The Expression, Refolding, and Purification of the Catalytic Domain of Human Collagenase-3 (MMP-13)
- 1 November 1998
- journal article
- Published by Elsevier in Protein Expression and Purification
- Vol. 14 (2) , 283-288
- https://doi.org/10.1006/prep.1998.0972
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- 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 InteractionJournal of Biological Chemistry, 1997
- The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis.Journal of Clinical Investigation, 1996
- Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage.Journal of Clinical Investigation, 1996
- Biochemical Characterization of Human Collagenase-3Journal of Biological Chemistry, 1996
- 1.56 Å structure of mature truncated human fibroblast collagenaseProteins-Structure Function and Bioinformatics, 1994
- The NMR structure of the inhibited catalytic domain of human stromelysin–1Nature Structural & Molecular Biology, 1994
- Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitorNature Structural & Molecular Biology, 1994
- Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with an InhibitorScience, 1994
- Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3D NMR experimentsBiochemistry, 1993
- Secondary structure and zinc ligation of human recombinant short-form stromelysin by multidimensional heteronuclear NMRBiochemistry, 1993