Chaperone machines for protein folding, unfolding and disaggregation

Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein

(2013) Dong-Hua Chen et al.   CELL

Hsp110 Is aBona FideChaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates

(2013) Rayees U. H. Mattoo et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP

(2013) Ruifeng Qi et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm

(2013) Y. Song et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolution

(2013) X. Fei et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency

(2013) Ting Zhang et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction

(2013) R. Rosenzweig et al.   SCIENCE

Structural Basis of the Unfolded Protein Response

(2012) Alexei Korennykh et al.   Annual Review of Cell and Developmental Biology

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

(2012) Anastasia Zhuravleva et al.   CELL

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

(2012) Daniel K. Clare et al.   CELL

The Amyloid State of Proteins in Human Diseases

(2012) David Eisenberg et al.   CELL

Metazoan Hsp70 machines use Hsp110 to power protein disaggregation

(2012) Heike Rampelt et al.   EMBO JOURNAL

The Role of the N-Domain in the ATPase Activity of the Mammalian AAA ATPase p97/VCP

(2012) Hajime Niwa et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A Molecular History of the Amyloidoses

(2012) Joel N. Buxbaum et al.   JOURNAL OF MOLECULAR BIOLOGY

Structure and Allostery of the Chaperonin GroEL

(2012) Helen R. Saibil et al.   JOURNAL OF MOLECULAR BIOLOGY

Molecular Model of the Human 26S Proteasome

(2012) Paula C.A. da Fonseca et al.   MOLECULAR CELL

Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones

(2012) Roman Kityk et al.   MOLECULAR 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

Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces

(2012) Fabian Seyffer et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

A tightly regulated molecular toggle controls AAA+ disaggregase

(2012) Yuki Oguchi et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling

(2012) N. Kalisman et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Identification of the Cdc48bullet20S Proteasome as an Ancient AAA+ Proteolytic Machine

(2012) D. Barthelme et al.   SCIENCE

The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT

(2012) Alexander Leitner et al.   STRUCTURE

AAA+ Proteases: ATP-Fueled Machines of Protein Destruction

(2011) Robert T. Sauer et al.   Annual Review of Biochemistry

Hsp90 structure and function studied by NMR spectroscopy

(2011) Tatiana Didenko et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones

(2011) Jing Li et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

Evolution and function of diverse Hsp90 homologs and cochaperone proteins

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

Quality control and fate determination of Hsp90 client proteins

(2011) Maria A. Theodoraki et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates

(2011) Rodrigo A. Maillard et al.   CELL

Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle

(2011) Yao Cong et al.   EMBO JOURNAL

Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex

(2011) Daniel R. Southworth et al.   MOLECULAR CELL

Structure and mechanism of the hexameric MecA–ClpC molecular machine

(2011) Feng Wang et al.   NATURE

Molecular chaperones in protein folding and proteostasis

(2011) F. Ulrich Hartl et al.   NATURE

The Mammalian Disaggregase Machinery: Hsp110 Synergizes with Hsp70 and Hsp40 to Catalyze Protein Disaggregation and Reactivation in a Cell-Free System

(2011) James Shorter   PLoS One

A sequential mechanism for clathrin cage disassembly by 70-kDa heat-shock cognate protein (Hsc70) and auxilin

(2011) A. Rothnie et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface

(2011) A. Ahmad et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation

(2011) M. Miot et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Conformational dynamics of the molecular chaperone Hsp90

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

The Stress of Protein Misfolding: From Single Cells to Multicellular Organisms

(2011) T. Gidalevitz et al.   Cold Spring Harbor Perspectives in Biology

Aging as an Event of Proteostasis Collapse

(2011) R. C. Taylor et al.   Cold Spring Harbor Perspectives in Biology

Mechanisms of the Hsp70 chaperone systemThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

(2010) Jason C. Young   Biochemistry and Cell Biology

Gymnastics of Molecular Chaperones

(2010) Matthias P. Mayer   MOLECULAR CELL

Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

(2010) Marco Retzlaff et al.   MOLECULAR CELL

Mechanism of folding chamber closure in a group II chaperonin

(2010) Junjie Zhang et al.   NATURE

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase

(2010) Sandeep K Sharma et al.   Nature Chemical Biology

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

(2010) Mikko Taipale et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

(2010) Harm H. Kampinga et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation

(2010) S. Lee et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Hsp90 and Environmental Stress Transform the Adaptive Value of Natural Genetic Variation

(2010) D. F. Jarosz et al.   SCIENCE

Local and Global Mobility in the ClpA AAA+ Chaperone Detected by Cryo-Electron Microscopy: Functional Connotations

(2010) Grégory Effantin et al.   STRUCTURE

Crystal Structure of Group II Chaperonin in the Open State

(2010) Yanwu Huo et al.   STRUCTURE

Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

(2009) Evan T. Powers et al.   Annual Review of Biochemistry

Structures of Asymmetric ClpX Hexamers Reveal Nucleotide-Dependent Motions in a AAA+ Protein-Unfolding Machine

(2009) Steven E. Glynn et al.   CELL

Chaperonin complex with a newly folded protein encapsulated in the folding chamber

(2009) D. K. Clare et al.   NATURE

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

(2009) Moritz Mickler et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding

(2009) Arthur L. Horwich et al.   QUARTERLY REVIEWS OF BIOPHYSICS

Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding

(2008) Sigrun Polier et al.   CELL

Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3

(2008) Kseniya Petrova et al.   EMBO JOURNAL

Determination of the Number of Active GroES Subunits in the Fused Heptamer GroES Required for Interactions with GroEL

(2008) Tatsuya Nojima et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Flexible Attachment of the N-Domains to the ClpA Ring Body Allows their Use On Demand

(2008) Susanne Cranz-Mileva et al.   JOURNAL OF MOLECULAR BIOLOGY

Molecular Basis for Regulation of the Heat Shock Transcription Factor σ32 by the DnaK and DnaJ Chaperones

(2008) Fernanda Rodriguez et al.   MOLECULAR CELL

Structure of the Hsp110:Hsc70 Nucleotide Exchange Machine

(2008) Jonathan P. Schuermann et al.   MOLECULAR CELL

GroEL stimulates protein folding through forced unfolding

(2008) Zong Lin et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Adapting Proteostasis for Disease Intervention

(2008) William E. Balch et al.   SCIENCE

Multiple States of a Nucleotide-Bound Group 2 Chaperonin

(2008) Daniel K. Clare et al.   STRUCTURE