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin, and gelatin. The identified inhibitors can be divided into two main classes, negatively charged and polyaromatic compounds which suggest the binding to different ectosteric sites
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additional information
irreversible covalent inhibitors can have a beneficial pharmacokinetic/pharmacodynamics profile but are still often avoided due to the risk of indiscriminate ovalent reactivity and the resulting adverse effects. To overcome this potential liability, we introduced an alkyne moiety as a latent electrophile into small molecule inhibitors of cathepsin K (CatK). Alkyne-based inhibitors do not show indiscriminate thiol reactivity but potently inhibit CatK protease activity by formation of an irreversible covalent bond with the catalytic cysteine residue. Binding mode of alkynes is irreversible and covalent
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additional information
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irreversible covalent inhibitors can have a beneficial pharmacokinetic/pharmacodynamics profile but are still often avoided due to the risk of indiscriminate ovalent reactivity and the resulting adverse effects. To overcome this potential liability, we introduced an alkyne moiety as a latent electrophile into small molecule inhibitors of cathepsin K (CatK). Alkyne-based inhibitors do not show indiscriminate thiol reactivity but potently inhibit CatK protease activity by formation of an irreversible covalent bond with the catalytic cysteine residue. Binding mode of alkynes is irreversible and covalent
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additional information
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not inhibitory are pepstatin, phenylmethylsulfonylfluoride, EDTA, 1,10-phenanthroline
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additional information
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construction of a three-dimensional pharmacophore model for cathepsin K inhibitor screening and development using the enzyme crystal structure complexed with a ketoamide inhibitor, docking and inhibitor binding structure, validation of pharmacophore hypothesis, overview
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additional information
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inhibitor development and structure-activity relationships, overview
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additional information
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inhibitory activities of N-cyano-tetrahydro-pyridazine derivatives, docking studies, overview
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additional information
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P2/S2 and P3/S3 interaction of cathepsin K inhibitors with pyrrolopyrimidine scaffold and structure of the common intermediate, overview
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additional information
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physiological inhibitors of osteoclast differentiation and activation, such as osteoprotegerin, interleukin-6, INF-gamma, can also directly suppress cathepsin K expression
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additional information
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structure-based design of diverse pyrimidine-based scaffolds for inhibitor design
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additional information
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not inhibited by pyrimidine nitrile
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additional information
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not inhibited by N-benzoyl-4-aminosalicylic acid (NSC159686), (2-biphenylylmethyl)malonic acid (NSC94914), 1,4,7,9B-tetraazaphenalene (NSC81462), 1-[1-(2-phenylethyl)-4-piperidinyl]-methanamine, 2-[(3-nitrophenyl)carbamoyl]benzoic acid (NSC408860), and methyl N-[1-(4-methoxyphenyl)-2,5-dioxopyrrolidin-3-yl]glycinate
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Acro-Osteolysis
Current research on pycnodysostosis.
Acro-Osteolysis
Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice.
Adenocarcinoma
Cathepsin K is selectively expressed in the stroma of lung adenocarcinoma but not in bronchioloalveolar carcinoma. A useful marker of invasive growth.
Adenocarcinoma
[Diagnostic value of biomarkers of bone metabolism in the gingival fluid in inflammatory-destructive and tumor oral pathology].
Adenocarcinoma of Lung
Cathepsin K is selectively expressed in the stroma of lung adenocarcinoma but not in bronchioloalveolar carcinoma. A useful marker of invasive growth.
Adenocarcinoma, Bronchiolo-Alveolar
Cathepsin K is selectively expressed in the stroma of lung adenocarcinoma but not in bronchioloalveolar carcinoma. A useful marker of invasive growth.
Adenoma, Oxyphilic
Cathepsin K (Clone EPR19992) Demonstrates Uniformly Positive Immunoreactivity in Renal Oncocytoma, Chromophobe Renal Cell Carcinoma, and Distal Tubules.
Alveolar Bone Loss
Adipokine Chemerin Bridges Metabolic Dyslipidemia and Alveolar Bone Loss in Mice.
Alveolar Bone Loss
Analysis of Cathepsin-K Activity at Tooth and Dental Implant Sites and the Potential of This Enzyme in Reflecting Alveolar Bone Loss.
Alveolar Bone Loss
Effects of Probiotic Culture Supernatant on Cariogenic Biofilm Formation and RANKL-Induced Osteoclastogenesis in RAW 264.7 Macrophages.
Alveolitis, Extrinsic Allergic
Cathepsin-K is a sensitive immunohistochemical marker for detection of micro-granulomas in hypersensitivity pneumonitis.
Amyloidosis
A putative role for cathepsin K in degradation of AA and AL amyloidosis.
Aneurysm
Cathepsin K gene disruption does not affect murine aneurysm formation.
Aneurysm
Differences in Elastin and Elastolytic Enzymes between Men and Women with Abdominal Aortic Aneurysm.
Aneurysm
Osteoclast-Like Cells in Aneurysmal Disease Exhibit an Enhanced Proteolytic Phenotype.
Angina, Stable
Decreased Cathepsin K Plasma Level may Reflect an Association of Osteopoenia/Osteoporosis with Coronary Atherosclerosis and Coronary Artery Calcification in Male Patients with Stable Angina.
Angiomyolipoma
Cathepsin K: A Novel Diagnostic and Predictive Biomarker for Renal Tumors.
Angiomyolipoma
Premelanosome-negative inflammatory angiomyolipoma of liver with expression of cathepsin K and TFE3.
Angiomyolipoma
t(6;11) renal cell carcinoma: a study of seven cases including two with aggressive behavior, and utility of CD68 (PG-M1) in the differential diagnosis with pure epithelioid PEComa/epithelioid angiomyolipoma.
Aortic Aneurysm, Abdominal
Assessing the targeting and fate of cathepsin k antibody-modified nanoparticles in a rat abdominal aortic aneurysm model.
Aortic Aneurysm, Abdominal
Cathepsin K Deficiency Reduces Elastase Perfusion-Induced Abdominal Aortic Aneurysms in Mice.
Arthralgia
Cathepsin K inhibition reduces CTXII levels and joint pain in the guinea pig model of spontaneous osteoarthritis.
Arthritis
Analysis of the kinetics of osteoclastogenesis in arthritic rats.
Arthritis
Cathepsin K deficiency partially inhibits, but does not prevent, bone destruction in human tumor necrosis factor-transgenic mice.
Arthritis
Cathepsin K Inhibitor Regulates Inflammation and Bone Destruction in Experimentally Induced Rat Periapical Lesions.
Arthritis
Cathepsin K inhibitors for osteoporosis and potential off-target effects.
Arthritis
Cathepsin K Is Involved in Development of Psoriasis-like Skin Lesions through TLR-Dependent Th17 Activation.
Arthritis
Cathepsin K-dependent toll-like receptor 9 signaling revealed in experimental arthritis.
Arthritis
Cathepsin K: a unique collagenolytic cysteine peptidase.
Arthritis
Design, synthesis and biological evaluation of inhibitors of cathepsin K on dedifferentiated chondrocytes.
Arthritis
Detection of femtomole quantities of mature cathepsin K with zymography.
Arthritis
Effect of a cathepsin K inhibitor on arthritis and bone mineral density in ovariectomized rats with collagen-induced arthritis.
Arthritis
Effect of M3 muscarinic acetylcholine receptor deficiency on collagen antibody-induced arthritis.
Arthritis
Extracellular cathepsin K exerts antimicrobial activity and is protective against chronic intestinal inflammation in mice.
Arthritis
Inhibition of cathepsin K alleviates autophagy-related inflammation in periodontitis-aggravating arthritis.
Arthritis
Invasive properties of fibroblast-like synoviocytes: correlation with growth characteristics and expression of MMP-1, MMP-3, and MMP-10.
Arthritis
Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency.
Arthritis
Role of cathepsin K in normal joints and in the development of arthritis.
Arthritis
Role of cathepsin K in structural changes in brachiocephalic artery during progression of atherosclerosis in apoE-deficient mice.
Arthritis
The anti-allergic compound tranilast attenuates inflammation and inhibits bone destruction in collagen-induced arthritis in mice.
Arthritis, Experimental
An inhibitor of cathepsin K, icariin suppresses cartilage and bone degradation in mice of collagen-induced arthritis.
Arthritis, Experimental
Effect of a cathepsin K inhibitor on arthritis and bone mineral density in ovariectomized rats with collagen-induced arthritis.
Arthritis, Experimental
Effects of the Cathepsin K Inhibitor ONO-5334 and Concomitant Use of ONO-5334 with Methotrexate on Collagen-Induced Arthritis in Cynomolgus Monkeys.
Arthritis, Experimental
Inhibition of cathepsin K reduces bone erosion, cartilage degradation and inflammation evoked by collagen-induced arthritis in mice.
Arthritis, Experimental
Joint Degradation in a Monkey Model of Collagen-Induced Arthritis: Role of Cathepsin K Based on Biochemical Markers and Histological Evaluation.
Arthritis, Experimental
Myricetin ameliorates the symptoms of collagen-induced arthritis in mice by inhibiting cathepsin K activity.
Arthritis, Psoriatic
Effect of Vitamin D on Peripheral Blood Mononuclear Cells from Patients with Psoriasis Vulgaris and Psoriatic Arthritis.
Arthritis, Psoriatic
Erosive arthritis in a patient with pycnodysostosis: an experiment of nature.
Arthritis, Rheumatoid
An inhibitor of cathepsin K, icariin suppresses cartilage and bone degradation in mice of collagen-induced arthritis.
Arthritis, Rheumatoid
Cathepsin K inhibitor-polymer conjugates: potential drugs for the treatment of osteoporosis and rheumatoid arthritis.
Arthritis, Rheumatoid
Comparison of cathepsins K and S expression within the rheumatoid and osteoarthritic synovium.
Arthritis, Rheumatoid
Cysteine proteinase cathepsin K mRNA is expressed in synovium of patients with rheumatoid arthritis and is detected at sites of synovial bone destruction.
Arthritis, Rheumatoid
Deficiency of cathepsin K prevents inflammation and bone erosion in rheumatoid arthritis and periodontitis and reveals its shared osteoimmune role.
Arthritis, Rheumatoid
Effect of a cathepsin K inhibitor on arthritis and bone mineral density in ovariectomized rats with collagen-induced arthritis.
Arthritis, Rheumatoid
Inhibition of cathepsin K reduces bone erosion, cartilage degradation and inflammation evoked by collagen-induced arthritis in mice.
Arthritis, Rheumatoid
Inhibition of cathepsin K with lysosomotropic macromolecular inhibitors.
Arthritis, Rheumatoid
KLF2 (kruppel like factor 2 [lung]) regulates osteoclastogenesis by modulating autophagy.
Arthritis, Rheumatoid
Myricetin ameliorates the symptoms of collagen-induced arthritis in mice by inhibiting cathepsin K activity.
Arthritis, Rheumatoid
Peptide aldehyde inhibitors of cathepsin K inhibit bone resorption both in vitro and in vivo.
Arthritis, Rheumatoid
Serum cathepsin K levels of patients with longstanding rheumatoid arthritis: correlation with radiological destruction.
Arthritis, Rheumatoid
The imbalance between osteoprotegerin and cathepsin K in the serum of patients with longstanding rheumatoid arthritis.
Arthritis, Rheumatoid
The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics.
Atherosclerosis
18F-FDG PET/MR-imaging in a Göttingen Minipig model of atherosclerosis: Correlations with histology and quantitative gene expression.
Atherosclerosis
Cathepsin cysteine proteases in cardiovascular disease.
Atherosclerosis
Cathepsin K inhibitors for osteoporosis and potential off-target effects.
Atherosclerosis
Cathepsin K: a unique collagenolytic cysteine peptidase.
Atherosclerosis
Cathepsin-K is a potential cardiovascular risk biomarker in prevalent hemodialysis patients.
Atherosclerosis
Detection of femtomole quantities of mature cathepsin K with zymography.
Atherosclerosis
Disruption of the cathepsin K gene reduces atherosclerosis progression and induces plaque fibrosis but accelerates macrophage foam cell formation.
Atherosclerosis
Expression of cathepsin K is regulated by shear stress in cultured endothelial cells and is increased in endothelium in human atherosclerosis.
Atherosclerosis
Extracellular cathepsin K exerts antimicrobial activity and is protective against chronic intestinal inflammation in mice.
Atherosclerosis
Gene profiling of cathepsin K deficiency in atherogenesis: profibrotic but lipogenic.
Atherosclerosis
Human macrophage foam cells degrade atherosclerotic plaques though cathepsin K mediated processes.
Atherosclerosis
Optical visualization of cathepsin K activity in atherosclerosis with a novel, protease-activatable fluorescence sensor.
Atherosclerosis
Role of cathepsin K in structural changes in brachiocephalic artery during progression of atherosclerosis in apoE-deficient mice.
Autoimmune Diseases
Cathepsin K-dependent toll-like receptor 9 signaling revealed in experimental arthritis.
Axial Spondyloarthritis
Sera of patients with axial spondyloarthritis (axSpA) enhance osteoclastogenic potential of monocytes isolated from healthy individuals.
Bone Diseases
Cathepsin K: a therapeutic target for bone diseases.
Bone Diseases
Circulating cathepsin K and cystatin C in patients with cancer related bone disease: clinical and therapeutic implications.
Bone Diseases
Evaluation of Dexamethasone-Induced Osteoporosis In Vivo Using Zebrafish Scales.
Bone Diseases
Inhibition of Osteoclast Differentiation by Ginsenoside Rg3 in RAW264.7 Cells via RANKL, JNK and p38 MAPK Pathways Through a Modulation of Cathepsin K: An In Silico and In Vitro Study.
Bone Diseases
Lessons from rare diseases of cartilage and bone.
Bone Diseases
New therapeutic agents for the treatment of bone diseases.
Bone Diseases
Osteopetrosis and osteoporosis: two sides of the same coin.
Bone Diseases, Metabolic
Differential turnover of cortical and trabecular bone in transgenic mice overexpressing cathepsin K.
Bone Diseases, Metabolic
Effects of ONO-5334, a novel orally-active inhibitor of cathepsin K, on bone metabolism.
Bone Diseases, Metabolic
Erosive arthritis in a patient with pycnodysostosis: an experiment of nature.
Bone Diseases, Metabolic
Odanacatib, a Cathepsin-K Inhibitor for Osteoporosis: A Two-Year Study in Postmenopausal Women With Low Bone Density.
Bone Diseases, Metabolic
Osteopenia due to enhanced cathepsin K release by BK channel ablation in osteoclasts.
Bone Diseases, Metabolic
Serum cathepsin K concentrations reflect osteoclastic activity in women with postmenopausal osteoporosis and patients with Paget's disease.
Bone Diseases, Metabolic
Serum Cathepsin K levels are not suitable to differentiate women with chronic bone disorders such as osteopenia and osteoporosis from healthy pre- and postmenopausal women.
Bone Diseases, Metabolic
The development and characterization of an ELISA specifically detecting the active form of cathepsin K.
Bone Resorption
(+)-Vitisin A inhibits osteoclast differentiation by preventing TRAF6 ubiquitination and TRAF6-TAK1 formation to suppress NFATc1 activation.
Bone Resorption
(-)-Epigallocatechin-3-gallate inhibits RANKL-induced osteoclastogenesis via downregulation of NFATc1 and suppression of HO-1-HMGB1-RAGE pathway.
Bone Resorption
A cytochemical assay for osteoclast cathepsin K activity.
Bone Resorption
A highly potent inhibitor of cathepsin K (relacatib) reduces biomarkers of bone resorption both in vitro and in an acute model of elevated bone turnover in vivo in monkeys.
Bone Resorption
A Mild Inhibition of Cathepsin K Paradoxically Stimulates the Resorptive Activity of Osteoclasts in Culture.
Bone Resorption
A nonsense mutation in the cathepsin K gene observed in a family with pycnodysostosis.
Bone Resorption
A novel approach to inhibit bone resorption: exosite inhibitors against cathepsin K.
Bone Resorption
A novel class of nonpeptidic biaryl inhibitors of human cathepsin K.
Bone Resorption
A phase 1 pooled PK/PD analysis of bone resorption biomarkers for odanacatib, a Cathepsin K inhibitor.
Bone Resorption
A potent small molecule, nonpeptide inhibitor of cathepsin K (SB 331750) prevents bone matrix resorption in the ovariectomized rat.
Bone Resorption
Abnormal bone architecture in mice expressing MyD88 in cells of the osteoclast lineage.
Bone Resorption
Accelerated turnover of metaphyseal trabecular bone in mice overexpressing cathepsin K.
Bone Resorption
Acid attack and cathepsin K in bone resorption around total hip replacement prosthesis.
Bone Resorption
Acidification of the osteoclastic resorption compartment provides insight into the coupling of bone formation to bone resorption.
Bone Resorption
Actin-binding protein coronin 1A controls osteoclastic bone resorption by regulating lysosomal secretion of cathepsin K.
Bone Resorption
Activation of the PGC-1?/NFATc-1 Pathway in Circulating Osteoclast Precursors Associated with Bone Destruction in Rheumatoid Arthritis.
Bone Resorption
Adenosine A2A receptor activation prevents wear particle-induced osteolysis.
Bone Resorption
Advances in the discovery of cathepsin K inhibitors on bone resorption.
Bone Resorption
Aging and menopause reprogram osteoclast precursors for aggressive bone resorption.
Bone Resorption
Altered Hematopoietic Stem Cell and Osteoclast Precursor Frequency in Cathepsin K Null Mice.
Bone Resorption
Ampelopsis brevipedunculata extract prevents bone loss by inhibiting osteoclastogenesis in vitro and in vivo.
Bone Resorption
An Ectosteric Inhibitor of Cathepsin K Inhibits Bone Resorption in Ovariectomized Mice.
Bone Resorption
An oral cathepsin K inhibitor ONO-5334 inhibits N-terminal and C-terminal collagen crosslinks in serum and urine at similar plasma concentrations in postmenopausal women.
Bone Resorption
Anthraquinone compounds from Morinda officinalis inhibit osteoclastic bone resorption in vitro.
Bone Resorption
Antibodies to Citrullinated Proteins (ACPA) Associate with Markers of Osteoclast Activation and Bone Destruction in the Bone Marrow of Patients with Rheumatoid Arthritis.
Bone Resorption
Antiosteoclastic activity of milk thistle extract after ovariectomy to suppress estrogen deficiency-induced osteoporosis.
Bone Resorption
Antiosteoporotic activity and constituents of Podocarpium podocarpum.
Bone Resorption
AP-1 and Mitf interact with NFATc1 to stimulate cathepsin K promoter activity in osteoclast precursors.
Bone Resorption
AP-1 stimulates the cathepsin K promoter in RAW 264.7 cells.
Bone Resorption
Associations of Serum Cathepsin K and Polymorphisms in CTSK Gene With Bone Mineral Density and Bone Metabolism Markers in Postmenopausal Chinese Women.
Bone Resorption
Augmented LPS responsiveness in type 1 diabetes-derived osteoclasts.
Bone Resorption
Autocrine and paracrine STIP1 signaling promote osteolytic bone metastasis in renal cell carcinoma.
Bone Resorption
Azanitrile Cathepsin K Inhibitors: Effects on Cell Toxicity, Osteoblast-Induced Mineralization and Osteoclast-Mediated Bone Resorption.
Bone Resorption
AZD8835 inhibits osteoclastogenesis and periodontitis-induced alveolar bone loss in rats.
Bone Resorption
Beneficial effect of 2'-acetylacteoside on ovariectomized mice via modulating the function of bone resorption.
Bone Resorption
Bicyclic peptidomimetic tetrahydrofuro[3,2-b]pyrrol-3-one and hexahydrofuro[3,2-b]pyridine-3-one based scaffolds: synthesis and cysteinyl proteinase inhibition.
Bone Resorption
Biosynthesis and processing of cathepsin K in cultured human osteoclasts.
Bone Resorption
Bone modeling and remodeling: potential as therapeutic targets for the treatment of osteoporosis.
Bone Resorption
Bone resorptive activity of human peripheral blood mononuclear cells after fusion with polyethylene glycol.
Bone Resorption
Boric acid inhibits alveolar bone loss in rat experimental periodontitis through diminished bone resorption and enhanced osteoblast formation.
Bone Resorption
Calcitonin-gene-related peptide stimulates stromal cell osteogenic differentiation and inhibits RANKL induced NF-kappaB activation, osteoclastogenesis and bone resorption.
Bone Resorption
Calcium/calmodulin-dependent kinase activity is required for efficient induction of osteoclast differentiation and bone resorption by receptor activator of nuclear factor kappa B ligand (RANKL).
Bone Resorption
cAMP-PKA signaling pathway regulates bone resorption mediated by processing of cathepsin K in cultured mouse osteoclasts.
Bone Resorption
Cannabinoid receptor 2 agonist prevents local and systemic inflammatory bone destruction in rheumatoid arthritis.
Bone Resorption
Cathepsin K activity-dependent regulation of osteoclast actin ring formation and bone resorption.
Bone Resorption
Cathepsin K and the design of inhibitors of cathepsin K.
Bone Resorption
Cathepsin K antisense oligodeoxynucleotide inhibits osteoclastic bone resorption.
Bone Resorption
Cathepsin K Controls Cortical Bone Formation by Degrading Periostin.
Bone Resorption
Cathepsin K Deficiency Ameliorates Systemic Lupus Erythematosus-like Manifestations in
Bone Resorption
Cathepsin K deficiency in mice induces structural and metabolic changes in the central nervous system that are associated with learning and memory deficits.
Bone Resorption
Cathepsin K in melanoma invasion.
Bone Resorption
Cathepsin K in treatment monitoring following intravenous zoledronic acid.
Bone Resorption
Cathepsin K inhibitor causes changes in crystallinity and crystal structure of newly-formed mandibular bone in rats.
Bone Resorption
Cathepsin K Inhibitor Regulates Inflammation and Bone Destruction in Experimentally Induced Rat Periapical Lesions.
Bone Resorption
Cathepsin K inhibitors for osteoporosis and potential off-target effects.
Bone Resorption
Cathepsin K Inhibitors for Osteoporosis: Biology, Potential Clinical Utility, and Lessons Learned.
Bone Resorption
Cathepsin K inhibitors prevent bone loss in estrogen-deficient rabbits.
Bone Resorption
Cathepsin K inhibitors: a novel target for osteoporosis therapy.
Bone Resorption
Cathepsin K knockout mice develop osteopetrosis due to a deficit in matrix degradation but not demineralization.
Bone Resorption
Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts.
Bone Resorption
Cathepsin K-deficient osteocytes prevent lactation-induced bone loss and parathyroid hormone suppression.
Bone Resorption
Cathepsin K-dependent toll-like receptor 9 signaling revealed in experimental arthritis.
Bone Resorption
Cathepsin K: a therapeutic target for bone diseases.
Bone Resorption
Cathepsin K: isolation and characterization of the murine cDNA and genomic sequence, the homologue of the human pycnodysostosis gene.
Bone Resorption
Cathepsin K: its skeletal actions and role as a therapeutic target in osteoporosis.
Bone Resorption
Cathepsin K: The Action in and Beyond Bone.
Bone Resorption
Cathepsin K: The association between Cathepsin K expression and sphenoid sinus invasion of pituitary adenomas.
Bone Resorption
Cbl-PI3K interaction regulates Cathepsin K secretion in osteoclasts.
Bone Resorption
CD147 promotes the formation of functional osteoclasts through NFATc1 signalling.
Bone Resorption
Cementocytes Express Receptor Activator of the Nuclear Factor Kappa-B Ligand in Response to Endodontic Infection in Mice.
Bone Resorption
Changes in micro-CT 3D bone parameters reflect effects of a potent cathepsin K inhibitor (SB-553484) on bone resorption and cortical bone formation in ovariectomized mice.
Bone Resorption
Characterization of mouse cathepsin K gene, the gene promoter, and the gene expression.
Bone Resorption
Chemerin Treatment Inhibits the Growth and Bone Invasion of Breast Cancer Cells.
Bone Resorption
Cherubism mice also deficient in c-Fos exhibit inflammatory bone destruction executed by macrophages that express MMP14 despite the absence of TRAP+ osteoclasts.
Bone Resorption
Chloroquine ameliorates bone loss induced by d-galactose in male rats via inhibition of ERK associated osteoclastogenesis and antioxidant effect.
Bone Resorption
Chondroitin sulfate promotes activation of cathepsin K.
Bone Resorption
Chronic Psychosocial Stress Impairs Bone Homeostasis: A Study in the Social Isolation Reared Rat.
Bone Resorption
Clinical disorders of bone resorption.
Bone Resorption
Cloning and expression of rhesus monkey cathepsin K.
Bone Resorption
Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate.
Bone Resorption
Comparison in localization between cystatin C and cathepsin K in osteoclasts and other cells in mouse tibia epiphysis by immunolight and immunoelectron microscopy.
Bone Resorption
Conjugated linoleic acid inhibits osteoclast differentiation of RAW264.7 cells by modulating RANKL signaling.
Bone Resorption
Coumarin Ameliorates Impaired Bone Turnover by Inhibiting the Formation of Advanced Glycation End Products in Diabetic Osteoblasts and Osteoclasts.
Bone Resorption
Craniosynostosis in pycnodysostosis: broadening the spectrum of the cranial flat bone abnormalities.
Bone Resorption
Cystatin B as an intracellular modulator of bone resorption.
Bone Resorption
Cysteine proteinase cathepsin K mRNA is expressed in synovium of patients with rheumatoid arthritis and is detected at sites of synovial bone destruction.
Bone Resorption
Design and synthesis of tri-ring P3 benzamide-containing aminonitriles as potent, selective, orally effective inhibitors of cathepsin K.
Bone Resorption
Design of cathepsin k inhibitors for osteoporosis.
Bone Resorption
Determination of bone markers in pycnodysostosis: effects of cathepsin K deficiency on bone matrix degradation.
Bone Resorption
Diclofenac sodium inhibits NFkappaB transcription in osteoclasts.
Bone Resorption
Different cysteine proteinases involved in bone resorption and osteoclast formation.
Bone Resorption
Differential turnover of cortical and trabecular bone in transgenic mice overexpressing cathepsin K.
Bone Resorption
Direct stimulation of osteoclastic bone resorption by bone morphogenetic protein (BMP)-2 and expression of BMP receptors in mature osteoclasts.
Bone Resorption
Discovery of a New Class of Cathepsin K Inhibitors in Rhizoma Drynariae as Potential Candidates for the Treatment of Osteoporosis.
Bone Resorption
Disruption of the Man-6-P Targeting Pathway in Mice Impairs Osteoclast Secretory Lysosome Biogenesis.
Bone Resorption
Distinct roles of cathepsin K and cathepsin L in osteoclastic bone resorption.
Bone Resorption
Drynariae Rhizoma promotes osteoblast differentiation and mineralization in MC3T3-E1 cells through regulation of bone morphogenetic protein-2, alkaline phosphatase, type I collagen and collagenase-1.
Bone Resorption
Effect of cathepsin K inhibitors on bone resorption.
Bone Resorption
Effect of nonsurgical periodontal therapy on crevicular fluid levels of Cathepsin K in periodontitis.
Bone Resorption
Effect of novel N-cyano-tetrahydro-pyridazine compounds, a class of cathepsin K inhibitors, on the bone resorptive activity of mature osteoclasts.
Bone Resorption
Effect of the cathepsin K inhibitor odanacatib administered once weekly on bone mineral density in Japanese patients with osteoporosis-a double-blind, randomized, dose-finding study.
Bone Resorption
Effect of the Cathepsin K Inhibitor Odanacatib on Bone Resorption Biomarkers in Healthy Postmenopausal Women: Two Double-Blind, Randomized, Placebo-Controlled Phase I Studies.
Bone Resorption
Effects and interaction of icariin, curculigoside, and berberine in er-xian decoction, a traditional chinese medicinal formula, on osteoclastic bone resorption.
Bone Resorption
Effects of 9cis,11trans and 10trans,12cis CLA on osteoclast formation and activity from human CD14+ monocytes.
Bone Resorption
Effects of angiotensin II type I receptor blocker losartan on orthodontic tooth movement.
Bone Resorption
Effects of novel cathepsin K inhibitor ONO-5334 on bone resorption markers: a study of four sustained release formulations with different pharmacokinetic patterns.
Bone Resorption
Effects of Odanacatib on the Radius and Tibia of Postmenopausal Women: Improvements in Bone Geometry, Microarchitecture and Estimated Bone Strength.
Bone Resorption
Efficacy of a cathepsin K inhibitor in a preclinical model for prevention and treatment of breast cancer bone metastasis.
Bone Resorption
Emerging and potential therapies for osteoporosis.
Bone Resorption
Emerging pharmacologic therapies for osteoporosis.
Bone Resorption
Emerging Therapies for Osteoporosis.
Bone Resorption
Erosive arthritis in a patient with pycnodysostosis: an experiment of nature.
Bone Resorption
Established and forthcoming drugs for the treatment of osteoporosis.
Bone Resorption
Evaluation of Dexamethasone-Induced Osteoporosis In Vivo Using Zebrafish Scales.
Bone Resorption
Everolimus suppresses cancellous bone loss, bone resorption, and cathepsin K expression by osteoclasts.
Bone Resorption
Expression and regulation of cathepsin K in skin fibroblasts.
Bone Resorption
Expression of bone resorption genes in osteoarthritis and in osteoporosis.
Bone Resorption
Expression of matrix-degrading cysteine proteinase cathepsin K in cholesteatoma.
Bone Resorption
Expression of the proteinase specialized in bone resorption, cathepsin K, in granulomatous inflammation.
Bone Resorption
Expression, maturation, and rhodamine-based fluorescence assay of human cathepsin K expressed in CHO cells.
Bone Resorption
Extracellular cathepsin K exerts antimicrobial activity and is protective against chronic intestinal inflammation in mice.
Bone Resorption
Extract of Magnoliae Flos inhibits ovariectomy-induced osteoporosis by blocking osteoclastogenesis and reducing osteoclast-mediated bone resorption.
Bone Resorption
Female estrogen receptor beta-/- mice are partially protected against age-related trabecular bone loss.
Bone Resorption
Fisetin Inhibits Osteoclast Differentiation via Downregulation of p38 and c-Fos-NFATc1 Signaling Pathways.
Bone Resorption
Fluoride decreased osteoclastic bone resorption through the inhibition of NFATc1 gene expression.
Bone Resorption
Fumitremorgin C Attenuates Osteoclast Formation and Function via Suppressing RANKL-Induced Signaling Pathways.
Bone Resorption
Functions of cathepsin K in bone resorption. Lessons from cathepsin K deficient mice.
Bone Resorption
Future directions for new medical entities in osteoporosis.
Bone Resorption
Future of anticathepsin K drugs: dual therapy for skeletal disease and atherosclerosis?
Bone Resorption
Genomic organization and chromosome localization of the human cathepsin K gene (CTSK).
Bone Resorption
High bone mineral density in pycnodysostotic patients with a novel mutation in the propeptide of cathepsin K.
Bone Resorption
High cathepsin K levels in men with differentiated thyroid cancer on suppressive L-thyroxine therapy.
Bone Resorption
High glucose downregulates the effects of autophagy on osteoclastogenesis via the AMPK/mTOR/ULK1 pathway.
Bone Resorption
Histochemical examination of systemic administration of eldecalcitol combined with guided bone regeneration for bone defect restoration in rats.
Bone Resorption
Histone deacetylases 1 and 2 inhibition suppresses cytokine production and osteoclast bone resorption in vitro.
Bone Resorption
HIV-1 replicates in human osteoclasts and enhances their differentiation in vitro.
Bone Resorption
Human Alternative Macrophages Populate Calcified Areas of Atherosclerotic Lesions and Display Impaired RANKL-Induced Osteoclastic Bone Resorption Activity.
Bone Resorption
Human breast adenocarcinoma (MDA-231) and human lung squamous cell carcinoma (Hara) do not have the ability to cause bone resorption by themselves during the establishment of bone metastasis.
Bone Resorption
Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme.
Bone Resorption
Human circulating monocytes can express receptor activator of nuclear factor-kappaB ligand and differentiate into functional osteoclasts without exogenous stimulation.
Bone Resorption
Human macrophage foam cells degrade atherosclerotic plaques though cathepsin K mediated processes.
Bone Resorption
Human osteoclast cathepsin K is processed intracellularly prior to attachment and bone resorption.
Bone Resorption
Identification of a nonbasic, nitrile-containing cathepsin K inhibitor (MK-1256) that is efficacious in a monkey model of osteoporosis.
Bone Resorption
Identification of angiogenin as the osteoclastic bone resorption-inhibitory factor in bovine milk.
Bone Resorption
Identification of NFAT binding sites that mediate stimulation of cathepsin K promoter activity by RANK ligand.
Bone Resorption
IL-17A suppresses the expression of bone resorption-related proteinases and osteoclast differentiation via IL-17RA or IL-17RC receptors in RAW264.7 cells.
Bone Resorption
IL-1alpha stimulates cathepsin K expression in osteoclasts via the tyrosine kinase-NF-kappaB pathway.
Bone Resorption
IL-37 inhibits lipopolysaccharide-induced osteoclast formation and bone resorption in vivo.
Bone Resorption
Impaired 1,25 dihydroxyvitamin D3 action and hypophosphatemia underlie the altered lacuno-canalicular remodeling observed in the Hyp mouse model of XLH.
Bone Resorption
Impaired bone resorption in cathepsin K-deficient mice is partially compensated for by enhanced osteoclastogenesis and increased expression of other proteases via an increased RANKL/OPG ratio.
Bone Resorption
Impaired osteoclast homeostasis in the cystatin B-deficient mouse model of progressive myoclonus epilepsy.
Bone Resorption
Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice.
Bone Resorption
In situ hybridization for matrix metalloproteinase-1 and cathepsin K in rat root-resorbing tissue induced by tooth movement.
Bone Resorption
In vitro and in vivo assessment of the proresolutive and antiresorptive actions of resolvin D1: relevance to arthritis.
Bone Resorption
Inactivation of autophagy ameliorates glucocorticoid-induced and ovariectomy-induced bone loss.
Bone Resorption
Increase in osteoclastogenesis in an obese Otsuka Long-Evans Tokushima fatty rat model.
Bone Resorption
Increased expression of the receptor for activation of NF-kappaB and decreased runt-related transcription factor 2 expression in bone of rats with streptozotocin-induced diabetes.
Bone Resorption
Increased numbers of osteoclasts expressing cysteine proteinase cathepsin K in patients with infected osteoradionecrosis and bisphosphonate-associated osteonecrosis-a paradoxical observation?
Bone Resorption
Inhibiting periapical lesions through AAV-RNAi silencing of cathepsin K.
Bone Resorption
Inhibition of bone resorption by the cathepsin K inhibitor odanacatib is fully reversible.
Bone Resorption
Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid.
Bone Resorption
Inhibition of cathepsin k for treatment of osteoporosis.
Bone Resorption
Inhibition of cathepsin K--a novel approach to antiresorptive therapy.
Bone Resorption
Inhibition of Drynariae Rhizoma extracts on bone resorption mediated by processing of cathepsin K in cultured mouse osteoclasts.
Bone Resorption
Inhibition of osteoclast differentiation and bone resorption by cathepsin K antisense oligonucleotides.
Bone Resorption
Inhibition of osteoclast differentiation and bone resorption by N-methylpyrrolidone.
Bone Resorption
Inhibition of Osteoclast Differentiation by Ginsenoside Rg3 in RAW264.7 Cells via RANKL, JNK and p38 MAPK Pathways Through a Modulation of Cathepsin K: An In Silico and In Vitro Study.
Bone Resorption
Inhibition of Ulmus davidiana Planch (Ulmaceae) on bone resorption mediated by processing of Cathepsin K in cultured mouse osteoclasts.
Bone Resorption
Inhibitors of cathepsin K: a patent review (2004 - 2010).
Bone Resorption
Inhibitory Effect of Cudratrixanthone U on RANKL-Induced Osteoclast Differentiation and Function in Macrophages and BMM Cells.
Bone Resorption
Inhibitory Effects of 2N1HIA (2-(3-(2-Fluoro-4-Methoxyphenyl)-6-Oxo-1(6H)-Pyridazinyl)-N-1H-Indol-5-Ylacetamide) on Osteoclast Differentiation via Suppressing Cathepsin K Expression.
Bone Resorption
Interferon-gamma down-regulates gene expression of cathepsin K in osteoclasts and inhibits osteoclast formation.
Bone Resorption
Interleukin-1? promotes the LC3-mediated secretory function of osteoclast precursors by stimulating the Ca²?-dependent activation of ERK.
Bone Resorption
Interventional value of total flavonoids from Rhizoma Drynariae on Cathepsin K, a potential target of osteoporosis.
Bone Resorption
Intracellular membrane trafficking pathways in bone-resorbing osteoclasts revealed by cloning and subcellular localization studies of small GTP-binding rab proteins.
Bone Resorption
Irp2 Knockout Causes Osteoporosis by Inhibition of Bone Remodeling.
Bone Resorption
Isorhamnetin 3-O-neohesperidoside promotes the resorption of crown-covered bone during tooth eruption by osteoclastogenesis.
Bone Resorption
JiangTang XiaoKe granule attenuates cathepsin K expression and improves IGF-1 expression in the bone of high fat diet induced KK-Ay diabetic mice.
Bone Resorption
Ketoamide-based inhibitors of cysteine protease, cathepsin K: P3 modifications.
Bone Resorption
Lanthanum Chloride Attenuates Osteoclast Formation and Function Via the Downregulation of Rankl-Induced Nf-?b and Nfatc1 Activities.
Bone Resorption
LDC000067 suppresses RANKL-induced osteoclastogenesis in vitro and prevents LPS-induced osteolysis in vivo.
Bone Resorption
Lessons from rare diseases of cartilage and bone.
Bone Resorption
Localization of rat cathepsin K in osteoclasts and resorption pits: inhibition of bone resorption and cathepsin K-activity by peptidyl vinyl sulfones.
Bone Resorption
Loss of Protein Kinase C-? Protects against LPS-Induced Osteolysis Owing to an Intrinsic Defect in Osteoclastic Bone Resorption.
Bone Resorption
Low bone turnover and reduced angiogenesis in streptozotocin-induced osteoporotic mice.
Bone Resorption
Low concentrations of alendronate increase the local invasive potential of osteoblastic sarcoma cell lines via connexin 43 activation.
Bone Resorption
Low-dose prednisolone in early rheumatoid arthritis inhibits collagen type I degradation by matrix metalloproteinases as assessed by serum 1CTP--a possible mechanism for specific inhibition of radiological destruction.
Bone Resorption
Low-intensity pulsed ultrasound protects subchondral bone in rabbit temporomandibular joint osteoarthritis by suppressing TGF-?1/Smad3 pathway.
Bone Resorption
Lysosomotropism of basic cathepsin K inhibitors contributes to increased cellular potencies against off-target cathepsins and reduced functional selectivity.
Bone Resorption
Matrix metalloproteinases (MMP) and cathepsin K contribute differently to osteoclastic activities.
Bone Resorption
MCP-1-induced human osteoclast-like cells are tartrate-resistant acid phosphatase, NFATc1, and calcitonin receptor-positive but require receptor activator of NFkappaB ligand for bone resorption.
Bone Resorption
Metabolic properties of the osteoclast.
Bone Resorption
Mineral trioxide aggregate inhibits osteoclastic bone resorption.
Bone Resorption
Molecular and cellular basis of bone resorption.
Bone Resorption
Molecular changes in Articular Cartilage and Subchondral Bone in the Rat Anterior Cruciate Ligament Transection and Meniscectomized Models of Osteoarthritis.
Bone Resorption
Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone.
Bone Resorption
Molecular mechanisms underlying osteoclast formation and activation.
Bone Resorption
Monocyte proliferation and differentiation to osteoclasts is affected by density of collagen covalently bound to a poly(dimethyl siloxane) culture surface.
Bone Resorption
Morning vs evening dosing of the cathepsin K inhibitor ONO-5334: effects on bone resorption in postmenopausal women in a randomized, phase 1 trial.
Bone Resorption
Multiple Fractures and Impaired Bone Fracture Healing in a Patient with Pycnodysostosis and Hypophosphatasia.
Bone Resorption
Muramyl dipeptide enhances lipopolysaccharide-induced osteoclast formation and bone resorption through increased RANKL expression in stromal cells.
Bone Resorption
Mutations of CTSK result in pycnodysostosis via a reduction in cathepsin K protein.
Bone Resorption
N-Acetylcysteine Attenuates Lipopolysaccharide-Induced Osteolysis by Restoring Bone Remodeling Balance via Reduction of Reactive Oxygen Species Formation During Osteoclastogenesis.
Bone Resorption
Natural inhibitors targeting osteoclast-mediated bone resorption.
Bone Resorption
Neohesperidin suppresses osteoclast differentiation, bone resorption and ovariectomised-induced osteoporosis in mice.
Bone Resorption
New insights into the regulation of cathepsin K gene expression by osteoprotegerin ligand.
Bone Resorption
New insights into treatment of osteoporosis in postmenopausal women.
Bone Resorption
New targets for intervention in the treatment of postmenopausal osteoporosis.
Bone Resorption
New treatment targets in osteoporosis.
Bone Resorption
Nicotine affects bone resorption and suppresses the expression of cathepsin K, MMP-9 and vacuolar-type H(+)-ATPase d2 and actin organization in osteoclasts.
Bone Resorption
Nirogacestat suppresses RANKL-Induced osteoclast formation in vitro and attenuates LPS-Induced bone resorption in vivo.
Bone Resorption
Non-covalent cathepsin k inhibitors for the treatment of osteoporosis.
Bone Resorption
Nonclinical and clinical pharmacological characterization of the potent and selective cathepsin K inhibitor MIV-711.
Bone Resorption
Novel anti-cancer strategy in bone tumors by targeting molecular and cellular modulators of bone resorption.
Bone Resorption
Novel biological markers of bone: from bone metabolism to bone physiology.
Bone Resorption
Novel route to the synthesis of peptides containing 2-amino-1'-hydroxymethyl ketones and their application as cathepsin K inhibitors.
Bone Resorption
Obesity-mediated inflammatory microenvironment stimulates osteoclastogenesis and bone loss in mice.
Bone Resorption
Odanacatib for the treatment of osteoporosis.
Bone Resorption
Odanacatib for the treatment of postmenopausal osteoporosis: results of the LOFT multicentre, randomised, double-blind, placebo-controlled trial and LOFT Extension study.
Bone Resorption
Odanacatib in postmenopausal women with low bone mineral density: a review of current clinical evidence.
Bone Resorption
Odanacatib in the treatment of postmenopausal women with low bone mineral density: Three-year continued therapy and resolution of effect.
Bone Resorption
Odanacatib, a cathepsin K inhibitor for the treatment of osteoporosis and other skeletal disorders associated with excessive bone remodeling.
Bone Resorption
Odanacatib, a Cathepsin-K Inhibitor for Osteoporosis: A Two-Year Study in Postmenopausal Women With Low Bone Density.
Bone Resorption
Odanacatib, a new drug for the treatment of osteoporosis: review of the results in postmenopausal women.
Bone Resorption
Odanacatib, effects of 16-month treatment and discontinuation of therapy on bone mass, turnover and strength in the ovariectomized rabbit model of osteopenia.
Bone Resorption
Odanacatib: an emerging novel treatment alternative for postmenopausal osteoporosis.
Bone Resorption
Optimized transfection of diced siRNA into mature primary human osteoclasts: inhibition of cathepsin K mediated bone resorption by siRNA.
Bone Resorption
Osseointegration and foreign body reaction: Titanium implants activate the immune system and suppress bone resorption during the first 4 weeks after implantation.
Bone Resorption
Osteoclast precursors acquire sensitivity to breast cancer derived factors early in differentiation.
Bone Resorption
Osteoclast-specific cathepsin K deletion stimulates S1P-dependent bone formation.
Bone Resorption
Osteoclastic bone degradation and the role of different cysteine proteinases and matrix metalloproteinases: differences between calvaria and long bone.
Bone Resorption
Osteoclasts from patients with autosomal dominant osteopetrosis type I caused by a T253I mutation in low-density lipoprotein receptor-related protein 5 are normal in vitro, but have decreased resorption capacity in vivo.
Bone Resorption
Osteogenic activity of yellow flag iris (Iris pseudacorus) extract modulating differentiation of osteoblasts and osteoclasts.
Bone Resorption
Osteopenia due to enhanced cathepsin K release by BK channel ablation in osteoclasts.
Bone Resorption
Osteoprotegerin differentially regulates protease expression in osteoclast cultures.
Bone Resorption
Overexpression of cathepsin K accelerates the resorption cycle and osteoblast differentiation in vitro.
Bone Resorption
Pain prediction by serum biomarkers of bone turnover in people with knee osteoarthritis: an observational study of TRAcP5b and cathepsin K in OA.
Bone Resorption
Peptide aldehyde inhibitors of cathepsin K inhibit bone resorption both in vitro and in vivo.
Bone Resorption
Peptidic 1-cyanopyrrolidines: synthesis and SAR of a series of potent, selective cathepsin inhibitors.
Bone Resorption
Peptidomimetic inhibitors of cathepsin K.
Bone Resorption
Pharmacokinetics and bone resorption evaluation of a novel Cathepsin K inhibitor (VEL-0230) in healthy adult horses.
Bone Resorption
Pharmacological topics of bone metabolism: recent advances in pharmacological management of osteoporosis.
Bone Resorption
PKC? deficiency perturbs bone homeostasis by selective uncoupling of cathepsin K secretion and ruffled border formation in osteoclasts.
Bone Resorption
Potent and selective cathepsin L inhibitors do not inhibit human osteoclast resorption in vitro.
Bone Resorption
Potent and selective inhibition of human cathepsin K leads to inhibition of bone resorption in vivo in a nonhuman primate.
Bone Resorption
Potent and selective ketoamide-based inhibitors of cysteine protease, cathepsin K.
Bone Resorption
Potent dipeptidylketone inhibitors of the cysteine protease cathepsin K.
Bone Resorption
Potential role of cathepsin K in the pathophysiology of mucopolysaccharidoses.
Bone Resorption
Potential role of odanacatib in the treatment of osteoporosis.
Bone Resorption
PP121 suppresses RANKL-Induced osteoclast formation in vitro and LPS-Induced bone resorption in vivo.
Bone Resorption
Preclinical evaluation of zoledronate using an in vitro mimetic cellular model for breast cancer metastatic bone disease.
Bone Resorption
Present and future pharmacotherapy for osteoporosis.
Bone Resorption
Preservation of type H vessels and osteoblasts by enhanced preosteoclast platelet-derived growth factor type BB attenuates glucocorticoid-induced osteoporosis in growing mice.
Bone Resorption
Prevalent and Emerging Therapies for Osteoporosis.
Bone Resorption
Preventive Effects of Chrysanthemum coronarium L. Extract on Bone Metabolism In Vitro and In Vivo.
Bone Resorption
Pristimerin Suppresses RANKL-Induced Osteoclastogenesis and Ameliorates Ovariectomy-Induced Bone Loss.
Bone Resorption
Protective Effect of Acteoside on Ovariectomy-Induced Bone Loss in Mice.
Bone Resorption
Proteolysis of human bone collagen by cathepsin K: characterization of the cleavage sites generating by cross-linked N-telopeptide neoepitope.
Bone Resorption
Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification.
Bone Resorption
Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency.
Bone Resorption
Pycnodysostosis- a rare disorder with distinctive craniofacial dysmorphia. A case report.
Bone Resorption
Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease.
Bone Resorption
Quantification of the expression levels of lysosomal cysteine proteinases in purified human osteoclastic cells by competitive RT-PCR.
Bone Resorption
Radiation alters osteoclastogenesis by regulating the cytoskeleton and lytic enzymes in RAW 264.7 cells and mouse bone marrow-derived macrophages.
Bone Resorption
RANK ligand and interferon gamma differentially regulate cathepsin gene expression in pre-osteoclastic cells.
Bone Resorption
RANKL and cathepsin K in diffuse sclerosing osteomyelitis of the mandible.
Bone Resorption
Regulation and enzymatic basis of bone resorption by human osteoclasts.
Bone Resorption
Regulation of collagenolytic cysteine protease synthesis by estrogen in osteoclasts.
Bone Resorption
Regulatory mechanism of NFATc1 in RANKL-induced osteoclast activation.
Bone Resorption
Regulatory properties of vitronectin and its glycosylation in collagen fibril formation and collagen-degrading enzyme cathepsin K activity.
Bone Resorption
Relation of Bone Mineral Density with Homocysteine and Cathepsin K levels in Postmenopausal Women.
Bone Resorption
Relevance of an in vitro osteoclastogenesis system to study receptor activator of NF-kB ligand and osteoprotegerin biological activities.
Bone Resorption
Repeated oral administration of a cathepsin K inhibitor significantly suppresses bone resorption in exercising horses with evidence of increased bone formation and maintained bone turnover.
Bone Resorption
Resveratrol inhibits myeloma cell growth, prevents osteoclast formation, and promotes osteoblast differentiation.
Bone Resorption
Retinoic acid induces two osteocalcin isoforms and inhibits markers of osteoclast activity in Atlantic cod (Gadus morhua) ex vivo cultured craniofacial tissues.
Bone Resorption
Role of cathepsin K in normal joints and in the development of arthritis.
Bone Resorption
Role of cathepsin K in the turnover of the dermal extracellular matrix during scar formation.
Bone Resorption
Role of NOD1 polymorphism in susceptibility and clinical progression of rheumatoid arthritis.
Bone Resorption
Role of odanacatib in reducing bone loss due to endodontic disease: An overview.
Bone Resorption
Scutellarin inhibits RANKL-mediated osteoclastogenesis and titanium particle-induced osteolysis via suppression of NF-?B and MAPK signaling pathway.
Bone Resorption
Serum and Urine Bone Resorption Markers and Pharmacokinetics of Cathepsin K Inhibitor ONO-5334 after Ascending Single Doses in Post-menopausal Women.
Bone Resorption
Serum Cathepsin K levels are not suitable to differentiate women with chronic bone disorders such as osteopenia and osteoporosis from healthy pre- and postmenopausal women.
Bone Resorption
Serum levels of cathepsin K decrease with age in both women and men.
Bone Resorption
Silencing of Ac45 Simultaneously Inhibits Osteoclast-Mediated Bone Resorption and Attenuates Dendritic Cell-Mediated Inflammation through Impairing Acidification and Cathepsin K Secretion.
Bone Resorption
Species differences between human and rat in the substrate specificity of cathepsin k.
Bone Resorption
Structure activity relationships of 5-, 6-, and 7-methyl-substituted azepan-3-one cathepsin K inhibitors.
Bone Resorption
Structure and chromosomal assignment of the human cathepsin K gene.
Bone Resorption
Study of immunoelectron microscopic localization of cathepsin K in osteoclasts and other bone cells in the mouse femur.
Bone Resorption
Substance P modulates bone remodeling properties of murine osteoblasts and osteoclasts.
Bone Resorption
Synovial tissue in rheumatoid arthritis is a source of osteoclast differentiation factor.
Bone Resorption
Synthesis and evaluation of cis-hexahydropyrrolo[3,2-b]pyrrol-3-one peptidomimetic inhibitors of CAC1 cysteinyl proteinases.
Bone Resorption
The Actin-Binding Protein Cofilin and Its Interaction With Cortactin Are Required for Podosome Patterning in Osteoclasts and Bone Resorption In Vivo and In Vitro.
Bone Resorption
The cathepsin K inhibitor odanacatib suppresses bone resorption in women with breast cancer and established bone metastases: results of a 4-week, double-blind, randomized, controlled trial.
Bone Resorption
The collagenolytic activity of cathepsin K is unique among mammalian proteinases.
Bone Resorption
The crystal structure of human procathepsin K.
Bone Resorption
The development and characterization of an ELISA specifically detecting the active form of cathepsin K.
Bone Resorption
The effect of molecules in mother-of-pearl on the decrease in bone resorption through the inhibition of osteoclast cathepsin K.
Bone Resorption
The effects of the cathepsin K inhibitor odanacatib on osteoclastic bone resorption and vesicular trafficking.
Bone Resorption
The expression of Clcn7 and Ostm1 in osteoclasts is coregulated by microphthalmia transcription factor.
Bone Resorption
The Future of Cysteine Cathepsins in Disease Management.
Bone Resorption
The future of osteoporosis treatment - a research update.
Bone Resorption
The inhibition of subchondral bone resorption in the early phase of experimental dog osteoarthritis by licofelone is associated with a reduction in the synthesis of MMP-13 and cathepsin K.
Bone Resorption
The Inhibitory Effect of Alisol A 24-Acetate from Alisma canaliculatum on Osteoclastogenesis.
Bone Resorption
The mouse osteopetrotic grey-lethal mutation induces a defect in osteoclast maturation/function.
Bone Resorption
The new partnership of genomics and chemistry for accelerated drug development.
Bone Resorption
The prenyl group contributes to activities of phytoestrogen 8-prenynaringenin in enhancing bone formation and inhibiting bone resorption in vitro.
Bone Resorption
The regulation of bone resorption in tooth formation and eruption processes in mouse alveolar crest devoid of cathepsin k.
Bone Resorption
The regulation of cathepsin K gene expression.
Bone Resorption
The resorptive apparatus of osteoclasts supports lysosomotropism and increases potency of basic versus non-basic inhibitors of cathepsin K.
Bone Resorption
The role of cathepsin K in normal bone resorption.
Bone Resorption
The role of cathepsin K in oral and maxillofacial disorders.
Bone Resorption
Thickened skull, scoliosis and other skeletal findings in Unverricht-Lundborg disease link cystatin B function to bone metabolism.
Bone Resorption
Thyroid-stimulating hormone maintains bone mass and strength by suppressing osteoclast differentiation.
Bone Resorption
Transforming growth factor-beta controls human osteoclastogenesis through the p38 MAPK and regulation of RANK expression.
Bone Resorption
Transmembrane protein 173 inhibits RANKL-induced osteoclast differentiation.
Bone Resorption
Treatment with a Potent Cathepsin K Inhibitor Preserves Cortical and Trabecular Bone Mass in Ovariectomized Monkeys.
Bone Resorption
Use of papain as a model for the structure-based design of cathepsin K inhibitors: crystal structures of two papain-inhibitor complexes demonstrate binding to S'-subsites.
Bone Resorption
Virtual screening of cathepsin k inhibitors using docking and pharmacophore models.
Bone Resorption
[Advances treatment of osteoporosis: new molecules, new strategies].
Bone Resorption
[Biological therapy for osteoporosis].
Bone Resorption
[Bone and bone related biochemical examinations. Bone and collagen related metabolites. Urinary and serum NTX as bone resorption markers]
Bone Resorption
[Bone remodeling: new therapeutic approaches]
Bone Resorption
[Cathepsin K and matrix metalloproteases activity in the bone tissue of OXYS rats with developing osteoporosis].
Bone Resorption
[New anti-osteoporotic drugs under development].
Bone Resorption
[Odanacatib (MK-0822)].
Bone Resorption
[Osteoporosis].
Bone Resorption
[Potential mechanism of transcription factor peroxisome proliferator-activated receptor-gamma coactivator-1 beta on promoting osteoclastogenesis].
Bone Resorption
[Reducing bone resorption by cathepsin K inhibitor and treatment of osteoporosis].
Bone Resorption
[Regulation of bone metabolism in osteoporosis : novel drugs for osteoporosis in development].
Bowen's Disease
Cathepsin K expression in basal cell carcinoma.
Breast Neoplasms
A cathepsin K inhibitor reduces breast cancer induced osteolysis and skeletal tumor burden.
Breast Neoplasms
A novel derivative of artemisinin inhibits cell proliferation and metastasis via down-regulation of cathepsin K in breast cancer.
Breast Neoplasms
Anti-IL-20 monoclonal antibody suppresses breast cancer progression and bone osteolysis in murine models.
Breast Neoplasms
Artemisinin inhibits breast cancer-induced osteolysis by inhibiting osteoclast formation and breast cancer cell proliferation.
Breast Neoplasms
Cathepsin K induces platelet dysfunction and affects cell signaling in breast cancer - molecularly distinct behavior of cathepsin K in breast cancer.
Breast Neoplasms
Cathepsin K regulates localization and secretion of Tartrate-Resistant Acid Phosphatase (TRAP) in TRAP-overexpressing MDA-MB-231 breast cancer cells.
Breast Neoplasms
Circulating cathepsin K and cystatin C in patients with cancer related bone disease: clinical and therapeutic implications.
Breast Neoplasms
Efficacy of a cathepsin K inhibitor in a preclinical model for prevention and treatment of breast cancer bone metastasis.
Breast Neoplasms
Epithelial and stromal cathepsin K and CXCL14 expression in breast tumor progression.
Breast Neoplasms
Hedgehog signaling induced by breast cancer cells promotes osteoclastogenesis and osteolysis.
Breast Neoplasms
Inhibition of osteoclast differentiation and bone resorption by cathepsin K antisense oligonucleotides.
Breast Neoplasms
Inhibitory effect of cathepsin K inhibitor (ODN-MK-0822) on invasion, migration and adhesion of human breast cancer cells in vitro.
Breast Neoplasms
Inhibitory Effects of Cathepsin K Inhibitor (ODN-MK-0822) on the Paracrine Pro-Osteoclast Factors of Breast Cancer Cells.
Breast Neoplasms
Obesity and Cathepsin K: A Complex Pathophysiological Relationship in Breast Cancer Metastases.
Breast Neoplasms
Serum interleukin-6 in patients with metastatic bone disease: correlation with cystatin C.
Breast Neoplasms
Simvastatin and MBCD Inhibit Breast Cancer-Induced Osteoclast Activity by Targeting Osteoclastogenic Factors.
Breast Neoplasms
The C-Terminal Intact Forms of Periostin (iPTN) Are Surrogate Markers for Osteolytic Lesions in Experimental Breast Cancer Bone Metastasis.
Breast Neoplasms
The cathepsin K inhibitor odanacatib suppresses bone resorption in women with breast cancer and established bone metastases: results of a 4-week, double-blind, randomized, controlled trial.
Breast Neoplasms
The osteoclast-associated protease cathepsin K is expressed in human breast carcinoma.
Bronchopulmonary Dysplasia
Cathepsin K deficiency aggravates lung injury in hyperoxia-exposed newborn mice.
Bronchopulmonary Dysplasia
Cathepsin K expression is diminished in infants with bronchopulmonary dysplasia.
Carcinogenesis
Proteins involved in cutaneous basal cell carcinoma development.
Carcinoma
A broad survey of cathepsin K immunoreactivity in human neoplasms.
Carcinoma
Basaloid squamous cell carcinoma of the maxillary sinus: Report of two cases in association with cathepsin K expression.
Carcinoma
Bone marrow-derived cathepsin K cleaves SPARC in bone metastasis.
Carcinoma
Cathepsin K (Clone EPR19992) Demonstrates Uniformly Positive Immunoreactivity in Renal Oncocytoma, Chromophobe Renal Cell Carcinoma, and Distal Tubules.
Carcinoma
Cathepsin K associates with lymph node metastasis and poor prognosis in oral squamous cell carcinoma.
Carcinoma
Cathepsin K expression in basal cell carcinoma.
Carcinoma
Cathepsin K expression in castration-resistant prostate carcinoma: a therapeutical target for patients at risk for bone metastases.
Carcinoma
Cathepsin K in the immunohistochemical diagnosis of melanocytic lesions.
Carcinoma
Cathepsin K inhibition-induced mitochondrial ROS enhances sensitivity of cancer cells to anti-cancer drugs through USP27x-mediated Bim protein stabilization.
Carcinoma
Cathepsin k is present in invasive oral tongue squamous cell carcinoma in vivo and in vitro.
Carcinoma
Cathepsin K is selectively expressed in the stroma of lung adenocarcinoma but not in bronchioloalveolar carcinoma. A useful marker of invasive growth.
Carcinoma
Cathepsin K modulates invasion, migration and adhesion of oral squamous cell carcinomas in vitro.
Carcinoma
Cathepsin K: A Novel Diagnostic and Predictive Biomarker for Renal Tumors.
Carcinoma
Cathepsin-K immunoreactivity distinguishes MiTF/TFE family renal translocation carcinomas from other renal carcinomas.
Carcinoma
Comprehensive analysis of 34 MiT family translocation renal cell carcinomas and review of the literature: investigating prognostic markers and therapy targets.
Carcinoma
Differential expression of cathepsin K in neoplasms harboring TFE3 gene fusions.
Carcinoma
Elevated Cathepsin K potentiates metastasis of epithelial ovarian cancer.
Carcinoma
Expression of cathepsins B, D and K in thymic epithelial tumours.
Carcinoma
Identification of Cathepsin K in the Peritoneal Metastasis of Ovarian Carcinoma Using In-silico, Gene Expression Analysis.
Carcinoma
Osteoclast-like giant cell rich carcinomas of the lung: a Clinicopathological, Immunohistochemical, and molecular study of three cases.
Carcinoma
Photoactivated inhibition of cathepsin K in a 3D tumor model.
Carcinoma
RNA sequencing of Xp11 translocation-associated cancers reveals novel gene fusions and distinctive clinicopathologic correlations.
Carcinoma
Stromal expression of cathepsin K in squamous cell carcinoma.
Carcinoma
TFE3 break-apart FISH has a higher sensitivity for Xp11.2 translocation-associated renal cell carcinoma compared with TFE3 or cathepsin K immunohistochemical staining alone: expanding the morphologic spectrum.
Carcinoma
The CD200-CD200R Axis Promotes Squamous Cell Carcinoma Metastasis via Regulation of Cathepsin K.
Carcinoma
VEGFA amplification/increased gene copy number and VEGFA mRNA expression in renal cell carcinoma with TFEB gene alterations.
Carcinoma, Basal Cell
Cathepsin K expression in basal cell carcinoma.
Carcinoma, Bronchogenic
Cathepsin K expression in human lung.
Carcinoma, Non-Small-Cell Lung
Serum cathepsin K and cystatin C concentration in patients with advanced non-small-cell lung cancer during chemotherapy.
Carcinoma, Non-Small-Cell Lung
The Potential Role of Cathepsin K in Non-Small Cell Lung Cancer.
Carcinoma, Ovarian Epithelial
Elevated Cathepsin K potentiates metastasis of epithelial ovarian cancer.
Carcinoma, Renal Cell
A broad survey of cathepsin K immunoreactivity in human neoplasms.
Carcinoma, Renal Cell
Cathepsin K (Clone EPR19992) Demonstrates Uniformly Positive Immunoreactivity in Renal Oncocytoma, Chromophobe Renal Cell Carcinoma, and Distal Tubules.
Carcinoma, Renal Cell
Cathepsin K in the immunohistochemical diagnosis of melanocytic lesions.
Carcinoma, Renal Cell
Cathepsin K: A Novel Diagnostic and Predictive Biomarker for Renal Tumors.
Carcinoma, Renal Cell
Cathepsin-K immunoreactivity distinguishes MiTF/TFE family renal translocation carcinomas from other renal carcinomas.
Carcinoma, Renal Cell
Comprehensive analysis of 34 MiT family translocation renal cell carcinomas and review of the literature: investigating prognostic markers and therapy targets.
Carcinoma, Renal Cell
Differential expression of cathepsin K in neoplasms harboring TFE3 gene fusions.
Carcinoma, Renal Cell
RNA sequencing of Xp11 translocation-associated cancers reveals novel gene fusions and distinctive clinicopathologic correlations.
Carcinoma, Renal Cell
TFE3 break-apart FISH has a higher sensitivity for Xp11.2 translocation-associated renal cell carcinoma compared with TFE3 or cathepsin K immunohistochemical staining alone: expanding the morphologic spectrum.
Carcinoma, Renal Cell
VEGFA amplification/increased gene copy number and VEGFA mRNA expression in renal cell carcinoma with TFEB gene alterations.
Carcinoma, Squamous Cell
Basaloid squamous cell carcinoma of the maxillary sinus: Report of two cases in association with cathepsin K expression.
Carcinoma, Squamous Cell
Cathepsin K expression in basal cell carcinoma.
Carcinoma, Squamous Cell
Cathepsin k is present in invasive oral tongue squamous cell carcinoma in vivo and in vitro.
Carcinoma, Squamous Cell
Expression of cathepsins B, D and K in thymic epithelial tumours.
Carcinoma, Squamous Cell
Stromal expression of cathepsin K in squamous cell carcinoma.
Carcinoma, Squamous Cell
The CD200-CD200R Axis Promotes Squamous Cell Carcinoma Metastasis via Regulation of Cathepsin K.
Cardiomegaly
Cathepsin K knockout alleviates aging-induced cardiac dysfunction.
Cardiomegaly
Cathepsin K Knockout Alleviates Pressure Overload-Induced Cardiac Hypertrophy.
Cardiomegaly
Cathepsin K knockout mitigates high-fat diet-induced cardiac hypertrophy and contractile dysfunction.
Cardiomyopathy, Dilated
Cathepsin K Knockout Alleviates Pressure Overload-Induced Cardiac Hypertrophy.
Cardiotoxicity
Cardiomyocyte-specific disruption of Cathepsin K protects against doxorubicin-induced cardiotoxicity.
Cardiotoxicity
Correction: Cardiomyocyte-specific disruption of Cathepsin K protects against doxorubicin-induced cardiotoxicity.
Cardiovascular Diseases
Cathepsin K - A classical bone biomarker in cardiovascular disease: The heart is not alone anymore.
Cardiovascular Diseases
Cathepsin K gene disruption does not affect murine aneurysm formation.
Cardiovascular Diseases
Cathepsin K knockout mitigates high-fat diet-induced cardiac hypertrophy and contractile dysfunction.
Cardiovascular Diseases
Cathepsin K knockout protects against cardiac dysfunction in diabetic mice.
Cardiovascular Diseases
Future of anticathepsin K drugs: dual therapy for skeletal disease and atherosclerosis?
Cardiovascular Diseases
Increased Circulating Cathepsin K in Patients with Chronic Heart Failure.
Cardiovascular Diseases
Mechanisms with clinical implications for atrial fibrillation-associated remodeling: cathepsin K expression, regulation, and therapeutic target and biomarker.
cathepsin k deficiency
A rare case of pycnodysostosis: Technical difficulties in managing long bone fractures.
cathepsin k deficiency
Ablation of cathepsin k activity in the young mouse causes hypermineralization of long bone and growth plates.
cathepsin k deficiency
Cathepsin K deficiency aggravates lung injury in hyperoxia-exposed newborn mice.
cathepsin k deficiency
Cathepsin K Deficiency Ameliorates Systemic Lupus Erythematosus-like Manifestations in
cathepsin k deficiency
Cathepsin K Deficiency Impaired Ischemia-Induced Neovascularization in Aged Mice.
cathepsin k deficiency
Cathepsin K deficiency in mice induces structural and metabolic changes in the central nervous system that are associated with learning and memory deficits.
cathepsin k deficiency
Cathepsin K deficiency in pycnodysostosis results in accumulation of non-digested phagocytosed collagen in fibroblasts.
cathepsin k deficiency
Cathepsin K deficiency partially inhibits, but does not prevent, bone destruction in human tumor necrosis factor-transgenic mice.
cathepsin k deficiency
Cathepsin K Deficiency Prevents the Aggravated Vascular Remodeling Response to Flow Cessation in ApoE-/- Mice.
cathepsin k deficiency
Cathepsin K deficiency promotes alveolar bone regeneration by promoting jaw bone marrow mesenchymal stem cells proliferation and differentiation via glycolysis pathway.
cathepsin k deficiency
Cathepsin K Deficiency Reduces Elastase Perfusion-Induced Abdominal Aortic Aneurysms in Mice.
cathepsin k deficiency
Cathepsin K Deficiency Suppresses Disuse-Induced Bone Loss.
cathepsin k deficiency
Cathepsin K inhibitors for osteoporosis and potential off-target effects.
cathepsin k deficiency
Cathepsin K osteoporosis trials, pycnodysostosis and mouse deficiency models: Commonalities and differences.
cathepsin k deficiency
Cathepsin K: isolation and characterization of the murine cDNA and genomic sequence, the homologue of the human pycnodysostosis gene.
cathepsin k deficiency
Clinical and Radiographic Features of Pycnodysostosis with Emphasis on Dentofacial Problems.
cathepsin k deficiency
Clinical disorders of bone resorption.
cathepsin k deficiency
Determination of bone markers in pycnodysostosis: effects of cathepsin K deficiency on bone matrix degradation.
cathepsin k deficiency
Disturbed remodeling and delayed fracture healing in pediatric pycnodysostosis patients.
cathepsin k deficiency
Effects of cathepsin K deficiency on intercellular junction proteins, luminal mucus layers, and extracellular matrix constituents in the mouse colon.
cathepsin k deficiency
Function of Cathepsin K in the Central Nervous System of Male Mice is Independent of Its Role in the Thyroid Gland.
cathepsin k deficiency
Functions of cathepsin K in bone resorption. Lessons from cathepsin K deficient mice.
cathepsin k deficiency
Gene profiling of cathepsin K deficiency in atherogenesis: profibrotic but lipogenic.
cathepsin k deficiency
Immunology. The toll of cathepsin K deficiency.
cathepsin k deficiency
Increased Bone Resorption during Lactation in Pycnodysostosis.
cathepsin k deficiency
Mechanisms of the anabolic effects of teriparatide on bone: insight from the treatment of a patient with pycnodysostosis.
cathepsin k deficiency
Orthognathic surgery in pycnodysostosis: a case report.
cathepsin k deficiency
Pedicle stress fracture: an unusual complication of pycnodysostosis.
cathepsin k deficiency
PLF-1 (Proliferin-1) Modulates Smooth Muscle Cell Proliferation and Development of Experimental Intimal Hyperplasia.
cathepsin k deficiency
Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency.
cathepsin k deficiency
Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease.
cathepsin k deficiency
Role of cathepsin K in structural changes in brachiocephalic artery during progression of atherosclerosis in apoE-deficient mice.
cathepsin k deficiency
The effect of cathepsin K deficiency on airway development and TGF-?1 degradation.
cathepsin k deficiency
Thyroid functions of mouse cathepsins B, K, and L.
cathepsin s deficiency
Deficiency of cathepsin S attenuates angiotensin II-induced abdominal aortic aneurysm formation in apolipoprotein E-deficient mice.
Cherubism
Multinucleated giant cells in various forms of giant cell containing lesions of the jaws express features of osteoclasts.
Cholesteatoma
Expression of matrix-degrading cysteine proteinase cathepsin K in cholesteatoma.
Chondroma
Cysteine proteinases in chondrosarcomas.
Chondrosarcoma
Cysteine proteinases in chondrosarcomas.
Chondrosarcoma
Expression of cathepsin K in chordoma.
Chordoma
Expression of cathepsin K in chordoma.
Chordoma
Expression of cathepsin K in skull base chordoma.
Chronic Periodontitis
Comparative evaluation of cathepsin K levels in gingival crevicular fluid among smoking and nonsmoking patients with chronic periodontitis.
Colitis
Extracellular cathepsin K exerts antimicrobial activity and is protective against chronic intestinal inflammation in mice.
Colitis, Ulcerative
Laboratory control of the osteoresorptive effects of glucorcorticoids in patients with purpose colitis.
Colorectal Neoplasms
Gut microbiota-stimulated cathepsin K secretion mediates TLR4-dependent M2 macrophage polarization and promotes tumor metastasis in colorectal cancer.
Coronary Artery Disease
Circulating cathepsin K as a potential novel biomarker of coronary artery disease.
Coronary Artery Disease
Decreased Cathepsin K Plasma Level may Reflect an Association of Osteopoenia/Osteoporosis with Coronary Atherosclerosis and Coronary Artery Calcification in Male Patients with Stable Angina.
Coronary Artery Disease
Increased serum cathepsin K in patients with coronary artery disease.
COVID-19
Pharmacoinformatics and hypothetical studies on allicin, curcumin, and gingerol as potential candidates against COVID-19-associated proteases.
Craniopharyngioma
Cathepsin B, D and K expression in adamantinomatous craniopharyngiomas relates to their levels of differentiation as determined by the patterns of retinoic acid receptor expression.
Craniosynostoses
Pycnodysostosis with craniosynostosis: case report of the craniofacial and oral features.
Crohn Disease
Cathepsin-k as a diagnostic marker in the identification of micro-granulomas in Crohn's disease.
Cysts
Expression of the proteinase specialized in bone resorption, cathepsin K, in granulomatous inflammation.
Cysts
Serum cathepsin K and cystatin C concentration in patients with advanced non-small-cell lung cancer during chemotherapy.
Dermatofibrosarcoma
Cathepsin K expression: a useful marker for the differential diagnosis of dermatofibroma and dermatofibrosarcoma protuberans.
Diabetes Mellitus, Type 1
Increased cathepsin K and tartrate-resistant acid phosphatase expression in bone of streptozotocin-induced diabetic rats.
Diabetes Mellitus, Type 2
Histological evidence that metformin reverses the adverse effects of diabetes on orthodontic tooth movement in rats.
Dwarfism
Ablation of cathepsin k activity in the young mouse causes hypermineralization of long bone and growth plates.
Dwarfism
Near Normalization of Adult Height and Body Proportions by Growth Hormone in Pycnodysostosis.
Echinococcosis
Expression of the proteinase specialized in bone resorption, cathepsin K, in granulomatous inflammation.
Encephalomyelitis
Extracellular cathepsin K exerts antimicrobial activity and is protective against chronic intestinal inflammation in mice.
Epilepsy
Micro-vibrations at 30?Hz on bone cells cultivated in vitro produce soluble factors for osteoclast inhibition and osteoblast activity.
Gaucher Disease
Pathologic gene expression in Gaucher disease: up-regulation of cysteine proteinases including osteoclastic cathepsin K.
Genetic Diseases, Inborn
Clinical and Radiographic Features of Pycnodysostosis with Emphasis on Dentofacial Problems.
Genetic Diseases, Inborn
Pycnodysostosis presenting as atypical stridor.
Genetic Diseases, Inborn
Pycnodysostosis with extreme sleep apnea: a possible alternative to tracheotomy.
Giant Cell Tumor of Bone
Cathepsin K is the principal protease in giant cell tumor of bone.
Giant Cell Tumor of Bone
Cysteine proteinases in chondrosarcomas.
Giant Cell Tumors
Cathepsin K is the principal protease in giant cell tumor of bone.
Giant Cell Tumors
Cysteine proteinases in chondrosarcomas.
Giant Cell Tumors
Localization of cathepsin K in human osteoclasts by in situ hybridization and immunohistochemistry.
Glioblastoma
Cathepsin K cleavage of SDF-1? inhibits its chemotactic activity towards glioblastoma stem-like cells.
Glioblastoma
Correction: Expression Analysis of All Protease Genes Reveals Cathepsin K to Be Overexpressed in Glioblastoma.
Glioblastoma
Expression analysis of all protease genes reveals cathepsin K to be overexpressed in glioblastoma.
Glioblastoma
Localization patterns of cathepsins K and X and their predictive value in glioblastoma.
Glioblastoma
Periarteriolar Glioblastoma Stem Cell Niches Express Bone Marrow Hematopoietic Stem Cell Niche Proteins.
Glioma
CD133+ and Nestin+ Glioma Stem-Like Cells Reside Around CD31+ Arterioles in Niches that Express SDF-1?, CXCR4, Osteopontin and Cathepsin K.
Glucose Intolerance
Cathepsin K knockout mitigates high-fat diet-induced cardiac hypertrophy and contractile dysfunction.
Glucose Metabolism Disorders
Impact of circulating cathepsin K on the coronary calcification and the clinical outcome in chronic kidney disease patients.
Granular Cell Tumor
A broad survey of cathepsin K immunoreactivity in human neoplasms.
Granuloma
ApoE-deficient mice on cholate-containing high-fat diet reveal a pathology similar to lung sarcoidosis.
Granuloma
Cathepsin-k as a diagnostic marker in the identification of micro-granulomas in Crohn's disease.
Granuloma
Mycobacteria-induced granuloma necrosis depends on IRF-1.
Heart Diseases
Cardiomyocyte-specific disruption of Cathepsin K protects against doxorubicin-induced cardiotoxicity.
Heart Diseases
Inappropriate cathepsin K secretion promotes its enzymatic activation driving heart and valve malformation.
Heart Failure
Cardiomyocyte-specific disruption of Cathepsin K protects against doxorubicin-induced cardiotoxicity.
Heart Failure
Increased Circulating Cathepsin K in Patients with Chronic Heart Failure.
Hematoma, Subdural, Chronic
Role of cathepsin K in the development of chronic subdural hematoma.
Histiocytoma, Benign Fibrous
Cathepsin K expression: a useful marker for the differential diagnosis of dermatofibroma and dermatofibrosarcoma protuberans.
Histiocytoma, Benign Fibrous
Could cathepsin-k be a driver of the myofibroblastic differentiation observed in dermatofibroma, atypical fibroxanthoma and pleomorphic dermal sarcoma?
Histiocytoma, Benign Fibrous
Cysteine proteinases in chondrosarcomas.
Histiocytoma, Benign Fibrous
Dermatofibrosarcoma Protuberans: The Current State of Multidisciplinary Management.
Histiocytoma, Benign Fibrous
Role of cathepsin K in the turnover of the dermal extracellular matrix during scar formation.
Hypercalcemia
Design of potent, selective, and orally bioavailable inhibitors of cysteine protease cathepsin k.
Hyperostosis
From disease to treatment: from rare skeletal disorders to treatments for osteoporosis.
Immune System Diseases
Emerging roles of cysteine cathepsins in disease and their potential as drug targets.
Immunoglobulin Light-chain Amyloidosis
A putative role for cathepsin K in degradation of AA and AL amyloidosis.
Infections
Fibroblast growth factor receptor 2 expression in apical periodontitis in mice.
Infections
HIV-1 replicates in human osteoclasts and enhances their differentiation in vitro.
Infections
Immune response and expression analysis of cathepsin K in goldfish during Aeromonas hydrophila infection.
Inflammatory Bowel Diseases
Extracellular cathepsin K exerts antimicrobial activity and is protective against chronic intestinal inflammation in mice.
Keloid
Role of cathepsin K in the turnover of the dermal extracellular matrix during scar formation.
Keratoconus
Collagenolytic proteinases in keratoconus.
Keratosis, Actinic
Cathepsin K expression in basal cell carcinoma.
Kidney Neoplasms
Cathepsin K (Clone EPR19992) Demonstrates Uniformly Positive Immunoreactivity in Renal Oncocytoma, Chromophobe Renal Cell Carcinoma, and Distal Tubules.
Kidney Neoplasms
Cathepsin K: A Novel Diagnostic and Predictive Biomarker for Renal Tumors.
Kidney Neoplasms
Cathepsin-K immunoreactivity distinguishes MiTF/TFE family renal translocation carcinomas from other renal carcinomas.
Kidney Neoplasms
RNA sequencing of Xp11 translocation-associated cancers reveals novel gene fusions and distinctive clinicopathologic correlations.
Kidney Neoplasms
TFE3 break-apart FISH has a higher sensitivity for Xp11.2 translocation-associated renal cell carcinoma compared with TFE3 or cathepsin K immunohistochemical staining alone: expanding the morphologic spectrum.
Kidney Neoplasms
TFE3-Fusion Variant Analysis Defines Specific Clinicopathologic Associations Among Xp11 Translocation Cancers.
Leiomyoma
Coexistence of Conventional Leiomyoma, Fumarate Hydratase-deficient Atypical Leiomyoma, and Perivascular Epithelioid Cell Tumor in a Uterus: A Case Study.
Leiomyoma
Renal Leiomyoma: A Contemporary Multi-institution Study of an Infrequent and Frequently Misclassified Neoplasm.
Leukemia
KLF2 (kruppel like factor 2 [lung]) regulates osteoclastogenesis by modulating autophagy.
Lichen Planus, Oral
Cathepsin K expression is increased in oral lichen planus.
Lung Diseases
Cathepsin K overexpression modifies lung development in newborn mice.
Lung Diseases
Single-walled carbon nanotubes induce airway hyperreactivity and parenchymal injury in mice.
Lung Diseases, Interstitial
Cathepsin-K is a sensitive immunohistochemical marker for detection of micro-granulomas in hypersensitivity pneumonitis.
Lung Injury
Cathepsin K deficiency aggravates lung injury in hyperoxia-exposed newborn mice.
Lung Neoplasms
Analysis of host- and tumor-derived proteinases using a custom dual species microarray reveals a protective role for stromal matrix metalloproteinase-12 in non-small cell lung cancer.
Lung Neoplasms
Serum cathepsin K and cystatin C concentration in patients with advanced non-small-cell lung cancer during chemotherapy.
Lung Neoplasms
The Potential Role of Cathepsin K in Non-Small Cell Lung Cancer.
Lymphangioleiomyomatosis
Cathepsin K in Lymphangioleiomyomatosis: LAM Cell-Fibroblast Interactions Enhance Protease Activity by Extracellular Acidification.
Lymphangioleiomyomatosis
Cathepsin K is Superior to HMB45 for the Diagnosis of Pulmonary Lymphangioleiomyomatosis.
Lymphangioleiomyomatosis
Cathepsin-k expression in pulmonary lymphangioleiomyomatosis.
Lymphatic Metastasis
Cathepsin K associates with lymph node metastasis and poor prognosis in oral squamous cell carcinoma.
Lysosomal Storage Diseases
Pycnodysostosis with unusual findings: a case report.
Melanoma
A broad survey of cathepsin K immunoreactivity in human neoplasms.
Melanoma
Cathepsin K expression in basal cell carcinoma.
Melanoma
Cathepsin K expression in melanoma is associated with metastases.
Melanoma
Cathepsin K in melanoma invasion.
Melanoma
Cathepsin K in the immunohistochemical diagnosis of melanocytic lesions.
Melanoma
Renal carcinoma with (6;11)(p21;q12) translocation: report of an adult case.
Memory Disorders
Cathepsin K deficiency in mice induces structural and metabolic changes in the central nervous system that are associated with learning and memory deficits.
Memory Disorders
Characterisation and metabolism of astroglia-rich primary cultures from cathepsin K-deficient mice.
Memory Disorders
Function of Cathepsin K in the Central Nervous System of Male Mice is Independent of Its Role in the Thyroid Gland.
Metabolic Diseases
Excessive activity of cathepsin K is associated with cartilage defects in a zebrafish model of mucolipidosis II.
Microphthalmos
Cathepsin K (Clone EPR19992) Demonstrates Uniformly Positive Immunoreactivity in Renal Oncocytoma, Chromophobe Renal Cell Carcinoma, and Distal Tubules.
Microphthalmos
Cathepsin K in the immunohistochemical diagnosis of melanocytic lesions.
Microphthalmos
Cathepsin-K immunoreactivity distinguishes MiTF/TFE family renal translocation carcinomas from other renal carcinomas.
Microphthalmos
Differential expression of cathepsin K in neoplasms harboring TFE3 gene fusions.
Microphthalmos
Essential role of p38 mitogen-activated protein kinase in cathepsin K gene expression during osteoclastogenesis through association of NFATc1 and PU.1.
Microphthalmos
Linking osteopetrosis and pycnodysostosis: regulation of cathepsin K expression by the microphthalmia transcription factor family.
Microphthalmos
Odontoblast-like MDPC-23 cells function as odontoclasts with the RANKL/M-CSF induction.
Microphthalmos
The expression of Clcn7 and Ostm1 in osteoclasts is coregulated by microphthalmia transcription factor.
Mucolipidoses
Excessive activity of cathepsin K is associated with cartilage defects in a zebrafish model of mucolipidosis II.
Mucopolysaccharidoses
Glycosaminoglycan-Mediated Loss of Cathepsin K Collagenolytic Activity in MPS I Contributes to Osteoclast and Growth Plate Abnormalities.
Mucopolysaccharidoses
Potential role of cathepsin K in the pathophysiology of mucopolysaccharidoses.
Mucopolysaccharidosis VI
Alternative Method for Full Oral Rehabilitation in Patients with Pycnodysostosis Syndrome: ?A Case Report.
Mucositis
Estimation of Bone Loss Biomarkers as a Diagnostic Tool for Peri-Implantitis.
Multiple Myeloma
Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease.
Myocardial Infarction
Endogenous reduction of miR-185 accelerates cardiac function recovery in mice following myocardial infarction via targeting of cathepsin K.
Myocardial Infarction
Levels of cathepsins in acute myocardial infarction.
Neoplasm Metastasis
A cathepsin K inhibitor reduces breast cancer induced osteolysis and skeletal tumor burden.
Neoplasm Metastasis
A novel derivative of artemisinin inhibits cell proliferation and metastasis via down-regulation of cathepsin K in breast cancer.
Neoplasm Metastasis
Bone marrow-derived cathepsin K cleaves SPARC in bone metastasis.
Neoplasm Metastasis
Cathepsin G enhances mammary tumor-induced osteolysis by generating soluble receptor activator of nuclear factor-kappaB ligand.
Neoplasm Metastasis
Cathepsin K associates with lymph node metastasis and poor prognosis in oral squamous cell carcinoma.
Neoplasm Metastasis
Cathepsin K expression in castration-resistant prostate carcinoma: a therapeutical target for patients at risk for bone metastases.
Neoplasm Metastasis
Cathepsin K expression in melanoma is associated with metastases.
Neoplasm Metastasis
Cathepsin K in the bone microenvironment: link between obesity and prostate cancer?
Neoplasm Metastasis
Cathepsin K inhibitors as treatment of bone metastasis.
Neoplasm Metastasis
Cathepsin K mRNA and protein expression in prostate cancer progression.
Neoplasm Metastasis
Cathepsin K: a unique collagenolytic cysteine peptidase.
Neoplasm Metastasis
Cathepsin K: The association between Cathepsin K expression and sphenoid sinus invasion of pituitary adenomas.
Neoplasm Metastasis
Cathepsins and osteosarcoma: Expression analysis identifies cathepsin K as an indicator of metastasis.
Neoplasm Metastasis
Circulating cathepsin K and cystatin C in patients with cancer related bone disease: clinical and therapeutic implications.
Neoplasm Metastasis
Coronin 3 promotes gastric cancer metastasis via the up-regulation of MMP-9 and cathepsin K.
Neoplasm Metastasis
Detection of femtomole quantities of mature cathepsin K with zymography.
Neoplasm Metastasis
Efficacy of a cathepsin K inhibitor in a preclinical model for prevention and treatment of breast cancer bone metastasis.
Neoplasm Metastasis
Elevated Cathepsin K potentiates metastasis of epithelial ovarian cancer.
Neoplasm Metastasis
Gut microbiota-stimulated cathepsin K secretion mediates TLR4-dependent M2 macrophage polarization and promotes tumor metastasis in colorectal cancer.
Neoplasm Metastasis
Identification of Cathepsin K in the Peritoneal Metastasis of Ovarian Carcinoma Using In-silico, Gene Expression Analysis.
Neoplasm Metastasis
Inhibition of osteoclast differentiation and bone resorption by cathepsin K antisense oligonucleotides.
Neoplasm Metastasis
Inhibitory effects of low intensity pulsed ultrasound on osteoclastogenesis induced in vitro by breast cancer cells.
Neoplasm Metastasis
Obesity and Cathepsin K: A Complex Pathophysiological Relationship in Breast Cancer Metastases.
Neoplasm Metastasis
Odanacatib, a cathepsin K inhibitor for the treatment of osteoporosis and other skeletal disorders associated with excessive bone remodeling.
Neoplasm Metastasis
Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease.
Neoplasm Metastasis
Role of the bone microenvironment in bone metastasis of malignant tumors - therapeutic implications.
Neoplasm Metastasis
Serum cathepsin K levels of patients with longstanding rheumatoid arthritis: correlation with radiological destruction.
Neoplasm Metastasis
Serum interleukin-6 in patients with metastatic bone disease: correlation with cystatin C.
Neoplasm Metastasis
Targeting cathepsin K diminishes prostate cancer establishment and growth in murine bone.
Neoplasm Metastasis
The C-Terminal Intact Forms of Periostin (iPTN) Are Surrogate Markers for Osteolytic Lesions in Experimental Breast Cancer Bone Metastasis.
Neoplasm Metastasis
The cathepsin K inhibitor odanacatib suppresses bone resorption in women with breast cancer and established bone metastases: results of a 4-week, double-blind, randomized, controlled trial.
Neoplasm Metastasis
The CD200-CD200R Axis Promotes Squamous Cell Carcinoma Metastasis via Regulation of Cathepsin K.
Neoplasm Metastasis
The osteoclast-associated protease cathepsin K is expressed in human breast carcinoma.
Neoplasm Metastasis
Zoledronic acid exhibits inhibitory effects on osteoblastic and osteolytic metastases of prostate cancer.
Neoplasm Metastasis
[Bony lesion with prostate cancer]
Neoplasm Metastasis
[Diagnostic value of biomarkers of bone metabolism in the gingival fluid in inflammatory-destructive and tumor oral pathology].
Neoplasm Metastasis
[Encounter of cancer cells with bone. Development of bone metastasis-specific targeting therapy].
Neoplasms
A broad survey of cathepsin K immunoreactivity in human neoplasms.
Neoplasms
A case of bilateral renal cell carcinoma associated with long-term dialysis showing false-positive immunoreactivity for TFE3 as Xp11 translocation renal cell carcinoma.
Neoplasms
A cathepsin K inhibitor reduces breast cancer induced osteolysis and skeletal tumor burden.
Neoplasms
A novel derivative of artemisinin inhibits cell proliferation and metastasis via down-regulation of cathepsin K in breast cancer.
Neoplasms
A novel partner of TFE3 in the Xp11 translocation renal cell carcinoma: clinicopathological analyses and detection of EWSR1-TFE3 fusion.
Neoplasms
A Rare Partner of TFE3 in the Xp11 Translocation Renal Cell Carcinoma: Clinicopathological Analyses and Detection of MED15-TFE3 Fusion.
Neoplasms
A soft coral-derived compound, 11-epi-sinulariolide acetate suppresses inflammatory response and bone destruction in adjuvant-induced arthritis.
Neoplasms
ALK-rearranged renal cell carcinoma with a novel PLEKHA7-ALK translocation and metanephric adenoma-like morphology.
Neoplasms
Aminothiazoles inhibit RANKL- and LPS-mediated osteoclastogenesis and PGE2 production in RAW 264.7 cells.
Neoplasms
Analysis of host- and tumor-derived proteinases using a custom dual species microarray reveals a protective role for stromal matrix metalloproteinase-12 in non-small cell lung cancer.
Neoplasms
Ankle loading ameliorates bone loss from breast cancer-associated bone metastasis.
Neoplasms
Association of bone loss with the upregulation of survival-related genes and concomitant downregulation of Mammalian target of rapamycin and osteoblast differentiation-related genes in the peripheral blood of late postmenopausal osteoporotic women.
Neoplasms
Azithromycin suppresses human osteoclast formation and activity in vitro.
Neoplasms
Basaloid squamous cell carcinoma of the maxillary sinus: Report of two cases in association with cathepsin K expression.
Neoplasms
Benign perivascular myoid cell tumor (myopericytoma) of the urinary tract: a report of 2 cases with an emphasis on differential diagnosis.
Neoplasms
BET Inhibitor JQ1 Blocks Inflammation and Bone Destruction.
Neoplasms
Bone marrow-derived cathepsin K cleaves SPARC in bone metastasis.
Neoplasms
C2K77 ELISA detects cleavage of type II collagen by cathepsin K in equine articular cartilage.
Neoplasms
Cathepsin K (Clone EPR19992) Demonstrates Uniformly Positive Immunoreactivity in Renal Oncocytoma, Chromophobe Renal Cell Carcinoma, and Distal Tubules.
Neoplasms
Cathepsin K deficiency partially inhibits, but does not prevent, bone destruction in human tumor necrosis factor-transgenic mice.
Neoplasms
Cathepsin K expression in a wide spectrum of perivascular epithelioid cell neoplasms (PEComas): a clinicopathological study emphasizing extrarenal PEComas.
Neoplasms
Cathepsin K expression in basal cell carcinoma.
Neoplasms
Cathepsin K expression in castration-resistant prostate carcinoma: a therapeutical target for patients at risk for bone metastases.
Neoplasms
Cathepsin K expression in clear cell "sugar" tumor (PEComa) of the lung.
Neoplasms
Cathepsin K expression in melanoma is associated with metastases.
Neoplasms
Cathepsin K in the bone microenvironment: link between obesity and prostate cancer?
Neoplasms
Cathepsin K in the immunohistochemical diagnosis of melanocytic lesions.
Neoplasms
Cathepsin K induces platelet dysfunction and affects cell signaling in breast cancer - molecularly distinct behavior of cathepsin K in breast cancer.
Neoplasms
Cathepsin K inhibition-induced mitochondrial ROS enhances sensitivity of cancer cells to anti-cancer drugs through USP27x-mediated Bim protein stabilization.
Neoplasms
Cathepsin K inhibitors as treatment of bone metastasis.
Neoplasms
Cathepsin K inhibitors for osteoporosis and potential off-target effects.
Neoplasms
Cathepsin k is present in invasive oral tongue squamous cell carcinoma in vivo and in vitro.
Neoplasms
Cathepsin K is selectively expressed in the stroma of lung adenocarcinoma but not in bronchioloalveolar carcinoma. A useful marker of invasive growth.
Neoplasms
Cathepsin K is Superior to HMB45 for the Diagnosis of Pulmonary Lymphangioleiomyomatosis.
Neoplasms
Cathepsin K is the principal protease in giant cell tumor of bone.
Neoplasms
Cathepsin K modulates invasion, migration and adhesion of oral squamous cell carcinomas in vitro.
Neoplasms
Cathepsin K: A Novel Diagnostic and Predictive Biomarker for Renal Tumors.
Neoplasms
Cathepsin K: a unique collagenolytic cysteine peptidase.
Neoplasms
Cathepsin K: The association between Cathepsin K expression and sphenoid sinus invasion of pituitary adenomas.
Neoplasms
Cathepsin-K immunoreactivity distinguishes MiTF/TFE family renal translocation carcinomas from other renal carcinomas.
Neoplasms
Cathepsins and osteosarcoma: Expression analysis identifies cathepsin K as an indicator of metastasis.
Neoplasms
CCR2 deficiency results in increased osteolysis in experimental periapical lesions in mice.
Neoplasms
CD133+ and Nestin+ Glioma Stem-Like Cells Reside Around CD31+ Arterioles in Niches that Express SDF-1?, CXCR4, Osteopontin and Cathepsin K.
Neoplasms
Circulating cathepsin K and cystatin C in patients with cancer related bone disease: clinical and therapeutic implications.
Neoplasms
Coexistence of Conventional Leiomyoma, Fumarate Hydratase-deficient Atypical Leiomyoma, and Perivascular Epithelioid Cell Tumor in a Uterus: A Case Study.
Neoplasms
Coexistent loss of INI1 and BRG1 expression in a rhabdoid renal cell carcinoma (RCC): implications for a possible role of SWI/SNF complex in the pathogenesis of RCC.
Neoplasms
Comparison of cathepsins K and S expression within the rheumatoid and osteoarthritic synovium.
Neoplasms
Complexity of cancer protease biology: Cathepsin K expression and function in cancer progression.
Neoplasms
Comprehensive analysis of 34 MiT family translocation renal cell carcinomas and review of the literature: investigating prognostic markers and therapy targets.
Neoplasms
Conjugated linoleic acid inhibits osteoclast differentiation of RAW264.7 cells by modulating RANKL signaling.
Neoplasms
Coronin 3 promotes gastric cancer metastasis via the up-regulation of MMP-9 and cathepsin K.
Neoplasms
Could cathepsin-k be a driver of the myofibroblastic differentiation observed in dermatofibroma, atypical fibroxanthoma and pleomorphic dermal sarcoma?
Neoplasms
Cysteine cathepsins B, X and K expression in peri-arteriolar glioblastoma stem cell niches.
Neoplasms
Cysteine proteinases in chondrosarcomas.
Neoplasms
Cytokine pattern determines the progression of experimental periodontal disease induced by Actinobacillus actinomycetemcomitans through the modulation of MMPs, RANKL, and their physiological inhibitors.
Neoplasms
Daphnetin inhibits RANKL-induced osteoclastogenesis in vitro.
Neoplasms
Detection of femtomole quantities of mature cathepsin K with zymography.
Neoplasms
Differential expression of cathepsin K in neoplasms harboring TFE3 gene fusions.
Neoplasms
Effects of 9cis,11trans and 10trans,12cis CLA on osteoclast formation and activity from human CD14+ monocytes.
Neoplasms
Emerging therapeutic targets in breast cancer bone metastasis.
Neoplasms
Estrogen-deficient osteoporosis enhances the recruitment and activity of osteoclasts by breast cancer cells.
Neoplasms
Exosomal tumor necrosis factor-? from hepatocellular cancer cells (Huh-7) promote osteoclast differentiation.
Neoplasms
Expanding the morphologic spectrum of chromophobe renal cell carcinoma: A study of 8 cases with papillary architecture.
Neoplasms
Expression of cathepsin K in chordoma.
Neoplasms
Expression of cathepsin K in neurofibromatosis 1-associated cutaneous malignant peripheral nerve sheath tumors and neurofibromas.
Neoplasms
Expression of cathepsin K in skull base chordoma.
Neoplasms
Expression profile of cathepsins indicates the potential of cathepsins B and D as prognostic factors in breast cancer patients.
Neoplasms
Extracellular cathepsin K exerts antimicrobial activity and is protective against chronic intestinal inflammation in mice.
Neoplasms
FGF-8 is involved in bone metastasis of prostate cancer.
Neoplasms
Fructus Ligustri Lucidi ethanol extract inhibits osteoclastogenesis in RAW264.7 cells via the RANKL signaling pathway.
Neoplasms
Fructus Ligustri Lucidi preserves bone quality through the regulation of gut microbiota diversity, oxidative stress, TMAO and Sirt6 levels in aging mice.
Neoplasms
Future directions of bone-targeted therapy for metastatic breast cancer.
Neoplasms
Gene Expression in Osteolysis: Review on the Identification of Altered Molecular Pathways in Preclinical and Clinical Studies.
Neoplasms
Gene expression relevant to osteoclastogenesis in the synovium and bone marrow of mature rats with collagen-induced arthritis.
Neoplasms
Gut microbiota-stimulated cathepsin K secretion mediates TLR4-dependent M2 macrophage polarization and promotes tumor metastasis in colorectal cancer.
Neoplasms
High fat diet-induced animal model of age-associated obesity and osteoporosis.
Neoplasms
Human breast adenocarcinoma (MDA-231) and human lung squamous cell carcinoma (Hara) do not have the ability to cause bone resorption by themselves during the establishment of bone metastasis.
Neoplasms
I?BET151 inhibits osteoclastogenesis via the RANKL signaling pathway in RAW264.7 macrophages.
Neoplasms
Increased osteoclast activity is associated with aggressiveness of osteosarcoma.
Neoplasms
Inhibitory Effects of Cathepsin K Inhibitor (ODN-MK-0822) on the Paracrine Pro-Osteoclast Factors of Breast Cancer Cells.
Neoplasms
Interactions between microenvironment and cancer cells in two animal models of bone metastasis.
Neoplasms
Interactions of myeloma cells with osteoclasts promote tumour expansion and bone degradation through activation of a complex signalling network and upregulation of cathepsin K, matrix metalloproteinases (MMPs) and urokinase plasminogen activator (uPA).
Neoplasms
Interferon-? Released by Activated CD8(+) T Lymphocytes Impairs the Calcium Resorption Potential of Osteoclasts in Calcified Human Aortic Valves.
Neoplasms
KLF2 (kruppel like factor 2 [lung]) regulates osteoclastogenesis by modulating autophagy.
Neoplasms
Linking osteopetrosis and pycnodysostosis: regulation of cathepsin K expression by the microphthalmia transcription factor family.
Neoplasms
Lkb1 deletion in periosteal mesenchymal progenitors induces osteogenic tumors through mTORC1 activation.
Neoplasms
Localization of cathepsin K in human osteoclasts by in situ hybridization and immunohistochemistry.
Neoplasms
Lysosomal cathepsin B participates in the podosome-mediated extracellular matrix degradation and invasion via secreted lysosomes in v-Src fibroblasts.
Neoplasms
Macrophage cathepsin K promotes prostate tumor progression in bone.
Neoplasms
Melanotic Xp11-associated tumor of the sigmoid colon: A case report.
Neoplasms
MiR-377 inhibits wear particle-induced osteolysis via targeting RANKL.
Neoplasms
Molecular-genetic analysis is essential for accurate classification of renal carcinoma resembling Xp11.2 translocation carcinoma.
Neoplasms
Morphologic heterogeneity and markers of renal cell carcinoma with t(6; 11)(p21; q12): a case report and literature review.
Neoplasms
Morphological, immunohistochemical, and chromosomal analysis of multicystic chromophobe renal cell carcinoma, an architecturally unusual challenging variant.
Neoplasms
New bone formation and osteolysis by a metastatic, highly invasive canine prostate carcinoma xenograft.
Neoplasms
Novel anti-cancer strategy in bone tumors by targeting molecular and cellular modulators of bone resorption.
Neoplasms
Oncogenic and osteolytic functions of histone demethylase NO66 in castration-resistant prostate cancer.
Neoplasms
Ortho-silicic Acid Inhibits RANKL-Induced Osteoclastogenesis and Reverses Ovariectomy-Induced Bone Loss In Vivo.
Neoplasms
Osteoclast precursors acquire sensitivity to breast cancer derived factors early in differentiation.
Neoplasms
Osteoprotegerin inhibits tumor-induced osteoclastogenesis and bone tumor growth in osteopetrotic mice.
Neoplasms
Patterns and localization of gene expression during intramembranous bone regeneration in the rat femoral marrow ablation model.
Neoplasms
PAX8 expression in sporadic hemangioblastoma of the kidney supports a primary renal cell lineage: implications for differential diagnosis.
Neoplasms
PEComas of the kidney and of the genitourinary tract.
Neoplasms
Photoactivated inhibition of cathepsin K in a 3D tumor model.
Neoplasms
Premelanosome-negative inflammatory angiomyolipoma of liver with expression of cathepsin K and TFE3.
Neoplasms
Primary cutaneous perivascular epithelioid cell tumor: a clinicopathological and molecular reappraisal.
Neoplasms
Primary Giant Cell Tumors of the Lung: A Clinicopathologic and Immunohistochemical Study of 3 Cases.
Neoplasms
Protocatechuic Acid Attenuates Trabecular Bone Loss in Ovariectomized Mice.
Neoplasms
Renal carcinoma with (6;11)(p21;q12) translocation: report of an adult case.
Neoplasms
Renal cell carcinoma with TFE3 translocation and succinate dehydrogenase B mutation.
Neoplasms
Renal cell carcinomas with t(6;11)(p21;q12) presenting with tubulocystic renal cell carcinoma-like features.
Neoplasms
Renal Cell Carcinomas With t(6;11)(p21;q12): A Clinicopathologic Study Emphasizing Unusual Morphology, Novel Alpha-TFEB Gene Fusion Point, Immunobiomarkers, and Ultrastructural Features, As Well As Detection of the Gene Fusion by Fluorescence In Situ Hybridization.
Neoplasms
Review of renal carcinoma with t(6;11)(p21;q12-13) with focus on clinical and pathobiological aspects.
Neoplasms
Serum cathepsin K and cystatin C concentration in patients with advanced non-small-cell lung cancer during chemotherapy.
Neoplasms
Stattic inhibits RANKL-mediated osteoclastogenesis by suppressing activation of STAT3 and NF-?B pathways.
Neoplasms
Stromal expression of cathepsin K in squamous cell carcinoma.
Neoplasms
t(6;11) renal cell carcinoma: a study of seven cases including two with aggressive behavior, and utility of CD68 (PG-M1) in the differential diagnosis with pure epithelioid PEComa/epithelioid angiomyolipoma.
Neoplasms
TFE3 break-apart FISH has a higher sensitivity for Xp11.2 translocation-associated renal cell carcinoma compared with TFE3 or cathepsin K immunohistochemical staining alone: expanding the morphologic spectrum.
Neoplasms
TFE3-Fusion Variant Analysis Defines Specific Clinicopathologic Associations Among Xp11 Translocation Cancers.
Neoplasms
The effects of mandibular osteotomy on maxillary orthodontic tooth movement and bone remodelling in a rat model.
Neoplasms
The Influence of Bone Type on the Gene Expression in Normal Bone and at the Bone-Implant Interface: Experiments in Animal Model.
Neoplasms
The osteoclast-associated protease cathepsin K is expressed in human breast carcinoma.
Neoplasms
The Potential Role of Cathepsin K in Non-Small Cell Lung Cancer.
Neoplasms
The role of cathepsin K in normal bone resorption.
Neoplasms
Tumor Cell-Derived Exosomes from the Prostate Cancer Cell Line TRAMP-C1 Impair Osteoclast Formation and Differentiation.
Neoplasms
Tumor necrosis factor alpha stimulates cathepsin K and V activity via juxtacrine monocyte-endothelial cell signaling and JNK activation.
Neoplasms
Use of molecular imaging to quantify response to IKK-2 inhibitor treatment in murine arthritis.
Neoplasms
Uterine PEComas: A Morphologic, Immunohistochemical, and Molecular Analysis of 32 Tumors.
Neoplasms
VEGFA amplification/increased gene copy number and VEGFA mRNA expression in renal cell carcinoma with TFEB gene alterations.
Neoplasms
Xp11 translocation renal cell carcinoma (RCC): extended immunohistochemical profile emphasizing novel RCC markers.
Neoplasms
Xp11 translocation renal cell carcinoma.
Neoplasms
Xp11.2 translocation renal cell carcinoma with NONO-TFE3 gene fusion: morphology, prognosis, and potential pitfall in detecting TFE3 gene rearrangement.
Neoplasms
[Diagnostic value of biomarkers of bone metabolism in the gingival fluid in inflammatory-destructive and tumor oral pathology].
Neoplasms
[Osteoimmunological aspects of periodontal inflammatory destructive changes at periimplantitis, chronic periodontitis and oncological diseases of the oral cavity].
Neoplasms
[Renal cell carcinoma with t(6;11)(p21.2;q13)/MALAT1-TFEB fusion: a clinical and pathological analysis].
Neuroblastoma
Intermittent hypoxia effect on osteoclastogenesis stimulated by neuroblastoma cells.
Neurofibroma
Expression of cathepsin K in neurofibromatosis 1-associated cutaneous malignant peripheral nerve sheath tumors and neurofibromas.
Neurofibromatoses
Expression of cathepsin K in neurofibromatosis 1-associated cutaneous malignant peripheral nerve sheath tumors and neurofibromas.
Neurofibrosarcoma
Expression of cathepsin K in neurofibromatosis 1-associated cutaneous malignant peripheral nerve sheath tumors and neurofibromas.
Nevus
Cathepsin K in the immunohistochemical diagnosis of melanocytic lesions.
Obesity
A single nucleotide polymorphism in the porcine cathepsin K (CTSK) gene is associated with back fat thickness and production traits in Italian Duroc pigs.
Obesity
Cathepsin K in adipocyte differentiation and its potential role in the pathogenesis of obesity.
Obesity
Cathepsin K in the bone microenvironment: link between obesity and prostate cancer?
Obesity
Cathepsin K inhibitors for osteoporosis and potential off-target effects.
Obesity
Cathepsin K: a unique collagenolytic cysteine peptidase.
Obesity
Cathepsin-K is a potential cardiovascular risk biomarker in prevalent hemodialysis patients.
Obesity
Deficiency and inhibition of cathepsin K reduce body weight gain and increase glucose metabolism in mice.
Obesity
Extracellular cathepsin K exerts antimicrobial activity and is protective against chronic intestinal inflammation in mice.
Obesity
Future of anticathepsin K drugs: dual therapy for skeletal disease and atherosclerosis?
Obesity
Identification of cathepsin K as a novel marker of adiposity in white adipose tissue.
Obesity
Obesity and Cathepsin K: A Complex Pathophysiological Relationship in Breast Cancer Metastases.
Optic Atrophy, Autosomal Dominant
Oxidative stress induced by fluoroquinolone enrofloxacin in zebrafish (Danio rerio) can be ameliorated after a prolonged exposure.
Osteitis Deformans
Serum cathepsin K concentrations reflect osteoclastic activity in women with postmenopausal osteoporosis and patients with Paget's disease.
Osteoarthritis
(1R,2R)-N-(1-Cyanocyclopropyl)-2-(6-methoxy-1,3,4,5-tetrahydropyrido[4,3-b]indole-2-carbonyl)cyclohexanecarboxamide (AZD4996): A Potent and Highly Selective Cathepsin K Inhibitor for the Treatment of Osteoarthritis.
Osteoarthritis
Acidic cysteine endoproteinase cathepsin K in the degeneration of the superficial articular hyaline cartilage in osteoarthritis.
Osteoarthritis
Analgesic effects of the cathepsin K inhibitor L-006235 in the monosodium iodoacetate model of osteoarthritis pain.
Osteoarthritis
Cathepsin cysteine proteases in cardiovascular disease.
Osteoarthritis
Cathepsin K inhibition reduces CTXII levels and joint pain in the guinea pig model of spontaneous osteoarthritis.
Osteoarthritis
Cathepsin K Localizes to Equine Bone
Osteoarthritis
Chicken collagen type II reduces articular cartilage destruction in a model of osteoarthritis in rats.
Osteoarthritis
Comparison of cathepsins K and S expression within the rheumatoid and osteoarthritic synovium.
Osteoarthritis
Disease-Modifying Effects of a Novel Cathepsin K Inhibitor in Osteoarthritis: A Randomized, Placebo-Controlled Study.
Osteoarthritis
Down-regulation of cathepsin K in synovium leads to progression of osteoarthritis in rabbits.
Osteoarthritis
Effects of cysteine proteases on the structural and mechanical properties of collagen fibers.
Osteoarthritis
Evidence to suggest that cathepsin K degrades articular cartilage in naturally occurring equine osteoarthritis.
Osteoarthritis
Expression of bone resorption genes in osteoarthritis and in osteoporosis.
Osteoarthritis
Genetically Engineered Mouse Models Reveal the Importance of Proteases as Osteoarthritis Drug Targets.
Osteoarthritis
Hyaluronan suppresses enhanced cathepsin K expression via activation of NF-?B with mechanical stress loading in a human chondrocytic HCS-2/8 cells.
Osteoarthritis
Increased type II collagen cleavage by cathepsin K and collagenase activities with aging and osteoarthritis in human articular cartilage.
Osteoarthritis
Inhibition of cathepsin K reduces cartilage degeneration in the anterior cruciate ligament transection rabbit and murine models of osteoarthritis.
Osteoarthritis
Nonclinical and clinical pharmacological characterization of the potent and selective cathepsin K inhibitor MIV-711.
Osteoarthritis
Protective effects of a cathepsin K inhibitor, SB-553484, in the canine partial medial meniscectomy model of osteoarthritis.
Osteoarthritis
Role of cathepsin K in normal joints and in the development of arthritis.
Osteoarthritis
The inhibition of subchondral bone resorption in the early phase of experimental dog osteoarthritis by licofelone is associated with a reduction in the synthesis of MMP-13 and cathepsin K.
Osteoarthritis
The protective effect of licofelone on experimental osteoarthritis is correlated with the downregulation of gene expression and protein synthesis of several major cartilage catabolic factors: MMP-13, cathepsin K and aggrecanases.
Osteoarthritis
The selective cathepsin K inhibitor MIV-711 attenuates joint pathology in experimental animal models of osteoarthritis.
Osteoarthritis
Up regulation of cathepsin K expression in articular chondrocytes in a transgenic mouse model for osteoarthritis.
Osteoarthritis, Knee
Pain prediction by serum biomarkers of bone turnover in people with knee osteoarthritis: an observational study of TRAcP5b and cathepsin K in OA.
Osteochondrodysplasias
From disease to treatment: from rare skeletal disorders to treatments for osteoporosis.
Osteochondrodysplasias
Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice.
Osteochondrodysplasias
The genetic basis of the osteochondrodysplasias.
Osteolysis
A cathepsin K inhibitor reduces breast cancer induced osteolysis and skeletal tumor burden.
Osteolysis
Blockade of NF-?B and MAPK Pathways by Ulinastatin Attenuates Particles-Stimulated Osteoclastogenesis in Vitro and in Vivo.
Osteolysis
Cathepsin K inhibitors as treatment of bone metastasis.
Osteolysis
Cathepsin K is the principal protease in giant cell tumor of bone.
Osteolysis
Large osteocyte lacunae in iliac crest infantile bone are not associated with impaired mineral distribution or signs of osteocytic osteolysis.
Osteolysis
Novel anti-cancer strategy in bone tumors by targeting molecular and cellular modulators of bone resorption.
Osteolysis
Novel pycnodysostosis mouse model uncovers cathepsin K function as a potential regulator of osteoclast apoptosis and senescence.
Osteolysis
Osteocytes respond to particles of clinically-relevant conventional and cross-linked polyethylene and metal alloys by up-regulation of resorptive and inflammatory pathways.
Osteomyelitis
RANKL and cathepsin K in diffuse sclerosing osteomyelitis of the mandible.
Osteopetrosis
Cathepsin K and the design of inhibitors of cathepsin K.
Osteopetrosis
Cathepsin K knockout mice develop osteopetrosis due to a deficit in matrix degradation but not demineralization.
Osteopetrosis
Clinical disorders of bone resorption.
Osteopetrosis
Functions of cathepsin K in bone resorption. Lessons from cathepsin K deficient mice.
Osteopetrosis
Impaired bone resorption in cathepsin K-deficient mice is partially compensated for by enhanced osteoclastogenesis and increased expression of other proteases via an increased RANKL/OPG ratio.
Osteopetrosis
Linking osteopetrosis and pycnodysostosis: regulation of cathepsin K expression by the microphthalmia transcription factor family.
Osteopetrosis
Novel pycnodysostosis mouse model uncovers cathepsin K function as a potential regulator of osteoclast apoptosis and senescence.
Osteopetrosis
Odontoblast-like MDPC-23 cells function as odontoclasts with the RANKL/M-CSF induction.
Osteopetrosis
Preservation of type H vessels and osteoblasts by enhanced preosteoclast platelet-derived growth factor type BB attenuates glucocorticoid-induced osteoporosis in growing mice.
Osteopetrosis
The resorptive apparatus of osteoclasts supports lysosomotropism and increases potency of basic versus non-basic inhibitors of cathepsin K.
Osteopetrosis
The role of cathepsin K in normal bone resorption.
Osteopetrosis
[A benign form of osteopetrosis. Case report]
Osteophyte
Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts.
Osteophyte
The relative importance of cysteine peptidases in osteoarthritis.
Osteoporosis
3D-QSAR and docking studies of aldehyde inhibitors of human cathepsin K.
Osteoporosis
A nonsense mutation in the cathepsin K gene observed in a family with pycnodysostosis.
Osteoporosis
A novel allosteric mechanism in the cysteine peptidase cathepsin K discovered by computational methods.
Osteoporosis
A novel approach to inhibit bone resorption: exosite inhibitors against cathepsin K.
Osteoporosis
A novel class of nonpeptidic biaryl inhibitors of human cathepsin K.
Osteoporosis
Advances in the discovery of cathepsin K inhibitors on bone resorption.
Osteoporosis
An allosteric site enables fine-tuning of cathepsin K by diverse effectors.
Osteoporosis
An atypical subtrochanteric femoral fracture from pycnodysostosis: a lesson from nature.
Osteoporosis
An orally active cathepsin K inhibitor, furan-2-carboxylic acid, 1-{1-[4-fluoro-2-(2-oxo-pyrrolidin-1-yl)-phenyl]-3-oxo-piperidin-4-ylcarbamoyl}-cyclohexyl)-amide (OST-4077), inhibits osteoclast activity in vitro and bone loss in ovariectomized rats.
Osteoporosis
Articular cartilage protection in Ctsk-/- mice is associated with cellular and molecular changes in subchondral bone and cartilage matrix.
Osteoporosis
Balicatib, a cathepsin K inhibitor, stimulates periosteal bone formation in monkeys.
Osteoporosis
Bone metabolism in 2012: Novel osteoporosis targets.
Osteoporosis
Bone-Targeting AAV-Mediated Gene Silencing in Osteoclasts for Osteoporosis Therapy.
Osteoporosis
Carbon-11 labeled cathepsin K inhibitors: Syntheses and preliminary in vivo evaluation.
Osteoporosis
Cathepsin cysteine proteases in cardiovascular disease.
Osteoporosis
Cathepsin K and the design of inhibitors of cathepsin K.
Osteoporosis
Cathepsin K deficiency in mice induces structural and metabolic changes in the central nervous system that are associated with learning and memory deficits.
Osteoporosis
Cathepsin K Deficiency Suppresses Disuse-Induced Bone Loss.
Osteoporosis
Cathepsin K Inhibition: A New Mechanism for the Treatment of Osteoporosis.
Osteoporosis
Cathepsin K inhibitor causes changes in crystallinity and crystal structure of newly-formed mandibular bone in rats.
Osteoporosis
Cathepsin K inhibitor-polymer conjugates: potential drugs for the treatment of osteoporosis and rheumatoid arthritis.
Osteoporosis
Cathepsin K inhibitors as treatment of bone metastasis.
Osteoporosis
Cathepsin K inhibitors for osteoporosis and potential off-target effects.
Osteoporosis
Cathepsin K Inhibitors for Osteoporosis: Biology, Potential Clinical Utility, and Lessons Learned.
Osteoporosis
Cathepsin K inhibitors increase distal femoral bone mineral density in rapidly growing rabbits.
Osteoporosis
Cathepsin K Inhibitors: A Novel Target but Promising Approach in the Treatment of Osteoporosis.
Osteoporosis
Cathepsin K inhibitors: a novel target for osteoporosis therapy.
Osteoporosis
Cathepsin K inhibitors: emerging treatment options for osteoporosis.
Osteoporosis
Cathepsin K Localizes to Equine Bone
Osteoporosis
Cathepsin K osteoporosis trials, pycnodysostosis and mouse deficiency models: Commonalities and differences.
Osteoporosis
Cathepsin K, osteoclastic resorption, and osteoporosis therapy.
Osteoporosis
Cathepsin K: a unique collagenolytic cysteine peptidase.
Osteoporosis
Cathepsin K: its skeletal actions and role as a therapeutic target in osteoporosis.
Osteoporosis
Changes in micro-CT 3D bone parameters reflect effects of a potent cathepsin K inhibitor (SB-553484) on bone resorption and cortical bone formation in ovariectomized mice.
Osteoporosis
Circulating cathepsin K and cystatin C in patients with cancer related bone disease: clinical and therapeutic implications.
Osteoporosis
Clinical and translational pharmacology of the cathepsin K inhibitor odanacatib studied for osteoporosis.
Osteoporosis
Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate.
Osteoporosis
Comparative proteomic and metabolomic analysis reveal the antiosteoporotic molecular mechanism of icariin from Epimedium brevicornu Maxim.
Osteoporosis
Congress Report: 5th Central and Eastern Europe (CEE) Summit on Osteoporosis in Bratislava, 2-3 December 2011.
Osteoporosis
Cyclic ketone inhibitors of the cysteine protease cathepsin K.
Osteoporosis
Cynomolgus monkey (Macaca fascicularis) cathepsin K: cloning, expression, purification, and activation.
Osteoporosis
Design and synthesis of tri-ring P3 benzamide-containing aminonitriles as potent, selective, orally effective inhibitors of cathepsin K.
Osteoporosis
Design of cathepsin k inhibitors for osteoporosis.
Osteoporosis
Design of potent, selective, and orally bioavailable inhibitors of cysteine protease cathepsin k.
Osteoporosis
Detection of femtomole quantities of mature cathepsin K with zymography.
Osteoporosis
Development of N-(Functionalized benzoyl)-homocycloleucyl-glycinonitriles as Potent Cathepsin K Inhibitors.
Osteoporosis
Discovery of a New Class of Cathepsin K Inhibitors in Rhizoma Drynariae as Potential Candidates for the Treatment of Osteoporosis.
Osteoporosis
Disposition and metabolism of the cathepsin k inhibitor odanacatib in humans.
Osteoporosis
Drug-induced morphea: report of a case induced by balicatib and review of the literature.
Osteoporosis
Drynaria total flavonoids decrease cathepsin K expression in ovariectomized rats.
Osteoporosis
Effect of cathepsin k inhibitor basicity on in vivo off-target activities.
Osteoporosis
Effect of odanacatib on bone turnover markers, bone density and geometry of the spine and hip of ovariectomized monkeys: A head-to-head comparison with alendronate.
Osteoporosis
Effect of the Cathepsin K Inhibitor Odanacatib on Bone Resorption Biomarkers in Healthy Postmenopausal Women: Two Double-Blind, Randomized, Placebo-Controlled Phase I Studies.
Osteoporosis
Effects of cysteine proteases on the structural and mechanical properties of collagen fibers.
Osteoporosis
Effects of Odanacatib on Bone Structure and Quality in Postmenopausal Women with Osteoporosis: 5-year Data from the Phase 3 Long-Term Odanacatib Fracture Trial (LOFT) and its Extension.
Osteoporosis
Efficacy of calcium supplementation for human bone health by mass spectrometry profiling and cathepsin K measurement in plasma samples.
Osteoporosis
Efficiency of turnip bioactive lipids in treating osteoporosis through activation of Osterix and suppression of Cathepsin K and TNF-? signaling in rats.
Osteoporosis
Emerging roles of cysteine cathepsins in disease and their potential as drug targets.
Osteoporosis
Formulation of self-microemulsifying drug delivery system (SMEDDS) by D-optimal mixture design to enhance the oral bioavailability of a new cathepsin K inhibitor (HL235).
Osteoporosis
From disease to treatment: from rare skeletal disorders to treatments for osteoporosis.
Osteoporosis
Future Developments in Osteoporosis Therapy.
Osteoporosis
Future directions in osteoporosis therapeutics.
Osteoporosis
Future of anticathepsin K drugs: dual therapy for skeletal disease and atherosclerosis?
Osteoporosis
Gumi Bao decoction regulates bone metabolism-related mRNA expression in glucocorticoid-induced osteoporosis in rats.
Osteoporosis
Identification of a nonbasic, nitrile-containing cathepsin K inhibitor (MK-1256) that is efficacious in a monkey model of osteoporosis.
Osteoporosis
Inhibition of bone resorption by the cathepsin K inhibitor odanacatib is fully reversible.
Osteoporosis
Inhibition of cathepsin k for treatment of osteoporosis.
Osteoporosis
Inhibition of cathepsin K promotes osseointegration of titanium implants in ovariectomised rats.
Osteoporosis
Inhibition of Cathepsin K: A Novel and Promising Treatment for Osteoporosis.
Osteoporosis
Inhibition of Osteoclast Differentiation by Ginsenoside Rg3 in RAW264.7 Cells via RANKL, JNK and p38 MAPK Pathways Through a Modulation of Cathepsin K: An In Silico and In Vitro Study.
Osteoporosis
Inhibitors of cathepsin K: a patent review (2004 - 2010).
Osteoporosis
Interventional value of total flavonoids from Rhizoma Drynariae on Cathepsin K, a potential target of osteoporosis.
Osteoporosis
Keto-1,3,4-oxadiazoles as cathepsin K inhibitors.
Osteoporosis
Laboratory control of the osteoresorptive effects of glucorcorticoids in patients with purpose colitis.
Osteoporosis
Leucocyte cathepsin K affects atherosclerotic lesion composition and bone mineral density in low-density lipoprotein receptor deficient mice.
Osteoporosis
Lysosomotropism of basic cathepsin K inhibitors contributes to increased cellular potencies against off-target cathepsins and reduced functional selectivity.
Osteoporosis
Modeling and simulation of bone mineral density response from a phase 2 study of ONO-5334, a new cathepsin K inhibitor, to support dose selection in osteoporosis.
Osteoporosis
Morning vs evening dosing of the cathepsin K inhibitor ONO-5334: effects on bone resorption in postmenopausal women in a randomized, phase 1 trial.
Osteoporosis
Morphea-like skin reactions in patients treated with the cathepsin K inhibitor balicatib.
Osteoporosis
Multiparameter analysis of serum levels of C-telopeptide crosslaps, bone-specific alkaline phosphatase, cathepsin K, osteoprotegerin and receptor activator of nuclear factor ?B ligand in the diagnosis of osteoporosis.
Osteoporosis
New antiresorptive therapies for postmenopausal osteoporosis.
Osteoporosis
New horizons in treatment of osteoporosis.
Osteoporosis
Non-covalent cathepsin k inhibitors for the treatment of osteoporosis.
Osteoporosis
Nonclinical and clinical pharmacological characterization of the potent and selective cathepsin K inhibitor MIV-711.
Osteoporosis
Novel advances in the treatment of osteoporosis.
Osteoporosis
Odanacatib for the treatment of osteoporosis.
Osteoporosis
Odanacatib Pharmacokinetics Comparison Between Chinese and Non-Chinese Postmenopausal Women.
Osteoporosis
Odanacatib reduces bone turnover and increases bone mass in the lumbar spine of skeletally mature ovariectomized rhesus monkeys.
Osteoporosis
Odanacatib, a Cathepsin K Cysteine Protease Inhibitor, Kills Hookworm In Vivo.
Osteoporosis
Odanacatib, a cathepsin K inhibitor for the treatment of osteoporosis and other skeletal disorders associated with excessive bone remodeling.
Osteoporosis
Odanacatib, a Cathepsin-K Inhibitor for Osteoporosis: A Two-Year Study in Postmenopausal Women With Low Bone Density.
Osteoporosis
Odanacatib, a new drug for the treatment of osteoporosis: review of the results in postmenopausal women.
Osteoporosis
Odanacatib, a Selective Cathepsin K inhibitor to Treat Osteoporosis: Safety, Tolerability, Pharmacokinetics and Pharmacodynamics - Results from Single Oral Dose Studies in Healthy Volunteers.
Osteoporosis
Odanacatib, a selective cathepsin K inhibitor, demonstrates comparable pharmacodynamics and pharmacokinetics in older men and postmenopausal women.
Osteoporosis
Odanacatib, effects of 16-month treatment and discontinuation of therapy on bone mass, turnover and strength in the ovariectomized rabbit model of osteopenia.
Osteoporosis
Osteopenia due to enhanced cathepsin K release by BK channel ablation in osteoclasts.
Osteoporosis
Osteoporosis in Rheumatic Diseases: Anti-rheumatic Drugs and the Skeleton.
Osteoporosis
Osteoporosis: A Review of Treatment Options.
Osteoporosis
Peptide aldehyde inhibitors of cathepsin K inhibit bone resorption both in vitro and in vivo.
Osteoporosis
Peptidomimetic inhibitors of cathepsin K.
Osteoporosis
Pharmacodynamic Effects on Biochemical Markers of Bone Turnover and Pharmacokinetics of the Cathepsin K Inhibitor, ONO-5334, in an Ascending Multiple-Dose, Phase 1 Study.
Osteoporosis
Pharmacological inhibitors to identify roles of cathepsin K in cell-based studies: a comparison of available tools.
Osteoporosis
Pharmacological topics of bone metabolism: recent advances in pharmacological management of osteoporosis.
Osteoporosis
Population pharmacokinetic and pharmacodynamic modeling of different formulations of ONO-5334, cathepsin K inhibitor, in Caucasian and Japanese postmenopausal females.
Osteoporosis
Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides.
Osteoporosis
Potent and selective ketoamide-based inhibitors of cysteine protease, cathepsin K.
Osteoporosis
Potential role of odanacatib in the treatment of osteoporosis.
Osteoporosis
Preclinical evaluation of [11 C]L-235 as a radioligand for Positron Emission Tomography cathepsin K imaging in bone.
Osteoporosis
Preparation of active recombinant cathepsin K expressed in bacteria as inclusion body.
Osteoporosis
Probing the activity modification space of the cysteine peptidase cathepsin K with novel allosteric modifiers.
Osteoporosis
Protective effect of resveratrol on estrogen deficiency-induced osteoporosis though attenuating NADPH oxidase 4/nuclear factor kappa B pathway by increasing miR-92b-3p expression.
Osteoporosis
Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification.
Osteoporosis
Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency.
Osteoporosis
Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease.
Osteoporosis
Randomized, controlled trial to assess the safety and efficacy of odanacatib in the treatment of men with osteoporosis.
Osteoporosis
Role of cathepsin K in structural changes in brachiocephalic artery during progression of atherosclerosis in apoE-deficient mice.
Osteoporosis
Serum cathepsin K as a marker of bone metabolism in postmenopausal women treated with alendronate.
Osteoporosis
Serum Cathepsin K levels are not suitable to differentiate women with chronic bone disorders such as osteopenia and osteoporosis from healthy pre- and postmenopausal women.
Osteoporosis
Serum cathepsin K levels of patients with longstanding rheumatoid arthritis: correlation with radiological destruction.
Osteoporosis
Soluble cathepsin K: a novel marker for the prediction of nontraumatic fractures?
Osteoporosis
Structural basis of collagen fiber degradation by cathepsin K.
Osteoporosis
Structural requirements for the collagenase and elastase activity of cathepsin K and its selective inhibition by an exosite inhibitor.
Osteoporosis
Tanshinones that selectively block the collagenase activity of cathepsin K provide a novel class of ectosteric antiresorptive agents for bone.
Osteoporosis
The development and characterization of an ELISA specifically detecting the active form of cathepsin K.
Osteoporosis
The effect of cathepsin K deficiency on airway development and TGF-?1 degradation.
Osteoporosis
The future of osteoporosis treatment - a research update.
Osteoporosis
The new partnership of genomics and chemistry for accelerated drug development.
Osteoporosis
The preventive effect of Cuscutae Semen polysaccharide on bone loss in the ovariectomized rat model.
Osteoporosis
The role of cathepsin K in normal bone resorption.
Osteoporosis
The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics.
Osteoporosis
Treatment with zoledronic acid subsequent to odanacatib prevents bone loss in postmenopausal women with osteoporosis.
Osteoporosis
Virtual screening of cathepsin k inhibitors using docking and pharmacophore models.
Osteoporosis
[Cathepsin K and matrix metalloproteases activity in the bone tissue of OXYS rats with developing osteoporosis].
Osteoporosis
[New approach for osteoporosis treatment: cathepsin K inhibitor, ONO-5334].
Osteoporosis
[Odanacatib (MK-0822)].
Osteoporosis
[Osteoporosis]
Osteoporosis
[Reducing bone resorption by cathepsin K inhibitor and treatment of osteoporosis].
Osteoporosis
[Up-and-coming therapeutics for osteoporosis].
Osteoporosis, Postmenopausal
Antiresorptive effect of a cathepsin K inhibitor ONO-5334 and its relationship to BMD increase in a phase II trial for postmenopausal osteoporosis.
Osteoporosis, Postmenopausal
Changes in micro-CT 3D bone parameters reflect effects of a potent cathepsin K inhibitor (SB-553484) on bone resorption and cortical bone formation in ovariectomized mice.
Osteoporosis, Postmenopausal
Discovery of a New Class of Cathepsin K Inhibitors in Rhizoma Drynariae as Potential Candidates for the Treatment of Osteoporosis.
Osteoporosis, Postmenopausal
Effect of ONO-5334 on bone mineral density and biochemical markers of bone turnover in postmenopausal osteoporosis: 2-year results from the OCEAN study.
Osteoporosis, Postmenopausal
Effect of SI-591, a new class of cathepsin K inhibitor with peptidomimetic structure, on bone metabolism in vitro and in vivo.
Osteoporosis, Postmenopausal
Effects of Odanacatib on the Radius and Tibia of Postmenopausal Women: Improvements in Bone Geometry, Microarchitecture and Estimated Bone Strength.
Osteoporosis, Postmenopausal
New targets for intervention in the treatment of postmenopausal osteoporosis.
Osteoporosis, Postmenopausal
Odanacatib for the treatment of postmenopausal osteoporosis.
Osteoporosis, Postmenopausal
Odanacatib for the treatment of postmenopausal osteoporosis: development history and design and participant characteristics of LOFT, the Long-Term Odanacatib Fracture Trial.
Osteoporosis, Postmenopausal
Odanacatib, a cathepsin K inhibitor for the treatment of osteoporosis and other skeletal disorders associated with excessive bone remodeling.
Osteoporosis, Postmenopausal
Odanacatib: a review of its potential in the management of osteoporosis in postmenopausal women.
Osteoporosis, Postmenopausal
Pharmacological inhibition of cathepsin K: A promising novel approach for postmenopausal osteoporosis therapy.
Osteoporosis, Postmenopausal
Potent and selective inhibition of human cathepsin K leads to inhibition of bone resorption in vivo in a nonhuman primate.
Osteoporosis, Postmenopausal
Safety and efficacy of the Cathepsin K inhibitor, ONO-5334, in postmenopausal osteoporosis - the OCEAN study.
Osteoporosis, Postmenopausal
Serum cathepsin K as a marker of bone metabolism in postmenopausal women treated with alendronate.
Osteoporosis, Postmenopausal
Serum cathepsin K concentrations reflect osteoclastic activity in women with postmenopausal osteoporosis and patients with Paget's disease.
Osteoporosis, Postmenopausal
The cathepsin K inhibitor AAE581 induces morphological changes in osteoclasts of treated patients.
Osteoporosis, Postmenopausal
The effect of the cathepsin K inhibitor ONO-5334 on trabecular and cortical bone in postmenopausal osteoporosis: The OCEAN study.
Osteoporosis, Postmenopausal
The effects of the cathepsin K inhibitor odanacatib on osteoclastic bone resorption and vesicular trafficking.
Osteoporosis, Postmenopausal
Treatment of postmenopausal osteoporosis with odanacatib.
Osteoradionecrosis
Increased numbers of osteoclasts expressing cysteine proteinase cathepsin K in patients with infected osteoradionecrosis and bisphosphonate-associated osteonecrosis-a paradoxical observation?
Osteosarcoma
An Activity-Based Probe for Cathepsin K Imaging with Excellent Potency and Selectivity.
Osteosarcoma
Cathepsin K expression and activity in canine osteosarcoma.
Osteosarcoma
Cathepsins and osteosarcoma: Expression analysis identifies cathepsin K as an indicator of metastasis.
Osteosarcoma
Cysteine proteinases in chondrosarcomas.
Osteosclerosis
Ablation of cathepsin k activity in the young mouse causes hypermineralization of long bone and growth plates.
Osteosclerosis
Current research on pycnodysostosis.
Osteosclerosis
Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice.
Osteosclerosis
Mechanisms of the anabolic effects of teriparatide on bone: insight from the treatment of a patient with pycnodysostosis.
Osteosclerosis
Orthognathic surgery in pycnodysostosis: a case report.
Osteosclerosis
The role of cathepsin K in normal bone resorption.
Osteosclerosis
Use of CBCT in the orthodontic diagnosis of a patient with pycnodysostosis.
Paget Disease, Extramammary
Overexpression of stromal cathepsin K expression correlates with invasiveness of extramammary Paget's disease.
Papilledema
Multisuture Craniosynostosis and Papilledema in Pycnodysostosis: A Paradox?
Paraganglioma
A broad survey of cathepsin K immunoreactivity in human neoplasms.
Peri-Implantitis
Cathepsin K levels in the crevicular fluid of dental implants: a pilot study.
Peri-Implantitis
Estimation of Bone Loss Biomarkers as a Diagnostic Tool for Peri-Implantitis.
Peri-Implantitis
Microbiological Profile and Human Immune Response Associated with Peri-Implantitis: A Systematic Review.
Peri-Implantitis
[Diagnostic possibilities of laboratory assessment of cathepsin K activity in gingival and peri-implant fluid under normal conditions and periimplantitis].
Peri-Implantitis
[Osteoimmunological aspects of periodontal inflammatory destructive changes at periimplantitis, chronic periodontitis and oncological diseases of the oral cavity].
Periapical Diseases
A small molecule, Odanacatib, inhibits inflammation and bone loss caused by endodontic disease.
Periapical Granuloma
Participation of osteoclastogenic factors in immunopathogenesis of human chronic periapical lesions.
Periapical Periodontitis
Ovariectomy Exacerbates Apical Periodontitis in Rats with an Increase in Expression of Proinflammatory Cytokines and Matrix Metalloproteinases.
Periodontal Diseases
Elevated Expression of Cathepsin K in Periodontal Ligament Fibroblast by Inflammatory Cytokines Accelerates Osteoclastogenesis via Paracrine Mechanism in Periodontal Disease.
Periodontal Diseases
Expression of cathepsin-K in gingival crevicular fluid of patients with periodontitis.
Periodontal Diseases
The silencing of cathepsin K used in gene therapy for periodontal disease reveals the role of cathepsin K in chronic infection and inflammation.
Periodontal Pocket
[Osteoimmunological aspects of periodontal inflammatory destructive changes at periimplantitis, chronic periodontitis and oncological diseases of the oral cavity].
Periodontitis
Azilsartan increases levels of IL-10, down-regulates MMP-2, MMP-9, RANKL/RANK, Cathepsin K and up-regulates OPG in an experimental periodontitis model.
Periodontitis
Cathepsin K Localizes to Equine Bone
Periodontitis
Deficiency of cathepsin K prevents inflammation and bone erosion in rheumatoid arthritis and periodontitis and reveals its shared osteoimmune role.
Periodontitis
Effect of nonsurgical periodontal therapy on crevicular fluid levels of Cathepsin K in periodontitis.
Periodontitis
Effects of Probiotic Culture Supernatant on Cariogenic Biofilm Formation and RANKL-Induced Osteoclastogenesis in RAW 264.7 Macrophages.
Periodontitis
Expression of cathepsin K in periodontitis and in gingival fibroblasts.
Periodontitis
Expression of cathepsin-K in gingival crevicular fluid of patients with periodontitis.
Periodontitis
Inhibition of cathepsin K alleviates autophagy-related inflammation in periodontitis-aggravating arthritis.
Periodontitis
Inhibition of Ctsk modulates periodontitis with arthritis via downregulation of TLR9 and autophagy.
Periodontitis
Role of enhancer of zeste homolog 2 in osteoclast formation and periodontitis development by downregulating microRNA-101-regulated VCAM-1.
Periodontitis
The silencing of cathepsin K used in gene therapy for periodontal disease reveals the role of cathepsin K in chronic infection and inflammation.
Perivascular Epithelioid Cell Neoplasms
A distinctive subset of PEComas harbors TFE3 gene fusions.
Perivascular Epithelioid Cell Neoplasms
Angiomyomatous Hamartoma of Lymph Nodes, Revisited: Clinico-pathologic Study of 21 Cases, Emphasizing Its Distinction from Lymphangioleiomyomatosis of Lymph Nodes.
Perivascular Epithelioid Cell Neoplasms
Cathepsin K (Clone EPR19992) Demonstrates Uniformly Positive Immunoreactivity in Renal Oncocytoma, Chromophobe Renal Cell Carcinoma, and Distal Tubules.
Perivascular Epithelioid Cell Neoplasms
Cathepsin K expression in a wide spectrum of perivascular epithelioid cell neoplasms (PEComas): a clinicopathological study emphasizing extrarenal PEComas.
Perivascular Epithelioid Cell Neoplasms
Cathepsin K expression in clear cell "sugar" tumor (PEComa) of the lung.
Perivascular Epithelioid Cell Neoplasms
Cathepsin K expression in the spectrum of perivascular epithelioid cell (PEC) lesions of the kidney.
Perivascular Epithelioid Cell Neoplasms
Cathepsin K in the immunohistochemical diagnosis of melanocytic lesions.
Perivascular Epithelioid Cell Neoplasms
Cathepsin K is Superior to HMB45 for the Diagnosis of Pulmonary Lymphangioleiomyomatosis.
Perivascular Epithelioid Cell Neoplasms
PEComas of the kidney and of the genitourinary tract.
Perivascular Epithelioid Cell Neoplasms
PNL2: A Useful Adjunct Biomarker to HMB45 in the Diagnosis of Uterine Perivascular Epithelioid Cell Tumor (PEComa).
Perivascular Epithelioid Cell Neoplasms
PNL2: An Adjunctive Biomarker for Renal Angiomyolipomas and PEComas.
Perivascular Epithelioid Cell Neoplasms
TFE3-Fusion Variant Analysis Defines Specific Clinicopathologic Associations Among Xp11 Translocation Cancers.
Persistent Infection
The silencing of cathepsin K used in gene therapy for periodontal disease reveals the role of cathepsin K in chronic infection and inflammation.
Pituitary Neoplasms
Cathepsin K: The association between Cathepsin K expression and sphenoid sinus invasion of pituitary adenomas.
Prostatic Hyperplasia
Circulating cathepsin K and cystatin C in patients with cancer related bone disease: clinical and therapeutic implications.
Prostatic Neoplasms
Anti-IL-20 Monoclonal Antibody Suppresses Prostate Cancer Growth and Bone Osteolysis in Murine Models.
Prostatic Neoplasms
Cathepsin K in the bone microenvironment: link between obesity and prostate cancer?
Prostatic Neoplasms
Cathepsin K mRNA and protein expression in prostate cancer progression.
Prostatic Neoplasms
Cathepsin K: The association between Cathepsin K expression and sphenoid sinus invasion of pituitary adenomas.
Prostatic Neoplasms
Circulating cathepsin K and cystatin C in patients with cancer related bone disease: clinical and therapeutic implications.
Prostatic Neoplasms
Does increased local bone resorption secondary to breast and prostate cancer result in increased cartilage degradation?
Prostatic Neoplasms
Serum interleukin-6 in patients with metastatic bone disease: correlation with cystatin C.
Prostatic Neoplasms
Targeting cathepsin K diminishes prostate cancer establishment and growth in murine bone.
Psoriasis
Effect of Vitamin D on Peripheral Blood Mononuclear Cells from Patients with Psoriasis Vulgaris and Psoriatic Arthritis.
Pulmonary Disease, Chronic Obstructive
Cigarette smoke activates the proto-oncogene c-src to promote airway inflammation and lung tissue destruction.
Pulmonary Fibrosis
Cathepsin K expression is diminished in infants with bronchopulmonary dysplasia.
Pulmonary Fibrosis
Overexpression of cathepsin K in mice decreases collagen deposition and lung resistance in response to bleomycin-induced pulmonary fibrosis.
Pycnodysostosis
A Case Report of Pycnodysostosis Associated with Multiple Pituitary Hormone Deficiencies and Response to Treatment
Pycnodysostosis
A case report of pycnodysostosis with atypical femur fracture diagnosed by next-generation sequencing of candidate genes.
Pycnodysostosis
A nonsense mutation in the cathepsin K gene observed in a family with pycnodysostosis.
Pycnodysostosis
A novel missense mutation in cathepsin K (CTSK) gene in a consanguineous Pakistani family with pycnodysostosis.
Pycnodysostosis
A novel mutation (R122Q) in the cathepsin K gene in a Chinese child with Pyknodysostosis.
Pycnodysostosis
A patient with pycnodysostosis presenting with seizures and porencephalic cysts.
Pycnodysostosis
A rare case of pycnodysostosis: Technical difficulties in managing long bone fractures.
Pycnodysostosis
Ablation of cathepsin k activity in the young mouse causes hypermineralization of long bone and growth plates.
Pycnodysostosis
Alternative Method for Full Oral Rehabilitation in Patients with Pycnodysostosis Syndrome: ?A Case Report.
Pycnodysostosis
An animal model for pycnodysostosis: the role of cathepsin K in bone remodelling.
Pycnodysostosis
Articular cartilage protection in Ctsk-/- mice is associated with cellular and molecular changes in subchondral bone and cartilage matrix.
Pycnodysostosis
Atypical femur fractures in a patient with pycnodysostosis: a case report.
Pycnodysostosis
Bilateral subtrochanteric femoral fracture due to a very rare disease: Pycnodisostosis.
Pycnodysostosis
Cathepsin K analysis in a pycnodysostosis cohort: demographic, genotypic and phenotypic features.
Pycnodysostosis
Cathepsin K and the design of inhibitors of cathepsin K.
Pycnodysostosis
Cathepsin K deficiency in pycnodysostosis results in accumulation of non-digested phagocytosed collagen in fibroblasts.
Pycnodysostosis
Cathepsin K gene mutations and 1q21 haplotypes in at patients with pycnodysostosis in an outbred population.
Pycnodysostosis
Cathepsin K Inhibitors for Osteoporosis: Biology, Potential Clinical Utility, and Lessons Learned.
Pycnodysostosis
Cathepsin K knockout mice develop osteopetrosis due to a deficit in matrix degradation but not demineralization.
Pycnodysostosis
Cathepsin K osteoporosis trials, pycnodysostosis and mouse deficiency models: Commonalities and differences.
Pycnodysostosis
Cathepsin K: isolation and characterization of the murine cDNA and genomic sequence, the homologue of the human pycnodysostosis gene.
Pycnodysostosis
Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis.
Pycnodysostosis
Characterization of the human extracellular matrix protein 1 gene on chromosome 1q21.
Pycnodysostosis
Clinical and animal research findings in pycnodysostosis and gene mutations of cathepsin K from 1996 to 2011.
Pycnodysostosis
Clinical and genetic evaluation of Danish patients with pycnodysostosis.
Pycnodysostosis
Clinical and Radiographic Features of Pycnodysostosis with Emphasis on Dentofacial Problems.
Pycnodysostosis
Clinical disorders of bone resorption.
Pycnodysostosis
Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate.
Pycnodysostosis
Craniosynostosis in pycnodysostosis: broadening the spectrum of the cranial flat bone abnormalities.
Pycnodysostosis
Current research on pycnodysostosis.
Pycnodysostosis
Decreased bone turnover and deterioration of bone structure in two cases of pycnodysostosis.
Pycnodysostosis
Determination of bone markers in pycnodysostosis: effects of cathepsin K deficiency on bone matrix degradation.
Pycnodysostosis
Disturbed remodeling and delayed fracture healing in pediatric pycnodysostosis patients.
Pycnodysostosis
Effects of cathepsin K on Emdogain-induced hard tissue formation by human periodontal ligament stem cells.
Pycnodysostosis
Erosive arthritis in a patient with pycnodysostosis: an experiment of nature.
Pycnodysostosis
From disease to treatment: from rare skeletal disorders to treatments for osteoporosis.
Pycnodysostosis
Functions of cathepsin K in bone resorption. Lessons from cathepsin K deficient mice.
Pycnodysostosis
Genetic study of eight Egyptian patients with pycnodysostosis: identification of novel CTSK mutations and founder effect.
Pycnodysostosis
Human osteopetrosis and other sclerosing disorders: recent genetic developments.
Pycnodysostosis
Ichthyosis vulgaris and pycnodysostosis: an unusual occurrence.
Pycnodysostosis
Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice.
Pycnodysostosis
Increased Bone Resorption during Lactation in Pycnodysostosis.
Pycnodysostosis
Linking osteopetrosis and pycnodysostosis: regulation of cathepsin K expression by the microphthalmia transcription factor family.
Pycnodysostosis
Mechanisms of the anabolic effects of teriparatide on bone: insight from the treatment of a patient with pycnodysostosis.
Pycnodysostosis
Molecular analysis of a novel cathepsin K gene mutation in a Chinese child with pycnodysostosis.
Pycnodysostosis
Molecular and clinical analysis in a series of patients with Pyknodysostosis reveals some uncommon phenotypic findings.
Pycnodysostosis
Multiple Fractures and Impaired Bone Fracture Healing in a Patient with Pycnodysostosis and Hypophosphatasia.
Pycnodysostosis
Mutations of CTSK result in pycnodysostosis via a reduction in cathepsin K protein.
Pycnodysostosis
Near Normalization of Adult Height and Body Proportions by Growth Hormone in Pycnodysostosis.
Pycnodysostosis
Novel Compound Heterozygous Mutations in the Cathepsin K Gene in Japanese Female Siblings with Pyknodysostosis.
Pycnodysostosis
Novel Mutation and White Matter Involvement in an Indian Child with Pycnodysostosis.
Pycnodysostosis
Novel mutations of the cathepsin K gene in patients with pycnodysostosis and their characterization.
Pycnodysostosis
Novel pycnodysostosis mouse model uncovers cathepsin K function as a potential regulator of osteoclast apoptosis and senescence.
Pycnodysostosis
Orthognathic surgery in pycnodysostosis: a case report.
Pycnodysostosis
Osteopetrosis and osteoporosis: two sides of the same coin.
Pycnodysostosis
Pedicle stress fracture: an unusual complication of pycnodysostosis.
Pycnodysostosis
Pycnodysostosis at otorhinolaryngology.
Pycnodysostosis
Pycnodysostosis presenting as atypical stridor.
Pycnodysostosis
Pycnodysostosis with extreme sleep apnea: a possible alternative to tracheotomy.
Pycnodysostosis
Pycnodysostosis with novel gene mutation and sporadic medullary thyroid carcinoma: A case report.
Pycnodysostosis
Pycnodysostosis with Osteomyelitis of Maxilla: Case Report of Radiological Analysis.
Pycnodysostosis
Pycnodysostosis with unusual findings: a case report.
Pycnodysostosis
Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency.
Pycnodysostosis
Pycnodysostosis: Novel Variants in
Pycnodysostosis
Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease.
Pycnodysostosis
Pyknodysostosis: visceral manifestations and simian crease.
Pycnodysostosis
Recent advances in osteoclast biology and pathological bone resorption.
Pycnodysostosis
Structure and chromosomal assignment of the human cathepsin K gene.
Pycnodysostosis
The role of cathepsin K in normal bone resorption.
Pycnodysostosis
Upper airway surgery of obstructive sleep apnea in pycnodysostosis: Case report and literature review.
Pycnodysostosis
Use of CBCT in the orthodontic diagnosis of a patient with pycnodysostosis.
Pycnodysostosis
[Family picnodisostosis, report of a case after 10 years of follow-up].
Pycnodysostosis
[Pycnodysostosis--common ancestor of some Danish patients. Examination and diagnosis based on molecular genetics]
Pycnodysostosis
[Pycnodysostosis: A rare disease with frequent fractures.]
Radicular Cyst
Participation of osteoclastogenic factors in immunopathogenesis of human chronic periapical lesions.
Renal Insufficiency, Chronic
Impact of circulating cathepsin K on the coronary calcification and the clinical outcome in chronic kidney disease patients.
Renal Insufficiency, Chronic
Novel biological markers of bone: from bone metabolism to bone physiology.
Rheumatic Diseases
Osteoporosis in Rheumatic Diseases: Anti-rheumatic Drugs and the Skeleton.
Root Resorption
Chemerin/ChemR23 regulates cementoblast function and tooth resorption in mice via inflammatory factors.
Root Resorption
Comparison of expression patterns of cathepsin K and MMP-9 in odontoclasts and osteoclasts in physiological root resorption in the rat molar.
Root Resorption
Differentiation and functions of osteoclasts and odontoclasts in mineralized tissue resorption.
Root Resorption
Immunolocalization of vacuolar-type H+-ATPase, cathepsin K, matrix metalloproteinase-9, and receptor activator of NFkappaB ligand in odontoclasts during physiological root resorption of human deciduous teeth.
Root Resorption
In situ hybridization for matrix metalloproteinase-1 and cathepsin K in rat root-resorbing tissue induced by tooth movement.
Root Resorption
Localization of cathepsin K in bovine odontoclasts during deciduous tooth resorption.
Root Resorption
The effect of cathepsin K inhibitor surface treatment on delayed tooth replantation in dogs.
Root Resorption
[Expression of cathepsin K and IL-6 mRNA in root-resorbing tissue during tooth movement in rats]
Sacroiliitis
Interleukin 6 is not a crucial regulator in an animal model of tumour necrosis factor-mediated bilateral sacroiliitis.
Sarcoidosis
ApoE-deficient mice on cholate-containing high-fat diet reveal a pathology similar to lung sarcoidosis.
Sarcoidosis
Lack of cathepsin activities alter or prevent the development of lung granulomas in a mouse model of sarcoidosis.
Sarcoma
A broad survey of cathepsin K immunoreactivity in human neoplasms.
Sarcoma
Cathepsin K in the immunohistochemical diagnosis of melanocytic lesions.
Sarcoma
Differential expression of cathepsin K in neoplasms harboring TFE3 gene fusions.
Sarcoma, Alveolar Soft Part
A broad survey of cathepsin K immunoreactivity in human neoplasms.
Sarcoma, Alveolar Soft Part
Cathepsin K in the immunohistochemical diagnosis of melanocytic lesions.
Sarcoma, Alveolar Soft Part
Differential expression of cathepsin K in neoplasms harboring TFE3 gene fusions.
Scleroderma, Localized
Role of cathepsin K in the turnover of the dermal extracellular matrix during scar formation.
Spondylitis, Ankylosing
Expression of cathepsin K and MMP-1 indicate persistent osteodestruktive activity in longstanding ankylosing spondylitis.
Spondylitis, Ankylosing
Serum levels of MMP-3 and cathepsin K in patients with ankylosing spondylitis: effect of TNFalpha antagonist therapy.
Spondylitis, Ankylosing
The development and characterization of an ELISA specifically detecting the active form of cathepsin K.
Squamous Cell Carcinoma of Head and Neck
Cathepsin K associates with lymph node metastasis and poor prognosis in oral squamous cell carcinoma.
Squamous Cell Carcinoma of Head and Neck
Cathepsin k is present in invasive oral tongue squamous cell carcinoma in vivo and in vitro.
Squamous Cell Carcinoma of Head and Neck
Cathepsin K modulates invasion, migration and adhesion of oral squamous cell carcinomas in vitro.
Stomach Neoplasms
Coronin 3 promotes gastric cancer metastasis via the up-regulation of MMP-9 and cathepsin K.
Stuttering
Communication Attitude of Kannada-Speaking School-Age Children Who Do and Do Not Stutter.
Synovitis
Spontaneous development of synovitis and cartilage degeneration in transgenic mice overexpressing cathepsin K.
Tendinopathy
Involvement of multinucleated giant cells synthesizing cathepsin K in calcified tendinitis of the rotator cuff tendons.
Tendinopathy
Sequential, but not Concurrent, Incubation of Cathepsin K and L with Type I Collagen Results in Extended Proteolysis.
Thrombosis
Disruption of the cathepsin K gene reduces atherosclerosis progression and induces plaque fibrosis but accelerates macrophage foam cell formation.
Thyroid Neoplasms
High cathepsin K levels in men with differentiated thyroid cancer on suppressive L-thyroxine therapy.
Tooth Resorption
Localization of cathepsin K in bovine odontoclasts during deciduous tooth resorption.
Tuberculosis, Pulmonary
Cathepsin K Contributes to Cavitation and Collagen Turnover in Pulmonary Tuberculosis.
Vascular Calcification
Cathepsin-K is a potential cardiovascular risk biomarker in prevalent hemodialysis patients.
Vascular Calcification
Impact of circulating cathepsin K on the coronary calcification and the clinical outcome in chronic kidney disease patients.
Vascular Calcification
Novel biological markers of bone: from bone metabolism to bone physiology.
Vascular Diseases
Circulating cathepsin K as a potential novel biomarker of coronary artery disease.
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0.288
(1'S)-7-(1-aminoethyl)-2-(2-methoxyphenyl)pyrazolo[1,5-a] pyrimidine hydrochloride
25°C, pH 5.5
0.241
(1'S)-7-(1-aminoethyl)-2-(3-trifluoromethylphenyl)pyrazolo-[1,5-a]pyrimidine hydrochloride
25°C, pH 5.5
0.077
(1'S)-7-(1-aminoethyl)-2-benzyl-3-phenylpyrazolo[1,5-a]pyrimidine hydrochloride
25°C, pH 5.5
0.236
(1'S)-7-(1-aminoethyl)-2-phenylpyrazolo[1,5-a]pyrimidine hydrochloride
25°C, pH 5.5
0.595
(1'S)-7-(1-aminoethyl)pyrazolo[1,5-a]pyrimidine-3-(N-methylcarboxamide) hydrochloride
25°C, pH 5.5
0.714
(1'S)-7-(1-aminoethyl)pyrazolo[1,5-a]pyrimidine-3-carboxylate hydrochloride
25°C, pH 5.5
0.0000025
1,4-anhydro-3,5,6-trideoxy-3-[(1-[4-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]benzamido]cyclohexane-1-carbonyl)amino]-L-erythro-hex-2-ulose
pH and temperature not specified in the publication
0.0000097
1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
37°C, pH 5.6
0.00001
2-amino-4-bromo-N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]benzamide
pH and temperature not specified in the publication
0.000006
Boc-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
37°C, pH 5.6
0.000022
dibenzyl [(2-oxopropane-1,3-diyl)bis[azanediyl[(2S)-4-methyl-1-oxopentane-1,2-diyl]]]biscarbamate
pH and temperature not specified in the publication
0.0000066
mPEG-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
37°C, pH 5.6
0.00000721
N'-cyano-N,N',4-trimethyl-2-(4'-(methylsulfonyl)-[1,1'-biphenyl]-3-yl)pentanehydrazide
racemic, pH and temperature not specified in the publication
0.00000114
N'-cyano-N,N',4-trimethyl-2-(4'-(methylsulfonyl)-[1,1'-biphenyl]-4-yl)pentanehydrazide
racemic, pH and temperature not specified in the publication
0.0000029
N'-cyano-N,N',4-trimethyl-2-([11,21:24,31-terphenyl]-14-yl)pentanehydrazide
pH and temperature not specified in the publication
0.0000014
N-(3-[[(3R)-3-([1,1'-biphenyl]-3-yl)-5-methylhex-1-en-2-yl]amino]-2-oxopropyl)-4-phenoxybenzene-1-sulfonamide
pH and temperature not specified in the publication
0.0000001
N-[(1S)-1-cyclohexyl-3-[(2Z)-2-[(4R)-3,4-dimethyl-1,3-thiazolidin-2-ylidene]hydrazinyl]-2,3-dioxopropyl]cycloheptanecarboxamide
pH and temperature not specified in the publication
0.0000087
N-[(2S)-4-methyl-1-oxo-1-[(3aS,6aR)-3-oxohexahydro-4H-furo[3,2-b]pyrrol-4-yl]pentan-2-yl]-4-(4-methylpiperazin-1-yl)benzamide
pH and temperature not specified in the publication
0.00000016
N-[(2S)-4-methyl-1-oxo-1-[[(4R)-3-oxo-1-(pyridine-2-sulfonyl)azepan-4-yl]amino]pentan-2-yl]-2,3-dihydro-1-benzofuran-2-carboxamide
pH and temperature not specified in the publication
0.0000006
N-[(2S)-4-methyl-1-[(3aS,6S,6aR)-6-methyl-3-oxohexahydro-4H-furo[3,2-b]pyrrol-4-yl]-1-oxopentan-2-yl]-4-[2-(1-methylpiperidin-4-yl)-1,3-thiazol-4-yl]benzamide
pH and temperature not specified in the publication
0.000000041
N-[(2S)-4-methyl-1-[[(4S,7R)-7-methyl-3-oxo-1-(pyridine-2-sulfonyl)azepan-4-yl]amino]-1-oxopentan-2-yl]-2,3-dihydro-1-benzofuran-2-carboxamide
pH and temperature not specified in the publication
0.028
NSC13345
at pH 5.5 and 25°C
0.00027
PHPMA-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
37°C, pH 5.6
0.000392
PHPMAGG-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
37°C, pH 5.6
0.0000113
STPHPMA-1-(N-benzyloxycarbonylleucyl)-5-(phenylalanylleucyl)carbohydrazide
37°C, pH 5.6
0.000002 - 0.000015
((S)-1-[1-[4(R,S)-((S)-2-benzyloxycarbonylamino-4-methylpentanoylamino)-3-oxoazepan-1-yl]methanoyl]-3-methylbutl)carbamic acid benzyl ester
0.0000023
((S)-1-[[(3R,S)-((S)-2-benzyloxycarbonylamino-4-methylpentanoylamino)-4-oxopyrrolidin-1-yl]methanoyl]-3-methylbutyl)carbamic acid benzyl ester
-
-
0.0000006
((S)-1-[[(3R,S)-((S)-2-benzyloxycarbonylmethylamino-4-methylpentanoylamino)-4-oxopyrrolidin-1-yl]methanoyl]-3-methylbutyl)carbamic acid benzyl ester
-
-
0.0000003
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[4'-(methylsulfanyl)biphenyl-2-yl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.0000017
(1R,2S)-N-(cyanomethyl)-2-[2-[4-(methylsulfanyl)phenyl]ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00000013
(2R)-2-[3'-[2-(4-tert-butylpiperazin-1-yl)-1,3-thiazol-4-yl]biphenyl-3-yl]-N-(cyanomethyl)-4-methylpentanamide
-
-
0.0000003
(2R)-N-(cyanomethyl)-2-[3'-(2-[[3-(dimethylamino)pyrrolidin-1-yl]methyl]-1,3-thiazol-4-yl)biphenyl-3-yl]-4-methylpentanamide
-
-
0.00000048
(2R)-N-(cyanomethyl)-4-methyl-2-[3'-[2-(piperazin-1-ylmethyl)-1,3-thiazol-4-yl]biphenyl-3-yl]pentanamide
-
-
0.0000008
(2R)-N-(cyanomethyl)-4-methyl-2-[4'-(4-methylpiperazin-1-yl)biphenyl-3-yl]pentanamide
-
-
0.018
(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
-
-
0.0019
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([2-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00024
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00073
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0015
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00029
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00043
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00045
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00057
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-3-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0011
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-4-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.001
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(thiophen-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.000098
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[methyl(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0012
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(methylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0022
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(phenylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0003
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-([[4-([[(dimethylamino)methyl]sulfonyl]amino)phenyl]carbonyl]amino)-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.005
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([2-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0007
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-fluoro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00056
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00047
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([4-[(ethylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0018
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2,4-dimethyl-1,3-thiazol-5-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00098
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00052
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00027
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00037
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0005
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0023
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-(methylsulfamoyl)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0017
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-([[4-(1-methylethyl)-1,3-thiazol-2-yl]sulfonyl]amino)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00042
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-sulfamoylphenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00064
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methyl-1H-imidazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0005
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methylethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0012
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2,2,2-trifluoroethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00055
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2-methylphenyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.003
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00026
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methylpyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0023
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(5-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00038
1,4-anhydro-3,5,6-trideoxy-3-[[4-methyl-N-(thiophen-3-ylcarbonyl)-L-leucyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00084
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0016
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0017
1,4-anhydro-3-[[(2S)-2-[([4-[(benzylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0015
1,4-anhydro-3-[[(2S)-2-[([4-[(butylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00044
1,4-anhydro-3-[[(2S)-2-[([4-[(cyclopropylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0008
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-chloropyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00082
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00073
1,4-anhydro-3-[[(2S)-2-[[(4-[[(3-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00095
1,4-anhydro-3-[[(2S)-2-[[(4-[[(4-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00095
1,4-anhydro-3-[[(2S)-2-[[(4-[[(cyclohexylmethyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.000006
1-(N-benzyloxycarbonyl-leucyl)-5-(N-Boc-phenylalanylleucyl)carbohydrazide
-
at 37°C, pH 6.0
0.0000027
2,2'-N,N'-bis(benzyloxycarbonyl)-L-leucinylcarbohydrazide
-
pH 5.5, room temperature
0.0005
2-methylpropyl [(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamate
-
-
0.0000025
3-(4-([4'-((1-[(cyanomethyl)carbamoyl]cyclohexyl)carbamoyl)biphenyl-4-yl]oxy)piperidin-1-yl)propanoic acid
-
Ki-value is below 0.0000025 mM
0.00023
3-bromo-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
0.00075
3-[[(2S)-2-[([3-acetyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.00095
3-[[(2S)-2-[[(4-[[(4-aminophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium phosphate, 5 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 6.5
0.0000025
4'-(4-tert-butylpiperazin-1-yl)-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)biphenyl-4-carboxamide
-
Ki-value is below 0.0000025 mM
0.0000025
4'-[4-(tert-butylamino)piperidin-1-yl]-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)biphenyl-4-carboxamide
-
Ki-value is below 0.0000025 mM
0.0000014
4-(2-[(3R)-3-aminopyrrolidin-1-yl]-1,3-thiazol-4-yl)-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
0.00000095
4-(dimethylamino)-N-[1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]benzamide
-
-
0.000054
4-(trifluoromethoxy)-N-(1-[[(1S)-1-([5-[3-(trifluoromethyl)phenyl]-1,3,4-oxadiazol-2-yl]carbonyl)butyl]carbamoyl]cyclohexyl)benzamide
-
-
0.00055
4-(trifluoromethoxy)-N-(1-[[(1S)-1-([5-[4-(trifluoromethyl)phenyl]-1,3,4-oxadiazol-2-yl]carbonyl)butyl]carbamoyl]cyclohexyl)benzamide
-
-
0.000032
4-amino-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
0.000018
4-bromo-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
0.000019
4-fluoro-N-[1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]benzamide
-
-
0.00000045
4-[2-(1,4'-bipiperidin-1'-yl)-1,3-thiazol-4-yl]-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
0.00000029
4-[2-(4-tert-butylpiperazin-1-yl)-1,3-thiazol-4-yl]-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)benzamide
-
-
0.000016
5-bromo-N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)thiophene-2-carboxamide
-
-
0.0000016
benzofuran-2-carboxylic acid [(S)-3-methyl-1-[2-oxo-3-(pyridin-2-ylsulfonylamino)propylcarbamoyl]butyl]amide
-
-
0.011
benzyl (1-[(cyanomethyl)carbamoyl]-2-hydroxypropyl)carbamate
-
-
0.00000025
benzyl (2S)-2-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)-4-methylpentanoate
-
Ki: value below 0.00000025 mM
0.00014
benzyl 1-cyano-3-pyrrolidinylcarbamate
-
pH 5.5, room temperature
0.003
benzyl [(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamate
-
-
0.03
benzyl [(1S)-2-[(cyanomethyl)amino]-1-(naphthalen-2-ylmethyl)-2-oxoethyl]carbamate
-
-
0.000084
benzyl [1-[(cyanomethyl)carbamoyl]cyclohexyl]carbamate
-
pH and temperature not specified in the publication
0.0000026 - 0.000147
cathepsin K propeptide
-
0.0000000041 - 0.0000000087
cystatin C
-
0.0000000054 - 0.0000000145
H-kininogen
-
0.0000000049 - 0.0000000135
L-kininogen
-
0.044
leupeptazin
-
pH and temperature not specified in the publication
0.0000025
MV061194
-
pH and temperature not specified in the publication
0.000000073
N-(1-([(cyanomethyl)amino]carbonyl)cyclohexyl)-4-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]benzamide
-
recombinant cathepsin K
0.00009
N-(1-cyano-3pyrrolidinyl)benzenesulfonamide
-
pH 5.5, room temperature
0.0000043
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(2-hydroxypropan-2-yl)biphenyl-4-yl]ethyl]-L-leucinamide
-
pH and temperature not specified in the publication
0.0000017
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1R)-2,2-difluoro-1-hydroxyethyl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
-
pH and temperature not specified in the publication
0.00001
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1S)-2,2-difluoro-1-hydroxyethyl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
-
pH and temperature not specified in the publication
0.00015
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-2-pyridin-4-yl-1,3-thiazole-4-carboxamide
-
-
0.0000025
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-(4-fluoropiperidin-4-yl)biphenyl-4-carboxamide
-
Ki-value is below 0.0000025 mM
0.000002
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-(dimethylamino)biphenyl-4-carboxamide
-
-
0.0000025
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-(piperazin-1-ylsulfonyl)biphenyl-4-carboxamide
-
Ki-value is below 0.0000025 mM
0.0000025
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-([(2S)-1-methylpyrrolidin-2-yl]methoxy)biphenyl-4-carboxamide
-
Ki-value is below 0.0000025 mM
0.0000025
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-([1-(2-hydroxyethyl)piperidin-4-yl]oxy)biphenyl-4-carboxamide
-
Ki-value is below 0.0000025 mM
0.0000061
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-([4-(2,2,2-trifluoroethyl)piperazin-1-yl]sulfonyl)biphenyl-4-carboxamide
-
-
0.0000054
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-isoxazol-5-ylbiphenyl-4-carboxamide
-
-
0.0000025
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-piperazin-1-ylbiphenyl-4-carboxamide
-
Ki-value is below 0.0000025 mM
0.00000067
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-[(1-methylpiperidin-3-yl)oxy]biphenyl-4-carboxamide
-
-
0.0000025
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-[(1-methylpiperidin-4-yl)oxy]biphenyl-4-carboxamide
-
Ki-value is below 0.0000025 mM
0.0000025
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4'-[methyl(1-methylpyrrolidin-3-yl)amino]biphenyl-4-carboxamide
-
Ki-value is below 0.0000025 mM
0.00000059
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-(4-[(1-methylethyl)amino]piperidin-1-yl)-1,3-thiazol-4-yl)benzamide
-
-
0.0000016
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-(4-[methyl(1-methylethyl)amino]piperidin-1-yl)-1,3-thiazol-4-yl)benzamide
-
-
0.0000023
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-morpholin-4-yl-1,3-thiazol-4-yl)benzamide
-
-
0.00000025
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[(4-methylpiperazin-1-yl)amino]-1,3-thiazol-4-yl)benzamide
-
-
0.0000016
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[(4-methylpiperazin-1-yl)methyl]-1,3-thiazol-4-yl)benzamide
-
-
0.00000079
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[3-(dimethylamino)pyrrolidin-1-yl]-1,3-thiazol-4-yl)benzamide
-
-
0.00000048
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[4-(2-methoxyethyl)piperazin-1-yl]-1,3-thiazol-4-yl)benzamide
-
-
0.00000047
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(2-[4-(tetrahydro-2H-pyran-4-yl)piperazin-1-yl]-1,3-thiazol-4-yl)benzamide
-
-
0.0000015
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(4-methylpiperazin-1-yl)benzamide
-
-
0.0000014
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(4-propylpiperazin-1-yl)benzamide
-
-
0.0000033
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-(dimethylamino)benzamide
-
-
0.000013
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-ethynylbenzamide
-
-
0.000019
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-morpholin-4-ylbenzamide
-
-
0.000014
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[(4-methylpiperazin-1-yl)carbonyl]benzamide
-
-
0.000013
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[(4-methylpiperazin-1-yl)sulfonyl]benzamide
-
-
0.00000095
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(1,4-dimethylpiperidin-4-yl)-1,3-thiazol-4-yl]benzamide
-
-
0.00000094
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(1-methylpiperidin-4-yl)-1,3-thiazol-4-yl]benzamide
-
-
0.0000025
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(4-morpholin-4-ylpiperidin-1-yl)-1,3-thiazol-4-yl]benzamide
-
Ki-value is below 0.0000025 mM
0.0000087
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(morpholin-4-ylmethyl)-1,3-thiazol-4-yl]benzamide
-
-
0.00000057
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)-4-[2-(piperidin-4-yloxy)-1,3-thiazol-4-yl]benzamide
-
-
0.00021
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)biphenyl-3-carboxamide
-
-
0.0000062
N-(1-[(cyanomethyl)carbamoyl]cyclohexyl)biphenyl-4-carboxamide
-
-
0.000035
N-(1-[[(1S)-1-[[5-(1-methylethyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamoyl]cyclohexyl)-4-(trifluoromethoxy)benzamide
-
-
0.000037
N-(1-[[(1S)-1-[[5-(3-methoxyphenyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamoyl]cyclohexyl)-4-(trifluoromethoxy)benzamide
-
-
0.000022
N-(1-[[(1S)-1-[[5-(4-methoxyphenyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamoyl]cyclohexyl)-4-(trifluoromethoxy)benzamide
-
-
0.000011
N-(2,3-dichlorophenyl)triazolyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
-
standard assay conditions
0.00041
N-(cyanomethyl)-1-[(3-phenylpropanoyl)amino]cyclohexanecarboxamide
-
-
0.00000008
N-(cyanomethyl)-4-methyl-2-[3'-(2-piperazin-1-yl-1,3-thiazol-4-yl)biphenyl-3-yl]pentanamide
-
-
0.00000013
N-(cyanomethyl)-4-methyl-2-[3'-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]biphenyl-3-yl]pentanamide
-
-
0.00000035
N-(cyanomethyl)-4-methyl-2-[4'-(2-piperazin-1-yl-1,3-thiazol-4-yl)biphenyl-3-yl]pentanamide
-
-
0.000015
N-4-benzyloxybenzoyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
-
standard assay conditions
0.00002
N-[(1-cyano-3-azetidinyl)methyl]benzenesulfonamide
-
pH 5.5, room temperature
0.00012
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
0.000054
N-[(1S)-1-((3-hydroxy-1-[(3-pyridin-2-ylphenyl)acetyl]azepan-4-yl)carbamoyl)-3-methylbutyl]-5-(2-morpholin-4-ylethoxy)-1-benzofuran-2-carboxamide
-
-
0.052
N-[(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]-2-phenylacetamide
-
-
0.0096
N-[(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]-3-phenylpropanamide
-
-
0.00012
N-[(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]-N2-(2,2,2-trifluoroethyl)-L-leucinamide
-
-
0.0000047
N-[(1S)-3-methyl-1-(((4R)-3-oxo-1-[(3-pyridin-2-ylphenyl)acetyl]azepan-4-yl)carbamoyl)butyl]-5-(2-morpholin-4-ylethoxy)-1-benzofuran-2-carboxamide
-
-
0.0000000048
N-[(1S)-3-methyl-1-([(4S)-3-oxo-1-[(3-pyridin-2-ylphenyl)acetyl]azepan-4-yl]carbamoyl)butyl]-5-(2-morpholin-4-ylethoxy)-1-benzofuran-2-carboxamide
-
-
0.0000079
N-[1-([(1S)-1-[(5-ethyl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
0.00000025 - 0.0000017
N-[1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
0.0000033
N-[1-([(1S)-1-[(5-methoxy-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
0.000029
N-[1-([(1S)-1-[(5-phenyl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
0.0013
N-[1-([(1S)-1-[(5-tert-butyl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
0.0000052
N-[1-([(1S)-1-[(5-thiophen-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
0.0000012
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
0.00035
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-5,5,5-trifluoro-D-leucinamide
-
-
0.013
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-D-leucinamide
-
-
0.0015
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-L-isoleucinamide
-
-
0.0000347
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-L-leucinamide
-
-
0.00049
N2-[(benzyloxy)carbonyl]-N-(cyanomethyl)-L-norleucinamide
-
-
0.000001
piperidine-4-carboxylic acid [3-methyl-1[1-(naphtho[1,2-d]oxazole-2-carbonyl)-3-phenyl-propylcarbamoyl]-butyl]-amide trifluoroacetate
-
21-24°C, pH 5.5
0.00055
procathepsin K
-
pH 5.5, room temperatur
-
0.00027
procathepsin L
-
pH 5.5, room temperatur
-
0.0007
procathepsin S
-
pH 5.5, room temperatur
-
0.000044
quinoline-2-carboxylic acid [(S)-1-((3R,S)-4-oxotetrahydrofuran-3ylcarbamoyl)-3-methylbutyl]amide
-
-
0.00000004
relacatib
-
pH and temperature not specified in the publication
0.000000041
relicatib
-
apparent value, pH and temperature not specified in the publication
0.00000016
SB-357114
-
in 100 mM sodium acetate buffer (pH 5.5), at 37°C
0.0000000008 - 0.0000000124
Stefin B
-
0.033
tert-butyl [(1S)-1-([5-[4-(dimethylamino)phenyl]-1,3,4-oxadiazol-2-yl]carbonyl)butyl]carbamate
-
-
0.00081
tert-butyl [(1S)-1-[(5-thiophen-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamate
-
-
0.0056
tert-butyl [(1S)-1-[[5-(1-methylethyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamate
-
-
0.017
tert-butyl [(1S)-1-[[5-(2-methoxyphenyl)-1,3,4-oxadiazol-2-yl]carbonyl]butyl]carbamate
-
-
0.000043
tert-butyl [1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]carbamate
-
-
0.00025
[(S)-1-((3R,S)-1-acetyl-4-oxopyrrolidin-3-ylcarbamoyl)-3-methylbutyl]carbamic acid benzyl ester
-
-
0.00014
[(S)-1-((3R,S)-4-oxotetrahydrofuran-3-ylcarbamoyl)-3-methylbutyl]carbamic acid benzyl ester
-
-
0.00015
[(S)-1-((4R,S)-3-oxotetrahydropyran-4-ylcarbamoyl)-3-methylbutyl]carbamic acid benzyl ester
-
-
0.000002
((S)-1-[1-[4(R,S)-((S)-2-benzyloxycarbonylamino-4-methylpentanoylamino)-3-oxoazepan-1-yl]methanoyl]-3-methylbutl)carbamic acid benzyl ester
-
the faster eluting diastereomer C34H46N4O7*0.4H2O
0.000015
((S)-1-[1-[4(R,S)-((S)-2-benzyloxycarbonylamino-4-methylpentanoylamino)-3-oxoazepan-1-yl]methanoyl]-3-methylbutl)carbamic acid benzyl ester
-
the slower eluting diastereomer C34H46N4O7*0.3H2O
0.0000026
cathepsin K propeptide
-
25°C, pH 6
-
0.000147
cathepsin K propeptide
-
25°C, pH 4
-
0.0000000041
cystatin C
-
-
-
0.0000000087
cystatin C
-
Y67L/L205A mutant cathepsin K
-
0.0000000054
H-kininogen
-
-
-
0.0000000145
H-kininogen
-
Y67L/L205A mutant cathepsin K
-
0.0000000049
L-kininogen
-
-
-
0.0000000135
L-kininogen
-
Y67L/L205A mutant cathepsin K
-
0.00000025
N-[1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
Ki: value below 0.00000025 mM
0.0000017
N-[1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]-4-(trifluoromethoxy)benzamide
-
-
0.0000000008
Stefin B
-
Y67L/L205A mutant cathepsin K
-
0.0000000124
Stefin B
-
wild-type cathepsin K
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00000028
(11R,12R)-14,14-difluoro-34-(methylsulfanyl)-N-(prop-2-yn-1-yl)-11,12,13,14,15,16-hexahydro[11,21:22,31-terphenyl]-12-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0195
(2E,4E)-5-(1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl)-3-methylpenta-2,4-dienoic acid
Homo sapiens
pH 5.5, 25°C, collagenase activity, 4.9% inhibition of activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin as substrate, no inhibition with gelatin as substrate
0.000003
(2R)-N-cyano-4-methyl-2-[4'-(piperazin-1-yl)[1,1'-biphenyl]-3-yl]pentanamide
Homo sapiens
pH and temperature not specified in the publication
0.0000048
(4-[[(2S)-2-([1-[([1,1'-biphenyl]-3-yl)amino]cyclohexane-1-carbonyl]amino)butyl]amino]phenoxy)acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.0062
1,6-dimethyl-1,2-dihydrophenanthro[1,2-b]furan-10,11-dione
Homo sapiens
pH and temperature not specified in the publication
0.000026
1-[(1H-imidazol-4-yl)methyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole
Homo sapiens
pH and temperature not specified in the publication
0.186
13-methyl-2H,10H-[1,3]benzodioxolo[5,6-c][1,3]dioxolo[4,5-i]phenanthridin-13-ium
Homo sapiens
pH 5.5, 25°C, collagenase activity, 14% inhibition of activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin as substrate, no inhibition with gelatin as substrate
0.0088 - 0.02724
2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-6-[5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl]-2,3-dihydro-4H-1-benzopyran-4-one
0.00001
2-cyano-4-(cyclohexylamino)-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.000009
2-cyano-4-(cyclohexylmethoxy)-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.000034
2-cyano-4-[(cyclohexylmethyl)(methyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.000015
2-cyano-4-[(cyclohexylmethyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.00013
2-cyano-4-[[(4,4-difluorocyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.00017
2-cyano-N-[(1-methyl-4-phenylpiperidin-4-yl)methyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.009
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methylene]bis(6-hydroxybenzoic acid)
Homo sapiens
pH 5.5, 25°C, collagenase activity, 1.7% inhibition of activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin as substrate, no inhibition with gelatin as substrate
0.0000002
4'-[(1S)-1-([(2S)-1-[(1-cyanocyclopropyl)amino]-4-fluoro-4-methyl-1-oxopentan-2-yl]amino)-2,2,2-trifluoroethyl][1,1'-biphenyl]-4-sulfonic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000002
4'-[(1S)-1-([(2S)-1-[(cyanomethyl)amino]-4-methyl-1-oxopentan-2-yl]amino)-2,2,2-trifluoroethyl][1,1'-biphenyl]-4-sulfonic acid
Homo sapiens
pH and temperature not specified in the publication
0.000001 - 0.000004
4-(cyclohexylamino)-6-(piperazin-1-yl)-1,3,5-triazine-2-carbonitrile
0.0001
4-cycloheptyl-6-[3-(piperidin-1-yl)propyl]pyrimidine-2-carbonitrile
Homo sapiens
pH and temperature not specified in the publication
0.0113 - 0.015
4-dihydrotanshinone
0.00029
4-fluoro-N-prop-2-yn-1-yl-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween20 (v/v), 37°C
0.00024
4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.0000048
4-[2-(4-methylpiperazin-1-yl)-4,5-dihydro-1,3-thiazol-4-yl]-N-(1-[[(3S,4R)-2-oxo-4-phenoxyazetidin-3-yl]carbamoyl]cyclohexyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0001
5-bromo-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.075
6,8-dihydroxy-3-(3,4,5-trihydroxyphenyl)-2,3-dihydro-1,4-benzodioxin-2-yl 3,4,5-trihydroxybenzoate
Homo sapiens
pH 5.5, 25°C, collagenase activity, 12% inhibition of activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin as substrate, no inhibition with gelatin as substrate
0.000001
7-(2,2-dimethylpropyl)-6-[(1,3-dioxo-2,8-diazaspiro[4.5]decan-2-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
IC50 below 1 nM, pH and temperature not specified in the publication
0.0143
acetyl-strophanthidin
Homo sapiens
pH 5.5, 25°C, collagenase activity, 5.4% inhibition of activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin as substrate, no inhibition with gelatin as substrate
0.088
ellipticine
Homo sapiens
pH 5.5, 25°C, 4.0% inhibition of activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin as substrate, no inhibition with gelatin as substrate
0.00879
kushennol F
Homo sapiens
pH and temperature not specified in the publication
0.000021
methyl 5-hydroxy-7,12-dioxo-7,12-dihydrodinaphtho[1,2-b:2',3'-d]furan-6-carboxylate
Homo sapiens
pH and temperature not specified in the publication
0.000021
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(1-hydroxycyclopropyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
pH and temperature not specified in the publication
0.026
N-(1-ethynylcyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween20 (v/v), 37°C
0.000047
N-(3-bromoprop-2-yn-1-yl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween20 (v/v), 37°C
0.00014
N-(4-benzyl-1-methylpiperidin-4-yl)-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.00000057
N-(cyanomethyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween20 (v/v), 37°C
0.000000005
N-(cyanomethyl)-N2-[(1S)-2,2,2-trifluoro-1-[4'-(piperazin-1-yl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
IC50 below 5 pM, pH and temperature not specified in the publication
0.00035
N-but-3-yn-2-yl-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween20 (v/v), 37°C
0.0000002
N-cyano-N2-[4-[4-(piperazin-1-yl)phenyl]thiophen-3-yl]-L-leucinamide
Homo sapiens
pH and temperature not specified in the publication
0.000044
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.0002
N-[(1S)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition is determined by a fluorometric assay with recombinant Cat K
0.0000068
N-[(2S)-1-[4-(benzyloxy)anilino]butan-2-yl]-N2-(morpholine-4-carbonyl)-L-leucinamide
Homo sapiens
pH and temperature not specified in the publication
0.000003
N-[(2S)-4-methyl-1-([2-[4-(2-methylpropoxy)anilino]ethyl]amino)-1-oxopentan-2-yl]-2,3-dihydro-1-benzofuran-2-carboxamide
Homo sapiens
IC50 below 3 nM, pH and temperature not specified in the publication
0.0000014
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-(4-propylpiperazin-1-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0000002
N-[1-[(cyanomethyl)carbamoyl]cyclohexyl]-4-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0000002
N2-[(1S)-1-[4'-(2-amino-2-oxoethyl)[1,1'-biphenyl]-4-yl]-2,2,2-trifluoroethyl]-N-(1-cyanocyclopropyl)-4-fluoro-L-leucinamide
Homo sapiens
pH and temperature not specified in the publication
0.08
NSC13345
Homo sapiens
at pH 5.5 and 25°C
0.00000056
odanacatib
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween20 (v/v), 37°C
0.000047
Phe-Phe-fluoromethylketone
Homo sapiens
pH and temperature not specified in the publication
0.08
S-[2-[2-(dihydroxymethyl)anilino]-2-oxoethyl] carbamothioate
Homo sapiens
pH and temperature not specified in the publication
0.0093
sclareol
Homo sapiens
pH 5.5, 25°C, 3.7% inhibition of activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin as substrate, no inhibition with gelatin as substrate
0.0000345
sodium (2S,3S)-3-[[(2S)-4-methyl-1-(2-methylpropoxy)pentan-2-yl]amino]oxirane-2-carboxylate
Homo sapiens
pH and temperature not specified in the publication
0.0272
sophoraflavanone G
Homo sapiens
pH and temperature not specified in the publication
0.005
suramin
Homo sapiens
pH 5.5, 25°C, 16.0% inhibition of activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin as substrate, no inhibition with gelatin as substrate
0.0000005
(1R)-1-benzyl-2-methylpropyl [(1S)-1-formylpentyl]carbamate
Homo sapiens
-
-
0.00000033
(1R)-1-benzyl-2-methylpropyl [(1S)-1-[(E)-[(morpholin-4-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.0000005
(1R)-N-(cyanomethyl)-5,5-difluoro-2-[4'-(methylsulfanyl)biphenyl-2-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000009
(1R,2R)-2-[1-benzyl-5-[4-(methylsulfanyl)phenyl]-1H-1,2,3-triazol-4-yl]-N-(cyanomethyl)-5,5-difluorocyclohexanecarboxamide
Homo sapiens
-
-
0.000002
(1R,2R)-N-(cyanomethyl)-2-(4-[4-[(difluoromethyl)sulfanyl]phenyl]pyridin-3-yl)-5,5-difluorocyclohexanecarboxamide
Homo sapiens
-
-
0.0000004
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[1-methyl-4-[4-(methylsulfanyl)phenyl]-1H-pyrazol-3-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0000001
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[2-methyl-4-[4-(methylsulfanyl)phenyl]-1,3-thiazol-5-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000001
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[2-[4-(methylsulfanyl)phenyl]pyridin-3-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000005
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[3-[4-(methylsulfanyl)phenyl]-1-oxidopyridin-4-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000008
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[3-[4-(methylsulfanyl)phenyl]-2-oxo-1,2-dihydropyridin-4-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000001
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[3-[4-(methylsulfanyl)phenyl]pyridin-4-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0000003
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[4'-(methylsulfanyl)biphenyl-2-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000004
(1R,2R)-N-(cyanomethyl)-5,5-difluoro-2-[5-[4-(methylsulfanyl)phenyl]-2-oxo-1,2-dihydropyridin-4-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0000018
(1S)-1-methyl-2-phenylethyl [(1S)-1-formylpentyl]carbamate
Homo sapiens
-
-
0.00000094
(1S)-1-methyl-2-phenylethyl [(1S)-1-[(E)-[(morpholin-4-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.0000014
(1S)-1-[(5,6-dichloro-1H-benzimidazol-1-yl)methyl]-2,2-dimethylpropyl [(1S)-1-methyl-2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamate
Homo sapiens
-
-
0.0000032
(1S)-1-[(5,6-dichloro-1H-benzimidazol-1-yl)methyl]-2,2-dimethylpropyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
Homo sapiens
-
-
0.0000021
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-([[(6-fluoropyridin-2-yl)carbonyl]amino]acetyl)pentyl]carbamate
Homo sapiens
-
-
0.000018
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-methyl-2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamate
Homo sapiens
-
-
0.000000072
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-[oxo(1H-pyrazol-5-ylamino)acetyl]pentyl]carbamate
Homo sapiens
-
-
0.00025
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-[[(morpholin-4-ylcarbonyl)amino]acetyl]pentyl]carbamate
Homo sapiens
-
value above 0.000250 mM
0.0000004
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
Homo sapiens
-
-
0.000065
(1S)-2,2-dimethyl-1-([3-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamate
Homo sapiens
-
-
0.0000064
(1S)-2,2-dimethyl-1-([4-[4-(trifluoromethyl)phenyl]-1H-imidazol-1-yl]methyl)propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
Homo sapiens
-
-
0.0000076
(1S)-2,2-dimethyl-1-([4-[4-(trifluoromethyl)phenyl]-1H-pyrazol-1-yl]methyl)propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
Homo sapiens
-
-
0.0000055
(1S)-2,2-dimethyl-1-[(3-pyridin-3-yl-1H-pyrazol-1-yl)methyl]propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
Homo sapiens
-
-
0.0000038
(1S)-2,2-dimethyl-1-[(3-pyridin-4-yl-1H-pyrazol-1-yl)methyl]propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
Homo sapiens
-
-
0.0003
(1S)-2,2-dimethyl-1-[[3-(trifluoromethyl)-1H-pyrazol-1-yl]methyl]propyl [(1S)-1-methyl-2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamate
Homo sapiens
-
-
0.000032
(1S)-2,2-dimethyl-1-[[3-(trifluoromethyl)-1H-pyrazol-1-yl]methyl]propyl [(1S)-1-[[(pyridin-2-ylsulfonyl)amino]acetyl]pentyl]carbamate
Homo sapiens
-
-
0.000028
(2R)-2-[3'-[2-(4-tert-butylpiperazin-1-yl)-1,3-thiazol-4-yl]biphenyl-3-yl]-N-(cyanomethyl)-4-methylpentanamide
Homo sapiens
-
IC50: in vitro bone resorption assay
0.00001
(2R)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl)-2-((R)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.000172
(2R)-N-(cyanomethyl)-2-[3'-(2-[[3-(dimethylamino)pyrrolidin-1-yl]methyl]-1,3-thiazol-4-yl)biphenyl-3-yl]-4-methylpentanamide
Homo sapiens
-
IC50: in vitro bone resorption assay
0.000043
(2R)-N-(cyanomethyl)-4-methyl-2-[3'-[2-(piperazin-1-ylmethyl)-1,3-thiazol-4-yl]biphenyl-3-yl]pentanamide
Homo sapiens
-
IC50: in vitro bone resorption assay
0.000003
(2R)-N-(cyanomethyl)-4-methyl-2-[4'-(1-piperazinyl)-[1,1'-biphenyl]-3-yl]pentanamide
Homo sapiens
-
IC 50: 3 nM, reversible inhibition
0.000095
(2R)-N-(cyanomethyl)-4-methyl-2-[4'-(4-methylpiperazin-1-yl)biphenyl-3-yl]pentanamide
Homo sapiens
-
IC50: in vitro bone resorption assay
0.0012
(2S)-2-(biphenyl-2-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methylpentanamide
Homo sapiens
-
-
0.00009
(2S)-2-(biphenyl-3-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methylpentanamide
Homo sapiens
-
-
0.0001
(2S)-2-(biphenyl-4-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methylpentanamide
Homo sapiens
-
-
0.0000069
(2S)-4-fluoro-4-methyl-N-(1-(2-(methylsulfonyl)phenyl)-3-oxopiperidin-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.000016
(2S)-4-fluoro-4-methyl-N-(1-(methylsulfonyl)-3-oxoazepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.000027
(2S)-4-fluoro-4-methyl-N-(1-(methylsulfonyl)-4-oxopyrrolidin-3-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.0000018 - 0.000002
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
0.0000057
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)piperidin-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.0000083
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-phenylpiperidin-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.000033
(2S)-4-fluoro-4-methyl-N-(3-oxoazepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.000085
(2S)-4-fluoro-4-methyl-N-(4-oxo-1-(pyridin-2-ylsulfonyl)pyrrolidin-3-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.0000098
(2S)-4-fluoro-4-methyl-N-(4-oxopyrrolidin-3-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.000159
(2S)-N-(1-(benzylsulfonyl)-3-oxoazepan-4-yl)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.0000042
(2S)-N-(1-acetyl-4-oxopyrrolidin-3-yl)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.0000029
(2S)-N-(1-benzoyl-4-oxopyrrolidin-3-yl)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.000069
(2S)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methyl-2-(3-phenoxyphenoxy)pentanamide
Homo sapiens
-
-
0.0006
(2S)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methyl-2-(4-phenoxyphenoxy)pentanamide
Homo sapiens
-
-
0.003
(2S)-N-[2-[(4-methoxyphenyl)amino]ethyl]-4-methyl-2-phenoxypentanamide
Homo sapiens
-
-
0.0000002
(S)-N-(1-cyanocyclopropyl)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.000011
1-(3-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.000024
1-(4-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.000004
1-(4-cyanophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.000099
1-(4-cyclohexylphenoxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.00013
1-(4-ethylphenoxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.02
1-(biphenyl-2-ylamino)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
Homo sapiens
-
value above 20 mM
0.000082
1-(biphenyl-3-ylamino)-N-[(1R)-2-[(4-methoxyphenyl)amino]-1-methylethyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0000039
1-(biphenyl-3-ylamino)-N-[(1S)-1-[[(4-methoxyphenyl)amino]methyl]butyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0000056
1-(biphenyl-3-ylamino)-N-[(1S)-1-[[(4-methoxyphenyl)amino]methyl]pentyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0000027
1-(biphenyl-3-ylamino)-N-[(1S)-1-[[(4-methoxyphenyl)amino]methyl]propyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000019
1-(biphenyl-3-ylamino)-N-[(1S)-2-[(4-methoxyphenyl)amino]-1-methylethyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000083
1-(biphenyl-3-ylamino)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.00032
1-(biphenyl-3-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0001
1-(biphenyl-4-ylamino)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.00019
1-(biphenyl-4-yloxy)-N-[2-[(4-methoxyphenyl)amino]ethyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.00000035
1-benzylcyclopentyl [(1S)-1-formylpentyl]carbamate
Homo sapiens
-
-
0.00000011
1-benzylcyclopentyl [(1S)-1-[(E)-[(2,3-dihydro-1H-indol-1-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.00002
1-cyano-3-azetidinyl cyclohexylmethyl ether
Homo sapiens
-
IC 50: 20 nM
0.000014
1-Isopropyl-2-methylpropyl (1S)-1-cyclohexylmethyl-2,3-dioxo-3-[(thien-2-ylmethyl)-amino]propylcarbamate
Homo sapiens
-
IC50: 14 nM
0.000047
1-Isopropyl-2-methylpropyl (1S)-1-isoprpyl-2,3-dioxo-3-[(thien-2-ylmethyl)-amino]propylcarbamate
Homo sapiens
-
IC50: 47 nM
0.00036
1-Isopropyl-2-methylpropyl (1S)-1-methyl-2,3-dioxo-3-[(thien-2-ylmethyl)-amino]propylcarbamate
Homo sapiens
-
IC50: 360 nM
0.0000051
1-Isopropyl-2-methylpropyl (1S)-1-[(isoxazol-3-ylamino)(oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 5.1 nM
0.000083
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(1,3,4-thiadiazol-2-ylamino)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 83 nM
0.00004
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(1,3-thiazol-2-ylamino)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 40 nM
0.00000077
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(1H-pyrazol-5-ylamino)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 0.77 nM
0.0000048
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(isoquinolin-2-ylamino)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 4.8 nM
0.000052
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(pyrazin-2-ylamino)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 52 nM
0.000032
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(pyridin-2-ylamino)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 32 nM
0.000095
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(pyridin-3-ylamino)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 95 nM
0.00025
1-Isopropyl-2-methylpropyl (1S)-1-[oxo(quinolin-2-ylamino)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 250 nM
0.000015
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(1-phenyl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
Homo sapiens
-
IC50: 15 nM
0.000062
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(1-pyridin-2-yl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
Homo sapiens
-
IC50: 62 nM
0.000025
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(1-pyridin-4-yl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
Homo sapiens
-
IC50: 25 nM
0.00000065
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(3-phenyl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
Homo sapiens
-
IC50: 0.65 nM
0.00000021
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(4-phenyl-1H-pyrazol-5-yl)amino]acetyl]pentylcarbamate
Homo sapiens
-
IC50: 0.21 nM
0.0000092
1-Isopropyl-2-methylpropyl (1S)-1-[oxo[(thien-2-ylmethyl)-amino]acetyl]pentylcarbamate
Homo sapiens
-
IC50: 9.2 nM
0.000015
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-cyclobutyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 15 nM
0.000022
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-cyclohexyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 22 nM
0.00002
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-cyclopentyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 20 nM
0.000026
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-ethyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 26 nM
0.000039
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-isobutyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 39 nM
0.000017
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-isopropyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 17 nM
0.00000041
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-methyl-1H-pyrazol-3-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 0.41 nM
0.000032
1-Isopropyl-2-methylpropyl (1S)-1-[[(1-methyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 32 nM
0.00000071
1-Isopropyl-2-methylpropyl (1S)-1-[[(3-methyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 0.71 nM
0.00000024
1-Isopropyl-2-methylpropyl (1S)-1-[[(4-bromo-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 0.24 nM
0.00000091
1-Isopropyl-2-methylpropyl (1S)-1-[[(4-cyano-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 0.91 nM
0.00000026
1-Isopropyl-2-methylpropyl (1S)-1-[[(4-fluoro-1H-indazol-3-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 0.26 nM
0.00000047
1-Isopropyl-2-methylpropyl (1S)-1-[[(4-methyl-1H-pyrazol-5-yl)amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 0.47 nM
0.000062
1-Isopropyl-2-methylpropyl (1S)-1-[[[1-(3,3-dimethyl)-1H-pyrazol-5-yl]amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 62 nM
0.000027
1-Isopropyl-2-methylpropyl (1S)-1-[[[1-(cyclopropylmethyl)-1H-pyrazol-5-yl]amino](oxo)acetyl]pentylcarbamate
Homo sapiens
-
IC50: 27 nM
0.000027
1-Isopropyl-2-methylpropyl (1S)-2,3-dioxo--1-phenyl-3-[(thien-2-ylmethyl)-amino]propylcarbamate
Homo sapiens
-
IC50: 27 nM
0.000024
1-Isopropyl-2-methylpropyl (1S)-3-methyl-1-[oxo[(thien-2-ylmethyl)-amino]acetyl]butylcarbamate
Homo sapiens
-
IC50: 24 nM
0.000087
1-Isopropyl-2-methylpropyl (1S,2S)-2-methyl-1-[oxo[(thien-2-ylmethyl)-amino]acetyl]butylcarbamate
Homo sapiens
-
IC50: 87 nM
0.012
1-Isopropyl-2-methylpropyl 2,3-dioxo-3-[(thien-2-ylmethyl)-amino]propylcarbamate
Homo sapiens
-
IC50: 0.012 mM
0.00013
1-methylethyl (2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazinecarboxylate
Homo sapiens
-
-
0.000006
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-(3-methylphenyl)urea
Homo sapiens
-
pH 5.5, 30°C
0.000025
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-phenylurea
Homo sapiens
-
pH 5.5, 30°C
0.000023
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-[3-(trifluoromethyl)phenyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.01
2-(3-methoxyphenyl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.0035
2-(3-methylphenyl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000288
2-(3-tert-butylphenyl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0000026
2-(4-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-3-oxoazepan-1-ylsulfonyl)pyridine 1-oxide
Homo sapiens
-
-
0.01
2-(biphenyl-3-yl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.00012
2-(cyclohexylamino)pyrimidine-4-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
2-(cyclohexylmethyl)-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00000001
2-cyano-4-(cyclohexylamino)-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000000009
2-cyano-4-(cyclohexylamino)-N-[2-(3-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000000022 - 0.000022
2-cyano-4-(cyclohexylamino)-N-[2-(4-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
0.00000075
2-cyano-4-(cyclohexylamino)-N-[2-(4-pyrrolidin-1-ylphenyl)ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000000047 - 0.000047
2-cyano-4-(cyclohexylamino)-N-[2-[4-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
0.000000031
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[3-[2-(1H-imidazol-1-yl)ethoxy]-4-methoxyphenyl]ethyl)pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000000003
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[3-[2-(1H-imidazol-1-yl)ethoxy]phenyl]ethyl)pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000000013
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[4-[(1-methylpiperidin-4-yl)oxy]phenyl]ethyl)pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000000011
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[4-[(4-methylpiperazin-1-yl)methyl]phenyl]ethyl)pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000000003 - 0.000003
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[4-[2-(1H-imidazol-1-yl)ethoxy]phenyl]ethyl)pyrimidine-5-carboxamide
0.000000003
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-(3-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
value below 0.000000003 mM
0.000000003 - 0.000003
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-(4-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
0.0000003
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-(4-pyrrolidin-1-ylphenyl)ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000000011
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-[3-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000000025 - 0.000025
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-[4-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
0.000038
2-cycloheptyl-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0001
2-cycloheptyl-3,5-dioxo-4-[3-(piperidin-1-yl)propyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
2-cycloheptyl-4-[2-(dimethylamino)ethyl]-3,5-dioxo-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
2-cycloheptyl-4-[3-(morpholin-4-yl)propyl]-3,5-dioxo-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000197
2-cyclohexyl-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00087
2-cyclopentyl-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.01
2-[3-(hydroxymethyl)phenyl]-3,5-dioxo-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.0000062
2-[[2-cyano-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methyl]-N-cyclohexyl-1,3-dioxo-2,8-diazaspiro[4.5]decane-8-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000042
2-[[2-cyano-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methyl]-N-methyl-1,3-dioxo-2,8-diazaspiro[4.5]decane-8-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
3,5-dioxo-2-phenyl-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000072
3,5-dioxo-2-[3-(propan-2-yl)phenyl]-4-propyl-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00446
3,5-dioxo-4-(2-phenylethyl)-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.012
3,5-dioxo-4-phenyl-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.01
3,5-dioxo-4-propyl-2-[4-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000182
3,5-dioxo-4-[2-(piperidin-1-yl)ethyl]-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000038
3,5-dioxo-4-[3-(piperidin-1-yl)propyl]-2-[3-(propan-2-yl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000017
3,5-dioxo-4-[3-(piperidin-1-yl)propyl]-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000045
3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-2-oxopropylcarbamate
Homo sapiens
-
-
0.000068
3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxo-N-(phenylsulfonyl)pyrrolidine-1-carboxamide
Homo sapiens
-
-
0.0000073
3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxo-N-phenylpyrrolidine-1-carboxamide
Homo sapiens
-
-
0.0000073
3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxamide
Homo sapiens
-
-
0.0000048
3-(4-[[(2S)-2-([[1-(biphenyl-3-ylamino)cyclohexyl]carbonyl]amino)butyl]amino]phenoxy)propanoic acid
Homo sapiens
-
-
0.00004
3-(benzyloxy)-1-cyanoazetidine
Homo sapiens
-
IC 50: 40 nM
0.001
3-(cyclohexylamino)benzonitrile
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
1
3-amino-4-[(tetrahydro-2-furanylmethyl)amino] benzoic acid
Homo sapiens
-
at pH 5.5 and 28°C
0.0001
3-[(benzyloxy)methyl]-1-cyanopyrrolidine
Homo sapiens
-
IC 50: 100 nM
0.0000045
3-[4-([(2S)-2-[(N-biphenyl-3-yl-L-leucyl)amino]butyl]amino)phenoxy]propanoic acid
Homo sapiens
-
-
0.00039
3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000096
4-(3,4-dimethylphenyl)-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000293
4-(3-cyanophenyl)-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000457
4-(3-cyclopentylphenyl)-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000181
4-(3-methylphenyl)-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000011
4-(3-tert-butylphenyl)-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000009
4-(4-acetylpiperazin-1-yl)-5-amino-6-[(2-methylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.00017
4-(cyclohexylamino)pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000132
4-(dimethylamino)-N-[1-([(1S)-1-[(5-furan-2-yl-1,3,4-oxadiazol-2-yl)carbonyl]butyl]carbamoyl)cyclohexyl]benzamide
Homo sapiens
-
IC50: in vitro bone resorption assay
0.001
4-benzyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0074
4-butyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000084
4-cycloheptyl-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0001
4-cycloheptyl-6-[3-(piperidin-1-yl)propyl]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00068
4-cyclohexyl-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000011
4-cyclooctyl-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.002
4-cyclopentyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0025
4-ethyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00478
4-methyl-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000985
4-phenyl-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.004074
4-propyl-6-[2-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000033
4-propyl-6-[3-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.001
4-propyl-6-[4-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000019
4-[(2,2-dimethylpropyl)(4-iodobenzyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000071
4-[(2,2-dimethylpropyl)amino]-5-(3-[4-[(4-methoxyphenyl)sulfonyl]piperazin-1-yl]prop-1-yn-1-yl)pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000086
4-[(2,2-dimethylpropyl)amino]-5-[3-(pyridin-3-yloxy)prop-1-yn-1-yl]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000071
4-[(2,2-dimethylpropyl)amino]-5-[3-[4-(4-methylpiperazin-1-yl)phenyl]prop-1-yn-1-yl]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000048
4-[(2,2-dimethylpropyl)[4-(1H-1,2,4-triazol-1-ylmethyl)benzyl]amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000073
4-[(2,2-dimethylpropyl)[4-(3-piperidin-1-ylprop-1-yn-1-yl)benzyl]amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000086
4-[(2,2-dimethylpropyl)[4-[3-(1H-1,2,4-triazol-1-yl)prop-1-yn-1-yl]benzyl]amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000038
4-[(2,2-dimethylpropyl)[4-[3-(4-methylpiperazin-1-yl)prop-1-yn-1-yl]benzyl]amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.00081
4-[2-(dimethylamino)ethyl]-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.001
4-[2-chloro-3-(trifluoromethyl)phenyl]-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0001
4-[3-(dimethylamino)propyl]-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000148
4-[3-(methylsulfonyl)phenyl]-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000112
4-[3-(morpholin-4-yl)propyl]-3,5-dioxo-2-[3-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1,2,4-triazine-6-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000004
4-[3-(pentan-3-ylamino)propyl]-6-[3-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000004
4-[3-(piperidin-1-yl)propyl]-6-[3-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00001
4-[3-(tert-butylamino)propyl]-6-[3-(trifluoromethyl)phenyl]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000034
4-[4-chloro-3-(trifluoromethyl)phenyl]-6-propylpyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000069
4-[benzyl(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.00028
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0000036
4-[[4-[3-(1,4'-bipiperidin-1'-yl)prop-1-yn-1-yl]benzyl](2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000064
4-[[4-[3-(4-acetylpiperazin-1-yl)prop-1-yn-1-yl]benzyl](2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000037
5-(3-[4-[(3-chloropropyl)sulfonyl]piperazin-1-yl]prop-1-yn-1-yl)-4-[(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000032
5-amino-4-(3-hydroxyazetidin-1-yl)-6-[(2-methylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000002
5-amino-4-(bicyclo[2.2.1]hept-2-ylamino)-6-morpholin-4-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000023
5-amino-4-(cyclohexylamino)-6-morpholin-4-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000013
5-amino-4-(cyclopentylamino)-6-morpholin-4-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.00011
5-amino-4-morpholin-4-yl-6-(phenylamino)pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.00034
5-amino-4-morpholin-4-yl-6-(tetrahydrofuran-3-ylamino)pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.00006
5-amino-4-morpholin-4-yl-6-piperidin-1-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000022
5-amino-4-morpholin-4-yl-6-pyrrolidin-1-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000014
5-amino-4-[(1,1-dioxidotetrahydrothiophen-3-yl)amino]-6-[(2-methylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.00056
5-amino-4-[(1-methylethyl)amino]-6-morpholin-4-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0003
5-amino-4-[(1-methylpropyl)amino]-6-morpholin-4-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000017
5-amino-4-[(2,2-dimethylpropyl)amino]-6-morpholin-4-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000024
5-amino-4-[(2-methoxyethyl)amino]-6-[(2-methylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000018
5-amino-4-[(2-methylpropyl)amino]-6-morpholin-4-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000006
5-amino-4-[(2-methylpropyl)amino]-6-piperazin-1-ylpyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000062
5-amino-4-[(2-methylpropyl)amino]-6-[(tetrazolidin-5-ylmethyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.00001
5-[3-(1,3-dihydro-2H-isoindol-2-yl)prop-1-yn-1-yl]-4-[(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000032
5-[3-(3,4-dihydroisoquinolin-2(1H)-yl)prop-1-yn-1-yl]-4-[(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000072
5-[3-(4,5-dichloro-1H-imidazol-1-yl)prop-1-yn-1-yl]-4-[(2,2-dimethylpropyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.000001
6-(4-chlorobenzyl)-7-(2,2,2-trifluoroethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.001
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.00022 - 0.0022
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.001
6-(4-chlorobenzyl)-7-(2-cyclooctylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.000017
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.0001 - 0.00011
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.000001
6-(4-chlorobenzyl)-7-(3,3,3-trifluoropropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.001
6-(4-chlorobenzyl)-7-(3-cyclohexylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.0001
6-(4-chlorobenzyl)-7-(4,4,4-trifluorobutyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0001
6-(4-chlorobenzyl)-7-(4,4-dimethylpentyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000006
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.0000023
6-(4-chlorobenzyl)-7-cyclohexyl-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.001
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.001
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.001
6-(4-chlorobenzyl)-7-[2-(piperidin-1-yl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.000014
6-(cyclohexylamino)-9-[(2S,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]-9H-purine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000006
6-(cyclohexylamino)-9-[2-(4-methylpiperazin-1-yl)ethyl]-9H-purine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.001
6-(cyclohexylamino)pyrazine-2-carbonitrile
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.001
6-(cyclohexylamino)pyridine-2-carbonitrile
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.0000012
6-benzyl-7-(2,2,2-trifluoroethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000015
6-benzyl-7-cyclohexyl-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.002
6-cyano-2-(3-trifluoromethyl-phenyl)-3,5-dioxo-1,2,4-triazine
Homo sapiens
-
pH and temperature not specified in the publication
0.0000065
6-[(1'-acetyl-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000004
6-[(4,5-dichloro-1H-imidazol-1-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000004
6-[(5,5-dimethyl-2,4-dioxo-1,3-oxazolidin-3-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0000027
6-[(8-acetyl-1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
6-[(8-benzyl-1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl)methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.000001
6-[4-[(diethylamino)methyl]benzyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.00029
6-[[4-(4-acetyl-1,4-diazepan-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.0059
6-[[4-(4-acetylpiperazin-1-yl)-2-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.00165
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.000079
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.0054
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4,4-difluorocyclohexyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.0000054
6-[[8-(2,4-dimethoxyphenyl)-1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl]methyl]-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
7-(2,2-dimethyl-propyl)-6-(1,3-dioxo-2,8-diaza-spiro[4.5]dec-2-ylmethyl)-7H-pyrrolo[2,3-d] pyrimidine-2-carbonitrile
Homo sapiens
-
below
0.000005
7-(2,2-dimethylpropyl)-6-(1H-1,2,3-triazol-1-ylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000006
7-(2,2-dimethylpropyl)-6-(1H-imidazol-1-ylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000002
7-(2,2-dimethylpropyl)-6-[(1'-methyl-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-1,3,8-triazaspiro[4.5]dec-3-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-3-propyl-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-8-propyl-1,3,8-triazaspiro[4.5]dec-3-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.000001
7-(2,2-dimethylpropyl)-6-[(2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(3-methyl-2,4-dioxo-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.0000017
7-(2,2-dimethylpropyl)-6-[(5-fluoro-1'-methyl-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0000017
7-(2,2-dimethylpropyl)-6-[(5-fluoro-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.0000019
7-(2,2-dimethylpropyl)-6-[(5-methoxy-1'-methyl-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(5-methoxy-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
0.000003
7-(2,2-dimethylpropyl)-6-[(pyridin-4-yloxy)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[4-(4-methylpiperazin-1-yl)benzyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[4-(morpholin-4-yl)benzyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.0000017
7-(2,2-dimethylpropyl)-6-[[2-oxo-1'-(propan-2-yl)spiro[indole-3,4'-piperidin]-1(2H)-yl]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[[4-(4-fluorophenyl)piperazin-1-yl]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0000022
7-(2,2-dimethylpropyl)-6-[[8-(morpholin-4-ylacetyl)-1,3-dioxo-2,8-diazaspiro[4.5]dec-2-yl]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00028
7-(2-cyclohexylethyl)-6-(4-methoxybenzyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00025
7-(2-cyclohexylethyl)-6-[(pyridin-2-yloxy)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00048
7-(2-cyclohexylethyl)-6-[(pyridin-2-ylsulfanyl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0000006 - 0.000061
balicatib
0.00004
benzyl 1-cyano-3-pyrrolidinylcarbamate
Homo sapiens
-
IC 50: 40 nM
0.0000006
benzyl [(2S)-1-{2-[(2-{(2S)-2-[(2-amino-3-phenylpropanoyl)amino]-4-methylpentanoyl}hydrazinyl)carbonyl]hydrazinyl}-4-methyl-1-oxopentan-2-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.000163
BML-244
Homo sapiens
-
pH and temperature not specified in the publication
0.000013
Boc-Phe-Leu-NHNH-CO-NHNH-Leu-Z
Homo sapiens
-
pH and temperature not specified in the publication
0.00066 - 0.00071
carbobenzyloxy-Phe-Phe-CH2F
Homo sapiens
-
pH 5.5, 22°C, recombinant enzyme, dependent on the substrate
0.000181
dibenzyl [(2-oxopropane-1,3-diyl)bis{imino[(2S)-4-methyl-1-oxopentane-1,2-diyl]}]biscarbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.0016
ethyl 3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxylate
Homo sapiens
-
-
0.000054
ethyl 4-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-3-oxoazepane-1-carboxylate
Homo sapiens
-
-
0.000009
ethyl 4-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-3-oxopiperidine-1-carboxylate
Homo sapiens
-
-
0.0000017
Ethyl 5-[((3S)-3[[(isopropyl-2-methylpropoxy)carbonyl]amide]-2-oxoheptanoyl)amino]-1H-pyrazole-4-carboxylate
Homo sapiens
-
IC50: 1.7 nM
0.00047
ethyl N-[[(2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazino]carbonyl]-b-alaninate
Homo sapiens
-
-
0.00052
ethyl N-[[(2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazino]carbonyl]glycinate
Homo sapiens
-
-
0.000053
K4b
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002 - 0.004807
L-873724
0.0000043
methyl 3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxylate
Homo sapiens
-
-
0.0335 - 0.037
methyl 5-acetoxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
Homo sapiens
-
pH 5.5, 22°C, recombinant enzyme, dependent on the substrate
0.0215 - 0.028
methyl 5-hydroxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
Homo sapiens
-
pH 5.5, 22°C, recombinant enzyme, dependent on the substrate
0.045 - 0.067
methyl 5-methoxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
Homo sapiens
-
pH 5.5, 22°C, recombinant enzyme, dependent on the substrate
0.04 - 0.042
methyl 5-propoxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
Homo sapiens
-
pH 5.5, 22°C, recombinant enzyme, dependent on the substrate
0.000027
methyl N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-methioninate
Homo sapiens
-
-
0.00018
methyl [[(2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazino]carbonyl]carbamate
Homo sapiens
-
-
0.0000023
Mu-Leu-Hph-fluoromethylketone
Homo sapiens
-
pH and temperature not specified in the publication
0.000023
MV061606
Homo sapiens
-
pH and temperature not specified in the publication
-
0.00000016
N-((S)-4-methyl-1-oxo-1-((S)-3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-ylamino)pentan-2-yl)benzofuran-2-carboxamide
Homo sapiens
-
-
0.000028
N-(1-([(cyanomethyl)amino]carbonyl)cyclohexyl)-4-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]benzamide
Homo sapiens
-
at the cellular level in human osteoclasts
0.00037
N-(1-cyano-3-pyrrolidinyl)benzamide
Homo sapiens
-
IC 50: 370 nM
0.00029
N-(1-cyano-3-pyrrolidinyl)[1,1'-biphenyl]-4-carboxamide
Homo sapiens
-
IC 50: 290 nM
0.00005
N-(1-cyano-3pyrrolidinyl)benzenesulfonamide
Homo sapiens
-
IC 50: 50 nM
0.0000002
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(1-hydroxycyclopropyl)biphenyl-4-yl]ethyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(2-hydroxypropan-2-yl)biphenyl-4-yl]ethyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4-(4-methyl-4,5-dihydro-1,3-thiazol-2-yl)phenyl]ethyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000003
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4-(quinolin-6-yl)phenyl]ethyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000003
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4-[5-(1-hydroxycyclopropyl)pyridin-2-yl]phenyl]ethyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000004
N-(1-cyanocyclopropyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4-[6-(methylsulfonyl)pyridin-3-yl]phenyl]ethyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000004
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1R)-2,2-difluoro-1-hydroxyethyl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000004
N-(1-cyanocyclopropyl)-N2-[(1S)-1-[4'-[(1S)-2,2-difluoro-1-hydroxyethyl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-4-fluoro-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000009
N-(2,3-dichlorophenyl)triazolyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
Homo sapiens
-
IC50: 9 nM
0.000006
N-(2-chlorophenyl)triazolyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
Homo sapiens
-
IC50: 6 nM
0.000001
N-(4-chlorophenyl)-2-methylalanyl-N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-L-leucinamide
Homo sapiens
-
IC50 is below 1 nM
0.000003
N-(5-isopropyl)pyridine-2-carboxyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
Homo sapiens
-
IC50: less than 3 nM
0.000349
N-(cyanomethyl)-4-methyl-2-[3'-(2-piperazin-1-yl-1,3-thiazol-4-yl)biphenyl-3-yl]pentanamide
Homo sapiens
-
IC50: in vitro bone resorption assay
0.000059
N-(cyanomethyl)-4-methyl-2-[3'-[2-(4-methylpiperazin-1-yl)-1,3-thiazol-4-yl]biphenyl-3-yl]pentanamide
Homo sapiens
-
IC50: in vitro bone resorption assay
0.000012
N-(cyanomethyl)-4-methyl-2-[4'-(2-piperazin-1-yl-1,3-thiazol-4-yl)biphenyl-3-yl]pentanamide
Homo sapiens
-
IC50: in vitro bone resorption assay
0.0000002
N-(cyanomethyl)-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
Homo sapiens
-
-
0.000006
N-4-benzyloxybenzoyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
Homo sapiens
-
IC50: 6 nM
0.000003
N-4-isopropylbenzoyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
Homo sapiens
-
IC50: less than 3 nM
0.000003
N-4-propylbenzoyl-L-leucine-(2-(4-methoxy)phenylaminoethyl)amide
Homo sapiens
-
IC50: less than 3 nM
0.000015
N-benzyl-3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxamide
Homo sapiens
-
-
0.013
N-[(1-cyano-2-pyrrolidinyl)methyl]benzamide
Homo sapiens
-
IC 50: 0.013 mM
0.012
N-[(1-cyano-2-pyrrolidinyl)methyl]benzenesulfonamide
Homo sapiens
-
IC 50: 0.012 mM
0.00007
N-[(1-cyano-3-azetidinyl)methyl]benzamide
Homo sapiens
-
IC 50: 70 nM
0.00002
N-[(1-cyano-3-azetidinyl)methyl]benzenesulfonamide
Homo sapiens
-
IC 50: 20 nM
0.000005
N-[(1-cyano-3-azetidinyl)methyl]cyclohexanecarboxamide
Homo sapiens
-
IC 50: 5 nM
0.0002
N-[(1-cyano-3pyrrolidinyl)methyl]benzenesulfonamide
Homo sapiens
-
IC 50: 200 nM
0.00019
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[(2-methyl-1H-imidazol-1-yl)acetyl]-L-leucinamide
Homo sapiens
-
IC50: 190 nM
0.000084
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[(4-phenylpiperidin-1-yl)acetyl]-L-leucinamide
Homo sapiens
-
IC50: 84 nM
0.000009
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[(4-pyridin-4-ylpiperazin-1-yl)acetyl]-L-leucinamide
Homo sapiens
-
IC50: 9 nM
0.000024
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[(5-methyl-1H-imidazol-4-yl)acetyl]-L-leucinamide
Homo sapiens
-
IC50: 24 nM
0.000001
N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-N2-[2-(4-chlorophenoxy)-2-methylpropanoyl]-L-leucinamide
Homo sapiens
-
IC50 is below 1 nM
0.000001
N-[(1S)-1-([(1R)-2-(benzyloxy)-1-cyanoethyl]carbamoyl)-3-methylbutyl]-1-methyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50 is below 1 nM
0.00043
N-[(1S)-1-([(1R)-2-(benzyloxy)-1-cyanoethyl]carbamoyl)-3-methylbutyl]-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 430 nM
0.000151
N-[(1S)-1-carbamoyl-3-(methylsulfonyl)propyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
Homo sapiens
-
-
0.000273
N-[(1S)-1-carbamoyl-3-phenylpropyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
Homo sapiens
-
-
0.0000006
N-[(1S)-1-cyano-2-phenylethyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
Homo sapiens
-
-
0.0000002
N-[(1S)-1-cyano-3-(methylsulfanyl)propyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
Homo sapiens
-
-
0.0000009
N-[(1S)-1-cyanoethyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
Homo sapiens
-
-
0.000041
N-[(1S)-1-[2-(methylsulfanyl)ethyl]-2-oxopropyl]-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucinamide
Homo sapiens
-
-
0.000109
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-3-(methylsulfonyl)-L-alaninamide
Homo sapiens
-
-
0.000174
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-alaninamide
Homo sapiens
-
-
0.000013
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-methioninamide
Homo sapiens
-
-
0.00012
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-methionine
Homo sapiens
-
-
0.00001
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-phenylalaninamide
Homo sapiens
-
-
0.000277
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N-(2,2,2-trifluoroethyl)-L-methioninamide
Homo sapiens
-
-
0.000238
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N-(methylsulfonyl)-L-methioninamide
Homo sapiens
-
-
0.000087
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N-benzyl-L-methioninamide
Homo sapiens
-
-
0.001045
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N-dimethyl-L-methioninamide
Homo sapiens
-
-
0.000067
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-N-methyl-L-methioninamide
Homo sapiens
-
-
0.000066
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-S-methyl-L-cysteinamide
Homo sapiens
-
-
0.000238
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucylglycinamide
Homo sapiens
-
-
0.0000075
N-[(1S)-3-methyl-1-([(1S)-1-methyl-2-oxo-3-[(pyridin-2-ylsulfonyl)amino]propyl]carbamoyl)butyl]-1-benzofuran-2-carboxamide
Homo sapiens
-
-
0.011
N-[2-[(4-methoxyphenyl)amino]ethyl]-1-(phenylamino)cyclohexanecarboxamide
Homo sapiens
-
-
0.003
N-[2-[(4-methoxyphenyl)amino]ethyl]-1-phenoxycyclohexanecarboxamide
Homo sapiens
-
-
0.0002
N-[2-[(4-methoxyphenyl)amino]ethyl]-1-[4-(1-methylethyl)phenoxy]cyclohexanecarboxamide
Homo sapiens
-
-
0.00006
N2-(3-cyclohexylphenyl)-N-[2-[(4-methoxyphenyl)amino]ethyl]-L-leucinamide
Homo sapiens
-
-
0.000011
N2-biphenyl-3-yl-N-[(1S)-1-[([4-[2-(1H-tetrazol-5-yl)ethoxy]phenyl]amino)methyl]propyl]-L-leucinamide
Homo sapiens
-
-
0.0000038
N2-biphenyl-3-yl-N-[(1S)-1-[[(4-methoxyphenyl)amino]methyl]propyl]-L-leucinamide
Homo sapiens
-
-
0.00001
N2-biphenyl-3-yl-N-[(1S)-2-[(4-methoxyphenyl)amino]-1-methylethyl]-L-leucinamide
Homo sapiens
-
-
0.00004
N2-biphenyl-3-yl-N-[2-[(4-methoxyphenyl)amino]ethyl]-L-leucinamide
Homo sapiens
-
-
0.0000005
N2-[(1S)-1-[4'-(1-carbamoylcyclopropyl)biphenyl-4-yl]-2,2,2-trifluoroethyl]-N-(1-cyanocyclopropyl)-4-fluoro-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
N2-[(1S)-1-[4'-[(2S)-1-amino-1-oxopropan-2-yl]biphenyl-4-yl]-2,2,2-trifluoroethyl]-N-(1-cyanocyclopropyl)-4-fluoro-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
N2-[(1S)-1-[4-[5-(1-carbamoylcyclopropyl)pyridin-2-yl]phenyl]-2,2,2-trifluoroethyl]-N-(1-cyanocyclopropyl)-4-fluoro-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000043
N2-[(benzyloxy)carbonyl]-N-((1S)-1-cyano-2-[4-(trifluoromethyl)phenyl]ethyl)-L-leucinamide
Homo sapiens
-
IC50: 43 nM
0.000009
N2-[(benzyloxy)carbonyl]-N-[(1R)-2-(benzyloxy)-1-cyanoethyl]-L-leucinamide
Homo sapiens
-
IC50: 9 nM
0.00024
N2-[(benzyloxy)carbonyl]-N-[(1R)-2-tert-butoxy-1-cyanoethyl]-L-leucinamide
Homo sapiens
-
IC50: 240 nM
0.00012
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-cyano-2-(3-methylphenyl)ethyl]-L-leucinamide
Homo sapiens
-
IC50: 120 nM
0.000063
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-cyano-2-(4-methoxyphenyl)ethyl]-L-leucinamide
Homo sapiens
-
IC50: 63 nM
0.000048
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-cyano-2-(4-methylphenyl)ethyl]-L-leucinamide
Homo sapiens
-
IC50: 48 nM
0.000398
N2-[(benzyloxy)carbonyl]-N-[(1S)-2-(4-tert-butoxyphenyl)-1-cyanoethyl]-L-leucinamide
Homo sapiens
-
IC50: 398 nM
0.00009
N2-[(benzyloxy)carbonyl]-N-[2-[(4-methoxyphenyl)amino]ethyl]-L-leucinamide
Homo sapiens
-
-
0.000046
NC-2300
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002 - 0.00105
odanacatib
0.5
piperidin-2-yl-[2-(trifluoromethyl)-6-[4-(trifluoromethyl)phenyl]pyridin-4-yl] methanol
Homo sapiens
-
at pH 5.5 and 28°C
0.0000007 - 0.000014
relacatib
0.00083
S-(1-methylethyl) (2E)-2-[(2S)-2-[(tert-butoxycarbonyl)amino]hexylidene]hydrazinecarbothioate
Homo sapiens
-
-
0.000055
tert-butyl ([1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]carbamoyl)carbamate
Homo sapiens
-
pH 5.5, 30°C
0.0000039
tert-butyl 3-((S)-4-fluoro-4-methyl-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamido)-4-oxopyrrolidine-1-carboxylate
Homo sapiens
-
-
0.0000048
tert-butyl 3-(4-[[(2S)-2-([[1-(biphenyl-3-ylamino)cyclohexyl]carbonyl]amino)butyl]amino]phenoxy)propanoate
Homo sapiens
-
-
0.0000064
tert-butyl 3-[4-([(2S)-2-[(N-biphenyl-3-yl-L-leucyl)amino]butyl]amino)phenoxy]propanoate
Homo sapiens
-
-
0.000051
tert-butyl [(1S)-1-formylpentyl]carbamate
Homo sapiens
-
-
0.00047
tert-butyl [(1S)-1-[(E)-(4,5-dihydro-1,3-thiazol-2-ylhydrazono)methyl]pentyl]carbamate
Homo sapiens
-
-
0.033
tert-butyl [(1S)-1-[(E)-(carbamimidoylhydrazono)methyl]pentyl]carbamate
Homo sapiens
-
-
0.00035
tert-butyl [(1S)-1-[(E)-(carbamoylhydrazono)methyl]pentyl]carbamate
Homo sapiens
-
-
0.000048
tert-butyl [(1S)-1-[(E)-[(2,3-dihydro-1H-indol-1-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.000093
tert-butyl [(1S)-1-[(E)-[(3,4-dihydroisoquinolin-2(1H)-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.000059
tert-butyl [(1S)-1-[(E)-[(3,4-dihydroquinolin-1(2H)-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.0002
tert-butyl [(1S)-1-[(E)-[(3-methylbutanoyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
IC50: 0.00016 mM (after addition of the semicarbazide in 15fold excess at pH 5.5) 0.011 mM (after addition of the semicarbazide in 15fold excess at pH 7.0)
0.00041
tert-butyl [(1S)-1-[(E)-[(benzylcarbamoyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.00004
tert-butyl [(1S)-1-[(E)-[(diethylcarbamoyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
IC50: 0.000047 mM (after addition of the semicarbazide in 15fold excess at pH 5.5) 0.0018 mM (after addition of the semicarbazide in 15fold excess at pH 7.0)
0.000072
tert-butyl [(1S)-1-[(E)-[(dimethylcarbamoyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.000072
tert-butyl [(1S)-1-[(E)-[(dimethylsulfamoyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
IC50: 0.00022 mM (after addition of the semicarbazide in 15fold excess at pH 5.5) 0.0019 mM (after addition of the semicarbazide in 15fold excess at pH 7.0)
0.00049
tert-butyl [(1S)-1-[(E)-[(ethylcarbamoyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
IC50: 0.0009 mM (after addition of the semicarbazide in 15fold excess at pH 5.5) above 0.013 mM (after addition of the semicarbazide in 15fold excess at pH 7.0)
0.00028
tert-butyl [(1S)-1-[(E)-[(methylcarbamoyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.000035
tert-butyl [(1S)-1-[(E)-[(morpholin-4-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
IC50: 0.00005 mM (after addition of the semicarbazide in 15fold excess at pH 5.5) 0.0021 mM (after addition of the semicarbazide in 15fold excess at pH 7.0)
0.0004
tert-butyl [(1S)-1-[(E)-[(phenylcarbamoyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.00022
tert-butyl [(1S)-1-[(E)-[(phenylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.000058
tert-butyl [(1S)-1-[(E)-[(piperidin-1-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.000036
tert-butyl [(1S)-1-[(E)-[(pyrrolidin-1-ylcarbonyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.00016
tert-butyl [(1S)-1-[(E)-[(tert-butylcarbamoyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.000024
tert-butyl [(1S)-1-[(E)-[(trifluoroacetyl)hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.011
tert-butyl [(1S)-1-[(E)-[methyl[(2-phenylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.00052
tert-butyl [(1S)-1-[(E)-[methyl[methyl(2-phenylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.00017
tert-butyl [(1S)-1-[(E)-[[(1-methylethyl)carbamothioyl]hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.00017
tert-butyl [(1S)-1-[(E)-[[(1-methylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.00026
tert-butyl [(1S)-1-[(E)-[[(2-phenylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.0011
tert-butyl [(1S)-1-[(E)-[[(morpholin-4-ylcarbonyl)oxy]imino]methyl]pentyl]carbamate
Homo sapiens
-
-
0.000045
tert-butyl [(1S)-1-[(E)-[[methyl(2-phenylethyl)carbamoyl]hydrazono]methyl]pentyl]carbamate
Homo sapiens
-
-
0.000001
[1-(2-cyano-tetrahydro-pyridazine-1-carbonyl)-2-methyl-propyl]-carbamic acid benzyl ester
Homo sapiens
-
pH 5.5, 30°C
additional information
2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-N-(2-phenylethyl)-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
0.0088
2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-6-[5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl]-2,3-dihydro-4H-1-benzopyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.02724
2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-6-[5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl]-2,3-dihydro-4H-1-benzopyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.000001
4-(cyclohexylamino)-6-(piperazin-1-yl)-1,3,5-triazine-2-carbonitrile
Homo sapiens
pH and temperature not specified in the publication
0.000004
4-(cyclohexylamino)-6-(piperazin-1-yl)-1,3,5-triazine-2-carbonitrile
Homo sapiens
pH and temperature not specified in the publication
0.0113
4-dihydrotanshinone
Homo sapiens
with elastin as substrate, at pH 5.5 and 37°C
0.015
4-dihydrotanshinone
Homo sapiens
with collagen type I as substrate, at pH 5.5 and 37°C
0.0000019
E-64
Homo sapiens
pH and temperature not specified in the publication
0.0117
E-64
Homo sapiens
at pH 5.5 and 25°C
0.0000018
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
-
0.000002
(2S)-4-fluoro-4-methyl-N-(3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl)-2-((S)-2,2,2-trifluoro-1-(4'-(methylsulfonyl)biphenyl-4-yl)ethylamino)pentanamide
Homo sapiens
-
racemate
0.000000022
2-cyano-4-(cyclohexylamino)-N-[2-(4-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000022
2-cyano-4-(cyclohexylamino)-N-[2-(4-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000000047
2-cyano-4-(cyclohexylamino)-N-[2-[4-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000047
2-cyano-4-(cyclohexylamino)-N-[2-[4-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000000003
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[4-[2-(1H-imidazol-1-yl)ethoxy]phenyl]ethyl)pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000003
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-(2-[4-[2-(1H-imidazol-1-yl)ethoxy]phenyl]ethyl)pyrimidine-5-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000000003
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-(4-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
value below 0.000000003 mM
0.000003
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-(4-methoxyphenyl)ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
IC50 less than 0.000003 mM, pH and temperature not specified in the publication
0.000000025
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-[4-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
-
0.000025
2-cyano-4-[(2,2-dimethylpropyl)amino]-N-[2-[4-(4-methylpiperazin-1-yl)phenyl]ethyl]pyrimidine-5-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00022
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0022
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000017
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000017
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0001
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000006
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000006
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-1,3,8-triazaspiro[4.5]dec-3-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
below
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-1,3,8-triazaspiro[4.5]dec-3-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
below
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-3-propyl-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
below
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-3-propyl-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-8-propyl-1,3,8-triazaspiro[4.5]dec-3-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
below
0.000001
7-(2,2-dimethylpropyl)-6-[(2,4-dioxo-8-propyl-1,3,8-triazaspiro[4.5]dec-3-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(3-methyl-2,4-dioxo-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
below
0.000001
7-(2,2-dimethylpropyl)-6-[(3-methyl-2,4-dioxo-1,3,8-triazaspiro[4.5]dec-8-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.0000017
7-(2,2-dimethylpropyl)-6-[(5-fluoro-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
-
0.0000017
7-(2,2-dimethylpropyl)-6-[(5-fluoro-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
7-(2,2-dimethylpropyl)-6-[(5-methoxy-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
below
0.000001
7-(2,2-dimethylpropyl)-6-[(5-methoxy-2-oxospiro[indole-3,4'-piperidin]-1(2H)-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM, pH and temperature not specified in the publication
0.0000006
balicatib
Homo sapiens
-
isolated Cat K
0.0000014
balicatib
Homo sapiens
-
pH and temperature not specified in the publication
0.000061
balicatib
Homo sapiens
-
Hep-G2 cell based assay
0.0000002
L-873724
Homo sapiens
-
isolated Cat K
0.0000002
L-873724
Homo sapiens
-
pH and temperature not specified in the publication
0.004807
L-873724
Homo sapiens
-
Hep-G2 cell based assay
0.0000002
odanacatib
Homo sapiens
-
isolated Cat K
0.0000002
odanacatib
Homo sapiens
-
pH and temperature not specified in the publication
0.000034
odanacatib
Homo sapiens
-
pH and temperature not specified in the publication
0.00105
odanacatib
Homo sapiens
-
Hep-G2 cell based assay
0.0000007
relacatib
Homo sapiens
-
pH and temperature not specified in the publication
0.000014
relacatib
Homo sapiens
-
Hep-G2 cell based assay
additional information
2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-N-(2-phenylethyl)-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 not detected
additional information
2-cyano-4-[[(4,4-dimethylcyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
IC50 is above 0.003 mM, inhibition is determined by a fluorometric assay with recombinant Cat K
additional information
2-cyano-N-(1-methyl-4-phenylpiperidin-4-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 not detected
additional information
2-cyano-N-(2-phenylethyl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 is above 0.003 mM, inhibition is determined by a fluorometric assay with recombinant Cat K
additional information
2-cyano-N-(4,5-dimethoxybiphenyl-2-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 is above 0.001 mM, inhibition is determined by a fluorometric assay with recombinant Cat K
additional information
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 not detected
additional information
2-cyano-N-[(1R)-2-pyridin-2-yl-1-(pyrrolidin-1-ylmethyl)ethyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 not detected
additional information
2-cyano-N-[5-[(1-methylpiperidin-4-yl)oxy]biphenyl-2-yl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 not detected
additional information
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 not detected
additional information
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)oxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 not detected
additional information
N-benzyl-2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 not detected
additional information
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylpropyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 not detected
additional information
(3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetic acid
Homo sapiens
-
KI value is above 5 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzoic acid
Homo sapiens
-
KI value is above 2 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is below 1 nM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(2-cyclooctylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(2-piperidin-1-ylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(3,3-dimethylbutyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is below 1 nM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(3-cyclohexylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-[[4-(1-acetyl-1,2,3,6-tetrahydropyridin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-[[4-(1-acetylpiperidin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-[[4-(4-acetylpiperazin-1-yl)-3-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 is above 1 M, with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
additional information
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 is above 2 M, with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
additional information
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1.5 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 is above 1 M, with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
additional information
7-(2-cyclohexylethyl)-6-(phenoxymethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
7-(2-cyclohexylethyl)-6-[(phenylamino)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
7-(2-cyclohexylethyl)-6-[[methyl(phenyl)amino]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetamide
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)propanamide
Homo sapiens
-
KI value is above 1.5 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
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Bossard, M.J.; Tomaszek, T.A.; Thompson, S.K.; Amegadzie, B.Y.; Hanning, C.R.; Jones, C.J.; Kurdyla, J.T.; McNulty, D.E.; Drake, F.H.; Gowen, M.; Levy, M.A.
Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation and substrate identification
J. Biol. Chem.
271
12517-12524
1996
Homo sapiens
brenda
Brmme, D.; Klaus, J.L.; Okamoto, K.; Rasnik, D.; Palmer, J.T.
Peptidyl vinly sulphones: a new class of potent and selective cysteine proteinase inhibitors
Biochem. J.
315
85-89
1996
Homo sapiens
brenda
Inaoka, T.; Bilbe, G.; Ishibashi, O.; Tezuka, K.; Kumegawa, M.; Kokubo, T.
Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone
Biochem. Biophys. Res. Commun.
206
89-96
1995
Homo sapiens
brenda
McGrath, M.E.; Klaus, J.L.; Barnes, M.G.; Brmme, D.
Crystal structure of human cathepsin K complexed with a potent inhibitor
Nature Struct. Biol.
4
105-109
1997
Homo sapiens
brenda
Zhao, B.; Janson, C.A.; Amegadzie, B.Y.; D'Alessio, K.; Griffin, C.; Hanning, C.R.; Jones, C.; Kurdyla, J.; McQueney, M.; Qiu, X.; Smith, W.W.; Abdel-Meguid, S.S.
Crystal structure of human osteoclast cathepsin K complexed with E-64
Nature Struct. Biol.
4
109-111
1997
Homo sapiens
brenda
Schick, C.; Pemberton, P.A.; Shi, G.P.; Kamachi, Y.; Cataltepe, S.; Bartuski, A.J.; Gornstein, E.R.; Brmme, D.; Chapman, H.A.; Silverman, G.A.
Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen I: a kinetic analysis
Biochemistry
37
5258-5266
1998
Homo sapiens
brenda
Linnevers, C.J.; McGrath, M.E.; Armstrong, R.; Mistry, F.R.; Barnes, M.G.; Klaus, J.L.; Palmer, J.T.; Katz, B.A.; Brmme, D.
Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex
Protein Sci.
6
919-921
1997
Homo sapiens
brenda
Littlewood-Evans, A.J.; Bilbe, G.; Bowler, W.B.; Farley, D.; Wlodarski, B.; Kokubo, T.; Inaoka, T.; Sloane, J.; Evans, D.B.; Gallagher, J.A.
The osteoclast-associated protease cathepsin K is expressed in human breast carcinoma
Cancer Res.
57
5386-5390
1997
Homo sapiens
brenda
Kafienah, W.; Brmme, D.; Buttle, D.J.; Croucher, L.J.; Hollander, A.P.
Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix
Biochem. J.
331
727-732
1996
Homo sapiens
-
brenda
McQueney, M.S.; Amegadzie, B.Y.; D'Alessio, K.; Hanning, C.R.; McLaughlin, M.M.; McNulty, D.; Carr, S.A.; Ijames, C.; Kurdyla, J.; Jones, C.S.
Autocatalytic activation of human cathepsin K
J. Biol. Chem.
272
13955-13960
1997
Homo sapiens
brenda
Brmme, D.; Okamoto, K.; Wang, B.B.; Biroc, S.
Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts
J. Biol. Chem.
271
2126-2132
1996
Homo sapiens
brenda
Drake, F.H.; Dodds, R.A.; James, I.E.; Connor, J.R.; Debouck, C.; Richardson, S.; Lee-Rykaczewski, E.; Coleman, L.; Rieman, D.; Barthlow, R.; Hastings, G.; Gowen, M.
Cathepsin K, but no cathepsins B, L, or S, is abundantly expressed in human osteoclasts
J. Biol. Chem.
271
12511-12516
1996
Homo sapiens
brenda
Thomson, S.K.; Halbert, S.M.; Bossard, M.J.; Tomaszek, T.A.; Levy, M.A.; Zhao, B.; Smith, W.W.; Abdel- Meguid, S.S.; Janson, C.A.; D'Alessio, K.J.; McQueney, M.S.; Amegadzie, B.Y.; Hanning, C.R.; DesJarlais, R.L.; Briand, J.; Sakkar, S.K.; Huddleston, M.J.; Ijames, C.F.; Carr, S.A; Garnes, K.T.; Shu, A.; Heys, J.R.; Bradbeer, J.; Zembryki, D.; Lee-Rykyczewski, L.; James, I.E.; Lark, M.W.; Drake, F.H.; Gowen, M.; Gleason, J.G.; Veber, D.F.
Design of potent and selective human cathepsin K inhibitors that span the active site
Proc. Natl. Acad. Sci. USA
94
1429-1454
1997
Homo sapiens
-
brenda
Brmme, D.; Okamoto, K.
Human cathepsin O2, a novel cystein protease highly expressed in osteoclastomas and ovary. Molecular cloning, sequencing and tissue distribution
Biol. Chem. Hoppe-Seyler
376
379-384
1995
Homo sapiens
brenda
Marquis, R.W.; Ru, Y.; LoCastro, S.M.; Zeng, J.; et al.
Azepanone-based Inhibitors of human and rat cathepsin K
J. Med. Chem.
44
1380-1395
2001
Homo sapiens, Rattus norvegicus
brenda
Robichaud, J.; Oballa, R.; Prasit, P.; Falgueyret, J.P.; Percival, M.D.; Wesolowski, G.; Rodan, S.B.; Kimmel, D.; Johnson, C.; Bryant, C.; Venkatraman, S.; Setti, E.; Mendonca, R.; Palmer, J.T.
A novel class of nonpeptidic biaryl inhibitors of human cathepsin K
J. Med. Chem.
46
3709-3727
2003
Oryctolagus cuniculus, Homo sapiens
brenda
Guay, J.; Falgueyret, J.P.; Ducret, A.; Percival, M.D.; Mancini, J.A.
Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides
Eur. J. Biochem.
267
6311-6318
2000
Homo sapiens
brenda
Falgueyret, J.P.; Oballa, R.M.; Okamoto, O.; Wesolowski, G.; Aubin, Y.; Rydzewski, R.M.; Prasit, P.; Riendeau, D.; Rodan, S.B.; Percival, M.D.
Novel, nonpeptidic cyanamides as potent and reversible inhibitors of human cathepsins K and L
J. Med. Chem.
44
94-104
2001
Homo sapiens
brenda
Billington, C.J.; Mason, P.; Magny, M.C.; Mort, J.S.
The slow-binding inhibition of cathepsin K by its propeptide
Biochem. Biophys. Res. Commun.
276
924-929
2000
Homo sapiens
brenda
Bossard, M.J.; Tomaszek, T.A.; Levy, M.A.; Ijames, C.F.; Huddleston, M.J.; Briand, J.; Thompson, S.; Halpert, S.; Veber, D.F.; Carr, S.A.; Meek, T.D.; Tew, D.G.
Mechanism of inhibition of cathepsin K by potent, selective 1,5-Diacylcarbohydrazides: A new class of mechanism-based inhibitors of thiol proteases
Biochemistry
38
15893-15902
1999
Homo sapiens
brenda
Wang, D.; Pechar, M.; Li, W.; Kopeckova, P.; Bromme, D.; Kopecek, J.
Inhibition of cathepsin K with lysosomotropic macromolecular inhibitors
Biochemistry
41
8849-8859
2002
Homo sapiens (P43235)
brenda
McGrath, M.E.; Sprengeler, P.A.; Hill, C.M.; Martichonok, V.; Cheung, H.; Somoza, J.R.; Palmer, J.T.; Janc, J.W.
Peptide ketobenzoxazole inhibitors bound to cathepsin K
Biochemistry
42
15018-15028
2003
Oryctolagus cuniculus, Homo sapiens
brenda
Marquis, R.W.; Ru, Y.; Zeng, J.; Trout, R.E.; LoCastro, S.M.; Gribble, A.D.; Witherington, J.; Fenwick, A.E.; Garnier, B.; Tomaszek, T.; Tew, D.; Hemling, M.E.; Quinn, C.J.; Smith, W.W.; Zhao, B.; McQueney, M.S.; Janson, C.A.; D'Alessio, K.; Veber, D.F.
Cyclic ketone inhibitors of the cysteine protease cathepsin K
J. Med. Chem.
44
725-736
2001
Homo sapiens
brenda
Altmann, E.; Renaud, J.; Green, J.; Farley, D.; Cutting, B.; Jahnke, W.
Arylaminoethyl amides as novel non-covalent cathepsin K inhibitors
J. Med. Chem.
45
2352-2354
2002
Oryctolagus cuniculus, Homo sapiens
brenda
Tavares, F.X.; Boncek, V.; Deaton, D.N.; Hassell, A.M.; Long, S.T.; Miller, A.B.; Payne, A.A.; Miller, L.R.; Shewchuk, L.M.; Wells-Knecht, K.; Willard, D.H., Jr.; Wright, L.L.; Zhou, H.Q.
Design of potent, selective, and orally bioavailable inhibitors of cysteine protease cathepsin k
J. Med. Chem.
47
588-599
2004
Homo sapiens, Rattus norvegicus
brenda
Hwang, H.S.; Chung, H.S.
Preparation of active recombinant cathepsin K expressed in bacteria as inclusion body
Protein Expr. Purif.
25
541-546
2002
Homo sapiens
brenda
Rapa, I.; Volante, M.; Cappia, S.; Rosas, R.; Scagliotti, G.V.; Papotti, M.
Cathepsin K is selectively expressed in the stroma of lung adenocarcinoma but not in bronchioloalveolar carcinoma. A useful marker of invasive growth
Am. J. Clin. Pathol.
125
847-854
2006
Homo sapiens
brenda
Buehling, F.; Roecken, C.; Brasch, F.; Hartig, R.; Yasuda, Y.; Saftig, P.; Broemme, D.; Welte, T.
Pivotal role of cathepsin K in lung fibrosis
Am. J. Pathol.
164
2203-2216
2004
Homo sapiens, Mus musculus
brenda
Lindeman, J.H.; Hanemaaijer, R.; Mulder, A.; Dijkstra, P.D.; Szuhai, K.; Bromme, D.; Verheijen, J.H.; Hogendoorn, P.C.
Cathepsin K is the principal protease in giant cell tumor of bone
Am. J. Pathol.
165
593-600
2004
Homo sapiens
brenda
Altmann, E.; Aichholz, R.; Betschart, C.; Buhl, T.; Green, J.; Lattmann, R.; Missbach, M.
Dipeptide nitrile inhibitors of cathepsin K
Bioorg. Med. Chem. Lett.
16
2549-2554
2006
Homo sapiens
brenda
Mandelin, J.; Hukkanen, M.; Li, T.F.; Korhonen, M.; Liljestroem, M.; Sillat, T.; Hanemaaijer, R.; Salo, J.; Santavirta, S.; Konttinen, Y.T.
Human osteoblasts produce cathepsin K
Bone
38
769-777
2006
Homo sapiens (P43235), Homo sapiens
brenda
Troen, B.R.
The role of cathepsin K in normal bone resorption
Drug News Perspect.
17
19-28
2004
Homo sapiens
brenda
Ljusberg, J.; Wang, Y.; Lang, P.; Norgard, M.; Dodds, R.; Hultenby, K.; Ek-Rylander, B.; Andersson, G.
Proteolytic excision of a repressive loop domain in tartrate-resistant acid phosphatase by cathepsin K in osteoclasts
J. Biol. Chem.
280
28370-28381
2005
Homo sapiens
brenda
Giraudeau, F.S.; McGinnis, R.E.; Gray, I.C.; OBrien, E.J.; Doncaster, K.E.; Spurr, N.K.; Ralston, S.H.; Reid, D.M.; Wood, J.
Characterization of common genetic variants in cathepsin K and testing for association with bone mineral density in a large cohort of perimenopausal women from Scotland
J. Bone Miner. Res.
19
31-41
2004
Homo sapiens
brenda
Xiao, Y.; Junfeng, H.; Tianhong, L.; Lu, W.; Shulin, C.; Yu, Z.; Xiaohua, L.; Weixia, J.; Sheng, Z.; Yanyun, G.; Guo, L.; Min, L.
Cathepsin K in adipocyte differentiation and its potential role of the pathogenesis of obesity
J. Clin. Endocrinol. Metab.
91
4520-4527
2006
Homo sapiens
brenda
Holzer, G.; Noske, H.; Lang, T.; Holzer, L.; Willinger, U.
Soluble cathepsin K: a novel marker for the prediction of nontraumatic fractures?
J. Lab. Clin. Med.
146
13-17
2005
Homo sapiens
brenda
Palmer, J.T.; Bryant, C.; Wang, D.X.; Davis, D.E.; Setti, E.L.; Rydzewski, R.M.; Venkatraman, S.; Tian, Z.Q.; Burrill, L.C.; Mendonca, R.V.; Springman, E.; McCarter, J.; Chung, T.; Cheung, H.; Janc, J.W.; McGrath, M.; Somoza, J.R.; Enriquez, P.; Yu, Z.W.; Strickley, R.M.; Liu, L.; Venuti, M.C.; Percival, M.D.; et al
Design and synthesis of tri-ring P3 benzamide-containing aminonitriles as potent, selective, orally effective inhibitors of cathepsin K
J. Med. Chem.
48
7520-7534
2005
Homo sapiens
brenda
Yamashita, D.S.; Xie, R.; Lin, H.; Wang, B.; Shi, S.D.; Quinn, C.J.; Hemling, M.E.; Hissong, C.; Tomaszek, T.A.; Veber, D.F.
Benzodioxocin-3-ones and N-acyl-3-amino-3-buten-2-ones: novel classes of cathepsin K cysteine protease inhibitors
J. Pept. Res.
63
265-269
2004
Homo sapiens
brenda
van den Brule, S.; Misson, P.; Buehling, F.; Lison, D.; Huaux, F.
Overexpression of cathepsin K during silica-induced lung fibrosis and control by TGF-beta
Respir. Res.
6
84
2005
Homo sapiens, Mus musculus
brenda
Lecaille, F.; Vandier, C.; Godat, E.; Herve-Grepinet, V.; Broemme, D.; Lalmanach, G.
Modulation of hypotensive effects of kinins by cathepsin K
Arch. Biochem. Biophys.
459
129-136
2007
Homo sapiens, Rattus norvegicus
brenda
Lecaille, F.; Broemme, D.; Lalmanach, G.
Biochemical properties and regulation of cathepsin K activity
Biochimie
90
208-226
2008
Homo sapiens
brenda
Jaffer, F.A.; Kim, D.E.; Quinti, L.; Tung, C.H.; Aikawa, E.; Pande, A.N.; Kohler, R.H.; Shi, G.P.; Libby, P.; Weissleder, R.
Optical visualization of cathepsin K activity in atherosclerosis with a novel, protease-activatable fluorescence sensor
Circulation
115
2292-2298
2007
Homo sapiens
brenda
Ruenger, T.M.; Quintanilla-Dieck, M.J.; Bhawan, J.
Role of cathepsin K in the turnover of the dermal extracellular matrix during scar formation
J. Invest. Dermatol.
127
293-297
2007
Homo sapiens
brenda
Quintanilla-Dieck, M.J.; Codriansky, K.; Keady, M.; Bhawan, J.; Ruenger, T.M.
Cathepsin K in Melanoma Invasion
J. Invest. Dermatol.
128
2281-2288
2008
Homo sapiens
brenda
Shinozuka, T.; Shimada, K.; Matsui, S.; Yamane, T.; Ama, M.; Fukuda, T.; Taki, M.; Naito, S.
4-Aminophenoxyacetic acids as a novel class of reversible cathepsin K inhibitors
Bioorg. Med. Chem. Lett.
16
1502-1505
2006
Homo sapiens
brenda
Palmer, J.T.; Hirschbein, B.L.; Cheung, H.; McCarter, J.; Janc, J.W.; Yu, Z.W.; Wesolowski, G.
Keto-1,3,4-oxadiazoles as cathepsin K inhibitors
Bioorg. Med. Chem. Lett.
16
2909-2914
2006
Homo sapiens
brenda
Setti, E.L.; Venkatraman, S.; Palmer, J.T.; Xie, X.; Cheung, H.; Yu, W.; Wesolowski, G.; Robichaud, J.
Design and synthesis of tetracyclic nonpeptidic biaryl nitrile inhibitors of cathepsin K
Bioorg. Med. Chem. Lett.
16
4296-4299
2006
Homo sapiens
brenda
Adkison, K.K.; Barrett, D.G.; Deaton, D.N.; Gampe, R.T.; Hassell, A.M.; Long, S.T.; McFadyen, R.B.; Miller, A.B.; Miller, L.R.; Payne, J.A.; Shewchuk, L.M.; Wells-Knecht, K.J.; Willard, D.H.; Wright, L.L.
Semicarbazone-based inhibitors of cathepsin K, are they prodrugs for aldehyde inhibitors?
Bioorg. Med. Chem. Lett.
16
978-983
2006
Homo sapiens
brenda
Barrett, D.G.; Catalano, J.G.; Deaton, D.N.; Long, S.T.; McFadyen, R.B.; Miller, A.B.; Miller, L.R.; Samano, V.; Tavares, F.X.; Wells-Knecht, K.J.; Wright, L.L.; Zhou, H.Q.
Acyclic, orally bioavailable ketone-based cathepsin K inhibitors
Bioorg. Med. Chem. Lett.
17
22-27
2007
Homo sapiens
brenda
Robichaud, J.; Bayly, C.I.; Black, W.C.; Desmarais, S.; Leger, S.; Masse, F.; McKay, D.J.; Oballa, R.M.; Paquet, J.; Percival, M.D.; Truchon, J.F.; Wesolowski, G.; Crane, S.N.
Beta-substituted cyclohexanecarboxamide cathepsin K inhibitors: modification of the 1,2-disubstituted aromatic core
Bioorg. Med. Chem. Lett.
17
3146-3151
2007
Oryctolagus cuniculus, Homo sapiens
brenda
Leger, S.; Bayly, C.I.; Black, W.C.; Desmarais, S.; Falgueyret, J.P.; Masse, F.; Percival, M.D.; Truchon, J.F.
Primary amides as selective inhibitors of cathepsin K
Bioorg. Med. Chem. Lett.
17
4328-4332
2007
Homo sapiens
brenda
Altmann, E.; Aichholz, R.; Betschart, C.; Buhl, T.; Green, J.; Irie, O.; Teno, N.; Lattmann, R.; Tintelnot-Blomley, M.; Missbach, M.
2-Cyano-pyrimidines: a new chemotype for inhibitors of the cysteine protease cathepsin K
J. Med. Chem.
50
591-594
2007
Homo sapiens
brenda
Dejica, V.M.; Mort, J.S.; Laverty, S.; Percival, M.D.; Antoniou, J.; Zukor, D.J.; Poole, A.R.
Cleavage of type II collagen by cathepsin K in human osteoarthritic cartilage
Am. J. Pathol.
173
161-169
2008
Homo sapiens
brenda
Neidhart, M.; Baraliakos, X.; Seemayer, C.; Zelder, C.; Gay, R.E.; Michel, B.A.; Boehm, H.; Gay, S.; Braun, J.
Expression of cathepsin K and MMP-1 indicate persistent osteodestruktive activity in longstanding ankylosing spondylitis
Ann. Rheum. Dis.
68
1334-1339
2008
Homo sapiens
brenda
Yang, M.; Sun, J.; Zhang, T.; Liu, J.; Zhang, J.; Shi, M.A.; Darakhshan, F.; Guerre-Millo, M.; Clement, K.; Gelb, B.D.; Dolgnov, G.; Shi, G.P.
Deficiency and inhibition of cathepsin K reduce body weight gain and increase glucose metabolism in mice
Arterioscler. Thromb. Vasc. Biol.
28
2202-2208
2008
Homo sapiens, Mus musculus
brenda
Zhao, Q.; Jia, Y.; Xiao, Y.
Cathepsin K: a therapeutic target for bone diseases
Biochem. Biophys. Res. Commun.
380
721-723
2009
Homo sapiens
brenda
Teno, N.; Irie, O.; Miyake, T.; Gohda, K.; Horiuchi, M.; Tada, S.; Nonomura, K.; Kometani, M.; Iwasaki, G.; Betschart, C.
New chemotypes for cathepsin K inhibitors
Bioorg. Med. Chem. Lett.
18
2599-2603
2008
Homo sapiens
brenda
Irie, O.; Ehara, T.; Iwasaki, A.; Yokokawa, F.; Sakaki, J.; Hirao, H.; Kanazawa, T.; Teno, N.; Horiuchi, M.; Umemura, I.; Gunji, H.; Masuya, K.; Hitomi, Y.; Iwasaki, G.; Nonomura, K.; Tanabe, K.; Fukaya, H.; Kosaka, T.; Snell, C.R.; Hallett, A.
Discovery of selective and nonpeptidic cathepsin S inhibitors
Bioorg. Med. Chem. Lett.
18
3959-3962
2008
Homo sapiens
brenda
Kim, S.H.; Jhon, D.J.; Song, J.H.; No, J.S.; Kang, N.S.
Effect of novel N-cyano-tetrahydro-pyridazine compounds, a class of cathepsin K inhibitors, on the bone resorptive activity of mature osteoclasts
Bioorg. Med. Chem. Lett.
18
3988-3991
2008
Homo sapiens
brenda
Irie, O.; Yokokawa, F.; Ehara, T.; Iwasaki, A.; Iwaki, Y.; Hitomi, Y.; Konishi, K.; Kishida, M.; Toyao, A.; Masuya, K.; Gunji, H.; Sakaki, J.; Iwasaki, G.; Hirao, H.; Kanazawa, T.; Tanabe, K.; Kosaka, T.; Hart, T.W.; Hallett, A.
4-Amino-2-cyanopyrimidines: novel scaffold for nonpeptidic cathepsin S inhibitors
Bioorg. Med. Chem. Lett.
18
4642-4646
2008
Homo sapiens (P43235)
brenda
Gauthier, J.Y.; Chauret, N.; Cromlish, W.; Desmarais, S.; Duong, l.e..T.; Falgueyret, J.P.; Kimmel, D.B.; Lamontagne, S.; Leger, S.; LeRiche, T.; Li, C.S.; Masse, F.; McKay, D.J.; Nicoll-Griffith, D.A.; Oballa, R.M.; Palmer, J.T.; Percival, M.D.; Riendeau, D.; Robichaud, J.; Rodan, G.A.; Rodan, S.B.; Seto, C.
The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K
Bioorg. Med. Chem. Lett.
18
923-928
2008
Canis lupus familiaris, Oryctolagus cuniculus, Macaca fascicularis, Homo sapiens, Macaca mulatta, Rattus norvegicus
brenda
Morley, A.D.; Kenny, P.W.; Burton, B.; Heald, R.A.; Macfaul, P.A.; Mullett, J.; Page, K.; Porres, S.S.; Ribeiro, L.R.; Smith, P.; Ward, S.; Wilkinson, T.J.
5-Aminopyrimidin-2-ylnitriles as cathepsin K inhibitors
Bioorg. Med. Chem. Lett.
19
1658-1661
2009
Homo sapiens
brenda
Boyd, M.J.; Crane, S.N.; Robichaud, J.; Scheigetz, J.; Black, W.C.; Chauret, N.; Wang, Q.; Masse, F.; Oballa, R.M.
Investigation of ketone warheads as alternatives to the nitrile for preparation of potent and selective cathepsin K inhibitors
Bioorg. Med. Chem. Lett.
19
675-679
2009
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
brenda
Ayesa, S.; Lindquist, C.; Agback, T.; Benkestock, K.; Classon, B.; Henderson, I.; Hewitt, E.; Jansson, K.; Kallin, A.; Sheppard, D.; Samuelsson, B.
Solid-phase parallel synthesis and SAR of 4-amidofuran-3-one inhibitors of cathepsin S: effect of sulfonamides P3 substituents on potency and selectivity
Bioorg. Med. Chem.
17
1307-1324
2009
Homo sapiens
brenda
Kozloff, K.M.; Quinti, L.; Patntirapong, S.; Hauschka, P.V.; Tung, C.H.; Weissleder, R.; Mahmood, U.
Non-invasive optical detection of cathepsin K-mediated fluorescence reveals osteoclast activity in vitro and in vivo
Bone
44
190-198
2009
Homo sapiens, Mus musculus
brenda
Ravikumar, M.; Pavan, S.; Bairy, S.; Pramod, A.B.; Sumakanth, M.; Kishore, M.; Sumithra, T.
Virtual screening of cathepsin K inhibitors using docking and pharmacophore models
Chem. Biol. Drug Des.
72
79-90
2008
Homo sapiens
brenda
Kleer, C.G.; Bloushtain-Qimron, N.; Chen, Y.H.; Carrasco, D.; Hu, M.; Yao, J.; Kraeft, S.K.; Collins, L.C.; Sabel, M.S.; Argani, P.; Gelman, R.; Schnitt, S.J.; Krop, I.E.; Polyak, K.
Epithelial and stromal cathepsin K and CXCL14 expression in breast tumor progression
Clin. Cancer Res.
14
5357-5367
2008
Homo sapiens
brenda
Svelander, L.; Erlandsson-Harris, H.; Astner, L.; Grabowska, U.; Klareskog, L.; Lindstrom, E.; Hewitt, E.
Inhibition of cathepsin K reduces bone erosion, cartilage degradation and inflammation evoked by collagen-induced arthritis in mice
Eur. J. Pharmacol.
613
155-162
2009
Homo sapiens, Mus musculus, Mus musculus DBA/1J
brenda
Tada, S.; Tsutsumi, K.; Ishihara, H.; Suzuki, K.; Gohda, K.; Teno, N.
Species differences between human and rat in the substrate specificity of cathepsin K
J. Biochem.
144
499-506
2008
Rattus norvegicus (O35186), Homo sapiens (P43235), Homo sapiens
brenda
Wilson, S.R.; Peters, C.; Saftig, P.; Broemme, D.
Cathepsin K activity-dependent regulation of osteoclast actin ring formation and bone resorption
J. Biol. Chem.
284
2584-2592
2009
Homo sapiens, Mus musculus, Mus musculus C57BL/6
brenda
Li, H.Y.; Ma, H.W.; Wang, H.Q.; Ma, W.H.
Molecular analysis of a novel cathepsin K gene mutation in a Chinese child with pycnodysostosis
J. Int. Med. Res.
37
264-269
2009
Homo sapiens
brenda
Teno, N.; Masuya, K.; Ehara, T.; Kosaka, T.; Miyake, T.; Irie, O.; Hitomi, Y.; Matsuura, N.; Umemura, I.; Iwasaki, G.; Fukaya, H.; Toriyama, K.; Uchiyama, N.; Nonomura, K.; Sugiyama, I.; Kometani, M.
Effect of cathepsin K inhibitors on bone resorption
J. Med. Chem.
51
5459-5462
2008
Homo sapiens, Rattus norvegicus
brenda
Irie, O.; Kosaka, T.; Ehara, T.; Yokokawa, F.; Kanazawa, T.; Hirao, H.; Iwasaki, A.; Sakaki, J.; Teno, N.; Hitomi, Y.; Iwasaki, G.; Fukaya, H.; Nonomura, K.; Tanabe, K.; Koizumi, S.; Uchiyama, N.; Bevan, S.J.; Malcangio, M.; Gentry, C.; Fox, A.J.; Yaqoob, M.; Culshaw, A.J.; Allan Hallett, A.J.
Discovery of orally bioavailable cathepsin S inhibitors for the reversal of neuropathic pain
J. Med. Chem.
51
5502-5505
2008
Homo sapiens, Rattus norvegicus
brenda
Li, Z.; Kienetz, M.; Cherney, M.M.; James, M.N.; Broemme, D.
The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex
J. Mol. Biol.
383
78-91
2008
Homo sapiens
brenda
O'Shea, P.D.; Chen, C.Y.; Gauvreau, D.; Gosselin, F.; Hughes, G.; Nadeau, C.; Volante, R.P.
A practical enantioselective synthesis of odanacatib, a potent Cathepsin K inhibitor, via triflate displacement of an alpha-trifluoromethylbenzyl triflate
J. Org. Chem.
74
1605-1610
2009
Homo sapiens
brenda
Wendling, D.; Cedoz, J.P.; Racadot, E.
Serum levels of MMP-3 and cathepsin K in patients with ankylosing spondylitis: effect of TNFalpha antagonist therapy
Joint Bone Spine
75
559-562
2008
Homo sapiens
brenda
Aydin, H.M.; Piskin, E.
Cathepsin K/TRAP: Can they be used to induce osteogenesis?
Med. Hypotheses
72
464-465
2009
Homo sapiens
brenda
Park, Y.; Kong, J.Y.; Cho, H.
A furanquinone from Paulownia tomentosa stem for a new cathepsin K inhibitor
Phytother. Res.
23
1485-1488
2009
Homo sapiens
brenda
Mikosch, P.; Kerschan-Schindl, K.; Woloszczuk, W.; Stettner, H.; Kudlacek, S.; Kresnik, E.; Gallowitsch, H.J.; Lind, P.; Pietschmann, P.
High cathepsin K levels in men with differentiated thyroid cancer on suppressive L-thyroxine therapy
Thyroid
18
27-33
2008
Homo sapiens
brenda
Li, W.A.; Barry, Z.T.; Cohen, J.D.; Wilder, C.L.; Deeds, R.J.; Keegan, P.M.; Platt, M.O.
Detection of femtomole quantities of mature cathepsin K with zymography
Anal. Biochem.
401
91-98
2010
Homo sapiens
brenda
Garg, G.; Pradeep, A.R.; Thorat, M.K.
Effect of nonsurgical periodontal therapy on crevicular fluid levels of Cathepsin K in periodontitis
Arch. Oral Biol.
54
1046-1051
2009
Homo sapiens
brenda
Desmarais, S.; Masse, F.; Percival, M.D.
Pharmacological inhibitors to identify roles of cathepsin K in cell-based studies: a comparison of available tools
Biol. Chem.
390
941-948
2009
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Rankovic, Z.; Cai, J.; Fradera, X.; Dempster, M.; Mistry, A.; Mitchell, A.; Long, C.; Hamilton, E.; King, A.; Boucharens, S.; Jamieson, C.; Gillespie, J.; Cumming, I.; Uitdehaag, J.; van Zeeland, M.
Dioxo-triazines as a novel series of cathepsin K inhibitors
Bioorg. Med. Chem. Lett.
20
1488-1490
2010
Homo sapiens
brenda
Rankovic, Z.; Cai, J.; Kerr, J.; Fradera, X.; Robinson, J.; Mistry, A.; Hamilton, E.; McGarry, G.; Andrews, F.; Caulfield, W.; Cumming, I.; Dempster, M.; Waller, J.; Scullion, P.; Martin, I.; Mitchell, A.; Long, C.; Baugh, M.; Westwood, P.; Kinghorn, E.; Bruin, J.; Hamilton, W.; Uitdehaag, J.; van Z, v.a.n..Z.e.
Design and optimization of a series of novel 2-cyano-pyrimidines as cathepsin K inhibitors
Bioorg. Med. Chem. Lett.
20
1524-1527
2010
Homo sapiens
brenda
Isabel, E.; Bateman, K.P.; Chauret, N.; Cromlish, W.; Desmarais, S.; Duong, l.e..T.; Falgueyret, J.P.; Gauthier, J.Y.; Lamontagne, S.; Lau, C.K.; Leger, S.; LeRiche, T.; Levesque, J.F.; Li, C.S.; Masse, F.; McKay, D.J.; Mellon, C.; Nicoll-Griffith, D.A.; Oballa, R.M.; Percival, M.D.; Riendeau, D.; Robichaud,
The discovery of MK-0674, an orally bioavailable cathepsin K inhibitor
Bioorg. Med. Chem. Lett.
20
887-892
2010
Homo sapiens
brenda
Li, J.; Petrassi, H.; Tumanut, C.; Masick, B.; Trussell, C.; Harris, J.
Substrate optimization for monitoring cathepsin C activity in live cells
Bioorg. Med. Chem.
17
1064-1070
2009
Homo sapiens
brenda
Barascuk, N.; Skjot-Arkil, H.; Register, T.C.; Larsen, L.; Byrjalsen, I.; Christiansen, C.; Karsdal, M.A.
Human macrophage foam cells degrade atherosclerotic plaques through cathepsin K mediated processes
BMC Cardiovasc. Disord.
10
19
2010
Homo sapiens
brenda
Fuller, K.; Lindstrom, E.; Edlund, M.; Henderson, I.; Grabowska, U.; Szewczyk, K.A.; Moss, R.; Samuelsson, B.; Chambers, T.J.
The resorptive apparatus of osteoclasts supports lysosomotropism and increases potency of basic versus non-basic inhibitors of cathepsin K
Bone
46
1400-1407
2010
Homo sapiens
brenda
Stoch, S.A.; Zajic, S.; Stone, J.; Miller, D.L.; Van Dyck, K.; Gutierrez, M.J.; De Decker, M.; Liu, L.; Liu, Q.; Scott, B.B.; Panebianco, D.; Jin, B.; Duong, L.T.; Gottesdiener, K.; Wagner, J.A.
Effect of the cathepsin K inhibitor odanacatib on bone resorption biomarkers in healthy postmenopausal women: two double-blind, randomized, placebo-controlled phase I studies
Clin. Pharmacol. Ther.
86
175-182
2009
Homo sapiens
brenda
Kometani, M.; Nonomura, K.; Tomoo, T.; Niwa, S.
Hurdles in the drug discovery of cathepsin K inhibitors
Curr. Top. Med. Chem.
10
733-744
2010
Homo sapiens
brenda
Black, W.C.
Peptidomimetic inhibitors of cathepsin K
Curr. Top. Med. Chem.
10
745-751
2010
Homo sapiens
brenda
Teno, N.; Masuya, K.
Orally bioavailable cathepsin K inhibitors with pyrrolopyrimidine scaffold
Curr. Top. Med. Chem.
10
752-766
2010
Homo sapiens
brenda
Pan, X.; Tan, N.; Zeng, G.; Huang, H.; Yan, H.
3D QSAR studies on ketoamides of human cathepsin K inhibitors based on two different alignment methods
Eur. J. Med. Chem.
45
667-681
2010
Homo sapiens
brenda
Quintanilla-Dieck, M.J.; Codriansky, K.; Keady, M.; Bhawan, J.; Ruenger, T.M.
Expression and regulation of cathepsin K in skin fibroblasts
Exp. Dermatol.
18
596-602
2009
Homo sapiens
brenda
Golovatch, P.; Mercer, B.A.; Lemaitre, V.; Wallace, A.; Foronjy, R.F.; D'Armiento, J.
Role for cathepsin K in emphysema in smoke-exposed guinea pigs
Exp. Lung Res.
35
631-645
2009
Cavia porcellus, Homo sapiens
brenda
Broemme, D.; Lecaille, F.
Cathepsin K inhibitors for osteoporosis and potential off-target effects
Expert Opin. Investig. Drugs
18
585-600
2009
Homo sapiens
brenda
Naumnik, W.; Niklinska, W.; Ossolinska, M.; Chyczewska, E.
Serum cathepsin K and cystatin C concentration in patients with advanced non-small-cell lung cancer during chemotherapy
Folia Histochem. Cytobiol.
47
207-213
2009
Homo sapiens
brenda
Podgorski, I.
Future of anticathepsin K drugs: dual therapy for skeletal disease and atherosclerosis?
Future Med. Chem.
1
21-34
2009
Homo sapiens
brenda
Lewiecki, E.M.
Odanacatib, a cathepsin K inhibitor for the treatment of osteoporosis and other skeletal disorders associated with excessive bone remodeling
IDrugs
12
799-809
2009
Homo sapiens
brenda
Yan, X.; Takahara, M.; Xie, L.; Oda, Y.; Nakahara, T.; Uchi, H.; Takeuchi, S.; Tu, Y.; Moroi, Y.; Furue, M.
Stromal expression of cathepsin K in squamous cell carcinoma
J. Eur. Acad. Dermatol. Venereol.
25
362-365
2011
Homo sapiens
brenda
Khan, B.; Ahmed, Z.; Ahmad, W.
A novel missense mutation in cathepsin K (CTSK) gene in a consanguineous Pakistani family with pycnodysostosis
J. Investig. Med.
58
720-724
2010
Homo sapiens
brenda
Munoz-Torres, M.; Reyes-Garcia, R.; Mezquita-Raya, P.; Fernandez-Garcia, D.; Alonso, G.; Luna, J.d.e..D.; Ruiz-Requena, M.E.; Escobar-Jimenez, F.
Serum cathepsin K as a marker of bone metabolism in postmenopausal women treated with alendronate
Maturitas
64
188-192
2009
Homo sapiens
brenda
Chappard, D.; Libouban, H.; Mindeholm, L.; Basle, M.F.; Legrand, E.; Audran, M.
The cathepsin K inhibitor AAE581 induces morphological changes in osteoclasts of treated patients
Microsc. Res. Tech.
73
726-732
2009
Homo sapiens
brenda
Lendeckel, U.; Kaehne, T.; Ten Have, S.; Bukowska, A.; Wolke, C.; Bogerts, B.; Keilhoff, G.; Bernstein, H.G.
Cathepsin K generates enkephalin from beta-endorphin: a new mechanism with possible relevance for schizophrenia
Neurochem. Int.
54
410-417
2009
Homo sapiens
brenda
Codriansky, K.A.; Quintanilla-Dieck, M.J.; Gan, S.; Keady, M.; Bhawan, J.; Ruenger, T.M.
Intracellular degradation of elastin by cathepsin K in skin fibroblasts--a possible role in photoaging
Photochem. Photobiol.
85
1356-1363
2009
Homo sapiens
brenda
Wilder, C.L.; Park, K.Y.; Keegan, P.M.; Platt, M.O.
Manipulating substrate and pH in zymography protocols selectively distinguishes cathepsins K, L, S, and V activity in cells and tissues
Arch. Biochem. Biophys.
516
52-57
2011
Homo sapiens
brenda
Novinec, M.; Kovacic, L.; Lenarcic, B.; Baici, A.
Conformational flexibility and allosteric regulation of cathepsin K
Biochem. J.
429
379-389
2010
Homo sapiens
brenda
Cherney, M.M.; Lecaille, F.; Kienitz, M.; Nallaseth, F.S.; Li, Z.; James, M.N.; Broemme, D.
Structure-activity analysis of cathepsin K/chondroitin 4-sulfate interactions
J. Biol. Chem.
286
8988-8998
2011
Homo sapiens (P43235)
brenda
Sharma, V.; Panwar, P.; O'Donoghue, A.J.; Cui, H.; Guido, R.V.; Craik, C.S.; Broemme, D.
Structural requirements for the collagenase and elastase activity of cathepsin K and its selective inhibition by an exosite inhibitor
Biochem. J.
465
163-173
2015
Homo sapiens (P43235), Homo sapiens
brenda
Borel, O.; Gineyts, E.; Bertholon, C.; Garnero, P.
Cathepsin K preferentially solubilizes matured bone matrix
Calcif. Tissue Int.
91
32-39
2012
Homo sapiens
brenda
Novinec, M.; Korenc, M.; Caflisch, A.; Ranganathan, R.; Lenarcic, B.; Baici, A.
A novel allosteric mechanism in the cysteine peptidase cathepsin K discovered by computational methods
Nat. Commun.
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Homo sapiens (P43235)
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Bitu, C.C.; Kauppila, J.H.; Bufalino, A.; Nurmenniemi, S.; Teppo, S.; Keinaenen, M.; Vilen, S.T.; Lehenkari, P.; Nyberg, P.; Coletta, R.D.; Salo, T.
Cathepsin K is present in invasive oral tongue squamous cell carcinoma in vivo and in vitro
PLoS ONE
8
e70925
2013
Homo sapiens
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Novinec, M.; Lenarcic, B.; Baici, A.
Probing the activity modification space of the cysteine peptidase cathepsin K with novel allosteric modifiers
PLoS ONE
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Homo sapiens
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Roy, S.; Dattagupta, J.; Biswas, S.
Expression of recombinant human cathepsin K is enhanced by codon optimization
Process Biochem.
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2012
Homo sapiens (P43235)
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Law, S.; Du, X.; Panwar, P.; Honson, N.S.; Pfeifer, T.; Roberge, M.; Broemme, D.
Identification of substrate-specific inhibitors of cathepsin K through high-throughput screening
Biochem. J.
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2019
Homo sapiens (P43235)
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Hira, V.V.; Verbovsek, U.; Breznik, B.; Srdic, M.; Novinec, M.; Kakar, H.; Wormer, J.; der Swaan, B.V.; Lenarcic, B.; Juliano, L.; Mehta, S.; Van Noorden, C.J.; Lah, T.T.
Cathepsin K cleavage of SDF-1alpha inhibits its chemotactic activity towards glioblastoma stem-like cells
Biochim. Biophys. Acta Mol. Cell Res.
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2017
Homo sapiens (P43235), Homo sapiens
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Keegan, P.M.; Anbazhakan, S.; Kang, B.; Pace, B.S.; Platt, M.O.
Biomechanical and biochemical regulation of cathepsin K expression in endothelial cells converge at AP-1 and NF-kappaB
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Homo sapiens (P43235), Homo sapiens
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Petek, N.; Stefane, B.; Novinec, M.; Svete, J.
Synthesis and biological evaluation of 7-(aminoalkyl)pyrazolo[1,5-a]pyrimidine derivatives as cathepsin K inhibitors
Bioorg. Chem.
84
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2019
Homo sapiens (P43235)
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Yuan, X.Y.; Ren, Z.; Wu, Y.; Bougault, C.; Brizuela, L.; Magne, D.; Buchet, R.; Mebarek, S.
Design, synthesis and biological evaluation of inhibitors of cathepsin K on dedifferentiated chondrocytes
Bioorg. Med. Chem.
27
1034-1042
2019
Homo sapiens (P43235), Homo sapiens, Mus musculus (P55097), Mus musculus
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Kruglyak, N.; Williams, D.E.; Chen, H.; Law, S.; Kaleta, J.; Villanueva, I.; Davies, J.E.; Andersen, R.J.; Broemme, D.
Leupeptazin, a highly modified tripeptide isolated from cultures of a Streptomyces sp. inhibits cathepsin K
Bioorg. Med. Chem. Lett.
27
1397-1400
2017
Homo sapiens
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Christensen, J.; Shastri, V.P.
Matrix-metalloproteinase-9 is cleaved and activated by cathepsin K
BMC Res. Notes
8
322
2015
Homo sapiens (P43235)
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Gu, X.; Peng, Y.; Zhao, Y.; Liang, X.; Tang, Y.; Liu, J.
A novel derivative of artemisinin inhibits cell proliferation and metastasis via down-regulation of cathepsin K in breast cancer
Eur. J. Pharmacol.
858
172382
2019
Homo sapiens (P43235)
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Qiu, Z.C.; Dong, X.L.; Dai, Y.; Xiao, G.K.; Wang, X.L.; Wong, K.C.; Wong, M.S.; Yao, X.S.
Discovery of a new class of cathepsin K inhibitors in Rhizoma Drynariae as potential candidates for the treatment of osteoporosis
Int. J. Mol. Sci.
17
E2116
2016
Homo sapiens (P43235)
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Mons, E.; Jansen, I.D.C.; Loboda, J.; van Doodewaerd, B.R.; Hermans, J.; Verdoes, M.; van Boeckel, C.A.A.; van Veelen, P.A.; Turk, B.; Turk, D.; Ovaa, H.
The Alkyne moiety as a latent electrophile in irreversible covalent small molecule inhibitors of cathepsin K
J. Am. Chem. Soc.
141
3507-3514
2019
Homo sapiens (P43235), Homo sapiens
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Lu, J.; Wang, M.; Wang, Z.; Fu, Z.; Lu, A.; Zhang, G.
Advances in the discovery of cathepsin K inhibitors on bone resorption
J. Enzyme Inhib. Med. Chem.
33
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2018
Homo sapiens (P43235)
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