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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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(R)-2-(N-((6-fluoropyridin-3-yl)methyl)-4-methoxyphenyl-sulfonamido)-N-hydroxy-3-methylbutanamide
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(S)-2,4-bis[(2,3-dihydroxybenzoyl)amino]butyric acid methyl ester
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(S)-2,5-bis[(2,3-dihydroxybenzoyl)amino]pentanoic acid methyl ester
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(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]-N-hydroxyhexanoamide
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(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]hexanenitrile
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(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]hexanoamide
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shows 33% inhibition against MMP-9 at 0.00025 mM
(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]hexanoic acid
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(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]hexanoic acid methyl ester
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(S)-2,6-bis[(2,3-dimethoxybenzoyl)amino]hexanoic acid methyl ester
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(S)-2,7-bis[(2,3-dihydroxybenzoyl)amino]heptanoic acid methyl ester
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(S)-2-acetyl-6-[(2,3-dihydroxybenzoyl)amino]hexanoic acid methyl ester
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(S)-2-benzoylamino-6-[(2,3-dihydroxybenzoyl)amino]-hexanoamide
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(S)-2-benzoylamino-6-[(2,3-dihydroxybenzoyl)amino]-hexanoic acid methyl ester
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(S)-6-benzoylamino-2-[(2,3-dihydroxybenzoyl)amino]-hexanoic acid methyl ester
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1,5-bis[(2,3-dihydroxybenzoyl)amino]pentane
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2-[(biphenyl-4-ylsulfonyl)(isobutyl)amino]-N-hydroxyacetamide
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50% inhibition at 34 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-2
3',4',5,6,7,8-hexamethoxyflavone
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i.e. nobiletin
3',4'-di-O-methylbutin-7-O-[(6''->1''')-3''',11'''-dimethyl-7'''-methylenedodeca-3''',10'''-dienyl]-beta-D-glucopyranoside
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0.0065-0.0259 mM suppresses MMP-9 activity in lipopolysaccharide-stimulated human monocytic cells without cytotoxicity
3',4'-di-O-methylquercetin-7-O-[(4''->13''')-2''',6''',10''',14'''-tetramethylhexadec-13'''-ol-14'''-enyl]-beta-D-glucopyranoside
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0.0065-0.0259 mM suppresses MMP-9 activity in lipopolysaccharide-stimulated human monocytic cells without cytotoxicity
3',4'-dihydroxy-5,6,7,8-tetramethoxyflavone
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3'-hydroxy-4',5,6,7,8-pentamethoxyflavone
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4'-hydroxy-3',5,6,7,8-pentamethoxyflavone
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4'-O-methylbutin-7-O-[(6->1''')-3''',11'''-dimethyl-7'''-hydroxymethylenedodecanyl]-beta-D-glucopyranoside
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0.0065-0.0259 mM suppresses MMP-9 activity in lipopolysaccharide-stimulated human monocytic cells without cytotoxicity
4'-O-methylkaempferol-3-O-[(4''->13''')-2''',6''',10''',14'''-tetramethylhexadecan-13'''-olyl]-beta-D-glucopyranoside
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0.0065-0.0259 mM suppresses MMP-9 activity in lipopolysaccharide-stimulated human monocytic cells without cytotoxicity
5-(1,5-dihydroxypentan-3-yl)-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
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5-(4-hydroxybutan-2-yl)-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
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5-(4-phenoxyphenyl)-5-(3-(1-nitrooxy-methyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
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5-(4-phenoxyphenyl)-5-(4-(1-nitrooxy-ethyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
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5-(4-phenoxyphenyl)-5-(4-(2-nitrooxy-ethyl)piperazin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
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5-(4-phenoxyphenyl)-5-(4-(2-nitrooxy-ethyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
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5-(4-phenoxyphenyl)-5-(bis-(2-nitrooxy-ethyl)-amino)pyrimidine-2,4,6(1H,3H,5H)-trione
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5-(4-phenoxyphenyl)-5-(methyl-(2-nitrooxy-ethyl)-amino)-pyrimidine-2,4,6(1H,3H,5H)-trione
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5-[3-(hydroxymethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
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5-[4-(2-hydroxyethyl)piperazin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
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5-[4-(2-hydroxyethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
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5-[4-(hydroxymethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
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adiponectin
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adiponectin can markedly suppress protein expression and activity of MMP9 in brain, induced by 1 h ischemia followed by 23 h reperfusion
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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 0.26 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-2
antibody REGA-3G12
highly selective, potent MMP-9 inhibition, the antibody recognizes the N-terminal part, not the C-terminal hemopexin and O-glycosylated domains, epitope mapping, overview
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BIIL284
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BIIL284 treatment (3 mg/kg once daily for 2 weeks) significantly reduces the extracellular matrix metalloproteinase-9 activity in stented arteries
carboxy-derivatized glucosamine
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62% inhibition of MMP-9 at 0.5 mg/ml
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CGS27023A
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50% inhibition at 8 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-2
chitooligosaccharides
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different molecular weight, inhibit both MMP-9 expression and activity, especially 1- to 3-kDa chitooligosaccharides, chitooligosaccharides-I in HT-1080 cells
cyclic CTT peptide
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a gelatinase inhibitor peptide
cyclic CTTHWGFTLC
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a specific gelatinase inhibitor
D-penicillamine
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10 mg/l, 43% inhibition
doxycyclin
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doxycycline significantly inhibits MMP-9 activity in gel zymography and also suppressed in situ gelatinase activity
hemopexin domain of MMP-9
the hemopexin domain of MMP-9 inhibits the degradation of gelatin. It also abolishes the degradation of gelatin by MMP-2. Blades 1 and 4 of the PEX9 domain are responsible for the gelatin degradation inhibitory activity of PEX9. The hemopexin domain of MMP-9 does not prevent the degradation of other MMP-9 substrates, such as a fluorogenic peptide, alphaB crystalline, or nonmuscular actin
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Immunoglobulins purified from antisera raised against gelatinase
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isovitexin
interacts with enzyme residues Glu241, Ala242, Pro255, Pro254, Thr251, Leu222, Tyr248, Arg241, Met247, His226, and Glu227, binding structure analysis, and modeling, overview
Melatonin
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i.e. N-acetyl-5-methoxytryptamine, used in protection during gastric ulcer, arresting cell injury, protein carbonyl formation, and lipid peroxidation in mice during gastroprotection, inhibits MMP-9 expression and activity
minocycline
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0.02 mM minocycline displays inhibitory action on MMP-9 expression and activity
MMP-9i
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MMP-9 inhibitor, an anthranilate hydroxamic acid derivative
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N,N'-[(2S)-6-[[(2,3-dihydroxyphenyl)carbonyl]amino]hexane-1,2-diyl]bis(2,3-dihydroxybenzamide)
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N-hydroxy-2-(isobutyl[(4-methoxyphenyl)sulfonyl]amino)acetamide
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50% inhibition at 2.9 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-2
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
NNGH
N-[(5R)-5-[[(2,3-dihydroxyphenyl)carbonyl]amino]-6-hydroxyhexyl]-2,3-dihydroxybenzamide
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N-[(5S)-5-[[(2,3-dihydroxyphenyl)carbonyl]amino]-6-hydroxyhexyl]-2,3-dihydroxybenzamide
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N-[(5S)-6-amino-5-[[(2,3-dihydroxyphenyl)carbonyl]amino]hexyl]-2,3-dihydroxybenzamide
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norcantharidin
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i.e. exo-7-oxabicylo-[2.2.1] heptane-2,3-dicarboxylic anhydride, norcantharidin inhibits gelatinase activity of MM-9 in a concentration- and time-dependent manner
pioglitazone
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pioglitazone reduces the upregulation of active form of MMP-9 after ischemia
polyhistidine
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0.001 mM, 68% inhibition
proanthocyanidins
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from the american cranberry, Vaccinium macrocarpon, decrease cellular viability of DU-145 cells via inhibition of MMP-9. The proanthocyanidins PACs increase the expression of TIMP-2, a known inhibitor of MMP activity, and decrease the expression of EMMPRIN, an inducer of MMP expression. Cranberry proanthocyanidins decrease MMP activity through the induction and/or inhibition of specific temporal MMP regulators, and by affecting either the phosphorylation status and/or expression of MAP kinase, PI-3 kinase, NF-kappaB and AP-1 pathway proteins
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procyanidin oligomers
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from Japanese quince, Chaenomeles japonica, fruit inhibit activity of MMP-9
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REGA-3G12 scFv with (His6)2
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monoclonal antibody REGA-3G12 single-chain variable fragment, 0.005 mM, 66% inhibition
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reversion-inducing cysteine-rich protein with Kazal motifs
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TIMP1
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interaction analysis and structure modeling, overview
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TIMP2
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interaction analysis and structure modeling, overview
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tissue inhibitor of matrix metalloproteinase 1
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strong inhibitor of MMP-9
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tissue inhibitor of matrix metalloproteinase-1
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TIMP-1
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tissue inhibitor of metalloproteinase 1
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tissue inhibitor of metalloproteinase TIMP-1
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tissue inhibitor of metalloproteinase TIMP-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 1
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tissue inhibitor of metalloproteinases 2
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TIMP-2, complete inhibition at 0.5 mg
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tissue inhibitor of metalloproteinases-1
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i.e. TIMP-1, plays a crucial role in the pathogenesis of hepatic fibrosis and thus may represent an important therapeutic target in the design of anti-fibrotic strategiesfor chronic liver disease, overview, molecular modeling of the three-dimensional structure of the MMP-9/TIMP-1 complex, overview
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vitexin
interacts with enzyme residues Gly186, Pro246, His236, Met247, Tyr248, Val223, and Leu188, binding structure analysis, and modeling, overview
1,10-phenanthroline
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strong inhibition at 1 mM
1,10-phenanthroline
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10 mM, 100% inhibition
1,10-phenanthroline
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totally inhibited by 10 mM 1,10-phenanthroline
BB-94
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broad-spectrum MMP inhibitor
doxycycline
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doxyxycline inhibits directlyMMP-9 enzymatic activity derived from tumor necrosis factor-alpha-stimulated vascular smooth muscle cells
doxycycline
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inhibitory mechanism and effect on osteoclastogenesis signaling induced by RANKL, both in vitro and in vivo, overview. Although Dox inhibits RANKL-induced osteoclastogenesis and down-modulates the mRNA expression of functional osteoclast markers, it neither affects RANKL-induced MAPKs phosphorylation nor NFATc1 gene expression in RAW264.7 monocytic cells
doxycycline
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totally inhibited by 10 mM doyxycline
EDTA
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complete inhibition at 10 mM
EDTA
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10 mM, 74% inhibition
EDTA
2 mM, severely inhibits enzyme activity due to chelation of metal ions
EDTA
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complete inhibition at 10 mM
GM6001
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GM6001
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MMP-9-specific inhibitor
GM6001
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MMP inhibitor, complete inhibition at 0.025 mM
ilomastat
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ilomastat
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a pan-MMP inhibitor, strong inhibition
MMP-9 inhibitor I
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MMP-9 inhibitor I
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highly specific inhibition of MMP-9
SB-3CT
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MMP-9-specific inhibitor
SB-3CT
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MMP9-specific inhibitor, MMP9 activity is reduced with SB-3CT resulting in reduced brain injury
TIMP-1
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TIMP-1
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formation of proMMP-9/TIMP-1 complexes
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TIMP-1
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major inhibitor of MMP-9
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TIMP-1
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i.e. tissue inhibitor of metalloproteinase 1, a natural inhibitor
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TIMP-2
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TIMP-2
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specific inhibitor for MMP9
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TIMP-2
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a MMP inhibitor
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Tissue inhibitor
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of metalloproteinase-2
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Tissue inhibitor
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of metalloproteinase-1; of metalloproteinase-2
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Tissue inhibitor
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of metalloproteinases, recombinant
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Tissue inhibitor of metalloproteinase-1
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Tissue inhibitor of metalloproteinase-1
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1 nM, 88% inhibition
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Tissue inhibitor of metalloproteinase-1
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Tissue inhibitor of metalloproteinase-1
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exogenous tissue inhibitor of metalloproteinase-1 has a greater inhibitory effect on endogenously active MMP-9 than on 4-aminophenylmercuric acetate-activated MMP-9
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Tissue inhibitor of metalloproteinase-1
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tissue inhibitor of metalloproteinases 1
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TIMP-1, complete inhibition at 0.5 mg
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tissue inhibitor of metalloproteinases 1
TIMP-1, the zymogen proMMP-9 trimers possess a 50fold higher affinity for TIMP-1 than the monomers, with a higher extent of TIMP-1 inhibition of angiogenesis induced by trimers compared with monomers
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tissue inhibitor of metalloproteinases 1
TIMP-1, the 65 kDa enzyme form lacking both the N- and C-terminal domains cannot be inhibited by TIMP-1 in contrast to the mature 82 kDa enzyme form
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tissue inhibitor of metalloproteinases 1
TIMP-1
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additional information
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the 230 kDa enzyme does not remain intact in 4 M urea, 0.5 M NaCl, 4 M CsCl or 4 M GdHCl. Glycosaminoglycan chains may interfere with inhibitors
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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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computational model of MMP9 activation and inhibition, overview
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additional information
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pre-exposure to pyrrolidine dithiocarmate suppresses pro-MMP-9 activity and protein levels in relaxin-treated THP-1 cells
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additional information
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following overexpression of arylsulfatase B, MMP9 declines 51%
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additional information
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MMP-9 is specifically regulated by p21-activated-kinase-1, ectopic expression of p21-activated-kinase-1 variants impairs Jun N-terminal kinase but not necrosis factor-kappaB pathway, which in turn suppresses the promoter activation and transcription of MMP-9
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additional information
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Notch1 knockdown decreases MMP9 expression
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additional information
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MMP-9 is decreased 12 months after natalizumab treatment in patients with relapsing-remitting multiple sclerosis
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additional information
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doublecortin synthesis suppresses the expression and activation of MMP9
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additional information
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downregulation of E26 transformation-specific DNA binding domain transcription factors suppresses the non-endothelial E26 transformation-specific DNA binding domain-target gene MMP9
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additional information
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hesperidin inhibits the secreted and cytosolic MMP-9 forms in HepG2 cells through the inhibition of nuclear factor-kappaB and AP-1
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additional information
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synthesis and inhibitory activity against MMP-9 of nobiletin metabolites, overview. The key intermediate is 2'0-hydroxy-3',4',5',6'-tetramethoxyacetophenone
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additional information
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design and synthesis of barbiturate-nitrate hybrids, barbiturate-based MMP inhibitors incorporating a nitric oxide donor/mimetic group, that inhibit MMP-9 activity and secretion, reducing effects on cell viability by inhibitors, overview
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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-9 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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epitope tagging of MMP-9 with monoclonal antibodies, overview
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additional information
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both NF-jB and AP-1 inhibitors inhibit MMP-9 expression
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additional information
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NK4 intervention suppresses MMP9 mRNA expression
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additional information
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gene expression of MMP-9 is significantly suppressed in the hearts of eplerenone-treated mice compared with controls
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additional information
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integrin-linked kinase gene knockdown leads to reduced MMP9 expression
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additional information
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borneol has no influence on MMP-9 activity
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additional information
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downregulation of E26 transformation-specific DNA binding domain transcription factors suppresses the non-endothelial E26 transformation-specific DNA binding domain-target gene MMP9
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additional information
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no inhibition by amiloride or plasminogen activator/plasmin inhibitor D-Phe-Pro-Arg-chloromethylketone dihydrochloride
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