Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements
Top Cited Papers
- 1 October 2006
- Vol. 127 (2) , 329-340
- https://doi.org/10.1016/j.cell.2006.09.027
Abstract
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This publication has 37 references indexed in Scilit:
- Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94Protein Science, 2006
- Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complexNature, 2006
- Structural Dissection of ATP Turnover in the Prototypical GHL ATPase TopoVIStructure, 2005
- Novel, Potent Small-Molecule Inhibitors of the Molecular Chaperone Hsp90 Discovered through Structure-Based DesignJournal of Medicinal Chemistry, 2005
- Development of Purine-Scaffold Small Molecule Inhibitors of Hsp90Current Cancer Drug Targets, 2003
- Disassembly of Transcriptional Regulatory Complexes by Molecular ChaperonesScience, 2002
- GHKL, an emergent ATPase/kinase superfamilyPublished by Elsevier ,2000
- GroEL–Substrate InteractionsCell, 2000
- Transformation of MutL by ATP Binding and HydrolysisCell, 1999
- Crystal Structure and ATPase Activity of MutLCell, 1998