Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions.-Reference-Cited by-同舟云学术

Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions.

Published:1992-08 Issue:22 Volume:267 Page:15398-15405
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Fridman R,Fuerst T.R.,Bird R.E.,Hoyhtya M,Oelkuct M,Kraus S,Komarek D,Liotta L.A.,Berman M.L.,Stetler-Stevenson W.G.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference40 articles.

1. Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation

2. Metalloproteinases and their inhibitors in matrix remodeling

3. Matrix metalloproteinases and their inhibitors in connective tissue remodeling

4. Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation.

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

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