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amyloid beta-protein + H2O
?
-
cleaves cell adhesion RHDS sequence
-
-
?
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
-
-
-
-
?
beta-2-glycoprotein I + H2O
clipped beta-2-glycoprotein I
-
cleavage at Lys317-Thr318
-
-
?
Boc-Glu(OBzl)-Ala-Arg-4-methylcoumaryl-7-amide + H2O
Boc-Glu(OBzl)-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
substrate S-2288
-
-
?
D-LPRANSNH-C3H7 + H2O
D-LPR + ANSNH-C3H7
-
-
-
-
?
factor fIX + H2O
?
-
factor IX
-
-
?
factor IX + H2O
activated factor IX + ?
factor IX + H2O
factor IXa + ?
factor IX + H2O
factor IXa + peptide
factor IX 10-mer + H2O
?
-
-
-
-
?
factor IX mutant G317E + H2O
?
-
-
-
-
?
factor IX mutant G317R + H2O
?
-
-
-
-
?
factor V + H2O
activated factor V + ?
-
fXIa cleaves COOH-terminal to R306, possibly at the fXa/plasmin cleavage site R348
-
-
?
factor VIII + H2O
activated factor VIII + ?
-
fXIa initially cleaves at R740 and R372 in the heavy chain and also makes several A3 cleavages most notably at R1652 and R1721
-
-
?
factor XI + H2O
activated factor XI + ?
-
-
-
?
Fibrinogen + H2O
?
-
Aalpha-chain and Bbeta-chain, gamma-chain after prolonged incubation
-
-
?
Gly-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-Gly-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Glu-L-Glu-L-Pro-L-Arg-4-nitroanilide + H2O
L-Glu-L-Glu-L-Pro-L-Arg + 4-nitroaniline
-
S-2366
-
-
?
L-pyro-Glu-Pro-Arg-4-nitroanilide + H2O
L-pyro-Glu-Pro-Arg + 4-nitroaniline
i.e. S-2366
-
-
?
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroGlu-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroglutamyl-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-7-amido-4-methylcoumarin + H2O
L-pyroglutamyl-L-prolyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
?
-
substrate S-299
-
-
?
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine + p-nitroaniline
-
-
-
-
?
N-benzoyl-L-arginine-p-nitroanilide + H2O
N-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-Cbz-D-arginylglycyl-L-arginyl-4-nitroanilide + H2O
N-Cbz-D-arginylglycyl-L-arginine + 4-nitroaniline
-
-
-
-
?
pefachrome Xa + H2O
?
-
-
-
?
platelet glycoprotein 1balpha + H2O
?
binding to the A3 domain of FXI
-
-
?
prochemerin + H2O
chemerin + ?
-
-
-
-
?
prochemerin chem163S + H2O
chemerin chem162R + chermerin chem158K
-
prochemerin is activated by a series of C-terminal proteolytic cleavages resulting in diverse chemerin forms with different levels of activity
-
-
?
proteinase-activated receptor 1E + H2O
?
-
-
-
-
?
pyroGlu-Pro-Arg-4-nitroanilide + H2O
?
pyroGlu-Pro-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
pyroglutamoyl-prolyl-arginyl-4-methylcoumarin 7-amide + H2O
?
-
-
-
?
S2366 + H2O
L-pyroGlu-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
SN-13a + H2O
?
-
specific substrate for factor XIa
-
-
?
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tissue factor pathway inhibitor + H2O
?
-
the cleavage of the protein occurs between the Kunitz (K)1 and K2 domains (Lys86/Thr87) and at the active sites of the K2 (Arg107/Gly108) and K3 (Arg199/Ala200) domains
-
-
?
Z-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
factor IX + H2O
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
?
factor IX + H2O
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
?
factor IX + H2O
activated factor IX + ?
-
-
683239, 684078, 717416, 717844, 718042, 718045, 752615, 752757, 752995, 753069, 754510, 754516, 755585 -
-
?
factor IX + H2O
activated factor IX + ?
-
-
-
?
factor IX + H2O
activated factor IX + ?
-
model for factor IX activation in which FXIa binds to activated platelets by one chain of the dimer, while binding to factor IX through the other
-
?
factor IX + H2O
activated factor IX + ?
factor XIa has a role in the intrinsic pathway of coagulation, and plays a significant role in venous thrombosis
-
-
?
factor IX + H2O
activated factor IX + ?
-
factor XIa is essential for the optimal activation of FIX
-
-
?
factor IX + H2O
activated factor IX + ?
-
two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX
-
-
?
factor IX + H2O
activated factor IX + ?
cleavage at Ala145 and Ala180
-
-
?
factor IX + H2O
activated factor IX + ?
-
cleavage at Ala145 and Ala180, activity of wild-type and mutant enzymes with wild-type and mutant substrate, overview
-
-
?
factor IX + H2O
activated factor IX + ?
-
cleavage of Arg145-Ala146, and Arg180-Val181, macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa mediate the formation of the Michaelis complex required for factor IX-activation, mechanisms of activation, overview
-
-
?
factor IX + H2O
activated factor IX + ?
natural cleavage sites on FIX performed by FXIa, overview
-
-
?
factor IX + H2O
activated factor IX + ?
FXI is converted to the active protease by cleavage of the Arg369-Ile370 bond on each subunit. This converts the catalytic domains to the active forms, and unmasks exosites on the apple domains required for FIX binding
-
-
?
factor IX + H2O
activated factor IX + ?
-
-
-
-
?
factor IX + H2O
activated factor IX + ?
-
-
-
-
?
factor IX + H2O
factor IXa + ?
-
-
-
-
?
factor IX + H2O
factor IXa + ?
-
-
-
?
factor IX + H2O
factor IXa + ?
-
FIX
-
-
?
factor IX + H2O
factor IXa + ?
-
after binding to factor XIa, factor IX undergoes a single cleavage to form the intermediate factor IXalpha. FIXalpha then rebinds to the A3 domain to undergo a second cleavage, generating factor IXalphabeta
-
-
?
factor IX + H2O
factor IXa + peptide
-
-
-
-
?
factor IX + H2O
factor IXa + peptide
-
-
containing 50% carbohydrate
?
factor IX + H2O
factor IXa + peptide
-
-
-
-
?
factor IX + H2O
factor IXa + peptide
-
-
-
?
kininogen + H2O
?
-
-
-
-
?
kininogen + H2O
?
-
-
-
?
kininogen + H2O
?
binding to the A2 domain of FXI
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
?
pro-HGF + H2O
?
-
HGF i. e. hepatocyte growth factor, pro-HGF is processed by cleavage at two sites: Arg494-Val 495 and Arg424-His425. Cleavage at Arg424-His425 is independent of a prior cleavage at the primary kinetically preferred Arg 494-Val495 site. The mutant substrate pro-HGF(R424A/R494E) is completely resistant to cleavage
-
?
pro-HGF + H2O
?
-
the enzyme may regulate processes that involve the HGF/c-Met pathway, such as tissue repair and angiogenesis
-
?
pyroGlu-Pro-Arg-4-nitroanilide + H2O
?
-
substrate S-2366
-
-
?
pyroGlu-Pro-Arg-4-nitroanilide + H2O
?
substrate S-2366
-
-
?
S-2366 + H2O
?
-
commercial chromogenic substrate
-
-
?
S-2366 + H2O
?
commercial chromogenic substrate
-
-
?
S-2366 + H2O
?
-
i.e. L-pyroglutamyl-L-prolyl-L-arginine-4-nitroanilide
-
-
?
additional information
?
-
-
not: fibrin
-
-
?
additional information
?
-
-
specific and saturable zinc-dependent FXIa binding is demonstrated to 250 sites per activated platelet and 6.5 sites per umbilical vein endothelial cell. No binding to HEK293 cells is detected
-
?
additional information
?
-
a conformational transition accompanies conversion of factor XI to factor XIa that conceals the Apple 3 domain zymogen factor XI platelet binding site and exposes the factor XIa platelet binding site within the catalytic domain possibly comprising residues Cys527-Cys542
-
-
?
additional information
?
-
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, overview
-
-
?
additional information
?
-
FXI contains 4 apple domains that form a disk structure with extensive interfaces at the base of the catalytic domain. Binding of FXI to platelets requires residues in the FXI A3 domain. Platelets bind and spread on glass coated with FXI
-
-
?
additional information
?
-
FXI is a homodimer, with each subunit containing four apple domains and a protease domain: the apple domains form a disk structure with binding sites for platelets
-
-
?
additional information
?
-
-
platelets bind and spread on glass coated with FXI. Platelets from ApoER2-deficient mice do not bind FXI
-
-
?
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(2,4-dibromo-3-[[(4-carbamimidamidobutyl)carbamoyl]oxy]-6-hydroxyphenyl)acetic acid
-
(2,4-dibromo-6-[[(4-carbamimidamidobutyl)carbamoyl]oxy]-3-hydroxyphenyl)acetic acid
-
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
-
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
-
(2S)-2-([[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]amino)-N-[(2S)-1-[[(2S)-5-carbamimidamido-1-oxo-1-(1,3-thiazol-2-yl)pentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]-2-(4-hydroxyphenyl)ethanamide
-
(2S)-2-([[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]amino)-N-[(2S)-1-[[(2S)-5-carbamimidamido-1-oxo-1-(1,3-thiazol-2-yl)pentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]-2-(pyridin-3-yl)ethanamide
-
(3R)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
-
(3R)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
-
(3S)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
-
(3S)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
-
(4S,7S)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,12,13,14,15-dodecahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
-
-
(4S,7S,10S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-10-phenyl-4,5,7,8,10,11,14,15-octahydro-1H-[1,4,7]triazacyclohexadecino[10,9-b]indole-3,6,9(2H)-trione
-
-
(4S,7S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,14,15-decahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
-
-
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
-
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5,6,7,8-tetrahydroisoquinoline-6-carboxamide
-
-
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]isoquinoline-6-carboxamide
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2,6-difluorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2-fluorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chlorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-fluorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methoxybenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methylbenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[2-(aminomethyl)-5-chlorobenzyl]urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(trifluoromethyl)benzyl]urea
-
-
1-[2-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl]guanidine
-
-
1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)benzyl]guanidine
-
-
1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]guanidine
-
-
2'-[(6-carbamimidoyl-1-ethyl-1H-indol-3-yl)methyl]-4-methyl-5'-[[(5-methylpyrazin-2-yl)methyl]carbamoyl]biphenyl-2-carboxylic acid
-
2,4-dibromo-3-([(4-carbamimidamidobutyl) carbamoyl]oxy)-6-hydroxyphenyl acetic acid
clavatadine A
2-(2-amino-2-oxoethyl)-3,5-dibromo-4-hydroxyphenyl (4-carbamimidamidobutyl)carbamate
clavatadine B
2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
-
2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
-
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-L-arginyl-L-valyl-L-arginyl)-1,3-thiazole
-
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N5-carbamoyl-L-ornithyl-L-valyl-L-arginyl)-1,3-thiazole
-
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
3'-[(2S,4R)-6-carbamimidoyl-4-methyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]-4-carbamoyl-5'-[(3-methylbutanoyl)amino]biphenyl-2-carboxylic acid
-
3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
-
3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl sulfate
-
-
3-alkoxy-4-chloro-7-guanidinoisocoumarin
-
-
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1,2-benzoxazole-6-carboxamide
-
-
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1H-indazole-6-carboxamide
-
-
3-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino]benzoic acid
-
-
3-[[N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(pyridin-3-yl)-L-alanyl]amino]benzoic acid
-
-
3-[[N2-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(pyrazin-2-ylmethyl)-L-asparaginyl]amino]benzoic acid
-
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N,N-dimethylbenzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N-methylbenzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-bromo-1H-imidazol-4-yl)-benzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-chloro-1H-imidazol-4-yl)-benzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-fluoro-1H-imidazol-4-yl)-benzamide
-
4-(2-(S-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzoic acid
-
4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)aniline
-
-
4-amidinophenylmethanesulfonyl fluoride
-
-
4-chloro-3-isothiureidoalkoxyisocoumarin
-
-
4-[(N-[(2E)-3-[2-(aminomethyl)-5-chlorophenyl]prop-2-enoyl]-L-phenylalanyl)amino]benzoic acid
-
-
4-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino]benzoic acid
-
-
4-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-tryptophyl)amino]benzoic acid
-
-
4-[(N2-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-[2-(morpholin-4-yl)ethyl]-L-asparaginyl)amino]benzoic acid
-
-
4-[[(2S)-2-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-4-(methylsulfonyl)butanoyl]amino]benzoic acid
-
-
4-[[N-[(2E)-3-[3-chloro-2-fluoro-6-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(1-ethyl-5-methyl-1H-pyrazol-3-yl)-L-alanyl]amino]benzoic acid
-
-
4-[[N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(thiophen-2-yl)-L-alanyl]amino]benzoic acid
-
-
5-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino]thiophene-2-carboxylic acid
-
-
5-[[3-(ethoxycarbonyl)-5-hydroxy-6-methoxy-1-benzofuran-2-yl]methoxy]-6-methoxy-2-methyl-1-benzofuran-3-carboxylic acid
-
-
alpha1-protease inhibitor
-
-
amyloid beta-precursor protein Kunitz domain
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview
-
basic pancreatic trypsin inhibitor
competitive inhibition
-
basic pancreatic trypsin inhibitor mutant K15R
-
-
D-Phe-Pro-Arg-CH2Cl
-
irreversibly inhibits both active sites of the enzyme
decasodium 1,2,3,4,6-pentakis-O-[3,5-bis(sulfonatooxy)benzoyl]-beta-D-threo-hexopyranose
-
complete inhibition at 1 mg/ml
decasodium 1,2,3,4,6-pentakis-O-[4-hydroxy-3,5-bis(sulfonatooxy)benzoyl]-beta-D-threo-hexopyranose
-
complete inhibition at 0.2 mg/ml
dextran sulfate M 10000
-
51% saturable maximal inhibition at 37°C
-
dextran sulfate M 500000
-
86% saturable maximal inhibition at 37°
-
diisopropyl fluorophosphate
-
-
diisopropylfluorphosphate
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview
disodium 3-([[3,5-dicyano-6-nitro-4-(4-phenoxyphenyl)pyridin-2-yl]sulfanyl]acetyl)benzene-1,2-diyl disulfate
-
-
disodium 4-[[3-(1,3-dioxo-5-[[4-(sulfonatooxy)phenyl]carbamoyl]-1,3-dihydro-2H-isoindol-2-yl)benzoyl]amino]phenyl sulfate
-
-
ethyl 2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
-
ethyl 2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
-
ethyl 7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-14-[(methoxycarbonyl)amino]-10-methyl-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecine-2-carboxylate
-
-
ethyl 7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-15-[(methoxycarbonyl)amino]-2,3,4,5,6,7-hexahydro-1H-8,12-(metheno)-1,9-benzodiazacyclotetradecine-2-carboxylate
-
-
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]leucinate
-
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]phenylalaninate
-
ethyl [(4E)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-14-[(methoxycarbonyl)amino]-1,6,7,9-tetrahydro-11,8-(azeno)-2,9-benzodiazacyclotridecin-2(3H)-yl]acetate
-
-
factor fIXai
-
factor IXai
-
fractionated heparin of 64 disaccharide units
-
70-80% saturable maximal inhibition at 37°C
-
hypersulfated heparin
-
54% saturable maximal inhibition at 37°C
-
methyl (4-[2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[2-[(benzyl[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)methyl]-5-chloro-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[5-chloro-2-[(1S)-1-([3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[5-chloro-2-[(1S)-1-([N-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[[N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(1-methyl-1H-pyrazol-3-yl)-L-alanyl]amino]phenyl)carbamate
-
-
methyl 2-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino][1,2,4]triazolo[1,5-a]pyridine-6-carboxylate
-
-
methyl 4-(2-((S)-1-(trans-4-(aminomethyl)-cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-benzoate
-
methyl 7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-14-[(methoxycarbonyl)amino]-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecine-2-carboxylate
-
-
methyl [(10S)-10-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,9,10,12-hexahydro-14,11-(azeno)-8,4-(metheno)-2,12-benzodiazacyclohexadecin-17-yl]carbamate
-
-
methyl [(10S)-13-chloro-10-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,9,10,12-hexahydro-14,11-(azeno)-8,4-(metheno)-2,12-benzodiazacyclohexadecin-17-yl]carbamate
-
-
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,3,4,10,11,13-hexahydro-2H-15,12-(azeno)-5,9-(metheno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
-
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,3,4,10,11,13-hexahydro-2H-5,9:15,12-di(azeno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
-
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-6-fluoro-2-oxo-1,3,4,10,11,13-hexahydro-2H-15,12-(azeno)-5,9-(metheno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
-
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-6-fluoro-2-oxo-1,3,4,10,11,13-hexahydro-2H-5,9:15,12-di(azeno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
-
methyl [(4E)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-10-methyl-2,3,6,7-tetrahydro-9H-11,8-(azeno)-1,9-benzoxazacyclotridecin-14-yl]carbamate
-
-
methyl [(4E)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-10-methyl-2-oxo-2,3,6,7-tetrahydro-1H-8,12-(metheno)-1,9,11-benzotriazacyclotetradecin-15-yl]carbamate
-
-
methyl [(4E)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2,2-dioxido-1,6,7,9-tetrahydro-3H-11,8-(azeno)-2,1,9-benzothiadiazacyclotridecin-14-yl]carbamate
-
-
methyl [(5S)-2-chloro-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-5,6,12,13,14,15-hexahydro-3H-1,4-(azeno)-7,11-(metheno)-3-benzazacycloheptadecin-17-yl]carbamate
-
-
methyl [(5S)-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-5,6,11,12,13,14-hexahydro-3H-1,4-(azeno)-7,10-etheno-3-benzazacyclohexadecin-16-yl]carbamate
-
-
methyl [(7E)-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3,5,6,9,10,11-hexahydro-1,4-(azeno)-3-benzazacyclotridecin-13-yl]carbamate
-
-
methyl [(9S)-12-chloro-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
-
methyl [(9S)-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
-
methyl [1-(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)-1,2,3,4-tetrahydroquinolin-6-yl]carbamate
-
-
methyl [10-chloro-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-(trifluoromethyl)-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [2-(4-chloro-1-methyl-1H-pyrazol-3-yl)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-10-methyl-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-(3-methyloxetan-3-yl)-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3,3-difluoro-4-oxo-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,5,9-benzotriazacyclotridecin-14-yl]carbamate
-
-
N-(3-amino-1H-indol-6-yl)-Nalpha-([[5-chloro-2-(1H-tetrazol-1-yl)phenyl]sulfinyl]acetyl)-L-phenylalaninamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1-(3-aminopropyl)cyclohexanecarboxamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2,6-difluoro-4-methoxybenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methoxybenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methylbenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)-2-fluorobenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)benzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylbenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5-chloro-2-fluorobenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-pyrazol-1-yl)phenyl]glycinamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycinamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(4H-1,2,4-triazol-4-yl)phenyl]glycinamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]benzene-1,4-dicarboxamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2,2-dimethylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(2,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(4-chlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorophenyl)sulfonyl]amino]methyl)-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(4-fluorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylacetyl)amino]methyl]-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylcarbonyl)amino]methyl]-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(phenylcarbamoyl)amino]methyl]-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]propyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-2-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]amino]-1-cyclohexyl-2-oxoethyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-carboxamide
-
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-3-oxo-3,4-dihydro-2H-1,4-benzothiazine-7-carboxamide
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-4-hydroxy-2-oxo-1,2,3,4-tetrahydroquinoline-6-carboxamide
-
-
N-[(3,4-dichlorobenzyl)carbamoyl]-L-leucyl-N-[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]-L-phenylalaninamide
-
N-[2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]-Na-(imidazo[1,2-a]pyrimidin-2-ylcarbonyl)-L-phenylalaninamide
-
-
N-[2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]-Nalpha-(1H-indazol-3-ylcarbonyl)-L-phenylalaninamide
-
-
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-(pent-4-enoylamino)acetyl]-L-leucinamide
-
-
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-[[(2S)-2-phenylpent-4-enoyl]amino]acetyl]-L-leucinamide
-
-
N2-(benzylcarbamoyl)-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
N2-acetyl-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N1-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-aspartamide
-
N2-[[1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
Na-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-fluoro-N-[4-(1H-tetrazol-5-yl)phenyl]-L-phenylalaninamide
-
-
Na-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-[4-(1H-tetrazol-5-yl)phenyl]-L-phenylalaninamide
-
-
Na-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N2-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tyrosinamide
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(1,2,3,4-tetrahydroisoquinolin-6-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(1-oxo-2,3-dihydro-1H-isoindol-5-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(2-oxoazepan-3-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(6-fluoro-1,3-benzothiazol-2-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-[4-[(methoxycarbonyl)amino]cyclohexyl]-L-phenylalaninamide
-
-
Nalpha-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tryptophanamide
-
nexin-2
-
heparin potentiates the inhibition
-
protease nexin-2
highly specific and potent inhibitor of FXIa, is about 775fold more potent than basic pancreatic trypsin inhibitor in FXIa inhibition, provides single-step slow equilibration inhibition
-
protease nexin-2 mutant F34A
-
-
protease nexin-2 mutant M17A
-
-
protease nexin-2 mutant P13A
-
-
protease nexin-2 mutant R15K
-
-
protease nexin-2 mutant R20A
-
-
protease nexin-2 mutant S19A
-
-
protein Z dependent protease inhibitor
-
-
S-2366
-
noncompetitive inhibition versus factor IX
serpins
inhibition of autolysis of fXIa
-
sodium 2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-3-(methoxycarbonyl)-1-benzofuran-5-yl sulfate
-
-
sodium 2-[[(3-carboxy-6-methoxy-2-methyl-1-benzofuran-5-yl)oxy]methyl]-3-(ethoxycarbonyl)-6-methoxy-1-benzofuran-5-yl sulfate
-
-
sodium 3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-(propan-2-yloxy)-1-benzofuran-5-yl sulfate
-
-
sodium 3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl sulfate
-
-
sodium 3-(ethoxycarbonyl)-6-methoxy-2-[([6-methoxy-2-methyl-3-[(prop-2-en-1-yloxy)carbonyl]-1-benzofuran-5-yl]oxy)methyl]-1-benzofuran-5-yl sulfate
-
-
sodium 6-ethoxy-3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-1-benzofuran-5-yl sulfate
-
most potent inhibitor
sodium 6-methoxy-3-(methoxycarbonyl)-2-([[6-methoxy-3-(methoxycarbonyl)-2-methyl-1-benzofuran-5-yl]oxy]methyl)-1-benzofuran-5-yl sulfate
-
-
sulfated pentagalloyl beta-D-glucopyranoside
-
-
trans-4-(aminomethyl)-N-((S)-1-(4-(3-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-1-(4-(4-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-1-(5-oxo-1-phenyl-4,5-dihydro-1H-1,2,4-triazol-3-yl)-2-phenylethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(2-phenyl-1H-imidazol-4-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-1,2,4-triazol-5-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-pyrazol-5-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-(4-sulfamoylphenyl)-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(5-phenyloxazol-2-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-[1-(1-methyl-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-oxido-2-phenylpyridin-4-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-oxido-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-oxido-5-phenylpyridin-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(5-chloro-4-phenyl-1H-imidazol-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(5-fluoro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-amino-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-chloro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-hydroxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-methoxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(biphenyl-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-[6-(methylamino)-4-phenylpyridin-2-yl]-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(2-phenylpyridin-4-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyrimidin-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(5-phenylpyridin-3-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyrimidin-4-yl)ethyl]cyclohexanecarboxamide
-
-
trans-N-((S)-1-(4-(3-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
reversible enzyme inhibition
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-fluoro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
trans-N-((S)-1-(4-(4-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylcyclohexanecarboxamide
-
-
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]cyclohexane-1,4-dicarboxamide
-
-
trans-N-[1-[3-(3-amino-1H-indazol-6-yl)phenyl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)-6-oxo-1,6-dihydropyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)pyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[1-[5-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
[4-(carbamimidamidomethyl)phenyl]boronic acid
-
-
[4-[(N-[3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]-L-phenylalanyl)amino]phenyl]acetic acid
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
-
-
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
-
4-aminobenzamidine
-
a reversible serine protease inhibitor, competitive versus substrate S-2366, noncompetitive versus substrate factor IX, inhibition of wild-type enzyme and recombinant peptide FXI/E361-V607
4-aminobenzamidine
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview
antithrombin
-
-
antithrombin
in presence of heaprin
-
benzamidine
-
weak inhibitor of FXIa
C1-inhibitor
-
-
ecotin
-
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-3-oxo-3,4-dihydro-2H-1,4-benzothiazine-7-carboxamide
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-3-oxo-3,4-dihydro-2H-1,4-benzothiazine-7-carboxamide
-
-
protease nexin 2
-
the major interactions required for factor XIa inhibition are localized to the catalytic domain of factor XIa and the Kunitz domain of protease nexin II
-
protease nexin 2
-
activated platelet surface has littlke or no direct effect on the rate of factor IX activation by factor Xia and the reaction proceeds at uninhibited rates when protease nexin 2 is present. Factor Xia-catalyzed FIX activation is completely inhibited by protease nexin 2 in solution or in the presence of umbilical vein endothelial cells
-
[4-[(N-[3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]-L-phenylalanyl)amino]phenyl]acetic acid
-
[4-[(N-[3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]-L-phenylalanyl)amino]phenyl]acetic acid
-
-
additional information
-
-
-
additional information
-
inhibition by recombinant Kunitz domain
-
additional information
the recombinant catalytic domain Ile370-Val607 of FXIa inhibits the binding of factor XIa to the platelets with a Ki of 3.5 nM, whereas the recombinant factor XI heavy chain does not
-
additional information
inhibitor design and synthesis, overview, inhibitor in vitro anticoagulant activity in human plasma
-
additional information
-
inhibitor design and synthesis, overview, inhibitor in vitro anticoagulant activity in human plasma
-
additional information
heparin accelerates inhibition of factor XIa. Heparin enhances antithrombin inhibition of catalytic domain-wild-type 212fold, but only 37-94fold for catalytic domain mutants
-
additional information
Arg184 may be part of a switch that holds FXI in an inactive conformation in the zymogen
-
additional information
not inhibited by protease nexin-2 mutant R15A
-
additional information
-
not inhibited by unfractionated heparin, enoxaparin, fondaparinux, sucrose octasulfate, chondroitin sulfate A, dermatan sulfate, and chondroitin sulfate C
-
additional information
-
potent activated factor VII inhibition with insect-derived serine protease inhibitor, but this protein is only 10fold selective over activated factor X. Inhibition by FXI neutralizing antibodies, which allow preexisting activated factor XI to remain active
-
additional information
-
a monoclonal antibody against FXI or activated factor XI reduces thrombus formation in balloon-injured iliac arteries
-
additional information
-
ketoarginine-based peptidomimetics are irreversible inhibitors of actived factor XI and form a covalent bond to the catalytic serine of the enzyme. Intravenous infusion is efficacious in a rat model of venous thrombosis. A pyridyl analog in a rat mesenteric bleeding model at a 4fold efficacious dose does not alter bleeding time
-
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0.09
benzyloxycarbonyl-Gly-Pro-4-nitroanilide
-
-
0.34
D-Ile-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
0.00012 - 0.151
factor IX
-
0.3
factor IX 10-mer
-
at pH 7.4 and 37°C
-
0.00038
factor IX mutant G317E
-
at 25°C, pH not specified in the publication
-
0.00035
factor IX mutant G317R
-
at 25°C, pH not specified in the publication
-
0.205 - 0.852
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
0.45 - 0.59
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
0.552 - 0.993
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
0.4 - 352
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide
0.000103
prochemerin chem163S
-
at pH 7.4 and 37°C
-
0.26 - 0.4
pyroGlu-Pro-Arg-4-nitroanilide
0.56
pyroGlu-Pro-Arg-p-nitroanilide
-
-
additional information
additional information
-
0.00012
factor IX
-
FXIa/PKA4, 37°C
-
0.00016
factor IX
-
FXIa/PKA4-Gly326, 37°C
-
0.0002
factor IX
-
factor FXIa, 37°C
-
0.0002 - 0.00021
factor IX
-
37°C, recombinant wild-type enzyme
-
0.00025
factor IX
-
at 25°C, pH not specified in the publication
-
0.0003
factor IX
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.00039 - 0.00047
factor IX
-
37°C, recombinant peptide FXI/E361-V607
-
0.053
factor IX
-
pH 7.4, 37°C, recombinant wild-type enzyme
-
0.151
factor IX
-
at 22°C
-
0.205
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.268
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.292
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.315
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.336
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.339
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.383
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.4
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.525
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.538
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.603
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.828
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.852
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.45
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
-
FXIa/PKA4
0.5
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
-
factor FXIa
0.59
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
-
FXIa/PKA4-Gly326
0.552
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K170A/R171A/R173A mutant
0.655
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K170A mutant
0.757
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-wild type
0.764
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K179A mutant
0.81
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-R173A mutant
0.812
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-R171A mutant
0.829
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K175A mutant
0.943
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-wild type
0.993
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-R37Q mutant
0.4
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide
-
-
233
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide
-
FXIa
352
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide
-
fXIaCD
0.26
pyroGlu-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
0.4
pyroGlu-Pro-Arg-4-nitroanilide
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.225
S-2366
-
37°C, recombinant wild-type enzyme
0.357
S-2366
-
37°C, recombinant peptide FXI/E361-V607
0.384
S-2366
-
mutant FXIa/G326C
additional information
additional information
kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of isolated subunits with each one active site, stoichiometry of FIX and FIXalphabeta binding to FXIa, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
110.2
D-Ile-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
0.00065 - 5.8
factor IX
-
0.083
factor IX 10-mer
-
at pH 7.4 and 37°C
-
8
Factor XI
-
pH 7.3, 37°C
-
5.8 - 201
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
250 - 430
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
98 - 148
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
67 - 117
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide
0.91
prochemerin chem163S
-
at pH 7.4 and 37°C
-
0.268 - 145
pyroGlu-Pro-Arg-4-nitroanilide
350
pyroGlu-Pro-Arg-p-nitroanilide
-
-
0.00065
factor IX
-
37°C, recombinant peptide FXI/E361-V607
-
0.2
factor IX
-
in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.334
factor IX
-
37°C, recombinant wild-type enzyme
-
0.55
factor IX
-
pH 7.4, 37°C, recombinant wild-type enzyme
-
0.66
factor IX
-
at 22°C
-
0.73
factor IX
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
3.4
factor IX
-
FXIa/PKA4, 37°C
-
5.7
factor IX
-
FXIa/PKA4-Gly326, 37°C
-
5.8
factor IX
-
factor FXIa, 37°C
-
5.8
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
7
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
8
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
14
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
21
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
29
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
30
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
42
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
58
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
86
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
95
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
95
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
201
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
250
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
-
FXIa/PKA4
310
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
-
factor FXIa
430
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
-
FXIa/PKA4-Gly326
98
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K170A mutant
115
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K170A/R171A/R173A mutant
115
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-R171A mutant
116
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K179A mutant
117
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K175A mutant
117
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-R173A mutant
119
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-wild type
148
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-R37Q mutant
148
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-wild type
67
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide
-
fXIaCD
117
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide
-
fXIa
0.268
pyroGlu-Pro-Arg-4-nitroanilide
-
pH 7.4, 37°C, recombinant wild-type enzyme
145
pyroGlu-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
113
S-2366
-
37°C, recombinant wild-type enzyme
121
S-2366
-
37°C, recombinant peptide FXI/E361-V607
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0.000005
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
at 25°C, pH not specified in the publication
0.0000012
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
at 25°C, pH not specified in the publication
0.00000215
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5,6,7,8-tetrahydroisoquinoline-6-carboxamide
-
at 25°C, pH not specified in the publication
0.000019
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]isoquinoline-6-carboxamide
-
at 25°C, pH not specified in the publication
0.000023
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2,6-difluorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000057
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2-fluorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000054
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chlorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000031
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-fluorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000075
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methoxybenzyl)urea
-
at 25°C, pH not specified in the publication
0.000053
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methylbenzyl)urea
-
at 25°C, pH not specified in the publication
0.0000058
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[2-(aminomethyl)-5-chlorobenzyl]urea
-
at 25°C, pH not specified in the publication
0.00024
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(trifluoromethyl)benzyl]urea
-
at 25°C, pH not specified in the publication
0.000275
2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
at pH 7.4 and 37°C
0.00015
2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
at pH 7.4 and 37°C
0.0000002
3'-[(2S,4R)-6-carbamimidoyl-4-methyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]-4-carbamoyl-5'-[(3-methylbutanoyl)amino]biphenyl-2-carboxylic acid
at pH 7.4 and 37°C
0.0011
3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
at pH 7.4 and 37°C
0.000125
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1,2-benzoxazole-6-carboxamide
-
at 25°C, pH not specified in the publication
0.000058
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1H-indazole-6-carboxamide
-
at 25°C, pH not specified in the publication
0.00286
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N,N-dimethylbenzamide
at pH 7.4 and 37°C
0.00035
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N-methylbenzamide
at pH 7.4 and 37°C
0.00003
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
at pH 7.4 and 37°C
0.000009
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-bromo-1H-imidazol-4-yl)-benzamide
at pH 7.4 and 37°C
0.000004
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-chloro-1H-imidazol-4-yl)-benzamide
at pH 7.4 and 37°C
0.00003
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-fluoro-1H-imidazol-4-yl)-benzamide
at pH 7.4 and 37°C
0.00059
4-(2-(S-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzoic acid
at pH 7.4 and 37°C
0.0000211 - 0.095
4-aminobenzamidine
0.000627
basic pancreatic trypsin inhibitor
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.0000041
basic pancreatic trypsin inhibitor mutant K15R
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00063
ethyl 2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
at pH 7.4 and 37°C
0.000495
ethyl 2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
at pH 7.4 and 37°C
0.0000067
methyl (4-[2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0000027 - 0.0000058
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
0.0000019
methyl (4-[5-chloro-2-[(1S)-1-([3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0000034
methyl (4-[5-chloro-2-[(1S)-1-([N-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0008
methyl 4-(2-((S)-1-(trans-4-(aminomethyl)-cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-benzoate
at pH 7.4 and 37°C
0.0005
methyl [(10S)-10-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,9,10,12-hexahydro-14,11-(azeno)-8,4-(metheno)-2,12-benzodiazacyclohexadecin-17-yl]carbamate
-
at 25°C, pH not specified in the publication
0.000092
methyl [(10S)-13-chloro-10-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,9,10,12-hexahydro-14,11-(azeno)-8,4-(metheno)-2,12-benzodiazacyclohexadecin-17-yl]carbamate
-
at 25°C, pH not specified in the publication
0.0000015
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,3,4,10,11,13-hexahydro-2H-15,12-(azeno)-5,9-(metheno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
at 37°C, pH not specified in the publication
0.00000032
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,3,4,10,11,13-hexahydro-2H-5,9:15,12-di(azeno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
at 37°C, pH not specified in the publication
0.00000053
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-6-fluoro-2-oxo-1,3,4,10,11,13-hexahydro-2H-15,12-(azeno)-5,9-(metheno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
at 37°C, pH not specified in the publication
0.00000002
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-6-fluoro-2-oxo-1,3,4,10,11,13-hexahydro-2H-5,9:15,12-di(azeno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
at 37°C, pH not specified in the publication
0.0000082
methyl [(5S)-2-chloro-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-5,6,12,13,14,15-hexahydro-3H-1,4-(azeno)-7,11-(metheno)-3-benzazacycloheptadecin-17-yl]carbamate
-
at 25°C, pH not specified in the publication
0.000071
methyl [(5S)-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-5,6,11,12,13,14-hexahydro-3H-1,4-(azeno)-7,10-etheno-3-benzazacyclohexadecin-16-yl]carbamate
-
at 25°C, pH not specified in the publication
0.000017 - 0.0081
methyl [(9S)-12-chloro-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
0.0064
methyl [(9S)-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
at 25°C, pH not specified in the publication
0.00000149
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1-(3-aminopropyl)cyclohexanecarboxamide
-
at 25°C, pH not specified in the publication
0.000065
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2,6-difluoro-4-methoxybenzamide
-
at 25°C, pH not specified in the publication
0.00028
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methoxybenzamide
-
at 25°C, pH not specified in the publication
0.0002
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methylbenzamide
-
at 25°C, pH not specified in the publication
0.00000103
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)-2-fluorobenzamide
-
at 25°C, pH not specified in the publication
0.00000116
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)benzamide
-
at 25°C, pH not specified in the publication
0.00039
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylbenzamide
-
at 25°C, pH not specified in the publication
0.00053
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5-chloro-2-fluorobenzamide
-
at 25°C, pH not specified in the publication
0.00045
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-pyrazol-1-yl)phenyl]glycinamide
-
at 25°C, pH not specified in the publication
0.0000015
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycinamide
-
at 25°C, pH not specified in the publication
0.000046
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(4H-1,2,4-triazol-4-yl)phenyl]glycinamide
-
at 25°C, pH not specified in the publication
0.00031
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]benzene-1,4-dicarboxamide
-
at 25°C, pH not specified in the publication
0.000001 - 0.0000047
protease nexin 2
-
0.00000081
protease nexin-2
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000492
protease nexin-2 mutant F34A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000081
protease nexin-2 mutant M17A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000296
protease nexin-2 mutant P13A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.0000113
protease nexin-2 mutant R15K
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000283
protease nexin-2 mutant R20A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000093
protease nexin-2 mutant S19A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00112
trans-4-(aminomethyl)-N-((S)-1-(4-(3-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00023
trans-4-(aminomethyl)-N-((S)-1-(4-(4-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.003074
trans-4-(aminomethyl)-N-((S)-1-(5-oxo-1-phenyl-4,5-dihydro-1H-1,2,4-triazol-3-yl)-2-phenylethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00164
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(2-phenyl-1H-imidazol-4-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00098
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-1,2,4-triazol-5-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00694
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-pyrazol-5-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00134
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-(4-sulfamoylphenyl)-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00012
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00144
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(5-phenyloxazol-2-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.000479
trans-4-(aminomethyl)-N-[1-(1-methyl-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00253
trans-4-(aminomethyl)-N-[1-(1-oxido-2-phenylpyridin-4-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00169
trans-4-(aminomethyl)-N-[1-(1-oxido-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.001063
trans-4-(aminomethyl)-N-[1-(1-oxido-5-phenylpyridin-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000012
trans-4-(aminomethyl)-N-[1-(5-chloro-4-phenyl-1H-imidazol-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00032
trans-4-(aminomethyl)-N-[1-(5-fluoro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000227
trans-4-(aminomethyl)-N-[1-(6-amino-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000206
trans-4-(aminomethyl)-N-[1-(6-chloro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000113
trans-4-(aminomethyl)-N-[1-(6-hydroxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000949
trans-4-(aminomethyl)-N-[1-(6-methoxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000936
trans-4-(aminomethyl)-N-[1-(biphenyl-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00086
trans-4-(aminomethyl)-N-[1-[6-(methylamino)-4-phenylpyridin-2-yl]-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000433
trans-4-(aminomethyl)-N-[2-phenyl-1-(2-phenylpyridin-4-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00012
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000377
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.01142
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyrimidin-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00033
trans-4-(aminomethyl)-N-[2-phenyl-1-(5-phenylpyridin-3-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.03021
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000331
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyrimidin-4-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000545
trans-N-((S)-1-(4-(3-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.000003
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.000003
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.0000003
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-fluoro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.0004
trans-N-((S)-1-(4-(4-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00000031
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
0.000068
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylcyclohexanecarboxamide
-
at 25°C, pH not specified in the publication
0.0029
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]cyclohexane-1,4-dicarboxamide
-
at 25°C, pH not specified in the publication
0.000021
trans-N-[1-[3-(3-amino-1H-indazol-6-yl)phenyl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.0000037
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)-6-oxo-1,6-dihydropyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000013
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)pyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.0000032
trans-N-[1-[5-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
additional information
additional information
-
0.0000211
4-aminobenzamidine
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000245
4-aminobenzamidine
-
mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000362
4-aminobenzamidine
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000396
4-aminobenzamidine
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000416
4-aminobenzamidine
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000419
4-aminobenzamidine
-
mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000497
4-aminobenzamidine
-
mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000513
4-aminobenzamidine
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000714
4-aminobenzamidine
-
mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000739
4-aminobenzamidine
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.000079
4-aminobenzamidine
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0001529
4-aminobenzamidine
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.06
4-aminobenzamidine
-
37°C, recombinant wild-type enzyme, versus substrate S-2366
0.085
4-aminobenzamidine
-
37°C, recombinant peptide FXI/E361-V607, versus substrate S-2366
0.086
4-aminobenzamidine
-
37°C, recombinant peptide FXI/E361-V607, versus substrate factor IX
0.095
4-aminobenzamidine
-
37°C, recombinant wild-type enzyme, versus substrate factor IX
0.52
Aprotinin
-
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, free FXIa
0.96
Aprotinin
-
FIX substrate, free FXIa
10.42
Aprotinin
-
FIX substrate, FXIa-FIX complex
1.43
leupeptin
-
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, free FXIa
2.91
leupeptin
-
FIX substrate, free FXIa
19.12
leupeptin
-
FIX substrate, FXIa-FIX complex
209
leupeptin
-
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, FXIa-FIX complex
0.0000027
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0000058
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 37°C, pH not specified in the publication
0.000017
methyl [(9S)-12-chloro-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
at 25°C, pH not specified in the publication
0.0081
methyl [(9S)-12-chloro-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
at 25°C, pH not specified in the publication
0.000001
protease nexin 2
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000011
protease nexin 2
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000013
protease nexin 2
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000013
protease nexin 2
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000014
protease nexin 2
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000015
protease nexin 2
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000015
protease nexin 2
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000047
protease nexin 2
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.42
S-2366
-
37°C, recombinant peptide FXI/E361-V607, versus substrate factor IX
0.425
S-2366
-
37°C, recombinant wild-type enzyme, versus substrate factor IX
0.00000031
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00000031
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
at 25°C, pH not specified in the publication
additional information
additional information
-
-
-
additional information
additional information
competition for platelet binding by the wild-type enzyme and mutants, overview
-
additional information
additional information
second-order inhibition rate constants, wild-type and mutant enzymes with different inhibitors, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000132
(3R)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
Homo sapiens
pH 7.4, 37°C
0.000533
(3R)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
Homo sapiens
pH 7.4, 37°C
0.00001
(3S)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
Homo sapiens
pH 7.4, 37°C
0.000028
(3S)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
Homo sapiens
pH 7.4, 37°C
0.1759
(4S,7S)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,12,13,14,15-dodecahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.1358
(4S,7S,10S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-10-phenyl-4,5,7,8,10,11,14,15-octahydro-1H-[1,4,7]triazacyclohexadecino[10,9-b]indole-3,6,9(2H)-trione
Homo sapiens
-
pH and temperature not specified in the publication
0.7678
(4S,7S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,14,15-decahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.000076 - 0.0002
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
0.0073
1-[2-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl]guanidine
Homo sapiens
-
-
0.0257
1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)benzyl]guanidine
Homo sapiens
-
-
0.0059
1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]guanidine
Homo sapiens
-
-
0.000007
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-L-arginyl-L-valyl-L-arginyl)-1,3-thiazole
Homo sapiens
pH 7.4, 37°C
0.00003
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N5-carbamoyl-L-ornithyl-L-valyl-L-arginyl)-1,3-thiazole
Homo sapiens
pH 7.4, 37°C
0.0014
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
Homo sapiens
-
-
0.0773
benzamidine
Homo sapiens
-
-
0.0000028
BMS-262084
Homo sapiens
at pH 7.4 and 37°C
0.12
boronic acid
Homo sapiens
-
-
0.0013
clavatadine A
Homo sapiens
-
0.027
clavatadine B
Homo sapiens
-
0.0014
decasodium 1,2,3,4,6-pentakis-O-[3,5-bis(sulfonatooxy)benzoyl]-beta-D-threo-hexopyranose
Homo sapiens
-
at pH 7.4 and 37°C
0.0005
decasodium 1,2,3,4,6-pentakis-O-[4-hydroxy-3,5-bis(sulfonatooxy)benzoyl]-beta-D-threo-hexopyranose
Homo sapiens
-
at pH 7.4 and 37°C
0.000403
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]leucinate
Homo sapiens
pH 7.4, 37°C
0.000258
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]phenylalaninate
Homo sapiens
pH 7.4, 37°C
0.0092
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2,2-dimethylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000045
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(2,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000063
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000114
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(4-chlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000093
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.0026
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorophenyl)sulfonyl]amino]methyl)-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.00016
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(4-fluorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.0023
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylacetyl)amino]methyl]-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.0022
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylcarbonyl)amino]methyl]-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.00192
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(phenylcarbamoyl)amino]methyl]-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.00092
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]propyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.00034
N-[(1S)-2-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]amino]-1-cyclohexyl-2-oxoethyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.00071
N-[(3,4-dichlorobenzyl)carbamoyl]-L-leucyl-N-[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.1031
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-(pent-4-enoylamino)acetyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.1459
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-[[(2S)-2-phenylpent-4-enoyl]amino]acetyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000136
N2-(benzylcarbamoyl)-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.027
N2-acetyl-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000356
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000008
N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N1-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-aspartamide
Homo sapiens
pH 7.4, 37°C
0.00001
N2-[[1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000006
Na-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N2-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tyrosinamide
Homo sapiens
pH 7.4, 37°C
0.000029
Nalpha-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tryptophanamide
Homo sapiens
pH 7.4, 37°C
0.022
[4-(carbamimidamidomethyl)phenyl]boronic acid
Homo sapiens
-
-
0.000076
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
Homo sapiens
pH 7.4, 37°C
0.0002
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
Homo sapiens
pH 7.4, 37°C
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C321S
-
the mutant shows wild type activity
C398Y
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
C482S
-
the mutant shows 1.45fold enhanced activity as compared with the wild type enzyme
E98A
-
the mutant has normal Km and kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
E98D
-
the mutant has normal Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
E98V
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
FXI/G326C
-
mutant of FXI with Gly326 residue mutated to Cys326
G104R
this mutation in the PK A2 domain associated with CRM+ PK deficiency causes decreased kininogen binding
G155E
is a rare example of a mutation causing CRM+ FXI deficieny
G193A
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193D
site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 1.6-36fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193E
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193K
site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 35-478fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193R
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193V
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G400V
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
I151A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
K145A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K148A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K149A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K170A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
K170A/R171A/R173A
catalytic domain with residues 170, 171, and 173 changed to alanine is designated CD-KRR/A
K175A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
K179A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
K192A
-
the mutant has normal Km value for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with increased value of Ki
K192E
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
K192Q
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
K192R
-
the mutant has decreased Km and kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
M102T
-
site-directed mutagenesis,missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
M18I
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
P520L
-
site-directed mutagenesis, similar to the wild-ype enzyme
R144A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R144A/K145A/R147A/K148A/K149A
site-directed mutagenesis of an autolysis loop residues, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R144A/K145A/R147A/R149A
contains Ala substitutions for Arg-144, Lys-145, Arg-147, and Arg-149 (residues 504, 505, 507, and 509, respectively, in fXI numbering)
R147A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R171A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
R173A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
R3704A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
R378C
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is normally secreted from the transfected cell, but shows negligible factor IX activation activity
S225F
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
S248A
binds platelets with reduced affinity compared with wild-type
S248N
binds platelets with 5fold reduced affinity compared with wild-type, the A3 domain is probably not affected significantly, as FXI-Asn248 is secreted, activated by activated factor XII, and activates FIX similar to wild-type activated factor IX. Is associated with bleeding and defective FXI binding to platelets but does not affect the activated partial thromboplastin time assay, which does not contain platelets
S248Q
binds platelets with reduced affinity compared with wild-type
S434A/K437A/T475A/C482S
to improve crystallizability a quadrupole mutant is generated
S434A/T475A/C482S/K437A
site-directed mutagenesis, crystal structure determination with bound benzylamidine
T575M
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is normally secreted from the transfected cell, but shows negligible factor IX activation activity
W569S
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
Y133S
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
Y143A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
Y5901A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with increased value of Ki
Y5901V
-
the mutant has normal Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
C362S/C482S
-
site-directed mutagenesis
C362S/C482S
site-directed mutagenesis, the mutant shows increased platelet binding compared to the wild-type enzyme
additional information
-
FXIa/PKA4 is made by replacing the FXI A4 domain with the A4 domain from prekallikrein. A dimeric version of FXI/PKA4 (FXI/PKA4-Gly326) is prepared as a control. Activated FXIa/PKA4 and FXIa/PKA4-Gly326 activate factor IX with kinetic parameters similar to that of FXIa. FXI/PKA4 and FXIa/PKA4-Gly326 have coagulant activity similar to FXI. FXIa/PKA4, FXIa/PKA4-Gly326 and FXIa have similar affinities for activated platelets. The dimeric proteins FXI and FXI/PKA4-Gly326 promote coagulation similarly, however, monomeric FXIa/PKA4 has greatly reduced activity. The activated monomeric FXIa/PKA4 activates factor IX poorly in the presence of activated platelets
additional information
chimeric recombinant enzyme mutants rFXI-PKA3 and rFXIa-PKA3, with fusion of FXI to the Apple 3 domain of prekallikrein, show unaffected platelet binding compared to the wild-type enzyme, overview
additional information
-
construction of FXI with a single catalytic active site, construction of recombinant FXI with the A4 domain replaced by the A4 domain from plasma prekallikrein, i.e. FXI/PKA4, overview
additional information
factor XI deficiency caused by compound heterozygous F11 gene mutation
additional information
mutations in the fXIa 170 helix are introduced into a modified human fXI cDNA (fXI-Ser-362,482), which contains serine substitutions for Cys-362 and Cys-482
additional information
two different mutations, c.1546 G>A (Val498Met) and c.1560dupG (Tyr503ValfsX32) in the F11 gene
additional information
-
two different mutations, c.1546 G>A (Val498Met) and c.1560dupG (Tyr503ValfsX32) in the F11 gene
additional information
FXI with substitutions for Cys321 still form stable dimers. The Cys321-Cys321 interchain bond forms poorly in FXI with a single alanine substitution of Leu284, Ile290, or Tyr329
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Bovine factor XI (plasma thromboplastin antecedent)
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Role of calcium ions and the heavy chain of factor XIa in the activation of human coagulation factor IX
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Mechanism-based isocoumarin inhibitors for trypsin and blood coagulation serine proteases: new anticoagulants
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1988
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Purification and characterization of human brain prolyl endopeptidase
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Protease nexin II interactions with coagulation factor XIa are contained within the Kunitz protease inhibitor domain of protease nexin II and the factor XIa catalytic domain
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2000
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Model for a factor IX activation complex on blood platelets: dimeric conformation of factor XIa is essential
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Homo sapiens
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Mutation of surface residues to promote crystallization of activated factor XI as a complex with benzamidine: an essential step for the iterative structure-based design of factor XI inhibitors
Acta Crystallogr. Sect. D
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2005
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Substrate-dependent modulation of the mechanism of factor XIa inhibition
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Homo sapiens
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Allosteric modification of factor XIa functional activity upon binding to polyanions
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Sinha, D.; Marcinkiewicz, M.; Lear, J.D.; Walsh, P.N.
Factor XIa dimer in the activation of factor IX
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2005
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Structural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2
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280
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2005
Homo sapiens (P03951)
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Crystal structures of the FXIa catalytic domain in complex with ecotin mutants reveal substrate-like interactions
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Homo sapiens
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Shi, T.; Giannakopoulos, B.; Iverson, G.M.; Cockerill, K.A.; Linnik, M.D.; Krilis, S.A.
Domain V of beta2-glycoprotein I binds factor XI/XIa and is cleaved at Lys317-Thr318
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Rezaie, A.R.; Sun, M.F.; Gailani, D.
Contributions of basic amino acids in the autolysis loop of factor XIa to serpin specificity
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45
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2006
Homo sapiens (P03951)
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Miller, T.N.; Sinha, D.; Baird, T.R.; Walsh, P.N.
A catalytic domain exosite (Cys527-Cys542) in factor XIa mediates binding to a site on activated platelets
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46
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2007
Homo sapiens (P03951)
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Sinha, D.; Marcinkiewicz, M.; Navaneetham, D.; Walsh, P.N.
Macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa mediate the formation of the Michaelis complex required for factor IX-activation
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46
9830-9839
2007
Homo sapiens
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Schmidt, A.E.; Sun, M.F.; Ogawa, T.; Bajaj, S.P.; Gailani, D.
Functional role of residue 193 (chymotrypsin numbering) in serine proteases: influence of side chain length and beta-branching on the catalytic activity of blood coagulation factor XIa
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47
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2008
Homo sapiens (P03951)
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Lazarova, T.I.; Jin, L.; Rynkiewicz, M.; Gorga, J.C.; Bibbins, F.; Meyers, H.V.; Babine, R.; Strickler, J.
Synthesis and in vitro biological evaluation of aryl boronic acids as potential inhibitors of factor XIa
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16
5022-5027
2006
Homo sapiens
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Characterization of novel forms of coagulation factor XIa. Independence of factor XIa subunits in factor IX activation
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283
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49
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Homo sapiens (P03951), Homo sapiens
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Homo sapiens
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Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor
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48
1517-1524
2009
Homo sapiens (P03951)
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Kravtsov, D.V.; Matafonov, A.; Tucker, E.I.; Sun, M.F.; Walsh, P.N.; Gruber, A.; Gailani, D.
Factor XI contributes to thrombin generation in the absence of factor XII
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2009
Homo sapiens (P03951)
brenda
Kwon, M.J.; Kim, H.J.; Bang, S.H.; Kim, S.H.
Severe factor XI deficiency in a Korean woman with a novel missense mutation (Val498Met) and duplication G mutation in exon 13 of the F11 gene
Blood Coagul. Fibrinolysis
19
679-683
2008
Homo sapiens (P03951), Homo sapiens
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Wang, J.; Wang, X.; Dai, J.; Ding, Q.; Fu, Q.; Wang, H.; Shen, L.; Li, D.
A case of factor XI deficiency caused by compound heterozygous F11 gene mutation
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15
603-606
2009
Homo sapiens (P03951)
brenda
Buchanan, M.S.; Carroll, A.R.; Wessling, D.; Jobling, M.; Avery, V.M.; Davis, R.A.; Feng, Y.; Xue, Y.; Oster, L.; Fex, T.; Deinum, J.; Hooper, J.N.; Quinn, R.J.
Clavatadine A, a natural product with selective recognition and irreversible inhibition of factor XIa
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2008
Homo sapiens (P03951)
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Factor XIa and tissue factor activity in patients with coronary artery disease
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99
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2008
Homo sapiens
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Singh, A.; Harnett, M.J.; Connors, J.M.; Camann, W.R.
Factor XI deficiency and obstetrical anesthesia
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108
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2009
Homo sapiens (P03951)
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Franchini, M.; Manzato, F.; Salvagno, G.L.; Montagnana, M.; Lippi, G.
The use of desmopressin in congenital factor XI deficiency: a systematic review
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2009
Homo sapiens (P03951), Homo sapiens
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Schumacher, W.A.; Luettgen, J.M.; Quan, M.L.; Seiffert, D.A.
Inhibition of factor XIa as a new approach to anticoagulation
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30
388-392
2010
Oryctolagus cuniculus, Mus musculus, Rattus norvegicus, Homo sapiens (P03951), Homo sapiens
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Emsley, J.; McEwan, P.A.; Gailani, D.
Structure and function of factor XI
Blood
115
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2010
Mus musculus, Homo sapiens (P03951)
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Gailani, D.; Smith, S.B.
Structural and functional features of factor XI
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7 Suppl 1
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2009
Homo sapiens (P03951)
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Renne, T.; Oschatz, C.; Seifert, S.; Mueller, F.; Antovic, J.; Karlman, M.; Benz, P.M.
Factor XI deficiency in animal models
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7 Suppl 1
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2009
Canis lupus familiaris, Felis catus, Mus musculus, Ornithorhynchus anatinus, Didelphis sp., Homo sapiens (P03951)
brenda
Maas, C.; Meijers, J.C.; Marquart, J.A.; Bakhtiari, K.; Weeterings, C.; de Groot, P.G.; Urbanus, R.T.
Activated factor V is a cofactor for the activation of factor XI by thrombin in plasma
Proc. Natl. Acad. Sci. USA
107
9083-9087
2010
Homo sapiens (P03951)
brenda
Livnat, T.; Tamarin, I.; Mor, Y.; Winckler, H.; Horowitz, Z.; Korianski, Y.; Bar-Zakay, B.; Seligsohn, U.; Salomon, O.
Recombinant activated factor VII and tranexamic acid are haemostatically effective during major surgery in factor XI-deficient patients with inhibitor antibodies
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102
487-492
2009
Homo sapiens
brenda
Hanessian, S.; Larsson, A.; Fex, T.; Knecht, W.; Blomberg, N.
Design and synthesis of macrocyclic indoles targeting blood coagulation cascade Factor XIa
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20
6925-6928
2010
Homo sapiens
brenda
Luszczak, J.; Undas, A.; Gissel, M.; Olszowska, M.; Butenas, S.
Activated factor XI and tissue factor in aortic stenosis: links with thrombin generation
Blood Coagul. Fibrinolysis
22
473-479
2011
Homo sapiens
brenda
Cheng, Q.; Tucker, E.; Pine, M.; Sisler, I.; Matafonov, A.; Sun, M.; White-Adams, T.; Smith, S.; Hanson, S.; McCarty, O.; Renne, T.; Gruber, A.; Gailani, D.
A role for factor XIIa-mediated factor XI activation in thrombus formation in vivo
Blood
116
3981-3989
2010
Mus musculus
brenda
Navaneetham, D.; Sinha, D.; Walsh, P.N.
Mechanisms and specificity of factor XIa and trypsin inhibition by protease nexin 2 and basic pancreatic trypsin inhibitor
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148
467-479
2010
Homo sapiens (P03951)
brenda
Su, Y.C.; Miller, T.N.; Navaneetham, D.; Schoonmaker, R.T.; Sinha, D.; Walsh, P.N.
The role of factor XIa (FXIa) catalytic domain exosite residues in substrate catalysis and inhibition by the Kunitz protease inhibitor domain of protease nexin 2
J. Biol. Chem.
286
31904-31914
2011
Homo sapiens
brenda
Itakura, A.; Verbout, N.G.; Phillips, K.G.; Insall, R.H.; Gailani, D.; Tucker, E.I.; Gruber, A.; McCarty, O.J.
Activated factor XI inhibits chemotaxis of polymorphonuclear leukocytes
J. Leukoc. Biol.
90
923-927
2011
Homo sapiens
brenda
Whelihan, M.F.; Orfeo, T.; Gissel, M.T.; Mann, K.G.
Coagulation procofactor activation by factor XIa
J. Thromb. Haemost.
8
1532-1539
2010
Homo sapiens
brenda
Carrieri, C.; Galasso, R.; Semeraro, F.; Ammollo, C.; Semeraro, N.; Colucci, M.
The role of thrombin activatable fibrinolysis inhibitor and factor XI in platelet-mediated fibrinolysis resistance: A thromboelastographic study in whole blood
J. Thromb. Haemost.
9
154-162
2011
Homo sapiens
brenda
Fradera, X.; Kazemier, B.; Carswell, E.; Cooke, A.; Oubrie, A.; Hamilton, W.; Dempster, M.; Krapp, S.; Nagel, S.; Jestel, A.
High-resolution crystal structures of factor XIa coagulation factor in complex with nonbasic high-affinity synthetic inhibitors
Acta Crystallogr. Sect. F
68
404-408
2012
Homo sapiens (P03951)
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Homo sapiens (P03951)
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Homo sapiens
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Homo sapiens
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Lu, Q.; Yang, L.; Manithody, C.; Wang, X.; Rezaie, A.R.
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Waters, E.K.; Hilden, I.; Sorensen, B.B.; Ezban, M.; Holm, P.K.
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Homo sapiens
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Zucker, M.; Seligsohn, U.; Yeheskel, A.; Mor-Cohen, R.
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Homo sapiens
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