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(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2 + H2O
?
-
hydrolyzed 60 times more rapidly by metalloproteinase-3 than metalloproteinase-1, little discrimination between metalloproteinase-3 and metalloproteinase-2
-
-
?
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 + H2O
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu + norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
-
-
-
?
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 + H2O
?
-
a fluorogenic substrate selectively hydrolyzed by stromelysin 1
-
-
?
(7-methoxycoumarin-4-yl)acetyl-P-L-G-L-(L)-2,3-diaminopropionylamide-A-R + H2O
?
-
-
-
?
(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
-
-
-
?
(7-Methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly + H2O
?
-
hydrolyzed equally well by metalloproteinase-3 and metalloproteinase-2, metalloproteinase-1 shows 25% of the activity compared to metalloproteinase-3
-
-
?
2,4-Dinitrophenyl-Arg-Pro-Lys-Pro-Leu-Ala-norvaline-Trp-NH2 + H2O
2,4-Dinitrophenyl-Arg-Pro-Lys-Pro-Leu-Ala + norvaline-Trp-NH2
-
-
-
?
2,4-Dinitrophenyl-Pro-Leu-Gly-Ile-Ala-Gly-Arg-NH2 + H2O
?
-
-
-
-
?
2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Leu-Trp-Ala-D-Arg-NH2
-
-
-
?
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
6-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]hexanoy-L-Arg-L-Pro-L-Lys-L-Pro-L-Leu-L-Ala-L-Nva-L-Trp-L-Lys(7-dimethylaminocoumarin-4-yl)-NH2 + H2O
?
-
-
-
-
?
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester + H2O
?
-
-
-
-
?
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 + H2O
?
-
-
-
-
?
Aggrecan core protein + H2O
?
-
-
-
-
?
alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
alpha1-Antichymotrypsin + H2O
?
-
cleaves at the P1'-P2' bond
-
-
?
alpha1-antitrypsin + H2O
?
-
-
-
?
Antithrombin III + H2O
?
-
cleavage of the P1-P1' bond in the reactive center
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Nle-NH2 + H2O
?
-
-
-
-
?
Azocoll + H2O
?
-
-
-
-
?
Carboxymethyltransferrin + H2O
?
-
-
-
-
?
Collagen type III + H2O
?
-
-
-
-
?
cytosolic protein Apaf-1 + H2O
?
decorin + H2O
transforming growth factor-beta + ?
-
-
-
?
DQ-collagen I + H2O
?
-
-
-
-
?
DQ-collagen IV + H2O
?
-
-
-
-
?
elastin fELN-125 + H2O
?
-
-
-
-
?
fibrin + H2O
fibrin fragments + ?
-
-
-
?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
Immunoglobulin G2a + H2O
?
-
-
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys (Dnp) + H2O
?
-
-
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
-
fluorogenic substrate
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
NFF2 + H2O
?
quenched fluorescence substrate
-
?
osteopontin + H2O
?
-
-
-
?
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
triple helical peptide alpha1(V) + H2O
?
-
collagen V fibrils
-
-
?
Collagen type IV + H2O
additional information
-
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
-
-
-
-
?
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
-
-
-
?
alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
-
alpha1-proteinase inhibitor, cleavage within the reactive site loop
-
-
?
alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
-
-
-
-
?
beta-casein + H2O
?
-
-
-
?
beta-casein + H2O
?
-
-
-
?
beta-casein + H2O
?
-
-
-
-
?
cartilage + H2O
?
-
-
-
?
cartilage + H2O
?
-
-
-
?
cartilage + H2O
?
-
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
casein zymography assay
-
-
?
casein + H2O
?
-
casein zymography assay method
-
-
?
cytosolic protein Apaf-1 + H2O
?
-
-
-
?
cytosolic protein Apaf-1 + H2O
?
the 130 kD full-length Apaf-1 is truncated to about 37 kD and 20 kD proteins
-
-
?
Elastin + H2O
?
-
limited activity
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
limited activity
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
limited activity
-
-
?
Elastin + H2O
?
-
limited activity
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
-
-
-
?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
-
-
-
-
?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
-
-
-
-
?
Gelatin + H2O
?
-
type 1
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
type 1
-
-
?
Gelatin + H2O
?
-
limited activity
-
-
?
Gelatin + H2O
?
-
type 1
-
-
?
Gelatin + H2O
?
-
type 1
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
cleavage activity is barely detected as a much lower activity as reported
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
limited activity
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
-
fluorogenic substrate
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
-
fluorogenic substrate
-
-
?
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
activation
-
-
?
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
an additional cytosolic protein, possibly Apaf-1, is required for activation, rat substrate
-
-
?
Procollagen + H2O
?
-
removal of the NH2-terminal propeptides
-
-
?
Procollagen + H2O
?
-
chicken type I
-
-
?
Procollagen + H2O
?
-
removal of the NH2-terminal propeptides
-
-
?
Collagen type IV + H2O
additional information
-
-
-
-
-
?
Collagen type IV + H2O
additional information
-
-
-
-
-
?
Collagen type IV + H2O
additional information
-
-
-
4 major fragments of MW 165000, 145000, 125000 and 110000
?
Collagen type IV + H2O
additional information
-
-
-
-
-
?
Collagen type IV + H2O
additional information
-
-
-
-
-
?
Collagen type IV + H2O
additional information
-
-
no degradation of type I collagen
-
-
?
Collagen type IV + H2O
additional information
-
-
limited activity
-
-
?
additional information
?
-
-
activates procollagenase
-
-
?
additional information
?
-
-
activates progelatinase B
-
-
?
additional information
?
-
-
enzyme is secreted from the cells as an inactive zymogen
-
-
?
additional information
?
-
-
degrades a number of extracellular matrix components
-
-
?
additional information
?
-
-
participates in activation of procollagenases and progelatinase B
-
-
?
additional information
?
-
-
cleavage sites in natural proteins
-
-
?
additional information
?
-
-
activates procollagenase
-
-
?
additional information
?
-
-
activates procollagenase
-
-
?
additional information
?
-
-
activates progelatinase B
-
-
?
additional information
?
-
-
enzyme is secreted from the cells as an inactive zymogen
-
-
?
additional information
?
-
-
degrades a number of extracellular matrix components
-
-
?
additional information
?
-
-
participates in activation of procollagenases and progelatinase B
-
-
?
additional information
?
-
-
cleavage sites in natural proteins
-
-
?
additional information
?
-
-
tyoe I collagen is no substrate
-
?
additional information
?
-
-
may play a role in the normal turnover of the connective tissue matrix as well as in the joint destruction of chronic synovitis
-
-
?
additional information
?
-
-
believed to play a role in pathological conditions such as arthritis and tumor invasion
-
-
?
additional information
?
-
-
degrading all of the major macromolecules of the extracellular matrix
-
?
additional information
?
-
-
required for the degradation of extracellular matrix components during normal embryo development, morphogenesis and tissue remodelling
-
?
additional information
?
-
-
stromelysin (MMP3), through its action on collagen and other matrix metalloproteinases, influences arterial wall remodeling
-
-
?
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
?
additional information
?
-
the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
-
-
?
additional information
?
-
-
the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
-
-
?
additional information
?
-
the enzyme degrades several dentin matrix proteins, a demineralized and pretreated dentin block is used for activity assays. Enzyme MMP-3 is capable of degrading the protein core of proteoglycans, resulting in the release of soluble glycosaminoglycans
-
-
?
additional information
?
-
-
enzyme attacks the basal lamina and tight junction proteins, opening the blood-brain barrier and thereby facilitating neutrophil influx
-
-
?
additional information
?
-
-
enzyme is expressed as a protective response and plays an important role in host defense during squamous cell carcinoma tumorigenesis
-
-
?
additional information
?
-
-
genetic ablation of MMP-3 does not significantly affect tumor growth and metastasis in the MMTV-PyMT model
-
-
?
additional information
?
-
-
MMPs belong to a family of over 20 neutral endopeptidases that are collectively able to cleave all extracellular matrix components as well as many non-extracellular matrix proteins. The stromelysins, MMP-3, MMP-10 and MMP-11, have a domain arrangement similar to that of collagenases, but they do not cleave interstitial collagens
-
-
?
additional information
?
-
-
degradation of glomerular basement membrane
-
-
?
additional information
?
-
-
activates procollagenase
-
-
?
additional information
?
-
-
activates progelatinase B
-
-
?
additional information
?
-
-
enzyme is secreted from the cells as an inactive zymogen
-
-
?
additional information
?
-
-
degrades a number of extracellular matrix components
-
-
?
additional information
?
-
-
participates in activation of procollagenases and progelatinase B
-
-
?
additional information
?
-
-
cleavage sites in natural proteins
-
-
?
additional information
?
-
-
cleavage at multiple chondroitin sulfate-binding sites along the protein core
-
-
?
additional information
?
-
-
glomerular basement membrane degradation by glomeruli may be attributable to stromelysin and suggest an important role for these proteinases in glomerular pathophysiology
-
-
?
additional information
?
-
-
activates procollagenase
-
-
?
additional information
?
-
-
activates progelatinase B
-
-
?
additional information
?
-
-
enzyme is secreted from the cells as an inactive zymogen
-
-
?
additional information
?
-
-
degrades a number of extracellular matrix components
-
-
?
additional information
?
-
-
participates in activation of procollagenases and progelatinase B
-
-
?
additional information
?
-
-
cleavage sites in natural proteins
-
-
?
Proteoglycan + H2O
additional information
-
-
-
-
-
?
Proteoglycan + H2O
additional information
-
-
-
-
-
?
Proteoglycan + H2O
additional information
-
-
cartilage
degradation to 12.0 S fragments by the HMW form and 10.3 S fragments by the KMW enzyme
?
Proteoglycan + H2O
additional information
-
-
-
-
-
?
Proteoglycan + H2O
additional information
-
-
-
-
-
?
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(1R,2S)-2-((R)-sec-butyl)-N-hydroxy-3-((4-methoxyphenyl)sulfonyl)cyclopropanecarboxamide
-
-
(1R,3S)-N-hydroxy-2-((4-methoxyphenyl)sulfonyl)-3-((pyridin-3-yloxy)methyl)cyclopropanecarboxamide
-
-
(1R,3S)-N-hydroxy-2-((4-methoxyphenyl)sulfonyl)-3-(5-phenylpentyl)cyclopropanecarboxamide
-
-
(2S)-3-(4-fluorophenyl)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
-
(2S)-3-(benzyloxy)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
-
(2S)-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
(2S)-N-methyl-3-(4-nitrophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
-
(2S)-N-methyl-3-(pentafluorophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
(2S)-N-methyl-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
(betaR)-beta-[[[(1S)-1-[[[(1S)-2-methoxy-1-phenylethyl]amino]carbonyl]-2,2-dimethylpropyl]amino]carbonyl]-2-methyl-[1,1'-biphenyl]-4-hexanoic acid
-
UK-370106-COOH, potent inhibitor
1-([[4-(3,4-dimethylphenoxy)phenyl]sulfonyl]methyl)-N-hydroxy-4-(prop-2-yn-1-yl)cyclohexanecarboxamide
-
-
1-acetyl-N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
1-cyclopropyl-N-hydroxy-4-[(4-phenoxyphenyl)sulfonyl]piperidine-4-carboxamide
-
-
1-cyclopropyl-N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
1-[(1S)-1-(4-fluorobenzyl)-2-oxo-2-(4-pyridin-2-ylpiperazin-1-yl)ethyl]-3-(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)urea
-
-
1-[(1S)-2-oxo-1-(pentafluorobenzyl)-2-(4-pyridin-2-ylpiperazin-1-yl)ethyl]-3-(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)urea
-
-
2(R)-[2-(4'-fluoro-4-biphenylyl)ethyl]-4-(S9-n-butyl-1,5-pentanedioic acid 1)-(alpha(S)-tert-butylglycine methylamide) amide
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(3'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-1-yl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-2-yl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenethyl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenoxy-cyclohexa-1,5-dienyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-propyl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-styryl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-thiophen-3-yl-phenyl)-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-phenyl-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(1H-indol-2-yl)-phenyl]-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(tetrahydro-furan-2-yl)-phenyl]-hexanoic acid
-
-
2-Butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2',6'-dimethyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-sulfamoyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(3'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-formyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfinyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfonyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methoxy-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methylsulfanyl-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[1,1',4',1'']terphenyl-4-yl-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-(1H-imidazol-2-yl)-biphenyl-4-yl]-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-(1H-tetrazol-5-yl)-biphenyl-4-yl]-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-[(N-methyl-aminooxy)-methyl]-biphenyl-4-yl]-hexanoic acid
-
-
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-{4'-[(N-methyl-aminooxy)-methyl]-biphenyl-4-yl}-hexanoic acid
-
-
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
-
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4-propyl-phenyl)-hexanoic acid
-
-
2-Butyl-6-(2',4'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
2-Butyl-6-(3',5'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
2-Butyl-6-(3'-chloro-4'-fluoro-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
2-Butyl-6-(4'-chloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
2-Butyl-6-(4'-cyano-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
2-Butyl-6-(4-cycloheptyl-phenyl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
2-Butyl-6-[4'-(N,N-dimethyl-aminooxymethyl)-biphenyl-4-yl]-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
2-[(2-biphenyl-4-ylethyl)(methyl)sulfamoyl]-N-hydroxyacetamide
-
-
2-[(3-biphenyl-4-ylazetidin-1-yl)sulfonyl]-N-hydroxyacetamide
-
-
2-[(3-biphenyl-4-ylpropyl)(methyl)sulfamoyl]-N-hydroxyacetamide
-
-
2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
-
-
2-[(4-biphenyl-4-ylpiperidin-1-yl)sulfonyl]-N-hydroxyacetamide
-
-
2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
-
-
2-[(biphenyl-4-ylmethyl)(methyl)sulfamoyl]-N-hydroxyacetamide
-
-
2-[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
-
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
-
2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
-
2-[[3-(biphenyl-4-yloxy)azetidin-1-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
-
-
2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
3-(4'-cyanobiphenyl-4-yloxy)-N-hydroxypropionamide
-
-
3-(hydroxycarbamoyl)-1-[(4-phenoxybenzoyl)amino]pentyl 2,2-dimethylpropanoate
-
-
3-ethyl-N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
3-[(4'-cyanobiphenyl-4-yl)oxy]-N-hydroxypropanamide
-
-
3-[(benzyloxy)methyl]-N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
3-[(benzylsulfanyl)methyl]-N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid
-
-
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid methyl ester
-
-
4'-{5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl}-biphenyl-4-carboxylic acid
-
-
4'-{5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl}-biphenyl-4-carboxylic acid methyl ester
-
-
4-(1-benzofuran-2-yl)-N-[(2S)-1-hydroxy-5-(hydroxyamino)-5-oxopentan-2-yl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(2S)-2-hydroxy-4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(2S)-4-(hydroxyamino)-2-(methoxymethoxy)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(2S)-5-(hydroxyamino)-1-(methoxymethoxy)-5-oxopentan-2-yl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(3R)-3-[(benzyloxy)methyl]-4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[(3S)-3-hydroxy-4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[3-(hydroxycarbamoyl)-6-phenylhexyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[3-benzyl-4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(1-benzofuran-2-yl)-N-[4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-(hydroxyamino)-3-methyl-4-oxo-1-[(4-phenoxybenzoyl)amino]butyl 2,2-dimethylpropanoate
-
-
4-([[4-(4-chlorophenoxy)phenyl]sulfonyl]methyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([[4-(biphenyl-4-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-(2-phenylethyl)piperidine-4-carboxamide
-
-
4-([[4-(biphenyl-4-yloxy)phenyl]sulfonyl]methyl)-N-hydroxypiperidine-4-carboxamide
-
-
4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
-
-
4-[(E)-2-(4-chlorophenyl)ethenyl]-N-[4-(hydroxyamino)-4-oxobutyl]benzamide
-
-
4-[[4-(4-chlorophenoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
5-methyl-5-(4-phenoxy-phenyl)-pyrimidine-2,4,6-trione
MPPT, enzyme binding structure analysis
6-(3'-Amino-biphenyl-4-yl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
6-(4'-Aminooxymethyl-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
6-(4'-Bromo-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
-
6-(4-Benzyl-phenyl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
6-(4-Benzyloxy-phenyl)-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
6-Biphenyl-4-yl-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
-
Alpha-macroglobulin
-
-
-
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]-carbonyl]amino]-3-hydroxy-N-methyl-(S)-propanamide
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]amino]-N,N-dimethyl-(S)-benzenepropanamide
amide substituted piperazine-based MMP inhibitor
-
-
-
benzyl [3-[(biphenyl-4-ylsulfonyl)(propan-2-yloxy)amino]-4-(hydroxyamino)-4-oxobutyl]carbamate
-
-
butanolic extract of propolis sample
-
-
-
carboxylic acid diphenylpiperidine inhibitor
-
-
-
dexamethasone
-
inhibits active MMP-3, significantly decreases the ratio of active MMP-3 to total MMP-3 activity
dichloro[[(methylsulfinyl-kappaS)methyl]phosphonate-kappaO'']platinum
-
-
galardin
-
Glycomed GM-6001, clinically advanced MMP inhibitor, effective in treatment of corneal ulcers
HONH-CO-CH2-CH(n-pentyl)-CO-Leu-Phe-NH2
-
-
Hydroxamate-containing peptide inhibitor
-
-
-
hydroxamic acid diphenylpiperidine inhibitor
-
-
-
hydroxamic acid inhibitor CGS 27023
-
-
hydroxamic acid substrate mimetic inhibitor
-
U24522
-
interleukin-1 receptor antagonist
-
inhibits active MMP-3
-
L-asparaginyl-L-asparaginylglycyl-L-histidine
-
N-(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)-N'-(2-phenethyl)urea
-
-
N-(biphenyl-4-ylsulfonyl)-N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]glycine
-
-
N-(Carboxyalkyl)dipeptide
-
Ala[N]homophenylalanine-Leu-anilide
-
N-alkyl-and heterocycle-substitited piperazine-based MMP inhibitor
-
-
-
N-hydroxy-1-(2-methoxyethyl)-4-[(4-phenoxyphenyl)sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-1-(2-methoxyethyl)-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-1-methyl-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethyl-3-[[(2-phenylethyl)sulfanyl]methyl]prolinamide
-
-
N-hydroxy-1-[(methylsulfonyl)oxy]-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-1-[[(4-phenoxyphenyl)sulfonyl]methyl]-4-(prop-2-yn-1-yl)cyclohexanecarboxamide
-
-
N-hydroxy-2-([4-[2-(trifluoromethyl)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
N-hydroxy-2-([4-[2-methyl-3'-(trifluoromethoxy)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
N-hydroxy-2-([4-[3'-(2-hydroxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
-
-
N-hydroxy-2-([4-[3'-(2-methoxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
-
-
N-hydroxy-2-([4-[3'-(methoxymethyl)-2-methylbiphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
N-hydroxy-2-methyl-2-[(4-[2-methyl-3'-[2-(methylamino)ethoxy]biphenyl-4-yl]piperidin-1-yl)sulfonyl]propanamide
-
-
N-hydroxy-2-[(4-[4-[6-(2-hydroxyethoxy)pyridin-2-yl]-3-methylphenyl]piperidin-1-yl)sulfonyl]-2-methylpropanamide
-
-
N-hydroxy-2-[N-(2-hydroxyethyl)biphenyl-4-sulfonamide] hydroxamic acid
-
-
N-hydroxy-2-[[4-(2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
-
-
N-hydroxy-2-[[4-(3'-methoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
-
-
N-hydroxy-2-[[4-(4-phenoxyphenyl)piperidin-1-yl]sulfonyl]acetamide
-
-
N-hydroxy-3-(hydroxymethyl)-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
N-hydroxy-3-[(1R)-1-hydroxy-2-(phenylsulfanyl)ethyl]-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
N-hydroxy-3-[(1S)-1-hydroxy-2-(phenylsulfanyl)ethyl]-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
N-hydroxy-3-[[(4-methoxybenzyl)sulfanyl]methyl]-1-[(4-methoxyphenyl)sulfonyl]-4,4-dimethylprolinamide
-
-
N-hydroxy-4-[(4-phenoxyphenyl)sulfonyl]-1-(prop-2-yn-1-yl)piperidine-4-carboxamide
-
-
N-hydroxy-4-[(4-phenoxyphenyl)sulfonyl]piperidine-4-carboxamide
-
-
N-hydroxy-4-[[(4-phenoxyphenyl)sulfonyl]methyl]-1-(2-phenylethyl)piperidine-4-carboxamide
-
-
N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]-1-(prop-2-en-1-yl)piperidine-4-carboxamide
-
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-(2-methylpropyl)phenyl-D-methioninamide
-
-
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
-
-
N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)acetamide
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-methoxyphenyl)sulfonyl]glycine
-
-
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
-
-
N-[1-(ethoxymethoxy)-3-(hydroxycarbamoyl)pentyl]-4-phenoxybenzamide
-
-
N-[1-(ethoxymethoxy)-4-(hydroxyamino)-3-methyl-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[1-hydroxy-4-(hydroxyamino)-3-methyl-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[3-(hydroxycarbamoyl)-1-[(2-methoxyethoxy)methoxy]pentyl]-4-phenoxybenzamide
-
-
N-[4-(hydroxyamino)-1-[(2-methoxyethoxy)methoxy]-3-methyl-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[4-(hydroxyamino)-3-methyl-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[4-(hydroxyamino)-4-oxobutyl]-4-phenoxybenzamide
-
-
N-[4-(hydroxyamino)-4-oxobutyl]-4-[(E)-2-(4-hydroxyphenyl)ethenyl]benzamide
-
-
N-[4-(hydroxyamino)-4-oxobutyl]-4-[(E)-2-(4-methoxyphenyl)ethenyl]benzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)-5,5-dimethylhexan-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)-7,7-dimethyl-6-oxooctan-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)hept-6-en-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)heptan-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)hexan-2-yl]-4-phenoxybenzamide
-
-
N-[4-(hydroxycarbamoyl)-1-(methoxymethoxy)octan-2-yl]-4-phenoxybenzamide
-
-
N-[4-hydroxy-5-(hydroxyamino)-1-(methoxymethoxy)-5-oxopentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-4-(naphthalen-1-ylmethyl)-5-oxopentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-4-methyl-5-oxopentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxo-4-(1l4-thiopyran-1-yl)pentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxo-4-(pyridin-2-ylmethyl)pentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxo-4-(pyridin-3-ylmethyl)pentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxo-4-(pyridin-4-ylmethyl)pentan-2-yl]-4-phenoxybenzamide
-
-
N-[5-(hydroxyamino)-1-(methoxymethoxy)-5-oxopentan-2-yl]-4-phenoxybenzamide
-
-
N-[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]-L-phenylalanine methyl ester
-
-
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
-
-
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)valinamide
-
-
Peptides based on the N-terminal domain of tissue inhibitor of metalloproteinase-1
-
-
-
Phthaloyl-N-(CH2)4-P(O2-)-Ile-(2-naphthyl)-Ala-NH-CH3
-
-
Specific metalloproteinase inhibitor
-
sulfonamide-and carbamide substituted piperazine-based MMP inhibitor
-
-
-
TIMP-3
-
is induced by enamel matrix derivative
-
Tissue inhibitor of metalloproteinases
-
TIMP-1 and TIMP-2
-
tissue inhibitor of metalloproteinases 1
TIMP-1, enzyme binding structure analysis and mechanism of inhibition, detailed overview and comparison to stromelysin-2, EC 3.4.24.22
-
tissue inhibitor of metalloproteinases 2
TIMP-2
-
TNF
-
inhibits active MMP-3
-
U24522
-
synthetic inhibitor known to inhibit proteoglycan-degrading metalloproteinases
UK-370106-COCHO
-
glyoxal inhibitor, created by conversion of the carboxylate group of UK-370106-COOH to a glyoxal group. At pH 5.5-6.5 the glyoxal inhibitor is a potent inhibitor of stromelysin-1
urea substituted piperazine-based MMP inhibitor
-
-
-
Z-L-tryptophan
inhibits full length stromelysin_1-477 and truncated stromelysin_100-264, enzyme binding structure and kinetics, chemical shift of the carboxylate carbon upon enzyme binding, overview. The tryptophan side chain can bind in the S1 specificity site of stromelysin with the tryptophan alpha carboxylate group coordinated to the active site zinc atom
[4-(4-phenyl-piperidin-1-yl)-benzenesulfonylamino]-acetic acid
PBSA, enzyme binding structure analysis
[dimethylpropanedioato(2-)-kappa2O1,O3][[(methylsulfinyl-kappaS)methyl]phosphonate-kappaO''']platinum
-
-
(2S)-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
-
(2S)-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
computational modeling of enzyme-inhibitor complex
(2S)-N-methyl-3-(pentafluorophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
i.e. PNU-142372
(2S)-N-methyl-3-(pentafluorophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
i.e. PNU-142372, computational modeling of enzyme-inhibitor complex
(2S)-N-methyl-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
i.e. PNU-107859
(2S)-N-methyl-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
i.e. PNU-107859, computational modeling of enzyme-inhibitor complex
1,10-phenanthroline
-
-
2(R)-[2-(4'-fluoro-4-biphenylyl)ethyl]-4-(S9-n-butyl-1,5-pentanedioic acid 1)-(alpha(S)-tert-butylglycine methylamide) amide
-
L-758,354
2(R)-[2-(4'-fluoro-4-biphenylyl)ethyl]-4-(S9-n-butyl-1,5-pentanedioic acid 1)-(alpha(S)-tert-butylglycine methylamide) amide
-
compound 26, L-758,354
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]-carbonyl]amino]-3-hydroxy-N-methyl-(S)-propanamide
-
-
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]-carbonyl]amino]-3-hydroxy-N-methyl-(S)-propanamide
-
computational modeling of enzyme-inhibitor complex
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]amino]-N,N-dimethyl-(S)-benzenepropanamide
-
-
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]amino]-N,N-dimethyl-(S)-benzenepropanamide
-
computational modeling of enzyme-inhibitor complex
curcumin
i.e. 1,7-bis (4-hydroxy-3-methoxyphenol)-1,6-heptadiene-3,5-dione, molecular docking and prediction of binding interactions of curcumin with active site residues
curcumin
-
curcumin dose dependently suppresses MMP-3 and-9 activity during eradication of Helicobacter pylori from infected mice
DTT
-
-
EDTA
-
-
N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)acetamide
-
-
N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)acetamide
-
computational modeling of enzyme-inhibitor complex
Specific metalloproteinase inhibitor
-
isolated from human amniotic fluid
-
Specific metalloproteinase inhibitor
-
bovine-nasal cartilage extract; isolated from human amniotic fluid; rabbit bone culture medium
-
TIMP-1
-
-
-
TIMP-1
-
upregulated with age
-
TIMP-1
-
determination in cell culture medium
-
TIMP-1
-
no apparent regulation of the expression of TIMP-1 by either tumor necrosis factor or enamel matrix derivative
-
TIMP-1
-
TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
-
TIMP-2
-
physiolocic inhibitor of matrix metalloproteinases
-
TIMP-2
-
determination in cell culture medium
-
TIMP-2
-
highly produced in brain microvessels
-
additional information
-
not: inhibitors for serine, cysteine or aspartic proteinases
-
additional information
-
not: inhibitors for serine, cysteine or aspartic proteinases; phosphoramidon
-
additional information
-
X-ray diffraction analysis of the three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme
-
additional information
-
the flavonols quercetin and kaempferol have higher anti-invasion potency and higher MMP-3 inhibitory activity than isoflavones genistein, genistin and daidzein, but neither flavonols nor isoflavones have any effect on MMP-3 secretion
-
additional information
-
ligand binding, inhibitory potencies, 3D-QSAR modelling, and crystal structures, overview. Usage of multitemplate alignment method for the development of a 3D QSAR model
-
additional information
drug discovery via thermodynamic additivity, thermodynamic additivity analysis using stromelysin-1 and a series of biphenyl hydroxamate ligands identified through fragment additivity, overview. Additivity arises from enthalpic effects, while interaction entropies are unfavorable, the thermodynamic behavior is masked by proton transfer
-
additional information
grapefruit seed extracts inhibit dentin matrix degradation by the enzyme. A grape seed extract mouthrinse and its active components not only have an anti-MMP action but also modify the dentin surface accessibility. The mouthrinse and its active components appear to limit the disorganization inside dentinal tubules induced by the MMP-3 action
-
additional information
interactions of curcumin with MMP-3 are compared to those of two known inhibitors of the enzyme, PBSA and MPPT, curcumin binds with affinity comparable to or better than the two known inhibitors
-
additional information
-
diisopropylphosphofluoridate; pepstatin; phenylmethanesulfonyl fluoride; soybean trypsin inhibitor
-
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0.0001
(2S)-3-(4-fluorophenyl)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25°C
0.002
(2S)-3-(benzyloxy)-N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25°C
0.0033
(2S)-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25°C
0.00033
(2S)-N-methyl-3-(4-nitrophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25°C
0.000018
(2S)-N-methyl-3-(pentafluorophenyl)-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25°C
0.00071
(2S)-N-methyl-3-phenyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)propanamide
-
pH 7.6, 25°C
0.00027
1-[(1S)-1-(4-fluorobenzyl)-2-oxo-2-(4-pyridin-2-ylpiperazin-1-yl)ethyl]-3-(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)urea
-
pH 7.6, 25°C
0.000014
1-[(1S)-2-oxo-1-(pentafluorobenzyl)-2-(4-pyridin-2-ylpiperazin-1-yl)ethyl]-3-(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)urea
-
pH 7.6, 25°C
0.0011
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(3'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.00001
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000037
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4'-trifluoromethyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.002
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-1-yl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.00012
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-naphthalen-2-yl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.00049
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenethyl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.0002
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-phenoxy-cyclohexa-1,5-dienyl)-hexanoic acid
-
pH 6.5, 25°C
0.00014
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-propyl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.00065
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-styryl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.000015
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-(4-thiophen-3-yl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.0038
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-phenyl-hexanoic acid
-
pH 6.5, 25°C
0.000012
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(1H-indol-2-yl)-phenyl]-hexanoic acid
-
pH 6.5, 25°C
0.0014
2-Butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-6-[4-(tetrahydro-furan-2-yl)-phenyl]-hexanoic acid
-
pH 6.5, 25°C
0.000004
2-Butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.0012
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2',6'-dimethyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000011
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.0094
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(2'-sulfamoyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000021
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(3'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000015
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-formyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000052
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfinyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000021
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methanesulfonyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000013
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methoxy-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000005
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-(4'-methylsulfanyl-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000039
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[1,1',4',1'']terphenyl-4-yl-hexanoic acid
-
pH 6.5, 25°C
0.000025
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-(1H-imidazol-2-yl)-biphenyl-4-yl]-hexanoic acid
-
pH 6.5, 25°C
0.00035
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-(1H-tetrazol-5-yl)-biphenyl-4-yl]-hexanoic acid
-
pH 6.5, 25°C
0.000049
2-Butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-6-[4'-[(N-methyl-aminooxy)-methyl]-biphenyl-4-yl]-hexanoic acid
-
pH 6.5, 25°C
0.000002
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4'-fluoro-biphenyl-4-yl)-hexanoic acid
-
pH 6.5, 25°C
0.000011
2-Butyl-4-[2,2-dimethyl-1-(pyridin-4-ylcarbamoyl)-propylcarbamoyl]-6-(4-propyl-phenyl)-hexanoic acid
-
pH 6.5, 25°C
0.000012
2-Butyl-6-(2',4'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.0015
2-Butyl-6-(3',5'-dichloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.000019
2-Butyl-6-(3'-chloro-4'-fluoro-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.000013
2-Butyl-6-(4'-chloro-biphenyl-4-yl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.000009
2-Butyl-6-(4'-cyano-biphenyl-4-yl)-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.000095
2-Butyl-6-(4-cycloheptyl-phenyl)-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.00004
2-Butyl-6-[4'-(N,N-dimethyl-aminooxymethyl)-biphenyl-4-yl]-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.00025
3-(4'-cyanobiphenyl-4-yloxy)-N-hydroxypropionamide
-
-
0.00069
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid
-
pH 6.5, 25°C
0.000031
4'-[5-Carboxy-3-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-nonyl]-biphenyl-4-carboxylic acid methyl ester
-
pH 6.5, 25°C
0.00005
5-methyl-5-(4-phenoxy-phenyl)-pyrimidine-2,4,6-trione
pH and temperature not specified in the publication
0.000027
6-(3'-Amino-biphenyl-4-yl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.000024
6-(4'-Aminooxymethyl-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.000011
6-(4'-Bromo-biphenyl-4-yl)-2-butyl-4-[(2,2-dimethyl-1-methylcarbamoyl-propylamino)-hydroxy-methyl]-hexanoic acid
-
pH 6.5, 25°C
0.0014
6-(4-Benzyl-phenyl)-2-butyl-4-(2,2-dimethyl-1-phenylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.000074
6-(4-Benzyloxy-phenyl)-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.0015
6-Biphenyl-4-yl-2-butyl-4-(2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-hexanoic acid
-
pH 6.5, 25°C
0.031
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]-carbonyl]amino]-3-hydroxy-N-methyl-(S)-propanamide
-
pH 7.6, 25°C
0.0023
alpha-[[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]amino]-N,N-dimethyl-(S)-benzenepropanamide
-
pH 7.6, 25°C
0.000036
curcumin
pH and temperature not specified in the publication
0.000013
hydroxamic acid inhibitor CGS 27023
-
pH 6.8, 37°C
0.00031
L-696,418
-
pH 6.5, 25°C
0.00013
L-asparaginyl-L-asparaginylglycyl-L-histidine
pH and temperature not specified in the publication
0.007
N-(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)-N'-(2-phenethyl)urea
-
pH 7.6, 25°C
0.00018
N-hydroxy-2-[N-(2-hydroxyethyl)biphenyl-4-sulfonamide] hydroxamic acid
-
-
0.0013
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
-
-
0.166
N-methyl-2-(([(5-thioxo-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]carbonyl)amino)acetamide
-
pH 7.6, 25°C
0.00029
N-[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]-L-phenylalanine methyl ester
-
pH 7.6, 25°C
0.00000013
tissue inhibitor of metalloproteinases 1
catalytic enzyme domain, pH 7.0, 37°C
-
0.00000055
tissue inhibitor of metalloproteinases 2
catalytic enzyme domain, pH 7.0, 37°C
-
0.001 - 0.0188
UK-370106-COCHO
0.0063 - 0.052
Z-L-tryptophan
0.000098
[4-(4-phenyl-piperidin-1-yl)-benzenesulfonylamino]-acetic acid
pH and temperature not specified in the publication
0.001
UK-370106-COCHO
-
pH 5.5-6.5, 25°C
0.0107
UK-370106-COCHO
-
pH 7.56, 37°C
0.0188
UK-370106-COCHO
-
pH 7.56, 25°C
0.0063
Z-L-tryptophan
pH 6.0, 25°C, recombinant full-length enzyme stromelysin1-477, enzyme contains Zn2+
0.021
Z-L-tryptophan
pH 6.0, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Zn2+
0.03
Z-L-tryptophan
pH 6.0, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Co2+
0.034
Z-L-tryptophan
pH 5.0, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Zn2+
0.052
Z-L-tryptophan
pH 7.1, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Zn2+
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Catalytic domain comparisons of human fibroblast-type collagenase, stromelysin-1, and matrilysin
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1997
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513-524
2000
Homo sapiens (P45452), Homo sapiens
brenda
Gomis-Rueth, F.X.; Maskos, K.; Betz, M.; Bergner, A.; Huber, R.; Suzuki, K.; Yoshida, N.; Nagase, H.; Brew, K.; Bourenkov, G.P.; Bartunik, H.; Bode, W.
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
Nature
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1997
Homo sapiens
brenda
del Mar Barbacid, M.; Fernandez-Resa, P.; Buesa, J.M.; Marquez, G.; Aracil, M.; Quesada, A.R.; Mira, E.
Expression and purification of human stromelysin 1 and 3 from baculovirus-infected insect cells
Protein Expr. Purif.
13
243-250
1998
Homo sapiens
brenda
Van Themsche, C.; Potworowski, E.F.; St-Pierre, Y.
Stromelysin-1 (MMP-3) is inducible in T lymphoma cells and accelerates the growth of lymphoid tumors in vivo
Biochem. Biophys. Res. Commun.
315
884-891
2004
Mus musculus
brenda
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
brenda
Huet, E.; Cauchard, J.; Berton, A.; Robinet, A.; Decarme, M.; Hornebeck, W.; Bellon, G.
Inhibition of plasmin-mediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5. [Erratum to document cited in CA140:297422]
Biochem. Pharmacol.
67
1011
2004
Homo sapiens
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brenda
McCawley, L.J.; Crawford, H.C.; King, L.E.; Mudgett, J.; Matrisian, L.M.
A protective role for matrix metalloproteinase-3 in squamous cell carcinoma
Cancer Res.
64
6965-6972
2004
Mus musculus
brenda
Chen, D.Y.; Lan, J.L.; Lin, F.J.; Hsieh, T.Y.
Elevated levels of soluble Fas (APO-1, CD95), soluble Fas ligand, and matrix metalloproteinase-3 in sera from patients with active untreated adult onset Stills disease
Clin. Rheumatol.
26
393-400
2007
Homo sapiens
brenda
Calabro, A.; Grappone, C.; Pellegrini, G.; Evangelista, S.; Tramontana, M.; Schuppan, D.; Herbst, H.; Milani, S.
Spatial and temporal pattern of expression of interstitial collagenase, stromelysin/transin, gelatinase A, and TIMP-1 during experimental gastric ulcer healing
Digestion
70
127-138
2004
Rattus norvegicus
brenda
Kim, H.J.; Fillmore, H.L.; Reeves, T.M.; Phillips, L.L.
Elevation of hippocampal MMP-3 expression and activity during trauma-induced synaptogenesis
Exp. Neurol.
192
60-72
2005
Rattus norvegicus
brenda
Lee, M.; Hadi, M.; Hallden, G.; Aponte, G.W.
Peptide YY and neuropeptide Y induce villin expression, reduce adhesion, and enhance migration in small intestinal cells through the regulation of CD63, matrix metalloproteinase-3, and Cdc42 activity
J. Biol. Chem.
280
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2005
Rattus norvegicus
brenda
Gonzalez-Cuevas, J.; Bueno-Topete, M.; Armendariz-Borunda, J.
Urokinase plasminogen activator stimulates function of active forms of stromelysin and gelatinases (MMP-2 and MMP-9) in cirrhotic tissue
J. Gastroenterol. Hepatol.
21
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2006
Rattus norvegicus
brenda
Park, C.H.; Lee, M.J.; Ahn, J.; Kim, S.; Kim, H.H.; Kim, K.H.; Eun, H.C.; Chung, J.H.
Heat shock-induced matrix metalloproteinase (MMP)-1 and MMP-3 are mediated through ERK and JNK activation and via an autocrine interleukin-6 loop
J. Invest. Dermatol.
123
1012-1019
2004
Homo sapiens
brenda
Jacobsen, E.J.; Mitchell, M.A.; Hendges, S.K.; Belonga, K.L.; Skaletzky, L.L.; Stelzer, L.S.; Lindberg, T.J.; Fritzen, E.L.; Schostarez, H.J.; OSullivan, T.J.; Maggiora, L.L.; Stuchly, C.W.; Laborde, A.L.; Kubicek, M.F.; Poorman, R.A.; Beck, J.M.; Miller, H.R.; Petzold, G.L.; Scott, P.S.; Truesdell, S.E.; Wallace, T.L.; Wilks, J.W.; Fisher, C.; Goodman, L.V.; Kaytes, P.S.; Ledbetter, S.R.; Powers, E.A.
Synthesis of a series of stromelysin-selective thiadiazole urea matrix metalloproteinase inhibitors
J. Med. Chem.
42
1525-1536
1999
Homo sapiens
brenda
Rizzo, R.C.; Toba, S.; Kuntz, I.D.
A molecular basis for the selectivity of thiadiazole urea inhibitors with stromelysin-1 and gelatinase-A from generalized born molecular dynamics simulations
J. Med. Chem.
47
3065-3074
2004
Homo sapiens
brenda
Tas, F.; Duranyildiz, D.; Oguz, H.; Disci, R.; Kurul, S.; Yasasever, V.; Topuz, E.
Serum matrix metalloproteinase-3 and tissue inhibitor of metalloproteinase-1 in patients with malignant melanoma
Med. Oncol.
22
39-44
2005
Homo sapiens
brenda
Gurney, K.J.; Estrada, E.Y.; Rosenberg, G.A.
Blood-brain barrier disruption by stromelysin-1 facilitates neutrophil infiltration in neuroinflammation
Neurobiol. Dis.
23
87-96
2006
Mus musculus
brenda
Uzan, C.; Cortez, A.; Dufournet, C.; Fauvet, R.; Siffroi, J.P.; Darai, E.
Eutopic endometrium and peritoneal, ovarian and bowel endometriotic tissues express a different profile of matrix metalloproteinases-2, -3 and -11, and of tissue inhibitor metalloproteinases-1 and -2
Virchows Arch.
445
603-609
2004
Homo sapiens
brenda
Geurts, N.; Martens, E.; Van Aelst, I.; Proost, P.; Opdenakker, G.; Van den Steen, P.E.
Beta-hematin interaction with the hemopexin domain of gelatinase B/MMP-9 provokes autocatalytic processing of the propeptide, thereby priming activation by MMP-3
Biochemistry
47
2689-2699
2008
Homo sapiens
brenda
Jin, X.; Yagi, M.; Akiyama, N.; Hirosaki, T.; Higashi, S.; Lin, C.Y.; Dickson, R.B.; Kitamura, H.; Miyazaki, K.
Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis
Cancer Sci.
97
1327-1334
2006
Mus musculus
brenda
Meijer, M.J.; Mieremet-Ooms, M.A.; van der Zon, A.M.; van Duijn, W.; van Hogezand, R.A.; Sier, C.F.; Hommes, D.W.; Lamers, C.B.; Verspaget, H.W.
Increased mucosal matrix metalloproteinase-1, -2, -3 and -9 activity in patients with inflammatory bowel disease and the relation with Crohns disease phenotype
Dig. Liver Dis.
39
733-739
2007
Homo sapiens
brenda
Fukuda, K.; Fujitsu, Y.; Kumagai, N.; Nishida, T.
Inhibition of matrix metalloproteinase-3 synthesis in human conjunctival fibroblasts by interleukin-4 or interleukin-13
Invest. Ophthalmol. Vis. Sci.
47
2857-2864
2006
Homo sapiens
brenda
Alcaraz, L.A.; Banci, L.; Bertini, I.; Cantini, F.; Donaire, A.; Gonnelli, L.
Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors
J. Biol. Inorg. Chem.
12
1197-1206
2007
Homo sapiens
brenda
Sasanelli, R.; Boccarelli, A.; Giordano, D.; Laforgia, M.; Arnesano, F.; Natile, G.; Cardellicchio, C.; Capozzi, M.A.; Coluccia, M.
Platinum complexes can inhibit matrix metalloproteinase activity: platinum-diethyl[(methylsulfinyl)methyl]phosphonate complexes as inhibitors of matrix metalloproteinases 2, 3, 9, and 12
J. Med. Chem.
50
3434-3441
2007
Homo sapiens
brenda
Handley, S.A.; Miller, V.L.
General and specific host responses to bacterial infection in Peyers patches: a role for stromelysin-1 (matrix metalloproteinase-3) during Salmonella enterica infection
Mol. Microbiol.
64
94-110
2007
Mus musculus
brenda
Baillat, D.; Leprivier, G.; Regnier, D.; Vintonenko, N.; Begue, A.; Stehelin, D.; Aumercier, M.
Stromelysin-1 expression is activated in vivo by Ets-1 through palindromic head-to-head Ets binding sites present in the promoter
Oncogene
25
5764-5776
2006
Oryctolagus cuniculus
brenda
Bhuvarahamurthy, V.; Kristiansen, G.O.; Johannsen, M.; Loening, S.A.; Schnorr, D.; Jung, K.; Staack, A.
In situ gene expression and localization of metalloproteinases MMP1, MMP2, MMP3, MMP9, and their inhibitors TIMP1 and TIMP2 in human renal cell carcinoma
Oncol. Rep.
15
1379-1384
2006
Homo sapiens
brenda
Chen, C.; Lin, K.; Yu, D.T.; Yang, C.; Huang, F.; Chen, H.; Liang, T.; Liao, H.; Tsai, C.; Wei, J.C.; Chou, C.
Serum matrix metalloproteinases and tissue inhibitors of metalloproteinases in ankylosing spondylitis: MMP-3 is a reproducibly sensitive and specific biomarker of disease activity
Rheumatology
45
414-420
2006
Homo sapiens
brenda
Whitlock, G.A.; Dack. K.N.; Dickinson, R.P.; Lewis M.L
A novel series of highly selective inhibitors of MMP-3
Bioorg. Med. Chem. Lett.
17
6750-6753
2007
Homo sapiens
brenda
Irace, C.; Cortese, C.; Migale, M.; Liberatoscioli, L.; Mannucci, L.; Federici, G.; Gnasso, A.
Stromelysin gene promoter polymorphism and common carotid geometry in diabetic subjects
Int. Angiol.
27
413-418
2008
Homo sapiens
brenda
Juncker-Jensen, A.; Romer, J.; Pennington, C.J.; Lund, L.R.; Almholt, K.
Spontaneous metastasis in matrix metalloproteinase 3-deficient mice
Mol. Carcinog.
48
618-625
2009
Mus musculus
brenda
Chang, Y.W.; Oh, H.C.; Jang, J.Y.; Hwangbo, Y.; Lee, J.W.; Lee, H.J.; Joo, K.R.; Dong, S.H.; Kim, S.S.; Kim, H.J.; Kim, B.H.; Chang, R.
IL-1beta and IL-8, matrix metalloproteinase 3, and pepsinogen secretion before and after H. pylori eradication in gastroduodenal phenotypes
Scand. J. Gastroenterol.
43
1184-1193
2008
Homo sapiens
brenda
Phromnoi, K.; Yodkeeree, S.; Anuchapreeda, S.; Limtrakul, P.
Inhibition of MMP-3 activity and invasion of the MDA-MB-231 human invasive breast carcinoma cell line by bioflavonoids
Acta Pharmacol. Sin.
30
1169-1176
2009
Homo sapiens
brenda
Genevay, S.; Finckh, A.; Mezin, F.; Tessitore, E.; Guerne, P.A.
Influence of cytokine inhibitors on concentration and activity of MMP-1 and MMP-3 in disc herniation
Arthritis Res. Ther.
11
R169
2009
Homo sapiens
brenda
Lijnen, H.R.; Van Hoef, B.; Rodriguez, J.A.; Paramo, J.A.
Stromelysin-2 (MMP-10) deficiency does not affect adipose tissue formation in a mouse model of nutritionally induced obesity
Biochem. Biophys. Res. Commun.
389
378-381
2009
Mus musculus
brenda
Lee, E.J.; Kim, S.Y.; Hyun, J.W.; Min, S.W.; Kim, D.H.; Kim, H.S.
Glycitein inhibits glioma cell invasion through down-regulation of MMP-3 and MMP-9 gene expression
Chem. Biol. Interact.
185
18-24
2010
Homo sapiens
brenda
Friese, R.S.; Rao, F.; Khandrika, S.; Thomas, B.; Ziegler, M.G.; Schmid-Schoenbein, G.W.; OConnor, D.T.
Matrix metalloproteinases: discrete elevations in essential hypertension and hypertensive end-stage renal disease
Clin. Exp. Hypertens.
31
521-533
2009
Homo sapiens
brenda
Pfaffen, S.; Hemmerle, T.; Weber, M.; Neri, D.
Isolation and characterization of human monoclonal antibodies specific to MMP-1A, MMP-2 and MMP-3
Exp. Cell Res.
316
836-847
2010
Mus musculus, Mus musculus Sv129
brenda
Komosinska-Vassev, K.; Olczyk, P.; Winsz-Szczotka, K.; Kuznik-Trocha, K.; Klimek, K.; Olczyk, K.
Age- and gender-dependent changes in connective tissue remodeling: physiological differences in circulating MMP-3, MMP-10, TIMP-1 and TIMP-2 Level
Gerontology
57
44-52
2010
Homo sapiens
brenda
Tuccinardi, T.; Ortore, G.; Santos, M.A.; Marques, S.M.; Nuti, E.; Rossello, A.; Martinelli, A.
Multitemplate alignment method for the development of a reliable 3D-QSAR model for the analysis of MMP3 inhibitors
J. Chem. Inf. Model.
49
1715-1724
2009
Homo sapiens
brenda
Green, J.A.; Elkington, P.T.; Pennington, C.J.; Roncaroli, F.; Dholakia, S.; Moores, R.C.; Bullen, A.; Porter, J.C.; Agranoff, D.; Edwards, D.R.; Friedland, J.S.
Mycobacterium tuberculosis upregulates microglial matrix metalloproteinase-1 and -3 expression and secretion via NF-kappaB- and activator protein-1-dependent monocyte networks
J. Immunol.
184
6492-6503
2010
Homo sapiens
brenda
Zeldich, E.; Koren, R.; Dard, M.; Weinberg, E.; Weinreb, M.; Nemcovsky, C.E.
Enamel matrix derivative induces the expression of tissue inhibitor of matrix metalloproteinase-3 in human gingival fibroblasts via extracellular signal-regulated kinase
J. Periodontal Res.
45
200-206
2010
Homo sapiens
brenda
Mun, S.H.; Kim, H.S.; Kim, J.W.; Ko, N.Y.; Kim, D.K.; Lee, B.Y.; Kim, B.; Won, H.S.; Shin, H.S.; Han, J.W.; Lee, H.Y.; Kim, Y.M.; Choi, W.S.
Oral administration of curcumin suppresses production of matrix metalloproteinase (MMP)-1 and MMP-3 to ameliorate collagen-induced arthritis: inhibition of the PKCdelta/JNK/c-Jun pathway
J. Pharmacol. Sci.
111
13-21
2009
Homo sapiens, Mus musculus, Mus musculus DBA/1J
brenda
Cuadrado, E.; Rosell, A.; Penalba, A.; Slevin, M.; Alvarez-Sabin, J.; Ortega-Aznar, A.; Montaner, J.
Vascular MMP-9/TIMP-2 and neuronal MMP-10 up-regulation in human brain after stroke: a combined laser microdissection and protein array study
J. Proteome Res.
8
3191-3197
2009
Homo sapiens
brenda
Husslein, H.; Haider, S.; Meinhardt, G.; Prast, J.; Sonderegger, S.; Knoefler, M.
Expression, regulation and functional characterization of matrix metalloproteinase-3 of human trophoblast
Placenta
30
284-291
2009
Homo sapiens
brenda
Johnson, J.L.; Dwivedi, A.; Somerville, M.; George, S.J.; Newby, A.C.
Matrix metalloproteinase (MMP)-3 activates MMP-9 mediated vascular smooth muscle cell migration and neointima formation in mice
Arterioscler. Thromb. Vasc. Biol.
31
e35-e44
2011
Mus musculus
brenda
Howe, N.; Ceruso, M.; Spink, E.; Malthouse, J.P.
pH stability of the stromelysin-1 catalytic domain and its mechanism of interaction with a glyoxal inhibitor
Biochim. Biophys. Acta
1814
1394-1403
2011
Escherichia coli
brenda
Ceruso, M.; Howe, N.; Malthouse, J.P.
Mechanism of the binding of Z-L-tryptophan and Z-L-phenylalanine to thermolysin and stromelysin-1 in aqueous solutions
Biochim. Biophys. Acta
1824
303-310
2012
Homo sapiens (P08254)
brenda
Liang, X.; Arunima, A.; Zhao, Y.; Bhaskaran, R.; Shende, A.; Byrne, T.S.; Fleeks, J.; Palmier, M.O.; Van Doren, S.R.
Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3
Biophys. J.
99
273-283
2010
Homo sapiens
brenda
Segueni, N.; Magid, A.A.; Decarme, M.; Rhouati, S.; Lahouel, M.; Antonicelli, F.; Lavaud, C.; Hornebeck, W.
Inhibition of stromelysin-1 by caffeic acid derivatives from a propolis sample from Algeria
Planta Med.
77
999-1004
2011
Homo sapiens
brenda
Kundu, P.; De, R.; Pal, I.; Mukhopadhyay, A.; Saha, D.; Swarnakar, S.
Curcumin alleviates matrix metalloproteinase-3 and -9 activities during eradication of Helicobacter pylori infection in cultured cells and mice
PLoS ONE
6
e16306
2011
Homo sapiens, Mus musculus
brenda
Soliman, E.; Labib, W.; El-Tantawi, G.; Hamimy, A.; Alhadidy, A.; Aldawoudy, A.
Role of matrix metalloproteinase-3 (MMP-3) and magnetic resonance imaging of sacroiliitis in assessing disease activity in ankylosing spondylitis
Rheumatol. Int.
32
1711-1720
2011
Homo sapiens
brenda
Kim, E.M.; Shin, E.J.; Lee, J.A.; Son, H.J.; Choi, D.H.; Han, J.M.; Hwang, O.
Caspase-9 activation and Apaf-1 cleavage by MMP-3
Biochem. Biophys. Res. Commun.
453
563-568
2014
Homo sapiens (P08254)
brenda
Wilfong, E.M.; Du, Y.; Toone, E.J.
An enthalpic basis of additivity in biphenyl hydroxamic acid ligands for stromelysin-1
Bioorg. Med. Chem. Lett.
22
6521-6524
2012
Homo sapiens (P08254)
brenda
Khaddam, M.; Salmon, B.; Le Denmat, D.; Tjaderhane, L.; Menashi, S.; Chaussain, C.; Rochefort, G.Y.; Boukpessi, T.
Grape seed extracts inhibit dentin matrix degradation by MMP-3
Front. Physiol.
5
425
2014
Homo sapiens (P08254)
brenda
Ijichi, K.; Brown, G.D.; Moore, C.S.; Lee, J.P.; Winokur, P.N.; Pagarigan, R.; Snyder, E.Y.; Bongarzone, E.R.; Crocker, S.J.
MMP-3 mediates psychosine-induced globoid cell formation: implications for leukodystrophy pathology
Glia
61
765-777
2013
Mus musculus (P28862), Mus musculus, Mus musculus C57BL/6 (P28862)
brenda
Batra, J.; Robinson, J.; Soares, A.; Fields, A.; Radisky, D.; Radisky, E.
Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: Binding studies and crystal structure
J. Biol. Chem.
287
15935-15946
2012
Homo sapiens (P08254), Homo sapiens
brenda
Mehner, C.; Miller, E.; Khauv, D.; Nassar, A.; Oberg, A.L.; Bamlet, W.R.; Zhang, L.; Waldmann, J.; Radisky, E.S.; Crawford, H.C.; Radisky, D.C.
Tumor cell-derived MMP3 orchestrates Rac1b and tissue alterations that promote pancreatic adenocarcinoma
Mol. Cancer Res.
12
1430-1439
2014
Homo sapiens (P08254)
brenda
Peng, M.; Jia, J.; Qin, W.
Plasma gelsolin and matrix metalloproteinase 3 as potential biomarkers for Alzheimer disease
Neurosci. Lett.
595
116-121
2015
Homo sapiens (P08254), Homo sapiens
brenda
Zuo, X.; Pan, W.; Feng, T.; Shi, X.; Dai, J.
Matrix metalloproteinase 3 promotes cellular anti-Dengue virus response via interaction with transcription factor NFkappaB in cell nucleus
PLoS ONE
9
e84748
2014
Homo sapiens (P08254), Homo sapiens
brenda
Jerah, A.; Hobani, Y.; Kumar, B.V.; Bidwai, A.
Curcumin binds in silico to anti-cancer drug target enzyme MMP-3 (human stromelysin-1) with affinity comparable to two known inhibitors of the enzyme
Bioinformation
11
387-392
2015
Homo sapiens (P08254)
brenda
Mirastschijski, U.; Dinesh, N.; Baskaran, S.; Wedekind, D.; Gavrilovic, J.; Murray, M.Y.; Bevan, D.; Kelm, S.
Novel specific human and mouse stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) antibodies for biochemical and immunohistochemical analyses
Wound Repair Regen.
27
309-323
2019
Mus musculus (P28862), Mus musculus, Mus musculus BL10 (P28862)
brenda