Unique Peptide Substrate Binding Properties of 110-kDa Heat-shock Protein (Hsp110) Determine Its Distinct Chaperone Activity
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Title
Unique Peptide Substrate Binding Properties of 110-kDa Heat-shock Protein (Hsp110) Determine Its Distinct Chaperone Activity
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 8, Pages 5661-5672
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2011-12-09
DOI
10.1074/jbc.m111.275057
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Note: Only part of the references are listed.- Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions
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- Hsp110 Chaperones Control Client Fate Determination in the Hsp70–Hsp90 Chaperone System
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- (2010) Magdalena Wisniewska et al. PLoS One
- Converging concepts of protein folding in vitro and in vivo
- (2009) F Ulrich Hartl et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding
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- The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding
- (2008) Jennifer L. Goeckeler et al. FEBS LETTERS
- Hsp110 Is a Nucleotide-activated Exchange Factor for Hsp70
- (2008) Claes Andréasson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structure of the Hsp110:Hsc70 Nucleotide Exchange Machine
- (2008) Jonathan P. Schuermann et al. MOLECULAR CELL
- Hsp110 Chaperones Regulate Prion Formation and Propagation in S. cerevisiae by Two Discrete Activities
- (2008) Heather Sadlish et al. PLoS One
- Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity
- (2008) C. Andreasson et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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