The Two-Stage Process of the Heat Shock Protein 90 Thermal Denaturation: Effect of Calcium and Magnesium
- 1 August 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 249 (1) , 197-201
- https://doi.org/10.1006/bbrc.1998.9108
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Domain Structures and Immunogenic Regions of the 90-kDa Heat-shock Protein (HSP90)Journal of Biological Chemistry, 1997
- The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 ConformationJournal of Biological Chemistry, 1997
- Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor AgentCell, 1997
- Characterization of the 90 kDa heat shock protein (HSP90)-associated ATP/GTPaseJournal of Biosciences, 1996
- Heat-induced Chaperone Activity of HSP90Journal of Biological Chemistry, 1996
- Structural Organization of Procaryotic and Eucaryotic Hsp90. INFLUENCE OF DIVALENT CATIONS ON STRUCTURE AND FUNCTIONJournal of Biological Chemistry, 1995
- Hsp85 conformational change within the heat shock temperature rangeBiochemical and Biophysical Research Communications, 1992
- Calculation of protein extinction coefficients from amino acid sequence dataAnalytical Biochemistry, 1989
- Purification and characterization of the 90-kDa heat-shock protein from mammalian tissuesEuropean Journal of Biochemistry, 1988
- [2]Scanning microcalorimetry in studying temperature-induced changes in proteinsPublished by Elsevier ,1986