Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
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Title
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
Authors
Keywords
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Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 19, Issue 12, Pages 1347-1355
Publisher
Springer Nature
Online
2012-11-19
DOI
10.1038/nsmb.2442
References
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Related references
Note: Only part of the references are listed.- Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
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- The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
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- Remodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretion
- (2009) Gabriele Bönemann et al. EMBO JOURNAL
- DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface
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- Coupling and Dynamics of Subunits in the Hexameric AAA+ Chaperone ClpB
- (2008) Nicolas D. Werbeck et al. JOURNAL OF MOLECULAR BIOLOGY
- Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
- (2008) Peter Tessarz et al. MOLECULAR MICROBIOLOGY
- Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
- (2008) Tobias Haslberger et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity
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- Hsp104 and ClpB: protein disaggregating machines
- (2008) Shannon M. Doyle et al. TRENDS IN BIOCHEMICAL SCIENCES
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