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(3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl)-carbamic acid tert-butyl ester
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2-[benzyl([[(2-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
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2-[benzyl([[(4-chlorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
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2-[benzyl([[(4-fluorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
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2-[benzyl([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
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3-[((1R,4S)-7,7-Dimethyl-2-oxo-bicyclo[2.2.1]hept-1-ylmethanesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[(2,4-Dinitro-phenylsulfanyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[(2,5-Dichloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
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3-[(3-Chloro-4-ethylamino-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[(3-Chloro-4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[(4-Bromo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[(4-Chloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[(4-Fluoro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[(5-Dimethylamino-naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[(Heptadecachlorooctane-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[3-(2,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
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3-[3-(3,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
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3-[3-(3-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
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3-[3-(4-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
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3-[3-(4-Chloro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
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3-[3-(4-Fluoro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
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3-[3-(4-Fluoro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
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3-[3-Benzoyl-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
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3-[Benzenesulfonyl-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[[3-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[[3-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[[4-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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3-[[4-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
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4-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
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Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
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pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
alpha2-Macroglobulin
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astragaloside IV
AST, inhibits matrix metalloproteinase-1 in photoaging skin. Astragaloside IV is one of the major active compoxadnents extracted from Astragalus membranaceus. Effects of AST against collagen reducxadtion in UV-induced skin aging in human skin fibroblasts, and mechanism of multiple anti-photoaging effects, overview
benzo[a]pyrene
increases the mRNA levels of matrix metalloproteinases MMP-1, MMP-2, MMP-3, and MMP-9 in vascular smooth muscle cells and promotes the migration and invasion of cells
C3H7-POOH-Ile-Trp-NHMe
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phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
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2-5 mM, 25°C, pH 7.4, Tris buffer, strong irreversible inhibition, inhibition increases with higher temperatures and inhibitor concentration
ClCH2CO-(N-OH)Phe-Ala-Ala-NH2
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dexamethasone
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significantly decreases active MMP-1 level and inhibits active MMP-1
disodium isostearyl 2-O-L-ascorbyl phosphate
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i.e. disodium 2-(1,3,3-trimethyl-n-butyl)-5,7,7-trimethyl-n-octyl-L-ascorbyl phosphate or VCP-IS-2Na, an amphiphilic vitamin C derivative, increases proliferation of normal human skin fibroblasts, NHDFs and NB1RGBs, by 123% and 135% and inhibits MMP-1 production by a maximum of 19% and 11% in NHDF and NB1RGB cells at 0.05 mM, respectively
epigallocatechin gallate
competitive. the galloyl group is important for inhibitory activity
epigallocatechin-3-gallate
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EtO-POOH-CH2-Leu-Trp-NHMe
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pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
EtO-POOH-Ile-Ala-Gly
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phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Ala-Gly-Gln-Arg-Gly
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phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Ala-Gly-Glu-Arg(NO2)-Gly
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phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Ala-Gly-Glu-Arg-Gly
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phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Leu-Gly
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phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Trp-NHMe
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phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Tyr(OBzl)-Gly
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phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Tyr-Gly
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phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
exopolysaccharide
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obtained from mycelial culture of Grifola frondosa HB0071 may contribute to inhibitory action in photoaging skin by reducing the MMP-1-related matrix degradation system
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fisetin
mixed-type inhibition
GM6001
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a broad-spectrum MMP inhibitor
hexyl-POOH-CH2-Leu-Trp-NHMe
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pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
hexyl-POOH-Leu-Trp-NHMe
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pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
hexyl-POOH-O-Leu-Trp-NHMe
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pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
HSCH(CH2C6H5)CO-Ala-Gly-Gln-D-Arg-NH2
Frog
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HSCH(CH2CH(CH3)2)CO -Ala-Gly-Gln-D-Arg-NH2
Frog
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HSCH2CH(NH2)CO-Ala-Gly-Gln-D-Arg-NH2
Frog
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marimastat
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i.e. BB-2516
mercaptophenylalanyl derivatives
Frog
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N-2-methylphenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
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N-2-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
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N-2-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
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N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
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N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
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N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
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N-4-chlorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
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N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
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N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
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N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
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N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
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N-4-fluorophenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
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N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
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N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
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N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
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N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
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N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
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N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
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N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
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N-4-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
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N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
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N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
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N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
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N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
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N-Hydroxy-3-[(2-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
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N-Hydroxy-3-[(3-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
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N-Hydroxy-3-[(4-iodo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
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N-Hydroxy-3-[(4-methoxy-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-(2,4,6-trimethyl-benzenesulfonyl)-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-(2-nitro-phenylsulfanyl)-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-(3-trifluoromethyl-benzenesulfonyl)-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-(4-nitro-phenylsulfanyl)-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-(nonachlorobutane-1-sulfonyl)-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-(quinoline-8-sulfonyl)-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-(toluene-4-sulfonyl)-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-pentafluorobenzenesulfonyl-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-phenylmethanesulfonyl-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-trichloromethanesulfonyl-amino]-propionamide
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N-Hydroxy-3-[(4-nitro-benzyl)-trifluoromethanesulfonyl-amino]-propionamide
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N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
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N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
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N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
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N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
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N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
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N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
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N-Hydroxy-3-[(naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
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N-Hydroxy-3-[(naphthalene-2-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
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N-Hydroxy-3-[1-(4-nitro-benzyl)-3-o-tolylsulfonyl-ureido]-propionamide
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N-Hydroxy-3-[1-(4-nitro-benzyl)-3-p-tolylsulfonyl-ureido]-propionamide
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N-Hydroxy-3-[1-(4-nitro-benzyl)-3-phenylsulfonyl-ureido]-propionamide
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N-Hydroxy-3-[dimethylsulfamoyl-(4-nitro-benzyl)-amino]-propionamide
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N-Hydroxy-3-[methanesulfonyl-(4-nitro-benzyl)-amino]-propionamide
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N-phenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
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N-phenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
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N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
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naphthoyl-Gly-PSI[POOHCH2]-Leu-Trp-NHBzl
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pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
PAI-1
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functions as an upstream regulator of a MMP-1-initiated collagenolytic phenotype, it blocks conversion of MMP-1 to its active form. Neutralization of endogenous PAI-1 with function blocking antibodies accelerates both collagenolysis and activation of MMP-1
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pedunculagin
potent inhibitory effect on MMP-1 and the increased type-I procollagen synthesis in ultraviolet B-induced human fibroblast
phthaloyl-Gly(P)-Ile-Trp-(R)NHCH-(Me)Ph
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phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
phthaloyl-Gly(P)-Ile-Trp-NHBzl
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50 µM, 25°C, pH 7.4, Tris buffer, reversible inhibition, protects the enzyme partially from inactivation by ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
phthaloyl-Gly-PSI[POOHNH]-Ile-Trp-(S)NHCH-(Me)Ph
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phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
TIMP-3
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is induced by enamel matrix derivative
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tissue inhibitor of matrix metalloproteinase-1
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tissue inhibitor of matrix metalloproteinase-2
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0.1 microM, inhibits both protease activity and migration in a 3-dimensional cross-linked collagen matrix
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Tissue inhibitor of metalloproteinase-1
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TIMP-1
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tissue inhibitors of metalloproteinase-1
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i.e. TIMP-1
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trocade
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i.e. RO-22-3555
[3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
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[4-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
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[5-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-2-methoxy-phenyl]-carbamic acid tert-butyl ester
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1,10-phenanthroline
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chelates the required Zn2+
Cys
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EDTA
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EDTA
complete inhibition at 20 mM
EDTA
complete inhibition at 20 mM
TIMP-1
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TIMP-1
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specific MMP-1 inhibitor. Inhibition of p38 signaling by SB203580 increases TIMP-1 secretion, as well as infection with Mycobacterium tuberculosis, overview
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TIMP-1
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determination in cell culture medium
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TIMP-1
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no apparent regulation of the expression of TIMP-1 by either tumor necrosis factor or enamel matrix derivative
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TIMP-1
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TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
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TIMP-1
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expression profile of MMPs/TIMP-1 after myocardial infarction, angiotensin II receptor blockade improves MMPs/TIMP-1 balance, overview
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TIMP-2
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TIMP-2
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expression of TIMP-2 in addition to bisphosphonate treatment markedly reduces the number of osteolytic lesions in breast cancer and increases overall survival compared with treatment with bisphosphonates alone
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TIMP-2
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determination in cell culture medium
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TIMP-2
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highly produced in brain microvessels
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tissue inhibitor of matrix metalloproteinase-1
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is not influenced by substance P
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tissue inhibitor of matrix metalloproteinase-1
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additional information
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no inhibition of MMP-1 by BAY 12-9566, quantitative structure-activity relationship analysis of some 5-amino-2-mercapto-1,3,4-thiadiazole based inhibitors, overview
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additional information
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human tissue factor pathway inhibitor-2 does not bind or inhibit activated matrix metalloproteinase-1
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additional information
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sulfur based inhibitors
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additional information
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the JNK inhibitor SP600125 inhibits rapamycin-induced MMP-1 gene transactivation and AP-1/DNA interactions, overview
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additional information
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panduratin A, isolated from Kaempferia pandurata, suppresses MMP-1 expression and enhances the expression of type-1 procollagen in UV-irradiated skin fibroblasts, overview
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additional information
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after hyperglycaemic treatment of keratinocytes, expression of matrix metalloproteinase-1 and alpha2beta1 integrin is significantly downregulated
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additional information
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not inhibitory: tissue inhibitor of matrix metalloproteinase-1
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additional information
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human fibroblast inhibitor effective against all vertebrate collagenases tested
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additional information
platelet-derived growth factor (PDGF) treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1
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