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(7-methoxy-coumarin-4-yl)acetyl-PLGL-beta-(2,4-dinitrophenylamino)-AAR-NH2 + H2O
(7-methoxy-coumarin-4-yl)acetyl-PL + GL-beta-(2,4-dinitrophenylamino)-AAR-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-beta-(2,4-dinitrophenylamino)Ala-Ala-Arg-NH2 + H2O
?
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2 + H2O
?
-
-
?
2,4-dinitrophenyl-Pro-beta-cyclohexylalanyl-Gly-Cys(Me)-His-Ala-Lys(N-Me-2-aminobenzoyl)-NH2 + H2O
?
-
a quenched fluorogenic substrate
-
-
?
2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Leu-Trp-Ala-D-Arg-NH2
-
and peptide substrates derived from, utility of substrate mapping form examining the subsite specificities and the optimization of proteinase substrates
-
?
60 S ribosomal protein L6 + H2O
?
-
-
-
-
?
65000 MW form of vitronectin + H2O
?
-
-
-
-
?
Ac-L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-NH2 + H2O
?
-
-
-
-
?
ADAM 2 + H2O
?
-
putative protein substrate with potential cleavage site
-
?
Aggrecan core protein + H2O
?
-
-
-
-
?
alpha 1(I) collagen + H2O
?
-
-
-
?
alpha 1(V) collagen + H2O
?
-
-
-
?
alpha 1(XI) collagen + H2O
?
-
-
-
?
alpha 2(V) collagen + H2O
?
-
-
-
?
alpha-amylase precursor + H2O
?
-
-
-
-
?
alpha-enolase + H2O
?
-
-
-
-
?
alpha-N-acetylglucosaminidase + H2O
?
-
-
-
-
?
amyloid protein precursor + H2O
?
-
-
-
-
?
amyloid-beta A4 protein precursor + H2O
?
-
-
-
-
?
annexin I + H2O
?
-
-
-
-
?
Arp2/3 complex subunit + H2O
?
-
-
-
-
?
arylsulfatase B precursor + H2O
?
-
-
-
-
?
beta-glucuronidase precursor + H2O
?
-
-
-
-
?
beta-hexosaminidase beta chain precursor + H2O
?
-
-
-
-
?
beta1-integrin + H2O
?
-
-
-
-
?
beta2 integrin subunit CD18 + H2O
?
-
-
-
-
?
betaB1 crystallin + H2O
?
-
main enzyme substrate in lens extract
-
-
?
Cartilage link protein + H2O
?
-
-
-
?
cathepsin E precursor + H2O
?
-
-
-
-
?
CB3 alpha 1(IV) collagen + H2O
?
-
-
-
?
CD25 + H2O
?
-
CD25 is proteolytic cleaved to its soluble form by MMP-9
-
-
?
CD316 antigen + H2O
?
-
-
-
-
?
chondroitin sulfate proteoglycan + H2O
?
-
-
-
-
?
citrate synthase + H2O
?
-
-
-
-
?
collagen I + H2O
?
-
-
-
-
?
collagen type II + H2O
?
-
-
-
-
?
Collagen type III + H2O
?
collagen type VII + H2O
?
-
-
-
-
?
collagen type XI + H2O
?
-
-
-
-
?
dentin sialoprotein + H2O
?
the enzyme highly efficiently cleaves dentin sialoprotein into distinct fragments in vitro, and the deletion of Mmp9 causes improper processing of dentin sialoprotein in natural teeth
-
-
?
desmoglein 3 + H2O
?
-
putative protein substrate with potential cleavage site
-
?
DGRNIYNIHVEDSLECVKGPNVAA + H2O
?
-
-
-
-
?
DNP-Pro-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2 + H2O
DNP-Pro-cyclohexyl-Ala-Gly + Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2
-
-
-
?
ECVKGPNVAAIVGGT + H2O
ECVKGPNVAA + IVGGT
-
-
-
-
?
endoglin + H2O
?
-
putative protein substrate with potential cleavage site
-
?
endothilin receptor + H2O
?
-
putative protein substrate with potential cleavage site
-
?
epidermal growth factor + H2O
?
epididymis-specific alpha-mannosidase precursor + H2O
?
-
-
-
-
?
fibrillar collagen + H2O
?
filamin B + H2O
?
-
-
-
-
?
fragments of human collagen type II + H2O
?
-
fragments obtained by cleavage with collagenases MMP-1, MMP-8, or MMP-13. Enzyme produces small remnant peptides with still intact immunodominant epitopes
-
-
?
galectin 3 + H2O
?
-
-
-
?
gelsolin + H2O
?
-
-
-
-
?
Golgi apparatus protein 1 precursor + H2O
?
-
-
-
-
?
heat shock protein 27 + H2O
?
-
-
-
-
?
heat shock protein 70 + H2O
?
-
-
-
-
?
heat shock protein 90 + H2O
?
-
-
-
-
?
histidyl-tRNA synthetase + H2O
?
-
-
-
-
?
HMGB1 protein + H2O
?
-
-
-
-
?
integrin beta5 + H2O
?
-
putative protein substrate with potential cleavage site
-
?
interleukin-1beta + H2O
?
-
-
-
-
?
islet amyloid polypeptide + H2O
?
kallikrein + H2O
?
-
putative protein substrate with potential cleavage site
-
?
L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-NH2 + H2O
?
-
-
-
-
?
ladinin 1 + H2O
?
-
putative protein substrate with potential cleavage site
-
?
laminin alpha3 chain + H2O
?
-
putative protein substrate with potential cleavage site
-
?
lipase A + H2O
?
-
-
-
-
?
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
?
-
-
-
?
myelin basic protein + H2O
?
-
-
-
?
N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-7-methoxycoumarin-4-yl acetyl + H2O
?
-
-
-
?
N-acetylglucosamine-6-sulfatase precursor + H2O
?
-
-
-
-
?
N-alpha-benzoyl-arginine p-nitroanilide + H2O
N-alpha-benzoyl-Arg + 4-nitroaniline
-
i.e. BAPNA
-
-
?
N-cadherin + H2O
?
-
-
-
-
?
Neonatal human proteoglycan + H2O
?
-
poor substrate, cleavage of the His16-Ile17 bond
-
-
?
nonmuscular actin + H2O
?
-
-
-
?
nucleolin + H2O
?
-
-
-
-
?
occludin + H2O
?
-
-
-
-
?
pancreatic alpha-amylase isozyme + H2O
?
-
-
-
-
?
peptide A13 + H2O
?
-
-
-
?
peptide A13R + H2O
?
-
-
-
?
peptide A3 + H2O
?
-
-
-
?
peptide A34 + H2O
?
-
-
-
?
peptide B74 + H2O
?
-
-
-
?
peptide C15 + H2O
?
-
non-selective peptide substrate
-
?
peptide C9 + H2O
?
-
-
-
?
peptide m1A11 + H2O
?
-
non-selective peptide substrate
-
?
peroxiredoxin 4 + H2O
?
-
-
-
-
?
phosphate regulating neutral endopeptidase + H2O
?
-
putative protein substrate with potential cleavage site
-
?
platelet factor 4 precursor + H2O
?
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
Proteoglycan + H2O
?
-
-
-
-
?
retinoic acid early inducible protein 1 alpha-precursor + H2O
?
-
-
-
-
?
retinoid-inducible serine carboxypeptidase precursor + H2O
?
-
-
-
-
?
SGFGSRYLTA + H2O
?
-
-
-
?
SGKGPRQITA + H2O
?
-
-
-
?
SGKIPRRLTA + H2O
?
-
-
-
?
SGKIPRTATA + H2O
?
-
-
-
?
SGKIPRTLTA + H2O
?
-
-
-
?
SGLKALMITA + H2O
?
-
-
-
-
?
SGLKAMITA + H2O
?
-
-
-
?
SGLPAKSTA + H2O
?
-
-
-
?
SGLRPAKSTA + H2O
?
-
-
-
-
?
SGPLFYSVTA + H2O
?
-
-
-
?
SGPRAVSTTA + H2O
?
-
-
-
?
SGQPHYLTTA + H2O
?
-
-
-
?
snRNP D3 + H2O
?
-
-
-
-
?
stathmin + H2O
?
-
-
-
-
?
stromelysin 1 + H2O
?
-
-
?
stromelysin1 + H2O
?
-
-
-
?
succinylated gelatin + H2O
?
-
-
-
-
?
tissue factor pathway inhibitor + H2O
?
-
-
-
?
transforming growth factor-beta + H2O
?
-
MMP9 mediates activation of latent transforming growth factor-beta
-
-
?
tubulin + H2O
?
-
-
-
-
?
Type IV collagen + H2O
?
-
-
-
-
?
type V collagen + H2O
?
-
-
-
-
?
type XI collagen + H2O
?
-
-
-
-
?
vascular endothelial-cadherin + H2O
?
-
-
-
?
Vitronectin + H2O
?
-
65000 MW and 75000 MW form of vitronectin
-
-
?
vitronectin of MW 65000 + H2O
?
-
-
-
-
?
vitronectin of MW 75000 + H2O
?
-
-
-
-
?
additional information
?
-
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-beta-(2,4-dinitrophenylamino)Ala-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-beta-(2,4-dinitrophenylamino)Ala-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
type IV
-
-
?
Collagen + H2O
?
-
type I, not native
-
-
?
Collagen + H2O
?
-
type I (denatured)
-
-
?
Collagen + H2O
?
-
type IV (native)
-
-
?
Collagen + H2O
?
-
cleavage of the carboxyl-terminal triple helix-containing region
-
-
?
Collagen + H2O
?
-
type I, binding, no cleavage
-
-
?
Collagen + H2O
?
-
type V (native)
-
-
?
Collagen + H2O
?
-
type XIV
-
-
?
Collagen + H2O
?
-
MMP-9 inhibits collagen-induced platelet aggregation
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
type V
-
-
?
Collagen + H2O
?
-
cleaves between residues Gly439-Val in both alpha1(V) and alpha(XI) and between residues Gly445-Leu in the alpha2(V) chain
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen type I + H2O
?
-
-
-
-
?
Collagen type I + H2O
?
-
soluble, native collagen type I, zymography
-
-
?
Collagen type I + H2O
?
-
-
-
-
?
Collagen type III + H2O
?
-
-
-
-
?
Collagen type III + H2O
?
-
MMP-9 cleaves native, triple helical type III collagen to generate a 3/4 fragment, zymography
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
collagen zymography
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type V + H2O
?
-
-
-
-
?
collagen type V + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
MMP-9 activity leads to elastin breakdown in an animal model of Kawasaki disease, a multisystem vasculitis leading to damage in the coronary circulationand aneurysm formation, overview
-
-
?
epidermal growth factor + H2O
?
-
-
-
-
?
epidermal growth factor + H2O
?
-
MMP-9 induces TGF-beta1 production in the airway epithelium through the cleavage of epidermal growth factor, EGF, and membrane-bound EGF-like ligands and activating epidermal growth factor receptor
-
-
?
fibrillar collagen + H2O
?
-
degradation
-
-
?
fibrillar collagen + H2O
?
-
degradation, MMP-9 is involved in development of osteoarthritis, overview
-
-
?
fibrillar collagen + H2O
?
-
degradation, cleavage within the triple helix
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Galectin-3 + H2O
?
-
-
-
-
?
Galectin-3 + H2O
?
-
a galactoside-binding protein, major cleavage site is the Ala62-Tyr63 bond
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography, mass spectrometrical analysis, overview
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
Gallus gallus Hy-Line Brown
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
683170, 683233, 683579, 683710, 683749, 683844, 683881, 684107, 695947, 696980, 697383, 699222, 699345, 699642, 699656, 699946, 700530, 702513, 707123, 707366, 707452, 707631, 707654, 707953, 707964, 707978, 708020, 708070, 708086, 708088, 708089, 708171, 708245, 708409, 708548, 708773, 708775, 708810, 708828, 709051, 709277, 709288, 709301, 709302, 709413, 709700, 709811, 710077, 710174, 710225, 710245, 710452, 710531, 710587, 717898, 717980, 718385 -
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
MMP-9 is involved in the degradation of the extracellular matrix, and is implicated in a variety of pathological conditions including cardiovascular and neoplastic diseases
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
gelatin zymography
-
-
?
Gelatin + H2O
?
-
gelatin zymography using gelatin and fluorescence-conjugated gelatin peptides
-
-
?
Gelatin + H2O
?
-
gelatin zymography, from porcine skin
-
-
?
Gelatin + H2O
?
-
-
683055, 683111, 683480, 683555, 683733, 683816, 696037, 696751, 699477, 707062, 707298, 707302, 707451, 707928, 708024, 708188, 708547, 708548, 708690, 708695, 708703, 708740, 708746, 709178, 709239, 709249, 709382, 709650, 709680, 709734, 709787, 709791, 709904, 710065, 710067, 710102, 717577, 718355 -
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
gelatin zymography, gelatin from porcine skin
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography, gelatin from porcine skin
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
683051, 683412, 683427, 683874, 700147, 701422, 708304, 709595, 709614, 709646, 709682, 709920, 709948, 710106, 710575, 710585, 710695 -
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
zymographic analysis
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
islet amyloid polypeptide + H2O
?
enzyme MMP-9 degrades amyloidogenic humanislet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
-
-
?
islet amyloid polypeptide + H2O
?
enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
-
-
?
islet amyloid polypeptide + H2O
?
enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
-
-
?
Laminin + H2O
?
-
degradation
-
-
?
Laminin + H2O
?
-
degradation
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
-
-
-
?
additional information
?
-
-
active host MMP-9 is expressed in walls and fluids of hydatid cysts of parasite Echinococcus granulosus in the environment of granulomatous reaction, in vivo activation of MMP-9 suggests its involvement in inflammatory reaction and in the chemotaxis of inflammatory cells to the cyst. However, the parasite can deal efficiently with MMP-9, overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
prefers hydrophobic aliphatic residues in subsite P1'
-
-
?
additional information
?
-
-
Asp432, Asp433, and His400 residues are important for the activity of gelatinase B, His400 may act as a zinc-binding ligand, Asp432 and Asp433 are probably involved in stabilization of the active site of the enzyme
-
-
?
additional information
?
-
-
tolerates only small amino acids such as Gly and Ala in P1
-
-
?
additional information
?
-
-
may be responsible for the pathological degradation and/or normal turnover of vitronectin
-
-
?
additional information
?
-
-
possible role of the enzyme in the structural tissue remodeling of the developing embryo
-
-
?
additional information
?
-
-
plays a role in tumor cell invasion and in destruction of cartilage in arthritis
-
-
?
additional information
?
-
-
enzyme may play a role in the destruction of the extracellular matrix, perhaps acting in concert with the metalloproteases produced by activated endothelial cells
-
-
?
additional information
?
-
associated with degradation of the extracellular matrix in normal and pathological conditions
-
?
additional information
?
-
-
central role in the degradation of the extracellular matrix
-
?
additional information
?
-
-
leading role in the catabolism of the macromolecular components of the extracellular matrix in a variety of normal and pathological processes, involved in inflammation, tissue remodeling and cancer
-
?
additional information
?
-
-
cells resistant to protein kinase C potentiated, transkription factor p53 mediated apoptosis express a higher level of matrix metalloproteinases MMP-9 and MMP-10. Matrix metalloproteinases function confers protection from protein kinase C/p53 induced apoptosis and are implicated in tumor cell resistance
-
-
?
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
?
-
-
enzyme and leucocyte elastase are essential for granulocyte-mediated proteolysis resulting in dermal-epidermal separation in epidermolysis bullosa acquisita and bullous pemphigoid patients skin
-
-
?
additional information
?
-
-
no substrate: L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala(CH3)-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-CONH2
-
-
?
additional information
?
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activated MMP-9 initially induces conformational changes in platelet membranes, affecting membrane fluidity, and hydroxyl radical formation and inhibits the Na+/H+ pump, both leading to inhibition of platelet aggregation, the latter via reduced Ca2+ mobilization, overview. MMP-9 also inhibits arachidonic acid, ADP, and U46619 inducetion of platelet aggregation, overview
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activation of MMP-9 may contribute to dentin matrix degradation, which occurs during caries progression and follows resin bonding. Inhibition of MMP-9 proteolytic activity may slow caries progression and increase the durability of resin-dentin bond, overview
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gelatinase B expression is a prognostic factor in patients with stage II/III rectal carcinoma treated by postoperative adjuvant therapy, overview
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MMP-9 activity is associated with poor prognosis in T3-T4 node-negative colorectal cancer, its expression is not correlated with MMP-2 and reversion-inducing cysteine-rich protein, RECK, expression in cancer cells, overview
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MMP-9 expression is increased in cancers, inhibition of MMP-9 has a therapeutic benefit to cancer
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MMP-9 is activated by monomeric hemin and by MMP-3 cleaving at Glu40-Met41 and Arg87-Phe88, and at Glu40-Met41 and Leu52-Leu53, respectively, no effect by hemoglobin, overview
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MMP-9 is involved in development of endometriosis, MMP-9 levels are decreased by about 50% after operation of endometriosis, overview
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MMP-9 is secreted by macrophages at wound sites and is involved in wound repair together with relaxin, molecular mechanism, overview. Transcription factor NF-kappaB is important in MMP gene regulation in macrophage cells, overview, relaxin-induced tissue remodeling through increasing MMP-9 expression is dependent on NF-kappaB activation
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the enzyme is involved in breakdown of extracellular matrix components, and basement membrane disruption, stroma and blood vessel penetration, and metastasis. It participates in tumor growth and angiogensis, overview
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varied enzyme conformations and in facilitating independent movements of the terminal domains may endorse recognition, binding, and processing of substrates, ligands, as well as receptors and marks this domain as an additional target for the design of selective regulators, overview
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the enzyme cleaves many substrates
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4-aminophenylmercuric acetate activation induces an autoproteolytic activation of the enzyme zymogen causing the removal of the propeptide followed by a further breakage and subsequent formation of a N- and C-truncated form of 67 kDa
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enzyme activity is determined using human teeth as substrate
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peptide A16 SGRR LLSRTA and peptide C11 SGRR LIHHTA are no substrates
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acrolein subtypes A and C from cigarette smoke induces persistent mucin production via activation of matrix metalloproteinase 9 through induction of pro-MMP-9 cleavage and activation and EGFR/MAPK signaling also leading to MMP-9 activation, regulation, overview
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gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
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MMP-9 activity plays a central role in modulating the clinical course and severity of respiratory tularemia, Pro-Gly-Pro, a potent neutrophil chemotactic tripeptide, is released from extracellular matrix through the action of MMP-9, MMP-9 is involved in leukocyte recruitment, pulmonary infection with the Gram-negative intracellular bacterium Francisella tularensis, a category A biological threat agent, induces MMP-9 expression, MMP-9 is associated with higher bacterial burdens in pulmonary and extrapulmonary tissues, development of more extensive histopathology predominated by neutrophils, and increased morbidity and mortality compared to mice lacking MMP-9
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MMP-9 inhibitor completely inhibits PAF-induced B16F10 metastasis
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MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
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MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
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MMP-9 plays an important role in degradation of gastric extracellular matrix proteins, MMP-9 is reduced by melatonin produced during gastric ulcer development, overview
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nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways, Sper/NO shows biphasic regulation of MMP-9 inactivated macrophages, overview
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MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
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MMP-9 plays an important role in degradation of gastric extracellular matrix proteins, MMP-9 is reduced by melatonin produced during gastric ulcer development, overview
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gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
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MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
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nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways, Sper/NO shows biphasic regulation of MMP-9 inactivated macrophages, overview
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MMP-9 activity plays a central role in modulating the clinical course and severity of respiratory tularemia, Pro-Gly-Pro, a potent neutrophil chemotactic tripeptide, is released from extracellular matrix through the action of MMP-9, MMP-9 is involved in leukocyte recruitment, pulmonary infection with the Gram-negative intracellular bacterium Francisella tularensis, a category A biological threat agent, induces MMP-9 expression, MMP-9 is associated with higher bacterial burdens in pulmonary and extrapulmonary tissues, development of more extensive histopathology predominated by neutrophils, and increased morbidity and mortality compared to mice lacking MMP-9
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enzyme may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen
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independent of its proteolytic function, enzyme has a biphasic effect on smooth muscle cell-mediated collagen gel contraction
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astrocyte-released MMP-9 is involved in interleukin-1beta induced neurotoxicity, probably via urokinase plasminogen activator, overview
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inhibition of MMP-9 prevents neutrophilic inflammation in ventilator-induced lung injury, VILI, and pulmonary hemorrhage, overview
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myogenic reactivity, inhibited in small renal arteries isolated from nonpregnant rats treated with recombinant human relaxin, is completely restored by incubation with MMP-9, MMP-9 rather than MMP-2 plays a central role in the vasodilatory effect of short-term relaxin administration, overview
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