Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP - Wikidata - awgldk - TriplyDB

Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP

Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP

http://www.wikidata.org/entity/Q35191039

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Targeting MT1-MMP as an ImmunoPET-Based Strategy for Imaging Gliomas The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain: CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTIONS Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis.Phthalimide neovascular factor 1 (PNF1) modulates MT1-MMP activity in human microvascular endothelial cells.Discoidin domain receptor 2 mediates collagen-induced activation of membrane-type 1 matrix metalloproteinase in human fibroblasts.Progress in matrix metalloproteinase research.Novel MT1-MMP small-molecule inhibitors based on insights into hemopexin domain function in tumor growth Establishment and validation of computational model for MT1-MMP dependent ECM degradation and intervention strategies High threshold of β1 integrin inhibition required to block collagen I-induced membrane type-1 matrix metalloproteinase (MT1-MMP) activation of matrix metalloproteinase 2 (MMP-2)Localizing matrix metalloproteinase activities in the pericellular environment.TACE activation by MAPK-mediated regulation of cell surface dimerization and TIMP3 association.Inhibition of matrix metalloproteinase 14 (MMP-14)-mediated cancer cell migration.The interface between catalytic and hemopexin domains in matrix metalloproteinase-1 conceals a collagen binding exosite.Expression of matrix metalloproteinases in bovine luteal cells induced by prostaglandin F2α, interferon γ and tumor necrosis factor α.Genomic profile of matrix and vasculature remodeling in TGF-alpha induced pulmonary fibrosis Defining requirements for collagenase cleavage in collagen type III using a bacterial collagen system.Highly sensitive and adaptable fluorescence-quenched pair discloses the substrate specificity profiles in diverse protease families.Peripheral membrane associations of matrix metalloproteinases.A Disintegrin and Metalloproteinase with Thrombospondin Motifs-5 (ADAMTS-5) Forms Catalytically Active Oligomers A matrix metalloproteinase-9 activation cascade by hepatic stellate cells in trans-differentiation in the three-dimensional extracellular matrix.The inactive 44-kDa processed form of membrane type 1 matrix metalloproteinase (MT1-MMP) enhances proteolytic activity via regulation of endocytosis of active MT1-MMP.Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase.Membrane type 1-matrix metalloproteinase: substrate diversity in pericellular proteolysis.Non-destructive and selective imaging of the functionally active, pro-invasive membrane type-1 matrix metalloproteinase (MT1-MMP) enzyme in cancer cells Development of a specific affinity-matured exosite inhibitor to MT1-MMP that efficiently inhibits tumor cell invasion in vitro and metastasis in vivo Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity.Monitoring and Inhibiting MT1-MMP during Cancer Initiation and Progression.Temporal and spatial expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases following myocardial infarction.Matrix metalloproteinase collagenolysis in health and disease.Matrix Metalloproteinase 14 promotes lung cancer by cleavage of Heparin-Binding EGF-like Growth Factor.Miniaturized antibodies for imaging membrane type-1 matrix metalloproteinase in cancers.Dimerization of MT1-MMP during cellular invasion detected by fluorescence resonance energy transfer.The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface.Posttranslational regulation of membrane type 1-matrix metalloproteinase (MT1-MMP) in mouse PTEN null prostate cancer cells: Enhanced surface expression and differential O-glycosylation of MT1-MMP Dimerization of endogenous MT1-MMP is a regulatory step in the activation of the 72-kDa gelatinase MMP-2 on fibroblasts and fibrosarcoma cells.Transient collagen triple helix binding to a key metalloproteinase in invasion and development.Basal localization of MT1-MMP is essential for epithelial cell morphogenesis in 3D collagen matrix.Membrane type 1 matrix metalloproteinase is a crucial promoter of synovial invasion in human rheumatoid arthritis.MT-LOOP-dependent localization of membrane type I matrix metalloproteinase (MT1-MMP) to the cell adhesion complexes promotes cancer cell invasion.

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P2860

Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP

http://www.wikidata.org/entity/Q35191039

description

2006 nî lūn-bûn

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2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

@zh-hk

2006年論文

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2006年論文

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2006年论文

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name

Cell surface collagenolysis re ...... rane-bound collagenase MT1-MMP

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Cell surface collagenolysis re ...... rane-bound collagenase MT1-MMP

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Cell surface collagenolysis re ...... rane-bound collagenase MT1-MMP

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Cell surface collagenolysis re ...... rane-bound collagenase MT1-MMP

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Cell surface collagenolysis re ...... rane-bound collagenase MT1-MMP

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Cell surface collagenolysis re ...... rane-bound collagenase MT1-MMP

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MBC.E06-08-0740

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Molecular Biology of the Cell

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Cell surface collagenolysis re ...... rane-bound collagenase MT1-MMP

@en

P2093

Hideaki Nagase

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Motoharu Seiki

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Noriko Ito

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Richard D Evans

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Sarah A Bird

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Yoshifumi Itoh

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P2860

A matrix metalloproteinase expressed on the surface of invasive tumour cells

The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity

Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion.

Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme

Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases

Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis

Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry

How matrix metalloproteinases regulate cell behavior

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5390-5399

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scholarly article

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10.1091/MBC.E06-08-0740

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12

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17

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2006-10-18T00:00:00Z

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17050733

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1679699

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