The matrix metalloproteinase 9 (mmp-9) hemopexin domain is a novel gelatin binding domain and acts as an antagonist.
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Reduced amelogenin-MMP20 interactions in amelogenesis imperfectaGelatinase B/MMP-9 in Tumour Pathogenesis and ProgressionBiochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decadeTransient opening of the perineurial barrier for analgesic drug deliveryNeutrophil MMP-9 proenzyme, unencumbered by TIMP-1, undergoes efficient activation in vivo and catalytically induces angiogenesis via a basic fibroblast growth factor (FGF-2)/FGFR-2 pathway.Latent MMP-9 is bound to TIMP-1 before secretion.Alterations of glutathione S-transferase and matrix metalloproteinase-9 expressions are early events in esophageal carcinogenesis.Matrix metalloproteinase inhibition enhances the rate of nerve regeneration in vivo by promoting dedifferentiation and mitosis of supporting schwann cellsMatrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer.Elevation of hemopexin-like fragment of matrix metalloproteinase-2 tissue levels inhibits ischemic wound healing and angiogenesis.The MMP-9/TIMP-1 axis controls the status of differentiation and function of myelin-forming Schwann cells in nerve regeneration.Spinal Glia Division Contributes to Conditioning Lesion-Induced Axon Regeneration Into the Injured Spinal Cord: Potential Role of Cyclic AMP-Induced Tissue Inhibitor of Metalloproteinase-1A 17-residue sequence from the matrix metalloproteinase-9 (MMP-9) hemopexin domain binds α4β1 integrin and inhibits MMP-9-induced functions in chronic lymphocytic leukemia B cells.Inhibitory effects of antisense RNA of HAb18G/CD147 on invasion of hepatocellular carcinoma cells in vitro.MMP-9 controls Schwann cell proliferation and phenotypic remodeling via IGF-1 and ErbB receptor-mediated activation of MEK/ERK pathway.Alendronate promotes plasmin-mediated MMP-9 inactivation by exposing cryptic plasmin degradation sites within the MMP-9 catalytic domain.The hemopexin domain of MMP-9 inhibits angiogenesis and retards the growth of intracranial glioblastoma xenograft in nude mice.Protease analysis by neoepitope approach reveals the activation of MMP-9 is achieved proteolytically in a test tissue cartilage model involved in bone formation.Chlorhexidine stabilizes the adhesive interface: a 2-year in vitro studyInhibition of MMP-9-dependent Degradation of Gelatin, but Not Other MMP-9 Substrates, by the MMP-9 Hemopexin Domain Blades 1 and 4.Chronic administration of hexarelin attenuates cardiac fibrosis in the spontaneously hypertensive rat.Biochemical characterization and structure determination of a potent, selective antibody inhibitor of human MMP9.Acute- and late-phase matrix metalloproteinase (MMP)-9 activity is comparable in female and male rats after peripheral nerve injury.Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances
P2860
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P2860
The matrix metalloproteinase 9 (mmp-9) hemopexin domain is a novel gelatin binding domain and acts as an antagonist.
description
2002 nî lūn-bûn
@nan
2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
The matrix metalloproteinase 9 ...... ain and acts as an antagonist.
@ast
The matrix metalloproteinase 9 ...... ain and acts as an antagonist.
@en
type
label
The matrix metalloproteinase 9 ...... ain and acts as an antagonist.
@ast
The matrix metalloproteinase 9 ...... ain and acts as an antagonist.
@en
prefLabel
The matrix metalloproteinase 9 ...... ain and acts as an antagonist.
@ast
The matrix metalloproteinase 9 ...... ain and acts as an antagonist.
@en
P2093
P356
P1476
The matrix metalloproteinase 9 ...... ain and acts as an antagonist.
@en
P2093
Bettina Jansen
Iris Behrmann
Joachim Grötzinger
Karin Schleinkofer
Siegfried Matern
Stephan Pötsch
Thomas Kernebeck
P304
50326-50332
P356
10.1074/JBC.M207446200
P407
P577
2002-10-15T00:00:00Z