Characterization of Folded, Intermediate, and Unfolded States of Recombinant Human Interstitial Collagenase
Open Access
- 1 April 1996
- journal article
- Published by Elsevier
- Vol. 271 (14) , 8015-8021
- https://doi.org/10.1074/jbc.271.14.8015
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propellerStructure, 1995
- Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to ItselfBiochemistry, 1994
- 1.56 Å structure of mature truncated human fibroblast collagenaseProteins-Structure Function and Bioinformatics, 1994
- Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with an InhibitorScience, 1994
- Structure-function relationship of human neutrophil collagenase: identification of regions responsible for substrate specificity and general proteinase activity.Proceedings of the National Academy of Sciences, 1993
- Matrix Metalloproteinases: A ReviewCritical Reviews in Oral Biology & Medicine, 1993
- Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activitiesBiochemical Journal, 1991
- A filter paper dye-binding assay for quantitative determination of protein without interference from reducing agents or detergentsAnalytical Biochemistry, 1990
- Protein folding: Hypotheses and experimentsProtein Journal, 1987
- Human skin fibroblast procollagenase: mechanisms of activation by organomercurials and trypsinBiochemistry, 1983