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(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(3-guanidinophenylcarbamate)
-
-
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(4-guanidinophenylcarbamate)
-
-
(1S,14S,17S,20S,23S,26S,33r)-26-amino-N-(4-carbamimidoylbenzyl)-20,23-bis(3-guanidinopropyl)-17-neopentyl-4,8,16,19,22,25,32-heptaoxo-3,9,15,18,21,24,31-heptaazabicyclo[31.2.2]heptatriacontane-14-carboxamide
-
(D-Arg)6 amide
-
IC50: 0.3 mM
(D-Arg)9 amide
-
IC50: 0.01 mM
(D-Arg)9-amide
-
protects RAW264.7 cells against anthrax toxemia with an IC50 of 0.0037 mM
(E)-N-((E)-5-(2-chloro-5-nitrobenzylidene)-4-oxothiazolidin-2-ylidene)-4-methylbenzenesulfonamide
-
competitive inhibitor
(N'Z,N''Z)-4,4'-oxybis(N'-(2-hydroxybenzylidene)benzenesulfonohydrazide)
-
competitive inhibitor
1,1'-((1R,3S,4S,6R)-4,6-bis(4-guanidinophenoxy)cyclohexane-1,3-diyl)diguanidine
meso compound
1,1'-((1R,3S,4S,6R)-4-((4-guanidinonaphthalen-1-yl)oxy)-6-(4-guanidinophenoxy)cyclohexane-1,3-diyl)diguanidine
racemate, blocks the S2 pocket
1,1'-((1S,3R,4R,6S)-4-((4-guanidinonaphthalen-1-yl)oxy)-6-(4-guanidinophenoxy)cyclohexane-1,3-diyl)diguanidine
blocks the S2 pocket
1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(azeno)-4,10-benzodiazacyclopentadecine
-
12% inhibition at 0.1 mM
1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
-
10% inhibition at 0.1 mM
1-[(1R,2R,4S,5S)-2,4-bis(4-carbamimidamidophenoxy)-5-[(4-carbamimidamidophenyl)amino]cyclohexyl]guanidine
-
-
1-[4-([(1S,2S,4R,5R)-5-carbamimidamido-2,4-bis[(4-carbamimidamidonaphthalen-1-yl)oxy]cyclohexyl]amino)naphthalen-1-yl]guanidine
-
-
11-amino-undecanoyl-RARRRKKRT
-
-
2-((1S,2S,4R,5R)-2,4-bis(2,4-diguanidinophenoxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-2-(2-amino-4-guanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(5-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)-2-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
-
noncompetitive inhibitor
2-Bromopalmitate
-
inhibits nodal processing by Flag-tagged furin
3'-oxo-6a,14a-dihydro-3'H-spiro[dibenzo[c,h]xanthene-7,1'-isobenzofuran]-3,11-diyl diacetate
-
-
3,3',3'',3'''-(1,4-phenylenebis(methanetriyl))tetrakis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2,3-dihydro-1H-inden-5-yl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2-bromophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2-chlorophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((3,4,5-trimethoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((4-isopropoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-(benzo[d][1,3]dioxol-5-ylmethylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-methylenebis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3-(alpha-acetonyl-benzyl)-4-(hydroxycoumarin)
-
-
3-allyl-1-methyl-1,2,3,4-tetrahydroisoquinoline
-
competitive inhibitor
3-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(4-amidomethyl)-benzamidine
MI-52, a substrate-analogous, noncovalent inhibitor. The furin-MI-52 complex is highly stable
3-guanidinomethylphenylacetyl-Val-Arg 4-amidinobenzylamide
-
3-hydroxy-5-(4-methoxyphenyl)-2-(4-phenoxy-3-sulfophenyl)-3H-pyrazol-2-ium
-
competitive inhibitor
4,10-bis[(4-methylphenyl)sulfonyl]-1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
-
-
4,6-bis(4-guanidinylphenoxy)-1-guanidinyl-3-(4-guanidinylphenylamino)cyclohexane
-
-
4,7-dibenzyl-1,2,9,10-tetradehydro-3,4,5,6,7,8-hexahydro-4,7-benzodiazacyclododecine
-
-
4-(2-aminoethyl)benzenesulphonyl fluoride
-
-
4-aminomethyl-phenylacetyl-Arg-Tle-Arg-4-aminomethyl-benzamidine
-
4-hydroxy-3-oxo-1-phenylbutylcoumarin
-
-
6-oxo-6H-benzo[c]chromen-3-yl 2-chlorobenzoate
-
-
8,11,22,25-tetrabenzyl-5,6,13,14,19,20,27,28-octadehydro-7,8,9,10,11,12,21,22,23,24,25,26-dodecahydrodibenzo[h,t][1,4,13,16]tetraazacyclotetracosine
-
-
8-amino-octanoyl-RARRRKKRT
-
-
Ac-Ac-RQIKIWFQNRRMKWKKRVR 4-amidinobenzylamide
-
Ac-AGYLLGKINLKALAALAKKILRVR 4-amidinobenzylamide
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Leu-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Arg-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Leu-NH2
-
-
Ac-RRRRRRRVR 4-amidinobenzylamide
-
Ac-YGRKKRRQRRRVR 4-amidinobenzylamide
-
acetyl-Val-Arg-4-amidinobenzylamide
-
-
acetyl-Val-Arg-4-aminomethyl-benzamidine
-
AEBSF
-
partially inhibits ectodomain shedding by 45%
alpha1-Aantichymotrypsin
-
incorporation of furin recognition sequences within the reactive site loop of alpha1-antiprypsin leads to the production of furin inhibitors, construction of a series of alpha1-antichymotrypsin mutants by modifying the P7-P1 region of the reactive site loop
-
alpha1-antitrypsin M352R
i.e. alpha1-PDX. Engineering of alpha1-antitrypsin variants, containing Arg at the P1 site within the reactive site loop, with improved specificity for the proprotein convertase furin using site-directed random mutagenesis, screening, overview. The engineered a1-antitrypsin variant carrying the RXXR consensus motif for furin within its reactive site loop. Furin-mediated maturation of bone morphogenetic protein-4 is completely inhibited by ectopic expression of the AVNR variant
-
alpha1-antitrypsin Portland variant
-
alpha1-AT
-
a naturally occurring serpin and a potent inhibitor of furin
-
alpha1-PDX inhibitor
-
-
-
antithrombin/heparin
-
not: antithrombin alone
-
Arg-Arg-Arg-Arg-Arg-Arg
-
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
-
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
-
Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
Arg-Arg-Arg-Val-Arg-4-amidinobenzylamide
-
Arg-Arg-Arg-Val-Arg-4-aminomethyl-benzamidine
-
Arg-Arg-Val-Arg 4-amidinobenzylamide
-
beta-Ala-TPRARRRKKRT-amide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Thr-Arg-4-amidinobenzylamide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)3-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-8-(amino)-3,6-dioxa-octanoyl-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-8-(amino)-3,6-dioxa-octanoyl-Val-Arg-4-amidinobenzylamide
-
-
Chloroquine
-
weakly affects proprotein convertase activity and E3E2 processing. Additive inhibitory effect of chloroquine and decanoyl-RVKR-chloromethyl ketone on viral infection
Cu(2,2':6,2''-terpyridine)Cl2
-
IC50: 0.0077 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-hydroxo-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.0072 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.0051 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
0.005 mM
Cu(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(di-[2-picolyl]amine)Cl2
-
IC50: 0.038 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
cyclo[glutaryl-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[glutaryl-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[glutaryl-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
-
D-Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Arg-Arg-Tle-Arg 4-amidinobenzylamide
-
D-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Arg-D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Arg-D-Arg-D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Tyr-Ala-Lys-Arg-CH2Cl
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
decanoyl-RVKR-chloromethyl ketone
decanoyl-RVKR-chloromethylketone
decanoyl-RVRR-chloromethyl ketone
-
-
diisopropyl fluorophosphate
DYYHFWHRGVKRSLSPHRPRHSR
-
i.e. profurin 39-62
E-64
-
minimal inhibition of ectodomain shedding
eglin c Arg replaced with Asp at P3
-
-
-
eglin c mutant D42R
-
-
-
eglin c mutant L45R
-
-
-
eglin variant M1 RVTR
-
-
-
eglin variant M2 RVKR
-
-
-
eglin variant M3 RVTRDERY
-
-
-
eglin variant M4 RVTRDRRY
-
-
-
eglin variant M5 RVTRDLDY
-
-
-
eglin variant M6 RVTRDLRR
-
-
-
eglin variant M7 RVTRDLRE
-
-
-
eglin variant M8 RVTRDARY
-
-
-
furin-Eda peptide acyclic
-
synthesis, overview. Designed a potent furin inhibitor that contains a highly reactive beta-turn inducing and radical generating enediynyl amino acid moiety, which is inserted between P1 and P19 residues of hfurin98-112 peptide, derived from the primary cleavage site of furin's own prodomain. The inhibitor displays a predominantly beta-turn structure. The inhibitor protects furin protein from self degradation
furin-Eda peptide cyclic
-
synthesis, overview
Glu-Gly-Arg-chloromethylketone
-
poor inhibitor
hfurin25-107
-
i.e. furin prodomain protein, competitive inhibitor, blockade of furin activity and furin-induced tumor cells malignant phenotypes by the chemically synthesized human furin prodomain, overview. Secondary structure of furin prodomain protein, overview
-
histone H1
-
efficiently blocks furin-dependent pro-von Willebrand factor processing in a dose-dependent manner, interaction between histone H1 and furin mainly takes place on the cell surface. H1 may be involved in extracellular and/or intracellular furin regulation
-
human proteinase inhibitor 8
-
-
-
inter-alpha-inhibitor protein IalphaIp
-
blocks furin activity in vitro and provides significant protection against cytotoxocity for murine peritoneal macrophages exposed to up to 500 ng/ml anthrax lethal toxin
-
L-1-chloro-3-(4-tosylamido)-7-amino-2-heptanone
-
-
lethal factor inhibitor 2
-
IC50: 0.002 mM
-
Lys-Arg chloromethyl ketone
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 4-[4-(2-amino-2-oxoethyl)piperazin-1-yl]butanamide bridged)
-
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]butanediamide bridged)
-
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]pentanediamide bridged)
-
m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
a competitive, noncovalent inhibitor, binding structure, overview
methyl 4-(bis(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl)benzoate
-
noncompetitive inhibitor
monensin
-
blocks the tumor necrosis factor alpha-induced activation of furin and subsequent neutral sphingomyelinase activation, without altering the basal level of furin
N''-[(1E)-[2-[(4-chlorobenzyl)oxy]phenyl]methylidene]carbonohydrazonic diamide
-
competitive inhibitor
N,N'-[[(1R,3S,4S,6R)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine
racemate, interferes directly with the catalytic competent conformation of the catalytic triad. Inhibition mechanism, overview
N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine
interferes directly with the catalytic competent conformation of the catalytic triad. Inhibition mechanism, overview
N-(benzo[d][1,3]dioxol-5-yl)-1,2,3,4-tetrahydroacridin-9-amine
-
competitive inhibitor
N-(thiazol-2-yl)-4-(5-((2,4,6-trioxotetrahydropyrimidin-5(6H)-ylidene)methyl)furan-2-yl)benzenesulfonamide
-
competitive inhibitor
N-tosyl-L-lysine chloromethyl ketone
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-2-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenoxy]acetamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-4-carbamimidamidobutanamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-5-carbamimidamidopentanamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-N'-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]propanediamide
-
-
N-[5-guanidino-2,4-bis-(4-guanidino-phenoxy)-cyclohexyl]-guanidine
-
-
N-[5-guanidino-2,4-bis-(5-guanidino-pyridin-2-yloxy)-cyclohexyl]-guanidine
-
-
N2(carbamidoyl)Arg-Ala-Arg-Val-Arg 4-amidinobenzylamide
-
N2(carbamidoyl)Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
N2-(3-aminomethyl-phenylacetyl)-Val-Arg 4-amidinobenzylamide
-
N2-(5-(guanidino)valeroyl)-Val-Arg 4-amidinobenzylamide
-
N2-(5-aminopentanoyl)-Val-Arg 4-amidinobenzylamide
-
N2-(5-guanidinopentanoly)-Val-Arg 4-amidinobenzylamide
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-aminopropyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-carbamimidamidopropyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-aminobutyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidamidobutyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-aminopentyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-carbamimidamidopentyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(piperidin-4-ylmethyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(aminomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(carbamimidamidomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(aminomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(carbamimidamidomethyl)benzyl]-L-argininamide
-
-
N2-acetyl-D-Leu-Leu-Leu-Leu-Arg-Val-Lys 4-amidinobenzylamide
-
N2-acetyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Tle-Arg 4-amidinobenzylamide
-
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Tle-Lys 4-amidinobenzylamide
-
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Val-Arg 4-amidinobenzylamide
-
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Val-Lys 4-amidinobenzylamide
-
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-lysinamide
-
-
N2-phenylacetyl-Ala-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
N2-phenylacetyl-Arg-Ala-Arg-Val-Arg 4-amidinobenzylamide
-
N2-phenylacetyl-Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
N2-phenylacetyl-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
N2-phenylacetyl-Arg-Val-Arg 4-amidinobenzylamide
-
Nalpha(carbamidoyl)Arg-Arg-Val-Arg 4-amidinobenzylamide
-
nona-L-arginine
-
most potent inhibitor
Octapeptidyl chloromethane inhibitor
-
potent irreversible inhibitor
-
p-chloromercuribenzenesulfonic acid
-
-
PenLen (rSAAS-(221-2546))
-
neuroendocrine protein proSAAS-derived peptide
Peptidyl chloroalkyl ketones
Phe-Pro-Arg-chloromethylketone
-
poor inhibitor
phenylacetyl-Arg-Pro-Arg-4-amidinobenzylamide
-
-
phenylacetyl-Arg-Thr-Arg-4-amidinobenzylamide
-
-
phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
a competitive, noncovalent inhibitor, binding structure, overview
phenylacetyl-Arg-Val-Arg-4-aminomethyl-benzamidine
-
phenylacetyl-Cit-Arg-Val-Arg-4-aminomethyl-benzamidine
-
phenylmethanesulfonyl fluoride
phenylmethylsulfonyl fluoride
-
-
Pro-Gly-Lys-Arg-CH2Cl
-
-
pro-hepcidin
-
hydrolytic activity of membrane furin against the fluorescent substrate Boc-RVRR-7-amino-4-methyl-coumarin is reduced by approximately 50% in presence of 2 micromol pro-hepcidin and completely abolished in presence of 5 micromol pro-hepcidin
-
profurin 39-62 DYYHFWHRGVKRSLSPHRPRHSR
-
-
profurin 48-62 VTKRSLSPHRPRHSR
-
peptide derived from proprotein convertase 1/3
profurin 54-62 SPHRPRHSR
-
peptide derived from proprotein convertase 1/3
proPC1/3 39-62 NHYLFKHKSHPRRSALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 39-62/A NAYLF KAKSAPRRSRRSALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 50-62 RRSRR SALHITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 50-83 RRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 55-62 SALHITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 55-62/A SALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 74-83 QQYEKERSKR
-
peptide derived from proprotein convertase 1/3
SAAS-(235-244)
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)
-
neuroendocrine protein proSAAS-derived peptide
-
SAAS-(235-246)P1'A
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)P2'A
-
neuroendocrine protein proSAAS-derived peptide
-
SAAS-(235-246)P3A
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)P3AP5A
-
neuroendocrine protein proSAAS-derived peptide
tosyl-Lys chloromethyl ketone
Zn(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Zn(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Zn(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
[Cu(2,2':6,2''-terpyridine)Cl2] (OCl4)
-
IC50: 0.0069 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
alpha1-antitrypsin
-
incorporation of furin recognition sequences within the reactive site loop of alpha1-antiprypsin leads to the production of furin inhibitors, construction of a series of alpha1-antitrypsin mutants by modifying the P7-P1 region of the reactive site loop
-
alpha1-antitrypsin
-
in cells overexpressing alpha1-antitrypsin, mRNA level of furin is reduced
-
alpha1-antitrypsin
-
not inhibited by normal antitrypsin M
-
alpha1-antitrypsin
-
type Pittsburgh as well as wild type
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-PDX
-
-
-
alpha1-PDX
-
a furin- and PC6-selective inhibitor, blocks cleavage of furin minimal consensus motifs, and of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase
-
antipain
-
-
antipain
-
minimal inhibition of ectodomain shedding
antithrombin
-
not
-
Arg-oxime
-
-
brefeldin A
-
blocks the tumor necrosis factor alpha-induced activation of furin and subsequent neutral sphingomyelinase activation, without altering the basal level of furin
brefeldin A
-
inhibits the secretion of furin
Ca2+
-
5-10 mM inhibit; activation below
Ca2+
-
100 mM; activation below
Ca2+
-
100 mM; activation below
CDTA
-
-
chymostatin
-
-
chymostatin
-
minimal inhibition of ectodomain shedding
Cu2+
-
IC50: 0.014 mM
CuSO4
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
-
efficiently inhibits ectodomain shedding by 95%
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
20 micromol results in a decrease in processed sol-membrane type-1 matrix metalloproteinase, significant decrease in motility compared to control cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
most inhibitory, inhibits Cryptosporidium parvum infection of HCT-8 cells in a dose-dependent manner, with ca. 50% inhibition occurring at a concentration of 0.01 mM
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
furin protease inhibitor, significantly diminishes secretion of S-tag-containing cysteine-rich FGF receptor products
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
significantly blocks the processing of ADAMTS4 in HEK-293 cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
blocks cleavage of the first and second motifs in human hepatoma cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
fully blocks the substrate cleavage by the wild-type enzyme
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
blocks furin activity, 99% inhibition of parathyroid hormone-related peptide maturation
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
furin inhibitor, pro-hepcidin activity is abolished
decanoyl-RVKR-chloromethyl ketone
-
-
decanoyl-RVKR-chloromethyl ketone
-
inhibition of furin inhibits processing of pro-B-type natriuretic peptide
decanoyl-RVKR-chloromethyl ketone
-
-
decanoyl-RVKR-chloromethyl ketone
-
furin inhibitor, inhibits E3E2 cleavage. Additive inhibitory effect of chloroquine and decanoyl-RVKR-chloromethyl ketone on viral infection
decanoyl-RVKR-chloromethylketone
-
the furin inhibitor reduces DHBV infection of primary duck hepatocytes
decanoyl-RVKR-chloromethylketone
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
moderately
EDTA
-
-
EDTA
-
97% inhibition, Ca2+ can reverse the inhibitory effect
EDTA
-
completely inhibits
Eglin c
-
engineered variants
Eglin c
-
engineered variants
EGTA
-
-
hexa-D-arginine
-
-
hexa-D-arginine
-
blocks furin activity, 85% inhibition of parathyroid hormone-related peptide maturation
Hg2+
-
-
HgCl2
-
-
iodoacetamide
-
about 50% inhibition
iodoacetamide
about 50% inhibition
leupeptin
-
-
leupeptin
-
minimal inhibition of ectodomain shedding
Lys-Arg chloromethyl ketone
-
-
Lys-Arg chloromethyl ketone
-
-
NaCl
-
600 mM
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Peptidyl chloroalkyl ketones
-
-
Peptidyl chloroalkyl ketones
-
-
phenylmethanesulfonyl fluoride
-
-
phenylmethanesulfonyl fluoride
-
not
phenylmethanesulfonyl fluoride
-
moderately
phenylmethanesulfonyl fluoride
-
not
siRNA
-
-
-
siRNA
-
furin mRNA knockdown, pro-hepcidin activity is diminished
-
tosyl-Lys chloromethyl ketone
-
-
tosyl-Lys chloromethyl ketone
-
-
TPRARRRKKRT
-
-
Zn2+
-
-
Zn2+
-
IC50: 0.021 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
ZnCl2
-
-
additional information
-
largely unaffected by aprotinin, leupeptin, pepstatin A, [4-amidino-phenyl]-methansulfonylfluoride, (4-[2-aminoethyl]-benzolsulfonylfluoride), phosphoramidon, bestatin, phenylmethylsulfonylfluoride, and antipain
-
additional information
-
cell-permeable, small-molecule compound, which inhibits at 15 micromol furin-mediated cleavage of pro-membrane type-1 matrix metalloproteinase, resulting in an almost complete inhibition of matrix metalloprotease-2-related cell motility in CHO cells
-
additional information
-
aprotinin has no effect on furin-like protease activity
-
additional information
-
a potent inhibitor containing a ketomethylene arginyl pseudopeptide bond; contains Cys near the active site His
-
additional information
-
not: pepstatin
-
additional information
-
Boc-RVRR-4-methylcoumarin-7-amide does not show any signs of substrate inhibition
-
additional information
-
the prodomain exhibits inhibitory action toward furin
-
additional information
-
siRNA-mediated depletion of endogenous c-Jun NH2-terminal kinase-interacting leucine zipper protein (JLP) or phosphoinositide kinase for position 5 containing a five finger domain (PIKfyve), profoundly delays microtubule-based transport of chimeric furin (Tac-furin) from endosomes to the trans-Golgi network in a CHO cell line, which is rescued upon ectopic expression of siRNA-resistant JLP or PIKfyve constructs
-
additional information
-
cell-permeable, small-molecule compound, which inhibits furin-mediated cleavage of pro-membrane type-1 matrix metalloproteinase, resulting in a 50% decrease in the invasiveness of the HT1080 cell
-
additional information
-
expression of furin in HaCaT cells declines with respect to time in response to UV radiation irrespective of the type or the dose used
-
additional information
-
O-glycosylation of substrate proBNP in the cleavage site region at Thr71 reduces furin cleaving activity, overview
-
additional information
-
no inhibition by metalloprotease inhibitor GM6001
-
additional information
-
EC values of furin inhibitors, overview. Inhibition of cell-surface PA83 processing in cell-based assays, overview
-
additional information
-
synthetic aromatic enediyne derivatives and their effects on protease activity of proprotein convertases furin, overview
-
additional information
peptidomimetic compounds based on a phenylacetyl-Arg-Val-Arg-4-(amidomethyl)benzamidine core structure belong to the strongest noncovalent enzyme inhibitors. Upon variation of the P5 position, dramatic changes of the Ki values are observed that cannot be explained by the known recognition motive. The Ki improves by approximately 2 orders of magnitude after addition of basic substituents, e.g., by modification of the Phac-moiety at P5 by a m- or p-guanidinomethyl group. Structure-guided drug design, overview
-
additional information
-
peptidomimetic compounds based on a phenylacetyl-Arg-Val-Arg-4-(amidomethyl)benzamidine core structure belong to the strongest noncovalent enzyme inhibitors. Upon variation of the P5 position, dramatic changes of the Ki values are observed that cannot be explained by the known recognition motive. The Ki improves by approximately 2 orders of magnitude after addition of basic substituents, e.g., by modification of the Phac-moiety at P5 by a m- or p-guanidinomethyl group. Structure-guided drug design, overview
-
additional information
active site distortions of human furin by a small molecule inhibitor N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine, analysis of binding structures of noncovalent 2,5-dideoxystreptamine-derived furin inhibitors, overview
-
additional information
-
active site distortions of human furin by a small molecule inhibitor N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine, analysis of binding structures of noncovalent 2,5-dideoxystreptamine-derived furin inhibitors, overview
-
additional information
analysis of the interactions of P4-P6 of furin with substrate-like peptide inhibitors using X-ray crystallography, substrate specificity is mediated at these binding sites, docking study, detailed overview
-
additional information
inhibitor constructuion, synthesis, and structure-function analysis, overview. Evaluation of inhibition of alphavirus propagation and inhibition of diphtheria toxin action
-
additional information
development of specific inhibitors of furin, synthesis of several truncated analogues of the bicyclic sunflower trypsin inhibitor (SFTI-1), or of compounds by various head-to-tail, head-to-side chain, and side-chain-to-tail cyclizations within multibasic octapeptides, or of several cationic cyclized peptides with cell-penetrating properties, overview. Inhibitory potency of these compounds is determined in enzyme kinetic assays with furin. Inhibitor docking study, crystal structure determination, and structure-function analysis. Modeling of furin in complex with inhibitors N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide, diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate, diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate, and diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate. Inhibition of respiratory syncytial virus propagation in A549 cells
-
additional information
no inhibition of human furin by DFP, 4-(2-aminoethyl)benzensulfonylfluorid (AEBSF), and PMSF
-
additional information
-
not: pepstatin
-
additional information
-
soluble hemojuvelin is reduced in cells treated with a furin inhibitor
-
additional information
-
pepstatin A, 1,10-ortho-phenanthroline, EDTA, or TAPI-0 do not inhibit ectodomain shedding
-
additional information
-
no inhibition by metalloprotease inhibitor GM6001
-
additional information
-
design of specific small molecule inhibitors targeting furi, overview
-
additional information
-
no inhibition by metalloprotease inhibitor GM6001
-
additional information
largely unaffected by aprotinin, leupeptin, pepstatin A, [4-amidino-phenyl]-methansulfonylfluoride, (4-[2-aminoethyl]-benzolsulfonylfluoride), phosphoramidon, bestatin, phenylmethylsulfonylfluoride, and antipain
-
additional information
-
largely unaffected by aprotinin, leupeptin, pepstatin A, [4-amidino-phenyl]-methansulfonylfluoride, (4-[2-aminoethyl]-benzolsulfonylfluoride), phosphoramidon, bestatin, phenylmethylsulfonylfluoride, and antipain
-
additional information
-
compounds 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(2-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(3-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(3-guanidinopyridin-4-yloxy)cyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-2,4-bis(2-amino-1H-benzo[d]imidazol-6-yloxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(pyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide and (1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(2-guanidinophenylcarbamate) do not inhibit
-