Related references
Note: Only part of the references are listed.Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein
Dong-Hua Chen et al.
CELL (2013)
Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates
Rayees U. H. Mattoo et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2013)
Structure and Allostery of the Chaperonin GroEL
Helen R. Saibil et al.
JOURNAL OF MOLECULAR BIOLOGY (2013)
Uncovering a Region of Heat Shock Protein 90 Important for Client Binding in E. coli and Chaperone Function in Yeast
Olivier Genest et al.
MOLECULAR CELL (2013)
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
Ruifeng Qi et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2013)
Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm
Yuyu Song et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2013)
Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution
Xue Fei et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2013)
Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction
Rina Rosenzweig et al.
SCIENCE (2013)
Structural Basis of the Unfolded Protein Response
Alexei Korennykh et al.
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, VOL 28 (2012)
Hsp90 structure and function studied by NMR spectroscopy
Tatiana Didenko et al.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH (2012)
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Jing Li et al.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH (2012)
Evolution and function of diverse Hsp90 homologs and cochaperone proteins
Jill L. Johnson
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH (2012)
Quality control and fate determination of Hsp90 client proteins
Maria A. Theodoraki et al.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH (2012)
An Interdomain Energetic Tug-of-War Creates the Allosterically Active State in Hsp70 Molecular Chaperones
Anastasia Zhuravleva et al.
CELL (2012)
ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin
Daniel K. Clare et al.
CELL (2012)
The Amyloid State of Proteins in Human Diseases
David Eisenberg et al.
CELL (2012)
Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
Yao Cong et al.
EMBO JOURNAL (2012)
Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
Heike Rampelt et al.
EMBO JOURNAL (2012)
The Role of the N-Domain in the ATPase Activity of the Mammalian AAA ATPase p97/VCP
Hajime Niwa et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2012)
A Molecular History of the Amyloidoses
Joel N. Buxbaum et al.
JOURNAL OF MOLECULAR BIOLOGY (2012)
Molecular Model of the Human 26S Proteasome
Paula C. A. da Fonseca et al.
MOLECULAR CELL (2012)
Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones
Roman Kityk et al.
MOLECULAR CELL (2012)
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA plus disaggregase at aggregate surfaces
Fabian Seyffer et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2012)
A tightly regulated molecular toggle controls AAA plus disaggregase
Yuki Oguchi et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2012)
Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling
Nir Kalisman et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2012)
Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency
Ting Zhang et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2012)
Identification of the Cdc48•20S Proteasome as an Ancient AAA+ Proteolytic Machine
Dominik Barthelme et al.
SCIENCE (2012)
The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT
Alexander Leitner et al.
STRUCTURE (2012)
AAA+ Proteases: ATP-Fueled Machines of Protein Destruction
Robert T. Sauer et al.
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 80 (2011)
ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates
Rodrigo A. Maillard et al.
CELL (2011)
Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex
Daniel R. Southworth et al.
MOLECULAR CELL (2011)
Structure and mechanism of the hexameric MecA-ClpC molecular machine
Feng Wang et al.
NATURE (2011)
Molecular chaperones in protein folding and proteostasis
F. Ulrich Hartl et al.
NATURE (2011)
The Mammalian Disaggregase Machinery: Hsp110 Synergizes with Hsp70 and Hsp40 to Catalyze Protein Disaggregation and Reactivation in a Cell-Free System
James Shorter
PLOS ONE (2011)
A sequential mechanism for clathrin cage disassembly by 70-kDa heat-shock cognate protein (Hsc70) and auxilin
Alice Rothnie et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2011)
Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface
Atta Ahmad et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2011)
Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation
Marika Miot et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2011)
Conformational dynamics of the molecular chaperone Hsp90
Kristin A. Krukenberg et al.
QUARTERLY REVIEWS OF BIOPHYSICS (2011)
The Stress of Protein Misfolding: From Single Cells to Multicellular Organisms
Tali Gidalevitz et al.
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY (2011)
Aging as an Event of Proteostasis Collapse
Rebecca C. Taylor et al.
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY (2011)
Mechanisms of the Hsp70 chaperone system
Jason C. Young
BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE (2010)
Gymnastics of Molecular Chaperones
Matthias P. Mayer
MOLECULAR CELL (2010)
Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1
Marco Retzlaff et al.
MOLECULAR CELL (2010)
Mechanism of folding chamber closure in a group II chaperonin
Junjie Zhang et al.
NATURE (2010)
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
Sandeep K. Sharma et al.
NATURE CHEMICAL BIOLOGY (2010)
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Mikko Taipale et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2010)
`The HSP70 chaperone machinery: J proteins as drivers of functional specificity
Harm H. Kampinga et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2010)
CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation
Sukyeong Lee et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)
Hsp90 and Environmental Stress Transform the Adaptive Value of Natural Genetic Variation
Daniel F. Jarosz et al.
SCIENCE (2010)
Local and Global Mobility in the ClpA AAA plus Chaperone Detected by Cryo-Electron Microscopy: Functional Connotations
Gregory Effantin et al.
STRUCTURE (2010)
Crystal Structure of Group II Chaperonin in the Open State
Yanwu Huo et al.
STRUCTURE (2010)
Targeting the dynamic HSP90 complex in cancer
Jane Trepel et al.
NATURE REVIEWS CANCER (2010)
Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
Evan T. Powers et al.
ANNUAL REVIEW OF BIOCHEMISTRY (2009)
Structures of Asymmetric ClpX Hexamers Reveal Nucleotide-Dependent Motions in a AAA plus Protein-Unfolding Machine
Steven E. Glynn et al.
CELL (2009)
Chaperonin complex with a newly folded protein encapsulated in the folding chamber
D. K. Clare et al.
NATURE (2009)
The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
Moritz Mickler et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2009)
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding
Arthur L. Horwich et al.
QUARTERLY REVIEWS OF BIOPHYSICS (2009)
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
Sigrun Polier et al.
CELL (2008)
Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3
Kseniya Petrova et al.
EMBO JOURNAL (2008)
Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL
Tatsuya Nojima et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
The flexible attachment of the N-domains to the ClpA ring body allows their use on demand
Susanne Cranz-Mileva et al.
JOURNAL OF MOLECULAR BIOLOGY (2008)
Molecular Basis for Regulation of the Heat Shock Transcription Factor σ32 by the DnaK and DnaJ Chaperones
Fernanda Rodriguez et al.
MOLECULAR CELL (2008)
Structure of the Hsp110: Hsc70 nucleotide exchange machine
Jonathan P. Schuermann et al.
MOLECULAR CELL (2008)
GroEL stimulates protein folding through forced unfolding
Zong Lin et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2008)
Adapting proteostasis for disease intervention
William E. Balch et al.
SCIENCE (2008)
Multiple states of a nucleotide-bound group 2 chaperonin
Daniel K. Clare et al.
STRUCTURE (2008)
Structural basis of J cochaperone binding and regulation of Hsp70
Jianwen Jiang et al.
MOLECULAR CELL (2007)
Structures of GRP94-Nucleotide complexes reveal mechanistic differences between the hsp90 chaperones
D. Eric Dollins et al.
MOLECULAR CELL (2007)
Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1
Qinglian Liu et al.
CELL (2007)
Topologies of a substrate protein bound to the chaperonin GroEL
Nadav Elad et al.
MOLECULAR CELL (2007)
Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain
L. Fang et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2006)
Structural analysis of E-coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
Andrew K. Shiau et al.
CELL (2006)
The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
Stephen Tam et al.
NATURE CELL BIOLOGY (2006)
Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state
Akira Kitamura et al.
NATURE CELL BIOLOGY (2006)
Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers
Christian Behrends et al.
MOLECULAR CELL (2006)
Structure of an Hsp90-Cdc37-Cdk4 complex
Cara K. Vaughan et al.
MOLECULAR CELL (2006)
Molecular chaperones and protein quality control
Bernd Bukau et al.
CELL (2006)
An expanded protein folding cage in the GroEL-gp31 complex
DK Clare et al.
JOURNAL OF MOLECULAR BIOLOGY (2006)
Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
MMU Ali et al.
NATURE (2006)
Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes
NA Ranson et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2006)
Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
J Hinnerwisch et al.
CELL (2005)
AAA+ proteins: Have engine, will work
PI Hanson et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2005)
Cooperativity in the thermosome
MG Bigotti et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)
Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy
HF Mendes et al.
TRENDS IN MOLECULAR MEDICINE (2005)
Nucleotide dependent motion and mechanism of action of p97/VCP
B DeLaBarre et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
J Weibezahn et al.
CELL (2004)
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL
F Motojima et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2004)
The structure of clpB: A molecular chaperone that rescues proteins from an aggregated state
S Lee et al.
CELL (2003)
The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate
JZ Li et al.
STRUCTURE (2003)
GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle
T Miyazaki et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc97
G Siligardi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease
PK Auluck et al.
SCIENCE (2002)
Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU
J Wang et al.
STRUCTURE (2001)
GroEL/GroES-mediated folding of a protein too large to be encapsulated
TK Chaudhuri et al.
CELL (2001)
Crystal and solution structures of an HsIUV protease-chaperone complex
MC Sousa et al.
CELL (2000)
The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains
C Prodromou et al.
EMBO JOURNAL (2000)
Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
GW Farr et al.
CELL (2000)
GHKL, an emergent ATPase/kinase superfamily
R Dutta et al.
TRENDS IN BIOCHEMICAL SCIENCES (2000)
Share Paper
