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(2E,6E)-farnesyl diphosphate + [H Ras]-L-cysteine
S-(2E,6E)-farnesyl-[H Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [K Ras]-L-cysteine
S-(2E,6E)-farnesyl-[K Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [N Ras]-L-cysteine
S-(2E,6E)-farnesyl-[N Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [Rho]-L-cysteine
S-(2E,6E)-farnesyl-[Rho]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + (protein)-L-cysteine
S-(2E,6E)-farnesyl protein + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [H Ras]-L-cysteine
S-(2E,6E)-farnesyl-[H Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [K Ras]-L-cysteine
S-(2E,6E)-farnesyl-[K Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [N Ras]-L-cysteine
S-(2E,6E)-farnesyl-[N Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
[protein]-S-((2E,6E)-farnesyl)-L-cysteine + diphosphate
-
assay at pH 7.5, 30°C
-
-
?
(2E,6E)-farnesyl diphosphate + [Rho]-L-cysteine
S-(2E,6E)-farnesyl-[Rho]-L-cysteine + diphosphate
-
-
-
?
(2Z)-geranylgeranyl diphosphate + protein cysteine
diphosphate + S-(2Z)-geranylgeranylcysteinyl protein
-
-
-
-
?
AAA-GPP + N-dansyl-GCVLS
?
-
-
-
-
?
APO-GPP + N-dansyl-GCVLS
?
-
-
-
-
?
dansyl-GCVDS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVDS + diphosphate
-
poor substrate for wild-type
-
-
?
dansyl-GCVKS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVKS + diphosphate
-
poor substrate for wild-type
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
farnesyl diphosphate + Ras oncoprotein p21
diphosphate + Ras-S-farnesyl oncoprotein p21
-
-
-
-
?
farnesyl diphosphate + Ras protein
diphosphate + S-farnesyl Ras protein
-
-
-
-
?
farnesyl diphosphate + Ras-Cys-Val-Ile-Met
diphosphate + Ras-S-farnesyl-Cys-Val-Ile-Met
-
-
-
-
?
farnesyl diphosphate + Ras-Cys-Val-Leu-Met
diphosphate + Ras-S-farnesyl-Cys-Val-Leu-Met
-
-
-
-
?
farnesyl triphosphate + [Ras]-Cys-Val-Ile-Met
triphosphate + [Ras]-S-farnesyl-Cys-Val-Ile-Met
-
-
-
-
?
HOM-GPP + N-dansyl-GCVLS
?
-
-
-
-
?
additional information
?
-
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
-
ir
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
Ftase has an autonomous recognition sequence, referred to as the CAAX box, where C is a cysteine, A is usually an aliphatic amino acid, and X can be a variety of amino acids
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
-
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
process required for the transforming activity of oncogenic variants of Ras, making enzyme a prime target for anticancer therapeutics
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
process necessary for the subcellular localisation of substrate to the plasma membrane
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
the enzyme catalyzes posttranslational modification of proteins, the farnesyl moieties attached to the substrates are direcly involved in protein-protein interactions as well as in protein-membrane interactions
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
substrate motif: carboxy-terminal -Ca1a2X box
-
-
?
additional information
?
-
FTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 15-carbon isoprenoid geranylgeranyl from its donor farnesyldiphosphate (FPP) is specific to FTase-I. Residues Lysalpha164, Hisbeta248, Argbeta291 and Tyrbeta300 in FTase can form hydrogen bonds with farnesyl diphosphate. When FTase is inhibited by a FTI, N-Ras and K-Ras can be alternatively prenylated by GGTase-I, EC 2.5.1.59, but H-Ras cannot
-
-
?
additional information
?
-
FTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 15-carbon isoprenoid geranylgeranyl from its donor farnesyldiphosphate (FPP) is specific to FTase-I. Residues Lysalpha164, Hisbeta248, Argbeta291 and Tyrbeta300 in FTase can form hydrogen bonds with farnesyl diphosphate. When FTase is inhibited by a FTI, N-Ras and K-Ras can be alternatively prenylated by GGTase-I, EC 2.5.1.59, but H-Ras cannot
-
-
?
additional information
?
-
-
biotin-GPP is not transferred to the peptide substrate to any measurable extent
-
-
?
additional information
?
-
FTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 15-carbon isoprenoid geranylgeranyl from its donor farnesyldiphosphate (FPP) is specific to FTase-I. Residues Lysalpha164, Hisbeta248, Argbeta291 and Tyrbeta300 in FTase can form hydrogen bonds with farnesyl diphosphate. When FTase is inhibited by a FTI, N-Ras and K-Ras can be alternatively prenylated by GGTase-I, EC 2.5.1.59, but H-Ras cannot
-
-
?
additional information
?
-
FTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 15-carbon isoprenoid geranylgeranyl from its donor farnesyldiphosphate (FPP) is specific to FTase-I. Residues Lysalpha164, Hisbeta248, Argbeta291 and Tyrbeta300 in FTase can form hydrogen bonds with farnesyl diphosphate. When FTase is inhibited by a FTI, N-Ras and K-Ras can be alternatively prenylated by GGTase-I, EC 2.5.1.59, but H-Ras cannot
-
-
?
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4-[2-[4-(3-chlorophenyl)-3-oxopiperazin-1-yl]-2-(1H-imidazol-5-yl)ethyl]benzonitrile
binds into the CAAX peptide site and competes with the CAAX substrate of FTase
lonafarnib
active in Ras-dependent and -independent malignant tumors
methyl (2S)-2-([(2S)-2-[(2-[[(2R)-2-amino-3-sulfanylpropyl]amino]-3-methylpentyl)oxy]-3-phenylpropanoyl]amino)-4-(methylsulfonyl)butanoate
a selective peptidomimetic enzme inhibitor
(+)-6-(camphorquinone-10-sulfonamido)-hexanoic acid
-
-
(-)-6-(camphorquinone-10-sulfonamido)-hexanoic acid
-
-
(2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-1-[2-(methylsulfanyl)ethyl]hydrazinyl)acetic acid
-
-
(2E)-2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]butanedioic acid
-
-
(2E,4E,8E)-5,9,13-trimethyltetradeca-2,4,8,12-tetraenoic acid
-
-
(2Z,4E)-5,9-dimethyl-3-(1-methyl-1H-imidazol-2-yl)deca-2,4,8-trienoic acid
-
-
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
-
-
(2Z,6E)-3-(3-methylbut-2-enyl)-7,11-dimethyldodeca-2,6,10-triene monophosphate
-
IC50: 16 nM
(2Z,6E)-3-allyl-7,11-dimethyldodeca-2,6,10-trien-1-yl 5-nitrofurfuryl N-methyl-N-(4-chlorobutyl)phosphoramidate
-
-
(2Z,6E)-3-allyl-7,11-dimethyldodeca-2,6,10-triene monophosphate
-
-
(2Z,6E)-3-tert-butyl-7,11-dimethyldodeca-2,6,10-trien-1-yl 5-nitrofurfuryl N-methyl-N-(4-chlorobutyl)phosphoramidate
-
-
(2Z,6E)-3-tert-butyl-7,11-dimethyldodeca-2,6,10-triene monophosphate
-
IC50: 13 nM
(2Z,6E,10E)-3-(3-methyl-1-but-2-enyl)-7,11-dimethyldodeca-2,6,10-trien-1-yl 5-nitrofurfuryl N-methyl-N-(4-chlorobutyl)phosphoramidate
-
-
(4E)-5,9-dimethyl-3-(1-methyl-1H-imidazol-2-yl)deca-4,8-dienoic acid
-
-
(4E,8E)-2-(ethoxycarbonyl)-5,9,13-trimethyl-2-[3-(1-methyl-1H-imidazol-2-yl)propyl]tetradeca-4,8,12-trienoic acid
-
-
(4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-4,8,12-trienoic acid
-
-
(4E,8E)-5,9,13-trimethyl-N-(phenylsulfonyl)tetradeca-4,8,12-trienamide
-
-
(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienamide
-
-
(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoic acid
-
-
(4E,8E)-N-hydroxy-5,9,13-trimethyltetradeca-4,8,12-trienamide
-
-
(4S)-4-([[5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophen-2-yl]carbonyl]amino)-5-tert-butoxy-5-oxopentanoic acid
-
-
(6E,10E)-7,11,15-trimethyl-3-oxohexadeca-6,10,14-trienoic acid
-
-
(7E,11E)-8,12,16-trimethyl-4-oxoheptadeca-7,11,15-trienoic acid
-
-
1-(1-[3,4-bis[(hydroxyacetyl)amino]phenyl]-4,4-dicyano-1-oxobut-3-en-2-yl)-3-(dimethylamino)pyridinium
-
-
1-(1H-imidazol-5-ylmethyl)-7-pyridin-4-yl-4-[[2-(trifluoromethoxy)phenyl]carbonyl]-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine
-
-
1-(4,4-dicyano-1-oxo-1-phenylbut-3-en-2-yl)-3-(dimethylamino)pyridinium
-
-
1-(4,4-dicyano-1-oxo-1-phenylbut-3-en-2-yl)-3-methylpyridinium
-
-
1-[(3Z)-1-(4-bromophenyl)-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-1-(4-chlorophenyl)-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-1-[3,4-bis[(hydroxyacetyl)amino]phenyl]-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-1-(3,4-dimethoxyphenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-methoxypyridinium
-
-
1-[(3Z)-4-cyano-1-(4-cyanophenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-1-(4-fluorophenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methoxyphenyl)-1-oxohept-3-en-2-yl]-2,4-dimethylpyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methoxyphenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methoxyphenyl)-1-oxohept-3-en-2-yl]-3-methoxypyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methylphenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-nitrophenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-(3,4,5-trimethoxyphenyl)hept-3-en-2-yl]-2,4-dimethylpyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-(3,4,5-trimethoxyphenyl)hept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-phenylhept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-phenylhept-3-en-2-yl]-3-methylpyridinium
-
-
1-[1-(4-bromophenyl)-4,4-dicyano-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[1-(4-chlorophenyl)-4,4-dicyano-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(3,4-dimethoxyphenyl)-1-oxobut-3-en-2-yl]-3-methoxypyridinium
-
-
1-[4,4-dicyano-1-(4-cyanophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(4-fluorophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-2,4-dimethylpyridinium
-
-
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-3-methoxypyridinium
-
-
1-[4,4-dicyano-1-(4-methylphenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(4-nitrophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-oxo-1-(3,4,5-trimethoxyphenyl)but-3-en-2-yl]-2,4-dimethylpyridinium
-
-
1-[4,4-dicyano-1-oxo-1-(3,4,5-trimethoxyphenyl)but-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
10-desmethoxystreptonigrin
-
-
18-oxa-2,5,9,11-tetraazahexacyclo[17.6.2.22,5.113,17.07,11.022,26]triaconta-1(26),7,9,13(28),14,16,19,21,22,24,26-undecaene-16-carbonitrile
-
-
2-amino-3-[2-butyl-4-(naphthalen-1-ylcarbonyl)piperazin-1-yl]propane-1-thiol
-
-
2-[(2E)-3,7-dimethyl-1-(1-methyl-1H-imidazol-2-yl)octa-2,6-dien-1-yl]butanedioic acid
-
-
2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]butanedioic acid
-
-
29-oxo-18-oxa-2,6,9,11-tetraazahexacyclo[17.5.3.12,5.113,17.07,11.022,26]nonacosa-7,9,13(28),14,16,19,21,26-octaene-16-carbonitrile
-
-
3-(4-chlorophenyl)-4-cyano-5-(isopropylthio)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)-N-adamantylthiophene-2-carboxamide
-
-
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-N'-[2-(methylsulfanyl)ethyl]-5-(propan-2-ylsulfanyl)thiophene-2-carbohydrazide
-
-
3-(4-chlorophenyl)-4-cyano-N-(naphthalen-1-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide
-
-
3-(4-chlorophenyl)-4-cyano-N-[2-(methylsulfanyl)ethyl]-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide
-
-
3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-ethynyl-5-[(1H-imidazol-4-ylacetyl)amino]thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl][[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynylthiophene-2-carboxylic acid
-
-
3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
3-allylfarnesol
-
potent inhibitor
3-allylfarnesyl diphosphate
-
IC50: 189 nM
3-methyl-2-[2-oxo-2-(10H-phenothiazin-10-yl)ethyl]indeno[1,2-c]pyrazol-4(2H)-one
-
most potent in vitro cytostatic activity inhibiting the growth of HCT-116, LOX IMVI and SK-MEL-5 cell lines
3-oxo-3-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanoic acid
-
-
3-tert-butylfarnesyl diphosphate
-
IC50: 31 nM
3-[3-[2-([2-[1-(tert-butoxycarbonyl)piperidin-4-yl]-1-([(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]methyl)ethyl]sulfamoyl)benzyl]phenyl]propanoic acid
-
-
4,4-(biphenyldiglyoxaldehyde)
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(3-cyclohexylpropanoyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(4-oxopentanoyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(5-oxohexanoyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(6-oxoheptanoyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(cycloheptylcarbonyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(cyclopentylcarbonyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(ethoxyacetyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-hexanoyl-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-pentanoyl-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-pentanoyl-N-pyrazin-2-ylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-pentanoyl-N-pyridin-3-ylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-[(3,3-dihydroxycyclobutyl)carbonyl]-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-[4-(dimethylamino)-4-oxobutanoyl]-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-(1-oxidopyridin-3-yl)-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-(1H-imidazol-4-ylmethyl)-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-(2,5-dihydro-1H-imidazol-5-ylmethyl)-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-isoxazol-5-yl-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-[2-(1H-imidazol-4-yl)ethyl]-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-(1-methylethyl)-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-(2-methylpropyl)-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-(cyclohexylmethyl)-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-butyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cycloheptyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[(3,5-dimethylisoxazol-4-yl)methyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[2-(1-methyl-1H-imidazol-5-yl)ethyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[2-(1H-imidazol-4-yl)ethyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[2-(6-methylpyridin-3-yl)ethyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[3-(1H-imidazol-4-yl)propyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[3-(2-oxopyrrolidin-1-yl)propyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclopentyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclopropyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-propyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-tert-butyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-cyano-3-(3,4-dihydroxyphenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(3-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(4-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(4-methoxyphenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(dibenzo[b,d]furan-1-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(naphthalen-2-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-[3-(methoxycarbonyl)phenyl]-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophene-2-carboxylic acid
-
-
4-ethynyl-5-([[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino)-3-phenylthiophene-2-carboxylic acid
-
-
4-oxo-4-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]butanoic acid
-
-
4-[(5-[[4-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-yl)piperidin-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(5-oxido-7-propyl-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(7-butyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(7-methyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(7-methyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)piperidin-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[2-[4-(3-chlorophenyl)-3-oxopiperazin-1-yl]-2-(1H-imidazol-5-yl)ethyl]benzonitrile
binds into the CAAX peptide site and competes with the CAAX substrate of FTase
4-[5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1,2-oxazol-3-yl]-N,N-dimethylaniline
in a model structure, the dimethylamine is in front of the zinc atom. The conformation is stabilized by two well-conserved hydrogen bond groups, one from the triazine to Arg 702
4-[[4-([[4-(4-chlorophenyl)-3-ethynylthiophen-2-yl]amino]methyl)-1H-imidazol-1-yl]methyl]benzonitrile
-
-
4-[[5-([4-[7-(3-morpholin-4-ylpropyl)-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl]azepan-1-yl]methyl)-1H-imidazol-1-yl]methyl]benzonitrile
-
-
5,9,13-trimethyl-8,12-tetradecadiene-2,3-dione
-
0.093 mM causes a 94% reduction in enzyme activity after 30 min
5,9-dimethyl-8-decene-2,3-dione
-
0.017 mM causes a 62% reduction in enzyme activity after 30 min
5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1-(4-methoxyphenyl)pyrrolidin-2-thione
in S-configuration, the compound binds rather low in the site of the enzyme, at the end of the farnesyldiphosphate far from the zinc. In R-configuration, there is a hydrogen bond between one the methoxy groups and Arg 702
5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1-[3-(trifluoromethyl)phenyl]pyrrolidine-2-thione
-
5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophene-2-carboxylic acid
-
-
5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophene-2-carboxylic acid
-
-
5-oxo-5-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]pentanoic acid
-
-
5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
-
-
5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-4-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
-
-
5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
-
-
5-[4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-2-[(pyridin-3-ylmethyl)carbamoyl]piperazin-1-yl]-5-oxopentyl acetate
-
-
6-[(4-hydroxyphenyl)(1H-imidazol-1-yl)methyl]-4-phenyl-1,2-dihydroquinolin-2-ol
-
-
acetylshikonin
-
inhibits FTPase activity in a dose-dependent manner
alphabeta-dehydrocurvularin
-
-
dehydrascorbic acid 6-palmitate
-
-
deoxyshikonin
-
inhibits FTPase activity in a dose-dependent manner
di-tert-butyl 2-[(2E,6E,10E)-1,3,7-trimethyl-1-(1-methyl-1H-imidazol-2-yl)dodeca-2,6,10-trien-1-yl]butanedioate
-
-
ethyl (2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-1-[2-(methylsulfanyl)ethyl]hydrazinyl)acetate
-
-
ethyl 3-(2,5-dimethoxyphenyl)-1,2-oxazole-5-carboxylate
-
ethyl 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate
-
-
ethyl 3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophene-2-carboxylate
-
-
ethyl 3-(4-chlorophenyl)-4-ethynyl-5-[(1H-imidazol-4-ylacetyl)amino]thiophene-2-carboxylate
-
-
ethyl 3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]amino)-4-ethynylthiophene-2-carboxylate
-
-
ethyl 3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl][[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynylthiophene-2-carboxylate
-
-
ethyl 3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate
-
-
ethyl 4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate
-
-
ethyl 4-ethynyl-5-([[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino)-3-phenylthiophene-2-carboxylate
-
-
ethyl 5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophene-2-carboxylate
-
-
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
-
-
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-4-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
-
-
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
-
-
ethyl N-(tert-butoxycarbonyl)-N-[2-(methylsulfanyl)ethyl]glycinate
-
-
ethyl N-(tert-butoxycarbonyl)glycinate
-
-
ethyl [[2-([[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]amino)ethyl]sulfanyl]acetate
-
-
KTSCVAM
-
40% inhibition of farnesylation in Toxoplasma gondii, 100% inhibition of enzyme in HeLa cells
KTSCVFM
-
80% inhibition of farnesylation in Toxoplasma gondii and 80% inhibition of enzyme in HeLa cells
KTSCVIA
-
50% inhibition of farnesylation in Toxoplasma gondii and no inhibition of enzyme in HeLa cells
KTSCVIF
-
no inhibition of farnesylation in Toxoplasma gondii, 80% inhibition of enzyme in HeLa cells
KTSSVIM
-
80% inhibition of farnesylation in Toxoplasma gondii, 100% inhibition of enzyme in HeLa cells
L-Cys-L-Val-L-Leu-L-Ser
-
-
methyl (2S)-2-([(2S)-2-[(2-[[(2R)-2-amino-3-sulfanylpropyl]amino]-3-methylpentyl)oxy]-3-phenylpropanoyl]amino)-4-(methylsulfonyl)butanoate
-
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-phenylalaninate
-
-
methyl N-([3-[methyl(1-methylidene-2,3-disulfanylpropyl)amino]-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-1-yl]acetyl)methioninate
-
-
methyl N-([5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophen-2-yl]carbonyl)-L-methioninate
-
-
methyl N-[(6E)-2-benzyl-5-(1-methylethyl)-8-(sulfanylmethyl)dec-6-enoyl]methioninate
-
-
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonothioyl]-D-methioninate
-
-
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-D-methioninate
-
-
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-isoleucyl-L-methioninate
-
-
methyl N-[[3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[4-cyano-3-(3,4-dihydroxyphenyl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophen-2-yl]carbonyl]-L-methioninate
-
-
N'-[(1Z)-1-(3-hydroxy-1-oxo-1H-inden-2-yl)ethylidene]-3-(10H-phenothiazin-10-yl)propanehydrazide
-
-
N-(1-benzyl-2-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]ethyl)-1-methyl-1H-imidazole-4-sulfonamide
-
-
N-(1-benzyl-2-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]ethyl)-2-methylbenzenesulfonamide
-
-
N-([2-[(1E,6E,10E)-4-carboxy-4-(ethoxycarbonyl)-7,11,15-trimethylhexadeca-1,6,10,14-tetraen-1-yl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methionine
-
-
N-([2-[(6E,10E)-4-carboxy-4-(ethoxycarbonyl)-7,11,15-trimethylhexadeca-6,10,14-trien-1-yl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methionine
-
-
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-D-methionine
-
-
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-L-methionine
-
-
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-D-methionine
-
-
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-L-methionine
-
-
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-D-methionine
-
-
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-L-methionine
-
-
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-D-methionine
-
-
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-L-methionine
-
-
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-D-methionine
-
-
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-L-methionine
-
-
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-D-methionine
-
-
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-L-methionine
-
-
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-D-methionine
-
-
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-L-methionine
-
-
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-D-methionine
-
-
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-L-methionine
-
-
N-[(6E)-2-benzyl-5-(1-methylethyl)-8-(sulfanylmethyl)dec-6-enoyl]methionine
-
-
N-[2-([2-[(2-amino-3-sulfanylpropyl)amino]-3-methylbutyl]amino)-3-phenylpropyl]methionine
-
-
N-[2-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]acetyl]amino)-3-methylpentyl]-N-(naphthalen-1-ylmethyl)glycylmethionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonothioyl]-D-methionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-D-methionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-isoleucyl-L-methionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-N-methyl-D-methionine
-
-
N-[[3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
-
-
N-[[4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
-
-
N-[[4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophen-2-yl]carbonyl]-L-methionine
-
-
N-[[5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophen-2-yl]carbonyl]-L-methionine
-
-
N2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-glutamine
-
-
Na-[(3S)-3-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-phenylbutanoyl]-L-phenylalaninamide
-
-
SCH-66336
-
lonafarnib, Sarasar
shikonine
-
inhibits FTPase activity in a dose-dependent manner
tert-butyl (2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoate
-
-
tert-butyl 2-[2-(methylsulfanyl)ethyl]hydrazinecarboxylate
-
-
tert-butyl 4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-2-[(pyridin-3-ylmethyl)carbamoyl]piperazine-1-carboxylate
-
-
tert-butyl 4-(3-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]-2-[[(1-methyl-1H-imidazol-4-yl)sulfonyl]amino]propyl)piperidine-1-carboxylate
-
-
-
tert-butyl 4-(3-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]-2-[[(2-methylphenyl)sulfonyl]amino]propyl)piperidine-1-carboxylate
-
-
Zn2+
inhibition of human farnesyltransferase by zinc complexation can be improved with triazine-isoxazole moieties. The replacement of the isoxazole unit by a pyrrolidin-2-one is detrimental to the inhibitory activity while the pyrrolidin-2-thione derivatives conserves the biological potential
[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]propanedioic acid
-
-
[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]propanedioic acid
-
-
[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]sulfamic acid
-
-
[3-(1-methyl-1H-imidazol-2-yl)propyl][(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]propanedioic acid
-
-
[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanedioic acid
-
-
[[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]amino]propanedioic acid
-
-
[[2-([[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]amino)ethyl]sulfanyl]acetic acid
-
-
BMS-214662
-
BMS-214662
bind into the CAAX peptide site and compete with the CAAX substrate of FTase
BMS-214662
-
-
BMS-214662
bind into the CAAX peptide site and compete with the CAAX substrate of FTase
lonafarnib
active in Ras-dependent and -independent malignant tumors
R115777
-
-
R115777
-
tipifarnid, Zarnestra
SCH66336
-
-
tipifarnib
-
additional information
inhibition mechanisms for FTase and GGTase-I, EC 2.5.1.59, are different. Two classes of FTase enzyme inhibitors, bisubstrate imidazole-containing derivatives linked by an acidic substituent and a peptidyl chain and peptidomimetic molecules, which can be divided into two groups, namely thiol and non-thiol compounds. Molecular modeling studies of FTase and protein-inhibitor interactions, overview
-
additional information
inhibition mechanisms for FTase and GGTase-I, EC 2.5.1.59, are different. Two classes of FTase enzyme inhibitors, bisubstrate imidazole-containing derivatives linked by an acidic substituent and a peptidyl chain and peptidomimetic molecules, which can be divided into two groups, namely thiol and non-thiol compounds. Molecular modeling studies of FTase and protein-inhibitor interactions, overview
-
additional information
-
higher concentrations of the alpha-dicarbonyl compound results in more rapid and more extensive inactivation
-
additional information
-
not: KTSSVIM
-
additional information
-
addition of a methionine residue at position 2 of 3-arylthiophenes greatly improves enzyme inhibition, antiparasitic effect of the compounds on proliferation of 4 protozoan parasites, i.e. Plasmodium falciparum, Trypanosoma brucei brucei, Trypanosoma cruzi and Leishmania donovani, overview. No inhibition by 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)-N-(adamant-1-ylmethyl)thiophene-2-carboxamide, 3-(4-chlorophenyl)-4-cyano-N-(naphthalen-1-ylmethyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide, methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-N-methyl-D-methioninate, ethyl 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate, and methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
additional information
inhibition mechanisms for FTase and GGTase-I, EC 2.5.1.59, are different. Two classes of FTase enzyme inhibitors, bisubstrate imidazole-containing derivatives linked by an acidic substituent and a peptidyl chain and peptidomimetic molecules, which can be divided into two groups, namely thiol and non-thiol compounds. Molecular modeling studies of FTase and protein-inhibitor interactions, overview
-
additional information
inhibition mechanisms for FTase and GGTase-I, EC 2.5.1.59, are different. Two classes of FTase enzyme inhibitors, bisubstrate imidazole-containing derivatives linked by an acidic substituent and a peptidyl chain and peptidomimetic molecules, which can be divided into two groups, namely thiol and non-thiol compounds. Molecular modeling studies of FTase and protein-inhibitor interactions, overview
-
additional information
-
introduction of an N-benzylimidazole moiety on protein farnesyltransferase inhibitors highly improves their antiparasitic activity against parasite cell proliferation, e.g. of Plasmodium falciparum, Leishmania donovani, Trypanosoma cruzi, and Trypanosoma brucei, overview. Generally compounds of the arylthiophene series are not very active on Plasmodium falciparum. No inhibition by ethyl 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate and methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
additional information
-
synthesis of a family of 30 benzoylated N-ylides and evaluation for the inhibitory activity on human protein farnesyltransferase. Most of these novel compounds posses in vitro inhibition potencies in the micromolar range. The nature of the substituents on the pyridine and phenyl units proves to be important in determining inhibitory activity and generally, the replacement of the cyanoacrylonitrile function by a cyanoethylacrylate group decreases the biological potential on farnesyltransferase, structure-activity relationship, overview
-
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Adenocarcinoma
Protein farnesyltransferase inhibitors block the growth of ras-dependent tumors in nude mice.
Adenocarcinoma of Lung
Inhibition of farnesyl protein transferase by monoterpene, curcumin derivatives and gallotannin.
Bone Diseases
Clinical Trial of the Protein Farnesylation Inhibitors Lonafarnib, Pravastatin, and Zoledronic Acid in Children With Hutchinson-Gilford Progeria Syndrome.
Bone Diseases
Survey of plasma proteins in children with progeria pre-therapy and on-therapy with lonafarnib.
Breast Neoplasms
Inhibition of farnesyl protein transferase sensitizes human MCF-7 breast cancer cells to roscovitine-mediated cell cycle arrest.
Breast Neoplasms
Preclinical antitumor activity and pharmacodynamic studies with the farnesyl protein transferase inhibitor R115777 in human breast cancer.
Breast Neoplasms
The use of molecular markers in farnesyltransferase inhibitor (FTI) therapy of breast cancer.
Carcinogenesis
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.
Carcinogenesis
Inhibitors of farnesyl protein transferase and MEK1,2 induce apoptosis in fibroblasts transformed with farnesylated but not geranylgeranylated H-Ras.
Carcinogenesis
Prediction and evaluation of protein farnesyltransferase inhibition by commercial drugs.
Carcinogenesis
Structure of protein geranylgeranyltransferase-I from the human pathogen Candida albicans complexed with a lipid substrate.
Carcinogenesis
Targeting the protein prenyltransferases efficiently reduces tumor development in mice with K-RAS-induced lung cancer.
Carcinoma
Antitumor effect of a farnesyl protein transferase inhibitor in mammary and lymphoid tumors overexpressing N-ras in transgenic mice.
Carcinoma
Effects of SCH 59228, an orally bioavailable farnesyl protein transferase inhibitor, on the growth of oncogene-transformed fibroblasts and a human colon carcinoma xenograft in nude mice.
Carcinoma
K- and N-Ras are geranylgeranylated in cells treated with farnesyl protein transferase inhibitors.
Carcinoma
Manumycin and gliotoxin derivative KT7595 block Ras farnesylation and cell growth but do not disturb lamin farnesylation and localization in human tumour cells.
Carcinoma
Selective cytotoxicity of farnesylamine to pancreatic carcinoma cells and Ki-ras-transformed fibroblasts.
Carcinoma, Hepatocellular
Inhibition of cell growth of human hepatoma cell line (Hep G2) by a farnesyl protein transferase inhibitor: a preferential suppression of ras farnesylation.
Carcinoma, Hepatocellular
Manumycin and gliotoxin derivative KT7595 block Ras farnesylation and cell growth but do not disturb lamin farnesylation and localization in human tumour cells.
Chagas Disease
The protein farnesyltransferase inhibitor Tipifarnib as a new lead for the development of drugs against Chagas disease.
Colonic Neoplasms
Establishment and characterization of acquired resistance to the farnesyl protein transferase inhibitor R115777 in a human colon cancer cell line.
Colonic Neoplasms
Relationship between flavonoid structure and inhibition of farnesyl protein transferase.
Colorectal Neoplasms
A phase II trial of farnesyl protein transferase inhibitor SCH 66336, given by twice-daily oral administration, in patients with metastatic colorectal cancer refractory to 5-fluorouracil and irinotecan.
Corneal Opacity
Inhibition of corneal inflammation by the topical use of Ras farnesyltransferase inhibitors: selective inhibition of macrophage localization.
Hematologic Neoplasms
Anti-inflammatory activity in vitro and in vivo of the protein farnesyltransferase inhibitor tipifarnib.
Hematologic Neoplasms
Antitumor effect of a farnesyl protein transferase inhibitor in mammary and lymphoid tumors overexpressing N-ras in transgenic mice.
Hematologic Neoplasms
Cancer therapy. New strategies and treatment modalities for optimizing patient outcomes.
Hematologic Neoplasms
Characterization of a human carcinoma cell line selected for resistance to the farnesyl transferase inhibitor 4-(2-(4-(8-chloro-3,10-dibromo-6,11-dihydro-5H-benzo-(5,6)-cyclohepta(1,2-b)-pyridin-11(R)-yl)-1-piperidinyl)-2-oxo-ethyl)-1-piperidinecarboxamide (SCH66336).
Hematologic Neoplasms
Farnesyl protein transferase inhibitors as targeted therapies for hematologic malignancies.
Hematologic Neoplasms
Farnesyltransferase inhibitors in hematologic malignancies: new horizons in therapy.
Herpes Simplex
Peptidomimetic design.
Hypersensitivity
Heat-shock protein 40 is the key farnesylation target in meristem size control, abscisic acid signaling, and drought resistance.
Leukemia
Activity of the farnesyl protein transferase inhibitor SCH66336 against BCR/ABL-induced murine leukemia and primary cells from patients with chronic myeloid leukemia.
Leukemia
Stereochemistry-dependent inhibition of RAS farnesylation by farnesyl phosphonic acids.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Activity of the farnesyl protein transferase inhibitor SCH66336 against BCR/ABL-induced murine leukemia and primary cells from patients with chronic myeloid leukemia.
Leukemia, Myeloid, Acute
The influence of farnesyl protein transferase inhibitor R115777 (Zarnestra) alone and in combination with purine nucleoside analogs on acute myeloid leukemia progenitors in vitro.
Leukemia, Myeloid, Acute
[Farnesyltransferase inhibitors: preliminary results in acute myeloid leukemia]
Lung Neoplasms
Combining an FPTase inhibitor with cisplatin facilitates induction of apoptosis in human A549 lung cancer cells.
Lymphoma
Antitumor effect of a farnesyl protein transferase inhibitor in mammary and lymphoid tumors overexpressing N-ras in transgenic mice.
Malaria
2-Oxo-tetrahydro-1,8-naphthyridines as selective inhibitors of malarial protein farnesyltransferase and as anti-malarials.
Malaria
A Review on Plasmodium falciparum-Protein Farnesyltransferase Inhibitors as Antimalarial Drug Targets.
Malaria
Alisiaquinones and alisiaquinol, dual inhibitors of Plasmodium falciparum enzyme targets from a New Caledonian deep water sponge.
Malaria
Novel N-(4-Piperidinyl)benzamide antimalarials with mammalian protein farnesyltransferase inhibitory activity.
Malaria
Protein farnesyl transferase inhibitors for the treatment of malaria and African trypanosomiasis.
Malaria
Protein farnesyltransferase inhibitors exhibit potent antimalarial activity.
Malaria
Protein prenyl transferase activities of Plasmodium falciparum.
Malaria
Structure based binding between protein farnesyl transferase and PRL-PTP of malaria parasite: An interaction study of prenylation process in Plasmodium.
Medulloblastoma
Apoptosis of medulloblastoma cells in vitro follows inhibition of farnesylation using manumycin A.
Multiple Sclerosis
Inhibition of Rho GTPases with protein prenyltransferase inhibitors prevents leukocyte recruitment to the central nervous system and attenuates clinical signs of disease in an animal model of multiple sclerosis.
Neoplasm Metastasis
Targeting the protein prenyltransferases efficiently reduces tumor development in mice with K-RAS-induced lung cancer.
Neoplasms
2'-benzoyloxycinnamaldehyde induces apoptosis in human carcinoma via reactive oxygen species.
Neoplasms
A peptidomimetic inhibitor of farnesyl:protein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines.
Neoplasms
A phase I and pharmacological study of the farnesyl protein transferase inhibitor L-778,123 in patients with solid malignancies.
Neoplasms
A phase I safety, pharmacological and biological study of the farnesyl protein transferase inhibitor, tipifarnib and capecitabine in advanced solid tumors.
Neoplasms
A phase I safety, pharmacological, and biological study of the farnesyl protein transferase inhibitor, lonafarnib (SCH 663366), in combination with cisplatin and gemcitabine in patients with advanced solid tumors.
Neoplasms
A Phase I trial of the farnesyl protein transferase inhibitor R115777 in combination with gemcitabine and cisplatin in patients with advanced cancer.
Neoplasms
A phase I trial of the novel farnesyl protein transferase inhibitor, BMS-214662, in combination with paclitaxel and carboplatin in patients with advanced cancer.
Neoplasms
Andrastins A-D, Penicillium roqueforti Metabolites consistently produced in blue-mold-ripened cheese.
Neoplasms
Antitumor activity of SCH 66336, an orally bioavailable tricyclic inhibitor of farnesyl protein transferase, in human tumor xenograft models and wap-ras transgenic mice.
Neoplasms
Antitumor effect of a farnesyl protein transferase inhibitor in mammary and lymphoid tumors overexpressing N-ras in transgenic mice.
Neoplasms
Antitumor effect of the cinnamaldehyde derivative CB403 through the arrest of cell cycle progression in the G2/M phase.
Neoplasms
Bioactive constituents and medicinal importance of genus Alnus.
Neoplasms
Caged protein prenyltransferase substrates: tools for understanding protein prenylation.
Neoplasms
Cancer therapy. New strategies and treatment modalities for optimizing patient outcomes.
Neoplasms
Carcinogen and dietary lipid regulate ras expression and localization in rat colon without affecting farnesylation kinetics.
Neoplasms
Characterization of a human carcinoma cell line selected for resistance to the farnesyl transferase inhibitor 4-(2-(4-(8-chloro-3,10-dibromo-6,11-dihydro-5H-benzo-(5,6)-cyclohepta(1,2-b)-pyridin-11(R)-yl)-1-piperidinyl)-2-oxo-ethyl)-1-piperidinecarboxamide (SCH66336).
Neoplasms
Clavaric acid: a triterpenoid inhibitor of farnesyl-protein transferase from Clavariadelphus truncatus.
Neoplasms
Combination therapy with the farnesyl protein transferase inhibitor SCH66336 and SCH58500 (p53 adenovirus) in preclinical cancer models.
Neoplasms
Combining the farnesyltransferase inhibitor lonafarnib with paclitaxel results in enhanced growth inhibitory effects on human ovarian cancer models in vitro and in vivo.
Neoplasms
Conformation of a novel tetrapeptide inhibitor NH2-D-Trp-D-Met-Phe(pCl)-Gla-NH2 bound to farnesyl-protein transferase.
Neoplasms
Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity.
Neoplasms
Current progress on farnesyl protein transferase inhibitors.
Neoplasms
Cytotoxic farnesyl glycosides from Pittosporum pancheri.
Neoplasms
Dietary fish oil inhibits the expression of farnesyl protein transferase and colon tumor development in rodents.
Neoplasms
Enzyme-Driven Membrane-Targeted Chimeric Peptide for Enhanced Tumor Photodynamic Immunotherapy.
Neoplasms
Evaluation of farnesyl:protein transferase and geranylgeranyl:protein transferase inhibitor combinations in preclinical models.
Neoplasms
Farnesyl protein transferase and tumor cell growth inhibitory activities of lipiferolide isolated from Liriodendron tulipifera.
Neoplasms
Farnesyl protein transferase inhibitors as potential cancer chemopreventives.
Neoplasms
Farnesyl protein transferase inhibitors as targeted therapies for hematologic malignancies.
Neoplasms
Farnesyl transferase inhibitors in myeloid disorders.
Neoplasms
Farnesyl transferase inhibitors in myeloid malignancies.
Neoplasms
Farnesyl: proteintransferase inhibitors as agents to inhibit tumor growth.
Neoplasms
Farnesyltransferase inhibitors (FTIs) in myeloid malignancies.
Neoplasms
Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB.
Neoplasms
Farnesyltransferase inhibitors and anti-Ras therapy.
Neoplasms
Farnesyltransferase inhibitors versus Ras inhibitors.
Neoplasms
High-performance liquid chromatography/mass spectrometry characterization of Ki4B-Ras in PSN-1 cells treated with the prenyltransferase inhibitor L-778,123.
Neoplasms
Identification of pharmacokinetically stable 3, 10-dibromo-8-chlorobenzocycloheptapyridine farnesyl protein transferase inhibitors with potent enzyme and cellular activities.
Neoplasms
Inhibition of DNA synthesis by a farnesyltransferase inhibitor involves inhibition of the p70(s6k) pathway.
Neoplasms
Inhibition of farnesyl protein transferase and P21ras memebrane association by d-limonene in human pancreas tumor cells in vitro.
Neoplasms
Inhibition of farnesyl protein transferase by monoterpene, curcumin derivatives and gallotannin.
Neoplasms
Inhibition of farnesyltransferase induces regression of mammary and salivary carcinomas in ras transgenic mice.
Neoplasms
Inhibition of protein farnesyltransferase: a possible mechanism of tumor prevention by dehydroepiandrosterone sulfate.
Neoplasms
Inhibition of protein farnesyltransferase: a possible mechanism of tumor prevention for dehydroepiandrosterone sulfate.
Neoplasms
Inhibition of RAS-targeted prenylation: protein farnesyl transferase inhibitors revisited.
Neoplasms
Inhibitors of farnesyl protein transferase and MEK1,2 induce apoptosis in fibroblasts transformed with farnesylated but not geranylgeranylated H-Ras.
Neoplasms
Inhibitors of farnesyl:protein transferase--a possible cancer chemotherapeutic.
Neoplasms
Inhibitors of farnesylation of Ras from a microbial natural products screening program.
Neoplasms
Inhibitors of prenyl transferases.
Neoplasms
Inhibitors of protein farnesyltransferase as novel anticancer agents.
Neoplasms
Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl diphosphate synthase inhibitors: an X-ray and NMR investigation.
Neoplasms
Manumycin A inhibits triple-negative breast cancer growth through LC3-mediated cytoplasmic vacuolation death.
Neoplasms
Molecular dynamics analysis of a series of 22 potential farnesyltransferase substrates containing a CaaX-motif.
Neoplasms
Mouse mammary tumor virus-Ki-rasB transgenic mice develop mammary carcinomas that can be growth-inhibited by a farnesyl:protein transferase inhibitor.
Neoplasms
NMR studies of novel inhibitors bound to farnesyl-protein transferase.
Neoplasms
Novel farnesol and geranylgeraniol analogues: A potential new class of anticancer agents directed against protein prenylation.
Neoplasms
Phase I and pharmacokinetic study of farnesyl protein transferase inhibitor R115777 in advanced cancer.
Neoplasms
Phase I clinical and pharmacologic study of chronic oral administration of the farnesyl protein transferase inhibitor R115777 in advanced cancer.
Neoplasms
Phase I pharmacokinetic and pharmacodynamic study of the prenyl transferase inhibitor AZD3409 in patients with advanced cancer.
Neoplasms
Potent, selective, and orally bioavailable tricyclic pyridyl acetamide N-oxide inhibitors of farnesyl protein transferase with enhanced in vivo antitumor activity.
Neoplasms
Pre-clinical development of farnesyltransferase inhibitors.
Neoplasms
Prevention of farnesylation of c-Ha-Ras protein enhances synergistically the cytotoxic action of doxorubicin in cycling but not in quiescent cells.
Neoplasms
Protein farnesylation inhibitors cause donut-shaped cell nuclei attributable to a centrosome separation defect.
Neoplasms
Protein farnesyltransferase in embryogenesis, adult homeostasis, and tumor development.
Neoplasms
Protein farnesyltransferase inhibitors block the growth of ras-dependent tumors in nude mice.
Neoplasms
Ras as a target in cancer therapy.
Neoplasms
Ras farnesyltransferase inhibition: a novel and safe approach for cancer chemotherapy.
Neoplasms
Relationship between flavonoid structure and inhibition of farnesyl protein transferase.
Neoplasms
Scaffold-based analysis of nonpeptide oncogenic FTase inhibitors using multiple similarity matching, binding affinity scoring and enzyme inhibition assay.
Neoplasms
Search for protein farnesyltransferase inhibitors of microbial origin: our strategy and results as well as the results obtained by other groups.
Neoplasms
Selective inhibition of ras-dependent transformation by a farnesyltransferase inhibitor.
Neoplasms
Synergy of the protein farnesyltransferase inhibitor SCH66336 and cisplatin in human cancer cell lines.
Neoplasms
Synthesis and biological evaluation of dimeric cinnamaldehydes as potent antitumor agents.
Neoplasms
The potential of farnesyltransferase inhibitors as cancer chemotherapeutics.
Neuroblastoma
Inhibition of farnesyl-protein-transferase in neuroblastoma cells by alpha-hydroxyfarnesylphosphonate.
Neuroblastoma
Neuroblastoma: inhibition of progression (Part II). Basic science in pediatric surgery.
Pancreatic Neoplasms
Inhibition of farnesyl protein transferase by monoterpene, curcumin derivatives and gallotannin.
Pancreatic Neoplasms
Modified radiosensitivity of pancreatic cancer xenografts by farnesyl protein transferase inhibitor and MEK inhibitor.
Parasitic Diseases
Thematic review series: Lipid Posttranslational Modifications. Fighting parasitic disease by blocking protein farnesylation.
Parasitic Diseases
Towards the synthesis of bisubstrate inhibitors of protein farnesyltransferase: Synthesis and biological evaluation of new farnesylpyrophosphate analogues.
Progeria
A protein farnesyltransferase inhibitor ameliorates disease in a mouse model of progeria.
Progeria
Assessing the efficacy of protein farnesyltransferase inhibitors in mouse models of progeria.
Progeria
Blocking protein farnesyltransferase improves nuclear blebbing in mouse fibroblasts with a targeted Hutchinson-Gilford progeria syndrome mutation.
Progeria
Protein farnesyltransferase inhibitors and progeria.
Progeria
Targeting protein prenylation in progeria.
Reperfusion Injury
FPTIII mitigates peroxisome-mediated oxidative stress in kidneys of spontaneously hypertensive diabetic rats.
Trypanosomiasis, African
Cloning, heterologous expression, and distinct substrate specificity of protein farnesyltransferase from Trypanosoma brucei.
Trypanosomiasis, African
Isothiazole dioxides: synthesis and inhibition of Trypanosoma brucei protein farnesyltransferase.
Trypanosomiasis, African
Protein farnesyl transferase inhibitors for the treatment of malaria and African trypanosomiasis.
Vasospasm, Intracranial
Potential role of Ras in cerebral vasospasm after experimental subarachnoid hemorrhage in rabbits.
Whooping Cough
Activation of a Ca2+-dependent K+ current in mouse fibroblasts by lysophosphatidic acid requires a pertussis toxin-sensitive G protein and Ras.
Whooping Cough
The CB(1) cannabinoid receptor is coupled to the activation of c-Jun N-terminal kinase.
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0.00024
methyl (2S)-2-([(2S)-2-[(2-[[(2R)-2-amino-3-sulfanylpropyl]amino]-3-methylpentyl)oxy]-3-phenylpropanoyl]amino)-4-(methylsulfonyl)butanoate
Homo sapiens
pH and temperature not specified in the publication
0.0065
(2E)-2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]butanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.13
(2E,4E,8E)-5,9,13-trimethyltetradeca-2,4,8,12-tetraenoic acid
Homo sapiens
-
30°C, pH 7.5
0.012 - 0.175
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
0.000016
(2Z,6E)-3-(3-methylbut-2-enyl)-7,11-dimethyldodeca-2,6,10-triene monophosphate
Homo sapiens
-
IC50: 16 nM
0.000013
(2Z,6E)-3-tert-butyl-7,11-dimethyldodeca-2,6,10-triene monophosphate
Homo sapiens
-
IC50: 13 nM
0.5
(4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-4,8,12-trienoic acid
Homo sapiens
-
30°C, pH 7.5
0.2
(4E,8E)-5,9,13-trimethyl-N-(phenylsulfonyl)tetradeca-4,8,12-trienamide
Homo sapiens
-
value above, 30°C, pH 7.5
0.2
(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienamide
Homo sapiens
-
value above, 30°C, pH 7.5
0.17
(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoic acid
Homo sapiens
-
30°C, pH 7.5
0.0104
(4S)-4-([[5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophen-2-yl]carbonyl]amino)-5-tert-butoxy-5-oxopentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.2
(6E,10E)-7,11,15-trimethyl-3-oxohexadeca-6,10,14-trienoic acid
Homo sapiens
-
30°C, pH 7.5
0.06
(7E,11E)-8,12,16-trimethyl-4-oxoheptadeca-7,11,15-trienoic acid
Homo sapiens
-
30°C, pH 7.5
0.0259
1-(1-[3,4-bis[(hydroxyacetyl)amino]phenyl]-4,4-dicyano-1-oxobut-3-en-2-yl)-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.000024
1-(1H-imidazol-5-ylmethyl)-7-pyridin-4-yl-4-[[2-(trifluoromethoxy)phenyl]carbonyl]-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine
Homo sapiens
-
-
0.0462
1-(4,4-dicyano-1-oxo-1-phenylbut-3-en-2-yl)-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0364
1-[(3Z)-1-(4-bromophenyl)-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0319
1-[(3Z)-1-(4-chlorophenyl)-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
55.22
1-[(3Z)-1-[3,4-bis[(hydroxyacetyl)amino]phenyl]-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0208
1-[(3Z)-4-cyano-1-(3,4-dimethoxyphenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-methoxypyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0239
1-[(3Z)-4-cyano-1-(4-cyanophenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0623
1-[(3Z)-4-cyano-1-(4-fluorophenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0627
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methoxyphenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0436
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methylphenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0435
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-(3,4,5-trimethoxyphenyl)hept-3-en-2-yl]-2,4-dimethylpyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.048
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-(3,4,5-trimethoxyphenyl)hept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0309
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-phenylhept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0197
1-[1-(4-bromophenyl)-4,4-dicyano-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0125
1-[1-(4-chlorophenyl)-4,4-dicyano-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0314
1-[4,4-dicyano-1-(3,4-dimethoxyphenyl)-1-oxobut-3-en-2-yl]-3-methoxypyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0462
1-[4,4-dicyano-1-(4-cyanophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0236
1-[4,4-dicyano-1-(4-fluorophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0274
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-2,4-dimethylpyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0222
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0273
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-3-methoxypyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0145
1-[4,4-dicyano-1-(4-methylphenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0282
1-[4,4-dicyano-1-(4-nitrophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0201
1-[4,4-dicyano-1-oxo-1-(3,4,5-trimethoxyphenyl)but-3-en-2-yl]-2,4-dimethylpyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0156
1-[4,4-dicyano-1-oxo-1-(3,4,5-trimethoxyphenyl)but-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
18-oxa-2,5,9,11-tetraazahexacyclo[17.6.2.22,5.113,17.07,11.022,26]triaconta-1(26),7,9,13(28),14,16,19,21,22,24,26-undecaene-16-carbonitrile
Homo sapiens
-
-
0.000001
2-amino-3-[2-butyl-4-(naphthalen-1-ylcarbonyl)piperazin-1-yl]propane-1-thiol
Homo sapiens
-
IC50 less than 0.000001 mM
0.59
2-[(2E)-3,7-dimethyl-1-(1-methyl-1H-imidazol-2-yl)octa-2,6-dien-1-yl]butanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.0054
2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]butanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.000001
29-oxo-18-oxa-2,6,9,11-tetraazahexacyclo[17.5.3.12,5.113,17.07,11.022,26]nonacosa-7,9,13(28),14,16,19,21,26-octaene-16-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM
0.016
3-(4-chlorophenyl)-4-cyano-5-(isopropylthio)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.05
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)-N-adamantylthiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.016
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
0.0019
3-(4-chlorophenyl)-4-cyano-N'-[2-(methylsulfanyl)ethyl]-5-(propan-2-ylsulfanyl)thiophene-2-carbohydrazide
Homo sapiens
-
pH and temperature not specified in the publication
0.0216
3-(4-chlorophenyl)-4-cyano-N-(naphthalen-1-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.024
3-(4-chlorophenyl)-4-cyano-N-[2-(methylsulfanyl)ethyl]-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.022
3-(4-chlorophenyl)-4-ethynyl-5-[(1H-imidazol-4-ylacetyl)amino]thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00097
3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl][[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.0033
3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.000189
3-allylfarnesyl diphosphate
Homo sapiens
-
IC50: 189 nM
0.00335
3-methyl-2-[2-oxo-2-(10H-phenothiazin-10-yl)ethyl]indeno[1,2-c]pyrazol-4(2H)-one
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.16
3-oxo-3-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanoic acid
Homo sapiens
-
30°C, pH 7.5
0.000031
3-tert-butylfarnesyl diphosphate
Homo sapiens
-
IC50: 31 nM
0.0008
3-[3-[2-([2-[1-(tert-butoxycarbonyl)piperidin-4-yl]-1-([(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]methyl)ethyl]sulfamoyl)benzyl]phenyl]propanoic acid
Homo sapiens
-
-
0.039
4-cyano-3-(3-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.02
4-cyano-3-(4-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.007
4-cyano-3-(4-methoxyphenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.015
4-cyano-3-(dibenzo[b,d]furan-1-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.0055
4-cyano-3-(naphthalen-2-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.0048
4-cyano-3-[3-(methoxycarbonyl)phenyl]-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00001
4-ethynyl-5-([[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino)-3-phenylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.13
4-oxo-4-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]butanoic acid
Homo sapiens
-
30°C, pH 7.5
0.000285
4-[(5-[[4-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.00031
4-[(5-[[4-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-yl)piperidin-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.0000465
4-[(5-[[4-(5-oxido-7-propyl-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.000043
4-[(5-[[4-(7-butyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.0000448
4-[(5-[[4-(7-methyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.000045
4-[(5-[[4-(7-methyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)piperidin-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.0373
4-[5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1,2-oxazol-3-yl]-N,N-dimethylaniline
Homo sapiens
pH 7.5, 30°C
0.0051
4-[[4-([[4-(4-chlorophenyl)-3-ethynylthiophen-2-yl]amino]methyl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
pH 7.5, 30°C
0.0000173
4-[[5-([4-[7-(3-morpholin-4-ylpropyl)-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl]azepan-1-yl]methyl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
-
0.0038
5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1-(4-methoxyphenyl)pyrrolidin-2-thione
Homo sapiens
pH 7.5, 30°C
0.0411
5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1-[3-(trifluoromethyl)phenyl]pyrrolidine-2-thione
Homo sapiens
pH 7.5, 30°C
0.02
5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophene-2-carboxylic acid
Homo sapiens
-
about, pH and temperature not specified in the publication
0.00037
5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.06
5-oxo-5-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]pentanoic acid
Homo sapiens
-
30°C, pH 7.5
0.00064
5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00038
5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-4-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00098
5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00018
6-[(4-hydroxyphenyl)(1H-imidazol-1-yl)methyl]-4-phenyl-1,2-dihydroquinolin-2-ol
Homo sapiens
-
-
0.0044
acetylgliotoxin
Homo sapiens
-
-
0.0487
alphabeta-dehydrocurvularin
Homo sapiens
-
-
0.0249
andrastin A
Homo sapiens
-
-
0.0471
andrastin B
Homo sapiens
-
-
0.0133
andrastin C
Homo sapiens
-
-
0.0000014
BMS-214662
Homo sapiens
-
-
0.000175
chaetomellic acid A
Homo sapiens
-
30°C, pH 7.5
0.0168
citreohybridone A
Homo sapiens
-
-
0.0036
citreohybridone B
Homo sapiens
-
-
0.7
di-tert-butyl 2-[(2E,6E,10E)-1,3,7-trimethyl-1-(1-methyl-1H-imidazol-2-yl)dodeca-2,6,10-trien-1-yl]butanedioate
Homo sapiens
-
30°C, pH 7.5
0.05
ethyl (2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-1-[2-(methylsulfanyl)ethyl]hydrazinyl)acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.0372
ethyl 3-(2,5-dimethoxyphenyl)-1,2-oxazole-5-carboxylate
Homo sapiens
pH 7.5, 30°C
0.021
ethyl 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.0012
ethyl 3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.1
ethyl 3-(4-chlorophenyl)-4-ethynyl-5-[(1H-imidazol-4-ylacetyl)amino]thiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.034
ethyl 3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]amino)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.000013
ethyl 3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl][[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.00019
ethyl 4-ethynyl-5-([[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino)-3-phenylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.00013
ethyl 5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.00029
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.00033
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-4-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.0021
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.0093
ethyl [[2-([[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]amino)ethyl]sulfanyl]acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.0000006 - 0.000015
FTI-276
0.0011
gliotoxin
Homo sapiens
-
-
0.0473
granaticin A
Homo sapiens
-
-
0.0448
granaticin B
Homo sapiens
-
-
0.058
kurasoin A
Homo sapiens
-
-
0.065
kurasoin B
Homo sapiens
-
-
0.0000018
L-739,750
Homo sapiens
-
-
0.000002
L-788,123
Homo sapiens
-
-
0.0066
L-Cys-L-Val-L-Leu-L-Ser
Homo sapiens
-
-
0.00024
methyl (2S)-2-([(2S)-2-[(2-[[(2R)-2-amino-3-sulfanylpropyl]amino]-3-methylpentyl)oxy]-3-phenylpropanoyl]amino)-4-(methylsulfonyl)butanoate
Homo sapiens
pH and temperature not specified in the publication
0.000022
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-phenylalaninate
Homo sapiens
-
-
0.00068
methyl N-([5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophen-2-yl]carbonyl)-L-methioninate
Homo sapiens
-
pH 7.5, 30°C
0.00046
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonothioyl]-D-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.05
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-D-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.05
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-isoleucyl-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.0046
methyl N-[[3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH 7.5, 30°C
0.023
methyl N-[[3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.0047
methyl N-[[4-cyano-3-(3,4-dihydroxyphenyl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.05
methyl N-[[4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.0056
methyl N-[[4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.05
methyl N-[[5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.00015
methyl N-[[5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH 7.5, 30°C
0.00373
N'-[(1Z)-1-(3-hydroxy-1-oxo-1H-inden-2-yl)ethylidene]-3-(10H-phenothiazin-10-yl)propanehydrazide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000056
N-(1-benzyl-2-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]ethyl)-1-methyl-1H-imidazole-4-sulfonamide
Homo sapiens
-
-
0.00016
N-(1-benzyl-2-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]ethyl)-2-methylbenzenesulfonamide
Homo sapiens
-
-
0.00064
N-([2-[(1E,6E,10E)-4-carboxy-4-(ethoxycarbonyl)-7,11,15-trimethylhexadeca-1,6,10,14-tetraen-1-yl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methionine
Homo sapiens
-
30°C, pH 7.5
0.00024
N-([2-[(6E,10E)-4-carboxy-4-(ethoxycarbonyl)-7,11,15-trimethylhexadeca-6,10,14-trien-1-yl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methionine
Homo sapiens
-
30°C, pH 7.5
0.000112
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-L-methionine
Homo sapiens
-
-
0.000075
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-D-methionine
Homo sapiens
-
-
0.000053
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-L-methionine
Homo sapiens
-
-
0.000053
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-D-methionine
Homo sapiens
-
-
0.000055
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-L-methionine
Homo sapiens
-
-
0.00005
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-D-methionine
Homo sapiens
-
-
0.000045
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-L-methionine
Homo sapiens
-
-
0.843
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-D-methionine
Homo sapiens
-
-
0.302
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-D-methionine
Homo sapiens
-
-
0.151
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-L-methionine
Homo sapiens
-
-
0.012
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-D-methionine
Homo sapiens
-
-
0.016
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-L-methionine
Homo sapiens
-
-
0.0000021
N-[2-([2-[(2-amino-3-sulfanylpropyl)amino]-3-methylbutyl]amino)-3-phenylpropyl]methionine
Homo sapiens
-
-
0.00000015
N-[2-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]acetyl]amino)-3-methylpentyl]-N-(naphthalen-1-ylmethyl)glycylmethionine
Homo sapiens
-
-
0.0017
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonothioyl]-D-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.00045
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-D-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.0019
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-isoleucyl-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.000067 - 0.000077
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
0.0018
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-N-methyl-D-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.000042
N-[[3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.00014
N-[[4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.0087
N-[[4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.0036
N-[[5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH 7.5, 30°C
0.000076
N2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-glutamine
Homo sapiens
-
pH and temperature not specified in the publication
0.0000285
Na-[(3S)-3-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-phenylbutanoyl]-L-phenylalaninamide
Homo sapiens
-
-
0.0237
O-methylthysanone
Homo sapiens
-
-
0.025
penicillic acid
Homo sapiens
-
-
0.00065
pepticinnamin A
Homo sapiens
-
-
-
0.0002
pepticinnamin B
Homo sapiens
-
-
-
0.0001
pepticinnamin C
Homo sapiens
-
-
-
0.001
pepticinnamin D
Homo sapiens
-
-
-
0.0003
pepticinnamin E
Homo sapiens
-
-
0.0005
pepticinnamin F
Homo sapiens
-
-
-
0.00000086
R115777
Homo sapiens
-
-
0.027
SCH-37370
Homo sapiens
-
-
0.00025
SCH-44342
Homo sapiens
-
-
0.0000019
SCH-66336
Homo sapiens
-
-
0.0145
sclerotiorin
Homo sapiens
-
-
0.048
spiculisporic acid
Homo sapiens
-
-
0.3
tert-butyl (2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoate
Homo sapiens
-
30°C, pH 7.5
0.0037
tert-butyl 4-(3-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]-2-[[(1-methyl-1H-imidazol-4-yl)sulfonyl]amino]propyl)piperidine-1-carboxylate
Homo sapiens
-
-
-
0.00405
tert-butyl 4-(3-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]-2-[[(2-methylphenyl)sulfonyl]amino]propyl)piperidine-1-carboxylate
Homo sapiens
-
-
0.0122
thysanone
Homo sapiens
-
-
0.0257
WS5995-C
Homo sapiens
-
-
0.0009
[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.00088
[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.085
[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]sulfamic acid
Homo sapiens
-
30°C, pH 7.5
0.021
[3-(1-methyl-1H-imidazol-2-yl)propyl][(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.01
[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.06
[[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]amino]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.0037
[[2-([[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]amino)ethyl]sulfanyl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.012
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
Homo sapiens
-
30°C, pH 7.5
0.175
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
Homo sapiens
-
30°C, pH 7.5
0.016
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.016
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0000006
FTI-276
Homo sapiens
-
-
0.000015
FTI-276
Homo sapiens
-
pH 7.5, 30°C
0.000067
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.000077
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH 7.5, 30°C
0.000077
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
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Park, H.W.; Beese, L.S.
Protein farnesyltransferase
Curr. Opin. Struct. Biol.
7
873-880
1997
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
brenda
Okolotowicz, K.J.; Lee, W.J.; Hartman, R.F.; Kim, A.Y.; Ottersberg, S.R.; Robinson, D.E., Jr.; Lefler, S.R.; Rose, S.D.
Inactivation of protein farnesyltransferase by active-site-targeted dicarbonyl compounds
Arch. Pharm.
334
194-202
2001
Homo sapiens
brenda
Ibrahim, M.; Azzouz, N.; Gerold, P.; Schwarz, R.T.
Identification and characterisation of Toxoplasma gondii protein farnesyltransferase
Int. J. Parasitol.
31
1489-1497
2001
Homo sapiens, Toxoplasma gondii
brenda
Wu, Z.; Demma, M.; Strickland, C.L.; Syto, R.; Le, H.V.; Windsor, W.T.; Weber, P.C.
High-level expression, purification, kinetic characterization and crystallization of protein farnesyltransferase b-subunit C-terminal mutants
Protein Eng.
12
341-348
1999
Homo sapiens, Rattus norvegicus
brenda
Reid, T.S.; Long, S.B.; Beese, L.S.
Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes
Biochemistry
43
9000-9008
2004
Homo sapiens
brenda
Maurer-Stroh, S.; Washietl, S.; Eisenhaber, F.
Protein prenyltransferases
Genome Biol.
4
212
2003
Homo sapiens
brenda
Reid, T.S.; Terry, K.L.; Casey, P.J.; Beese, L.S.
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity
J. Mol. Biol.
343
417-433
2004
Homo sapiens
brenda
Henriksen, B.S.; Zahn, T.J.; Evanseck, J.D.; Firestine, S.M.; Gibbs, R.A.
Computational and conformational evaluation of FTase alternative substrates: insight into a novel enzyme binding pocket
J. Chem. Inf. Model.
45
1047-1052
2005
Homo sapiens
brenda
Lane, K.T.; Beese, L.S.
Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I
J. Lipid Res.
47
681-699
2006
Homo sapiens
brenda
Clark, M.K.; Scott, S.A.; Wojtkowiak, J.; Chirco, R.; Mathieu, P.; Reiners, J.J.; Mattingly, R.R.; Borch, R.F.; Gibbs, R.A.
Synthesis, biochemical, and cellular evaluation of farnesyl monophosphate prodrugs as farnesyltransferase inhibitors
J. Med. Chem.
50
3274-3282
2007
Homo sapiens
brenda
Cui, G.; Merz, K.M.
Computational studies of the farnesyltransferase ternary complex part II: the conformational activation of farnesyldiphosphate
Biochemistry
46
12375-12381
2007
Homo sapiens
brenda
Gilleron, P.; Wlodarczyk, N.; Houssin, R.; Farce, A.; Laconde, G.; Goossens, J.F.; Lemoine, A.; Pommery, N.; Henichart, J.P.; Millet, R.
Design, synthesis and biological evaluation of substituted dioxodibenzothiazepines and dibenzocycloheptanes as farnesyltransferase inhibitors
Bioorg. Med. Chem. Lett.
17
5465-5471
2007
Homo sapiens
brenda
Bolchi, C.; Pallavicini, M.; Rusconi, C.; Diomede, L.; Ferri, N.; Corsini, A.; Fumagalli, L.; Pedretti, A.; Vistoli, G.; Valoti, E.
Peptidomimetic inhibitors of farnesyltransferase with high in vitro activity and significant cellular potency
Bioorg. Med. Chem. Lett.
17
6192-6196
2007
Homo sapiens
brenda
Braun, T.; Fenaux, P.
Farnesyltransferase inhibitors and their potential role in therapy for myelodysplastic syndromes and acute myeloid leukaemia
Br. J. Haematol.
141
576-586
2008
Homo sapiens
brenda
Nguyen, U.T.; Cramer, J.; Gomis, J.; Reents, R.; Gutierrez-Rodriguez, M.; Goody, R.S.; Alexandrov, K.; Waldmann, H.
Exploiting the substrate tolerance of farnesyltransferase for site-selective protein derivatization
Chembiochem
8
408-423
2007
Homo sapiens
brenda
Equbal, T.; Silakari, O.; Ravikumar, M.
Exploring three-dimensional quantitative structural activity relationship (3D-QSAR) analysis of SCH 66336 (Sarasar) analogues of farnesyltransferase inhibitors
Eur. J. Med. Chem.
43
204-209
2008
Homo sapiens
brenda
Iwasaki, S.; Omura, S.
Search for protein farnesyltransferase inhibitors of microbial origin: our strategy and results as well as the results obtained by other groups
J. Antibiot.
60
1-12
2007
Homo sapiens
brenda
Puntambekar, D.S.; Giridhar, R.; Yadav, M.R.
Inhibition of farnesyltransferase: a rational approach to treat cancer?
J. Enzyme Inhib. Med. Chem.
22
127-140
2007
Homo sapiens
brenda
Kim, S.J.; Kwon, B.; Kim, S.; Baek, N.; Yang, J.H.; Lee, J.J.; Lee, S.I.; Kwon, Y.; Park, H.W.; Lee, J.H.; Park, J.; Kim, D.K.
Farnesyl protein transferase inhibitory components of Lithospermum erythrorhizon
Nat. Prod. Sci.
13
328-331
2007
Homo sapiens, Rattus norvegicus
-
brenda
Duez, S.; Coudray, L.; Mouray, E.; Grellier, P.; Dubois, J.
Towards the synthesis of bisubstrate inhibitors of protein farnesyltransferase: Synthesis and biological evaluation of new farnesylpyrophosphate analogues
Bioorg. Med. Chem.
18
543-556
2010
Saccharomyces cerevisiae, Homo sapiens, Plasmodium falciparum, Trypanosoma brucei
brenda
Hast, M.A.; Fletcher, S.; Cummings, C.G.; Pusateri, E.E.; Blaskovich, M.A.; Rivas, K.; Gelb, M.H.; Van Voorhis, W.C.; Sebti, S.M.; Hamilton, A.D.; Beese, L.S.
Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase
Chem. Biol.
16
181-192
2009
Homo sapiens, Plasmodium falciparum, Rattus norvegicus
brenda
Zhou, J.; Vos, C.C.; Gjyrezi, A.; Yoshida, M.; Khuri, F.R.; Tamanoi, F.; Giannakakou, P.
The protein farnesyltransferase regulates HDAC6 activity in a microtubule-dependent manner
J. Biol. Chem.
284
9648-9655
2009
Homo sapiens (P49354), Homo sapiens
brenda
Coudray, L.; de Figueiredo, R.M.; Duez, S.; Cortial, S.; Dubois, J.
Synthesis of imidazole-containing analogues of farnesyl pyrophosphate and evaluation of their biological activity on protein farnesyltransferase
J. Enzyme Inhib. Med. Chem.
24
972-985
2009
Saccharomyces cerevisiae, Homo sapiens, Plasmodium falciparum
brenda
Baciu-Atudosie, L.; Ghinet, A.; Farce, A.; Dubois, J.; Belei, D.; Bicu, E.
Synthesis and biological evaluation of new phenothiazine derivatives bearing a pyrazole unit as protein farnesyltransferase inhibitors
Bioorg. Med. Chem. Lett.
22
6896-6902
2012
Homo sapiens
brenda
Hougland, J.L.; Gangopadhyay, S.A.; Fierke, C.A.
Expansion of protein farnesyltransferase specificity using "tunable" active site interactions: development of bioengineered prenylation pathways
J. Biol. Chem.
287
38090-38100
2012
Homo sapiens
brenda
Lethu, S.; Bosc, D.; Mouray, E.; Grellier, P.; Dubois, J.
New protein farnesyltransferase inhibitors in the 3-arylthiophene 2-carboxylic acid series: diversification of the aryl moiety by solid-phase synthesis
J. Enzyme Inhib. Med. Chem.
28
163-171
2013
Saccharomyces cerevisiae, Homo sapiens, Trypanosoma brucei
brenda
Abuhaie, C.M.; Ghinet, A.; Farce, A.; Dubois, J.; Rigo, B.; Bicu, E.
Synthesis and biological evaluation of a new series of N-ylides as protein farnesyltransferase inhibitors
Bioorg. Med. Chem. Lett.
23
5887-5892
2013
Homo sapiens
brenda
Shen, M.; Pan, P.; Li, Y.; Li, D.; Yu, H.; Hou, T.
Farnesyltransferase and geranylgeranyltransferase I: structures, mechanism, inhibitors and molecular modeling
Drug Discov. Today
20
267-276
2015
Homo sapiens (P49354), Homo sapiens (P49356), Rattus norvegicus (Q02293), Rattus norvegicus (Q04631)
brenda
Bosc, D.; Mouray, E.; Cojean, S.; Franco, C.H.; Loiseau, P.M.; Freitas-Junior, L.H.; Moraes, C.B.; Grellier, P.; Dubois, J.
Highly improved antiparasitic activity after introduction of an N-benzylimidazole moiety on protein farnesyltransferase inhibitors
Eur. J. Med. Chem.
109
173-186
2016
Homo sapiens, Trypanosoma brucei
brenda
Bosc, D.; Mouray, E.; Grellier, P.; Cojean, S.; Loiseau, P.; Dubois, J.
Introduction of methionine mimics on 3-arylthiophene: Influence on protein farnesyltransferase inhibition and on antiparasitic activity
MedChemComm
4
1034-1041
2013
Homo sapiens, Trypanosoma brucei
-
brenda
Lucescu, L.; Ghinet, A.; Shova, S.; Magnez, R.; Thuru, X.; Farce, A.; Rigo, B.; Belei, D.; Dubois, J.; Bicu, E.
Exploring isoxazoles and pyrrolidinones decorated with the 4,6-dimethoxy-1,3,5-triazine unit as human farnesyltransferase inhibitors
Arch. Pharm.
352
e1800227
2019
Homo sapiens (P49354 and P49356)
brenda
Hagemann, A.; Mueller, G.; Manthey, I.; Bachmann, H.S.
Exploring the putative self-binding property of the human farnesyltransferase alpha-subunit
FEBS Lett.
591
3637-3648
2017
Homo sapiens (P49354 and P49356), Homo sapiens, Rattus norvegicus (Q04631 AND Q02293)
brenda