Size-dependent Disaggregation of Stable Protein Aggregates by the DnaK Chaperone Machinery
Open Access
- 1 July 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (28) , 21107-21113
- https://doi.org/10.1074/jbc.m001293200
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpBThe EMBO Journal, 1999
- The Protein Import Motor of MitochondriaCell, 1999
- Temperature-Controlled Activity of DnaK−DnaJ−GrpE Chaperones: Protein-Folding Arrest and Recovery during and after Heat Shock Depends on the Substrate Protein and the GrpE ConcentrationBiochemistry, 1998
- Interaction of Hsp70 chaperones with substratesNature Structural & Molecular Biology, 1997
- The ATPase Activity of Chaperonin GroEL Is Highly Stimulated at Elevated TemperaturesBiochemical and Biophysical Research Communications, 1996
- Substrate Shuttling Between the DnaK and GroEL Systems Indicates a Chaperone Network Promoting Protein FoldingJournal of Molecular Biology, 1996
- Post-translational protein import and foldingCurrent Opinion in Cell Biology, 1994
- Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein FoldingScience, 1994
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent mannerCell, 1990