ClpB chaperone passively threads soluble denatured proteins through its central pore
Author:
Affiliation:
1. Department of Biology; Faculty of Science and Engineering; Konan University; Okamoto 8-9-1 Kobe 658-8501 Japan
2. Institute for Integrative Neurobiology; Konan University; Okamoto 8-9-1 Kobe 658-8501 Japan
Publisher
Wiley
Subject
Cell Biology,Genetics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/gtc.12188/fullpdf
Reference43 articles.
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2. Structural basis for intersubunit signaling in a protein disaggregating machine;Biter;Proc. Natl Acad. Sci. USA,2012
3. DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine;Doyle;J. Biol. Chem.,2012
4. Allosteric communication between the nucleotide binding domains of caseinolytic peptidase B;Fernandez-Higuero;J. Biol. Chem.,2011
5. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins;Glover;Cell,1998
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