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

Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle

(2021) Maximilian M. Biebl et al.   Nature Communications

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

(2020) Alexandra Rehn et al.   Nature Communications

Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90

(2020) Sophie L. Mader et al.   Nature Communications

Allosteric Mechanism of the Hsp90 Chaperone Interactions with Cochaperones and Client Proteins by Modulating Communication Spines of Coupled Regulatory Switches: Integrative Atomistic Modeling of Hsp90 Signaling in Dynamic Interaction Networks

(2020) Lindy Astl et al.   Journal of Chemical Information and Modeling

Dynamic allosteric communication pathway directing differential activation of the glucocorticoid receptor

(2020) C. Köhler et al.   Science Advances

The Charged Linker Modulates the Conformations and Molecular Interactions of Hsp90

(2020) Abraham López et al.   CHEMBIOCHEM

The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation

(2020) Kaushik Bhattacharya et al.   Nature Communications

ATSAS 3.0: expanded functionality and new tools for small-angle scattering data analysis

(2020) Karen Manalastas-Cantos et al.   JOURNAL OF APPLIED CRYSTALLOGRAPHY

Chaperone-Bound Clients: The Importance of Being Dynamic

(2019) Sebastian Hiller   TRENDS IN BIOCHEMICAL SCIENCES

Hsp70- and Hsp90-Mediated Regulation of the Conformation of p53 DNA Binding Domain and p53 Cancer Variants

(2019) Marta Boysen et al.   MOLECULAR CELL

Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries

(2019) Vinay Dahiya et al.   MOLECULAR CELL

Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1

(2019) Wanping Xu et al.   Nature Communications

Regulation of α-synuclein by chaperones in mammalian cells

(2019) Björn M. Burmann et al.   NATURE

Ultrashort Broadband Cooperative Pulses for Multidimensional Biomolecular NMR Experiments

(2018) Sam Asami et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System

(2018) Tania Morán Luengo et al.   MOLECULAR CELL

Reversible inhibition of the ClpP protease via an N-terminal conformational switch

(2018) Siavash Vahidi 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

Single-molecule force spectroscopy reveals folding steps associated with hormone binding and activation of the glucocorticoid receptor

(2018) Thomas Suren et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

(2018) Javier Oroz et al.   Nature Communications

Large Rotation of the N-terminal Domain of Hsp90 Is Important for Interaction with Some but Not All Client Proteins

(2017) Soumya Daturpalli et al.   JOURNAL OF MOLECULAR BIOLOGY

The Plasticity of the Hsp90 Co-chaperone System

(2017) Priyanka Sahasrabudhe et al.   MOLECULAR CELL

Allosteric Regulation Points Control the Conformational Dynamics of the Molecular Chaperone Hsp90

(2016) Alexandra Rehn et al.   JOURNAL OF MOLECULAR BIOLOGY

Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37

(2016) Dimitra Keramisanou et al.   MOLECULAR CELL

Structural basis for the antifolding activity of a molecular chaperone

(2016) Chengdong Huang et al.   NATURE

Multidomain structure and correlated dynamics determined by self-consistent FRET networks

(2016) Björn Hellenkamp et al.   NATURE METHODS

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

(2016) K. A. Verba et al.   SCIENCE

Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90

(2015) Edgar E. Boczek et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering

(2015) Giancarlo Tria et al.   IUCrJ

Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action

(2014) G. Elif Karagöz et al.   CELL

Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein

(2014) Oliver Robin Lorenz et al.   MOLECULAR CELL

The structure of the box C/D enzyme reveals regulation of RNA methylation

(2013) Audrone Lapinaite et al.   NATURE

An Interdomain Energetic Tug-of-War Creates the Allosterically Active State in Hsp70 Molecular Chaperones

(2012) Anastasia Zhuravleva et al.   CELL

Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition

(2012) Mikko Taipale et al.   CELL

Uncovering a Region of Heat Shock Protein 90 Important for Client Binding in E. coli and Chaperone Function in Yeast

(2012) Olivier Genest et al.   MOLECULAR CELL

HSP90: The Rosetta stone for cellular protein dynamics?

(2011) Diane C. DeZwaan et al.   CELL CYCLE

Dynamic Interaction of Hsp90 with Its Client Protein p53

(2011) Sung Jean Park et al.   JOURNAL OF MOLECULAR BIOLOGY

Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF

(2011) Cameron D. Mackereth et al.   NATURE

Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53

(2011) Franz Hagn et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The client protein p53 adopts a molten globule–like state in the presence of Hsp90

(2011) Sung Jean Park et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Conformational dynamics of the molecular chaperone Hsp90

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

Stereospecific Isotopic Labeling of Methyl Groups for NMR Spectroscopic Studies of High-Molecular-Weight Proteins

(2010) Pierre Gans et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

An Efficient Protocol for NMR-Spectroscopy-Based Structure Determination of Protein Complexes in Solution

(2010) Bernd Simon et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

(2010) Lars M. Ittner et al.   CELL

Enhancing the Stability and Solubility of the Glucocorticoid Receptor Ligand-Binding Domain by High-Throughput Library Screening

(2010) Tobias Seitz et al.   JOURNAL OF MOLECULAR BIOLOGY

SEDVIEW, Real-time Sedimentation Analysis

(2010) David B. Hayes et al.   MACROMOLECULAR BIOSCIENCE

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

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

Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

(2009) Marco D Mukrasch et al.   PLOS BIOLOGY

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

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

Understanding ligand-based modulation of the Hsp90 molecular chaperone dynamics at atomic resolution

(2008) G. Colombo et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90

(2008) Kristin A. Krukenberg et al.   STRUCTURE