GroEL Traps Dimeric and Monomeric Unfolding Intermediates of Citrate Synthase
Open Access
- 1 December 1998
- journal article
- Published by Elsevier
- Vol. 273 (50) , 33305-33310
- https://doi.org/10.1074/jbc.273.50.33305
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Two conformational states of β-lactamase bound to GroEL: a biophysical characterizationJournal of Molecular Biology, 1998
- Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL 1 1Edited by J. KarnJournal of Molecular Biology, 1997
- Interaction of GroEL with Conformational States of Horse CytochromeJournal of Molecular Biology, 1996
- Dynamics of the GroEL – Protein Complex: Effects of Nucleotides and Folding MutantsJournal of Molecular Biology, 1996
- Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding ReactionCell, 1996
- Protein folding in the central cavity of the GroEL–GroES chaperonin complexNature, 1996
- The Origins and Consequences of Asymmetry in the Chaperonin Reaction CycleJournal of Molecular Biology, 1995
- Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat shock protein inductionFEBS Letters, 1991
- Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme AJournal of Molecular Biology, 1984
- Crystallographic refinement and atomic models of two different forms of citrate synthase at 2·7 and 1·7 Å resolutionJournal of Molecular Biology, 1982