Importance of cycle timing for the function of the molecular chaperone Hsp90
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Title
Importance of cycle timing for the function of the molecular chaperone Hsp90
Authors
Keywords
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Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 23, Issue 11, Pages 1020-1028
Publisher
Springer Nature
Online
2016-10-11
DOI
10.1038/nsmb.3305
References
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Related references
Note: Only part of the references are listed.- Hsp90: Breaking the Symmetry
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- Designed Hsp90 Heterodimers Reveal an Asymmetric ATPase-Driven Mechanism In Vivo
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- Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein
- (2014) Oliver Robin Lorenz et al. MOLECULAR CELL
- Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle
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- Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation
- (2012) Joanna Soroka et al. MOLECULAR CELL
- Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity
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- The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis
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- Post-translational modifications of Hsp90 and their contributions to chaperone regulation
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- Global Functional Map of the p23 Molecular Chaperone Reveals an Extensive Cellular Network
- (2011) Frank J. Echtenkamp et al. MOLECULAR CELL
- Mutations that increase both Hsp90 ATPase activity in vitro and Hsp90 drug resistance in vivo
- (2010) Anna Zurawska et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
- SEDVIEW, Real-time Sedimentation Analysis
- (2010) David B. Hayes et al. MACROMOLECULAR BIOSCIENCE
- Biological and Structural Basis for Aha1 Regulation of Hsp90 ATPase Activity in Maintaining Proteostasis in the Human Disease Cystic Fibrosis
- (2010) Atanas V. Koulov et al. MOLECULAR BIOLOGY OF THE CELL
- Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1
- (2010) Marco Retzlaff et al. MOLECULAR CELL
- HSP90 at the hub of protein homeostasis: emerging mechanistic insights
- (2010) Mikko Taipale et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle
- (2010) Jing Li et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
- (2009) Moritz Mickler et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
- (2009) Martin Hessling et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Specific Arabidopsis HSP90.2 alleles recapitulate RAR1 cochaperone function in plant NB-LRR disease resistance protein regulation
- (2009) D. A. Hubert et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s
- (2008) Cara K. Vaughan et al. FEBS Journal
- Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90
- (2008) Kristin A. Krukenberg et al. STRUCTURE
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