Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle

Pimitespib in patients with advanced gastrointestinal stromal tumor (CHAPTER-GIST-301): a randomized, double-blind, placebo-controlled phase III trial

(2022) Y. Kurokawa et al.   ANNALS OF ONCOLOGY

Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects

(2021) Kaitlyn Hohrman et al.   GENETICS

Selective Inhibition of the Hsp90a isoform

(2021) Brian Blagg et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism

(2021) Ray Yu-Ruei Wang et al.   NATURE

Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism

(2021) Chari M. Noddings et al.   NATURE

Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network

(2021) Abraham Lopez et al.   Science Advances

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

(2020) Alexandra Rehn et al.   Nature Communications

Post-translational modifications of Hsp90 and translating the chaperone code

(2020) Sarah J. Backe et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions

(2020) Marissa E. Dean et al.   CELL STRESS & CHAPERONES

Hsp90 Co-chaperones Form Plastic Genetic Networks Adapted to Client Maturation

(2020) Maximilian M. Biebl et al.   Cell Reports

The disruption of protein−protein interactions with co-chaperones and client substrates as a strategy towards Hsp90 inhibition

(2020) Michael A. Serwetnyk et al.   Acta Pharmaceutica Sinica B

The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation

(2019) Rebecca Mercier et al.   Nature Communications

The sensitivity to Hsp90 inhibitors of both normal and oncogenically transformed cells is determined by the equilibrium between cellular quiescence and activity

(2019) Pablo C. Echeverria et al.   PLoS One

Dynamic Aha1 co‐chaperone binding to human Hsp90

(2019) Javier Oroz et al.   PROTEIN SCIENCE

The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range

(2019) Hannah Girstmair et al.   Nature Communications

Aha-type co-chaperones: the alpha or the omega of the Hsp90 ATPase cycle?

(2019) Paul LaPointe et al.   BIOLOGICAL CHEMISTRY

Two closed ATP- and ADP-dependent conformations in yeast Hsp90 chaperone detected by Mn(II) EPR spectroscopic techniques

(2019) Angeliki Giannoulis et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development

(2018) Len Neckers et al.   CELL STRESS & CHAPERONES

EzMol: A Web Server Wizard for the Rapid Visualization and Image Production of Protein and Nucleic Acid Structures

(2018) Christopher R. Reynolds et al.   JOURNAL OF MOLECULAR BIOLOGY

Functional and physical interaction between yeast Hsp90 and Hsp70

(2018) Andrea N. Kravats et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

A switch point in the molecular chaperone Hsp90 responding to client interaction

(2018) Daniel Andreas Rutz et al.   Nature Communications

Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor

(2018) Anuj Khandelwal et al.   Nature Communications

The Plasticity of the Hsp90 Co-chaperone System

(2017) Priyanka Sahasrabudhe et al.   MOLECULAR CELL

The HSP90 chaperone machinery

(2017) Florian H. Schopf et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans

(2017) Abbey D. Zuehlke et al.   Nature Communications

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies

(2017) Lindsey B. Shelton et al.   Frontiers in Neuroscience

Importance of cycle timing for the function of the molecular chaperone Hsp90

(2016) Bettina K Zierer et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase

(2016) K. A. Verba et al.   SCIENCE

Importance of cycle timing for the function of the molecular chaperone Hsp90

(2016) Bettina K Zierer et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The Mechanism of Hsp90 ATPase Stimulation by Aha1

(2016) Annemarie Wolmarans et al.   Scientific Reports

Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 Function

(2016) Parul Mishra et al.   Cell Reports

Targeting Hsp90/Hsp70-Based Protein Quality Control for Treatment of Adult Onset Neurodegenerative Diseases

(2015) William B. Pratt et al.   Annual Review of Pharmacology and Toxicology

Maximizing the Therapeutic Potential of HSP90 Inhibitors

(2015) L. M. Butler et al.   MOLECULAR CANCER RESEARCH

Posttranslational modification and conformational state of Heat Shock Protein 90 differentially affect binding of chemically diverse small molecule inhibitors

(2015) Kristin Beebe et al.   Oncotarget

A Mutation in the Catalytic Loop of Hsp90 Specifically Impairs ATPase Stimulation by Aha1p, But Not Hch1p

(2014) Natalie K. Horvat et al.   JOURNAL OF MOLECULAR BIOLOGY

Asymmetric Hsp90 N Domain SUMOylation Recruits Aha1 and ATP-Competitive Inhibitors

(2014) Mehdi Mollapour et al.   MOLECULAR CELL

Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity

(2013) Annerleim Walton-Diaz et al.   Future Medicinal Chemistry

Interaction of Heat Shock Protein 90 and the Co-chaperone Cpr6 with Ura2, a Bifunctional Enzyme Required for Pyrimidine Biosynthesis

(2013) Abbey D. Zuehlke et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle

(2013) Jing Li et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Chaperoning the Chaperone: A Role for the Co-chaperone Cpr7 in Modulating Hsp90 Function in Saccharomyces cerevisiae

(2012) Abbey D. Zuehlke et al.   GENETICS

Dynamic Tyrosine Phosphorylation Modulates Cycling of the HSP90-P50CDC37-AHA1 Chaperone Machine

(2012) Wanping Xu et al.   MOLECULAR CELL

The Co-Chaperone Hch1 Regulates Hsp90 Function Differently than Its Homologue Aha1 and Confers Sensitivity to Yeast to the Hsp90 Inhibitor NVP-AUY922

(2012) Heather Armstrong et al.   PLoS One

Evolution and function of diverse Hsp90 homologs and cochaperone proteins

(2011) Jill L. Johnson   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

Conformational dynamics of the molecular chaperone Hsp90

(2011) Kristin A. Krukenberg et al.   QUARTERLY REVIEWS OF BIOPHYSICS

Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

(2010) Marco Retzlaff et al.   MOLECULAR CELL

Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle

(2010) Jing Li et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands

(2008) Christian Radauer et al.   BMC EVOLUTIONARY BIOLOGY

Silencing of HSP90 Cochaperone AHA1 Expression Decreases Client Protein Activation and Increases Cellular Sensitivity to the HSP90 Inhibitor 17-Allylamino-17-Demethoxygeldanamycin

(2008) J. L. Holmes et al.   CANCER RESEARCH

NVP-AUY922: A Novel Heat Shock Protein 90 Inhibitor Active against Xenograft Tumor Growth, Angiogenesis, and Metastasis

(2008) S. A. Eccles et al.   CANCER RESEARCH

Species-Dependent Ensembles of Conserved Conformational States Define the Hsp90 Chaperone ATPase Cycle

(2008) Daniel R. Southworth et al.   MOLECULAR CELL