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4-(4'-(dimethylaminophenylazo)-benzoyl)-Arg-Tyr-Tyr-Arg-Ala-Asp-Asp-Ala-Asn-Val-Glu-(EDANS)-NH2 + H2O
?
-
-
-
-
?
bovine lysyl oxidase-like precursor protein + H2O
?
-
cleaved at a Gly-Asp and Ser-Asp bond
-
-
?
chordin + H2O
?
-
-
-
-
?
Collagen type I + H2O
?
-
affinity of C-terminal CUB/EGF PCP constructs for collagen type I is weaker than that for procollagen type I
-
-
?
FAPYYGDEPMDF + H2O
FAPYYG + DEPMDF
-
low enzyme activity
-
-
?
FYRADQPR + H2O
FYRA + DQPR
-
-
-
-
?
lamin 5 + H2O
?
-
gamma2 chain cleaved at a Gly-Asp bond, also cleavage of alpha3 chain
-
-
?
Mca-YVADAPK(Dnp)-OH + H2O
?
-
-
-
-
?
mini-procollagen III + H2O
?
-
-
-
-
?
pC-collagen + H2O
?
-
-
-
-
?
pro-apoA-I + H2O
apoA-I + apoA-I propeptide
-
-
-
?
pro-apoAI + H2O
mature apoAI + ?
-
-
-
-
?
pro-collagen type I + H2O
?
-
-
-
-
?
pro-collagen type II + H2O
?
-
-
-
-
?
pro-collagen type III + H2O
?
-
-
-
-
?
pro-lysyl oxidase + H2O
?
-
cleaved at site Met-Val-Gyl-Asp-Asp-Pro
-
-
?
probiglycan + H2O
?
-
-
-
-
?
Procollagen + H2O
?
-
-
-
-
?
procollagen + H2O
collagen + collagen propeptide
-
-
-
?
procollagen 1 + H2O
?
-
-
-
-
?
procollagen C-propeptide + H2O
?
procollagen I + H2O
pCcollagen + oligopeptide
Procollagen type I + H2O
?
procollagen type I + H2O
collagen type I + collagen type I propeptide
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
procollagen type II + H2O
?
-
-
-
-
?
Procollagen type II + H2O
Type II pNcollagen + C-propeptides
procollagen type III + H2O
?
-
-
-
-
?
Procollagen type III + H2O
Type III pNcollagen + C-propeptides
procollagen type VII + H2O
?
-
cleaved at an Ala-Asp bond
-
-
?
PYYGDE + H2O
PYYG + DE
-
-
-
-
?
PYYGDEP + H2O
PYYG + DEP
-
-
-
-
?
PYYGDEPM + H2O
PYYG + DEPM
-
high enzyme activity
-
-
?
thrombospondin-1 + H2O
?
-
thrombospondin-1 is differently cleaved by both BMP1 and its catalytic domain
-
-
?
truncated procollagen VII + H2O
?
-
the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. The C-terminal domains of BMP1 are important for substrate recognition and for controlling and restricting its proteolytic activity via exosite binding
-
-
?
Type I/III/III pCcollagen + H2O
Type I/II/III collagen + C-propeptides
YYGDEPM + H2O
YYG + DEPM
-
-
-
-
?
YYRADDAN + H2O
YYRA + DDAN
-
low enzyme activity
-
-
?
additional information
?
-
procollagen C-propeptide + H2O
?
cleaves the C-propeptides of type I procollagen during the synthesis of extracellular matrix collagen fibrils
-
?
procollagen C-propeptide + H2O
?
cleaves the C-propeptides of type I procollagen during the synthesis of extracellular matrix collagen fibrils
-
?
procollagen I + H2O
pCcollagen + oligopeptide
-
-
-
-
?
procollagen I + H2O
pCcollagen + oligopeptide
-
-
-
-
?
procollagen I + H2O
pCcollagen + oligopeptide
-
-
-
-
?
Procollagen type I + H2O
?
-
enzyme is involved in the processing of type I procollagen
-
-
?
Procollagen type I + H2O
?
-
-
-
-
?
Procollagen type I + H2O
?
-
constructs containing EGF domains bind more strongly than those consisting of CUB domains only
-
-
?
procollagen type I + H2O
collagen type I + collagen type I propeptide
-
-
-
?
procollagen type I + H2O
collagen type I + collagen type I propeptide
usage of chicken embryo fibroblasts tendon procollagen type I labeled biosynthetically with H3-tryptophan
-
-
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
-
-
-
-
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
-
-
pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
-
specifically cleaves an Ala-Asp bond in both the pro-alpha1(I) and pro-alpha2(I) chains
-
-
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
-
limited proteolysis of COOH-terminal extension peptides
-
-
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
-
specifically cleaves carboxyl-terminal propeptides of a homotrimer of pro-alpha1(I) chains and type II and III procollagens, but it does not cleave type IV procollagen
-
-
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
-
-
-
-
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
-
-
-
-
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
-
-
pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
-
cleavage occurs at the physiological site, i.e. at the specific Ala-Asp bond in the pro-alpha1(I) and pro-alpha2(I) chains, and at the specific Gly-Asp bond in the pro-alpha1(III)
pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides
?
Procollagen type II + H2O
Type II pNcollagen + C-propeptides
-
-
-
-
?
Procollagen type II + H2O
Type II pNcollagen + C-propeptides
-
-
pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides
?
Procollagen type II + H2O
Type II pNcollagen + C-propeptides
-
cleavage of C-terminal extension propeptide
-
-
?
Procollagen type II + H2O
Type II pNcollagen + C-propeptides
-
-
-
-
?
Procollagen type II + H2O
Type II pNcollagen + C-propeptides
-
-
pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides
?
Procollagen type II + H2O
Type II pNcollagen + C-propeptides
-
-
pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides
?
Procollagen type III + H2O
Type III pNcollagen + C-propeptides
-
-
-
-
?
Procollagen type III + H2O
Type III pNcollagen + C-propeptides
-
-
pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides
?
Procollagen type III + H2O
Type III pNcollagen + C-propeptides
-
cleavage of C-terminal extension propeptide
-
-
?
Procollagen type III + H2O
Type III pNcollagen + C-propeptides
-
-
-
-
?
Procollagen type III + H2O
Type III pNcollagen + C-propeptides
-
-
-
-
?
Procollagen type III + H2O
Type III pNcollagen + C-propeptides
-
-
pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides
?
Procollagen type III + H2O
Type III pNcollagen + C-propeptides
-
-
pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides
?
Type I/III/III pCcollagen + H2O
Type I/II/III collagen + C-propeptides
-
pCcollagen is an intermediate in the processing of procollagen to collagen containing the carboxyl propeptides but not the amino propeptides
-
?
Type I/III/III pCcollagen + H2O
Type I/II/III collagen + C-propeptides
-
pCcollagen is an intermediate in the processing of procollagen to collagen containing the carboxyl propeptides but not the amino propeptides
-
?
additional information
?
-
-
in a reaction with modified procollagen the enzyme preferentially cleaves the C-propeptides from the pro-alpha chains in the order pro-alpha1, pro-alpha1 and then pro-alpha2
-
-
?
additional information
?
-
-
in a reaction with modified procollagen the enzyme preferentially cleaves the C-propeptides from the pro-alpha chains in the order pro-alpha1, pro-alpha1 and then pro-alpha2
-
-
?
additional information
?
-
-
enzyme correctly cleaves both the native and the denatured material obtained from partly renatured underhydroxylated procollagen by sedimentation
-
-
?
additional information
?
-
-
the protease domain cleaves other matrix proteins such as fibronectin, collagen I and collagen IV, which are left intact by the full-length enzyme
-
-
?
additional information
?
-
-
the enzyme cleaves both pro-collagen and non-collagen substrates involved in forming functional collagen fibrils. Enzyme cleavage sequences in enzyme substrates types I, II, and III collagen indicate a substrate preference for P3 Met or Tyr, for P2 Arg or Tyr, for P1 Ala or Gly, for P1' Asp, for P2' Asp, Glu, or Gln; and for P3' Ala or Pro
-
-
?
additional information
?
-
-
substrate specificity, overview, peptides PYYGD and PYYGAEPM are no sbstrates for the enzyme
-
-
?
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(3R)-3-(3-[[acetyl(methyl)amino]methyl]-1,2,4-oxadiazol-5-yl)-6-cyclohexyl-N-hydroxyhexanamide
-
-
(3R)-3-[3-(6-aminopyridin-3-yl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
-
-
(3R)-3-[3-(aminomethyl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
-
-
(3R)-3-[3-([[(aminooxy)sulfinyl]amino]methyl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
-
-
(3R)-3-[3-[(acetylamino)methyl]-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
-
-
(3R)-3-[3-[(carbamoylamino)methyl]-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
-
-
(3R)-3-[3-[(cyclobutylamino)methyl]-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
-
-
(3R)-3-[3-[(tert-butylamino)methyl]-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
-
-
(3R)-6-cyclohexyl-3-(3-[[(cyclopropylsulfonyl)amino]methyl]-1,2,4-oxadiazol-5-yl)-N-hydroxyhexanamide
-
-
(3R)-6-cyclohexyl-3-[3-(2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
-
(3R)-6-cyclohexyl-3-[3-(2-furyl)-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
-
(3R)-6-cyclohexyl-3-[3-[(cyclopropylamino)methyl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
-
(3R)-6-cyclohexyl-3-[3-[(dimethylamino)methyl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
-
(3R)-6-cyclohexyl-3-[3-[(ethylamino)methyl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
-
(3R)-6-cyclohexyl-3-[3-[6-(dimethylamino)pyridin-3-yl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-phenyl-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyrazin-2-yl-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyridin-2-yl-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyridin-3-yl-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyridin-4-yl-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyrimidin-2-yl-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyrimidin-5-yl-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-[2-[(methylsulfinyl)amino]ethyl]-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-[[(1-methylethyl)amino]methyl]-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-(3-[[(2-hydroxy-1,1-dimethylethyl)amino]methyl]-1,2,4-oxadiazol-5-yl)hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(1-methyl-1H-imidazol-2-yl)-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(1H-pyrazol-4-yl)-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(4H-pyrazol-3-yl)-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(6-methylpyridazin-3-yl)-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(morpholin-4-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(pyridin-2-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(pyridin-3-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(pyridin-4-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(pyrrolidin-1-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-[(4-hydroxypiperidin-1-yl)methyl]-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-[(methylamino)methyl]-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-[6-(4-methylpiperazin-1-yl)pyridin-3-yl]-1,2,4-oxadiazol-5-yl]hexanamide
-
-
(3R)-6-cyclohexyl-N-hydroxy-3-[3-[6-(methylamino)pyridin-3-yl]-1,2,4-oxadiazol-5-yl]hexanamide
-
-
1,4-dithio-L-threitol
-
-
1-acetyl-L-prolyl-L-tyrosyl-L-tyrosyl-N-hydroxyglycinamide
-
-
1H-pyrazol-4-yl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
-
-
2-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)-N,N-dimethylpyridine-4-carboxamide
-
-
2-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)-N-methylpyridine-4-carboxamide
-
-
2-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridine-4-carboxamide
-
-
2-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridine-4-carboxylic acid
-
-
2-(N-((3s,5s,7s)-adamantan-1-yl)-4-methoxyphenylsulfonamido)-N-hydroxyacetamide
-
9-21% inhibition at 0.010 mM
2-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-5-methyl-1,3-oxazole-4-carboxamide
-
-
2-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-N,N-dimethyl-5-methyl-1,3-oxazole-4-carboxamide
-
-
2-[[3-(hydroxyamino)-3-oxopropyl][2-(4-methoxyphenyl)ethyl]sulfamoyl]benzoic acid
-
32% inhibition at 0.010 mM
3-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)benzoic acid
-
-
4-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)benzoic acid
-
-
4-[benzyl[(4-methoxyphenyl)sulfonyl]amino]-N-hydroxybutanamide
-
-
4-[[3-(hydroxyamino)-3-oxopropyl](2-phenylethyl)sulfamoyl]benzoic acid
-
-
4-[[3-(hydroxyamino)-3-oxopropyl][2-(4-methoxyphenyl)ethyl]sulfamoyl]-N-phenylbenzamide
-
-
5-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridine-2-carboxylic acid
-
-
5-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridine-3-carboxylic acid
-
-
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-(phenylsulfonyl)-1,2,4-oxadiazole-3-carboxamide
-
-
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-[(3,4-dimethoxyphenyl)sulfonyl]-1,2,4-oxadiazole-3-carboxamide
-
-
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-[(4-fluorophenyl)sulfonyl]-1,2,4-oxadiazole-3-carboxamide
-
-
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-[(4-methoxyphenyl)sulfonyl]-1,2,4-oxadiazole-3-carboxamide
-
-
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-[(4-methylphenyl)sulfonyl]-1,2,4-oxadiazole-3-carboxamide
-
-
5-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-1,2,4-oxadiazole-3-carboxamide
-
i.e. UK-383,367. Good selectivity over matrix metalloproteinases involved in wound healing, effective in a cell-based model of collagen deposition and in penetrating human skin in vitro
5-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-N,N-dimethyl-1,2,4-oxadiazole-3-carboxamide
-
good selectivity over matrix metalloproteinases involved in wound healing
5-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-N-isopropyl-1,2,4-oxadiazole-3-carboxamide
-
-
Ac-Met-Val-Gly-Asp-Asp-Pro-Tyr-Asn-NH2
-
weak inhibitor
acidic dipeptide hydroxamate derivates
-
mimic the location of aspartic acid residues in the P1' and P2' positions of the PCP cleavage site in procollagen
-
alpha2-Macroglobulin
-
-
-
Arg
-
inhibits at 5-10 mM
Asp-Pro-Ile-Val-Cys-Pro-Pro-Leu-Asn-Cys-Ser-Gln-Pro-Val-His-Leu-Pro-Asp-Gln
peptide derived from amino acids 727-745 of chordin
Bovine alpha2-macroglobulin
-
-
-
butyl [[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetate
-
-
Chicken alpha2-macroglobulin
-
-
-
cyclopropyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
di-/tripeptidic hydroxamic acid derivates
-
-
-
diisopropylphosphofluoridate
ethyl 3-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)benzoate
-
-
ethyl 4-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)benzoate
-
-
ethyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
-
-
Fetal bovine serum
-
weak
-
Gln-Lys-Arg-Thr-Val-Ile-Cys-Asp-Pro-Ile-Val-Cys-Pro-Pro-Leu-Asn
Lys
-
inhibits at 5-10 mM
methyl 4-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)piperidine-1-sulfinate
-
-
methyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
-
-
methyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]methylamidosulfite
-
-
methyl [4-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)phenyl]amidosulfite
-
-
methyl [5-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridin-2-yl]amidosulfite
-
-
N-ethylmaleimide
-
inhibits at 20 mM
N-hydroxy-4-[[(4-methoxyphenyl)sulfonyl](2-phenylethyl)amino]butanamide
-
-
N-hydroxy-4-[[(4-methoxyphenyl)sulfonyl](phenyl)amino]butanamide
-
-
N-hydroxy-N2-(4-methoxybenzyl)-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
-
N-hydroxy-N2-(4-methoxyphenyl)-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-L-alpha-asparagine
-
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-(2-phenylethyl)glycinamide
-
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-phenylglycinamide
-
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-[4-(trifluoromethyl)benzyl]glycinamide
-
-
N-hydroxy-N2-[2-(4-methoxyphenyl)ethyl]-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
-
N-hydroxy-N3-(2-phenylethyl)-N3-(phenylsulfonyl)-beta-alaninamide
-
-
N-hydroxy-N3-(4-methoxyphenyl)-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
-
-
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
-
-
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-(2-phenylethyl)-beta-alaninamide
-
-
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-phenyl-b-alaninamide
-
-
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-[2-(4-nitrophenyl)ethyl]-beta-alaninamide
-
-
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-[2-(4-sulfamoylphenyl)ethyl]-beta-alaninamide
-
-
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-[2-(morpholin-4-yl)ethyl]-beta-alaninamide
-
-
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-[2-(pyridin-2-yl)ethyl]-beta-alaninamide
-
-
N-hydroxy-N3-[(4-[[(4-methoxyphenyl)carbamoyl]amino]phenyl)sulfonyl]-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N-hydroxy-N3-[2-(2-methoxyphenyl)ethyl]-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
-
45% inhibition at 0.010 mM
N-hydroxy-N3-[2-(3-methoxyphenyl)ethyl]-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
-
-
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-([4-[(methylcarbamoyl)amino]phenyl]sulfonyl)-beta-alaninamide
-
-
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-([4-[(phenoxycarbamoyl)amino]phenyl]sulfonyl)-beta-alaninamide
-
-
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-([4-[(phenylcarbamoyl)amino]phenyl]sulfonyl)-beta-alaninamide
-
-
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
-
-
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[(4-[[(2-phenylethyl)carbamoyl]amino]phenyl)sulfonyl]-beta-alaninamide
-
-
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[[2-(methylsulfonyl)phenyl]sulfonyl]-beta-alaninamide
-
-
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[[4-(methylsulfonyl)phenyl]sulfonyl]-beta-alaninamide
-
-
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[[4-([[4-(trifluoromethyl)phenyl]carbamoyl]amino)phenyl]sulfonyl]-beta-alaninamide
-
-
N-hydroxy-N3-[[2-(N'-hydroxycarbamimidoyl)phenyl]sulfonyl]-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N-hydroxy-N3-[[3-(N'-hydroxycarbamimidoyl)phenyl]sulfonyl]-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N-hydroxy-N3-[[4-(N'-hydroxycarbamimidoyl)phenyl]sulfonyl]-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N-[(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)carbonyl]glycine
-
-
N-[(hydroxyamino)methyl]-L-alpha-aspartyl-N-methyl-L-alpha-glutamine
-
-
N-[2-(4-methoxyphenyl)ethyl]-4-(methylsulfonyl)-N-(2-sulfanylethyl)benzenesulfonamide
-
-
N-[2-(4-methoxyphenyl)ethyl]-4-(methylsulfonyl)-N-(3-sulfanylpropyl)benzenesulfonamide
-
-
N-[2-[carbamoyl(hydroxy)amino]ethyl]-N-[2-(4-methoxyphenyl)ethyl]-4-(methylsulfonyl)benzenesulfonamide
-
-
N2-(4-chlorobenzyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
-
N2-(4-fluorobenzyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
-
N2-(butylsulfonyl)-N-hydroxy-N2-[2-(4-methoxyphenyl)ethyl]glycinamide
-
-
N2-(diphenylmethyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
-
N2-benzyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-L-alpha-asparagine
-
-
N2-benzyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
-
N2-butan-2-yl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
-
N2-[2-(4-methoxyphenyl)ethyl]-N2-[[4-(methylsulfonyl)phenyl]sulfonyl]-N-sulfanylglycinamide
-
-
N2-[2-(carboxymethyl)-4-(hydroxyamino)-4-oxobutanoyl]-N-methyl-L-alpha-glutamine
-
-
N2-[3-carboxy-2-(sulfanylmethyl)propanoyl]-N-methyl-L-alpha-glutamine
-
-
N3-(butylsulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N3-(cyclohexylmethyl)-N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
-
-
N3-([4-[(biphenyl-4-ylcarbamoyl)amino]phenyl]sulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N3-([4-[(diphenoxycarbamoyl)amino]phenyl]sulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N3-([4-[(diphenylcarbamoyl)amino]phenyl]sulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N3-([4-[amino(phenylsulfonyl)methyl]phenyl]sulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N3-benzyl-N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
-
-
N3-butan-2-yl-N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
-
-
N3-[(4-tert-butylphenyl)sulfonyl]-N-hydroxy-N3-(2-phenylethyl)-beta-alaninamide
-
-
N3-[(4-[[(4-chlorophenyl)carbamoyl]amino]phenyl)sulfonyl]-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
-
-
N3-[2-(3,4-dimethoxyphenyl)ethyl]-N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
-
-
N3-[2-(4-methoxyphenyl)ethyl]-N3-[[4-(methylsulfonyl)phenyl]sulfonyl]-N-sulfanyl-beta-alaninamide
-
-
NaCl
-
inhibits at 200-500 mM
phenyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
-
-
pyridin-2-yl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
-
-
pyridin-3-yl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
-
-
small molecule ox(adi)azolyl-hydroxamic acid derivates
-
-
-
sulfonamide hydrxamate derivates of ornithine analogs
-
-
-
Synthetic peptides
-
with amino acid sequences similar to the amino acid sequence around the sites at which the C-propeptides are cleaved during the conversion of procollagen to collagen in vivo, e.g. Tyr-Tyr-Arg-Ala-Asp-Asp-Ala, 35-60% inhibition at 6-12 mM, shorter peptides containing the Ala-Asp bond cleaved by the enzyme are less effective
-
Tris-HCl buffer
-
inhibits at 200-500 mM
Tyr-Tyr-Arg-Ala-Asp-Asp-Ala
-
weak inhibitor
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
-
-
1,10-phenanthroline
-
-
Cd2+
-
CdCl2
concanavalin A
-
-
-
CuCl2
-
-
CuCl2
-
inhibits at 0.01-0.1 mM
Cys-Asp-Pro-Ile-Val-Cys
minimal inhibitory peptide, derived from amino acids 726-731 of chordin. Peptide is not cleaved but instead undergoes cyclization by disulfide formation
Cys-Asp-Pro-Ile-Val-Cys
-
inhibits procollagen C-endopeptidase activity in vitro
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
diisopropylphosphofluoridate
-
weak
diisopropylphosphofluoridate
-
weak
DTT
-
-
EDTA
a common inhibitor of several astacin metalloproteases
EDTA
a common inhibitor of several astacin metalloproteases
EDTA
a common inhibitor of several astacin metalloproteases
EGTA
-
-
Gln-Lys-Arg-Thr-Val-Ile-Cys-Asp-Pro-Ile-Val-Cys-Pro-Pro-Leu-Asn
peptide derived from amino acids 720-735 of chordin. Peptide is not cleaved but instead undergoes cyclization by disulfide formation
Gln-Lys-Arg-Thr-Val-Ile-Cys-Asp-Pro-Ile-Val-Cys-Pro-Pro-Leu-Asn
-
inhibits procollagen C-endopeptidase activity in vitro
L-arginine
-
weak
L-lysine
-
-
leupeptin
-
-
metal chelators
-
-
-
pepstatin
-
A
ZnCl2
-
-
additional information
-
not: cysteine proteinases; not: inhibitors of serine
-
additional information
-
not: cysteine proteinases; not: inhibitors of serine
-
additional information
-
not: cysteine proteinases; not: inhibitors of serine
-
additional information
-
procollagen C-proteinase enhancer-1 is not an inhibitor of BMP-1
-
additional information
-
the cyclic form AS1.11c (Gln-Lys-Arg-Thr-Val-Ile-Cys-Asp-Pro-Ile-Val-Cys-Pro-Pro-Leu-Asn) does not inhibit procollagen C-endopeptidase activity on procollagen type I
-
additional information
-
design from substrate leads and synthesis of procollagen C-proteinase inhibitors, overview. The compounds are optimized for potency and selectivity, with N-substituted aryl sulfonamide hydroxamates having the best combination of these properties
-
additional information
-
not: inhibitors of serine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Adenocarcinoma
Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family.
Adenocarcinoma
Involvement of beta3A subunit of adaptor protein-3 in intracellular trafficking of receptor-like protein tyrosine phosphatase PCP-2.
Adenocarcinoma
Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin.
Adenoma, Pleomorphic
Expression of bone morphogenetic proteins in salivary pleomorphic adenomas.
Alveolar Bone Loss
Proteinase bone morphogenetic protein 1, but not tolloid-like 1, plays a dominant role in maintaining periodontal homeostasis.
Atherosclerosis
Procollagen C-endopeptidase Enhancer Protein 2 (PCPE2) Reduces Atherosclerosis in Mice by Enhancing Scavenger Receptor Class B1 (SR-BI)-mediated High-density Lipoprotein (HDL)-Cholesteryl Ester Uptake.
Carcinogenesis
Pathologic significance of a novel oncoprotein in thyroid cancer progression.
Carcinoma
Expression of bone morphogenetic proteins of human neoplastic epithelial cells.
Carcinoma, Squamous Cell
Expression of bone morphogenetic proteins of human neoplastic epithelial cells.
Colonic Neoplasms
Bone Morphogenetic Protein 1 Targeting COL1A1 and COL1A2 to Regulate the Epithelial-Mesenchymal Transition Process of Colon Cancer SW620 Cells.
Colonic Neoplasms
Protein-tyrosine phosphatase PCP-2 inhibits beta-catenin signaling and increases E-cadherin-dependent cell adhesion.
Connective Tissue Diseases
Dermatosparaxis in a Himalayan cat: II. Ultrastructural studies of dermal collagen.
Crohn Disease
Intestinal fibrosis is associated with lack of response to Infliximab therapy in Crohn's disease.
Dental Caries
CCN2/CTGF expression via cellular uptake of BMP-1 is associated with reparative dentinogenesis.
Dentinogenesis Imperfecta
Essential Roles of Bone Morphogenetic Protein-1 and Mammalian Tolloid-like 1 in Postnatal Root Dentin Formation.
Ehlers-Danlos Syndrome
Procollagen peptidase deficiency in a form of the Ehlers-Danlos syndrome.
Ehlers-Danlos Syndrome
[The biochemistry of collagen and the locomotor apparatus. Hereditary diseases of connective tissue and rheumatologic diseases (part 2)]
Endometriosis
The inhibition of bone morphogenetic protein 1 attenuates endometriosis lesions in vivo and in vitro.
Epidermolysis Bullosa Dystrophica
Interaction of Complement Defence Collagens C1q and Mannose-Binding Lectin with BMP-1/Tolloid-like Proteinases.
Epidermolysis Bullosa Dystrophica
Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen.
Epilepsy
Proteomic analysis of cerebrospinal fluid from patients with idiopathic temporal lobe epilepsy.
Gastroschisis
Mutational analysis of the BMP-1 gene in patients with gastroschisis.
Genetic Diseases, Inborn
Dermatosparaxis in a Himalayan cat: I. Biochemical studies of dermal collagen.
Glaucoma
Identification and expression of a novel type I procollagen C-proteinase enhancer protein gene from the glaucoma candidate region on 3q21-q24.
Glaucoma, Open-Angle
Identification and expression of a novel type I procollagen C-proteinase enhancer protein gene from the glaucoma candidate region on 3q21-q24.
Granuloma
Increased inflammatory cytokines and new collagen formation in cutaneous tuberculosis and sarcoidosis.
Heart Failure
Osteopontin-mediated myocardial fibrosis in heart failure: a role for lysyl oxidase?
Hepatitis B, Chronic
Evaluation of serum procollagen C-proteinase enhancer 1 level as a fibrosis marker in patients with chronic hepatitis B.
Herpes Zoster
Cloning and uterus/oviduct-specific expression of a novel estrogen-regulated gene (ERG1)
Infections
Bone morphogenetic protein-1 (BMP-1) cleaves human proapolipoprotein A1 and regulates its activation for lipid binding.
Infections
Gene expression profiling in AGS cells stimulated with Helicobacter pylori isogenic strains (cagA positive or cagA negative).
Infections
Genome-Wide Association Study Identifies TLL1 Variant Associated With Development of Hepatocellular Carcinoma After Eradication of Hepatitis C Virus Infection.
Infections
Infection of human astrocytoma cells with simian-human immunodeficiency virus results in up-regulation of gene expression and altered growth properties.
Inflammatory Bowel Diseases
An integrated in silico approach to understand protein-protein interactions: human meprin-? with fetuin-A.
Keloid
Aberrant connective tissue differentiation towards cartilage and bone underlies human keloids in African Americans.
Keloid
Premature Collagen Fibril Formation, Fibroblast-Mast Cell Interactions and Mast Cell-Mediated Phagocytosis of Collagen in Keloids.
Kidney Diseases
Experimental Biology 2020 Meeting Abstracts.
Langer-Giedion Syndrome
BMP-1 sublocalization on human chromosome 8. Molecular anatomy and orthopaedic implications.
Langer-Giedion Syndrome
Mapping of the bone morphogenetic protein 1 gene (BMP1) to 8p21: removal of BMP1 from candidacy for the bone disorder in Langer-Giedion syndrome.
Leiomyoma
[Changes of mRNAs encoding alternatively spliced variants of procollagen C-endopeptidase in leiomyomas uteri depending on the phase of menstrual cycle and in postmenopausal women]
Liver Cirrhosis
Correction: Procollagen C-Proteinase Enhancer 1 (PCPE-1) as a Plasma Marker of Muscle and Liver Fibrosis in Mice.
Liver Cirrhosis
Data comparing the plasma levels of procollagen C-proteinase enhancer 1 (PCPE-1) in healthy individuals and liver fibrosis patients.
Liver Cirrhosis
Procollagen C-Proteinase Enhancer 1 (PCPE-1) as a Plasma Marker of Muscle and Liver Fibrosis in Mice.
Liver Cirrhosis
Procollagen C-Proteinase Enhancer 1 (PCPE-1) in Liver Fibrosis.
Liver Cirrhosis
Up-regulation of type I procollagen C-proteinase enhancer protein messenger RNA in rats with CCl4-induced liver fibrosis.
Lymphoma
Proteomic profiling of pretreatment serum from HIV-infected patients identifies candidate markers predictive of lymphoma development.
Melanoma
Interaction of Complement Defence Collagens C1q and Mannose-Binding Lectin with BMP-1/Tolloid-like Proteinases.
Muscular Dystrophy, Duchenne
Expression profile analysis to predict potential biomarkers for glaucoma: BMP1, DMD and GEM.
Neoplasm Metastasis
Monoamine oxidase-A targeting probe for prostate cancer imaging and inhibition of metastasis.
Neoplasm Metastasis
Suppression of pancreatic ductal adenocarcinoma growth and metastasis by fibrillar collagens produced selectively by tumor cells.
Neoplasms
An integrated in silico approach to understand protein-protein interactions: human meprin-? with fetuin-A.
Neoplasms
BMP-1 disrupts cell adhesion and enhances TGF-? activation through cleavage of the matricellular protein thrombospondin-1.
Neoplasms
Proteolytic control of TGF-? co-receptor activity by BMP-1/tolloid-like proteases revealed by quantitative iTRAQ proteomics.
Neoplasms
Suppression of pancreatic ductal adenocarcinoma growth and metastasis by fibrillar collagens produced selectively by tumor cells.
Neoplasms
Survival impact of psammoma body, stromal calcification, and bone formation in papillary thyroid carcinoma.
Neoplasms
The Advantages and Disadvantages of Sfrp1 and Sfrp2 Expression in Pathological Events.
Neoplasms
XBMP-1B (Xtld), a Xenopus homolog of dorso-ventral polarity gene in Drosophila, modifies tissue phenotypes of ventral explants.
Neoplasms
[Changes of mRNAs encoding alternatively spliced variants of procollagen C-endopeptidase in leiomyomas uteri depending on the phase of menstrual cycle and in postmenopausal women]
Osteogenesis Imperfecta
BMP1 and TLL1 Are Required for Maintaining Periodontal Homeostasis.
Osteogenesis Imperfecta
Essential Roles of Bone Morphogenetic Protein-1 and Mammalian Tolloid-like 1 in Postnatal Root Dentin Formation.
Osteogenesis Imperfecta
Proteinase bone morphogenetic protein 1, but not tolloid-like 1, plays a dominant role in maintaining periodontal homeostasis.
Osteogenesis Imperfecta
Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects.
procollagen c-endopeptidase deficiency
Mutational analysis of the Drosophila tolloid gene, a human BMP-1 homolog.
procollagen c-endopeptidase deficiency
Procollagen peptidase deficiency in a form of the Ehlers-Danlos syndrome.
procollagen c-endopeptidase deficiency
[The biochemistry of collagen and the locomotor apparatus. Hereditary diseases of connective tissue and rheumatologic diseases (part 2)]
Pulmonary Disease, Chronic Obstructive
Chronic Obstructive Pulmonary Disease Phenotype Dictates Cancer-Promoting Stromal Gene Expression Programs.
Sarcoidosis
Increased inflammatory cytokines and new collagen formation in cutaneous tuberculosis and sarcoidosis.
Stomach Neoplasms
High expression of bone morphogenetic protein 1 (BMP1) is associated with a poor survival rate in human gastric cancer, a dataset approaches.
Stomach Neoplasms
Upregulation of bone morphogenetic protein 1 is associated with poor prognosis of late-stage gastric Cancer patients.
Thyroid Cancer, Papillary
Immunohistochemical analyses to determine pathogenesis of tenosynovitis with psammomatous calcification in the wrist: A case report.
Thyroid Neoplasms
Pathologic significance of a novel oncoprotein in thyroid cancer progression.
Thyroid Nodule
Pathologic significance of a novel oncoprotein in thyroid cancer progression.
Tuberculosis
Increased inflammatory cytokines and new collagen formation in cutaneous tuberculosis and sarcoidosis.
Virus Diseases
Association between Interferon-Lambda-3 rs12979860, TLL1 rs17047200 and DDR1 rs4618569 Variant Polymorphisms with the Course and Outcome of SARS-CoV-2 Patients.
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0.000003
(3R)-3-(3-[[acetyl(methyl)amino]methyl]-1,2,4-oxadiazol-5-yl)-6-cyclohexyl-N-hydroxyhexanamide
Homo sapiens
-
-
0.000018
(3R)-3-[3-(6-aminopyridin-3-yl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
Homo sapiens
-
-
0.000122
(3R)-3-[3-(aminomethyl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
Homo sapiens
-
-
0.000098
(3R)-3-[3-([[(aminooxy)sulfinyl]amino]methyl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
Homo sapiens
-
-
0.000019
(3R)-3-[3-[(acetylamino)methyl]-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
Homo sapiens
-
-
0.000324
(3R)-3-[3-[(carbamoylamino)methyl]-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
Homo sapiens
-
-
0.000006
(3R)-3-[3-[(cyclobutylamino)methyl]-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
Homo sapiens
-
-
0.00001
(3R)-3-[3-[(tert-butylamino)methyl]-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
Homo sapiens
-
-
0.000015
(3R)-6-cyclohexyl-3-(3-[[(cyclopropylsulfonyl)amino]methyl]-1,2,4-oxadiazol-5-yl)-N-hydroxyhexanamide
Homo sapiens
-
-
0.00001
(3R)-6-cyclohexyl-3-[3-(2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
Homo sapiens
-
-
0.000046
(3R)-6-cyclohexyl-3-[3-(2-furyl)-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
Homo sapiens
-
-
0.000006
(3R)-6-cyclohexyl-3-[3-[(cyclopropylamino)methyl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
Homo sapiens
-
-
0.000031
(3R)-6-cyclohexyl-3-[3-[(dimethylamino)methyl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
Homo sapiens
-
-
0.000021
(3R)-6-cyclohexyl-3-[3-[(ethylamino)methyl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
Homo sapiens
-
-
0.000028
(3R)-6-cyclohexyl-3-[3-[6-(dimethylamino)pyridin-3-yl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
Homo sapiens
-
-
0.000116
(3R)-6-cyclohexyl-N-hydroxy-3-(3-phenyl-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.000014
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyrazin-2-yl-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.000025
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyridin-2-yl-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.000023
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyridin-3-yl-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.000002
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyridin-4-yl-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.000023
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyrimidin-2-yl-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.000014
(3R)-6-cyclohexyl-N-hydroxy-3-(3-pyrimidin-5-yl-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.00002
(3R)-6-cyclohexyl-N-hydroxy-3-(3-[2-[(methylsulfinyl)amino]ethyl]-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.000029
(3R)-6-cyclohexyl-N-hydroxy-3-(3-[[(1-methylethyl)amino]methyl]-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.000008
(3R)-6-cyclohexyl-N-hydroxy-3-(3-[[(2-hydroxy-1,1-dimethylethyl)amino]methyl]-1,2,4-oxadiazol-5-yl)hexanamide
Homo sapiens
-
-
0.000092
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(1-methyl-1H-imidazol-2-yl)-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000039
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(1H-pyrazol-4-yl)-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000074
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(4H-pyrazol-3-yl)-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.00003
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(6-methylpyridazin-3-yl)-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000005
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(morpholin-4-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000006
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(pyridin-2-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000006
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(pyridin-3-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000028
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(pyridin-4-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000024
(3R)-6-cyclohexyl-N-hydroxy-3-[3-(pyrrolidin-1-ylmethyl)-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000013
(3R)-6-cyclohexyl-N-hydroxy-3-[3-[(4-hydroxypiperidin-1-yl)methyl]-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000023
(3R)-6-cyclohexyl-N-hydroxy-3-[3-[(methylamino)methyl]-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000008
(3R)-6-cyclohexyl-N-hydroxy-3-[3-[6-(4-methylpiperazin-1-yl)pyridin-3-yl]-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.000013
(3R)-6-cyclohexyl-N-hydroxy-3-[3-[6-(methylamino)pyridin-3-yl]-1,2,4-oxadiazol-5-yl]hexanamide
Homo sapiens
-
-
0.042
1-acetyl-L-prolyl-L-tyrosyl-L-tyrosyl-N-hydroxyglycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000088
1H-pyrazol-4-yl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
Homo sapiens
-
-
0.000017
2-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)-N,N-dimethylpyridine-4-carboxamide
Homo sapiens
-
-
0.00003
2-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)-N-methylpyridine-4-carboxamide
Homo sapiens
-
-
0.000017
2-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridine-4-carboxamide
Homo sapiens
-
-
0.000006
2-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridine-4-carboxylic acid
Homo sapiens
-
-
0.000017
2-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-5-methyl-1,3-oxazole-4-carboxamide
Homo sapiens
-
-
0.000017
2-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-N,N-dimethyl-5-methyl-1,3-oxazole-4-carboxamide
Homo sapiens
-
-
0.000006
3-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)benzoic acid
Homo sapiens
-
-
0.000032
4-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)benzoic acid
Homo sapiens
-
-
0.01
4-[benzyl[(4-methoxyphenyl)sulfonyl]amino]-N-hydroxybutanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.001
4-[[3-(hydroxyamino)-3-oxopropyl](2-phenylethyl)sulfamoyl]benzoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00041
4-[[3-(hydroxyamino)-3-oxopropyl][2-(4-methoxyphenyl)ethyl]sulfamoyl]-N-phenylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000059
5-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridine-2-carboxylic acid
Homo sapiens
-
-
0.000017
5-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridine-3-carboxylic acid
Homo sapiens
-
-
0.000007
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-(phenylsulfonyl)-1,2,4-oxadiazole-3-carboxamide
Homo sapiens
-
-
0.0000018
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-[(3,4-dimethoxyphenyl)sulfonyl]-1,2,4-oxadiazole-3-carboxamide
Homo sapiens
-
-
0.000033
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-[(4-fluorophenyl)sulfonyl]-1,2,4-oxadiazole-3-carboxamide
Homo sapiens
-
-
0.000017
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-[(4-methoxyphenyl)sulfonyl]-1,2,4-oxadiazole-3-carboxamide
Homo sapiens
-
-
0.000014
5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-N-[(4-methylphenyl)sulfonyl]-1,2,4-oxadiazole-3-carboxamide
Homo sapiens
-
-
0.000044
5-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-1,2,4-oxadiazole-3-carboxamide
Homo sapiens
-
-
0.00001
5-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-N,N-dimethyl-1,2,4-oxadiazole-3-carboxamide
Homo sapiens
-
-
0.000021
5-[(3R)-6-cyclohexyl-1-(hydroxyamino)-1-oxohexan-3-yl]-N-isopropyl-1,2,4-oxadiazole-3-carboxamide
Homo sapiens
-
-
0.167
butyl [[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
cyclopropyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
Homo sapiens
-
-
0.000184
ethyl 3-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)benzoate
Homo sapiens
-
-
0.000154
ethyl 4-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)benzoate
Homo sapiens
-
-
0.000026
ethyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
Homo sapiens
-
-
0.000003
methyl 4-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)piperidine-1-sulfinate
Homo sapiens
-
-
0.000011
methyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
Homo sapiens
-
-
0.000038
methyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]methylamidosulfite
Homo sapiens
-
-
0.000003
methyl [4-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)phenyl]amidosulfite
Homo sapiens
-
-
0.000027
methyl [5-(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)pyridin-2-yl]amidosulfite
Homo sapiens
-
-
0.0049
N-hydroxy-4-[[(4-methoxyphenyl)sulfonyl](2-phenylethyl)amino]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.028
N-hydroxy-4-[[(4-methoxyphenyl)sulfonyl](phenyl)amino]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.029
N-hydroxy-N2-(4-methoxybenzyl)-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.073
N-hydroxy-N2-(4-methoxyphenyl)-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-L-alpha-asparagine
Homo sapiens
-
pH and temperature not specified in the publication
0.018
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-(2-phenylethyl)glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.069
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-phenylglycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.067
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-[4-(trifluoromethyl)benzyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.018
N-hydroxy-N2-[2-(4-methoxyphenyl)ethyl]-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0022
N-hydroxy-N3-(2-phenylethyl)-N3-(phenylsulfonyl)-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0017
N-hydroxy-N3-(4-methoxyphenyl)-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.166
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-(2-phenylethyl)-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.003
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-phenyl-b-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.011
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-[2-(4-nitrophenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.023
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-[2-(4-sulfamoylphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.081
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-[2-(morpholin-4-yl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0081
N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-N3-[2-(pyridin-2-yl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00035
N-hydroxy-N3-[(4-[[(4-methoxyphenyl)carbamoyl]amino]phenyl)sulfonyl]-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0023
N-hydroxy-N3-[2-(3-methoxyphenyl)ethyl]-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00006
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-([4-[(methylcarbamoyl)amino]phenyl]sulfonyl)-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00001
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-([4-[(phenoxycarbamoyl)amino]phenyl]sulfonyl)-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000093
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-([4-[(phenylcarbamoyl)amino]phenyl]sulfonyl)-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.001
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[(4-[[(2-phenylethyl)carbamoyl]amino]phenyl)sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0091
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[[2-(methylsulfonyl)phenyl]sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00029
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[[4-(methylsulfonyl)phenyl]sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000042
N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-N3-[[4-([[4-(trifluoromethyl)phenyl]carbamoyl]amino)phenyl]sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0071
N-hydroxy-N3-[[2-(N'-hydroxycarbamimidoyl)phenyl]sulfonyl]-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
N-hydroxy-N3-[[3-(N'-hydroxycarbamimidoyl)phenyl]sulfonyl]-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00008
N-hydroxy-N3-[[4-(N'-hydroxycarbamimidoyl)phenyl]sulfonyl]-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
N-[(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)carbonyl]glycine
Homo sapiens
-
-
1.5
N-[(hydroxyamino)methyl]-L-alpha-aspartyl-N-methyl-L-alpha-glutamine
Homo sapiens
-
pH and temperature not specified in the publication
0.0094
N-[2-(4-methoxyphenyl)ethyl]-4-(methylsulfonyl)-N-(2-sulfanylethyl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.014
N-[2-(4-methoxyphenyl)ethyl]-4-(methylsulfonyl)-N-(3-sulfanylpropyl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.1
N-[2-[carbamoyl(hydroxy)amino]ethyl]-N-[2-(4-methoxyphenyl)ethyl]-4-(methylsulfonyl)benzenesulfonamide
Homo sapiens
-
above, pH and temperature not specified in the publication
0.019
N2-(4-chlorobenzyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.034
N2-(4-fluorobenzyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.055
N2-(butylsulfonyl)-N-hydroxy-N2-[2-(4-methoxyphenyl)ethyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.102
N2-(diphenylmethyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0028
N2-benzyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-L-alpha-asparagine
Homo sapiens
-
pH and temperature not specified in the publication
0.016
N2-benzyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.112
N2-butan-2-yl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0047
N2-[2-(4-methoxyphenyl)ethyl]-N2-[[4-(methylsulfonyl)phenyl]sulfonyl]-N-sulfanylglycinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.04
N2-[2-(carboxymethyl)-4-(hydroxyamino)-4-oxobutanoyl]-N-methyl-L-alpha-glutamine
Homo sapiens
-
pH and temperature not specified in the publication
0.085
N2-[3-carboxy-2-(sulfanylmethyl)propanoyl]-N-methyl-L-alpha-glutamine
Homo sapiens
-
pH and temperature not specified in the publication
0.0067
N3-(butylsulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.001
N3-(cyclohexylmethyl)-N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000073
N3-([4-[(biphenyl-4-ylcarbamoyl)amino]phenyl]sulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00038
N3-([4-[(diphenoxycarbamoyl)amino]phenyl]sulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00078
N3-([4-[(diphenylcarbamoyl)amino]phenyl]sulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00047
N3-([4-[amino(phenylsulfonyl)methyl]phenyl]sulfonyl)-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0045
N3-benzyl-N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0017
N3-butan-2-yl-N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.017
N3-[(4-tert-butylphenyl)sulfonyl]-N-hydroxy-N3-(2-phenylethyl)-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
N3-[(4-[[(4-chlorophenyl)carbamoyl]amino]phenyl)sulfonyl]-N-hydroxy-N3-[2-(4-methoxyphenyl)ethyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.042
N3-[2-(3,4-dimethoxyphenyl)ethyl]-N-hydroxy-N3-[(4-methoxyphenyl)sulfonyl]-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.013
N3-[2-(4-methoxyphenyl)ethyl]-N3-[[4-(methylsulfonyl)phenyl]sulfonyl]-N-sulfanyl-beta-alaninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000026
phenyl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
Homo sapiens
-
-
0.000107
pyridin-2-yl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
Homo sapiens
-
-
0.000026
pyridin-3-yl [(5-[(1R)-4-cyclohexyl-1-[2-(hydroxyamino)-2-oxoethyl]butyl]-1,2,4-oxadiazol-3-yl)methyl]amidosulfite
Homo sapiens
-
-
0.345
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
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Hojima, Y.; van der Rest, M.; Prockop, P.J.
Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization
J. Biol. Chem.
260
15996-16003
1985
Gallus gallus
brenda
Kessler, E.; Adar, R.
Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55-kDa enhancer glycoprotein
Eur. J. Biochem.
186
115-121
1989
Mus musculus
brenda
Kadler, K.E.; Watson, R.B.
Procollagen C-peptidase: procollagen C-proteinase
Methods Enzymol.
248
771-781
1995
Gallus gallus, Mus musculus
brenda
Kessler, E.; Takahara, K.; Biniaminov, L.; Brusel, M.; Greenspan, D.S.
Bone morphogenic protein-1: the type I procollagen C-proteinase
Science
271
360-362
1971
Mus musculus
brenda
Leung, M.K.K.; Fessler, L.I.; Greenberg, D.B.; Fessler, J.H.
Separate amino and carboxyl procollagen peptidases in chick embryo tendon
J. Biol. Chem.
254
224-232
1979
Gallus gallus
brenda
Morris, N.P.; Fessler, L.I.; Fessler, J.H.
Procollagen propeptide release by procollagen peptidases and bacterial collagenase
J. Biol. Chem.
254
11024-11032
1979
Gallus gallus
brenda
Davidson, J.M.; Mc Eneany, L.S.G.; Bornstein, P.
Procollagen processing. Limited proteolysis of COOH-terminal extension peptides by a cathepsin-like protease secreted by tendon fibroblasts
Eur. J. Biochem.
100
551-558
1979
Gallus gallus
brenda
Njieha, F.K.; Morikawa, T.; Tuderman, L.; Prockop, D.J.
Partial purification of a procollagen C-proteinase. Inhibition by synthetic peptides and sequential cleavage of type I procollagen
Biochemistry
21
757-764
1982
Gallus gallus
brenda
Hojima, Y.; Behta, B.; Romanic, A.M.; Prockop, D.J.
Cadmium ions inhibit procollagen C-proteinase and cupric ions inhibit procollagen N-proteinase
Matrix Biol.
14
113-120
1994
Gallus gallus
brenda
Kessler, E.; Adar, R.; Goldberg, B.; Niece, R.
Partial purification and characterization of a procollagen C-proteinase from the culture medium of mouse fibroblasts
Coll. Relat. Res.
6
249-266
1986
Mus musculus
brenda
Adar, R.; Kessler, E.; Goldberg, B.
Evidence for a protein that enhances the activity of type I procollagen C-proteinase
Coll. Relat. Res.
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267-277
1986
Mus musculus
brenda
Garrigue-Antar, L.; Barker, C.; Kadler, K.E.
Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity
J. Biol. Chem.
276
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2001
Homo sapiens (P13497)
brenda
Hartigan, N.; Garrigue-Antar, L.; Kadler, K.E.
Bone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activity
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Homo sapiens (P13497)
brenda
Hintze, V.; Hoewel, M.; Wermter, C.; Grosse Berkhoff, E.; Becker-Pauly, C.; Beermann, B.; Yiallouros, I.; Stoecker, W.
The interaction of recombinant subdomains of the procollagen C-proteinase with procollagen I provides a quantitative explanation for functional differences between the two splice variants, mammalian tolloid and bone morphogenetic protein 1
Biochemistry
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6741-6748
2006
Homo sapiens
brenda
Kessler, E.
Procollagen C-endopeptidase
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2004
Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus, Strongylocentrotus purpuratus, Xenopus laevis
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brenda
Moali, C.; Font, B.; Ruggiero, F.; Eichenberger, D.; Rousselle, P.; Francois, V.; Oldberg, A.; Bruckner-Tuderman, L.; Hulmes, D.J.
Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1
J. Biol. Chem.
280
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2005
Homo sapiens
brenda
Wermter, C.; Hoewel, M.; Hintze, V.; Bombosch, B.; Aufenvenne, K.; Yiallouros, I.; Stoecker, W.
The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains
Biol. Chem.
388
513-521
2007
Homo sapiens
brenda
Ge, G.; Zhang, Y.; Steiglitz, B.M.; Greenspan, D.S.
Mammalian tolloid-like 1 binds procollagen C-proteinase enhancer protein 1 and differs from bone morphogenetic protein 1 in the functional roles of homologous protein domains
J. Biol. Chem.
281
10786-10798
2006
Homo sapiens
brenda
Fish, P.V.; Allan, G.A.; Bailey, S.; Blagg, J.; Butt, R.; Collis, M.G.; Greiling, D.; James, K.; Kendall, J.; McElroy, A.; McCleverty, D.; Reed, C.; Webster, R.; Whitlock, G.A.
Potent and selective nonpeptidic inhibitors of procollagen C-proteinase
J. Med. Chem.
50
3442-3456
2007
Homo sapiens
brenda
Reid, R.R.; Mogford, J.E.; Butt, R.; deGiorgio-Miller, A.; Mustoe, T.A.
Inhibition of procollagen C-proteinase reduces scar hypertrophy in a rabbit model of cutaneous scarring
Wound Repair Regen.
14
138-141
2006
Oryctolagus cuniculus
brenda
Lesiak, M.; Augusciak-Duma, A.; Szydlo, A.; Pruszczynska, K.; Sieron, A.L.
Specific inhibition of procollagen C-endopeptidase activity by synthetic peptide with conservative sequence found in chordin
Acta Biochim. Pol.
55
297-305
2008
Homo sapiens (P13497)
brenda
Bailey, S.; Fish, P.V.; Billotte, S.; Bordner, J.; Greiling, D.; James, K.; McElroy, A.; Mills, J.E.; Reed, C.; Webster, R.
Succinyl hydroxamates as potent and selective non-peptidic inhibitors of procollagen C-proteinase: design, synthesis, and evaluation as topically applied, dermal anti-scarring agents
Bioorg. Med. Chem. Lett.
18
6562-6567
2008
Homo sapiens
brenda
Kobayashi, K.; Luo, M.; Zhang, Y.; Wilkes, D.C.; Ge, G.; Grieskamp, T.; Yamada, C.; Liu, T.C.; Huang, G.; Basson, C.T.; Kispert, A.; Greenspan, D.S.; Sato, T.N.
Secreted Frizzled-related protein 2 is a procollagen C proteinase enhancer with a role in fibrosis associated with myocardial infarction
Nat. Cell Biol.
11
46-55
2009
Mus musculus
brenda
Mesilaty-Gross, S.; Anikster, Y.; Vilensky, B.; Wolf, I.; Phillip, M.; Gat-Yablonski, G.
Different patterns of human serum procollagen C-proteinase enhancer1 (PCPE1)
Clin. Chim. Acta
403
76-80
2009
Homo sapiens
brenda
Kronenberg, D.; Vadon-Le Goff, S.; Bourhis, J.M.; Font, B.; Eichenberger, D.; Hulmes, D.J.; Moali, C.
Strong cooperativity and loose geometry between CUB domains are the basis for procollagen C-proteinase enhancer activity
J. Biol. Chem.
284
33437-33446
2009
Homo sapiens
brenda
Bekhouche, M.; Kronenberg, D.; Vadon-Le Goff, S.; Bijakowski, C.; Lim, N.H.; Font, B.; Kessler, E.; Colige, A.; Nagase, H.; Murphy, G.; Hulmes, D.J.; Moali, C.
Role of the netrin-like domain of procollagen C-proteinase enhancer-1 in the control of metalloproteinase activity
J. Biol. Chem.
285
15950-15959
2010
Homo sapiens
brenda
Zhu, J.; Gardner, J.; Pullinger, C.R.; Kane, J.P.; Thompson, J.F.; Francone, O.L.
Regulation of apoAI processing by procollagen C-proteinase enhancer-2 and bone morphogenetic protein-1
J. Lipid Res.
50
1330-1339
2009
Homo sapiens
brenda
Lesiak, M.; Augusciak-Duma, A.; Szydlo, A.; Sieron, A.L.
Blocking angiogenesis with peptides that inhibit the activity of procollagen C-endopeptidase
Pharmacol. Rep.
61
468-476
2009
Homo sapiens
brenda
Canty-Laird, E.G.; Lu, Y.; Kadler, K.E.
Stepwise proteolytic activation of type I procollagen to collagen within the secretory pathway of tendon fibroblasts in situ
Biochem. J.
441
707-717
2012
Gallus gallus, Mus musculus, Rattus norvegicus
brenda
Canty-Laird, E.; Carre, G.A.; Mandon-Pepin, B.; Kadler, K.E.; Fabre, S.
First evidence of bone morphogenetic protein 1 expression and activity in sheep ovarian follicles
Biol. Reprod.
83
138-146
2010
Ovis aries
brenda
Vadon-Le Goff, S.; Kronenberg, D.; Bourhis, J.M.; Bijakowski, C.; Raynal, N.; Ruggiero, F.; Farndale, R.W.; Stoecker, W.; Hulmes, D.J.; Moali, C.
Procollagen C-proteinase enhancer stimulates procollagen processing by binding to the C-propeptide region only
J. Biol. Chem.
286
38932-38938
2011
Homo sapiens
brenda
Turtle, E.; Chow, N.; Yang, C.; Sosa, S.; Bauer, U.; Brenner, M.; Solow-Cordero, D.; Ho, W.B.
Design and synthesis of procollagen C-proteinase inhibitors
Bioorg. Med. Chem. Lett.
22
7397-7401
2012
Homo sapiens
brenda
Chaudhuri, A.; Chakraborty, S.
Structure-activity relationship of astacin metalloproteases A comparative study using EDTA
Curr. Enzyme Inhib.
14
131-140
2018
Drosophila melanogaster (P25723), Mus musculus (P98063), Xenopus laevis (P98070)
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brenda
Moschcovich, L.; Kessler, E.
Data comparing the kinetics of procollagen type I processing by bone morphogenetic protein 1 (BMP-1) with and without procollagen C-proteinase enhancer 1 (PCPE-1)
Data Brief
9
883-887
2016
Homo sapiens (P13497)
brenda
Pollard, R.D.; Blesso, C.N.; Zabalawi, M.; Fulp, B.; Gerelus, M.; Zhu, X.; Lyons, E.W.; Nuradin, N.; Francone, O.L.; Li, X.A.; Sahoo, D.; Thomas, M.J.; Sorci-Thomas, M.G.
Procollagen C-endopeptidase enhancer protein 2 (PCPE2) reduces atherosclerosis in mice by enhancing scavenger receptor class B1 (SR-BI)-mediated high-density lipoprotein (HDL)-cholesteryl ester uptake
J. Biol. Chem.
290
15496-15511
2015
Mus musculus (P98063)
brenda