The Role of the C-terminal Domain of Human Collagenase-3 (MMP-13) in the Activation of Procollagenase-3, Substrate Specificity, and Tissue Inhibitor of Metalloproteinase Interaction-Reference-Cited by-同舟云学术

The Role of the C-terminal Domain of Human Collagenase-3 (MMP-13) in the Activation of Procollagenase-3, Substrate Specificity, and Tissue Inhibitor of Metalloproteinase Interaction

Published:1997-03 Issue:12 Volume:272 Page:7608-7616
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Knäuper Vera,Cowell Susan,Smith Bryan,López-Otin Carlos,O'Shea Mark,Morris Helen,Zardi Luciano,Murphy Gillian

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

1. Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas

2. Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein.

3. Comparison of human stromelysin and collagenase by cloning and sequence analysis

4. Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases.

5. Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage.

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