(Q52524228)

English

The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding. Binding properties of recombinant gelatinase A C domain to extracellular matrix and basement membrane componen

scientific article published in March 1997

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding. Binding properties of recombinant gelatinase A C domain to extracellular matrix and basement membrane componen (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

1 reference

based on heuristic

inferred from title

author name string

Wallon UM

1

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

Overall CM

2

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

language of work or name

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publication date

1 March 1997

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

272

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

11

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

7473-7481

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

The matrix-degrading metalloproteinases

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Evidence for the involvement of type II domains in collagen binding by 72 kDa type IV procollagenase

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Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen

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The collagenase gene family in humans consists of at least four members

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Crystal structure of the haemopexin-like C-terminal domain of gelatinase A

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The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function

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21 January 2018

The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinases-2 and tissue inhibitor of metalloproteinases-1.

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Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2

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A matrix metalloproteinase expressed on the surface of invasive tumour cells

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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

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

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Human fibroblast stromelysin catalytic domain: expression, purification, and characterization of a C-terminally truncated form

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Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP).

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21 January 2018

The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type II-like repeats

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21 January 2018

Specific alterations in the expression of alpha 3 beta 1 and alpha 6 beta 4 integrins in highly invasive and metastatic variants of human prostate carcinoma cells selected by in vitro invasion through reconstituted basement membrane

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The nucleotide sequence of bacteriophage phiX174.

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases

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

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Identifiers

10.1074/JBC.272.11.7473

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/9054449

ResearchGate publication ID

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