Human 92kDa type IV collagenase: Functional analysis of fibronectin and carboxyl-end domains
- 1 January 1993
- journal article
- Published by Elsevier in Kidney International
- Vol. 43 (1) , 158-162
- https://doi.org/10.1038/ki.1993.26
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Sequence-specific proton NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain bBiochemistry, 1991
- The collagen‐binding site of type‐II units of bovine seminal fluid protein PDC‐109 and fibronectinEuropean Journal of Biochemistry, 1990
- Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin)Biochemistry, 1990
- Active-site zinc ligands and activated H2O of zinc enzymes.Proceedings of the National Academy of Sciences, 1990
- Metalloproteinases and their inhibitors in matrix remodelingTrends in Genetics, 1990
- Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.Proceedings of the National Academy of Sciences, 1989
- High-Resolution Epitope Mapping of hGH-Receptor Interactions by Alanine-Scanning MutagenesisScience, 1989
- Tissue cooperation in a proteolytic cascade activating human interstitial collagenase.Proceedings of the National Academy of Sciences, 1989
- A general method ofin vitropreparation and specific mutagenesis of DNA fragments: study of protein and DNA interactionsNucleic Acids Research, 1988
- Human skin fibroblast stromelysin: structure, glycosylation, substrate specificity, and differential expression in normal and tumorigenic cells.Proceedings of the National Academy of Sciences, 1987