Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli
- 1 November 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 303 (5) , 655-666
- https://doi.org/10.1006/jmbi.2000.4165
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Kenya
- Korea Science and Engineering Foundation
- Lotte Foundation
This publication has 49 references indexed in Scilit:
- The structures of HslU and the ATP-dependent protease HslU–HslVNature, 2000
- Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone networkProceedings of the National Academy of Sciences, 1999
- At Sixes and Sevens: Characterization of the Symmetry Mismatch of the ClpAP Chaperone-Assisted ProteaseJournal of Structural Biology, 1998
- Hsp104, Hsp70, and Hsp40: A Novel Chaperone System that Rescues Previously Aggregated ProteinsPublished by Elsevier ,1998
- Enzymatic and Structural Similarities between theEscherichia coli ATP-dependent Proteases, ClpXP and ClpAPJournal of Biological Chemistry, 1998
- Regulation by proteolysis: energy-dependent proteases and their targetsMicrobiological Reviews, 1992
- The mechanism and functions of ATP‐dependent proteases in bacterial and animal cellsEuropean Journal of Biochemistry, 1992
- Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes.Proceedings of the National Academy of Sciences, 1990
- Electron microscopy and image analysis of the multicatalytic proteinaseFEBS Letters, 1988
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976