Contribution of the C-terminal domain of metalloproteinases to binding by tissue inhibitor of metalloproteinases. C-terminal truncated stromelysin and matrilysin exhibit equally compromised binding affinities as compared to full-length stromelysin.-Reference-Cited by-同舟云学术

Contribution of the C-terminal domain of metalloproteinases to binding by tissue inhibitor of metalloproteinases. C-terminal truncated stromelysin and matrilysin exhibit equally compromised binding affinities as compared to full-length stromelysin.

Published:1994-04 Issue:17 Volume:269 Page:12692-12697
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Baragi V.M.,Fliszar C.J.,Conroy M.C.,Ye Q.Z.,Shipley J.M.,Welgus H.G.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. The matrix-degrading metalloproteinases

2. Matrix metalloproteinases and their inhibitors in connective tissue remodeling

3. 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)

4. Tissue Inhibitor of Metalloproteinase (TIMP-2)

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

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