Energy landscape remodeling mechanism of Hsp70-chaperone-accelerated protein folding

Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein

(2020) Rahmi Imamoglu et al.   Nature Communications

Kinetics of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function

(2020) Si Wu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli

(2019) Liang Zhao et al.   Cell Reports

Protein folding while chaperone bound is dependent on weak interactions

(2019) Kevin Wu et al.   Nature Communications

Folding while bound to chaperones

(2018) Scott Horowitz et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System

(2018) Tania Morán Luengo et al.   MOLECULAR CELL

Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins

(2018) Pierre Goloubinoff et al.   Nature Chemical Biology

Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium

(2017) Shaon Chakrabarti et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

(2017) Jiao Yang et al.   Nature Communications

Alternative modes of client binding enable functional plasticity of Hsp70

(2016) Alireza Mashaghi et al.   NATURE

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

How Hsp70 Molecular Machines Interact with Their Substrates to Mediate Diverse Physiological Functions

(2015) Eugenia M. Clerico et al.   JOURNAL OF MOLECULAR BIOLOGY

Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR

(2015) David S. Libich et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

How Co-translational Folding of Multi-domain Protein Is Affected by Elongation Schedule: Molecular Simulations

(2015) Tomohiro Tanaka et al.   PLoS Computational Biology

Energy landscape views for interplays among folding, binding, and allostery of calmodulin domains

(2014) W. Li et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption

(2014) Paolo De Los Rios et al.   eLife

Molecular Chaperone Functions in Protein Folding and Proteostasis

(2013) Yujin E. Kim et al.   Annual Review of Biochemistry

Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides

(2013) Smriti Priya et al.   FEBS LETTERS

Structural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK

(2013) Michael Zahn et al.   JOURNAL OF MOLECULAR BIOLOGY

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

(2012) Anastasia Zhuravleva et al.   CELL

Coarse-grained molecular simulations of large biomolecules

(2012) Shoji Takada   CURRENT OPINION IN STRUCTURAL BIOLOGY

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

Multiscale Ensemble Modeling of Intrinsically Disordered Proteins: p53 N-Terminal Domain

(2011) Tsuyoshi Terakawa et al.   BIOPHYSICAL JOURNAL

CafeMol: A Coarse-Grained Biomolecular Simulator for Simulating Proteins at Work

(2011) Hiroo Kenzaki et al.   Journal of Chemical Theory and Computation

Simulation of Chaperonin Effect on Protein Folding: A Shift from Nucleation–Condensation to Framework Mechanism

(2011) Sebastian Kmiecik et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

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

Frustration, specific sequence dependence, and nonlinearity in large-amplitude fluctuations of allosteric proteins

(2011) Wenfei Li et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Multiscale methods for protein folding simulations

(2010) Wenfei Li et al.   METHODS

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

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

Reconciling theories of chaperonin accelerated folding with experimental evidence

(2009) Andrew I. Jewett et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

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

The intramolecular chaperone-mediated protein folding

(2008) Yu-Jen Chen et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Rattling the cage: computational models of chaperonin-mediated protein folding

(2008) Jeremy England et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Coarse-grained Models for Simulations of Multiprotein Complexes: Application to Ubiquitin Binding

(2007) Young C. Kim et al.   JOURNAL OF MOLECULAR BIOLOGY