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Information on EC 3.4.24.B4 - matrix metalloproteinase-13 and Organism(s) Homo sapiens and UniProt Accession P45452

for references in articles please use BRENDA:EC3.4.24.B4
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.B4 matrix metalloproteinase-13
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This record set is specific for:
Homo sapiens
UNIPROT: P45452
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
proteolytic degradation of proteins
Synonyms
mmp-13, mmp13, collagenase-3, matrix metalloproteinase-13, matrix metalloproteinase 13, collagenase 3, mmp13a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
collagenase 3
-
collagenase-3
-
M10.013
Merops-ID
matrix metalloproteinase-13
-
MMP13
collagenase
-
-
collagenase 3
-
-
collagenase-3
-
-
M10.013
-
Merops-ID
matrix metalloproteinase 13
-
-
matrix metalloproteinase-13
-
-
additional information
-
MMP-13 belongs to the collagenase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
preference for cleavage at Gly- or -Leu
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
175449-82-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
show the reaction diagram
-
-
-
?
collagen type II + H2O
?
show the reaction diagram
Mca-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
type II collagen + H2O
?
show the reaction diagram
-
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly-norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly + norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2
show the reaction diagram
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly-Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly + Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
show the reaction diagram
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu + Gly-Leu-Dpa-Ala-Arg-NH2
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GPLGMRGL-NH2 + H2O
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl-GPLGMRSGL-NH2 + H2O
2,4-dinitrophenyl-GPLGM + RSGL-NH2
show the reaction diagram
-
-
-
?
Ac-PLG(S)LLG-OEt thioester + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-PLG-[2-mercapto-4-methyl-pentanoyl]-LG-OC2H5 + H2O
?
show the reaction diagram
-
colorimetric substrate
-
-
?
aggrecan + H2O
?
show the reaction diagram
alpha1-Antichymotrypsin + H2O
?
show the reaction diagram
-
cleavage of peptide bond Ala362-Leu363
-
?
alpha2-antichymotrypsin + H2O
?
show the reaction diagram
-
degradation, cleavage site is Ala362-Leu363
-
?
alpha2-chain of type IV collagen + H2O
?
show the reaction diagram
-
cleavage sites at amino acid residues 881 and 1000 in the triple-helical region
-
?
alpha2-macroglobulin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha4-chain of type IV collagen + H2O
?
show the reaction diagram
-
cleavage site at amino acid residue 86 in the triple-helical region
-
?
beta-casein + H2O
?
show the reaction diagram
-
-
-
?
bovine type B gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type I + H2O
?
show the reaction diagram
collagen type I beta1,2 chain + H2O
collagen type I alpha1,2 chain
show the reaction diagram
-
wild-type enzyme and enzyme fragment 249-451
-
?
collagen type II + H2O
?
show the reaction diagram
Collagen type III + H2O
?
show the reaction diagram
-
5 to 6fold less active compared to substrate collagen type II
-
?
collagen type IV + H2O
?
show the reaction diagram
collagen type IV chain alpha1 + H2O
?
show the reaction diagram
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
collagen type IV chain alpha2 + H2O
?
show the reaction diagram
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
collagen type IX + H2O
?
show the reaction diagram
collagen type VI + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type X + H2O
48 kDa fragment
show the reaction diagram
-
wild-type enzyme and enzyme fragment 249-451
-
?
collagen type X + H2O
?
show the reaction diagram
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
collagen type XIV + H2O
?
show the reaction diagram
decorin + H2O
?
show the reaction diagram
-
-
-
-
?
DP1 Degrading Peptides hydrogel + H2O
?
show the reaction diagram
-
-
-
-
?
DP2 Degrading Peptides hydrogel + H2O
?
show the reaction diagram
-
-
-
-
?
DP3 Degrading Peptides hydrogel + H2O
IKVKIKV + IKVKIKVKV(D)PPTG
show the reaction diagram
-
-
-
-
?
factor XII + H2O
?
show the reaction diagram
-
cleavage site is Gly376-Leu377
-
?
fibrillin-1 + H2O
?
show the reaction diagram
fibrillin-2 + H2O
?
show the reaction diagram
fibrinogen alpha chain + H2O
?
show the reaction diagram
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
fibronectin + H2O
fragments of MW 100 kDa, 43 kDa, 35 kDa, and 29 kDa
show the reaction diagram
-
native and recombinant substrate, whole substrate molecule and fragments, wild-type enzyme and enzyme fragment 249-451
from intact plasma fibronectin
?
GABA-Pro-Cha-Abu-Smc-His-Ala-Dab(5-FAM)-Ala-Lys-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
interstitial collagen type I + H2O
?
show the reaction diagram
-
fibrillar collagen
-
?
interstitial collagen type II + H2O
?
show the reaction diagram
-
fibrillar collagen, best substrate, cleavage sites are Gly906-Leu907, Gly909-Gln910, and Gly912-Ile913
-
?
interstitial collagen type III + H2O
?
show the reaction diagram
-
fibrillar collagen
-
?
KKGCGPLALYG-Dabcyl-Hex + H2O
?
show the reaction diagram
-
-
-
-
?
large tenascin C isoform + H2O
?
show the reaction diagram
Mca-Pro-(cyclohexyl)-Ala-Gly-Nva-His-Ala-Dap-(Dnp)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
MCA-Pro-Cha-Gly-Nva-His-Ala-Dpa-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
perlecan + H2O
?
show the reaction diagram
-
-
-
?
plasminogen activator inhibitor + H2O
?
show the reaction diagram
-
degradation
-
?
plasminogen activator inhibitor 2 + H2O
?
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
serglycin + H2O
?
show the reaction diagram
-
-
-
-
?
syndecan 4 + H2O
?
show the reaction diagram
-
-
-
-
?
TIMP1 + H2O
?
show the reaction diagram
-
-
-
-
?
Transforming growth factor + H2O
?
show the reaction diagram
-
cleavage site at amino acid residue 150 in the latency-associated peptide
-
?
transforming growth factor-beta1 + H2O
?
show the reaction diagram
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
type II collagen + H2O
?
show the reaction diagram
type II gelatin + H2O
?
show the reaction diagram
type III collagen + H2O
?
show the reaction diagram
-
fibrillar type
-
-
?
type-II collagen + H2O
?
show the reaction diagram
-
the osteoarthritic cartilage type-II collagen is preferentially cleaved by the proinflammatory cytokine-induced MMP-13
-
-
?
xylosyltransferase 1 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
type II collagen + H2O
?
show the reaction diagram
-
-
-
?
collagen type II + H2O
?
show the reaction diagram
-
-
-
-
?
fibrillin-1 + H2O
?
show the reaction diagram
-
enzyme affects microfibril organization and integrity, leadint ot loss of normal microfibril function
-
?
fibrillin-2 + H2O
?
show the reaction diagram
-
enzyme affects microfibril organization and integrity, leadint ot loss of normal microfibril function
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
interstitial collagen type I + H2O
?
show the reaction diagram
-
fibrillar collagen
-
?
interstitial collagen type II + H2O
?
show the reaction diagram
-
fibrillar collagen, best substrate, cleavage sites are Gly906-Leu907, Gly909-Gln910, and Gly912-Ile913
-
?
interstitial collagen type III + H2O
?
show the reaction diagram
-
fibrillar collagen
-
?
protein + H2O
peptides
show the reaction diagram
Type I collagen + H2O
?
show the reaction diagram
type II collagen + H2O
?
show the reaction diagram
type II gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
type III collagen + H2O
?
show the reaction diagram
-
fibrillar type
-
-
?
type-II collagen + H2O
?
show the reaction diagram
-
the osteoarthritic cartilage type-II collagen is preferentially cleaved by the proinflammatory cytokine-induced MMP-13
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
three Zn2+ and three Ca2+ ions per crystallographically independent sununit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
-
(2S,3R)-2-[(cyclopropylmethyl)amino]-N1-hydroxy-N4-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-3-methylbutanediamide
-
(2Z,5E)-2-(1,2-benzothiazol-3-ylimino)-5-(2-methoxybenzylidene)-1,3-thiazolidin-4-one
-
(2Z,5E)-2-(1,2-benzothiazol-3-ylimino)-5-(3-methoxybenzylidene)-1,3-thiazolidin-4-one
-
(3S,3'S)-astaxanthin
i.e. 3S,3’S-dihydoxy-beta, beta-carotene-4,4’-dione, active metabolite of some soft drugs, binds to enzyme at or near active site
(E)-2-(4-(2-(biphenyl-4-yl)vinyl)-N-isopropoxyphenylsulfonamido)-N-hydroxyacetamide
-
(R)-2-(4'-(4-chlorobenzyloxy)-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxy-3-methylbutanamide
-
2-(4'-(4-chlorobenzyloxy)-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxyacetamide
-
2-(4'-butoxy-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxyacetamide
-
2-(5-((4-butylphenyl)ethynyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
-
2-(5-(4-ethylphenyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
-
2-(5-(4-fluorophenyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
-
2-(benzo[d]isothiazol-3-ylimino)-5-(4-methoxybenzylidene)thiazolidin-4-one
potent and selective MMP-13 inhibitor
4-([(2-([(3-methoxyphenyl)methyl]carbamoyl)-4-oxo-3H,4H-thieno[2,3-d]pyrimidin-5-yl)methoxy]methyl)benzoic acid
highly potent and selective MMP-13 inhibitor. Compound shows shows more than 2600fold selectivity over the other related metalloenzymes. The disodium salt formulation is well absorbed in all species tested at the oral dose of 10-20 mg/kg. Compound is active in in bovine nasal cartilage explants assay
4-([5-[2-(benzylcarbamoyl)-6-methylpyridin-4-yl]-2H-tetrazol-2-yl]methyl)benzoic acid
-
4-([5-[2-(benzylcarbamoyl)-6-methylpyridin-4-yl]-2H-tetrazol-2-yl]methyl)cyclohexanecarboxylic acid
-
4-([6-[(4-methoxybenzyl)carbamoyl]-4-oxopyrido[3,4-d]pyrimidin-3(4H)-yl]methyl)benzoic acid
-
4-oxo-N-[[40-([[(5-oxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)methyl]sulfonyl]methyl)biphenyl-3-yl]methyl]-3,4-dihydroquinazoline-2-carboxamide
compound exhibits excellent potency and selectivity (greater than 170fold) over MMP1, 2, 3, 7, 8, 9, 10, 12, and 14 and tumor necrosis factor-alpha converting enzyme
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-chloro-4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-chlorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-cyanobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-hydroxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-chlorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-fluoro-3-hydroxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-fluoro-3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-fluoro-3-methylbenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[([3-[(3-methoxybenzyl)carbamoyl]benzoyl]amino)methyl]benzoic acid
-
4-[([3-[2-(3-methoxybenzyl)-2H-tetrazol-5-yl]benzoyl]amino)methyl]benzoic acid
-
4-[([3-[2-(4-methoxybenzyl)-2H-tetrazol-5-yl]benzoyl]amino)methyl]benzoic acid
-
4-[2-([6-fluoro-2-[([[3-(methyloxy)phenyl]methyl]amino)-carbonyl]-4-oxo-3,4-dihydroquinazolin-5-yl]oxy)ethyl]-benzoic acid
inhibitor exhibits excellent potency and selectivity for MMP-13 over other MMPs. No overt toxicity is observed in a preliminary repeat dose oral toxicity study of compound in rats. A single oral dose of the monosodium salt significantly reduces degradation products released from articular cartilage into the joint cavity in a rat MIA model in vivo
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
-
4-[[5-(2-methyl-6-[[3-(propan-2-yloxy)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]cyclohexanecarboxylic acid
-
4-[[5-(2-methyl-6-[[3-(trifluoromethyl)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]benzoic acid
-
4-[[5-(2-[[3-(trifluoromethyl)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]benzoic acid
-
4-[[5-(2-[[4-fluoro-3-(trifluoromethyl)benzyl]carbamoyl]-6-methylpyridin-4-yl)-2H-tetrazol-2-yl]methyl]cyclohexanecarboxylic acid
-
cilostazol
docking-based screening of existing drugs and binding free-energy calculation suggests eltrombopag, cilostazol and domperidone as potential MMP-13 inhibitors
domperidone
docking-based screening of existing drugs and binding free-energy calculation suggests eltrombopag, cilostazol and domperidone as potential MMP-13 inhibitors
eltrombopag
docking-based screening of existing drugs and binding free-energy calculation suggests eltrombopag, cilostazol and domperidone as potential MMP-13 inhibitors
hydroxamic acid inhibitor CGS 27023
hydroxamic acid inhibitor WAY-151693
complex formation with the catalytic fragment of the enzyme
marimastat
the intact peptide backbone scaffold is optimum to fix the inhibitor into the rigid environment of the MMP13 binding site
N,N'-bis(3-methoxybenzyl)benzene-1,3-dicarboxamide
-
N,N'-bis(3-methylbenzyl)pyrimidine-4,6-dicarboxamide
50% inhibition at 72 nM
N,N'-bis(4-fluoro-3-methylbenzyl)pyrimidine-4,6-dicarboxamide
50% inhibition at 8 nM
N,N'-bis(pyridin-3-ylmethyl)pyrimidine-4,6-dicarboxamide
N,N'-dibenzylpyrimidine-4,6-dicarboxamide
50% inhibition at 400 nM
N-(3-methoxybenzyl)-4-oxo-3,4-dihydroquinazoline-2-carboxamide
lead compound for the development of thieno[2,3-d]pyrimidine-2-carboxamide inhibitors
N-hydroxy-2-(N-isopropoxy-4'-(methylthio)biphenyl-4-ylsulfonamido)acetamide
-
N-hydroxy-2-(N-isopropoxy-4'-methoxybiphenyl-4-ylsulfonamido)acetamide
-
N-hydroxy-2-(N-isopropoxy-4-phenoxyphenylsulfonamido)-acetamide
-
N-hydroxy-2-(N-isopropoxy-5-(4-methoxyphenyl)thiophene-2-sulfonamido)acetamide
-
N2,N5-bis(3-methylbenzyl)-6-oxo-1,6-dihydropyrimidine-2,5-dicarboxamide
compound shows about 75fold selectivity over metalloproteases MMP3, MMP12
N2,N5-bis(4-fluoro-3-methylbenzyl)-6-oxo-1,6-dihydropyrimidine-2,5-dicarboxamide
compound shows about 65fold and 47fold selectivity over metalloproteases MMP3, MMP12, respectively
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(2-methylpropyl)glycinamide
-
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)-L-valinamide
-
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
-
N2-(biphenyl-4-ylsulfonyl)-N-hydroxyglycinamide
-
N2-({4'-[(4-chlorobenzyl)oxy]biphenyl-4-yl}sulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
-
(2R)-N,3-dihydroxy-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]propanamide
-
-
(2R)-N-hydroxy-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]-2-(tetrahydro-2H-pyran-4-yl)ethanamide
-
-
(2R)-N-hydroxy-3-methyl-2-[(naphthalen-2-ylsulfonyl)amino]butanamide
-
-
(2R)-N-hydroxy-3-methyl-2-[methyl(naphthalen-2-ylsulfonyl)amino]butanamide
-
-
(2R)-N-hydroxy-4-(4-hydroxyphenyl)-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]butanamide
-
-
(2R)-[1-(tert-butoxycarbonyl)piperidin-4-yl][([5-[4-(dimethylamino)phenyl]thiophen-2-yl]sulfonyl)amino]ethanoic acid
-
-
(2R,3R)-4-[[4-(2-chloro-4-fluorophenoxy)phenyl]sulfonyl]-N,2-dihydroxy-2-methylmorpholine-3-carboxamide
-
-
(2R,4S)-1-((4-[(2-chlorobenzyl)oxy]phenyl)sulfonyl)-N,4-dihydroxypiperidine-2-carboxamide
-
i.e. rTACE, 50% inhibition at 12 nM
(2S,3R)-1-acetyl-N-hydroxy-2-methyl-4-[[4-(2-methylbenzyl)phenyl]sulfonyl]piperidine-3-carboxamide
-
-
(3S)-N,3-dihydroxy-4-[(3'-methylbiphenyl-4-yl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 0.43 nM, not inhibitory to aggrecanase
(3S)-N,3-dihydroxy-4-[(4'-methylbiphenyl-4-yl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 0.39 nM, not inhibitory to aggrecanase
(3S)-N,3-dihydroxy-4-[(4-(2,4-dichlorobenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition of enzyme at 0.95 nM, 50% inhibition of aggrecanase at 8.1 nM
(3S)-N,3-dihydroxy-4-[(4-(2-chlorobenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 2.7 nM
(3S)-N,3-dihydroxy-4-[(4-(3-chlorobenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 2.4 nM
(3S)-N,3-dihydroxy-4-[(4-(3-methylbenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 5 nM
(3S)-N,3-dihydroxy-4-[(4-(4-chlorobenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 0.88 nM, selective for enzyme
(3S)-N,3-dihydroxy-4-[(4-(4-methylbenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 1.3 nM
(4-[[([5-[2-(ethoxycarbonyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]phenyl)acetic acid
-
-
(4R)-1-[4-(4-fluorophenoxy)benzyl]-N-hydroxy-2-oxoimidazolidine-4-carboxamide
-
-
(4S)-4-[4-(4-fluorophenoxy)phenyl]-N-hydroxy-5-oxo-D-prolinamide
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-(1-cyclohexanecarbonyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-(1-iso-propylcarbamoyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2,2-dimethylpropionyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2,2-dimethylpropyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2-methylpropane-1-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(3,3-dimethylbutyryl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(benzenesulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(methane-1-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(phenylmethanesulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(propane-1-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(propane-2-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(tetrahydropyran-4-carbonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-benzylpiperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-iso-butylpiperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-diethylcarbamoylpiperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-iso-butyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-isopropylcarbamoyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-tertbutylcarbamoyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-[1-(benzenesulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-[1-(toluene-4-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(butane-1-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
1,5-anhydro-2,3-dideoxy-3-[[4-(2,4-dichlorophenoxy)phenyl]sulfonyl]-4-C-(hydroxycarbamoyl)-D-threo-pentitol
-
-
1-(4-amino-2-methylquinolin-6-yl)-3-(4-methoxyphenyl)urea
-
-
1-(4-phenoxyphenyl)-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(1-hydroxyethyl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(1-methoxyethyl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(2-methoxyphenyl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(2-phenylethyl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(propan-2-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(pyrazin-2-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(pyridin-2-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(pyridin-4-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(pyrimidin-4-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(6-[4-[4-(4-fluorophenyl)-1,3-oxazol-2-yl]phenoxy]pyridin-3-yl)-1,7,9-triazaspiro[4.5]decane-6,8,10-trione
-
-
1-acetyl-4-hydroxypyrrolidine-2-carboxylic acid
-
binding structure, modelling, overview
1-cyclopropyl-4-[(4-[4-[(1,3-dibenzyl-1,3-dimethyltriazan-2-yl)carbonyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
-
-
1-cyclopropyl-4-[[4-(4-[[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl]piperidin-1-yl)phenyl]sulfonyl]-N-hydroxypiperidine-4-carboxamide
-
-
1-cyclopropyl-N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)piperidine-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
1-cyclopropyl-N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]piperidine-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
1-cyclopropyl-N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]piperidine-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
1-[4-((4-phenoxy)phenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
comparison of selectivity with other matrix metalloproteinases
1-[4-(1,3-benzodioxol-5-yloxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
comparison of selectivity with other matrix metalloproteinases
1-[4-(3-methoxyphenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
comparison of selectivity with other matrix metalloproteinases
1-[4-(4-chlorophenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
comparison of selectivity with other matrix metalloproteinases
2,3-dihydro-1,4-benzodioxine-2-carboxylic acid
-
binding structure, modelling, overview
2,3-dihydro-1,4-benzodioxine-5-carboxylic acid
-
binding structure, modelling, overview
2-(2-[(2-chlorobenzoyl)amino]-1,3-thiazol-4-yl)acetic acid
-
binding structure, modelling, overview
2-(ethyl[[4-(prop-1-yn-1-yloxy)phenyl]sulfonyl]amino)-5-phenylpentane(thioperox)ic O-acid
-
-
2-butanoyl-1H-indole-5-carboxamide
-
-
2-chloro-N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-4-carboxamide
-
-
2-chloro-N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyrimidine-4-carboxamide
-
-
2-fluoro-N-hydroxy-6-([4-[4-(trifluoromethoxy)phenoxy]piperidin-1-yl]sulfonyl)benzamide
-
-
2-fluoroisophthalic acid
-
binding structure, modelling, overview
2-[(4-chlorobenzyl)sulfanyl]-6-methylpyrimidin-4-ol
-
competitive
2-[benzyl[(4-methoxyphenyl)sulfonyl]amino]-N-hydroxy-3,5-dimethylbenzamide
-
WAY- 152177
2-[[(4'-chlorobiphenyl-4-yl)oxy]methyl]-N-hydroxy-4-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)butanamide
-
-
2-[[(4'-cyanobiphenyl-4-yl)oxy]methyl]-N-hydroxy-4-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)butanamide
-
-
2-[[(4'-[[(5-bromo-4-methoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]methyl]-3-methylbutanoic acid
-
-
2-[[[4-(4-chlorophenoxy)phenyl]sulfonyl](methyl)amino]-N-hydroxy-3-[(4-methylpiperazin-1-yl)methyl]benzamide
-
-
3-(carboxymethyl)-2-methylenepentanedioic acid
-
binding structure, modelling, overview
3-[(4-methoxyphenyl)sulfonyl]propane-1-thiol
-
-
3-[(4-phenoxyphenyl)sulfonyl]cyclohexanethiol
-
-
3-[[4-(phenylsulfanyl)phenyl]sulfonyl]cyclohexanethiol
-
-
4'-aminobiphenyl-4-sulfonamide
-
competitive
4-((R)-carboxy-[5-[4'-(2-methoxyethoxy)-phenyl]-thiophene-2-sulfonylamino]-methyl)-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-(2-cyanophenoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-(2-phenylethoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-(3-methoxy-4-nitrophenoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-(3-[3-[3-(3,4-difluorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]prop-2-yn-1-yl]phenyl)butanoic acid
-
-
4-(4-methylphenoxy)-N-(pyridin-3-ylmethyl)benzamide
-
-
4-(4-methylphenoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-(4-methylphenoxy)-N-[2-(pyridin-4-yl)ethyl]benzamide
-
-
4-(4-nitrophenoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-(4-[[(3R)-3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl]ethynyl]phenoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-(4-[[(3R)-3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl]ethynyl]phenoxy)-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-(4-[[(3S)-3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl]ethynyl]phenoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-(4-[[(3S)-3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl]ethynyl]phenoxy)-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-(benzyloxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-([4-[(5-[[4-(dimethylamino)phenyl]amino]-5-oxopentyl)oxy]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([4-[4-(2,4-dimethylphenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(2-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(2-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(2-ethoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(2-fluorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(4'-fluorobiphenyl-2-yl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(4-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(4-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([6-[(4-methoxybenzyl)carbamoyl]-4-oxopyrido[3,4-d]pyrimidin-3(4H)-yl]methyl)benzoic acid
-
a less potent MMP13 inhibitor
4-([[4-(4-chlorophenoxy)phenyl]sulfonyl]methyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([[4-(4-fluorophenoxy)phenyl]sulfonyl]amino)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-methoxy-N,N'-bis(pyridin-3-ylmethyl)benzene-1,3-dicarboxamide
-
competitive
4-methoxy-N-(pyridin-4-ylmethyl)benzamide
-
-
4-phenoxy-N-(pyridin-4-ylmethyl)benzamide
-
-
4-[(4-[3-[(2,2-dimethylpentanoyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[3-[(2,4-dimethylbenzoyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[3-[(cyclohexylcarbonyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[3-[4-(dimethylamino)phenyl]-3-oxopropoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[4-[(1,3-diethenyl-1,3-dimethyltriazan-2-yl)carbonyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[4-[4-(dimethylamino)benzoyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
MMP-13 selective
4-[(4-[4-[4-(dimethylamino)phenyl]-4-oxobutoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[4-[bis(3,5-dimethylpiperidin-1-yl)carbamoyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxy-1-(2-methoxyethyl)piperidine-4-carboxamide
-
-
4-[(R)-(benzofuran-2-sulfonylamino)-carboxy-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-(benzo[b]thiophene-2-sulfonylamino)-carboxy-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-dimethylamino-biphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-ethoxybiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-fluorobiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-methoxybiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-methylbiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(5-phenylthiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(5-pyridin-2-yl-thiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(5-pyridin-4-yl-thiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(3',4'-difluorophenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(3',4'-methylenedioxyphenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(3,4-dimethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(3-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid 1-ethyl-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid 4-tetrahydropyranyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid butyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid cyclohexyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid ethyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
inhibitor of MMP-13 having no activity against MMP-1 (collagenase-1) or tumor necrosis factor-R converting enzyme
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid methyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid neopentyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid propyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-hydroxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-iso-propoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-methylphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid
-
-
4-[(R)-carboxy-[5-(4'-n-propoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid
-
-
4-[(R)-carboxy-[5-(4'-piperidin-1-yl-phenyl)-thiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-piperidin-1-yl-phenyl)-thiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-trifluoromethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-trifluoromethylphenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-trifluoromethylphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-phenylthiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[([[5-(1H-indol-5-yl)-1-methyl-1H-pyrazol-3-yl]carbonyl]amino)methyl]benzoic acid
-
-
4-[2-[4-(4-[[5-(2-ethoxyethyl)-2,4,6-trioxohexahydropyrimidin-5-yl]oxy]phenoxy)phenyl]-1,3-oxazol-4-yl]benzonitrile
-
-
4-[4-(2,6,8,10-tetraoxo-1,7,9-triazaspiro[4.5]dec-1-yl)phenoxy]benzoic acid
-
comparison of selectivity with other matrix metalloproteinases
4-[4-(methylcarbamoyl)phenoxy]-N-(pyridin-4-ylmethyl)benzamide
-
-
4-[4-[(3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl)ethynyl]phenoxy]-N-(pyridin-4-ylmethyl)benzamide
-
-
4-[4-[(3-methoxy-1-azabicyclo[2.2.2]oct-3-yl)ethynyl]phenoxy]-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-[4-[(E)-2-(1-azabicyclo[2.2.2]oct-2-en-3-yl)ethenyl]phenoxy]-N-(pyridin-4-ylmethyl)benzamide
-
-
4-[4-[(E)-2-(1-azabicyclo[2.2.2]oct-2-en-3-yl)ethenyl]phenoxy]-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-[4-[(E)-2-(3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl)ethenyl]phenoxy]-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-[4-[2-(3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl)ethyl]phenoxy]-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-[carboxy-[5-(4-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[carboxy-[5-(6-methoxy-pyridin-3-yl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[[([5-[2-(ethoxycarbonyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]benzoic acid
-
-
4-[[([5-[2-(ethoxymethyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]benzoic acid
-
-
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
4-[[4-(3-[[4-(dimethylamino)benzoyl]amino]propoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[[4-(4-[[1-ethynyl-1,3-dimethyl-3-(prop-2-yn-1-yl)triazan-2-yl]carbonyl]piperidin-1-yl)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[[4-(4-[[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl]piperidin-1-yl)phenyl]sulfonyl]-N-hydroxy-1-(2-methoxyethyl)piperidine-4-carboxamide
-
-
4-[[4-(4-[[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl]piperidin-1-yl)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[[4-(4-[[4-(dimethylamino)phenyl]amino]-4-oxobutoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[[4-([5-[4-(dimethylamino)phenyl]-5-oxopentyl]oxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
MMP-13 selective
4-[[4-oxo-6-(3-phenylprop-1-yn-1-yl)quinazolin-3(4H)-yl]methyl]benzoic acid
-
-
4-[[6-(2-[3-[3-(hydroxyamino)-3-oxopropoxy]phenyl]-1,3-oxazol-5-yl)-4-oxoquinazolin-3(4H)-yl]methyl]benzoic acid
-
-
5-(2-ethoxyethyl)-5-[4-[4-(1,3,4-oxadiazol-2-yl)phenoxy]phenoxy]pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(3,4-difluorobenzyl)-7-methyl-4,6-dioxo-N-[[2-(3-sulfanylpropoxy)pyridin-4-yl]methyl]-3a,4,5,6-tetrahydrothieno[3,2-c]pyridine-2-carboxamide
-
-
5-(4-chlorophenoxy)-5-methylpyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(4-chlorophenyl)-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
5-(5-chloropyridin-2-yl)-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
-
5-hexyl-5-(4-phenoxyphenoxy)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-methyl-5-(4-phenoxyphenoxy)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-[3-[(4-carboxybenzyl)carbamoyl]-1-methyl-1H-pyrazol-5-yl]-1H-indole-2-carboxylic acid
-
-
5-[3-[(acetylamino)methyl]phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
-
5-[4-(1-benzofuran-2-ylmethoxy)phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
-
5-[4-(1H-imidazol-1-yl)phenyl]-4-methyl-1,2-dihydro-3H-pyrazol-3-one
-
-
5-[4-(acetylamino)phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
-
6-hydroxy-2-(methylsulfanyl)-4-pyrimidinecarboxylic acid
-
binding structure, modelling, overview
alendronate
-
inhibits the in vitro invasion and random cell migration, 99% inhibition at 0.4 mM and physiological Ca2+-concentration, 67% inhibition at 0.4 mM and high Ca2+-concentration
ALS 1-0635
-
noncompetitive
-
benzyl 6-benzyl-5,7-dioxo-6,7-dihydro-5H-[1,3]thiazolo[3,2-c]pyrimidine-2-carboxylate
-
competitive, does not ligate the catalytic zinc, zinc binding is unnecessary to achieve nanomolar affinity, extremely selective for inhibition of MMP13 over all other MMPs
bone morphogenetic protein 2
-
down-regulation of enzyme expression in osteoblasts, can be overcome by noggin
-
bone morphogenetic protein 4
-
down-regulation of enzyme expression in osteoblasts, can be overcome by noggin
-
bone morphogenetic protein 6
-
down-regulation of enzyme expression in osteoblasts, can be overcome by noggin
-
CGS027023
-
-
cipemastat
-
-
CL 82198
-
specific inhibitor
CL-82198
-
a specific MMP-13 inhibitor, inhibits also the metastatic activity of chloramphenicol-treated cells
clodronate
-
77% inhibition at 0.4 mM and physiological Ca2+-concentration, 35.7% inhibition at 0.4 mM and high Ca2+-concentration
CP-471474
-
-
ethyl 5-(1-methyl-1H-imidazol-5-yl)-1H-indole-2-carboxylate
-
-
ethyl 5-(1-methyl-3-[[(6-oxo-1,6-dihydropyridin-3-yl)methyl]carbamoyl]-1H-pyrazol-5-yl)-1H-indole-2-carboxylate
-
-
ethyl 5-(3-methylpyridin-4-yl)-1H-indole-2-carboxylate
-
-
ethyl 5-(acetylamino)-1H-indole-2-carboxylate
-
-
ethyl 5-(pyridin-2-yl)-1H-indole-2-carboxylate
-
-
ethyl 5-(pyridin-3-yl)-1H-indole-2-carboxylate
-
-
ethyl 5-(pyridin-4-yl)-1H-indole-2-carboxylate
-
-
ethyl 5-carbamoyl-1H-indole-2-carboxylate
-
-
ethyl 5-phenyl-1H-indole-2-carboxylate
-
-
ethyl 5-[(methylsulfonyl)amino]-1H-indole-2-carboxylate
-
-
ethyl 5-[1-methyl-3-[(pyridin-4-ylmethyl)carbamoyl]-1H-pyrazol-5-yl]-1H-indole-2-carboxylate
-
-
ethyl 5-[3-(methoxycarbonyl)-1-methyl-1H-pyrazol-5-yl]-1H-indole-2-carboxylate
-
-
ethyl 5-[5-methyl-2-[(pyridin-4-ylmethyl)carbamoyl]pyridin-4-yl]-1H-indole-2-carboxylate
-
-
furin
-
inhibition of enzyme induction by TGFbeta1 in chondrocytes
-
hydroxamic acid-based inhibitor CT1399
-
-
-
hydroxamic acid-based inhibitor CT1847
-
-
-
ilomastat
-
a broad-spectrum MMP inhibitor
mannose-6-phosphate/insulin-like growth factor 2 receptor
-
inhibition of enzyme induction by TGFbeta1 in chondrocytes
-
matrix metalloprotease inhibitor GW9471
-
broad spectrum
methyl 3-[4-(1H-imidazol-1-yl)phenyl]propanoate
-
-
methyl 4-[4-(2,6,8,10-tetraoxo-1,7,9-triazaspiro[4.5]dec-1-yl)phenoxy]benzoate
-
comparison of selectivity with other matrix metalloproteinases
minocycline
-
inhibits MMP-13 activity in synoviocytes
N,N'-bis(3-methylbenzyl)pyrimidine-4,6-dicarboxamide
-
extremely selective for inhibition of MMP13 over all other MMPs
N,N'-bis(pyridin-3-ylmethyl)pyrimidine-4,6-dicarboxamide
-
-
N,N-bis(2,6-dimethylmorpholin-4-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis(3,5-dimethylpiperidin-1-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis(4-acetylpiperazin-1-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis(7,8-dimethoxy-3,4-dihydroisoquinolin-2(1H)-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-(2,4-dimethylphenyl)piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-(2-fluorophenyl)piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-(4-acetylphenyl)piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-(4-fluorophenyl)piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-[1-(dimethylamino)ethyl]piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-di(3,4-dihydroisoquinolin-2(1H)-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N-(2-hydroxyethyl)-4-(4-methylphenoxy)benzamide
-
-
N-(3-methoxybenzyl)-4-(4-methylphenoxy)benzamide
-
-
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
-
i.e. PF152, a non-hydroxamic acid and a potent and highly selective MMP-13 inhibitor, that binds the S1' active site pocket of the enzyme and is not a ligand to the catalytic zinc atom
N-(cyclohexylmethyl)-4-(4-methylphenoxy)benzamide
-
-
N-(pyridin-4-ylmethyl)biphenyl-4-carboxamide
-
-
N-([4'-[(1-benzofuran-2-ylcarbonyl)amino]biphenyl-4-yl]sulfonyl)valine
-
-
N-([4'-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-threonine
-
-
N-([4'-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
-
-
N-([4'-[([4-[(1-methoxy-2-methyl-1-oxopropan-2-yl)oxy]-3-methyl-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
-
-
N-([4'-[([4-[(2-carboxypropan-2-yl)oxy]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
-
-
N-benzyl-4-(4-methylphenoxy)benzamide
-
-
N-hydroxy-1-(2-methoxyethyl)-4-([4-[4-(phenylcarbamoyl)piperidin-1-yl]phenyl]sulfonyl)piperidine-4-carboxamide
-
-
N-hydroxy-2,2-dimethyl-4-[[4-(pyridin-4-yloxy)phenyl]sulfonyl]thiomorpholine-3-carboxamide
-
-
N-hydroxy-2,6-dimethoxy-3-[[(4-methoxyphenyl)sulfonyl](pyridin-3-ylmethyl)amino]pyridine-4-carboxamide
-
-
N-hydroxy-2-[(2-methylpropyl)(naphthalen-2-ylsulfonyl)amino]acetamide
-
-
N-hydroxy-2-[(naphthalen-2-ylsulfonyl)amino]acetamide
-
-
N-hydroxy-2-[[(4-methoxyphenyl)sulfonyl](pyridin-3-ylmethyl)amino]-3-methylbenzamide
-
-
N-hydroxy-3-methyl-2-(methyl[[4-(pyridin-4-yloxy)phenyl]sulfonyl]amino)benzamide
-
-
N-hydroxy-3-methyl-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-4-([4-[(4-hydroxybut-2-yn-1-yl)oxy]phenyl]sulfonyl)-2,2-dimethylthiomorpholine-3-carboxamide
-
-
N-hydroxy-4-([4-[4-(2-hydroxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(2-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(3,3,6-trimethoxycyclohexa-1,5-dien-1-yl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(3-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(4,4,6-trimethoxycyclohexa-1,5-dien-1-yl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(4-methoxy-2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(4-methoxyphenoxy)butoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(4-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(naphthalen-1-yl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-oxo-4-(piperidin-1-yl)butoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[(4-[3-[(4-methoxybenzoyl)amino]propoxy]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[(4-[4-[(4-methoxyphenyl)amino]-4-oxobutoxy]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[(4-[4-[2-(trifluoromethyl)phenyl]piperidin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[(4-[4-[2-methoxy-5-(propan-2-yl)phenyl]piperidin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[(4-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[[4-(3-[[4-(trifluoromethoxy)benzoyl]amino]propoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-oxo-4-[[4-(trifluoromethoxy)phenyl]amino]butoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[[4-(4-phenylpiperidin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[[4-(4-[methyl[4-(trifluoromethoxy)phenyl]amino]-4-oxobutoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]-1-(prop-2-yn-1-yl)piperidine-4-carboxamide
-
i.e. SC-276
N-hydroxy-N2-(2-methylpropyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-(2,3,3a,7a-tetrahydro-1-benzofuran-5-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-5-phenyl-D-norvalinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-leucinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-threoninamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-(quinolin-2-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-(quinolin-3-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-(quinolin-6-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-[(6-propoxynaphthalen-2-yl)sulfonyl]-D-valinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-[[6-(2-methylpropoxy)naphthalen-2-yl]sulfonyl]-D-valinamide
-
-
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(2-phenylethyl)-D-valinamide
-
-
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(3-phenylpropyl)-D-valinamide
-
-
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(pyridin-2-ylmethyl)-D-valinamide
-
-
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(pyridin-3-ylmethyl)-D-valinamide
-
-
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(pyridin-4-ylmethyl)-D-valinamide
-
-
N-hydroxy-N2-methyl-3-[(4-phenoxyphenyl)sulfonyl]-L-alaninamide
-
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-(pyridin-4-ylmethyl)valinamide
-
-
N-hydroxy-N2-[(6-hydroxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-hydroxy-N2-[(6-methoxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-hydroxy-N2-[(7-hydroxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-hydroxy-N2-[(7-methoxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-hydroxy-N2-[2-(morpholin-4-yl)ethyl]-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-N2-[[6-(3-methylbutoxy)naphthalen-2-yl]sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-methyl-4-(4-methylphenoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
N-methyl-4-(4-methylphenoxy)benzamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(3-[[(furan-2-ylcarbonyl)amino]methyl]phenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-ethoxyphenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-methoxyphenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-methylphenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-phenoxyphenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[3-([[(2-methylfuran-3-yl)carbonyl]amino]methyl)phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(1H-pyrazol-3-ylmethoxy)phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(methylcarbamoyl)phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(methylsulfamoyl)phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(1,5-dimethyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(1-methyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(5-methyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(6-methylpyridin-2-yl)methoxy]phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(methylsulfonyl)amino]phenyl]furan-2-carboxamide
-
-
N-[(4'-[[(3,4-dimethyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(3-methyl-4-phenoxy-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(3-methyl-4-phenyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-amino-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-cyano-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-ethenyl-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-ethoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-ethyl-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-hydroxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-methoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4-[5-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]pyridin-2-yl]phenyl)sulfonyl]-L-threonine
-
replacing a backbone benzene with a pyridine and valine with threonine results in greatly reduced plasma protein binding of the compound
N-[(4-[5-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]pyridin-2-yl]phenyl)sulfonyl]-L-valine
-
-
N-[2-(4,5-dihydro-1,3-oxazol-2-yl)-1H-indol-5-yl]acetamide
-
-
N-[2-(4-[benzyl[2-(hydroxycarbamoyl)-4,6-dimethylphenyl]sulfamoyl]phenoxy)ethyl]-1-benzofuran-2-carboxamide
-
WAY-170523
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1,5-dimethyl-1H-pyrazole-3-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-imidazole-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-pyrazole-3-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-pyrazole-4-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-methyl-1,3-thiazole-4-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-3-methylfuran-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-3-methylpyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-5-ethylpyridine-3-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-5-methylfuran-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-methylpyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-7-methylimidazo[1,2-a]pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-8-methylimidazo[1,2-a]pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]imidazo[1,2-a]pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-3-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-4-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyrimidine-4-carboxamide
-
-
N-[3-(5-[[1-cyclopropyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[1-cyclopropyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[3-(5-[[2-(methylamino)-2-oxo-1-(tetrahydro-2H-pyran-4-yl)ethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[2-(methylamino)-2-oxo-1-(tetrahydro-2H-pyran-4-yl)ethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[3-(5-[[3-hydroxy-3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[3-hydroxy-3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[3-(5-[[3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[3-(dimethylamino)propyl]-4-(4-methylphenoxy)benzamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-1-benzofuran-2-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-1-methyl-1H-pyrazole-3-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-4,5-dimethylfuran-2-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-5-methyl-1H-pyrazole-3-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-5-methylfuran-2-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-6-methylpyridine-2-carboxamide
-
-
N-[4-(morpholin-4-yl)butyl]-1-benzofuran-2-carboxamide
-
i.e. CL-82198
N-[[(3-phenyl-1,2-oxazol-5-yl)methyl]carbamothioyl]benzamide
-
competitive, is synergic with acetohydroxamic acid
N-[[4'-([[3-methyl-4-(methylamino)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[3-methyl-4-(morpholin-4-yl)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[3-methyl-4-(prop-1-yn-1-yl)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(3-hydroxypropyl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(3-methoxypropyl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(acetylamino)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(dimethylamino)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(furan-2-yl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4-(4-fluorophenoxy)phenyl]sulfonyl]-N-[1-(hydroxycarbamoyl)cyclopentyl]-b-alanine
-
-
N-[[4-(5-[[(4-cyano-3-methyl-1-benzofuran-2-yl)carbonyl]amino]pyridin-2-yl)phenyl]sulfonyl]-L-valine
-
-
N2-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-(3a,7a-dihydro-1-benzothiophen-5-ylsulfonyl)-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-benzyl-N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
-
-
N2-ethyl-1H-indole-2,5-dicarboxamide
-
-
N2-[(2S)-2-[[(4-benzylbenzyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl]-N,3-dimethyl-L-valinamide
-
-
N2-[(2S)-2-[[(4-benzylbenzyl)(hydroxy)phosphoryl]methyl]-6-phenoxyhexanoyl]-N,3-dimethyl-L-valinamide
-
-
N2-[(3,4-dimethoxyphenyl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-[(4'-bromobiphenyl-4-yl)sulfonyl]-N-hydroxy-D-valinamide
-
-
N2-[(6-ethoxynaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-[(6-ethylnaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-[(7-ethoxynaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-[2-(dimethylamino)ethyl]-N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
-
-
N2-[[6-(benzyloxy)naphthalen-2-yl]sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
O-tert-butyl-N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-serinamide
-
-
P53
-
down-regulation of enzyme expression, possibly contributes to the dysregulation of the enzyme observed in cancer
PD-331179
-
-
Ro32-3555
-
a broad-spectrum MMP inhibitor
RS 102,481
-
a small molecule preferential inhibitor of MMP13, the compound is able to potently inhibit the release of type II collagen degradation peptides from human osteoarthritis articular cartilage explants
SC-276
-
-
tissue matrix metalloproteinase inhibitor fragments of TIMP-1
-
-
-
tissue matrix metalloproteinase inhibitor fragments of TIMP-2
-
-
-
tissue matrix metalloproteinase inhibitor hybrid N.TIMP-1/C.TIMP-2
-
complex formation is not affected by the C-terminal domain of the enzyme, inhibition mechanism, wild-type enzyme and enzyme fragment 249-451
-
tissue matrix metalloproteinase inhibitor TIMP-1
-
tissue matrix metalloproteinase inhibitor TIMP-2
-
tissue matrix metalloproteinase inhibitor TIMP-3
-
tissue matrix metalloproteinase inhibitor-1
-
in a ratio of enzyme to inhibitor of 1:1
-
tissue matrix metalloproteinase inhibitor-2
-
in a ratio of enzyme to inhibitor of 1:1
-
tissue matrix metalloproteinase inhibitor-3
-
fast inhibition, in a ratio of enzyme to inhibitor of 1:1
-
transforming growth factor-beta1
-
i.e. TGFbeta1, accelerates the decay of the enzymes mRNA and decreased enzyme expression in osteoblasts
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12-O-tetradecanoyl phorbol 13-acetate
-
8fold activation of transcriptional activity in chondrocytes
amino phenylmercuric acetate
-
activation
hepatocyte growth factor
-
stimulation of enzyme expression in osteoarthritic chondrocytes
-
integrins
-
e.g. integrin alpha1beta and alpha2beta1, induction via MAPkinase
-
interleukin-1
-
alpha and beta form, induction of enzyme expression, which is inhibited by 15-deoxy-DELTA12,14-prostaglandin J2, induction of enzyme expression in chondrosarcoma cells requires nuclear factor-kappaB nuclear translocation, p38 MAPkinase activity, c-Jun N-terminal kinase activity
-
interleukin-1beta
-
activates, hyaluronan inhibits interleukin-1beta-stimulated MMP-13 via CD44 in arthritic chondrocytes
-
oncostatin
-
induction of enzyme expression, requires phosphorylation of JAK3
-
p-aminophenylmercuric acetate
-
purified proMMP-13 is activated using 1 mM amino phenyl mercuric acid for 20 h at 35°C
Smad
-
indirect stimulation via regulation of transforming growth factor-beta responsive genes
-
stromelysin-1
-
concentration-dependent activation by cleavage of the proform
-
transforming growth factor-beta
-
enhances MMP-13 expression
-
transforming growth factor-beta1
-
strong induction of enzyme expression in KMST fibroblasts, increase of enzyme expression by inhibition of p38 mitose-activated protein kinase
-
Tumor necrosis factor alpha
-
induction of enzyme expression, which is inhibited by 15-deoxy-DELTA12,14-prostaglandin J2
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005
(2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
or above, pH not specified in the publication, temperature not specified in the publication
0.0029
(2S,3R)-2-[(cyclopropylmethyl)amino]-N1-hydroxy-N4-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-3-methylbutanediamide
or above, pH not specified in the publication, temperature not specified in the publication
0.0000223
4-([5-[2-(benzylcarbamoyl)-6-methylpyridin-4-yl]-2H-tetrazol-2-yl]methyl)benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000313
4-([5-[2-(benzylcarbamoyl)-6-methylpyridin-4-yl]-2H-tetrazol-2-yl]methyl)cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000036
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000075
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000434
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.00000026
4-[(5-[2-[(3-chloro-4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000181
4-[(5-[2-[(3-chlorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000067
4-[(5-[2-[(3-cyanobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000286
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000221
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000759
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000015
4-[(5-[2-[(3-hydroxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.00000018
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.00000016
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000021
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.000227
4-[(5-[2-[(4-chlorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000014
4-[(5-[2-[(4-fluoro-3-hydroxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000003
4-[(5-[2-[(4-fluoro-3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.00000022
4-[(5-[2-[(4-fluoro-3-methylbenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000053
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000044
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000653
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000044
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000042
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000367
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000015
4-[[5-(2-methyl-6-[[3-(propan-2-yloxy)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000025
4-[[5-(2-methyl-6-[[3-(trifluoromethyl)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000165
4-[[5-(2-[[3-(trifluoromethyl)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.00000062
4-[[5-(2-[[4-fluoro-3-(trifluoromethyl)benzyl]carbamoyl]-6-methylpyridin-4-yl)-2H-tetrazol-2-yl]methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000019
hydroxamic acid inhibitor CGS 27023
pH 6.8
0.0000003
marimastat
pH not specified in the publication, temperature not specified in the publication
0.0000005
matrix metalloprotease inhibitor GW9471
-
37°C, recombinant enzyme
0.0000058
N-hydroxy-2-(N-isopropoxy-4'-methoxybiphenyl-4-ylsulfonamido)acetamide
pH not specified in the publication, 25°C
0.0000015
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)-L-valinamide
pH not specified in the publication, 25°C
0.00002
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
pH not specified in the publication, 25°C
0.0000015
N2-(biphenyl-4-ylsulfonyl)-N-hydroxyglycinamide
pH not specified in the publication, 25°C
0.0000082
N2-({4'-[(4-chlorobenzyl)oxy]biphenyl-4-yl}sulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
pH not specified in the publication, 25°C
0.0000047
1-(4-phenoxyphenyl)-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
-
0.00000033
1-[4-((4-phenoxy)phenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
-
0.0000058
1-[4-(1,3-benzodioxol-5-yloxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
-
0.0000019
1-[4-(3-methoxyphenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
-
0.00000095
1-[4-(4-chlorophenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
-
0.00000028
4-([[4-(4-chlorophenoxy)phenyl]sulfonyl]methyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH 7.5
0.0000005
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
pH 7.5
0.0000027
4-[4-(2,6,8,10-tetraoxo-1,7,9-triazaspiro[4.5]dec-1-yl)phenoxy]benzoic acid
-
-
0.00000127
4-[carboxy-[5-(4-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
pH 7.5
0.00000078
ALS 1-0635
-
pH not specified in the publication, temperature not specified in the publication
-
0.00000019
cipemastat
-
pH 7.5
0.0000042
methyl 4-[4-(2,6,8,10-tetraoxo-1,7,9-triazaspiro[4.5]dec-1-yl)phenoxy]benzoate
-
-
0.0000015
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
0.00000003
N-hydroxy-2,2-dimethyl-4-[[4-(pyridin-4-yloxy)phenyl]sulfonyl]thiomorpholine-3-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
(2Z,5E)-2-(1,2-benzothiazol-3-ylimino)-5-(2-methoxybenzylidene)-1,3-thiazolidin-4-one
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
(2Z,5E)-2-(1,2-benzothiazol-3-ylimino)-5-(3-methoxybenzylidene)-1,3-thiazolidin-4-one
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.000041
(E)-2-(4-(2-(biphenyl-4-yl)vinyl)-N-isopropoxyphenylsulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000003
(R)-2-(4'-(4-chlorobenzyloxy)-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxy-3-methylbutanamide
Homo sapiens
pH not specified in the publication, 25°C
0.000019
2-(4'-(4-chlorobenzyloxy)-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000015
2-(4'-butoxy-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.00026
2-(5-((4-butylphenyl)ethynyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000091
2-(5-(4-ethylphenyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.0006
2-(5-(4-fluorophenyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000036
2-(benzo[d]isothiazol-3-ylimino)-5-(4-methoxybenzylidene)thiazolidin-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0000000069
4-([(2-([(3-methoxyphenyl)methyl]carbamoyl)-4-oxo-3H,4H-thieno[2,3-d]pyrimidin-5-yl)methoxy]methyl)benzoic acid
Homo sapiens
pH 7.5, 37°C
0.000071
4-oxo-N-[[40-([[(5-oxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)methyl]sulfonyl]methyl)biphenyl-3-yl]methyl]-3,4-dihydroquinazoline-2-carboxamide
Homo sapiens
pH 7.5, 37°C
0.0017
4-[([3-[(3-methoxybenzyl)carbamoyl]benzoyl]amino)methyl]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00053
4-[([3-[2-(3-methoxybenzyl)-2H-tetrazol-5-yl]benzoyl]amino)methyl]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00013
4-[([3-[2-(4-methoxybenzyl)-2H-tetrazol-5-yl]benzoyl]amino)methyl]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000000039
4-[2-([6-fluoro-2-[([[3-(methyloxy)phenyl]methyl]amino)-carbonyl]-4-oxo-3,4-dihydroquinazolin-5-yl]oxy)ethyl]-benzoic acid
Homo sapiens
pH 7.5, 37°C
0.00000067
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000012
N-(3-methoxybenzyl)-4-oxo-3,4-dihydroquinazoline-2-carboxamide
Homo sapiens
pH 7.5, 37°C
0.0000072
N-hydroxy-2-(N-isopropoxy-4'-(methylthio)biphenyl-4-ylsulfonamido)acetamide
Homo sapiens
pH not specified in the publication, 25°C
0.00001
N-hydroxy-2-(N-isopropoxy-4'-methoxybiphenyl-4-ylsulfonamido)acetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000063
N-hydroxy-2-(N-isopropoxy-4-phenoxyphenylsulfonamido)-acetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000025
N-hydroxy-2-(N-isopropoxy-5-(4-methoxyphenyl)thiophene-2-sulfonamido)acetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000096
N2,N5-bis(3-methylbenzyl)-6-oxo-1,6-dihydropyrimidine-2,5-dicarboxamide
Homo sapiens
pH 7.5, 22°C
0.000068
N2,N5-bis(4-fluoro-3-methylbenzyl)-6-oxo-1,6-dihydropyrimidine-2,5-dicarboxamide
Homo sapiens
pH 7.5, 22°C
0.000039
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(2-methylpropyl)glycinamide
Homo sapiens
pH not specified in the publication, 25°C
0.000045
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
Homo sapiens
pH not specified in the publication, 25°C
0.0000028
N2-(biphenyl-4-ylsulfonyl)-N-hydroxyglycinamide
Homo sapiens
pH not specified in the publication, 25°C
0.0000013
(2R)-N,3-dihydroxy-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]propanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000012
(2R)-N-hydroxy-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]-2-(tetrahydro-2H-pyran-4-yl)ethanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000033
(2R)-N-hydroxy-3-methyl-2-[(naphthalen-2-ylsulfonyl)amino]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000029
(2R)-N-hydroxy-3-methyl-2-[methyl(naphthalen-2-ylsulfonyl)amino]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000028
(2R)-N-hydroxy-4-(4-hydroxyphenyl)-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000003
(2R)-[1-(tert-butoxycarbonyl)piperidin-4-yl][([5-[4-(dimethylamino)phenyl]thiophen-2-yl]sulfonyl)amino]ethanoic acid
Homo sapiens
-
pH 7.5
0.00000095
(2R,3R)-4-[[4-(2-chloro-4-fluorophenoxy)phenyl]sulfonyl]-N,2-dihydroxy-2-methylmorpholine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000003
(2S,3R)-1-acetyl-N-hydroxy-2-methyl-4-[[4-(2-methylbenzyl)phenyl]sulfonyl]piperidine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000003
(4-[[([5-[2-(ethoxycarbonyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]phenyl)acetic acid
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.000003
(4R)-1-[4-(4-fluorophenoxy)benzyl]-N-hydroxy-2-oxoimidazolidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000007
(4S)-4-[4-(4-fluorophenoxy)phenyl]-N-hydroxy-5-oxo-D-prolinamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000009
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-(1-cyclohexanecarbonyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.0000008
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-(1-iso-propylcarbamoyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.000008
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2,2-dimethylpropionyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.000049
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2,2-dimethylpropyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000055
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2-methylpropane-1-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000036
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(3,3-dimethylbutyryl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000007
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(benzenesulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000127
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(methane-1-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000007
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(phenylmethanesulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000069
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(propane-1-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.000004
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(propane-2-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000017
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(tetrahydropyran-4-carbonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000076
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-benzylpiperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.000028
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-iso-butylpiperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000028
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-diethylcarbamoylpiperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.000016
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-iso-butyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.0000016
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-isopropylcarbamoyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.0000014
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-tertbutylcarbamoyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.0000012
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-[1-(benzenesulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000014
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-[1-(toluene-4-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000047
(R)-[5-(4-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(butane-1-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000009
1,5-anhydro-2,3-dideoxy-3-[[4-(2,4-dichlorophenoxy)phenyl]sulfonyl]-4-C-(hydroxycarbamoyl)-D-threo-pentitol
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000033
1-(4-phenoxyphenyl)-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000036
1-(6-[4-[4-(4-fluorophenyl)-1,3-oxazol-2-yl]phenoxy]pyridin-3-yl)-1,7,9-triazaspiro[4.5]decane-6,8,10-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000045
2-(ethyl[[4-(prop-1-yn-1-yloxy)phenyl]sulfonyl]amino)-5-phenylpentane(thioperox)ic O-acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.5
2-butanoyl-1H-indole-5-carboxamide
Homo sapiens
-
IC50 above 0.5 mM, in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.000027
2-chloro-N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000003
2-chloro-N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000122
2-fluoro-N-hydroxy-6-([4-[4-(trifluoromethoxy)phenoxy]piperidin-1-yl]sulfonyl)benzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000015
2-[benzyl[(4-methoxyphenyl)sulfonyl]amino]-N-hydroxy-3,5-dimethylbenzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000000016
2-[[(4'-chlorobiphenyl-4-yl)oxy]methyl]-N-hydroxy-4-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)butanamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000002
2-[[(4'-cyanobiphenyl-4-yl)oxy]methyl]-N-hydroxy-4-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)butanamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000018
2-[[(4'-[[(5-bromo-4-methoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]methyl]-3-methylbutanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000008
2-[[[4-(4-chlorophenoxy)phenyl]sulfonyl](methyl)amino]-N-hydroxy-3-[(4-methylpiperazin-1-yl)methyl]benzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000009
4-((R)-carboxy-[5-[4'-(2-methoxyethoxy)-phenyl]-thiophene-2-sulfonylamino]-methyl)-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000018
4-([4-[(5-[[4-(dimethylamino)phenyl]amino]-5-oxopentyl)oxy]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00000672
4-([6-[(4-methoxybenzyl)carbamoyl]-4-oxopyrido[3,4-d]pyrimidin-3(4H)-yl]methyl)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000003
4-([[4-(4-chlorophenoxy)phenyl]sulfonyl]methyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH 7.5
0.0000005 - 0.00000075
4-([[4-(4-fluorophenoxy)phenyl]sulfonyl]amino)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
0.0000082
4-[(4-[3-[(2,2-dimethylpentanoyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
4-[(4-[3-[(2,4-dimethylbenzoyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000082
4-[(4-[3-[(cyclohexylcarbonyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000009
4-[(4-[3-[4-(dimethylamino)phenyl]-3-oxopropoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
4-[(4-[4-[4-(dimethylamino)benzoyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
4-[(4-[4-[4-(dimethylamino)phenyl]-4-oxobutoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.001325
4-[(R)-(benzofuran-2-sulfonylamino)-carboxy-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000145
4-[(R)-(benzo[b]thiophene-2-sulfonylamino)-carboxy-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000003
4-[(R)-carboxy-(4'-dimethylamino-biphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000005
4-[(R)-carboxy-(4'-ethoxybiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000024
4-[(R)-carboxy-(4'-fluorobiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000005
4-[(R)-carboxy-(4'-methoxybiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000007
4-[(R)-carboxy-(4'-methylbiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000068
4-[(R)-carboxy-(5-phenylthiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000018
4-[(R)-carboxy-(5-pyridin-2-yl-thiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.00009
4-[(R)-carboxy-(5-pyridin-4-yl-thiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.009
4-[(R)-carboxy-[5-(3',4'-difluorophenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000197
4-[(R)-carboxy-[5-(3',4'-methylenedioxyphenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000575
4-[(R)-carboxy-[5-(3,4-dimethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.001058
4-[(R)-carboxy-[5-(3-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000004
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid 1-ethyl-propyl ester
Homo sapiens
-
pH 7.5
0.0000004
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid 4-tetrahydropyranyl ester
Homo sapiens
-
pH 7.5
0.0000008
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid butyl ester
Homo sapiens
-
pH 7.5
0.0000005
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid cyclohexyl ester
Homo sapiens
-
pH 7.5
0.000002
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid ethyl ester
Homo sapiens
-
pH 7.5
0.0000006
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-butyl ester
Homo sapiens
-
pH 7.5
0.0000005
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000035
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid methyl ester
Homo sapiens
-
pH 7.5
0.0000009
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid neopentyl ester
Homo sapiens
-
pH 7.5
0.000001
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid propyl ester
Homo sapiens
-
pH 7.5
0.0000006
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000033
4-[(R)-carboxy-[5-(4'-hydroxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.000004
4-[(R)-carboxy-[5-(4'-iso-propoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000006
4-[(R)-carboxy-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000013
4-[(R)-carboxy-[5-(4'-methylphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.000011
4-[(R)-carboxy-[5-(4'-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid
Homo sapiens
-
pH 7.5
0.0000008
4-[(R)-carboxy-[5-(4'-n-propoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid
Homo sapiens
-
pH 7.5
0.0000013
4-[(R)-carboxy-[5-(4'-piperidin-1-yl-phenyl)-thiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.00000075
4-[(R)-carboxy-[5-(4'-piperidin-1-yl-phenyl)-thiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000022
4-[(R)-carboxy-[5-(4'-trifluoromethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000615
4-[(R)-carboxy-[5-(4'-trifluoromethylphenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000039
4-[(R)-carboxy-[5-(4'-trifluoromethylphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000121
4-[(R)-carboxy-[5-phenylthiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.026
4-[([[5-(1H-indol-5-yl)-1-methyl-1H-pyrazol-3-yl]carbonyl]amino)methyl]benzoic acid
Homo sapiens
-
IC50 above 0.026 mM; in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00000036
4-[2-[4-(4-[[5-(2-ethoxyethyl)-2,4,6-trioxohexahydropyrimidin-5-yl]oxy]phenoxy)phenyl]-1,3-oxazol-4-yl]benzonitrile
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000019
4-[carboxy-[5-(4-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.00005
4-[carboxy-[5-(6-methoxy-pyridin-3-yl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000001
4-[[([5-[2-(ethoxycarbonyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]benzoic acid
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00025
4-[[([5-[2-(ethoxymethyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]benzoic acid
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00000067
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000016
4-[[4-(3-[[4-(dimethylamino)benzoyl]amino]propoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000017
4-[[4-(4-[[4-(dimethylamino)phenyl]amino]-4-oxobutoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000004
4-[[4-([5-[4-(dimethylamino)phenyl]-5-oxopentyl]oxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00000154
4-[[4-oxo-6-(3-phenylprop-1-yn-1-yl)quinazolin-3(4H)-yl]methyl]benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00001
5-(2-ethoxyethyl)-5-[4-[4-(1,3,4-oxadiazol-2-yl)phenoxy]phenoxy]pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00039
5-(4-chlorophenoxy)-5-methylpyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00043
5-(4-chlorophenyl)-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000245
5-(5-chloropyridin-2-yl)-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000078
5-hexyl-5-(4-phenoxyphenoxy)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000065
5-methyl-5-(4-phenoxyphenoxy)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.025
5-[3-[(4-carboxybenzyl)carbamoyl]-1-methyl-1H-pyrazol-5-yl]-1H-indole-2-carboxylic acid
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.0033
5-[3-[(acetylamino)methyl]phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000006
5-[4-(1-benzofuran-2-ylmethoxy)phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00155
5-[4-(acetylamino)phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00003
benzyl 6-benzyl-5,7-dioxo-6,7-dihydro-5H-[1,3]thiazolo[3,2-c]pyrimidine-2-carboxylate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000012
CGS027023
Homo sapiens
-
pH and temperature not specified in the publication
0.0000035
cipemastat
Homo sapiens
-
pH 7.5
0.0025
ethyl 5-(1-methyl-1H-imidazol-5-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00012
ethyl 5-(1-methyl-3-[[(6-oxo-1,6-dihydropyridin-3-yl)methyl]carbamoyl]-1H-pyrazol-5-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.0096
ethyl 5-(3-methylpyridin-4-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.031
ethyl 5-(acetylamino)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.5
ethyl 5-(pyridin-2-yl)-1H-indole-2-carboxylate
Homo sapiens
-
IC50 above 0.5 mM, in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.015
ethyl 5-(pyridin-3-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.082
ethyl 5-(pyridin-4-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.039
ethyl 5-carbamoyl-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.5
ethyl 5-phenyl-1H-indole-2-carboxylate
Homo sapiens
-
IC50 above 0.5 mM, in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.097
ethyl 5-[(methylsulfonyl)amino]-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00009
ethyl 5-[1-methyl-3-[(pyridin-4-ylmethyl)carbamoyl]-1H-pyrazol-5-yl]-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.0024
ethyl 5-[3-(methoxycarbonyl)-1-methyl-1H-pyrazol-5-yl]-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00015
ethyl 5-[5-methyl-2-[(pyridin-4-ylmethyl)carbamoyl]pyridin-4-yl]-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.0000066 - 0.000008
N,N'-bis(pyridin-3-ylmethyl)pyrimidine-4,6-dicarboxamide
0.0000012 - 0.000002
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
0.0000013
N-([4'-[(1-benzofuran-2-ylcarbonyl)amino]biphenyl-4-yl]sulfonyl)valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000013
N-([4'-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-threonine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000013
N-([4'-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000025
N-([4'-[([4-[(1-methoxy-2-methyl-1-oxopropan-2-yl)oxy]-3-methyl-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000149
N-([4'-[([4-[(2-carboxypropan-2-yl)oxy]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000047
N-hydroxy-2,6-dimethoxy-3-[[(4-methoxyphenyl)sulfonyl](pyridin-3-ylmethyl)amino]pyridine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000008
N-hydroxy-2-[(2-methylpropyl)(naphthalen-2-ylsulfonyl)amino]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00018
N-hydroxy-2-[(naphthalen-2-ylsulfonyl)amino]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
N-hydroxy-2-[[(4-methoxyphenyl)sulfonyl](pyridin-3-ylmethyl)amino]-3-methylbenzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000004
N-hydroxy-3-methyl-2-(methyl[[4-(pyridin-4-yloxy)phenyl]sulfonyl]amino)benzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000034
N-hydroxy-3-methyl-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
N-hydroxy-4-([4-[(4-hydroxybut-2-yn-1-yl)oxy]phenyl]sulfonyl)-2,2-dimethylthiomorpholine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000009
N-hydroxy-4-([4-[4-(4-methoxyphenoxy)butoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000012
N-hydroxy-4-([4-[4-oxo-4-(piperidin-1-yl)butoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000016
N-hydroxy-4-[(4-[3-[(4-methoxybenzoyl)amino]propoxy]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000003
N-hydroxy-4-[(4-[4-[(4-methoxyphenyl)amino]-4-oxobutoxy]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00000066
N-hydroxy-4-[[4-(3-[[4-(trifluoromethoxy)benzoyl]amino]propoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
N-hydroxy-4-[[4-(4-oxo-4-[[4-(trifluoromethoxy)phenyl]amino]butoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000033
N-hydroxy-4-[[4-(4-[methyl[4-(trifluoromethoxy)phenyl]amino]-4-oxobutoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]-1-(prop-2-yn-1-yl)piperidine-4-carboxamide
Homo sapiens
-
IC50 below 1 nM, pH and temperature not specified in the publication
0.000007
N-hydroxy-N2-(2-methylpropyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000006
N-hydroxy-N2-(3-methylbutyl)-N2-(2,3,3a,7a-tetrahydro-1-benzofuran-5-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000026
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-5-phenyl-D-norvalinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000006
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000032
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-threoninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000003
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0001
N-hydroxy-N2-(3-methylbutyl)-N2-(quinolin-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000361
N-hydroxy-N2-(3-methylbutyl)-N2-(quinolin-3-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000012
N-hydroxy-N2-(3-methylbutyl)-N2-(quinolin-6-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00001
N-hydroxy-N2-(3-methylbutyl)-N2-[(6-propoxynaphthalen-2-yl)sulfonyl]-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000013
N-hydroxy-N2-(3-methylbutyl)-N2-[[6-(2-methylpropoxy)naphthalen-2-yl]sulfonyl]-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000002
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(2-phenylethyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000024
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(3-phenylpropyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000022
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(pyridin-2-ylmethyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000015
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(pyridin-3-ylmethyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000007
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(pyridin-4-ylmethyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000004
N-hydroxy-N2-methyl-3-[(4-phenoxyphenyl)sulfonyl]-L-alaninamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000001
N-hydroxy-N2-[(6-hydroxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000013
N-hydroxy-N2-[(6-methoxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000242
N-hydroxy-N2-[(7-hydroxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00048
N-hydroxy-N2-[(7-methoxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000018
N-hydroxy-N2-[2-(morpholin-4-yl)ethyl]-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000176
N-hydroxy-N2-[[6-(3-methylbutoxy)naphthalen-2-yl]sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000075
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(3-[[(furan-2-ylcarbonyl)amino]methyl]phenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000032
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-ethoxyphenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00022
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-methoxyphenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00029
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-methylphenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.05
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-phenoxyphenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00033
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[3-([[(2-methylfuran-3-yl)carbonyl]amino]methyl)phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000006
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(1H-pyrazol-3-ylmethoxy)phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.006
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(methylcarbamoyl)phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00048
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(methylsulfamoyl)phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000004
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(1,5-dimethyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000025
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(1-methyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000002
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(5-methyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00004
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(6-methylpyridin-2-yl)methoxy]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00046
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(methylsulfonyl)amino]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000048
N-[(4'-[[(3,4-dimethyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000019
N-[(4'-[[(3-methyl-4-phenoxy-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000015
N-[(4'-[[(3-methyl-4-phenyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000043
N-[(4'-[[(4-amino-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000037
N-[(4'-[[(4-cyano-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000061
N-[(4'-[[(4-ethenyl-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000074
N-[(4'-[[(4-ethoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000023
N-[(4'-[[(4-ethyl-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000061
N-[(4'-[[(4-hydroxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000095
N-[(4'-[[(4-methoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000035
N-[(4-[5-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]pyridin-2-yl]phenyl)sulfonyl]-L-threonine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00004
N-[(4-[5-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]pyridin-2-yl]phenyl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.22
N-[2-(4,5-dihydro-1,3-oxazol-2-yl)-1H-indol-5-yl]acetamide
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.000017
N-[2-(4-[benzyl[2-(hydroxycarbamoyl)-4,6-dimethylphenyl]sulfamoyl]phenoxy)ethyl]-1-benzofuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000072
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1,5-dimethyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00031
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-imidazole-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00014
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-pyrazole-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000007
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000008
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-methyl-1,3-thiazole-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00018
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-3-methylfuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-3-methylpyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000029
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-5-ethylpyridine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000011
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-5-methylfuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000009
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000004
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-methylpyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00014
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-7-methylimidazo[1,2-a]pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00011
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-8-methylimidazo[1,2-a]pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]imidazo[1,2-a]pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000008
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000042
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000031
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00001
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000036
N-[3-(5-[[1-cyclopropyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000028
N-[3-(5-[[1-cyclopropyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000002
N-[3-(5-[[2-(methylamino)-2-oxo-1-(tetrahydro-2H-pyran-4-yl)ethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000002
N-[3-(5-[[2-(methylamino)-2-oxo-1-(tetrahydro-2H-pyran-4-yl)ethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000005
N-[3-(5-[[3-hydroxy-3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000025
N-[3-(5-[[3-hydroxy-3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000009
N-[3-(5-[[3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000006
N-[3-(5-[[3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00062
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-1-benzofuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000031
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-1-methyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000063
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-4,5-dimethylfuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000088
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-5-methyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000057
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-5-methylfuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000017
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-6-methylpyridine-2-carboxamide
Homo sapiens
-
above, pH not specified in the publication, temperature not specified in the publication
0.01
N-[4-(morpholin-4-yl)butyl]-1-benzofuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000008
N-[[4'-([[3-methyl-4-(methylamino)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000032
N-[[4'-([[3-methyl-4-(morpholin-4-yl)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000095
N-[[4'-([[3-methyl-4-(prop-1-yn-1-yl)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000071
N-[[4'-([[4-(3-hydroxypropyl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000011
N-[[4'-([[4-(3-methoxypropyl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000025
N-[[4'-([[4-(acetylamino)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000065
N-[[4'-([[4-(dimethylamino)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000064
N-[[4'-([[4-(furan-2-yl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000009
N-[[4-(4-fluorophenoxy)phenyl]sulfonyl]-N-[1-(hydroxycarbamoyl)cyclopentyl]-b-alanine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000014
N-[[4-(5-[[(4-cyano-3-methyl-1-benzofuran-2-yl)carbonyl]amino]pyridin-2-yl)phenyl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000005
N2-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000018
N2-(3a,7a-dihydro-1-benzothiophen-5-ylsulfonyl)-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000038
N2-benzyl-N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.5
N2-ethyl-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50 above 0.5 mM, in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.000014
N2-[(2S)-2-[[(4-benzylbenzyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl]-N,3-dimethyl-L-valinamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
N2-[(2S)-2-[[(4-benzylbenzyl)(hydroxy)phosphoryl]methyl]-6-phenoxyhexanoyl]-N,3-dimethyl-L-valinamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.003892
N2-[(3,4-dimethoxyphenyl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000036
N2-[(6-ethoxynaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000003
N2-[(6-ethylnaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000603
N2-[(7-ethoxynaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000032
N2-[2-(dimethylamino)ethyl]-N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000165
N2-[[6-(benzyloxy)naphthalen-2-yl]sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000022
O-tert-butyl-N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-serinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
SC-276
Homo sapiens
-
IC50 above 1 nM, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
7.4
-
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
22
-
assay at room temperature
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
articular, and osteoarthritic
Manually annotated by BRENDA team
rheumatoid synovial fibroblast
Manually annotated by BRENDA team
MMP-13 is the principal proteinase expressed by the mesenchymal stromal cells of giant cell tumor
Manually annotated by BRENDA team
-
MMP-13 is mainly produced by neurons, but also by astrocytes
Manually annotated by BRENDA team
-
upregulation of active MMP-13 in rat brains after 90 min of cerebral ischemia
Manually annotated by BRENDA team
-
melanoma cell line
Manually annotated by BRENDA team
-
from rheumatoid arthritis patients
Manually annotated by BRENDA team
-
MMP-13 real-time RT-PCR expression analysis, overview
Manually annotated by BRENDA team
-
fetal osteoblasts
Manually annotated by BRENDA team
-
fibrosaocoma cell line
Manually annotated by BRENDA team
-
from keratocyst odontogenic tumours, stromal tissue and mesenchymal cells, distribution of MMP-13 expression, overview
Manually annotated by BRENDA team
-
MMP-13 is mainly produced by neurons, but also by atrocytes
Manually annotated by BRENDA team
-
overexpression of MMP13
Manually annotated by BRENDA team
-
expression by fibroblasts in adult gingival and in fetal skin wounds characterized by rapid collagen remodeling and scarless healing
Manually annotated by BRENDA team
-
enzyme expression is related to tumor aggresiveness
Manually annotated by BRENDA team
-
expression of MMP13 in the synovial membrane of patients with rheumatoid and osteoarthritis
Manually annotated by BRENDA team
-
high expression of MMP13 in rheumatoid arthritis synovial tissue
Manually annotated by BRENDA team
-
nearly all chondrocyte-like cells are immunopositive, whereas fibroblast-like cells and fibrochondrocytes are more rarely labelled
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in cartilage
Manually annotated by BRENDA team
-
MMP-13 activation and its nuclear translocation is an early consequence of an ischemic stimulus
Manually annotated by BRENDA team
additional information
-
interleukin-1 at 2 ng/ml stimulates the secretion of MMP-13 in both osteoarthritis or rheumatoid arthritis chondrocytes
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
physiological function
malfunction
-
knockdown of MMP13 strongly enhances pigmentation of melanocytes
metabolism
-
interleukin-1beta treatment induces COX-2 and MMP-13 expressions in association with activation of ERKs, p38 MAPK, JNKs, and NF-kappaB in skin fibroblasts. Phorbol-12-myristate-13-acetate treatment also induces COX-2 and MMP-13 expressions in association with p38 MAPK activation. Glucosamine-hydrochloride differentially downregulates COX-2 andMMP-13 expression in the interleukin-1beta- or phorpbol-12-myristate-13-acetate-treated skin fibroblasts via the p38 MAPK-independent COX-2 translational inhibition and the p38 MAPK-dependent MMP-13 transcriptional suppression, respectively
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MMP13_HUMAN
471
0
53820
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43100
analytical untracentrifugation
53800
1 * 53800, calculated
24000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 35000, enzyme fragment 249-451, SDS-PAGE, x * 24000, mature enzyme, SDS-PAGE
25000
-
x * 25000, SDS-PAGE
35000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 35000, enzyme fragment 249-451, SDS-PAGE, x * 24000, mature enzyme, SDS-PAGE
48000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 48000, mature enzyme, SDS-PAGE
50000
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 53800, calculated
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
glycoprotein
-
N-glycosylated
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a complex of human MMP-13 with bovine TIMP-2 is crystallized using the sitting-drop vapour diffusion method in 100 mM MES (pH 6.5), 200 mM magnesium acetate, 20% (w/v) PEG 8000
comparison of more than 40 X-ray co-crystal structures of the human MMP-13 with bound inhibitors to gain the structural insights such as conserved direct interactions with binding site residues, namely Ala-238, Thr-245 and Thr-247. Docking-based screening of existing drugs and binding free-energy calculation suggests eltrombopag, cilostazol and domperidone as potential MMP-13 inhibitors
crystal structures of catalytically inactive full-length MMP-13 mutant E223A in complex with peptides of 14-26 amino acids derived from the cleaved prodomain during activation. Peptides are bound to the active site of the enzyme by forming an extended beta-strand with Glu40 or Tyr46 inserted into the S1' specificity pocket
enzyme catalytic domain in complex with inhibitor N,N'-bis(pyridin-3-ylmethyl)pyrimidine-4,6-dicarboxamide, N,N'-bis(3-methylbenzyl)pyrimidine-4,6-dicarboxamide or N,N'-bis(4-fluoro-3-methylbenzyl)pyrimidine-4,6-dicarboxamide
in complex with inhibitor SM-25453, comparison with structure of EC 3.4.24.17 with inhibitor
molecular dynamics simulations and multiway explorative data analysis on MMP13 complexed with Marimastat and two cis-1(S)2(R)-amino-2-indanol ligands, and comparison with proteases ADAMTS4, ADAMTS5. Determinant characteristics for ligand binding and selectivity among the three enzymes are to be found in the different protein conformation flexibility
molecular modeling of binding of homochiral (3S,3’S)-astaxanthin to enzyme
recombinant enzyme, hanging-drop vapour diffusion method, 20 mM Tris-HCl, pH 7.3, 5 mM CaCl2, 300 mM NaCl, addition of 1 M ammonium sulfate solution, pH 9.0, equilibrated against ammonium sulfate at 1.2 M, 20°C, 1 week, X-ray structure determination at 2.7 A resolution and analyis of the C-terminal haemopexin-like domain
hanging drop vapor diffusion method, using 10% (w/v) PEG4000, 1 M ammonium formate, and 100 mM Tris, pH 8.0
-
X-ray crystal structure of MMP-13 complexed with inhibitor
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E223A
catalytically inactive
F55S
naturally occuring dominant mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia
H213N
naturally occuring recessive mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia
M1K
naturally occuring recessive mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia
M72T
naturally occuring dominant mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant catalytic enzyme fragment from Escherichia coli
CTD affinity column chromatography
-
purification and refolding of recombinant His-tagged catalytic domain
-
recombinant enzyme and truncated mutant from myeloma cell culture medium
-
recombinant procollagenase 3 from NSO mouse myeloma cell culture medium
-
recombinant refolded enzyme form Escherichia coli
-
SP Sepharose column chromatography and Superdex 75 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of a truncated enzyme in Escherichia coli BL21(DE3)
expression of the catalytic enzyme fragment in Escherichia coli BL21(DE3)
expression of wild-type and mutant MMP13 in HEK-293 cells
MMP13 real-time RT-PCR expression analysis
a fragment of human MMP-13 corresponding to residues 104-274 is expressed in Escherichia coli BL21(DE3) cells
-
activation by aminophenylmercuric acetate, expression of procollagenase 3 and a C-terminal truncated form of procollagenase 3 comprising amino acid residues 249-451 in mouse myeloma cells, secretion to the cell culture medium
-
expression in Escherichia coli
-
expression of procollagenase 3 in NSO mouse myeloma cells, secretion to the medium
-
HEK-293-EBNA cells
-
matrix metalloproteinase gene MMP13 and the antiapoptotic genes Birc2, cIAP1, and Birc3, cIAP2, form an amplicon located on chromosome 11q22, and show elevated expression in osteosarcomas
-
MMP-13 expression analysis by semi-quantitative RT–PCR
-
MMP-13 expression and promoter activity analysis, overview
-
MMP-13 quantitative real-time PCR expression analysis, overview
-
MMP-13 real-time PCR expression analysis, overview
-
MMP-13 real-time RT-PCR expression analysis, overview
-
MMP-13 RT-PCR expression analysis, overview
-
overexpression in Escherichia coli BL21(DE3)
-
quantitative real-time PCR MMP-13 expression analysis
-
real-time quantitative PCR MMP-13 expression analysis
-
real-time quantitative PCR MMP-13 expression analysis, overview
-
the MMP-13 gene is localized on chromosome 11q22.3, MMP13 DNA and amino acid sequence determination and analysis, genotyping
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
siRNA knockdown of transcription factor Runx2 decreases MMP-13 expression in giant cell tumor stromal cells
the Runx2 transcription factor is known to have a binding site in the MMP-13 promoter region and activates MMP-13 expression constitutively in giant cell tumor cells. Inhibition of the ERK and JNK signaling pathways inhibits the upregulation of MMP-13 in these cells
(Z)-1-[N-methyl-N-[6-(N-methylammoniohexyl)amino]]diazen-1-ium-1,2-diolate, i.e. MAHMA-NONOate, induces the expression of MMP-13 via release of NO, which induces MMP-13 expression by JNK and NF-kappaB activation in chondrocytes, mechanism, overview. NO-induced MMP-13 expression is not suppressed by extracellular signal-regulated kinase inhibitor PD98059, or inhibitors of p38 kinase, i.e. SB203580, but is inhibited by a c-jun terminal kinase inhibitor SP600125 and inhibitors of NF-kappaB, i.e. SN-50
-
adiponectin and interleukin-1beta induce MMP-13 expression and secretion in cell cultures, adiponectin plays a role in the pathogenesis of arthritis as a proinflammatory mediator
-
after epidermal growth factor stimulation MMP13 is up-regulated
-
ALK1 stimulates MMP-13 expression in chondrocytes
-
both the JNK inhibitor SP 600125 and PI-3K/Akt inhibitor LY 294002 can inhibit chloramphenicol-induced c-Jun phosphorylation, MMP-13 expression, and cell invasion
-
chloramphenicol causes mitochondrial stress, decreases ATP biosynthesis, and induces MMP-13 expression, and solid-tumor cell invasion. Chloramphenicol also activated c-Jun N-terminal kinases, JNK, and PI-3K/Akt signaling, leading to c-Jun protein phosphorylation. The activated c-Jun protein activates binding to the MMP-13 promoter and also upregulates the amount of MMP-13. Other antibiotics that cause mitochondrial stress and a decrease in ATP biosynthesis also induce MMP-13 expression. Chloramphenicol-induction of MMP-13 expression is observed in nine solid-tumor cell lines, including H1299, HepG2, A549, CL-10, NCI-N87, Huh7, SAS, GBM8401, and Hep1, but not in leukemia suspensions, including THP-1, HL-60, and Jurkat cells
-
connective tissue growth factor, CTGF, a secreted protein that binds to integrins, increases the migration and expression of MMP-13 in chondrosarcoma JJ012 cells through the alphanybeta3 integrin, FAK, ERK, and NF-kappaB signal transduction pathway. The induction is inhibited by MAPK kinase inhibitors PD98059 and U0126, but not by RAD peptide. Also treatment of JJ012 cells with NF-kappaB inhibitor PDTC or IkappaB protease inhibitor TPCK inhibits CTGF-induced cell migration and MMP-13 up-regulation, overview
-
Cyr61 increases the binding of c-Fos and c-Jun to the activator protein-1 element on the MMP-13 promoter, and Cyr61 enhances the migration of chondrosarcoma cells by increasing MMP-13 expression through the alphanybeta3 integrin receptor, FAK, ERK, c-Fos/c-Jun and activator protein-1 signal transduction pathway. The upregulation of MMP-13 is antagonized by decoy agonist AP-1-binding site, AP-1 oligonucleotide, but not by NF-kappaB oligonucleotide or scrambled oligonucleotide, as well as by RGD, PD98059 and FAK(Y397F) and ERK2 mutant. Pretreatment with RGD and PD98059 or transfection with FAK and ERK2 mutant of JJ012 cells inhibits the Cyr61-induced increase in AP-1 promoter activity
-
doxycycline decreases MMP-13 expression in synoviocytes but not cartilage
-
epigallocatechin-3-gallate, EGCG, from Camellia sinensis inhibits advanced glycation end product-induced expression of matrix metalloproteinase-13 in chondrocytes involving suppression of p38-MAPK and JNK activation, overview
-
GDNF-induced MMP-13 expression and glioma migration are attenuated by MEK/extracellular signal-regulating kinase and c-Jun N-terminal protein kinase inhibitors, PD98059 and SP600125, as well as ERK and JNKdominant-negative mutants. AP-1 inhibitors, tanshinone IIA and curcumin, also reduce GDNF-induced glioma cell migration
-
glial cell line-derived neurotrophic factor, GDNF, induces cell migration and MMP-13 expression in glioma cells
-
glucosamine-hydrochloride differentially downregulates COX-2 andMMP-13 expression in the interleukin-1beta-treated or phorpbol-12-myristate-13-acetate-treated skin fibroblasts via the p38 MAPK-independent COX-2 translational inhibition and the p38 MAPK-dependent MMP-13 transcriptional suppression, respectively
-
in the chondrocytes pretreated with the JNK inhibitor SP600125, stimulation with interleukin-1beta shows an 88% increase in miR-27b expression and an 14fold increase in MMP-13 mRNA expression compared with controls. Pretreatment of osteoarthritic chondrocytes with the p38 MAPK inhibitor SB202190 suppresses interleukin-1beta-induced MMP-13 mRNA expression by 90%
-
inhibitor of growth 2, ING2, upregulates expression of MMP13, which enhances cancer invasion and metastasis. MMP13 expression is further enhanced by combination of the synergistically acting ING2 and HDAC1
-
interleukin-1 and oncostatin M induce MMP-13 expression
-
interleukin-1beta and FN-f stimulate MMP-13 expression, dependent on AP-1 activation
-
interleukin-1beta and tumor necrosis factor-alpha induce MMP-13 expression. When CCAAT/enhancer binding protein beta, i.e. C/EBPbeta and liver-enriched activator protein, LAP, are overexpressed in C-28/I2 cells, endogenous MMP-13 expression is stimulated up to 32fold. Both C/EBPbeta and AP-1 are essential regulators of the MMP-13 promoter
-
interleukin-1beta induces MMP-13 expression, mediated by extracellular signal-regulated protein kinase, p38 kinase, and c-Jun N-terminal kinase of the MAPK family signal transduction molecules. The interleukin-1beta-induced expression of MMP-13 is selectively inhibited by ERK MAPK pathway inhibitor U0126, and by the imidazo[5,1-c][1,4]thiazine derivative ITZ-1, overview. It is also less selectively inhibited by the p38 kinase inhibitor SB203580 and the JNK inhibitor SP600125
-
interleukin-1beta induces MMP-13 expression, which is potently inhibited by interferon-gamma healthy chondrocytes mediated by STAT1
-
interleukin-1beta treatment induces COX-2 and MMP-13 expressions in association with activation of ERKs, p38 MAPK, JNKs, and NF-kappaB in skin fibroblasts. Phorbol-12-myristate-13-acetate treatment also induces COX-2 and MMP-13 expressions in association with p38 MAPK activation
-
MMP-13 expression is induced by advanced glycation end products, e.g. pentosidine or N3-carboxymethyllysine, the induction is significantly inhibited by SB202190 and SP600125
-
p38gamma mitogen-activated protein kinase suppresses chondrocyte production of MMP-13 in response to catabolic stimulation. Inhibition of both p38alpha and p38gamma with BIRB796 results in less inhibition of MMP-13 production in response to interleukin-1beta or FN-f than does inhibition of only p38alpha with SB203580
-
pyrrolidine dithiocarbamate, a NF-kappaB inhibitor, upregulates MMP-1 and MMP-13 in interleukin-1beta-stimulated rheumatoid arthritis fibroblast-like synoviocytes in a stimuli-specific manner or by an NF-kappaB independent mechanism
-
Roxithromycin suppresses the expression of MMP-13 mRNA not only in Ca9-22 cells, but also in other human epithelial cell lines. Roxithromycin strongly inhibits the expression of Runx2 mRNA. Furthermore, Runx2 siRNA inhibits the induction of MMP-13 in Ca9-22 cells
-
strong stimulus of a combination of interleukin-1alpha plus oncostatin M, inducing MMP13 expression
-
the bFGF-ERK-Elk-1 signaling axis is responsible for the potent induction of MMP-13 in primary articular chondrocytes. Phosphorylation renders Elk-1 competent for induction of MMP-13 gene transcription, while sumoylation has the opposite effect. Unphosphorylatable Elk-1 S383A mutant and unphosphorylated Elk-1 are inactive, while mutation of the SUMO modification site of Elk-1 to GAL4-Elk-1K230R/K249R increases its activity. bFGF-mediated activation of Elk-1 is regulated by the SUMO pathway
-
the NF-kappaB inhibitors fenofibrate, N-acetylcysteine and MG132 decrease MMP-13 expression in interleukin-1beta-stimulated fibroblast-like synoviocytes
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme form inclusion bodies after expression in Escherichia coli
-
a chromatographic method is used to refold the Histidine-tagged (His-tagged) catalytic domain of MMP-13. After the optimization of gradient elution modes and chromatographic conditions, the recovery yield reaches 83% with a relative activity of 92%. Addition of small molecule inhibitors to prevent slight autoproteolytic degradation does not affect the secondary structure of the protein
-
in 50 mM MES, pH 6.5, 500 mM NaCl, 10 mM CaCl2, 1.0 mM ZnCl2, and decreasing concentrations of urea (4-0 M)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
generation of a neutralizing antibody specifc for the active form of MMP-13, but not for the latent form, or other MMPs. antibody can be used to measure active MMP-13 selectively by an enzyme-linked immunosorbet assay. The antibody suppresses the cleavage of type II collagen in human articular chondrocyte cultures, and is thought to inhibit MMP-13 activity effectively
medicine
patients with alcoholic liver cirrhosis (stage A, B, C) display increased blood serum levels of MMP13 and reduced concentrations of glutamic acid and glutamine compared to the control group. No significant differences are observed in the activity of MMP1 in alcoholics with or without liver cirrhosis or in controls
diagnostics
-
MMP-13 is a predictive markers for cisplatin resistance in head and neck squamous cell cancer
drug development
-
the enzyme is a target for design of tetracycline-based drugs
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heikkilae, P.; Teronen, O.; Moilanen, M.; Konttinen, Y.T.; Hanemaaijer, R.; Laitinen, M.; Maisi, P.; van der Pluijm, G.; Bartlett, J.D.; Salo, T.; Sorsa, T.
Bisphosphonates inhibit stromelysin-1 (MMP-3), matrix metalloelastase (MMP-12), collagenase-3 (MMP-13) and enamelysin (MMP-20), but not urokinase-type plasminogen activator, and diminish invasion and migration of human malignant and endothelial cell lines
Anticancer Drugs
13
245-254
2002
Homo sapiens
Manually annotated by BRENDA team
Leeman, M.F.; Curran, S.; Murray, G.I.
The structure, regulation, and function of human matrix metalloproteinase-13
Crit. Rev. Biochem. Mol. Biol.
37
149-166
2002
Homo sapiens
Manually annotated by BRENDA team
Knaeuper, V.; Lopez-Otin, C.; Smith, B.; Knight, G.; Murphy, G.
Biochemical characterization of human collagenase-3
J. Biol. Chem.
271
1544-1550
1996
Homo sapiens
Manually annotated by BRENDA team
Knaeuper, V.; Cowell, S.; Smith, B.; Lopez-Otin, C.; O'Shea, M.; Morris, H.; Zardi, L.; Murphy, G.
The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction
J. Biol. Chem.
272
7608-7616
1997
Homo sapiens
Manually annotated by BRENDA team
Deng, S.J.; Bickett, D.M.; Mitchell, J.L.; Lambert, M.H.; Blackburn, R.K.; Carter, H.L., 3rd; Neugebauer, J.; Pahel, G.; Weiner, M.P.; Moss, M.L.
Substrate specificity of human collagenase 3 assessed using a phage-displayed peptide library
J. Biol. Chem.
275
31422-31427
2000
Homo sapiens
Manually annotated by BRENDA team
Gomis-Rueth, F.X.; Gohlke, U.; Betz, M.; Knauper, V.; Murphy, G.; Lopez-Otin, C.; Bode, W.
The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain
J. Mol. Biol.
264
556-566
1996
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Gonnella, N.C.; Koehn, J.; Pathak, N.; Ganu, V.; Melton, R.; Parker, D.; Hu, S.I.; Nam, K.Y.
Solution structure of the catalytic domain of human collagenase-3 (MMP-13) complexed to a potent non-peptidic sulfonamide inhibitor: binding comparison with stromelysin-1 and collagenase-1
J. Mol. Biol.
301
513-524
2000
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Moy, F.J.; Chanda, P.K.; Chen, J.M.; Cosmi, S.; Edris, W.; Levin, J.I.; Powers, R.
High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor
J. Mol. Biol.
302
671-689
2000
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Kohno, T.; Hochigai, H.; Yamashita, E.; Tsukihara, T.; Kanaoka, M.
Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453
Biochem. Biophys. Res. Commun.
344
315-322
2006
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Bikadi, Z.; Hazai, E.; Zsila, F.; Lockwood, S.F.
Molecular modeling of non-covalent binding of homochiral (3S,3S)-astaxanthin to matrix metalloproteinase-13 (MMP-13)
Bioorg. Med. Chem.
14
5451-5458
2006
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Noe, M.C.; Snow, S.L.; Wolf-Gouveia, L.A.; Mitchell, P.G.; Lopresti-Morrow, L.; Reeves, L.M.; Yocum, S.A.; Liras, J.L.; Vaughn, M.
3-Hydroxy-4-arylsulfonyltetrahydropyranyl-3-hydroxamic acids are novel inhibitors of MMP-13 and aggrecanase
Bioorg. Med. Chem. Lett.
14
4727-4730
2004
Homo sapiens
Manually annotated by BRENDA team
Kim, S.H.; Pudzianowski, A.T.; Leavitt, K.J.; Barbosa, J.; McDonnell, P.A.; Metzler, W.J.; Rankin, B.M.; Liu, R.; Vaccaro, W.; Pitts, W.
Structure-based design of potent and selective inhibitors of collagenase-3 (MMP-13)
Bioorg. Med. Chem. Lett.
15
1101-1106
2005
Homo sapiens
Manually annotated by BRENDA team
Engel, C.K.; Pirard, B.; Schimanski, S.; Kirsch, R.; Habermann, J.; Klingler, O.; Schlotte, V.; Weithmann, K.U.; Wendt, K.U.
Structural basis for the highly selective inhibition of MMP-13
Chem. Biol.
12
181-189
2005
Homo sapiens (P45452)
Manually annotated by BRENDA team
Sulkala, M.; Paeaekkoenen, V.; Larmas, M.; Salo, T.; Tjaederhane, L.
Matrix metalloproteinase-13 (MMP-13, collagenase-3) is highly expressed in human tooth pulp
Connect. Tissue Res.
45
231-237
2004
Homo sapiens
Manually annotated by BRENDA team
Corte, M.D.; Gonzalez, L.O.; Corte, M.G.; Quintela, I.; Pidal, I.; Bongera, M.; Vizoso, F.
Collagenase-3 (MMP-13) expression in cutaneous malignant melanoma
Int. J. Biol. Markers
20
242-248
2006
Homo sapiens
Manually annotated by BRENDA team
Toriseva, M.J.; Ala-Aho, R.; Karvinen, J.; Baker, A.H.; Marjomaeki, V.S.; Heino, J.; Kaehaeri, V.M.
Collagenase-3 (MMP-13) enhances remodeling of three-dimensional collagen and promotes survival of human skin fibroblasts
J. Invest. Dermatol.
127
49-59
2006
Homo sapiens
Manually annotated by BRENDA team
Kuivanen, T.T.; Jeskanen, L.; Kylloenen, L.; Impola, U.; Saarialho-Kere, U.K.
Transformation-specific matrix metalloproteinases, MMP-7 and MMP-13, are present in epithelial cells of keratoacanthomas
Mod. Pathol.
19
1203-1212
2006
Homo sapiens
Manually annotated by BRENDA team
Leonardi, R.; Loreto, C.; Barbato, E.; Caltabiano, R.; Lombardo, C.; Musumeci, G.; Muzio, L.L.
MMP-13 (collagenase 3) localization in human temporomandibular joint discs with internal derangement
Acta Histochem.
110
314-318
2008
Homo sapiens
Manually annotated by BRENDA team
Suri, L.; Damoulis, P.D.; Le, T.; Gagari, E.
Expression of MMP-13 (collagenase-3) in long-term cultures of human dental pulp cells
Arch. Oral Biol.
53
791-799
2008
Homo sapiens
Manually annotated by BRENDA team
Maskos, K.; Lang, R.; Tschesche, H.; Bode, W.
Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2
J. Mol. Biol.
366
1222-1231
2007
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Leivonen, S.K.; Ala-Aho, R.; Koli, K.; Grenman, R.; Peltonen, J.; Kaehaeri, V.M.
Activation of Smad signaling enhances collagenase-3 (MMP-13) expression and invasion of head and neck squamous carcinoma cells
Oncogene
25
2588-2600
2006
Homo sapiens
Manually annotated by BRENDA team
Rodriguez Faba, O.; Fernandez Gomez, J.M.; Palou Redorta, J.; Escaf Barmadah, S.; Vizoso, F.; Villavicencio Mavrich, H.
Significance of collagenase 3 (matrix metalloproteinase 13) in invasive bladder cancer: correlation with pathological parameters
Urol. Int.
78
140-144
2007
Homo sapiens
Manually annotated by BRENDA team
Zhang, B.; Cao, X.; Liu, Y.; Cao, W.; Zhang, F.; Zhang, S.; Li, H.; Ning, L.; Fu, L.; Niu, Y.; Niu, R.; Sun, B.; Hao, X.
Tumor-derived matrix metalloproteinase-13 (MMP-13) correlates with poor prognoses of invasive breast cancer
BMC Cancer
8
83
2008
Homo sapiens
Manually annotated by BRENDA team
Cuadrado, E.; Rosell, A.; Borrell-Pages, M.; Garcia-Bonilla, L.; Hernandez-Guillamon, M.; Ortega-Aznar, A.; Montaner, J.
Matrix metalloproteinase-13 is activated and is found in the nucleus of neural cells after cerebral ischemia
J. Cereb. Blood Flow Metab.
29
398-410
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Monovich, L.G.; Tommasi, R.A.; Fujimoto, R.A.; Blancuzzi, V.; Clark, K.; Cornell, W.D.; Doti, R.; Doughty, J.; Fang, J.; Farley, D.; Fitt, J.; Ganu, V.; Goldberg, R.; Goldstein, R.; Lavoie, S.; Kulathila, R.; Macchia, W.; Parker, D.T.; Melton, R.; OByrne, E.; Pastor, G.; Pellas, T.; Quadros, E.; Reel, N.
Discovery of potent, selective, and orally active carboxylic acid based inhibitors of matrix metalloproteinase-13
J. Med. Chem.
52
3523-3538
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Sakao, K.; Takahashi, K.A.; Mazda, O.; Arai, Y.; Tonomura, H.; Inoue, A.; Saito, M.; Fujioka, M.; Takamiya, H.; Imanishi, J.; Kubo, T.
Enhanced expression of interleukin-6, matrix metalloproteinase-13, and receptor activator of NF-kappaB ligand in cells derived from osteoarthritic subchondral bone
J. Orthop. Sci.
13
202-210
2008
Homo sapiens
Manually annotated by BRENDA team
Ahmad, R.; Sylvester, J.; Ahmad, M.; Zafarullah, M.
Adaptor proteins and Ras synergistically regulate IL-1-induced ADAMTS-4 expression in human chondrocytes
J. Immunol.
182
5081-5087
2009
Homo sapiens (P45452)
Manually annotated by BRENDA team
Kolodziej, S.A.; Hockerman, S.L.; Boehm, T.L.; Carroll, J.N.; DeCrescenzo, G.A.; McDonald, J.J.; Mischke, D.A.; Munie, G.E.; Fletcher, T.R.; Rico, J.G.; Stehle, N.W.; Swearingen, C.; Becker, D.P.
Orally bioavailable dual MMP-1/MMP-14 sparing, MMP-13 selective alpha-sulfone hydroxamates
Bioorg. Med. Chem. Lett.
20
3557-3560
2010
Homo sapiens
Manually annotated by BRENDA team
Luukkaa, H.; Klemi, P.; Leivo, I.; Maekitie, A.A.; Irish, J.; Gilbert, R.; Perez-Ordonez, B.; Hirsimaeki, P.; Vahlberg, T.; Kivisaari, A.; Kaehaeri, V.M.; Grenman, R.
Expression of matrix metalloproteinase-1, -7, -9, -13, Ki-67, and HER-2 in epithelial-myoepithelial salivary gland cancer
Head Neck
32
1019-1027
2009
Homo sapiens
Manually annotated by BRENDA team
Ansell, A.; Jerhammar, F.; Ceder, R.; Grafstroem, R.; Grenman, R.; Roberg, K.
Matrix metalloproteinase-7 and -13 expression associate to cisplatin resistance in head and neck cancer cell lines
Oral Oncol.
45
866-871
2009
Homo sapiens
Manually annotated by BRENDA team
Lausch, E.; Keppler, R.; Hilbert, K.; Cormier-Daire, V.; Nikkel, S.; Nishimura, G.; Unger, S.; Spranger, J.; Superti-Furga, A.; Zabel, B.
Mutations in MMP9 and MMP13 determine the mode of inheritance and the clinical spectrum of metaphyseal anadysplasia
Am. J. Hum. Genet.
85
168-178
2009
Mus musculus, Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Choi, H.M.; Lee, Y.A.; Lee, S.H.; Hong, S.J.; Hahm, D.H.; Choi, S.Y.; Yang, H.I.; Yoo, M.C.; Kim, K.S.
Adiponectin may contribute to synovitis and joint destruction in rheumatoid arthritis by stimulating vascular endothelial growth factor, matrix metalloproteinase-1, and matrix metalloproteinase-13 expression in fibroblast-like synoviocytes more than proinflammatory mediators
Arthritis Res. Ther.
11
R161
2009
Homo sapiens
Manually annotated by BRENDA team
Rasheed, Z.; Anbazhagan, A.N.; Akhtar, N.; Ramamurthy, S.; Voss, F.R.; Haqqi, T.M.
Green tea polyphenol epigallocatechin-3-gallate inhibits advanced glycation end product-induced expression of tumor necrosis factor-alpha and matrix metalloproteinase-13 in human chondrocytes
Arthritis Res. Ther.
11
R71
2009
Homo sapiens
Manually annotated by BRENDA team
Baragi, V.M.; Becher, G.; Bendele, A.M.; Biesinger, R.; Bluhm, H.; Boer, J.; Deng, H.; Dodd, R.; Essers, M.; Feuerstein, T. et al.
A new class of potent matrix metalloproteinase 13 inhibitors for potential treatment of osteoarthritis: Evidence of histologic and clinical efficacy without musculoskeletal toxicity in rat models
Arthritis Rheum.
60
2008-2018
2009
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hayashida, M.; Okazaki, K.; Fukushi, J.; Sakamoto, A.; Iwamoto, Y.
CCAAT/enhancer binding protein beta mediates expression of matrix metalloproteinase 13 in human articular chondrocytes in inflammatory arthritis
Arthritis Rheum.
60
708-716
2009
Homo sapiens
Manually annotated by BRENDA team
Akhtar, N.; Rasheed, Z.; Ramamurthy, S.; Anbazhagan, A.N.; Voss, F.R.; Haqqi, T.M.
MicroRNA-27b regulates the expression of matrix metalloproteinase 13 in human osteoarthritis chondrocytes
Arthritis Rheum.
62
1361-1371
2010
Homo sapiens
Manually annotated by BRENDA team
Borzi, R.M.; Olivotto, E.; Pagani, S.; Vitellozzi, R.; Neri, S.; Battistelli, M.; Falcieri, E.; Facchini, A.; Flamigni, F.; Penzo, M.; Platano, D.; Santi, S.; Facchini, A.; Marcu, K.B.
Matrix metalloproteinase 13 loss associated with impaired extracellular matrix remodeling disrupts chondrocyte differentiation by concerted effects on multiple regulatory factors
Arthritis Rheum.
62
2370-2381
2010
Homo sapiens
Manually annotated by BRENDA team
Settle, S.; Vickery, L.; Nemirovskiy, O.; Vidmar, T.; Bendele, A.; Messing, D.; Ruminski, P.; Schnute, M.; Sunyer, T.
Cartilage degradation biomarkers predict efficacy of a novel highly selective matrix metalloproteinase 13 inhibitor in a dog model of osteoarthritis: Multivariate analysis confirmed that modulation of type II collagen aggrecan degradation peptides paralle
Arthritis Rheum.
62
3006-3015
2010
Canis lupus familiaris, Homo sapiens
Manually annotated by BRENDA team
Lu, D.Y.; Leung, Y.M.; Cheung, C.W.; Chen, Y.R.; Wong, K.L.
Glial cell line-derived neurotrophic factor induces cell migration and matrix metalloproteinase-13 expression in glioma cells
Biochem. Pharmacol.
80
1201-1209
2010
Homo sapiens
Manually annotated by BRENDA team
Li, W.; Hu, Y.; Li, J.; Thomason, J.R.; DeVincentis, D.; Du, X.; Wu, J.; Hotchandani, R.; Rush, T.S.; Skotnicki, J.S.; Tam, S.; Chockalingam, P.S.; Morris, E.A.; Levin, J.I.
3,4-Disubstituted benzofuran P1 MMP-13 inhibitors: optimization of selectivity and reduction of protein binding
Bioorg. Med. Chem. Lett.
19
4546-4550
2009
Homo sapiens
Manually annotated by BRENDA team
Heim-Riether, A.; Taylor, S.J.; Liang, S.; Gao, D.A.; Xiong, Z.; Michael August, E.; Collins, B.K.; Farmer, B.T.; Haverty, K.; Hill-Drzewi, M.; Junker, H.D.; Mariana Margarit, S.; Moss, N.; Neumann, T.; Proudfoot, J.R.; Keenan, L.S.; Sekul, R.; Zhang, Q.; Li, J.; Farrow, N.A.
Improving potency and selectivity of a new class of non-Zn-chelating MMP-13 inhibitors
Bioorg. Med. Chem. Lett.
19
5321-5324
2009
Homo sapiens
Manually annotated by BRENDA team
Kolodziej, S.A.; Hockerman, S.L.; DeCrescenzo, G.A.; McDonald, J.J.; Mischke, D.A.; Munie, G.E.; Fletcher, T.R.; Stehle, N.; Swearingen, C.; Becker, D.P.
MMP-13 selective isonipecotamide alpha-sulfone hydroxamates
Bioorg. Med. Chem. Lett.
20
3561-3564
2010
Homo sapiens
Manually annotated by BRENDA team
Gao, D.A.; Xiong, Z.; Heim-Riether, A.; Amodeo, L.; August, E.M.; Cao, X.; Ciccarelli, L.; Collins, B.K.; Harrington, K.; Haverty, K.; Hill-Drzewi, M.; Li, X.; Liang, S.; Margarit, S.M.; Moss, N.; Nagaraja, N.; Proudfoot, J.; Roman, R.; Schlyer, S.; Keenan, L.S.; Taylor, S.; Wellenzohn, B.; Wiedenmayer, D.; Li, J.; Farrow, N.A.
SAR studies of non-zinc-chelating MMP-13 inhibitors: improving selectivity and metabolic stability
Bioorg. Med. Chem. Lett.
20
5039-5043
2010
Homo sapiens
Manually annotated by BRENDA team
Schnute, M.E.; OBrien, P.M.; Nahra, J.; Morris, M.; Howard Roark, W.; Hanau, C.E.; Ruminski, P.G.; Scholten, J.A.; Fletcher, T.R.; Hamper, B.C.; Carroll, J.N.; Patt, W.C.; Shieh, H.S.; Collins, B.; Pavlovsky, A.G.; Palmquist, K.E.; Aston, K.W.; Hitchcock, J.; Rogers, M.D.; McDonald, J.; Johnson, A.R.; Munie, G.E.
Discovery of (pyridin-4-yl)-2H-tetrazole as a novel scaffold to identify highly selective matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis
Bioorg. Med. Chem. Lett.
20
576-580
2010
Homo sapiens (P45452)
Manually annotated by BRENDA team
Ziegler, N.; Alonso, A.; Steinberg, T.; Woodnutt, D.; Kohl, A.; Muessig, E.; Schulz, S.; Tomakidi, P.
Mechano-transduction in periodontal ligament cells identifies activated states of MAP-kinases p42/44 and p38-stress kinase as a mechanism for MMP-13 expression
BMC Cell Biol.
11
10
2010
Homo sapiens
Manually annotated by BRENDA team
Tardif, G.; Hum, D.; Pelletier, J.; Duval, N.; Martel-Pelletier, J.
Regulation of the IGFBP-5 and MMP-13 genes by the microRNAs miR-140 and miR-27a in human osteoarthritic chondrocytes
BMC Musculoskelet. Disord.
10
148
2009
Homo sapiens
Manually annotated by BRENDA team
Mak, I.W.; Cowan, R.W.; Popovic, S.; Colterjohn, N.; Singh, G.; Ghert, M.
Upregulation of MMP-13 via Runx2 in the stromal cell of Giant Cell Tumor of bone
Bone
45
377-386
2009
Homo sapiens (P45452)
Manually annotated by BRENDA team
Ma, O.; Cai, W.W.; Zender, L.; Dayaram, T.; Shen, J.; Herron, A.J.; Lowe, S.W.; Man, T.K.; Lau, C.C.; Donehower, L.A.
MMP13, Birc2 (cIAP1), and Birc3 (cIAP2), amplified on chromosome 9, collaborate with p53 deficiency in mouse osteosarcoma progression
Cancer Res.
69
2559-2567
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Tan, T.W.; Yang, W.H.; Lin, Y.T.; Hsu, S.F.; Li, T.M.; Kao, S.T.; Chen, W.C.; Fong, Y.C.; Tang, C.H.
Cyr61 increases migration and MMP-13 expression via alphavbeta3 integrin, FAK, ERK and AP-1-dependent pathway in human chondrosarcoma cells
Carcinogenesis
30
258-268
2009
Homo sapiens
Manually annotated by BRENDA team
Lecomte, J.; Louis, K.; Detry, B.; Blacher, S.; Lambert, V.; Bekaert, S.; Munaut, C.; Paupert, J.; Blaise, P.; Foidart, J.M.; Rakic, J.M.; Krane, S.M.; Noel, A.
Bone marrow-derived mesenchymal cells and MMP13 contribute to experimental choroidal neovascularization
Cell. Mol. Life Sci.
68
677-686
2011
Homo sapiens (P45452), Homo sapiens, Mus musculus, Mus musculus C57BL/6
Manually annotated by BRENDA team
Kim, K.S.; Oh, d.a..H.; Choi, H.M.; Bang, J.S.; Ryu, C.J.; Kim, J.H.; Yoo, M.C.; Yang, H.I.
Pyrrolidine dithiocarbamate, a NF-kappaB inhibitor, upregulates MMP-1 and MMP-13 in IL-1beta-stimulated rheumatoid arthritis fibroblast-like synoviocytes
Eur. J. Pharmacol.
613
167-175
2009
Homo sapiens
Manually annotated by BRENDA team
Mak, I.W.; Seidlitz, E.P.; Cowan, R.W.; Turcotte, R.E.; Popovic, S.; Wu, W.C.; Singh, G.; Ghert, M.
Evidence for the role of matrix metalloproteinase-13 in bone resorption by giant cell tumor of bone
Hum. Pathol.
41
1320-1329
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Kumamoto, K.; Fujita, K.; Kurotani, R.; Saito, M.; Unoki, M.; Hagiwara, N.; Shiga, H.; Bowman, E.D.; Yanaihara, N.; Okamura, S.; Nagashima, M.; Miyamoto, K.; Takenoshita, S.; Yokota, J.; Harris, C.C.
ING2 is upregulated in colon cancer and increases invasion by enhanced MMP13 expression
Int. J. Cancer
125
1306-1315
2009
Homo sapiens
Manually annotated by BRENDA team
Yang, L.; Guo, A.; Gu, J.C.
c-Jun N-terminal kinase and nuclear factor kappaB mediate nitric oxide-induced expression of matrix metalloproteinase-13
Int. Orthop.
35
1261-1266
2011
Homo sapiens
Manually annotated by BRENDA team
Tan, T.W.; Lai, C.H.; Huang, C.Y.; Yang, W.H.; Chen, H.T.; Hsu, H.C.; Fong, Y.C.; Tang, C.H.
CTGF enhances migration and MMP-13 up-regulation via alphanybeta3 integrin, FAK, ERK, and NF-kappaB-dependent pathway in human chondrosarcoma cells
J. Cell. Biochem.
107
345-356
2009
Homo sapiens
Manually annotated by BRENDA team
Hernandez Rios, M.; Sorsa, T.; Obregon, F.; Tervahartiala, T.; Valenzuela, M.A.; Pozo, P.; Dutzan, N.; Lesaffre, E.; Molas, M.; Gamonal, J.
Proteolytic roles of matrix metalloproteinase (MMP)-13 during progression of chronic periodontitis: initial evidence for MMP-13/MMP-9 activation cascade
J. Clin. Periodontol.
36
1011-1017
2009
Homo sapiens
Manually annotated by BRENDA team
Pirhan, D.; Atilla, G.; Emingil, G.; Tervahartiala, T.; Sorsa, T.; Berdeli, A.
MMP-13 promoter polymorphisms in patients with chronic periodontitis: effects on GCF MMP-13 levels and outcome of periodontal therapy
J. Clin. Periodontol.
36
474-481
2009
Homo sapiens
Manually annotated by BRENDA team
Hong, H.; Park, Y.K.; Choi, M.S.; Ryu, N.H.; Song, D.K.; Suh, S.I.; Nam, K.Y.; Park, G.Y.; Jang, B.C.
Differential down-regulation of COX-2 and MMP-13 in human skin fibroblasts by glucosamine-hydrochloride
J. Dermatol. Sci.
56
43-50
2009
Homo sapiens
Manually annotated by BRENDA team
Blaney Davidson, E.N.; Remst, D.F.; Vitters, E.L.; van Beuningen, H.M.; Blom, A.B.; Goumans, M.J.; van den Berg, W.B.; van der Kraan, P.M.
Increase in ALK1/ALK5 ratio as a cause for elevated MMP-13 expression in osteoarthritis in humans and mice
J. Immunol.
182
7937-7945
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Nuti, E.; Casalini, F.; Avramova, S.I.; Santamaria, S.; Cercignani, G.; Marinelli, L.; La Pietra, V.; Novellino, E.; Orlandini, E.; Nencetti, S.; Tuccinardi, T.; Martinelli, A.; Lim, N.H.; Visse, R.; Nagase, H.; Rossello, A.
N-O-isopropyl sulfonamido-based hydroxamates: design, synthesis and biological evaluation of selective matrix metalloproteinase-13 inhibitors as potential therapeutic agents for osteoarthritis
J. Med. Chem.
52
4757-4773
2009
Homo sapiens (P45452)
Manually annotated by BRENDA team
Fortier, L.A.; Motta, T.; Greenwald, R.A.; Divers, T.J.; Mayr, K.G.
Synoviocytes are more sensitive than cartilage to the effects of minocycline and doxycycline on IL-1alpha and MMP-13-induced catabolic gene responses
J. Orthop. Res.
28
522-528
2010
Homo sapiens
Manually annotated by BRENDA team
Julovi, S.M.; Ito, H.; Nishitani, K.; Jackson, C.J.; Nakamura, T.
Hyaluronan inhibits matrix metalloproteinase-13 in human arthritic chondrocytes via CD44 and P38
J. Orthop. Res.
29
258-264
2010
Homo sapiens
Manually annotated by BRENDA team
Tabuchi, S.; Sakuta, T.; Oyama, T.; Tokuda, M.; Tatsuyama, S.; Kajihara, T.; Nagaoka, S.; Beppu, M.; Sugihara, K.; Ikebe, T.; Shirasuna, K.; Torii, M.
Runt-related gene 2 is involved in the inhibition of matrix metalloproteinase-13 expression by roxithromycin in human gingival epithelial cell cultures
J. Periodontal Res.
44
283-288
2009
Homo sapiens
Manually annotated by BRENDA team
Kimura, H.; Yukitake, H.; Suzuki, H.; Tajima, Y.; Gomaibashi, K.; Morimoto, S.; Funabashi, Y.; Yamada, K.; Takizawa, M.
The chondroprotective agent ITZ-1 inhibits interleukin-1beta-induced matrix metalloproteinase-13 production and suppresses nitric oxide-induced chondrocyte death
J. Pharmacol. Sci.
110
201-211
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Li, J.J.; Johnson, A.R.
Selective MMP13 inhibitors
Med. Res. Rev.
31
863-894
2011
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Im, H.; Sharrocks, A.; Lin, X.; Yan, D.; Kim, J.; Van Wijnen, A.; Hipskind, R.
Basic fibroblast growth factor induces matrix metalloproteinase-13 via eRK MAP kinase-altered phosphorylation and sumoylation of Elk-1 in human adult articular chondrocytes
Open Access Rheumatol.
1
151-161
2009
Homo sapiens
Manually annotated by BRENDA team
Kardesler, L.; Biyikoglu, B.; Cetinkalp, S.; Pitkala, M.; Sorsa, T.; Buduneli, N.
Crevicular fluid matrix metalloproteinase-8, -13, and TIMP-1 levels in type 2 diabetics
Oral Dis.
16
476-481
2010
Homo sapiens
Manually annotated by BRENDA team
Leonardi, R.; Matthews, J.B.; Caltabiano, R.; Greco, M.; Lombardo, C.; Loreto, C.; Santarelli, A.; Muzio, L.L.
MMP-13 expression in keratocyst odontogenic tumour associated with NBCCS and sporadic keratocysts
Oral Dis.
16
795-800
2010
Homo sapiens
Manually annotated by BRENDA team
Ahmad, R.; El Mabrouk, M.; Sylvester, J.; Zafarullah, M.
Human osteoarthritic chondrocytes are impaired in matrix metalloproteinase-13 inhibition by IFN-gamma due to reduced IFN-gamma receptor levels
Osteoarthritis Cartilage
17
1049-1055
2009
Homo sapiens
Manually annotated by BRENDA team
Long, D.L.; Loeser, R.F.
p38gamma mitogen-activated protein kinase suppresses chondrocyte production of MMP-13 in response to catabolic stimulation
Osteoarthritis Cartilage
18
1203-1210
2010
Homo sapiens
Manually annotated by BRENDA team
Kothapalli, R.; Khan, A.M.; Basappa, A.M.; Gopalsamy, A.; Chong, Y.S.; Annamalai, L.
Cheminformatics-based drug design approach for identification of inhibitors targeting the characteristic residues of MMP-13 hemopexin domain
PLoS ONE
5
e12494
2010
Homo sapiens
Manually annotated by BRENDA team
Kim, K.S.; Choi, H.M.; Lee, Y.A.; Choi, I.A.; Lee, S.H.; Hong, S.J.; Yang, H.I.; Yoo, M.C.
Expression levels and association of gelatinases MMP-2 and MMP-9 and collagenases MMP-1 and MMP-13 with VEGF in synovial fluid of patients with arthritis
Rheumatol. Int.
31
543-547
2010
Homo sapiens
Manually annotated by BRENDA team
Li, C.H.; Cheng, Y.W.; Liao, P.L.; Yang, Y.T.; Kang, J.J.
Chloramphenicol causes mitochondrial stress, decreases ATP biosynthesis, induces matrix metalloproteinase-13 expression, and solid-tumor cell invasion
Toxicol. Sci.
116
140-150
2010
Homo sapiens
Manually annotated by BRENDA team
Giano, M.C.; Pochan, D.J.; Schneider, J.P.
Controlled biodegradation of self-assembling beta-hairpin peptide hydrogels by proteolysis with matrix metalloproteinase-13
Biomaterials
32
6471-6477
2011
Homo sapiens
Manually annotated by BRENDA team
Fobian, Y.M.; Freskos, J.N.; Barta, T.E.; Bedell, L.J.; Heintz, R.; Kassab, D.J.; Kiefer, J.R.; Mischke, B.V.; Molyneaux, J.M.; Mullins, P.; Munie, G.E.; Becker, D.P.
MMP-13 selective alpha-sulfone hydroxamates: Identification of selective P1 amides
Bioorg. Med. Chem. Lett.
21
2823-2825
2011
Homo sapiens
Manually annotated by BRENDA team
De Savi, C.; Morley, A.D.; Ting, A.; Nash, I.; Karabelas, K.; Wood, C.M.; James, M.; Norris, S.J.; Karoutchi, G.; Rankine, N.; Hamlin, G.; Macfaul, P.A.; Ryan, D.; Baker, S.V.; Hargreaves, D.; Gerhardt, S.
Selective non zinc binding inhibitors of MMP13
Bioorg. Med. Chem. Lett.
21
4215-4219
2011
Homo sapiens
Manually annotated by BRENDA team
Tommasi, R.A.; Weiler, S.; McQuire, L.W.; Rogel, O.; Chambers, M.; Clark, K.; Doughty, J.; Fang, J.; Ganu, V.; Grob, J.; Goldberg, R.; Goldstein, R.; Lavoie, S.; Kulathila, R.; Macchia, W.; Melton, R.; Springer, C.; Walker, M.; Zhang, J.; Zhu, L.; Shultz, M.
Potent and selective 2-naphthylsulfonamide substituted hydroxamic acid inhibitors of matrix metalloproteinase-13
Bioorg. Med. Chem. Lett.
21
6440-6445
2011
Homo sapiens
Manually annotated by BRENDA team
Vicini, P.; Crasc, L.; Incerti, M.; Ronsisvalle, S.; Cardile, V.; Panico, A.
Benzisothiazolyliminothiazolidin-4-ones with chondroprotective properties: Searching for potent and selective inhibitors of MMP-13
ChemMedChem
6
1199-1202
2011
Homo sapiens (P45452)
Manually annotated by BRENDA team
Zhang, L.; Yang, M.; Yang, D.; Cavey, G.; Davidson, P.; Gibson, G.
Molecular interactions of MMP-13 C-terminal domain with chondrocyte proteins
Connect. Tissue Res.
51
230-239
2010
Homo sapiens
Manually annotated by BRENDA team
Taylor, S.J.; Abeywardane, A.; Liang, S.; Muegge, I.; Padyana, A.K.; Xiong, Z.; Hill-Drzewi, M.; Farmer, B.; Li, X.; Collins, B.; Li, J.X.; Heim-Riether, A.; Proudfoot, J.; Zhang, Q.; Goldberg, D.; Zuvela-Jelaska, L.; Zaher, H.; Li, J.; Farrow, N.A.
Fragment-based discovery of indole inhibitors of matrix metalloproteinase-13
J. Med. Chem.
54
8174-8187
2011
Homo sapiens
Manually annotated by BRENDA team
Meierjohann, S.; Hufnagel, A.; Wende, E.; Kleinschmidt, M.A.; Wolf, K.; Friedl, P.; Gaubatz, S.; Schartl, M.
MMP13 mediates cell cycle progression in melanocytes and melanoma cells: in vitro studies of migration and proliferation
Mol. Cancer
9
201
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Naito, S.; Takahashi, T.; Onoda, J.; Yamauchi, A.; Kawai, T.; Kishino, J.; Yamane, S.; Fujii, I.; Fukui, N.; Numata, Y.
Development of a neutralizing antibody specific for the active form of matrix metalloproteinase-13
Biochemistry
51
8877-8884
2012
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Nara, H.; Sato, K.; Naito, T.; Mototani, H.; Oki, H.; Yamamoto, Y.; Kuno, H.; Santou, T.; Kanzaki, N.; Terauchi, J.; Uchikawa, O.; Kori, M.
Thieno[2,3-d]pyrimidine-2-carboxamides bearing a carboxybenzene group at 5-position: Highly potent, selective, and orally available MMP-13 inhibitors interacting with the S1'' binding site
Bioorg. Med. Chem.
22
5487-5505
2014
Homo sapiens (P45452)
Manually annotated by BRENDA team
Lu, H.; Wang, S.; Li, Q.; Wang, Y.
Design, synthesis and evaluation of 6-oxo-1, 6-dihydropyrimidine-2,5-dicarboxamide derivatives as MMP 13 inhibitors
Chem. Res. Chin. Univ.
29
67-70
2013
Homo sapiens (P45452)
-
Manually annotated by BRENDA team
Stura, E.A.; Visse, R.; Cuniasse, P.; Dive, V.; Nagase, H.
Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain
FASEB J.
27
4395-4405
2013
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Howes, J.M.; Bihan, D.; Slatter, D.A.; Hamaia, S.W.; Packman, L.C.; Knauper, V.; Visse, R.; Farndale, R.W.
The recognition of collagen and triple-helical toolkit peptides by MMP-13: sequence specificity for binding and cleavage
J. Biol. Chem.
289
24091-24101
2014
Homo sapiens (P45452)
Manually annotated by BRENDA team
Nara, H.; Sato, K.; Naito, T.; Mototani, H.; Oki, H.; Yamamoto, Y.; Kuno, H.; Santou, T.; Kanzaki, N.; Terauchi, J.; Uchikawa, O.; Kori, M.
Discovery of novel, highly potent, and selective quinazoline-2-carboxamide-based matrix metalloproteinase (MMP)-13 inhibitors without a zinc binding group using a structure-based design approach
J. Med. Chem.
57
8886-8902
2014
Homo sapiens (P45452)
Manually annotated by BRENDA team
Filomia, F.; Saxena, P.; Durante, C.; De Rienzo, F.; Cocchi, M.; Menziani, M.
Computational insights into ADAMTS4, ADAMTS5 and MMP13 inhibitor selectivity
Mol. Inform.
31
421-430
2012
Homo sapiens (P45452)
Manually annotated by BRENDA team
Nara, H.; Sato, K.; Kaieda, A.; Oki, H.; Kuno, H.; Santou, T.; Kanzaki, N.; Terauchi, J.; Uchikawa, O.; Kori, M.
Design, synthesis, and biological activity of novel, potent, and highly selective fused pyrimidine-2-carboxamide-4-one-based matrix metalloproteinase (MMP)-13 zinc-binding inhibitors
Bioorg. Med. Chem.
24
6149-6165
2016
Homo sapiens (P45452)
Manually annotated by BRENDA team
Satish Kumar, K.; Velayutham, R.; Roy, K.K.
A systematic computational analysis of human matrix metalloproteinase 13 (MMP-13) crystal structures and structure-based identification of prospective drug candidates as MMP-13 inhibitors repurposable for osteoarthritis
J. Biomol. Struct. Dyn.
12
1-13
2019
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team
Zhang, R.; Zhang, L.; Li, C.; Chen, B.; Li, Q.; Fang, X.; Shen, Y.
Refolding of recombinant histidine-tagged catalytic domain of MMP-13 from escherichia coli with ion-exchange chromatography for higher bioactivity
J. Liq. Chromatogr. Relat. Technol.
38
561-568
2015
Homo sapiens
-
Manually annotated by BRENDA team
Prystupa, A.; Szpetnar, M.; Boguszewska-Czubara, A.; Grzybowski, A.; Sak, J.; Zaluska, W.
Activity of MMP1 and MMP13 and amino acid metabolism in patients with alcoholic liver cirrhosis
Med. Sci. Monit.
21
1008-1014
2015
Homo sapiens (P45452), Homo sapiens
Manually annotated by BRENDA team