3.4.24.24: gelatinase A
This is an abbreviated version!
For detailed information about gelatinase A, go to the full flat file.
Word Map on EC 3.4.24.24
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3.4.24.24
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mmp-9
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metalloproteinases
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zymography
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metastasis
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timp-2
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endothelial
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angiogenesis
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artery
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fibrosis
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necrosis
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gelatinolytic
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invasiveness
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transwell
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basement
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tnf
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mt1-mmp
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plasminogen
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cardiac
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neutrophil
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aortic
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vessel
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integrins
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fibronectin
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upa
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melanoma
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laminin
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matrigel
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vimentin
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myocardial
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interstitial
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proteinases
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lymph
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ventricular
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e-cadherin
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nude
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angiogenic
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aneurysm
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mesenchymal
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stromelysins
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anti-metastatic
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fak
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medicine
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elastin
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cox-2
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synthesis
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urokinase
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collagenases
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urokinase-type
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collagenolytic
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tgf-beta1
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diagnostics
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lipocalin
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boyden
- 3.4.24.24
- mmp-9
- metalloproteinases
-
zymography
- metastasis
- timp-2
- endothelial
- angiogenesis
- artery
- fibrosis
- necrosis
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gelatinolytic
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invasiveness
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transwell
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basement
- tnf
- mt1-mmp
- plasminogen
- cardiac
- neutrophil
- aortic
- vessel
- integrins
- fibronectin
- upa
- melanoma
- laminin
- matrigel
- vimentin
- myocardial
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interstitial
- proteinases
- lymph
- ventricular
- e-cadherin
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nude
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angiogenic
- aneurysm
- mesenchymal
- stromelysins
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anti-metastatic
- fak
- medicine
- elastin
- cox-2
- synthesis
- urokinase
- collagenases
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urokinase-type
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collagenolytic
- tgf-beta1
- diagnostics
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lipocalin
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boyden
Reaction
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-/-Ile-Ala-Gly-Gln =
Synonyms
72 kDa Gelatinase, 72 kDa Gelatinase type A, 72 kDa type IV collagenase, 72-kDa Gelatinase, Collagenase IV, Collagenase type IV, GelA, gelatinase, gelatinase A, human gelatinase A, human matrix metalloproteinase 2, human matrix metalloproteinase-2, LvMMP-2, matrix metallopeptidase 2, matrix metalloprotease 2, Matrix metalloproteinase 2, matrix metalloproteinase-2, matrix metalloprotenase-2, metalloproteinase-2, metrix metalloproteinase-2, MMP 2, MMP-2, MMP2, progelatinase, Type IV collagen metalloproteinase, Type IV collagenase, Type IV collagenase/gelatinase
ECTree
3.4.24.24 gelatinase AAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.24 - gelatinase A
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2 + H2O
?
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a quenched fluorogenic substrate
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-
?
(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
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-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys(2,4-dinitrophenyl)-Gly + H2O
?
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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
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-
?
110000 MW cell-surface amyloid protein precursor + H2O
?
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amyloid protein precursor of Alzheimer's disease, cleavage to a 1000 MW form of the protein
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-
?
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
?
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-
-
?
Bovine fibrinogen + H2O
?
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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
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-
?
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2 + H2O
?
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-
-
?
Galectin-3 + H2O
?
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a galactoside-binding protein, major cleavage site: Ala62-Tyr63
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-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln
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-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Ser-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Ser-Gln
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-
-
?
Gly-Pro-Gln-Gly-Ile-Phe-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Phe-Gly-Gln
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-
-
?
Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Trp-Gly-Gln
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-
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?
LS276-THP + H2O
?
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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
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-
?
Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
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quenched fluorescent peptide
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?
Neonatal human proteoglycan + H2O
?
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cleavage of the His16-Ile17 bond and the Leu25-Leu26 bond
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-
?
Collagen + H2O
?
degradation of beta- and gamma-chains, weak activity with alpha-chains
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-
?
Collagen + H2O
?
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soluble triple helical type I collagen, 3/4- and 1/4-length collagen fragments are formed
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-
?
Gelatin + H2O
?
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-
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?
Gelatin + H2O
?
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gelatin zymography
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-
?
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
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-
?
additional information
?
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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
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-
?
additional information
?
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specificity: tolerates only small amino acids such as Gly and Ala in subsite P1, prefers hydrophobic, aliphatic residues in subsite P1'
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-
?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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may be responsible for the pathological degradation and/or normal turnover of vitronectin
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?
additional information
?
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constitutively expressed in human rheumatoid synovial cells
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-
?
additional information
?
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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
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-
?
additional information
?
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facilitates tmumor metastasis and angiogenesis by hydrolyzing components of the extracwllular matrix
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?
additional information
?
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facilitates tmumor metastasis and angiogenesis by hydrolyzing components of the extracwllular matrix
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?
additional information
?
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implicated in tumor cell metastasis and angiogenesis
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?
additional information
?
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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
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?
additional information
?
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plays a key role in angiogenesis and tumor metastasis
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?
additional information
?
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plays a key role in angiogenesis and tumor metastasis
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?
additional information
?
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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
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-
?
additional information
?
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collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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intervertebral disc degeneration is associated with the increased expression of several matrix metalloproteinases, in particular MMP-2, overview
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?
additional information
?
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the enzyme degrades proteins of the extracellular matrix in the uterus and might be involved in the growth of leiomyoma and corresponding myometrium, overview
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-
?
additional information
?
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TSP-1 acts in LRP-mediated clearance of MMP-2, TIMP-2 complexing leads to MMP-2 accumulation in the cells
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-
?
additional information
?
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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
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-
?
additional information
?
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the enzyme shows strong interaction with TSP-1 and CBD123, surface plasmon resonance analysis, overview
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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enzyme activity is determined using human teeth as substrate
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-
?
