Grp94 Works Upstream of BiP in Protein Remodeling Under Heat Stress

The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) Oligomers

(2021) Yi Jin et al.   JOURNAL OF MOLECULAR BIOLOGY

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

The ER chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation.

(2019) Ming Sun et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Intermolecular Interactions between Hsp90 and Hsp70

(2019) Shannon M. Doyle et al.   JOURNAL OF MOLECULAR BIOLOGY

Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines

(2019) Eugenia M. Clerico et al.   BIOCHEMICAL JOURNAL

GRP78: A cell's response to stress

(2019) Ibrahim M. Ibrahim et al.   LIFE SCIENCES

The Hsp70 chaperone network

(2019) Rina Rosenzweig et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity

(2019) Hongtao Li et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Molecular Mechanism of J-Domain-Triggered ATP Hydrolysis by Hsp70 Chaperones

(2018) Roman Kityk et al.   MOLECULAR CELL

Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate

(2018) Mathias Rosam et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70

(2018) Naveen K. C. Gowda et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Intra-molecular pathways of allosteric control in Hsp70s

(2018) Matthias P. Mayer   PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES

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

Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate

(2018) Mathias Rosam et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70

(2018) Naveen K. C. Gowda et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease

(2018) Abdullah Hoter et al.   INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling

(2018) Olivier Genest et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends

(2018) Kristine Faye R. Pobre et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Hsp70–Hsp90 Chaperone Cascade in Protein Folding

(2018) Tania Morán Luengo et al.   TRENDS IN CELL BIOLOGY

The HSP90 chaperone machinery

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

Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s

(2017) Jiao Yang et al.   Nature Communications

Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site

(2017) John D. Huck et al.   Cell Reports

AMPylation targets the rate-limiting step of BiP’s ATPase cycle for its functional inactivation

(2017) Steffen Preissler et al.   eLife

Review: The HSP90 molecular chaperone-an enigmatic ATPase

(2016) Laurence H. Pearl   BIOPOLYMERS

Clients and Oncogenic Roles of Molecular Chaperone gp96/grp94

(2016) Ephraim A. Ansa-Addo et al.   CURRENT TOPICS IN MEDICINAL CHEMISTRY

Members of the Hsp70 Family Recognize Distinct Types of Sequences to Execute ER Quality Control

(2016) Julia Behnke et al.   MOLECULAR CELL

Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate

(2016) Nuri Sung et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling

(2015) Olivier Genest et al.   JOURNAL OF MOLECULAR BIOLOGY

BiP and Its Nucleotide Exchange Factors Grp170 and Sil1: Mechanisms of Action and Biological Functions

(2015) Julia Behnke et al.   JOURNAL OF MOLECULAR BIOLOGY

Hsp90: Breaking the Symmetry

(2015) Matthias P. Mayer et al.   MOLECULAR CELL

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

Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP

(2015) Jiao Yang et al.   STRUCTURE

Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker

(2015) Steffen Preissler et al.   eLife

Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles

(2014) Elaine Kirschke et al.   CELL

MZB1 is a GRP94 cochaperone that enables proper immunoglobulin heavy chain biosynthesis upon ER stress

(2014) M. Rosenbaum et al.   GENES & DEVELOPMENT

Physical Interaction between Bacterial Heat Shock Protein (Hsp) 90 and Hsp70 Chaperones Mediates Their Cooperative Action to Refold Denatured Proteins

(2014) Hitoshi Nakamoto et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2

(2013) Pallav D Patel et al.   Nature Chemical Biology

Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins

(2013) N. K. C. Gowda et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Protein Folding in the Endoplasmic Reticulum

(2013) I. Braakman et al.   Cold Spring Harbor Perspectives in Biology

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

GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum

(2011) Michal Marzec et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions

(2011) Moritz Marcinowski et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling

(2011) O. Genest 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

Erratum: Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone

(2011) Bei Liu et al.   Nature Communications

Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity

(2010) Yuko Motojima-Miyazaki et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP

(2010) Jeanne Bonomo et al.   BIOPHYSICAL CHEMISTRY

ATP Binding to Hsp90 Is Sufficient for Effective Chaperoning of p53 Protein

(2010) Dawid Walerych et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

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

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

GRP94 in ER quality control and stress responses

(2010) Davide Eletto et al.   SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY

Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine

(2009) Christian Graf et al.   EMBO JOURNAL

An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells

(2009) Olga Ostrovsky et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

ERdj3, a Luminal ER DnaJ Homologue, Binds Directly to Unfolded Proteins in the Mammalian ER: Identification of Critical Residues†

(2008) Yi Jin et al.   BIOCHEMISTRY

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

Regulated release of ERdj3 from unfolded proteins by BiP

(2008) Yi Jin et al.   EMBO JOURNAL