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.
Open Access
- 1 August 1992
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (22) , 15398-15405
- https://doi.org/10.1016/s0021-9258(19)49547-1
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Higher-order complex formation between the 72-kilodalton type IV collagenase and tissue inhibitor of metalloproteinases-2Biochemistry, 1992
- Conformational stability, folding, and ligand-binding affinity of single-chain Fv immunoglobulin fragments expressed in Escherichia coliBiochemistry, 1991
- Human fibroblast stromelysin catalytic domain: expression, purification, and characterization of a C-terminally truncated formBiochemistry, 1991
- Tumor Cell Invasion Inhibited by TIMP-2JNCI Journal of the National Cancer Institute, 1991
- The complex between a tissue inhibitor of metalloproteinases (TIMP‐2) and 72‐kDa progelatinase is a metalloproteinase inhibitorEuropean Journal of Biochemistry, 1991
- Evidence for the involvement of type II domains in collagen binding by 72 kDa type IV procollagenaseFEBS Letters, 1991
- Cancer metastasis and angiogenesis: An imbalance of positive and negative regulationCell, 1991
- An internal cysteine plays a role in the maintenance of the latency of human fibroblast collagenaseBiochemistry, 1991
- Metalloproteinases and their inhibitors in matrix remodelingTrends in Genetics, 1990
- Biosynthesis of type IV procollagensBiochemistry, 1980