Dimerization of Hsp90 Is Required for in Vivo Function
Open Access
- 1 November 2007
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 282 (48) , 35386-35395
- https://doi.org/10.1074/jbc.m703844200
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Dihydroquinone Ansamycins: Toward Resolving the Conflict between Low in Vitro Affinity and High Cellular Potency of Geldanamycin DerivativesBiochemistry, 2006
- Chaperoning Checkpoint Kinase 1 (Chk1), an Hsp90 Client, with Purified ChaperonesPublished by Elsevier ,2006
- The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client ProteinsJournal of Molecular Biology, 2005
- Rebuilt AAA + motors reveal operating principles for ATP-fuelled machinesNature, 2005
- Independent ATPase Activity of Hsp90 Subunits Creates a Flexible Assembly PlatformJournal of Molecular Biology, 2004
- The Co-chaperone Sba1 Connects the ATPase Reaction of Hsp90 to the Progression of the Chaperone CycleJournal of Molecular Biology, 2004
- X-ray Tomography Generates 3-D Reconstructions of the Yeast, Saccharomyces cerevisiae, at 60-nm ResolutionMolecular Biology of the Cell, 2004
- Stimulation of the weak ATPase activity of human Hsp90 by a client protein 1 1Edited by G. von HeijneJournal of Molecular Biology, 2002
- Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl .alpha.-chymotrypsin using different denaturantsBiochemistry, 1988
- [11] Coupled assay of Na+,K+-ATPase activityPublished by Elsevier ,1988