(Q28258413)

English

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)

scientific article published in January 1998

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scholarly article

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8 November 2019

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) (English)

1 reference

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8 November 2019

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8 November 2019

author name string

S Zucker

1

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8 November 2019

M Drews

2

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8 November 2019

C Conner

3

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8 November 2019

H D Foda

4

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8 November 2019

K E Langley

6

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8 November 2019

W F Bahou

7

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8 November 2019

A J Docherty

8

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8 November 2019

J Cao

9

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publication date

1 January 1998

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8 November 2019

Journal of Biological Chemistry

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8 November 2019

273

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8 November 2019

1216-1222

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8 November 2019

2

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8 November 2019

Regulation of matrix metalloproteinase expression in human vein and microvascular endothelial cells. Effects of tumour necrosis factor alpha, interleukin 1 and phorbol ester

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

21 January 2018

Type IV collagenase(s) and TIMPs modulate endothelial cell morphogenesis in vitro.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

21 January 2018

Matrix metalloproteinases: a review

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

21 January 2018

The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

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.273.2.1216

21 January 2018

A matrix metalloproteinase expressed on the surface of invasive tumour cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

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.273.2.1216

21 January 2018

Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

21 January 2018

Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

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.273.2.1216

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.273.2.1216

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.273.2.1216

21 January 2018

The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

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.273.2.1216

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.273.2.1216

21 January 2018

Eps15 is constitutively oligomerized due to homophilic interaction of its coiled-coil region

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

21 January 2018

Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

21 January 2018

The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

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.273.2.1216

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.273.2.1216

21 January 2018

Membrane proteases in focus

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.1216

21 January 2018

Identifiers

10.1074/JBC.273.2.1216

2 references

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9422789%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2 references

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9422789%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

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