About: The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study

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description	1998 թվականի հունվարին հրատարակված գիտական հոդված (hy) 1998 թուականի Յունուարին հրատարակուած գիտական յօդուած (hyw) artículu científicu espublizáu en 1998 (ast) vědecký článek publikovaný v roce 1998 (cs) наукова стаття, опублікована в січні 1998 (uk) vedecký článok (publikovaný 1998/01/09) (sk) مقالة علمية (نشرت في 9-1-1998) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific journal article (en) im Januar 1998 veröffentlichter wissenschaftlicher Artikel (de) wetenschappelijk artikel (gepubliceerd op 1998/01/09) (nl)
publication date	wds:Q28619177-936585E0-C2E6-4156-8151-377ECCF6D844
publication date	1998-01-09 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28619177-3F01A3C0-1B30-47A3-8DA3-856D60DA3227
language of work or name	English
author name string	wds:Q28619177-0009F3F2-AB52-4B67-9616-9A64E59D8F7D wds:Q28619177-1FEF1C53-D1BA-4EBE-B3CE-A548888112F8 wds:Q28619177-216433C9-13E5-44A2-A56D-259DD09495ED wds:Q28619177-24801600-13B0-46D1-91BE-63308DC15E1C wds:Q28619177-6C54724B-2A3D-4155-8FD3-D491DFA49CA7 wds:Q28619177-736B4A86-AE75-4BF8-AAC5-939D13B6AA02 wds:Q28619177-7BAB59C6-DAF0-4C78-BE53-2ACDA67718E5 wds:Q28619177-7FAE5C3A-4484-4CF3-BC92-6196E23857F1 wds:Q28619177-DC22E2BD-E1D3-4231-9179-CD52788CF702 wds:Q28619177-E8FB37E2-8D0A-4F10-98EC-546EABEEC601
OpenCitations bibliographic resource ID	wds:Q28619177-0E43C8C7-14CD-4F70-9943-77E976AC1533
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/2078345
author name string	T. Tamura T. Crabbe M. J. Butler G. Murphy H. Will S. J. Atkinson J. Clements G. S. Butler M. P. d'Ortho S. Schade van Westrum
OpenCitations bibliographic resource ID	2078345
rdfs:label	The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (en) The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (nl) The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (ast)
skos:prefLabel	The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (en) The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (nl) The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (ast)
name	The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (en) The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (nl) The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (ast)
title	wds:Q28619177-32032FFC-3019-4EBC-A4DD-788035961B85
title	The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study (en)
page(s)	wds:Q28619177-5191A029-BB41-4BF5-A1F5-CDF7311CB30F
page(s)	871–880
instance of	wds:Q28619177-A7FE0A2F-0D6E-4AD9-B379-F6538A8724AC
instance of	scholarly article
PubMed ID	wds:Q28619177-EE0017F2-1BBF-4A47-BD10-77A226BC090C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9422744
PubMed ID	9422744
published in	wds:Q28619177-63A6E77D-E824-4B52-BADA-AE09226BF685
published in	Journal of Biological Chemistry
issue	wds:Q28619177-DAAE32AE-2604-45C8-8C44-5816787AF16C
volume	wds:Q28619177-4513D1FE-97B4-47AC-96A0-C0795949030B
issue	2
volume	273
DOI	wds:Q28619177-8C1BB0AF-35F7-4824-A542-4565240B3B76
DOI	http://dx.doi.org/10.1074/JBC.273.2.871
DOI	10.1074/JBC.273.2.871
ResearchGate publication ID	wds:Q28619177-EE9C8E24-CA35-42A9-B10C-2795A826817E
ResearchGate publication ID	13807016
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28619177
is cites work of	The cysteine-rich domain of the secreted proprotein convertases PC5A and PACE4 functions as a cell surface anchor and interacts with tissue inhibitors of metalloproteinases Proteolysis and cell migration: creating a path? Matrix metalloproteinases in tumour invasion and metastasis Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP The influence of type 2 diabetes mellitus on the expression of inflammatory mediators and tissue inhibitor of metalloproteinases-2 in human chronic periodontitis Activation and localization of matrix metalloproteinase-2 and -9 in the skeletal muscle of the muscular dystrophy dog (CXMDJ). Selective involvement of TIMP-2 in the second activational cleavage of pro-MMP-2: refinement of the pro-MMP-2 activation mechanism Dimerization of endogenous MT1-MMP is a regulatory step in the activation of the 72-kDa gelatinase MMP-2 on fibroblasts and fibrosarcoma cells TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains Is there new hope for therapeutic matrix metalloproteinase inhibition? Activation of proMMP-2 and Src by HHV8 vGPCR in human pulmonary arterial endothelial cells 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. Expression and activation of pro-gelatinase A by human melanoma cell lines with different tumorigenic potential Protein tyrosine phosphorylation in signalling pathways leading to the activation of gelatinase A: activation of gelatinase A by treatment with the protein tyrosine phosphatase inhibitor sodium orthovanadate Expression and activation of pro-MMP-2 and pro-MMP-9 during rat liver regeneration The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface Identification of novel, functional genetic variants in the human matrix metalloproteinase-2 gene: role of Sp1 in allele-specific transcriptional regulation Gelatinase activities in the airways of premature infants and development of bronchopulmonary dysplasia. Evaluation of some newer matrix metalloproteinases Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins Complex roles of tissue inhibitors of metalloproteinases in cancer 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 Membrane type 1 matrix metalloproteinase and gelatinase A synergistically degrade type 1 collagen in a cell model Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain Multiscale models of angiogenesis 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 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. Loss of MMP-2 disrupts skeletal and craniofacial development and results in decreased bone mineralization, joint erosion and defects in osteoblast and osteoclast growth Calcium‐induced activation and truncation of promatrix metalloproteinase‐9 linked to the core protein of chondroitin sulfate proteoglycans Quantitative analysis of mRNA expression of TIMPs in the periprosthetic interface tissue of loose hips by real-time PCR system

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