N-terminal Residues Regulate the Catalytic Efficiency of the Hsp90 ATPase Cycle
Open Access
- 1 November 2002
- journal article
- Published by Elsevier
- Vol. 277 (47), 44905-44910
- https://doi.org/10.1074/jbc.m208457200
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Coordinated ATP Hydrolysis by the Hsp90 DimerJournal of Biological Chemistry, 2001
- Hsp90: Chaperoning signal transductionJournal of Cellular Physiology, 2001
- Evidence for Iterative Ratcheting of Receptor-Bound hsp70 between Its ATP and ADP Conformations during Assembly of Glucocorticoid Receptor·hsp90 HeterocomplexesBiochemistry, 2001
- C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle 1 1Edited by R. HuberJournal of Molecular Biology, 2000
- The ATPase cycle of Hsp90 drives a molecular clamp' via transient dimerization of the N-terminal domainsThe EMBO Journal, 2000
- In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP HydrolysisThe Journal of cell biology, 1998
- ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone invivoThe EMBO Journal, 1998
- The hsp90-based Chaperone System: Involvement in Signal Transduction from a Variety of Hormone and Growth Factor ReceptorsExperimental Biology and Medicine, 1998
- Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular ChaperoneCell, 1997
- ATP-binding Properties of Human Hsp90Published by Elsevier ,1997