Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles
Published 2017 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles
Authors
Keywords
-
Journal
eLife
Volume 6, Issue -, Pages -
Publisher
eLife Sciences Organisation, Ltd.
Online
2017-07-15
DOI
10.7554/elife.28030
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Alternative modes of client binding enable functional plasticity of Hsp70
- (2016) Alireza Mashaghi et al. NATURE
- Structural basis for the antifolding activity of a molecular chaperone
- (2016) Chengdong Huang et al. NATURE
- Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling
- (2016) Paolo De Los Rios et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Clathrin-coat disassembly illuminates the mechanisms of Hsp70 force generation
- (2016) Rui Sousa et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Hsp70 biases the folding pathways of client proteins
- (2016) Ashok Sekhar et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- In vivo aspects of protein folding and quality control
- (2016) D. Balchin et al. SCIENCE
- Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling
- (2016) Paolo De Los Rios et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Clathrin-coat disassembly illuminates the mechanisms of Hsp70 force generation
- (2016) Rui Sousa et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Methyl groups as NMR probes for biomolecular interactions
- (2015) Silke Wiesner et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins
- (2015) Rime Kerfah et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- How Hsp70 Molecular Machines Interact with Their Substrates to Mediate Diverse Physiological Functions
- (2015) Eugenia M. Clerico et al. JOURNAL OF MOLECULAR BIOLOGY
- Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
- (2015) Nadinath B. Nillegoda et al. NATURE
- Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone
- (2015) Jung Ho Lee et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Mapping the conformation of a client protein through the Hsp70 functional cycle
- (2015) Ashok Sekhar et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Bringing Dynamic Molecular Machines into Focus by Methyl-TROSY NMR
- (2014) Rina Rosenzweig et al. Annual Review of Biochemistry
- Crystal Structure of the Stress-Inducible Human Heat Shock Protein 70 Substrate-Binding Domain in Complex with Peptide Substrate
- (2014) Pingfeng Zhang et al. PLoS One
- Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein
- (2014) Ruth Kellner et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone
- (2014) T. Saio et al. SCIENCE
- The Cotranslational Function of Ribosome-Associated Hsp70 in Eukaryotic Protein Homeostasis
- (2013) Felix Willmund et al. CELL
- Structural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK
- (2013) Michael Zahn et al. JOURNAL OF MOLECULAR BIOLOGY
- Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
- (2013) Ruifeng Qi et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Hsp70 chaperone dynamics and molecular mechanism
- (2013) Matthias P. Mayer TRENDS IN BIOCHEMICAL SCIENCES
- An Interdomain Energetic Tug-of-War Creates the Allosterically Active State in Hsp70 Molecular Chaperones
- (2012) Anastasia Zhuravleva et al. CELL
- Studying “Invisible” Excited Protein States in Slow Exchange with a Major State Conformation
- (2012) Pramodh Vallurupalli et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones
- (2012) Roman Kityk et al. MOLECULAR CELL
- Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
- (2012) Ashok Sekhar et al. PROTEIN SCIENCE
- Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system
- (2012) Ashok Sekhar et al. PROTEIN SCIENCE
- DnaK Functions as a Central Hub in the E. coli Chaperone Network
- (2012) Giulia Calloni et al. Cell Reports
- Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK)
- (2011) Andrea D. Thompson et al. CELL STRESS & CHAPERONES
- Conserved, Disordered C Terminus of DnaK Enhances Cellular Survival upon Stress and DnaKin VitroChaperone Activity
- (2011) Robert G. Smock et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Molecular chaperones in protein folding and proteostasis
- (2011) F. Ulrich Hartl et al. NATURE
- Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating
- (2011) Till Böcking et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Mechanics of Hsp70 chaperones enables differential interaction with client proteins
- (2011) Rainer Schlecht et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Stereospecific Isotopic Labeling of Methyl Groups for NMR Spectroscopic Studies of High-Molecular-Weight Proteins
- (2010) Pierre Gans et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- A simple strategy for 13C,1H labeling at the Ile-γ2 methyl position in highly deuterated proteins
- (2010) Amy M. Ruschak et al. JOURNAL OF BIOMOLECULAR NMR
- Determination of Isoleucine Side-Chain Conformations in Ground and Excited States of Proteins from Chemical Shifts
- (2010) D. Flemming Hansen et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
- (2010) Sandeep K Sharma et al. Nature Chemical Biology
- Protein dynamics and conformational disorder in molecular recognition
- (2009) Tanja Mittag et al. JOURNAL OF MOLECULAR RECOGNITION
- SecB—A chaperone dedicated to protein translocation
- (2009) Philipp Bechtluft et al. Molecular BioSystems
- The role of dynamic conformational ensembles in biomolecular recognition
- (2009) David D Boehr et al. Nature Chemical Biology
- Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
- (2009) E. B. Bertelsen et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands
- (2009) Angela A. Lilly et al. PROTEIN SCIENCE
- Molecular Basis for Regulation of the Heat Shock Transcription Factor σ32 by the DnaK and DnaJ Chaperones
- (2008) Fernanda Rodriguez et al. MOLECULAR CELL
- The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG
- (2003) Shawn Y. Stevens et al. PROTEIN SCIENCE
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started