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(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
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(2R)-2-[(4-biphenylylcarbonyl)amino]-N-hydroxy-3-(1H-indol-3-yl)propionamide
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(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid
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(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid benzyl ester
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(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-(1H-indol-3-yl)propionic acid methyl ester
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(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-methylbutanoic acid tert-butyl ester
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(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid
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(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid methyl ester
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(2R)-3-(1H-indol-3yl)-2-[[4-(phenylazo)benzenesulfonyl]amino]propionic acid
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(2R)-3-(1H-indol-3yl)-2-[[4-[phenylaminocarbonyl]-benzenesulfonyl]amino]propionic acid benzyl ester
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(2R)-3-methyl-2-[4-[phenoxybenzenesulfonyl]amino]butanoic acid
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(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)-amino]benzenesulfonyl]amino]butanoic acid
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(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)amino]benzenesulfonyl]amino]butanoic acid tert-butyl ester
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(2R)-3-methyl-2-[[4-[2-[4-methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid
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(2R)-3-methyl-2-[[4-[2-[methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid tert-butyl ester
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(2R)-3-methyl-2-[[5-[(4-methylphenyl)ethynyl]thiophene-2-sulfonyl]-amino]butanoic acid methyl ester
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(2R)-N-(benzyloxy)-2-[(4-biphenylsulfonyl)amino]-3-phenylpropionamide
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(2R)-N-hydroxy-3-methyl-2-[(4-phenoxybenzenesulfonyl)amino]butanamide
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(2R)-[(4-biphenylsulfonyl)amino]-N-hydroxy-3-phenylpropionamide
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(4-phenoxyphenylsulfonyl)methylthiirane
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selective inhibitor of MMP2
2-(4-(4-[(2-thiiranylpropyl)sulfonyl]phenoxy)phenyl)acetic acid
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selective inhibitor
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
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2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
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2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
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2-[(biphenyl-4-ylsulfonyl)(isobutyl)amino]-N-hydroxyacetamide
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50% inhibition at 13 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
2-[(biphenyl-4-ylsulfonyl)(isopropoxy)amino]-N-hydroxyacetamide
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50% inhibition at 12 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
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2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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4-(2-phenyl-2H-tetrazol-5-yl)benzenesulfonyl chloride
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4-(3-phenylureido) benzenesulfonyl chloride
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4-(4-phenoxphenylsulfonyl)butane-1,2-dithiol
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4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
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5-(4-phenoxphenylsulfonyl)pentane-1,2-dithiol
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advanced glycation products
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inhibit the enzyme mediated through upregulation of the advanced glycation product receptor, overview
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Ag-3340
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i.e. N-hydroxy-2,2-dimethyl-4-[(4-phenoxyphenyl)sulfonyl]thiomorpholine-3-carboxamide, 50% inhibition at 0.083 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
alpha2 macroglobulin
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APP-IP-TIMP-2
inhibition evaluation and kinetics, mechanism in concanavalin A-stimulated HT1080 fibrosarcoma cells, expression of APP-IP-TIMP-2 in HT1080 cells, overview. The ten amino acid residue sequence of APP-derived MMP-2 selective inhibitory peptide (APP-IP) is added to the N-terminus of tissue inhibitors of metalloproteinase 2, TIMP-2. The APP-IP and TIMP-2 regions of the fusion protein are designed to interact with the active site and the hemopexin-like domain of MMP-2, respectively.The reactive site of the TIMP-2 region, which has broad specificity against MMPs, is blocked by the APP-IP adduct. The recombinant APP-IP-TIMP-2 shows strong inhibitory activity toward MMP-2 whereas its inhibitory activity toward MMP-1, MMP-3, MMP-7, MMP-8, MMP-9, or MT1--MMP is six orders of magnitude or more weaker. Compared with the decapeptide APP-IP, APP-IP-TIMP-2 shows a much longer half-life in cultured tumor cells
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batimastat
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i.e. BB-94, a peptidomimetic inhibitor
benzyloxycarbonyl-L-Trp-OH
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beta-amyloid precursor protein
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APP
CGS27023A
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50% inhibition at 20 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
chitooligosaccharides
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inhibit MMP-2 enzyme expression, decrease of the gene expression and transcriptional activity of MMP-2, and catalytic activity in primary dermal fibroblasts, chitooligosaccharides of 3-5 kDa are most effective
curcumin
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treatment of whole cell, significant inhibition of enzyme activity after 15 days with concomitant decrease in expression of membrane type-1 matrix metalloproteinase and focal adhesion kinase to almost background level
D-tryptophan benzyl ester trifluoroacetate
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D-tryptophan methyl ester tosylate
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dibenzofuran-2-sulfonyl chloride
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dimethyl sulfoxide
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presence of 2% dimethyl sulfoxide disrupts interactions of enzyme with substrate and thereby reduces activity by 70%
extracellular domain of beta-amyloid peptide
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the extracellular domain of beta-amyloid precursor protein contains an inhibitor against MMP-2, the inhibitor is localized within the ISYGNDALMP sequence of APP, overview
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GNDAMPL
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APP-IP delta N3
isovitexin
interacts with enzyme residues Glu121, Leu83, Ala84, Pro140, Ile141, His120, Ala136, Leu116, Ala139, and Leu137, binding structure analysis, and modelling, overview
ISYGADALMP
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APP-IP delta N/A
ISYGNAALMP
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APP-IP delta D/A
ISYGNDAAMP
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APP-IP delta L/A
ISYGNDAL
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APP-IP delta C2
ISYGNDALM
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APP-IP delta C1
ISYGNDALMPSL
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APP586-597
ISYGNDALMPSLTETK
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APP586-601
methyl 2-(4-(4-[(2-thiiranylpropyl)-sulfonyl]phenoxy)phenyl)acetate
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mechanism-based inhibitor, selective for enzyme
N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-naphthylalanyl-L-alanine-2-aminoethyl amide
TAPI-1
N-hydroxy-2-(isobutyl[(4-methoxyphenyl)sulfonyl]amino)acetamide
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50% inhibition at 6.9 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
N-hydroxy-2-([4-[2-(trifluoromethyl)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
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N-hydroxy-2-([4-[2-methyl-3'-(trifluoromethoxy)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
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N-hydroxy-2-([4-[3'-(2-hydroxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
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N-hydroxy-2-([4-[3'-(2-methoxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
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N-hydroxy-2-([4-[3'-(methoxymethyl)-2-methylbiphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
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N-hydroxy-2-methyl-2-[(4-[2-methyl-3'-[2-(methylamino)ethoxy]biphenyl-4-yl]piperidin-1-yl)sulfonyl]propanamide
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N-hydroxy-2-[(4-[4-[6-(2-hydroxyethoxy)pyridin-2-yl]-3-methylphenyl]piperidin-1-yl)sulfonyl]-2-methylpropanamide
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N-hydroxy-2-[[4-(2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
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N-hydroxy-2-[[4-(3'-methoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
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N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
NNGH
NaCl
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binding to heparin and fibronectin can be disrupted by 0.3 M NaCl
peptide P713
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inhibits the binding of the CBD as well as MMP-2E404A to gelatin, no inhibition of MMP-2 lacking thr CBD domain, competitively, P713 inhibits MMP-2 activities by blocking substrate access to the CBD exodomain, mechanism, overview
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procollagen C-terminal proteinase enhancer
PCPE
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procyanidin oligomers
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from Japanese quince, Chaenomeles japonica, fruit inhibit activity of MMP-2
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RECK
reversion-inducing cysteine-rich protein with Kazal motifs
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SB-3CT
mechanism-based synthetic inhibitor
SC-74020
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hydroxamic acid inhibitor
Stromelysin catalytic domain inhibitors
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gelatinase A synthetic 19000 MW catalytic domain
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SYGNDAMPL
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APP-IP delta N1
ter-butyloxycarbonyl-L-Trp-OH
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TIMP-3
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
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tissue factor pathway inhibitor
TFPI-2
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Tissue inhibitor of metalloproteinase-1
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Tissue inhibitor of metalloproteinase-2
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Tissue inhibitor of metalloproteinases
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tissue inhibitor of metalloproteinases-2
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tissue inhibitors of metalloproteinase 2
TIMP2
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vitexin
interacts with enzyme residues Leu83, Ala84, His130, Pro140, Ala139, Met138, Ala, 136, Leu137, Thr143, Tyr142, Val117, His120, and Ile141, binding structure analysis, and modelling, overview
YGNDAMPL
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APP-IP delta N2
Zn2+
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required, synthetic 19000 MW catalytic domain, inhibition at high concentration
1,10-phenanthroline
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1,10-phenanthroline
complete inhibition
1,10-phenanthroline
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a non-specific inhibitor of metalloproteinases
EDTA
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EGTA
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GSH
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GSSG
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ilomastat
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ilomastat
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a pan-MMP inhibitor, strong inhibition
ISYGNDALMP
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synthetic decapeptide APP-IP(APP586-595)
ISYGNDALMP
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APP-derived inhibitory peptide, APP-IP, selective inhibition of MMP-2, An MMP-2 mutant, with deleted hemopexin-like domain and three fibronectin-like type II domains, and native MMP-2 showed similar affinities for APP-IP, suggesting that only the catalytic domain of MMP-2 is essential for the interaction, mutational interaction analysis, overview, inhibition of recombinant wild-type enzyme and truncated enzyme mutants, overview
L-cysteine
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L-histidine
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L-homocysteine
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L-methionine
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N-acetylcysteine
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TIMP-1
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TIMP-1
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
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TIMP-2
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TIMP-2
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specific for MMP-2
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TIMP-2
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pro-MMP-2-TIMP-2 complexes are endocytosed into HT-1080 cells
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TIMP-4
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tissue inhibitor of metalloproteinases
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TIMP-4
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
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Tissue inhibitor of metalloproteinase-2
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Tissue inhibitor of metalloproteinase-2
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Tissue inhibitor of metalloproteinase-2
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TIMP-2, not only a potent inhibitor of the activated enzyme but also prevents the generation of low-molecular-mass species and full enzymic activity from the zymogen
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Tissue inhibitor of metalloproteinase-2
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activity of the inhibitor is regulated by C-terminal domain interactions
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Tissue inhibitor of metalloproteinase-2
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purification and characterization of a two-chain form of the inhibitor and a low MW TIMP-like protein, proteolytic processing of TIMP-2 plays a role in the regulation of gelatinase A in the extracellular matrix
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Tissue inhibitor of metalloproteinase-2
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Tissue inhibitor of metalloproteinase-2
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gelatinase A/TIMP-2-complex may be a matrix metalloproteinase of the second step: it starts its proteolytic attack after it has switched off the activity of other matrix metalloproteinases
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Tissue inhibitor of metalloproteinases
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Tissue inhibitor of metalloproteinases
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tissue inhibitor of metalloproteinases-2
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TIMP-2, complex formation with MMP-14 and MMP-2 activates the enzyme, overview
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tissue inhibitor of metalloproteinases-2
TIMP-2, a physiological inhibitor of MMPs. proMMP-2 can be secreted either in a free form or already complexed with TIMP-2 through its C-terminal domain. In the first case, a TIMP-2 that inhibits a cell membrane-anchored MT1-MMP by interaction between its N-terminal inhibitory domain and the catalytic domain of MT1-MMP, acts as a binding site for free proMMP-2 by interaction between the proMMP-2 Hpx-like domain and the TIMP-2 C-terminal domain. ProMMP-2 present in the resulting MT1-MMP-TIMP-2-proMMP-2 complex can then be activated by another adjacent TIMP-2-free MT1-MMP. In the second case, the N-terminal inhibitory domain of TIMP-2 in the proMMP-2-TIMP-2 complex can interact with a cell membrane-anchored MT1-MMP. This proMMP-2 is then activated by an adjacent free MT1-MMP. To illustrate this process, it has been shown that proMMP-2 colocalizes with TIMP-2 and MT1-MMP inside caveolae on the surface of endothelial cells. Extracellular association of proMMP-2 and TIMP-2 depends on TIMP-2 phosphorylation by extracellular c-Src tyrosine kinase
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additional information
PMSF, benzamidine, E-64, and pepstatin A are poor inhibitors
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additional information
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PMSF, benzamidine, E-64, and pepstatin A are poor inhibitors
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additional information
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not: inhibitors of serine, cysteine or aspartic proteinases
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additional information
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dithiothreitol does not interfere with heparin binding
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additional information
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inhibition of MMP-2 gelatinolysis by targeting exodomain-substrate interactions
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additional information
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inhibitor synthesis and molecular docking, overview
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additional information
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inhibition potency of sulfur-containing compounds, overview
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additional information
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allyl isothiocyanate and N-acetylcysteinyl-allyl isothiocyanate downregulate MMP-2 expression in SK-Hep1 hepatoma cells, as well as adhesion, invasion, and migration, overview
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additional information
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CBD123 decreases active MMP-2 levels in HT-1080 cells, but only marginally the content of pro-MMP-2, overview
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additional information
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simultaneous binding of each ligand heparan sulfate and hirudin to the exosites is necessary for the complete inhibition of MMP-2 degradation by thrombin
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additional information
enzyme residue Cys102 plays a role in inhibition of catalytic activity through a cysteine-zinc ion pairing, this pairing is disrupted by the intermolecular disulfide bond in the MMP-2 homodimer, resulting in enzyme activation. Disruption of the cysteine-zinc ion pairing by homodimerization of MMP-2 opens the active site, but it may accommodate only small peptide substrates. Thus, MMP-2 propeptide processing is a prerequisite to gain its proteolytic activity against large substrates, including gelatin
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additional information
molecular design of a highly selective and strong protein inhibitor against matrix metalloproteinase-2, overview
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additional information
while TIMP-2, TIMP-3 and TIMP-4 are able to strongly interact with proMMP-2, TIMP-2 is the only one contributing to cell-surface activation of the proenzyme by MT1-MMP. Such antagonistic properties of TIMP-2 (inhibition vs. activation) highlight its seminal role in the control of pericellular MMP-2 activity
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additional information
Ficus deltoidea leaf extract inhibits matrix metalloproteinase-2, 8 and 9, molecular docking, molecular dynamics, molecular dynamic simulation analysis, overview. Computational docking analysis reveals that vitexin and isovitexin binds to the active site of the three tested MMPs
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additional information
omega-3 and omega-6 fatty acids act as inhibitors of matrix metalloproteinase-2 activity. Omega-3 and omega-6 fatty acids contribute to the structure and function of the phospholipid bilayers in cellular membranes and act as precursors of lipid-mediated signaling molecules
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additional information
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calreticulin-deficient null mice embryos show increased MMP-2 expression and activity, phosphatidylinositol 3 kinase inhibitor decreases the MMP-2 expression, overview
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additional information
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inhibition potency of sulfur-containing compounds, overview
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