The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites
- 1 March 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 306 (4) , 889-899
- https://doi.org/10.1006/jmbi.2001.4455
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpBThe EMBO Journal, 1999
- Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone networkProceedings of the National Academy of Sciences, 1999
- ClpB Cooperates with DnaK, DnaJ, and GrpE in Suppressing Protein AggregationJournal of Biological Chemistry, 1999
- Heat-inactivated proteins are rescued by the DnaK⋅J-GrpE set and ClpB chaperonesProceedings of the National Academy of Sciences, 1999
- Hsp104, Hsp70, and Hsp40: A Novel Chaperone System that Rescues Previously Aggregated ProteinsPublished by Elsevier ,1998
- Mechanism of protein remodeling by ClpA chaperoneProceedings of the National Academy of Sciences, 1997
- HSP100/Clp proteins: a common mechanism explains diverse functionsTrends in Biochemical Sciences, 1996
- Variations on a theme: Combined molecular chaperone and proteolysis functions in Clp/HSP100 proteinsJournal of Biosciences, 1996
- Protein disaggregation mediated by heat-shock protein Hspl04Nature, 1994
- HSP104 Required for Induced ThermotoleranceScience, 1990