The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL
Open Access
- 1 October 1996
- Vol. 87 (2) , 241-251
- https://doi.org/10.1016/s0092-8674(00)81342-2
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Inter-ring Communication is Disrupted in the GroEL Mutant Arg13 → Gly; Ala126 → Val with Known Crystal StructureJournal of Molecular Biology, 1996
- The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγSNature Structural & Molecular Biology, 1996
- SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related FieldsJournal of Structural Biology, 1996
- A Model-Based Approach for Determining Orientations of Biological Macromolecules Imaged by Cryoelectron MicroscopyJournal of Structural Biology, 1996
- The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.Proceedings of the National Academy of Sciences, 1995
- Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolutionNature Structural & Molecular Biology, 1995
- The Origins and Consequences of Asymmetry in the Chaperonin Reaction CycleJournal of Molecular Biology, 1995
- Residues in chaperonin GroEL required for polypeptide binding and releaseNature, 1994
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopyNature, 1994