Reversible Thermal Transition in GrpE, the Nucleotide Exchange Factor of the DnaK Heat-Shock System
Open Access
- 1 March 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (9) , 6098-6104
- https://doi.org/10.1074/jbc.m009290200
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- The Hsp70 and Hsp60 Chaperone MachinesCell, 1998
- The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system 1 1Edited by J.KarnJournal of Molecular Biology, 1997
- The Second Step of ATP Binding to DnaK Induces Peptide ReleaseJournal of Molecular Biology, 1996
- Structural Analysis of Substrate Binding by the Molecular Chaperone DnaKScience, 1996
- The Role of ATP in the Functional Cycle of the DnaK Chaperone SystemJournal of Molecular Biology, 1995
- The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.Proceedings of the National Academy of Sciences, 1994
- Kinetics of Molecular Chaperone ActionScience, 1994
- ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysisNature, 1993
- Different conformations for the same polypeptide bound to chaperones DnaK and GroELNature, 1992
- Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.Proceedings of the National Academy of Sciences, 1991