Species-Dependent Ensembles of Conserved Conformational States Define the Hsp90 Chaperone ATPase Cycle
Open Access
- 1 December 2008
- journal article
- research article
- Published by Elsevier in Molecular Cell
- Vol. 32 (5) , 631-640
- https://doi.org/10.1016/j.molcel.2008.10.024
Abstract
No abstract availableKeywords
Funding Information
- American Cancer Society
- University of California (bio03-10401)
- Howard Hughes Medical Institute
This publication has 45 references indexed in Scilit:
- Intra- and Intermonomer Interactions Are Required to Synergistically Facilitate ATP Hydrolysis in Hsp90Journal of Biological Chemistry, 2008
- The ATPase Cycle of the Endoplasmic Chaperone Grp94Journal of Biological Chemistry, 2007
- Negative staining and image classification — powerful tools in modern electron microscopyBiological Procedures Online, 2004
- Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone InteractionsPublished by Elsevier ,2003
- Multi-resolution contour-based fitting of macromolecular structuresJournal of Molecular Biology, 2002
- Hsp90: Chaperoning signal transductionJournal of Cellular Physiology, 2001
- Modulation of Akt kinase activity by binding to Hsp90Proceedings of the National Academy of Sciences, 2000
- EMAN: Semiautomated Software for High-Resolution Single-Particle ReconstructionsJournal of Structural Biology, 1999
- Transformation of MutL by ATP Binding and HydrolysisCell, 1999
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991