About: Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific journal article

Attributes	Values
rdf:type	Item
description	artículu científicu espublizáu en 1996 (ast) vědecký článek publikovaný v roce 1996 (cs) 1996 թվականի ապրիլին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована у квітні 1996 (uk) 1996 թուականի Ապրիլին հրատարակուած գիտական յօդուած (hyw) article publié dans la revue scientifique Journal of Biological Chemistry (fr) wetenschappelijk artikel (gepubliceerd op 1996/04/12) (nl) vedecký článok (publikovaný 1996/04/12) (sk) مقالة علمية (نشرت في 12-4-1996) (ar) scientific journal article (en) im April 1996 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28618997-995BAB38-A2BB-4C23-8575-C3E4662F03FB
publication date	1996-04-12 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28618997-DF61F847-70D9-4A3E-97F8-9C3A2913FB78
language of work or name	English
author name string	wds:Q28618997-3204427B-B192-4E84-9AB3-7107D5B7E4C5 wds:Q28618997-E924C034-134D-4DF2-AC87-C5977A40A73F
OpenCitations bibliographic resource ID	wds:Q28618997-976A9E77-FE25-49DD-A8B3-3DF84A9203EC
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1272881
author name string	S. J. Weiss D. Pei
OpenCitations bibliographic resource ID	1272881
rdfs:label	Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (en) Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (nl) Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (ast)
skos:prefLabel	Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (en) Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (nl) Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (ast)
name	Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (en) Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (nl) Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (ast)
title	wds:Q28618997-B9C737BA-8FB3-4EAC-B0B2-A1C0D3CE2A93
title	Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity (en)
page(s)	wds:Q28618997-0EE7E580-A1AC-447D-82E9-C15DA3AEB1F2
page(s)	9135–9140
instance of	wds:Q28618997-AEC7C0EA-8457-45E1-BB30-F3EAFD4F241D
instance of	scholarly article
main subject	wds:Q28618997-10A4AB8A-2A6D-4FDE-817B-B49D530B3773
main subject	transmembrane protein
PubMed ID	wds:Q28618997-EF531FC6-F1FC-4061-AA6C-CCEDB3BB2B13
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8621565
PubMed ID	8621565
published in	wds:Q28618997-06807254-3DDD-43A6-8AB9-C092C1E8DA68
published in	Journal of Biological Chemistry
issue	wds:Q28618997-1068A74F-F3D4-45F2-8F8E-8F9B170DA52E
volume	wds:Q28618997-80B3391F-D4EC-4D07-B3A7-278C3E482D28
issue	15
volume	271
DOI	wds:Q28618997-B1D12F4C-68FD-4AC7-BF87-DA45A521956A
DOI	http://dx.doi.org/10.1074/JBC.271.15.9135
DOI	10.1074/JBC.271.15.9135
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28618997
is cites work of	Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway Proteolysis and cell migration: creating a path? Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3. Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion Sequence-specific silencing of MT1-MMP expression suppresses tumor cell migration and invasion: importance of MT1-MMP as a therapeutic target for invasive tumors A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities Membrane type-1 matrix metalloprotease and stromelysin-3 cleave more efficiently synthetic substrates containing unusual amino acids in their P1' positions Morbillivirus infection of the mouse central nervous system induces region-specific upregulation of MMPs and TIMPs correlated to inflammatory cytokine expression Myocardial remodelling and matrix metalloproteinases in heart failure: turmoil within the interstitium Matrix metalloproteinases as stromal effectors of human carcinoma progression: therapeutic implications Matrix metalloproteinases in remodeling of the normal and neoplastic mammary gland Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface Roles of the matrix metalloproteinases in mammary gland development and cancer Hepatoprotective effect of MMP-19 deficiency in a mouse model of chronic liver fibrosis Localization of matrix metalloproteinase 2 within the aneurysmal and normal aortic wall Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2. The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis The involvement of the fibronectin type II-like modules of human gelatinase A in cell surface localization and activation. Membrane-type 1 matrix metalloproteinase is required for normal alveolar development. Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins Reactive site-modified tissue inhibitor of metalloproteinases-2 inhibits the cell-mediated activation of progelatinase A. Activation of matrix-metalloproteinase-2 and membrane-type-1-matrix-metalloproteinase in endothelial cells and induction of vascular permeability in vivo by human immunodeficiency virus-1 Tat protein and basic fibroblast growth factor Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage Local overexpression of TIMP-1 prevents aortic aneurysm degeneration and rupture in a rat model CA-MMP: a matrix metalloproteinase with a novel cysteine array, but without the classic cysteine switch. Matrix metalloproteinases in lung: multiple, multifarious, and multifaceted Human breast cancer cell-mediated bone collagen degradation requires plasminogen activation and matrix metalloproteinase activity Membrane type 1 matrix metalloproteinase and gelatinase A synergistically degrade type 1 collagen in a cell model Membrane-type 1 matrix metalloprotease (MT1-MMP) enables invasive migration of glioma cells in central nervous system white matter Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites Relating matrix metalloproteinase structure to function: why the "hemopexin" domain? Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage. MT1-MMP correlates with MMP-2 activation potential seen after epithelial to mesenchymal transition in human breast carcinoma cells. S100A4 regulates membrane induced activation of matrix metalloproteinase-2 in osteosarcoma cells Membrane-type matrix metalloproteinases (MT-MMPs): expression and function during glioma invasion The influence of MMP-14, TIMP-2 and MMP-2 expression on breast cancer prognosis Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration Membrane type 1-matrix metalloproteinase induces endothelial cell morphogenic differentiation by a caspase-dependent mechanism Inhibited Angiogenesis in Aging: A Role for TIMP-2 Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion. Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2. Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion The propeptide domain of membrane type 1 matrix metalloproteinase is required for binding of tissue inhibitor of metalloproteinases and for activation of pro-gelatinase A Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 190 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software