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(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2 + H2O
?
-
a quenched fluorogenic substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-2,6-diaminopimelyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-DPA-Ala-Arg-NH2
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys(2,4-dinitrophenyl)-Gly + H2O
?
-
a short 11-amino-acid collagen-like peptide substrate, NFF-1, cleavage of NFF-1 by MMP-2 does not require CBD-mediated substrate binding for degradation to occur
-
-
?
110000 MW cell-surface amyloid protein precursor + H2O
?
-
amyloid protein precursor of Alzheimer's disease, cleavage to a 1000 MW form of the protein
-
-
?
2,4-dinitrophenyl-L-Pro-L-Gln-Gly-L-Ile-L-Ala-Gly-L-Gln-D-Arg + H2O
?
-
-
-
-
?
2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Ala-NH2 + H2O
?
-
-
-
-
?
7-methylcoumaryl-L-Pro-L-Lys-L-Gln-L-Gln-L-Phe-L-Phe-Gly-L-Leu-L-Lys-(2,4-dinitrophenyl)-Gly + H2O
?
-
-
-
-
?
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt + H2O
?
-
-
-
?
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester + H2O
?
-
-
-
-
?
alpha1(V)436-447 fTHP + H2O
?
-
-
-
?
Azocoll + H2O
?
-
-
-
-
?
Bovine fibrinogen + H2O
?
-
proteolytic processing of bovine fibrinogen bringing about the formation of a product unable to form fibrin clots, preferential binding of MMP-2 to the beta-chain of fibrinogen through its haemopexin-like domain, removal of the domain dramatically alters the proteolytic reaction mechanism, molecular docking and modelling, overview
-
-
?
Cartilage proteoglycan + H2O
?
-
-
-
-
?
collagen type V + H2O
?
-
-
-
-
?
collagene type IV + H2O
?
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2 + H2O
?
-
-
-
?
extracellular matrix components + H2O
?
-
-
?
fibrillin-1 + H2O
?
from eye oxytalan fibers, degradation in vitro
-
-
?
fibrillin-2 + H2O
?
from eye oxytalan fibers, degradation in vitro
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Galectin-3 + H2O
?
-
a galactoside-binding protein, major cleavage site: Ala62-Tyr63
-
-
?
gelatin type I + H2O
?
-
-
-
-
?
gelatin type IV + H2O
?
-
-
-
-
?
gelatin type V + H2O
?
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Ser-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Ser-Gln
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Phe-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Phe-Gly-Gln
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Trp-Gly-Gln
-
-
-
?
LS276-THP + H2O
?
-
development and evaluation of an activatable NIR fluorescent probe LS276-THP for in vivo detection of cancer-related matrix metalloproteinase activity based on a triplehelical peptide substrate with high specificity for MMP-2 and MMP-9 relative to other members of the MMP family, overview. Triple-helical peptides are suitable for highly specific in vivo detection of tumor-related MMP-2 and MMP-9 activity
-
-
?
Mca-KPLGL-(Dpa)-AR-NH2 + H2O
?
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
-
quenched fluorescent peptide
-
?
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2 + H2O
?
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
MOAcPLGLA2pr(Dnp)-AR-NH2 + H2O
?
-
fluorogenic quenching substrate
-
?
Neonatal human proteoglycan + H2O
?
-
cleavage of the His16-Ile17 bond and the Leu25-Leu26 bond
-
-
?
peptide A13P + H2O
?
-
-
-
?
peptide A21 + H2O
?
-
-
-
?
peptide A21A + H2O
?
-
-
-
?
peptide B37 + H2O
?
-
-
-
?
peptide B49 + H2O
?
-
-
-
?
peptide B74P + H2O
?
-
-
-
?
peptide B74R + H2O
?
-
-
-
?
peptide C15 + H2O
?
non-selective peptide substrate
-
?
peptide C9R + H2O
?
-
-
-
?
peptide m1A11 + H2O
?
non-selective peptide substrate
-
?
peroxynitrite-treated fibrinogen + H2O
?
-
-
-
-
?
Progelatinase B + H2O
?
-
activation to an 82000 MW active form
-
-
?
type V collagen + H2O
?
-
-
-
?
Vitronectin + H2O
?
-
a 65000 MW and a 75000 MW form
-
-
?
vitronectin of MW 65000 + H2O
?
-
-
-
-
?
vitronectin of MW 65000 and 75000 + H2O
?
-
-
-
-
?
vitronectin of MW 75000 + H2O
?
-
-
-
-
?
additional information
?
-
Collagen + H2O
?
degradation of beta- and gamma-chains, weak activity with alpha-chains
-
-
?
Collagen + H2O
?
-
soluble triple helical type I collagen, 3/4- and 1/4-length collagen fragments are formed
-
-
?
Collagen + H2O
?
-
fibrillar collagen
-
-
?
Collagen + H2O
?
-
no cleavage of interstitial collagens
-
-
?
Collagen + H2O
?
-
denatured collagen
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
type V
-
-
?
Collagen + H2O
?
-
type IV (to a lesser extent)
-
-
?
Collagen + H2O
?
-
binds type I collagen but does not cleave
-
-
?
Collagen + H2O
?
-
no cleavage of interstitial collagens
-
-
?
Collagen + H2O
?
-
several types
-
?
Collagen + H2O
?
-
type IV
-
-
?
Collagen + H2O
?
-
type V
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
collagen zymography
-
-
?
collagene type IV + H2O
?
-
-
-
-
?
collagene type IV + H2O
?
-
DQ-collagen type IV zymography
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
ephB1 + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
Gallus gallus Hy-Line Brown
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
670119, 683134, 683140, 683314, 683466, 683507, 683579, 683710, 683804, 712166, 712613, 712625 -
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
683134, 683140, 683314, 683430, 683442, 683466, 683579, 683710, 683746, 683804, 683842 -
-
?
Gelatin + H2O
?
-
gelatin zymography using porcine gelatin type A
-
-
?
Gelatin + H2O
?
fluorescein-conjugated gelatin
-
-
?
Gelatin + H2O
?
fluorescent substrate for use in the assay
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Laminin + H2O
?
-
-
-
-
?
peptide A13 + H2O
?
-
-
-
?
peptide A13 + H2O
?
-
-
?
peptide A13R + H2O
?
-
-
-
?
peptide A13R + H2O
?
-
-
?
peptide A3 + H2O
?
-
-
-
?
peptide A34 + H2O
?
-
-
-
?
peptide A34 + H2O
?
-
-
?
peptide B74 + H2O
?
-
-
-
?
peptide B74 + H2O
?
-
-
?
peptide C9 + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
degradation
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type IV collagen + H2O
?
-
-
-
?
Type IV collagen + H2O
?
-
-
-
?
Type IV collagen + H2O
?
degradation
-
-
?
additional information
?
-
rMMP-2 degrades collagen effectively and the hydrolysate reveals scavenging activities on both 2, 2'-diphenyl-1-picrylhydrazyl free radical and hydrogen peroxide
-
-
?
additional information
?
-
-
Akt signaling is involved in the activation of MMP-2, and this Akt-induced activation of MMP-2 is responsible for reorganization of the actin cytoskeleton into a cortical pattern with parallel rounding of chondrogenic competent cells, MMP-2 regulation, not related to Erk signaling, overview
-
-
?
additional information
?
-
-
specificity: tolerates only small amino acids such as Gly and Ala in subsite P1, prefers hydrophobic, aliphatic residues in subsite P1'
-
-
?
additional information
?
-
-
laminin,native or denatured type I collagen, native or denatured types II, IV, V, and X collagen or the NC1 domain of type VII collagen, elastin,SPARC, tenascin and MatrigelTM are not bound by the recombinant C domain
-
?
additional information
?
-
-
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 and DABCYL-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-EDANS are no substrates
-
?
additional information
?
-
-
may be responsible for the pathological degradation and/or normal turnover of vitronectin
-
-
?
additional information
?
-
-
constitutively expressed in human rheumatoid synovial cells
-
-
?
additional information
?
-
-
activation of progelatinase B is mediated by gelatinase A species that may be localized in the surface of tumor cells and enhance matrix degradation during cancer metastasis
-
-
?
additional information
?
-
facilitates tmumor metastasis and angiogenesis by hydrolyzing components of the extracwllular matrix
-
?
additional information
?
-
-
facilitates tmumor metastasis and angiogenesis by hydrolyzing components of the extracwllular matrix
-
?
additional information
?
-
-
implicated in tumor cell metastasis and angiogenesis
-
?
additional information
?
-
-
important role in extracellular matrix degradation during cell migration and tissue remodeling, involved in development, inflammation, wound healing, tumor invasion, metastasis and other physiological and pathological processes
-
?
additional information
?
-
-
important role in tumor angiogenesis
-
?
additional information
?
-
plays a key role in angiogenesis and tumor metastasis
-
?
additional information
?
-
-
plays a key role in angiogenesis and tumor metastasis
-
?
additional information
?
-
-
collagen binding domain is absolutely required for enzyme-dependent cleavage of full-length collagen alpha-chain, but not for short protein fragments such as those generated by hydrolysis of gelatin
-
-
?
additional information
?
-
-
collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen
-
-
?
additional information
?
-
-
investigation of ligand binding properties of the three fibronectin type II repeats of enzyme using collagen mimic peptide (L-Pro-L-Pro-Gly)6 and propeptide segment PIIKFPGDVA. Each module interacts essentially as an autonomous unit with these peptides, but enzyme shows cooperative participation toward a closer mimic of collagen, ((Gly-L-Pro-L-Pro-)12)3 in triple helical configuration
-
-
?
additional information
?
-
-
activation of MMP-2 may contribute to dentin matrix degradation, which occurs during caries progression and follows rresin bonding. Inhibition of MMP-2 proteolytic activity may slow caries progression and increase the durability of resin-dentin bond, overview
-
-
?
additional information
?
-
-
chitooligosaccharides may play an important role in the prevention and treatment of several MMP-2 mediated health problems such as metastasis and wrinkle formation, overview
-
-
?
additional information
?
-
-
intervertebral disc degeneration is associated with the increased expression of several matrix metalloproteinases, in particular MMP-2, overview
-
-
?
additional information
?
-
-
the enzyme degrades proteins of the extracellular matrix in the uterus and might be involved in the growth of leiomyoma and corresponding myometrium, overview
-
-
?
additional information
?
-
-
TSP-1 acts in LRP-mediated clearance of MMP-2, TIMP-2 complexing leads to MMP-2 accumulation in the cells
-
-
?
additional information
?
-
-
MMP-2 CBD-binding peptides from a random peptide library screening using biotinylated recombinant CBD domain, and interactions of immobilized synthetic peptides with the recombinant CBD, MMP-2E404A, MMP-2DELTACBD and AlkCBD, overview
-
-
?
additional information
?
-
-
the enzyme shows strong interaction with TSP-1 and CBD123, surface plasmon resonance analysis, overview
-
-
?
additional information
?
-
-
gel zymography for activity determination
-
-
?
additional information
?
-
-
kinetic and binding effects in peptide substrate selectivity of matrix metalloproteinase-2, molecular dynamics and QM/MM calculations, computational analysis of binding and hydrolysis reaction by MMP-2 of two peptide substrates selected by the enzyme from a phage peptide library, molecular dynamics simulations of the Michaelis complex, overview
-
-
?
additional information
?
-
the proteinase has the capacity to degrade several extracellular matrix components such as type IV collagens as well as all nonfibrillar collagens, laminin, fibronectin, casein, elastin, and even fibrillar collagens
-
-
?
additional information
?
-
-
the proteinase has the capacity to degrade several extracellular matrix components such as type IV collagens as well as all nonfibrillar collagens, laminin, fibronectin, casein, elastin, and even fibrillar collagens
-
-
?
additional information
?
-
enzyme activity is determined using human teeth as substrate
-
-
?
additional information
?
-
-
MMP-2 shows gelatinolytic activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
collagen type IV + H2O
?
-
-
-
-
?
collagene type IV + H2O
?
-
-
-
-
?
extracellular matrix components + H2O
?
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
degradation
-
-
?
additional information
?
-
Collagen + H2O
?
degradation of beta- and gamma-chains, weak activity with alpha-chains
-
-
?
Collagen + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
Gallus gallus Hy-Line Brown
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Type IV collagen + H2O
?
-
-
-
?
Type IV collagen + H2O
?
degradation
-
-
?
additional information
?
-
rMMP-2 degrades collagen effectively and the hydrolysate reveals scavenging activities on both 2, 2'-diphenyl-1-picrylhydrazyl free radical and hydrogen peroxide
-
-
?
additional information
?
-
-
Akt signaling is involved in the activation of MMP-2, and this Akt-induced activation of MMP-2 is responsible for reorganization of the actin cytoskeleton into a cortical pattern with parallel rounding of chondrogenic competent cells, MMP-2 regulation, not related to Erk signaling, overview
-
-
?
additional information
?
-
-
may be responsible for the pathological degradation and/or normal turnover of vitronectin
-
-
?
additional information
?
-
-
constitutively expressed in human rheumatoid synovial cells
-
-
?
additional information
?
-
-
activation of progelatinase B is mediated by gelatinase A species that may be localized in the surface of tumor cells and enhance matrix degradation during cancer metastasis
-
-
?
additional information
?
-
facilitates tmumor metastasis and angiogenesis by hydrolyzing components of the extracwllular matrix
-
?
additional information
?
-
-
facilitates tmumor metastasis and angiogenesis by hydrolyzing components of the extracwllular matrix
-
?
additional information
?
-
-
implicated in tumor cell metastasis and angiogenesis
-
?
additional information
?
-
-
important role in extracellular matrix degradation during cell migration and tissue remodeling, involved in development, inflammation, wound healing, tumor invasion, metastasis and other physiological and pathological processes
-
?
additional information
?
-
-
important role in tumor angiogenesis
-
?
additional information
?
-
plays a key role in angiogenesis and tumor metastasis
-
?
additional information
?
-
-
plays a key role in angiogenesis and tumor metastasis
-
?
additional information
?
-
-
collagen binding domain is absolutely required for enzyme-dependent cleavage of full-length collagen alpha-chain, but not for short protein fragments such as those generated by hydrolysis of gelatin
-
-
?
additional information
?
-
-
collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen
-
-
?
additional information
?
-
-
activation of MMP-2 may contribute to dentin matrix degradation, which occurs during caries progression and follows rresin bonding. Inhibition of MMP-2 proteolytic activity may slow caries progression and increase the durability of resin-dentin bond, overview
-
-
?
additional information
?
-
-
chitooligosaccharides may play an important role in the prevention and treatment of several MMP-2 mediated health problems such as metastasis and wrinkle formation, overview
-
-
?
additional information
?
-
-
intervertebral disc degeneration is associated with the increased expression of several matrix metalloproteinases, in particular MMP-2, overview
-
-
?
additional information
?
-
-
the enzyme degrades proteins of the extracellular matrix in the uterus and might be involved in the growth of leiomyoma and corresponding myometrium, overview
-
-
?
additional information
?
-
-
TSP-1 acts in LRP-mediated clearance of MMP-2, TIMP-2 complexing leads to MMP-2 accumulation in the cells
-
-
?
additional information
?
-
the proteinase has the capacity to degrade several extracellular matrix components such as type IV collagens as well as all nonfibrillar collagens, laminin, fibronectin, casein, elastin, and even fibrillar collagens
-
-
?
additional information
?
-
-
the proteinase has the capacity to degrade several extracellular matrix components such as type IV collagens as well as all nonfibrillar collagens, laminin, fibronectin, casein, elastin, and even fibrillar collagens
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
(2R)-2-[(4-biphenylylcarbonyl)amino]-N-hydroxy-3-(1H-indol-3-yl)propionamide
-
-
(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid
-
-
(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid benzyl ester
-
-
(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-(1H-indol-3-yl)propionic acid methyl ester
-
-
(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-methylbutanoic acid tert-butyl ester
-
-
(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid
-
-
(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid methyl ester
-
-
(2R)-3-(1H-indol-3yl)-2-[[4-(phenylazo)benzenesulfonyl]amino]propionic acid
-
-
(2R)-3-(1H-indol-3yl)-2-[[4-[phenylaminocarbonyl]-benzenesulfonyl]amino]propionic acid benzyl ester
-
-
(2R)-3-methyl-2-[4-[phenoxybenzenesulfonyl]amino]butanoic acid
-
-
(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)-amino]benzenesulfonyl]amino]butanoic acid
-
-
(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)amino]benzenesulfonyl]amino]butanoic acid tert-butyl ester
-
-
(2R)-3-methyl-2-[[4-[2-[4-methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid
-
-
(2R)-3-methyl-2-[[4-[2-[methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid tert-butyl ester
-
-
(2R)-3-methyl-2-[[5-[(4-methylphenyl)ethynyl]thiophene-2-sulfonyl]-amino]butanoic acid methyl ester
-
-
(2R)-N-(benzyloxy)-2-[(4-biphenylsulfonyl)amino]-3-phenylpropionamide
-
-
(2R)-N-hydroxy-3-methyl-2-[(4-phenoxybenzenesulfonyl)amino]butanamide
-
-
(2R)-[(4-biphenylsulfonyl)amino]-N-hydroxy-3-phenylpropionamide
-
-
(4-phenoxyphenylsulfonyl)methylthiirane
-
selective inhibitor of MMP2
2-(4-(4-[(2-thiiranylpropyl)sulfonyl]phenoxy)phenyl)acetic acid
-
selective inhibitor
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
-
-
2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-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-ylsulfonyl)(isobutyl)amino]-N-hydroxyacetamide
-
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
-
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
-
-
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
-
-
4-(2-phenyl-2H-tetrazol-5-yl)benzenesulfonyl chloride
-
-
4-(3-phenylureido) benzenesulfonyl chloride
-
-
4-(4-phenoxphenylsulfonyl)butane-1,2-dithiol
-
4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
-
-
5-(4-phenoxphenylsulfonyl)pentane-1,2-dithiol
-
advanced glycation products
-
inhibit the enzyme mediated through upregulation of the advanced glycation product receptor, overview
-
Ag-3340
-
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
-
-
-
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
-
batimastat
-
i.e. BB-94, a peptidomimetic inhibitor
benzyloxycarbonyl-L-Trp-OH
-
-
beta-amyloid precursor protein
-
APP
CGS27023A
-
50% inhibition at 20 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
chitooligosaccharides
-
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
-
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
-
-
D-tryptophan methyl ester tosylate
-
-
dibenzofuran-2-sulfonyl chloride
-
-
dimethyl sulfoxide
-
presence of 2% dimethyl sulfoxide disrupts interactions of enzyme with substrate and thereby reduces activity by 70%
extracellular domain of beta-amyloid peptide
-
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
-
GNDAMPL
-
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
-
APP-IP delta N/A
ISYGNAALMP
-
APP-IP delta D/A
ISYGNDAAMP
-
APP-IP delta L/A
ISYGNDAL
-
APP-IP delta C2
ISYGNDALM
-
APP-IP delta C1
ISYGNDALMPSL
-
APP586-597
ISYGNDALMPSLTETK
-
APP586-601
methyl 2-(4-(4-[(2-thiiranylpropyl)-sulfonyl]phenoxy)phenyl)acetate
-
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
-
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
-
-
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-[[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-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
NNGH
NaCl
-
binding to heparin and fibronectin can be disrupted by 0.3 M NaCl
peptide P713
-
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
-
procollagen C-terminal proteinase enhancer
PCPE
-
procyanidin oligomers
-
from Japanese quince, Chaenomeles japonica, fruit inhibit activity of MMP-2
-
RECK
reversion-inducing cysteine-rich protein with Kazal motifs
-
SB-3CT
mechanism-based synthetic inhibitor
SC-74020
-
hydroxamic acid inhibitor
Stromelysin catalytic domain inhibitors
-
gelatinase A synthetic 19000 MW catalytic domain
-
SYGNDAMPL
-
APP-IP delta N1
ter-butyloxycarbonyl-L-Trp-OH
-
-
TIMP-3
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
-
tissue factor pathway inhibitor
TFPI-2
-
Tissue inhibitor of metalloproteinase-1
-
-
-
Tissue inhibitor of metalloproteinase-2
-
Tissue inhibitor of metalloproteinases
-
tissue inhibitor of metalloproteinases-2
-
tissue inhibitors of metalloproteinase 2
TIMP2
-
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
-
APP-IP delta N2
Zn2+
-
required, synthetic 19000 MW catalytic domain, inhibition at high concentration
1,10-phenanthroline
-
-
1,10-phenanthroline
complete inhibition
1,10-phenanthroline
-
a non-specific inhibitor of metalloproteinases
EDTA
-
-
EGTA
-
-
GSH
-
-
GSSG
-
-
ilomastat
-
-
ilomastat
-
a pan-MMP inhibitor, strong inhibition
ISYGNDALMP
-
synthetic decapeptide APP-IP(APP586-595)
ISYGNDALMP
-
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
-
-
L-histidine
-
-
L-homocysteine
-
-
L-methionine
-
-
N-acetylcysteine
-
-
TIMP-1
-
-
-
TIMP-1
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
-
TIMP-2
-
-
-
TIMP-2
-
specific for MMP-2
-
TIMP-2
-
pro-MMP-2-TIMP-2 complexes are endocytosed into HT-1080 cells
-
TIMP-4
-
tissue inhibitor of metalloproteinases
-
TIMP-4
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
-
Tissue inhibitor of metalloproteinase-2
-
-
-
Tissue inhibitor of metalloproteinase-2
-
-
-
Tissue inhibitor of metalloproteinase-2
-
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
-
Tissue inhibitor of metalloproteinase-2
-
activity of the inhibitor is regulated by C-terminal domain interactions
-
Tissue inhibitor of metalloproteinase-2
-
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
-
Tissue inhibitor of metalloproteinase-2
-
-
-
Tissue inhibitor of metalloproteinase-2
-
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
-
Tissue inhibitor of metalloproteinases
-
-
-
Tissue inhibitor of metalloproteinases
-
-
-
tissue inhibitor of metalloproteinases-2
-
TIMP-2, complex formation with MMP-14 and MMP-2 activates the enzyme, overview
-
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
-
additional information
PMSF, benzamidine, E-64, and pepstatin A are poor inhibitors
-
additional information
-
PMSF, benzamidine, E-64, and pepstatin A are poor inhibitors
-
additional information
-
not: inhibitors of serine, cysteine or aspartic proteinases
-
additional information
-
dithiothreitol does not interfere with heparin binding
-
additional information
-
inhibition of MMP-2 gelatinolysis by targeting exodomain-substrate interactions
-
additional information
-
inhibitor synthesis and molecular docking, overview
-
additional information
-
inhibition potency of sulfur-containing compounds, overview
-
additional information
-
allyl isothiocyanate and N-acetylcysteinyl-allyl isothiocyanate downregulate MMP-2 expression in SK-Hep1 hepatoma cells, as well as adhesion, invasion, and migration, overview
-
additional information
-
CBD123 decreases active MMP-2 levels in HT-1080 cells, but only marginally the content of pro-MMP-2, overview
-
additional information
-
simultaneous binding of each ligand heparan sulfate and hirudin to the exosites is necessary for the complete inhibition of MMP-2 degradation by thrombin
-
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
-
additional information
molecular design of a highly selective and strong protein inhibitor against matrix metalloproteinase-2, overview
-
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
-
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
-
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
-
additional information
-
calreticulin-deficient null mice embryos show increased MMP-2 expression and activity, phosphatidylinositol 3 kinase inhibitor decreases the MMP-2 expression, overview
-
additional information
-
inhibition potency of sulfur-containing compounds, overview
-
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4-aminophenylmercuric acetate
-
-
aminophenylmercuric acetate
-
-
heparan sulfate
-
essential for thrombin-mediated activation of pro-MMP-2
interleukin 1beta
-
increases enzyme expression and activity in cardiac microvascular endothelial cells, involvement of PKC and/or MAPK signaling cascades, overview, the activation is inhibited by 52% by Gö6976, a PKC inhibitor, at 100 nM, while inhibitors SN50 and SP600125 have no effect on the activation
-
membrane-type 1 matrix metalloproteinase
-
activity in the extracellular environment is modulated by this activator
-
MMP-14
-
MMP-14 activates MMP-2 during degeneration of invertebral disc, a major activation pathway of MMP-2 involves complex formation with MMP-14 and a tissue inhibitor of metalloproteinases-2, TIMP-2, overview
-
p-aminophenyl-mercuric acetate
-
-
prostaglandin E2
PGE2, significantly increases MMP-2 activity as well as tube formation in endothelial cells. The PGE2-mediated elevation of MMP-2 activity is associated with the pro-angiogenic responses
syndecan-1
-
expression of syndecan-1 increases thrombin-mediated activation of pro-MMP-2 in K562 cells
-
thrombin
-
dependent on, molecular mechanisms underlying thrombin-mediated MMP-2 activation, overview. Interaction of MMP-2 with exosites 1 and 2 of thrombin is crucial for thrombin- mediated MMP-2 degradation, and inhibition of this interaction by heparan sulfate or hirudin fragment results in a decrease in MMP-2 degradation, interaction between exosite 1 and hemopexin-like domain of MMP-2
-
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
-
additional information
-
rapid activation of the zymogen by 4-aminophenylmercuric acetate
-
additional information
-
no activation by endopeptidases (trypsin, chymotrypsin, plasmin, plasma kallikrein, thrombin, neutrophil elastase, cathepsin G, matrix metalloproteinase 3, thermolysin)
-
additional information
-
interaction of the zymogen with fetuin or asialofetuin results in cleavage to lower MW forms and activation
-
additional information
-
activation of pro-MMP-2 by 4-aminophenylmercuric acetate
-
additional information
-
sonicated bacterial extract from Porphyromonas gingivalis (0.0001 mg/ml at 37°C for 18 h) activates MMP-2
-
additional information
heparan sulfate is required for thrombin-mediated activation of pro-MMP-2 by binding to thrombin, presumably through conformational changes at the active site of the enzyme. Homodimerization of the enzyme enhances thrombin-mediated activation of pro-MMP-2. 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
-
additional information
involvement of MT1MMP and TIMP-2 in MMP-2 activation during progression of endometriosis, overview
-
additional information
-
involvement of MT1MMP and TIMP-2 in MMP-2 activation during progression of endometriosis, overview
-
additional information
-
a complex formed by MT1-MMP, TIMP-2, and MMP-2 and located at the cell surface, is involved in MMP-2 activation, overview
-
additional information
-
rapid activation of the zymogen by 4-aminophenylmercuric acetate
-
additional information
-
trypsin is a poor activator
-
additional information
-
implantation of 9L glioma cells into brain increases the expression of MMP-2, overview
-
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0.00028
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.000123
(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.0000092
(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.00012
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.0785
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.000188
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
Homo sapiens
-
-
0.000009
2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000534
2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
Homo sapiens
-
-
0.000776
2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.00062
2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.00438
2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000017
2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000998
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000457
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
Homo sapiens
-
-
0.001208
2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.141
ascorbic acid
Homo sapiens
-
recombinant enzyme
0.195
GSH
Homo sapiens
-
recombinant enzyme
0.547
GSSG
Homo sapiens
-
recombinant enzyme
0.0000005 - 0.0000011
ilomastat
0.0073 - 0.015
ISYGNDALMP
Homo sapiens
-
pH 7.5, 37°C, recombinant fragments of MMP-2
0.061
L-cysteine
Homo sapiens
-
recombinant enzyme
0.118
L-histidine
Homo sapiens
-
recombinant enzyme
0.727
L-homocysteine
Homo sapiens
-
recombinant enzyme
8.68
L-methionine
Homo sapiens
-
recombinant enzyme
1
N-acetylcysteine
Homo sapiens
-
recombinant enzyme
0.00308
N-hydroxy-2-([4-[2-(trifluoromethyl)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
Homo sapiens
-
-
0.000173
N-hydroxy-2-([4-[2-methyl-3'-(trifluoromethoxy)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
Homo sapiens
-
-
0.000262
N-hydroxy-2-([4-[3'-(2-hydroxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
Homo sapiens
-
-
0.000853
N-hydroxy-2-([4-[3'-(2-methoxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
Homo sapiens
-
-
0.000196
N-hydroxy-2-([4-[3'-(methoxymethyl)-2-methylbiphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
Homo sapiens
-
-
0.000196
N-hydroxy-2-methyl-2-[(4-[2-methyl-3'-[2-(methylamino)ethoxy]biphenyl-4-yl]piperidin-1-yl)sulfonyl]propanamide
Homo sapiens
-
-
0.000529
N-hydroxy-2-[(4-[4-[6-(2-hydroxyethoxy)pyridin-2-yl]-3-methylphenyl]piperidin-1-yl)sulfonyl]-2-methylpropanamide
Homo sapiens
-
-
0.00032
N-hydroxy-2-[[4-(2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
Homo sapiens
-
-
0.000222
N-hydroxy-2-[[4-(3'-methoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
Homo sapiens
-
-
0.01
peptide P713
Homo sapiens
-
pH 7.0, 22°C
-
0.0342
UK-370106
Homo sapiens
-
-
additional information
additional information
-
0.0000005
ilomastat
Homo sapiens
-
pH 7.4, 37°C
0.0000011
ilomastat
Homo sapiens
-
-
additional information
additional information
Homo sapiens
-
-
-
additional information
additional information
Homo sapiens
-
-
-
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-
brenda
-
aged arterial wall, colocalization of activated enzyme and transforming growth factor TGF-beta1. Treatment of young aortic rings with activated enzyme enhances active transforming growth factor TGF-beta-1, collagen, and fibronectin expression to the level of untreated old counterparts
brenda
-
melanoma cell
brenda
-
brenda
-
brenda
the enzyme is overexpressed in tumors, it is expressed in all tumors tested
brenda
-
brenda
-
brenda
higher intensity of staining of MMP-2 is observed in regions of invasion of the muscularis mucosa compared with superficial portions of the tumor in colorectal cancer
brenda
-
demineralized dentin matrix, extraction is best at acidic conditions of pH 2-3 compared to pH 7.4-EDTA-containing extracts
brenda
-
nucleus pulposus of intervertebral disc
brenda
-
brenda
-
-
brenda
-
-
brenda
very high expression
brenda
-
secretory
brenda
oxytalan fibers
brenda
low expression
brenda
-
tumor periphery
brenda
-
induced by acetic acid injection
brenda
higher expression
brenda
-
high expression level of MMP-2 increasing during growth
brenda
higher expression
brenda
-
-
brenda
-
HSC-180 cell
brenda
-
-
brenda
-
-
brenda
-
brenda
-
leukemia cell line, secretion of MMP-2
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
low expression
brenda
-
derived from premenopausal women aged 45-55 years who underwent total abdominal hysterectomy
brenda
-
brenda
-
brenda
-
-
brenda
-
regional lymph node invasion and distant metastases are more frequently observed in the MMP-2 positive cases, the MMP-2/TIMP-2 ratio is also positively correlated with MMP-2 activity, overview
brenda
beta-cell
brenda
-
stimulated, release of MMP-2 in vitro
brenda
-
-
brenda
-
secretion of MMP-2
brenda
-
brenda
-
plasma prepared from blood emerging from a skin wound inflicted for the measurement of the bleeding time, shed blood, and simultaneously from venous blood in 27 healthy human volunteers, with and without treatment of the individuals with acetylsalicylic acid before. MMP-2 activity is higher in shed blood. Acetylsalicylic acid has no effect on MMP-2 secretion, overview
brenda
-
male and female
brenda
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
Mycobacterium tuberculosis stimulates matrix metalloproteinases secretion in the host. Analysis of the patterns of matrix metalloproteinase 9 (MMP-9) and 2 (MMP-2) isoforms in sputum samples, overview
brenda
low expression
brenda
-
brenda
-
GelA is expressed in fibroblasts surrounding apoptotic cells, spatial localization of MT1-MMP and GelA mRNAs in the tail during natural metamorphosis, overview
brenda
-
brenda
-
brenda
-
-
brenda
-
brenda
-
fibroids of different size show equal MMP-2 activity
brenda
-
brenda
-
-
-
brenda
-
brenda
-
-
-
brenda
-
low content
brenda
-
endplate
brenda
-
secretion of MMP-2
brenda
-
human platelets contain matrix metalloproteinase 2 and release it upon activation
brenda
-
brenda
-
expression analysis in brain after implantation of 9L glioma cells, overview
brenda
-
low activity
brenda
-
brenda
-
recombinant enzyme
brenda
-
recombinant MMP-2
brenda
-
recombinant pro-MMP-2
brenda
recombinant pro-enzyme and recombinant mature, activated enzyme
brenda
-
from Rous-sarcoma virus-transformed chicken embryo fibroblasts
brenda
-
-
brenda
-
from human rheumatoid synovial cells
brenda
-
conditioned medium from T98G human glioblastoma cells
brenda
-
from H-ras-transformed human bronchial epithelial cells (TBE-1)
brenda
-
latent proenzyme
brenda
-
from HeLa cells co-infected with each of the recombinant Vaccinia viruses and with vTF7-3
brenda
-
from calvariae
brenda
-
of synoviocytes
brenda
-
brenda
-
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
primary dermal
brenda
from periodontal ligaments
brenda
-
-
brenda
-
cardiac
brenda
-
GelA is expressed in fibroblasts surrounding apoptotic cells of intestine and tail
brenda
-
brenda
the enzyme is upregultaed compared to control brain
brenda
-
brenda
-
-
brenda
low expression
brenda
-
-
brenda
-
-
brenda
-
brenda
-
fibrosarcoma cell
brenda
-
tumour cells developed in mice, high expression level
brenda
higher expression
brenda
-
GelA is expressed in fibroblasts surrounding apoptotic cells, expression of GelA is downregulated in the intestine by the end of metamorphosis when the tail is completely resorbed, and the adult intestine has formed
brenda
-
cirrhotic liver
brenda
-
-
brenda
-
brenda
-
high activity
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
brenda
Gallus gallus Hy-Line Brown
-
infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
-
brenda
-
brenda
-
-
-
brenda
-
brenda
distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers, quantification of MMP2 in muscle, overview
brenda
distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers, quantification of MMP2 in muscle, overview. On average, about 57% of the MMP2, along with most of the GAPDH, in the skinned fibers is freely diffusible in the cytosol, about 6% of the MMP2 dissociates with the subsequent 10-min Triton X-100 treatment, and about 37% of the MMP2 remains in the skinned fiber
brenda
-
-
brenda
-
hepatoma cell line
brenda
-
pulmonary artery smooth muscle
brenda
-
brenda
-
vascular smooth muscle, colocalization of activated enzyme and transforming growth factor TGF-beta1. Treatment of vascular smooth muscle cells in vitro with activated enzyme enhances active transforming growth factor TGF-beta-1, collagen, and fibronectin expression to the level of untreated old counterparts
brenda
-
-
brenda
-
brenda
-
-
brenda
-
tissue samples of oral squamous cell carcinomas
brenda
-
activity of MMP-2 in odontogenic region of the rat incisor tooth after post shortening procedure, overview
brenda
-
activity of MMP-2 in odontogenic region of the rat incisor tooth after post shortening procedure, overview
-
brenda
-
enzyme level and expression analysis in response to advanced glycation products
brenda
-
stimulated, release of MMP-2 in vitro
brenda
-
brenda
eutopic, and ectopic, ovarian
brenda
additional information
-
expression analysis of MMP-2 in dog tumor tissues, overview
brenda
additional information
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
brenda
additional information
-
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
brenda
additional information
Gallus gallus Hy-Line Brown
-
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
-
brenda
additional information
ubiquitous expression of MMP-2
brenda
additional information
quantitative real time PCR enzyme expression analysis and immunohistochemic analysis in glioblastoma
brenda
additional information
-
quantitative real time PCR enzyme expression analysis and immunohistochemic analysis in glioblastoma
brenda
additional information
circulating hMMP2is significantly increased in diabetic patients compared to controls and significantly correlated with the serum C-peptide levels
brenda
additional information
-
circulating hMMP2is significantly increased in diabetic patients compared to controls and significantly correlated with the serum C-peptide levels
brenda
additional information
-
MMP-2 immunoexpression in all phases of estrous cycle
brenda
additional information
the enzyme is highly expressed in epidermis, located to endoplasmic reticulum in S2 cells
brenda
additional information
-
the enzyme is highly expressed in epidermis, located to endoplasmic reticulum in S2 cells
brenda
additional information
-
MMP-2 is increased in tumor cells
brenda
additional information
in rat soleus muscle and other tissues, pro- and active MMP2 show gelatinase activity, as well as a higher band that has been reported previously to represent a rodent-specific glycosylated MMP2
brenda
additional information
-
MMP-2 activity in tissues taken from newborn piglets undergoing hypoxia and reoxygenation, overview
brenda
additional information
-
co-localization of MT1-MMP and GelA mRNAs during amphibian development, overview
brenda
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evolution
MMP-2 is a member of the matrix metalloproteinase family
malfunction
-
the inactivation of the MMP-2 gene prevents thrombosis induced by weak, but not strong, stimuli but produces only a moderate prolongation of the bleeding time. MMP-2 deficient mice have hyporeactive platelets, a defective thrombotic response and mildly impaired hemostasis
malfunction
in de novo formed fat pads, resulting from preadipocytes with Mmp2 knockdown, the expression of aP2, Ppar-gamma and adiponectin is significantly lower, and collagen is more preserved. The fat pad weights as well as size and density of adipocytes or blood vessels are not significantly different from controls, phenotype, overview
malfunction
induction of diabetes in transgenic mice overexpressing human MMP2 show ignificant improvements in glycemia, glucose tolerance and insulin secretion compared to diabetic wild-type mice. Increased hMMP2 levels in mice correlate with significant reduction in islet beta-cell apoptosis compared to wild-type counterparts, and an inhibitor of hMMP2 reverses this mitigating activity against diabetes
malfunction
knockdown of LvMMP-2 expression decreases shrimp cumulative mortality upon oxidative stress. Knocked-down expression of LvMMP-2 depresse sthe expression of penaeidin2 and beta-defensin. Downregulation of LvMMP-2 suppresses the cumulative mortality of shrimp infected with white spot syndrome virus (WSSV) or with Vibrio alginolyticus
malfunction
women with endometriosis show decreased MMP-2 activity in eutopic endometrium as compared to women without endometriosis, while ectopic ovarian endometrioma show significantly elevated MMP-2 activity with disease severity. Increased MMP-2 activation with disease progression
malfunction
-
in de novo formed fat pads, resulting from preadipocytes with Mmp2 knockdown, the expression of aP2, Ppar-gamma and adiponectin is significantly lower, and collagen is more preserved. The fat pad weights as well as size and density of adipocytes or blood vessels are not significantly different from controls, phenotype, overview
-
metabolism
-
evaluation of the effect that the hormonal fluctuations of the reproductive cycle have on the stromal remodeling and the expression and activity of matrix metalloproteinases MMP-2 and -9 in the adult female gerbil prostate, overview
metabolism
expansion of adipose tissue is dependent on adipogenesis, angiogenesis and extracellular matrix remodeling by the gelatinase subfamily of the matrix metalloproteinases, overview
metabolism
aortic stiffness is an independent risk factor for development of cardiovascular diseases. Activation of renin-angiotensin-aldosterone system (RAAS) including angiotensin converting enzyme (ACE) activity leads to overproduction of angiotensin II (ANGII) from its precursor angiotensin I (ANGI). ANGII leads to overexpression and activation of matrix metalloproteinase-2 (MMP2), which is critically associated with pathophysiology of aortic stiffness
metabolism
-
expansion of adipose tissue is dependent on adipogenesis, angiogenesis and extracellular matrix remodeling by the gelatinase subfamily of the matrix metalloproteinases, overview
-
physiological function
-
platelet-derived MMP-2 facilitates thrombus formation
physiological function
-
in adult rats, in opposite to development of tooth, the MMP-9 and MMP-2 present in the odontogenic region does not seem to play a direct role in the remodeling matrix, even after post-shortening procedures which to lead an acceleration of the eruption process in the incisor
physiological function
enzyme MMP-2 is considered a major enzyme involved in the turnover of the extracellular matrix. The enzyme is involved in the degradation of fibrillin-1 and fibrillin-2, the degradation patterns differ between the eye and the periodontal ligaments, possibly reflecting the sensitivity of fibrillin-1 and fibrillin-2 of each type of oxytalan fiber against enzyme MMP-2
physiological function
the enzyme act as important oncogenes that improve invasiveness of cancer cells
physiological function
the enzyme gelatinase A is involved in adipogenesis, selective modulation of MMP-2 levels affects adipogenesis
physiological function
chronic progression of diabetes is associated with decreased pancreatic islet mass due to apoptosis of beta-cells. Patients with diabetes have increased circulating matrix metalloproteinase-2 (MMP2). MMP2 might inhibit cell apoptosis, including islet beta-cells. The increased activation of Akt and BAD induced by hMMP2 in beta-cells compared to controls, links this signaling pathway to the anti-apoptotic activity of hMMP2, a property that is reversible by both an hMMP2 inhibitor and antibody against integrin-beta3. hMMP2 may attenuate the severity of diabetes by protecting islet beta-cells from apoptosis through an integrin-mediated activation of the Akt/BAD pathway. Preliminary treatment of cells, e.g. HepG2 cells, HUVE cells, and NHM cells, with active hMMP2 for 30-min significantly inhibits apoptosis (induced by starvation), hMMP2 inhibits apoptosis of beta-cell lines, which is modulated by intergrins
physiological function
LvMMP-2 plays a role in innate immunity response. Promoter activity of LvMMP-2 is enhanced by LvNRF2 in a ARE site dependent-manner. Overexpression of Lvc-Jun in S2 cells demonstrates that AP-1 factor c-Jun is also involved in LvMMP-2 regulation
physiological function
matrix metalloproteinase MMP-2 degrades components of the extracellular matrix, denatured interstitial type I collagen and native type IV collagen. MMP-2 is a key player in cancer invasion and metastasis. Different mechanisms contribute to regulate the activity of MMP-2 during its molecular existence: expression, secretion, activation, extra/pericellular localization, inhibition, endocytosis and lysosomal degradation. Epigenetic control also contributes to MMP-2 regulation. Levels of control of extra/pericellular MMP-2, overview The enzyme is present in the extracellular compartment for degrading denatured type I collagen. Cell membrane-bound MMP-2 can also act as transducers and trigger outside-in signaling. Binding of proMMP-2 to alphavbeta3 integrin on the surface of lung cancer cells stimulates tumor angiogenesis by activating PI3K/AKT pathway and HIF-1alpha, leading to VEGF-A expression
physiological function
matrix metalloproteinase-2 (gelatinase A) is a mediator of cancer metastasis, but it is also thought to be involved in several aspects of cancer development, including cell growth and inflammation. MMP-2 may be associated with colorectal cancer development and invasion in the Tunisian population
physiological function
MMP-2 isoforms do not seem to be directly involved with Mycobacterium tuberculosis evolution of infection
physiological function
potential role of the MMP system in avian oviduct development, avian reproductive system differs from that of mammals. The gelatinases, stromelysins and matrilysins, all belonging to the MMP family, are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin. Gelatinolytic activity of MMPs in the chicken oviduct during maturation, overview
physiological function
regulation of matrix metalloproteinase-2 activity by COX-2-PGE2-pAKT axis promotes angiogenesis in endometriosis. Analysis of the regulation of MMP-2 activity in endothelial cells and on angiogenesis during progression of ovarian endometriosis, overview. Involvement of MT1MMP and TIMP-2 in MMP-2 activation during progression of endometriosis
physiological function
the enzyme exhibits gelatinolytic activity which is enhanced by p-aminophenylmercuric acetate (APMA). The APMA treated enzyme probably also produces proteolytic products of myosin and other muscle proteins
physiological function
Gallus gallus Hy-Line Brown
-
potential role of the MMP system in avian oviduct development, avian reproductive system differs from that of mammals. The gelatinases, stromelysins and matrilysins, all belonging to the MMP family, are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin. Gelatinolytic activity of MMPs in the chicken oviduct during maturation, overview
-
physiological function
-
the enzyme gelatinase A is involved in adipogenesis, selective modulation of MMP-2 levels affects adipogenesis
-
physiological function
-
in adult rats, in opposite to development of tooth, the MMP-9 and MMP-2 present in the odontogenic region does not seem to play a direct role in the remodeling matrix, even after post-shortening procedures which to lead an acceleration of the eruption process in the incisor
-
additional information
-
the SDF-1a/CXCR4 axis is involved in osteopontininduced MMP-2 expression and activity, overview
additional information
-
thrombin-dependent MMP-2 activity is regulated by heparan sulfate, molecular mechanism, regulatory role of hemopexin-like domain in MMP-2 degradation, overview
additional information
crucial role of the fibronectin-like domain in enzymatic activities, it is involved in substrate binding
additional information
-
crucial role of the fibronectin-like domain in enzymatic activities, it is involved in substrate binding
additional information
enzyme MMP-2 forms heterodimers with various proteins, including TIMP-2, TIMP-3, TIMP-4, and glycosaminoglycans. 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
additional information
MMP-2 has two isoforms: the 72 kDa latent form and an active form of 62 kDa, which is generated from the 10 kDa pro-domain cut-off. MMP-2 isoforms identification and determination of activities, overview
additional information
-
MMP-2 has two isoforms: the 72 kDa latent form and an active form of 62 kDa, which is generated from the 10 kDa pro-domain cut-off. MMP-2 isoforms identification and determination of activities, overview
additional information
the Zn2+-binding motif of the catalytic domain is preceded by three cysteine-rich repeats comparable to the collagen-binding fibronectin type II (FN-II) repeats, which are required for recognizing collagen and elastin
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20000
-
GaCD, without fibronectin-like insert, SDS-PAGE
25920
-
recombinant C domain, elektrospray mass spectrometry
26500
-
recombinant C domain, SDS-PAGE
38000
-
GaCDfn, with fibronectin-like insert, SDS-PAGE
47052
-
x * 66000, SDS-PAGE, x * 66518, calculated, enzyme mutant E404A, x * 59000, SDS-PAGE, x * 47052, calculated, enzyme mutant lacking collagen-binding domain
57000
-
x * 57000, human, active form, SDS-PAGE
59000
-
x * 66000, SDS-PAGE, x * 66518, calculated, enzyme mutant E404A, x * 59000, SDS-PAGE, x * 47052, calculated, enzyme mutant lacking collagen-binding domain
61000
-
x * 61000, rabbit, active form, SDS-PAGE under nonreducing conditions
64000
x * 72000, native proMMP-2, x * 64000, recombinant MMP-2
66518
-
x * 66000, SDS-PAGE, x * 66518, calculated, enzyme mutant E404A, x * 59000, SDS-PAGE, x * 47052, calculated, enzyme mutant lacking collagen-binding domain
67000
-
x * 67000, human, active form, SDS-PAGE under reducing condition
45000
-
active form lacking the C-terminal domain, SDS-PAGE
45000
-
x * 72000, proenzyme, x * 62000 and x * 45000, active species, SDS-PAGE
62000
-
SDS-PAGE
62000
-
active MMP-2, SDS-PAGE
62000
-
x * 62000, human, active enzyme, SDS-PAGE under reducing conditions
62000
-
x * 72000, proenzyme, x * 62000 and x * 45000, active species, SDS-PAGE
62000
-
x * 72000, latent MMP-2, SDS-PAGE, x * 62000, activ MMP-2, SDS-PAGE
65000
-
x * 65000, rabbit, latent form, SDS-PAGE under nonreducing conditions
65000
-
x * 65000, rabbit, active form, SDS-PAGE under reducing conditions
66000
-
x * 66000, human, active form, SDS-PAGE
66000
-
x * 66000, SDS-PAGE, x * 66518, calculated, enzyme mutant E404A, x * 59000, SDS-PAGE, x * 47052, calculated, enzyme mutant lacking collagen-binding domain
66000
-
x * 72000, pro-MMP-2, SDS-PAGE, x * 66000, activated MMP-2, SDS-PAGE
68000
-
proMMP-2, SDS-PAGE
68000
-
x * 68000, active MMP-2, SDS-PAGE, x * 72000, proMMP-2, SDS-PAGE
72000
-
-
72000
-
pro-MMP-2, SDS-PAGE
72000
-
x * 72000, human, zymogen, SDS-PAGE under reducing conditions
72000
-
x * 72000, human, zymogen, SDS-PAGE
72000
-
x * 72000, rabbit, latent form, SDS-PAGE under reducing conditions
72000
-
x * 72000, proenzyme, x * 62000 and x * 45000, active species, SDS-PAGE
72000
-
x * 68000, active MMP-2, SDS-PAGE, x * 72000, proMMP-2, SDS-PAGE
72000
-
x * 72000, latent MMP-2, SDS-PAGE, x * 62000, activ MMP-2, SDS-PAGE
72000
x * 72000, native proMMP-2, x * 64000, recombinant MMP-2
72000
-
x * 72000, pro-MMP-2, SDS-PAGE, x * 66000, activated MMP-2, SDS-PAGE
72000
-
x * 72000, proMMP-2, SDS-PAGE
72000
x * 72000, zymogen, SDS-PAGE
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homodimer
homodimerization of enzyme MMP-2, through an intermolecular disulfide bond between Cys102 and the neighboring Cys102, requires Ca2+ but is not associated with protein kinase C-mediated phosphorylation. The cleavage is followed by intermolecular autoproteolytic cleavage at the Asn109-Tyr peptide bond, resulting in full enzymatic activation. Homodimerization of the enzyme enhances thrombin-mediated activation of pro-MMP-2
?
x * 40000, recombinant MMP-2(111-461), SDS-PAGE, x * 70890, sequence calculation
?
-
x * 72000, proenzyme, x * 62000 and x * 45000, active species, SDS-PAGE
?
x * 72000, enzyme proform, SDS-PAGE, x * 66000, mature active enzyme, SDS-PAGE
?
Gallus gallus Hy-Line Brown
-
x * 72000, enzyme proform, SDS-PAGE, x * 66000, mature active enzyme, SDS-PAGE
-
?
-
x * 62000, human, active enzyme, SDS-PAGE under reducing conditions
?
-
x * 57000, human, active form, SDS-PAGE
?
-
x * 72000, human, zymogen, SDS-PAGE under reducing conditions
?
-
x * 67000, human, active form, SDS-PAGE under reducing condition
?
-
x * 72000, human, zymogen, SDS-PAGE
?
-
x * 66000, human, active form, SDS-PAGE
?
-
x * 66000, SDS-PAGE, x * 66518, calculated, enzyme mutant E404A, x * 59000, SDS-PAGE, x * 47052, calculated, enzyme mutant lacking collagen-binding domain
?
-
x * 68000, active MMP-2, SDS-PAGE, x * 72000, proMMP-2, SDS-PAGE
?
-
x * 72000, latent MMP-2, SDS-PAGE, x * 62000, activ MMP-2, SDS-PAGE
?
x * 72000, native proMMP-2, x * 64000, recombinant MMP-2
?
-
x * 72000, proMMP-2, SDS-PAGE
?
x * 72000, zymogen, SDS-PAGE
?
-
x * 65000, rabbit, latent form, SDS-PAGE under nonreducing conditions
?
-
x * 61000, rabbit, active form, SDS-PAGE under nonreducing conditions
?
-
x * 72000, rabbit, latent form, SDS-PAGE under reducing conditions
?
-
x * 65000, rabbit, active form, SDS-PAGE under reducing conditions
?
-
x * 72000, pro-MMP-2, SDS-PAGE, x * 66000, activated MMP-2, SDS-PAGE
additional information
the deduced amino acid sequence of MMP-2 contains a signal peptide, a propeptide domain, a catalytic domain with three repeats of fibronectin-type II region and a C-terminal hemopexin-like domain. Three-dimensional and secondary enzyme structure analysis
additional information
-
native and denatured collagen binding properties reside in the fibronectin type II modules of enzyme, that is the collagen binding domain. Enzyme utilizes the collagen binding domain in cis for collagen binding and triple helicase activity
additional information
-
modeling of the interaction of fibrinogen with different truncated forms of MMP-2, i.e. the autoinhibitory procatalytic domain, the catalytic domain, the catalytic domain lacking the fibronectin-like domain, the fibronectin-like domain alone, and the haemopexin-like domain, using crystal structures isolated from the full-length proMMP-2, PDB ID 1CK7, overview
additional information
proMMP-2 consists of a signal peptide, a pro-peptide, a collagenase-like domain 1, a collagen-binding domain, a collagenase-like domain 2, and a hemopexin-like domain
additional information
enzyme MMP-2 forms heterodimers with various proteins, including TIMP-2, TIMP-3, TIMP-4, and glycosaminoglycans
additional information
MMP-2 has two isoforms: the 72 kDa latent form and an active form of 62 kDa, which is generated from the 10 kDa pro-domain cut-off. MMP-2 isoforms identification and determination of activities, overview
additional information
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MMP-2 has two isoforms: the 72 kDa latent form and an active form of 62 kDa, which is generated from the 10 kDa pro-domain cut-off. MMP-2 isoforms identification and determination of activities, overview
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C102S
site-directed mutagenesis
C233S
site-directed mutagenesis
C247S
site-directed mutagenesis
C259S
site-directed mutagenesis
C274S
site-directed mutagenesis
C291S
site-directed mutagenesis
C305S
site-directed mutagenesis
C317S
site-directed mutagenesis
C332S
site-directed mutagenesis
C349S
site-directed mutagenesis
C363S
site-directed mutagenesis
C375S
site-directed mutagenesis
C395S
site-directed mutagenesis
C60S
site-directed mutagenesis
C65S
site-directed mutagenesis
D49A
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site-directed mutagenesis
E412D
site-directed mutagenesis
K50G
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site-directed mutagenesis
K50R
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site-directed mutagenesis
R19L
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site-directed mutagenesis
R19L/R38L
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site-directed mutagenesis
R38L
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site-directed mutagenesis
S160A
site-directed mutagenesis
S365A
site-directed mutagenesis
S575A
site-directed mutagenesis
S644A
site-directed mutagenesis
S647A
site-directed mutagenesis
T250A
site-directed mutagenesis
T354A
site-directed mutagenesis
T377A/T378A
site-directed mutagenesis
T455A
site-directed mutagenesis
T73A
site-directed mutagenesis
T96A
site-directed mutagenesis
Y25A
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site-directed mutagenesis
Y37A
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site-directed mutagenesis
Y46A
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site-directed mutagenesis
Y52A
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site-directed mutagenesis
down
peptide isoleucine-tryptophan (Ile-Trp) inhibits expression and activity of matrix metalloproteinase-2 in rat aorta
E404A
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no enzymic activity, competition with isolated collagen-binding domain and with matrix metalloproteinase MMP-9 binding to native and denatured type I collagen
E404A
proteolytically inactive pro-MMP-2 mutant
additional information
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recombinant collagen binding domain of enzyme, competitive inhibition of gelatin binding to intact enzyme by 73%, inhibition of enzyme-dependent cleavage of an 11 amino acid short protein fragment by less than 10%
additional information
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recombinant enzyme lacking collagen-binding domain, does not block binding to gelatin of either enzyme mutant E404A or matrix metalloproteinase MMP-9 mutant E402A
additional information
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construction of MMP-2 truncation mutants overview, an MMP-2 mutant, with deleted hemopexin-like domain and three fibronectin-like type II domains, and native MMP-2 show similar affinities for APP-IP, chimeric proteases, consisting of various parts of the MMP-2 catalytic domain and those of MMP-7 or MMP-9, show that Ala88 and Gly94 in the non-prime side and Tyr145 and Thr146 in the prime side of the substrate-binding cleft of MMP-2 contribute separately to the selective inhibition bei APP-PI, mutational interaction analysis, overview
additional information
generation of transgenic C57BL/6 mice overexpressing human MMP2, phenotype, overview
additional information
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generation of transgenic C57BL/6 mice overexpressing human MMP2, phenotype, overview
additional information
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calreticulin-deficient null mice embryos show increased MMP-2 expression and activity, but unaltered TIMP-2 inhibitor levels, the embryos show defects in the heart and body wall, phenotype, overview
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cDNA cloned and expressed in Escherichia coli JM-109
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cDNA of the mutated enzyme used to transfect HEK 293 cells
cDNA, recombinant C domain expressed in Escherichia coli
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cloned and expressed in Escherichia coli
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cloned and overexpressed in a bacterial system, Escherichia coli BL21(DE3)pLysS
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expression of GST-tagged MMP-2 in Escherichia coli strain DH5alpha in inclusion bodies
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expression of His- and myc-tagged pro-MMP-2
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expression of the first, second, and third module, i.e. CBD1, CBD2 and CBD3 polypeptides, and of the fibronectin type-II-like modelues of MMP-2 in Escherichia coli
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expression of the His-tagged enzyme without pro-domain and of the isolated MMP-2 CBD domain in Escherichia coli in inclusion bodies
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full-length progelatinase A
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gene LvMMP-2, DNA and amino acid sequence determination and analysis, sequence compariosns and phylogenetic analysis, quantitative real-time RT-PCR enzyme expression analysis
gene MMP-2 , cloning from skeletal muscle, DNA and amino acid sequence determination and analysis, sequence comparissons, expression of recombinant His-tagged MMP-2 in truncated form in Escherichia coli inclusion bodies
gene MMP-2, quantitative real time PCR expression analysis in glioblastoma
gene MMP2, genotyping in Tunesian population. The levels of MMP-2 mRNA expression in patients containing the CC genotype are much higher compared with cells with the CT genotype. The frequency of the MMP-2 CC genotype is significantly higher in colorectal cancer patients when compared with controls
gene MMP2, quantitative RT-PCR enzyme expression analysis
gene MMP2, sequence comparisons, enzyme expression analysis
gene MMP2, the gene is located on the long arm of chromosome 16 at position q12.2, the cDNA for MMP-2 codes for a 660 residues preproenzyme containing a 29 residues signal peptide responsible for translocation to the endoplasmic reticulum and followed by the 72-kDa-proenzyme. The human MMP2 gene lacks a conventional TATA-box or classical transcription response elements found in other MMP genes, the constitutive expression depends on p53-, Sp1-, Sp3-and AP-2-binding sites but the promoter contains other cis-regulatory elements including C/EBP, ATF2, PEA3/Ets, c-myc and AP-1 binding sites. Transcriptionally active MMP-2 in invasive cancer cells is characterized by hypomethylation of CpG regions in the MMP2 promoter and low levels of histone H3 lysine-27 trimethylation
MMP-2 expression analysis in embryonic tissues of wild-type and caireticulin-deficient mice, overview
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MMP-2 expression analysis in SK-Hep1 hepatoma cells, overview
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MMP-2 gene cloning from the body wall of sea cucumber, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged MMP-2(111-461) comprising the catalytic domain in Escherichia coli strain BL21(DE3) in inclusion bodies
pro-gelatinase A in transfected mammalian cell lines
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pro-MMP-2 expressed in a recombinant vaccinia virus mammalian cell expression system
recombinant enzyme from HeLa S3 cells infected with vaccinia virus encoding the full-length cDNA of pro-MMP-2
recombinant expression of soluble and functional full-length enzyme from plasmid pET5a-MMP-2 in the cytoplasm of Escherichia coli strain BL21(DE3)/pLysS, subcloning in Escherichia coli strain DH5alpha, method development and evaluation, overview
recombinant expression of wild-type and mutant full-length MMP-2 or MMP-2 with C-terminal Myc and His tags in COS-1 cells, secretion of the enzyme to the cell culture medium
recombinant proMMP-2 expressed in Sf9 cells
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second fibronectin type II module, residues 278-336, produced in Escherichia coli
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truncated MMP-2 catalytic domain MMP-2C
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gene MMP2, sequence comparisons, enzyme expression analysis
gene MMP2, sequence comparisons, enzyme expression analysis
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