Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
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Title
Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
Authors
Keywords
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Journal
Nature Communications
Volume 10, Issue 1, Pages -
Publisher
Springer Science and Business Media LLC
Online
2019-06-12
DOI
10.1038/s41467-019-10463-y
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Note: Only part of the references are listed.- Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
- (2018) Ashleigh B. Bachman et al. Nature Communications
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- (2018) Gabrielle Stetz et al. Scientific Reports
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- (2018) Annemarie Wolmarans et al. BIOLOGICAL CHEMISTRY
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- (2017) Soumya Daturpalli et al. JOURNAL OF MOLECULAR BIOLOGY
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- (2016) Andrea Schulze et al. Nature Chemical Biology
- Importance of cycle timing for the function of the molecular chaperone Hsp90
- (2016) Bettina K Zierer et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Importance of cycle timing for the function of the molecular chaperone Hsp90
- (2016) Bettina K Zierer et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Asymmetric Hsp90 N Domain SUMOylation Recruits Aha1 and ATP-Competitive Inhibitors
- (2014) Mehdi Mollapour et al. MOLECULAR CELL
- Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery
- (2014) C. Ratzke et al. Nature Communications
- Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
- (2013) Nikolai Hentze et al. Jove-Journal of Visualized Experiments
- Structure, Function and Regulation of the Hsp90 Machinery
- (2013) Johannes Buchner et al. Biomedical Journal
- Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation
- (2012) Joanna Soroka et al. MOLECULAR CELL
- Dynamic Tyrosine Phosphorylation Modulates Cycling of the HSP90-P50CDC37-AHA1 Chaperone Machine
- (2012) Wanping Xu et al. MOLECULAR CELL
- The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis
- (2012) Christian N. Cunningham et al. PROTEIN SCIENCE
- Comet: An open-source MS/MS sequence database search tool
- (2012) Jimmy K. Eng et al. PROTEOMICS
- Post-translational modifications of Hsp90 and their contributions to chaperone regulation
- (2011) Mehdi Mollapour et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
- Dynamic Interaction of Hsp90 with Its Client Protein p53
- (2011) Sung Jean Park et al. JOURNAL OF MOLECULAR BIOLOGY
- 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
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- N-terminal domain of human Hsp90 triggers binding to the cochaperone p23
- (2010) G. E. Karagoz et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Species-Dependent Ensembles of Conserved Conformational States Define the Hsp90 Chaperone ATPase Cycle
- (2008) Daniel R. Southworth et al. MOLECULAR CELL
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