Common functionally important motions of the nucleotide-binding domain of Hsp70

Improvement of the Treatment of Loop Structures in the UNRES Force Field by Inclusion of Coupling between Backbone- and Side-Chain-Local Conformational States

(2013) Paweł Krupa et al.   Journal of Chemical Theory and Computation

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

(2012) Anastasia Zhuravleva et al.   CELL

Extension of UNRES Force Field to Treat Polypeptide Chains with d-Amino Acid Residues

(2012) Adam K. Sieradzan et al.   Journal of Chemical Theory and Computation

Simulation of the Opening and Closing of Hsp70 Chaperones by Coarse-Grained Molecular Dynamics

(2012) Ewa Gołaś et al.   Journal of Chemical Theory and Computation

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

(2012) Roman Kityk et al.   MOLECULAR CELL

The importance of slow motions for protein functional loops

(2012) Aris Skliros et al.   PHYSICAL BIOLOGY

Molecular Mechanism of Allosteric Communication in Hsp70 Revealed by Molecular Dynamics Simulations

(2012) Federica Chiappori et al.   PLoS Computational Biology

Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones

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

Binding of a Small Molecule at a Protein–Protein Interface Regulates the Chaperone Activity of Hsp70–Hsp40

(2010) Susanne Wisén et al.   ACS Chemical Biology

Human Inducible Hsp70: Structures, Dynamics, and Interdomain Communication from All-Atom Molecular Dynamics Simulations

(2010) Adrien Nicolaï et al.   Journal of Chemical Theory and Computation

Models To Approximate the Motions of Protein Loops

(2010) Aris Skliros et al.   Journal of Chemical Theory and Computation

Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target

(2010) Christopher G. Evans et al.   JOURNAL OF MEDICINAL CHEMISTRY

The Conformational Dynamics of the Mitochondrial Hsp70 Chaperone

(2010) Koyeli Mapa et al.   MOLECULAR CELL

An interdomain sector mediating allostery in Hsp70 molecular chaperones

(2010) Robert G Smock et al.   Molecular Systems Biology

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

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

Crystal Structures of the ATPase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78

(2010) Magdalena Wisniewska et al.   PLoS One

ATP-Induced Conformational Changes in Hsp70: Molecular Dynamics and Experimental Validation of an in Silico Predicted Conformation

(2009) Hyung-June Woo et al.   BIOCHEMISTRY

Allostery in Hsp70 Chaperones Is Transduced by Subdomain Rotations

(2009) Akash Bhattacharya et al.   JOURNAL OF MOLECULAR 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

GROMACS 4:  Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

(2008) Berk Hess et al.   Journal of Chemical Theory and Computation

Principal Component Analysis for Protein Folding Dynamics

(2008) Gia G. Maisuradze et al.   JOURNAL OF MOLECULAR BIOLOGY

Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2

(2008) Zhen Xu et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY