Common functionally important motions of the nucleotide‐binding domain of H sp70-Reference-Cited by-同舟云学术

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Common functionally important motions of the nucleotide‐binding domain of H sp70

Published:2014-12-18 Issue:2 Volume:83 Page:282-299
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Gołaś Ewa I.¹,Czaplewski Cezary¹,Scheraga Harold A.²,Liwo Adam¹

Affiliation:

1. Faculty of Chemistry, University of Gdańsk80‐308Gdańsk Poland

2. Baker Laboratory of Chemistry and Chemical BiologyCornell UniversityIthaca New York14853‐1301

Funder

U.S. Department of Energy

Fundacja na rzecz Nauki Polskiej

National Institutes of Health

National Science Foundation

Narodowe Centrum Nauki

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.24731

Reference40 articles.

1. Hsp70 chaperones: Cellular functions and molecular mechanism

2. Molecular Chaperones and Protein Quality Control

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

4. Hsp70 Chaperone Ligands Control Domain Association via an Allosteric Mechanism Mediated by the Interdomain Linker

5. Hsp70 Chaperones

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication;PLOS Computational Biology;2017-01-17

2. Building Graphs To Describe Dynamics, Kinetics, and Energetics in the d-ALa:d-Lac Ligase VanA;Journal of Chemical Information and Modeling;2016-09-12

3. Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes;Structure;2016-07

4. Molecular dynamics simulation and docking studies on novel mutants (T11V, T12P and D364S) of the nucleotide-binding domain of human heat shock 70 kDa protein;Biologia;2015-12

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