(Q77696604)

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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

scientific article published on 01 December 1998

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9856998%20AND%20SRC:MED&resulttype=core&format=json

7 December 2019

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 (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9856998%20AND%20SRC:MED&resulttype=core&format=json

7 December 2019

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J Cao

1

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7 December 2019

M Drews

2

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7 December 2019

H M Lee

3

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7 December 2019

C Conner

4

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7 December 2019

W F Bahou

5

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7 December 2019

S Zucker

6

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7 December 2019

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1 December 1998

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7 December 2019

Journal of Biological Chemistry

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7 December 2019

273

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7 December 2019

52

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7 December 2019

34745-34752

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7 December 2019

Matrix metalloproteinases: a review

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Structural features of a superfamily of zinc-endopeptidases: the metzincins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

A matrix metalloproteinase expressed on the surface of invasive tumour cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP)

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

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)

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Membrane type matrix metalloproteinase 1 activates pro-gelatinase A without furin cleavage of the N-terminal domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Cloning and developmental expression of a membrane-type matrix metalloproteinase from chicken.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

An internal cysteine plays a role in the maintenance of the latency of human fibroblast collagenase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Metal and pH dependence of heptapeptide catalysis by human matrilysin.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Three-dimensional type I collagen lattices induce coordinate expression of matrix metalloproteinases MT1-MMP and MMP-2 in microvascular endothelial cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Thrombin induces the activation of progelatinase A in vascular endothelial cells. Physiologic regulation of angiogenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

The C-terminal domain of tissue inhibitor of metalloproteinases-2 is required for cell binding but not for antimetalloproteinase activity.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Disruption of the cysteine-75 and zinc ion coordination is not sufficient to activate the precursor of human matrix metalloproteinase 3 (stromelysin 1).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Activation of progelatinase A and progelatinase A/TIMP-2 complex by membrane type 2-matrix metalloproteinase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

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.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Cell surface binding of TIMP-2 and pro-MMP-2/TIMP-2 complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.52.34745

21 January 2018

Identifiers

10.1074/JBC.273.52.34745

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9856998%20AND%20SRC:MED&resulttype=core&format=json

7 December 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9856998%20AND%20SRC:MED&resulttype=core&format=json

7 December 2019

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