In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System
Authors:
- Joseph P HendrickJHJoseph P Hendrick
- Walid A HouryWHWalid A Houry
- F.ULrich HartlFHF.ULrich Hartl
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroELCell, 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
- Determination of Regions in the Dihydrofolate Reductase Structure That Interact with the Molecular Chaperonin GroELBiochemistry, 1996
- Chaperonin-mediated folding of actin and tubulin.Journal of Cell Biology, 1996
- Successive action of Escherichia coli chaperones in vivoMolecular Microbiology, 1994
- Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein FoldingScience, 1994
- Folding in vivo of bacterial cytoplasmic proteins: Role of GroELCell, 1993
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- Host participation in bacteriophage lambda head assemblyJournal of Molecular Biology, 1973