The role of ADAM 15 in glomerular mesangial cell migration. - Wikidata - wikimedia - TriplyDB

The role of ADAM 15 in glomerular mesangial cell migration.

The role of ADAM 15 in glomerular mesangial cell migration.

http://www.wikidata.org/entity/Q34136288

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Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23 ADAM15 disintegrin is associated with aggressive prostate and breast cancer disease Expression of ADAM15 in rheumatoid synovium: up-regulation by vascular endothelial growth factor and possible implications for angiogenesis The splicing and fate of ADAM33 transcripts in primary human airways fibroblasts ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers ADAM8: a new therapeutic target for asthma Selective modulation of integrin-mediated cell migration by distinct ADAM family members Proteomic analysis of S-nitrosylated proteins in mesangial cells.ADAM15 gene structure and differential alternative exon use in human tissues.ADAM33 gene polymorphisms identified to be associated with asthma in a Chinese Li population.ADAMTS and ADAM metalloproteinases in osteoarthritis - looking beyond the 'usual suspects'.ADAM15 regulates endothelial permeability and neutrophil migration via Src/ERK1/2 signalling ADAM9 is a novel product of polymorphonuclear neutrophils: regulation of expression and contributions to extracellular matrix protein degradation during acute lung injury.ADAM15 exerts an antiapoptotic effect on osteoarthritic chondrocytes via up-regulation of the X-linked inhibitor of apoptosis.Characterization of oxygen-induced retinopathy in mice carrying an inactivating point mutation in the catalytic site of ADAM15.Anchoring junctions as drug targets: role in contraceptive development.Potential role for ADAM15 in pathological neovascularization in mice.ADAM proteases, ErbB pathways and cancer.Leukocyte cell surface proteinases: regulation of expression, functions, and mechanisms of surface localization.Increased expression of ADAM33 protein in asthmatic patients as compared to non-asthmatic controls.Activin receptor signaling regulates prostatic epithelial cell adhesion and viability.Implication of ADAM-8, -9, -10, -12, -15, -17, and ADAMTS-1 in implantational remodeling of a mouse uterus.Proteolytic processing of delta-like 1 by ADAM proteases.Urinary concentrations of ADAM 12 from breast cancer patients pre- and post-surgery vs. cancer-free controls: a clinical study for biomarker validation.Matrix metalloproteinases, a disintegrin and metalloproteinases, and a disintegrin and metalloproteinases with thrombospondin motifs in non-neoplastic diseases.ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets.ADAM15 modulates outside-in signalling in chondrocyte-matrix interactions.The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation.Fine Tuning Cell Migration by a Disintegrin and Metalloproteinases.Role of ADAM-15 in wound healing and melanoma development.Critical role of ADAM15 in tumor progression: targeting multiple factors for metastasis promotion.Aberrant alternative exon use and increased copy number of human metalloprotease-disintegrin ADAM15 gene in breast cancer cells.An assessment of ADAMs in bone cells: absence of TACE activity prevents osteoclast recruitment and the formation of the marrow cavity in developing long bones.Hyaluronan induces the selective accumulation of matrix- and cell-associated proteoglycans by mesangial cells.ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase A disintegrin and metalloproteinase 15 contributes to atherosclerosis by mediating endothelial barrier dysfunction via Src family kinase activity.Inhibition of airway smooth muscle adhesion and migration by the disintegrin domain of ADAM-15.Association of ADAM33 gene polymorphisms with asthma in Indian children.Multiple non-catalytic ADAMs are novel integrin α4 ligands.Development of lupus nephritis is associated with qualitative changes in the glomerular collagen IV matrix composition.

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P2860

The role of ADAM 15 in glomerular mesangial cell migration.

http://www.wikidata.org/entity/Q34136288

description

2002 nî lūn-bûn

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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2002 թվականի հունիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

The role of ADAM 15 in glomerular mesangial cell migration.

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The role of ADAM 15 in glomerular mesangial cell migration.

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The role of ADAM 15 in glomerular mesangial cell migration.

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type

label

The role of ADAM 15 in glomerular mesangial cell migration.

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The role of ADAM 15 in glomerular mesangial cell migration.

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The role of ADAM 15 in glomerular mesangial cell migration.

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prefLabel

The role of ADAM 15 in glomerular mesangial cell migration.

@ast

The role of ADAM 15 in glomerular mesangial cell migration.

@en

The role of ADAM 15 in glomerular mesangial cell migration.

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Journal of Biological Chemistry

P1476

The role of ADAM 15 in glomerular mesangial cell migration.

@en

P2093

John D Williams

http://www.w3.org/2001/XMLSchema#string

John Martin

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Lisa V Eynstone

http://www.w3.org/2001/XMLSchema#string

Malcolm Davies

http://www.w3.org/2001/XMLSchema#string

Robert Steadman

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P2860

Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene

Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3

A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.

ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions

A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells

ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix

Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5

ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain

Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence.

A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion.

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33683-33689

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10.1074/JBC.M200988200

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37

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277

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2002-06-28T00:00:00Z

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12091380

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