About: 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

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About: 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 Goto Sponge NotDistinct Permalink

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scientific article published on 01 December 1998

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 1998 (uk) article scientifique publié en 1998 (fr) im Dezember 1998 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'avientu de 1998 (ast) scientific article published on 01 December 1998 (en)
publication date	wds:Q77696604-52E78332-CF89-48EC-91FB-0CE1465A4315
publication date	1998-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q77696604-05C693FA-2DF6-4105-9B8F-51840933FDA8
language of work or name	English
cites work	wds:Q77696604-05915460-A852-469A-A67D-DD51FD49EDAD wds:Q77696604-100059EC-8BCE-4239-A315-D60A111A0EE9 wds:Q77696604-28BC4E36-F680-41C3-808D-CF5E7992A6A0 wds:Q77696604-301D8B71-8172-4B39-AD3B-BF2725DC3F8C wds:Q77696604-3E5E326D-1DAE-4FE6-9AC7-6370E683C7EE wds:Q77696604-40661F07-B6FF-4F9F-9EE3-89E393EA8C77 wds:Q77696604-4B598D72-31F2-465C-98A8-DE62A272F279 wds:Q77696604-4EBDA514-D305-4A05-A8C5-93BF99B87F15 wds:Q77696604-4FB35B60-B38F-4DDC-A9B8-293770AFF312 wds:Q77696604-5988990F-278B-4B2C-B27E-858661720A59 wds:Q77696604-61BB2A89-6636-4D3F-A035-74DCF5C3E23B wds:Q77696604-651116C8-CBCA-4990-9CC0-DB988CD6AF44 wds:Q77696604-6BA6AAEE-15CF-4D75-A9EF-0673D59B877C wds:Q77696604-72C343CC-778A-40EE-8FE8-087F1B4C1C8F wds:Q77696604-79642A1B-CD26-4CCB-B63A-7B16BBDE1354 wds:Q77696604-915F91F7-CDB2-432B-9339-83D1DAA604D4 wds:Q77696604-A095E3DB-DF15-4AC9-BF39-DFD67DF6BC27 wds:Q77696604-A84497CA-8D2C-455E-BB39-6D6A31960041 wds:Q77696604-B1E0217B-D68B-4C5E-A38E-58F88FFBD2F8 wds:Q77696604-B31C519E-E0F3-4FD2-81FF-5180C73241F0 wds:Q77696604-C7EF8BF0-AD0D-4F36-BE9F-C87E51A2F1AD wds:Q77696604-CA5BF985-9E22-4629-9750-277D0FD1A4A0 wds:Q77696604-CEF12C76-B746-406F-BF43-E98DF7FA344F wds:Q77696604-D5587126-0D59-4D7C-A369-D78346C169DC wds:Q77696604-D8802B73-99E8-4F60-A80E-553252C77FEA wds:Q77696604-DA8512BC-07E7-4713-90F3-57B8F39F2721 wds:Q77696604-E7E21727-84E1-4625-B461-6067C15306D3 wds:Q77696604-EA2474BD-9B5D-41B9-8D7C-861D8C3FB3AF wds:Q77696604-EC6BE659-26ED-49A1-BF59-4EDAF00B82BF wds:Q77696604-F84D512A-A62C-40D1-ACED-4BC7C23A0FC4
cites work	The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells Three-dimensional type I collagen lattices induce coordinate expression of matrix metalloproteinases MT1-MMP and MMP-2 in microvascular endothelial cells Site-directed mutagenesis by overlap extension using the polymerase chain reaction Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3. Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity Thrombin induces the activation of progelatinase A in vascular endothelial cells. Physiologic regulation of angiogenesis Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease Cell surface binding of TIMP-2 and pro-MMP-2/TIMP-2 complex Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family A matrix metalloproteinase expressed on the surface of invasive tumour cells The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family Matrix metalloproteinases: a review Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2 Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP) Structural features of a superfamily of zinc-endopeptidases: the metzincins Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP) The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. The C-terminal domain of tissue inhibitor of metalloproteinases-2 is required for cell binding but not for antimetalloproteinase activity. Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes Activation of progelatinase A and progelatinase A/TIMP-2 complex by membrane type 2-matrix metalloproteinase Cloning and developmental expression of a membrane-type matrix metalloproteinase from chicken. Disruption of the cysteine-75 and zinc ion coordination is not sufficient to activate the precursor of human matrix metalloproteinase 3 (stromelysin 1). Metal and pH dependence of heptapeptide catalysis by human matrilysin. Membrane type matrix metalloproteinase 1 activates pro-gelatinase A without furin cleavage of the N-terminal domain Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts An internal cysteine plays a role in the maintenance of the latency of human fibroblast collagenase. Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain
author name string	wds:Q77696604-15BAA658-095F-4ACA-AD16-BF668129C0B0 wds:Q77696604-2196C9CD-FCBC-4720-97BA-139F77DC0550 wds:Q77696604-38B34E0B-E785-490F-98F7-6BAAF2835597 wds:Q77696604-69B83377-A619-4B30-A702-375128FB4AA2 wds:Q77696604-B9C46212-62C8-48B2-96C8-EB636F16525E wds:Q77696604-E6493D1D-E4BF-4B2A-A21C-8CE099D49258
author name string	J Cao H M Lee M Drews S Zucker C Conner W F Bahou
rdfs:label	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 (en) 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 (nl)
skos:prefLabel	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 (en) 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 (nl)
name	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 (en) 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 (nl)
title	wds:Q77696604-66B985A8-3DDB-49EC-8E08-8BBE726583B9
title	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 (en)
page(s)	wds:Q77696604-2F17CB8D-E142-4D71-B6F5-19982C879793
page(s)	34745-34752
instance of	wds:Q77696604-09AB203A-D2A6-4DFF-BFC2-A97BFF235FF5
instance of	scholarly article
PubMed ID	wds:Q77696604-B03DF2DC-15FD-400F-8E58-AD7B4BD1CC56
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9856998
PubMed ID	9856998
published in	wds:Q77696604-855956B6-F0F3-40EC-815F-40E6D2605715
published in	Journal of Biological Chemistry

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