(Q35069132)

English

Decipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.

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scholarly article

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Europe PubMed Central

PubMed publication ID

6 August 2017

Decipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70. (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

energy landscape

1 reference

based on heuristic

inferred from title

author name string

Adrien Nicolaï

1

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Patrice Delarue

2

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Patrick Senet

3

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

publication date

12 December 2013

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Europe PubMed Central

PubMed publication ID

6 August 2017

PLOS Computational Biology

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Europe PubMed Central

PubMed publication ID

6 August 2017

9

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

12

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

e1003379

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

copyright license

Creative Commons Attribution 4.0 International

12 December 2013

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

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1 reference

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The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding

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Nucleotide-dependent conformational states of actin

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Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

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Allostery in Hsp70 chaperones is transduced by subdomain rotations

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Structure of the Hsp110:Hsc70 nucleotide exchange machine

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Contact rearrangements form coupled networks from local motions in allosteric proteins

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Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1

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Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker

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Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy.

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Molecular dynamics: survey of methods for simulating the activity of proteins

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Molecular chaperones and protein quality control

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The changing landscape of protein allostery

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Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics

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Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state

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Allosteric regulation of chaperonins.

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Hsp70 chaperones: cellular functions and molecular mechanism

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Pathways of chaperone-mediated protein folding in the cytosol

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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Allosteric proteins and cellular control systems

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Molecular dynamics simulations of biomolecules

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Structure of a new crystal form of human Hsp70 ATPase domain

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A database of macromolecular motions

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Structural analysis of substrate binding by the molecular chaperone DnaK

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Essential dynamics of proteins

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Low-energy structures of two dipeptides and their relationship to bend conformations.

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Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70

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Conformational substates in proteins

1 reference

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Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

1 reference

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Dynamics of folded proteins

1 reference

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An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones

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Biochemistry. Enzyme motions inside and out.

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

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21 January 2018

A normal mode analysis of structural plasticity in the biomolecular motor F(1)-ATPase

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Comparative normal mode analysis of LFA-1 integrin I-domains.

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The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP-induced rearrangement of the substrate binding domain

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The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles

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21 January 2018

Allosteric regulation of Hsp70 chaperones by a proline switch

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21 January 2018

Dihedral angle principal component analysis of molecular dynamics simulations.

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21 January 2018

Mechanics of Hsp70 chaperones enables differential interaction with client proteins.

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21 January 2018

Solution small-angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments

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https://api.crossref.org/works/10.1371%2FJOURNAL.PCBI.1003379

21 January 2018

The conformational dynamics of the mitochondrial Hsp70 chaperone

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https://api.crossref.org/works/10.1371%2FJOURNAL.PCBI.1003379

21 January 2018

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

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21 January 2018

Convergence of sampling in protein simulations.

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Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation.

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21 January 2018

Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states

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https://api.crossref.org/works/10.1371%2FJOURNAL.PCBI.1003379

21 January 2018

Directed evolution of the DnaK chaperone: mutations in the lid domain result in enhanced chaperone activity

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PCBI.1003379

21 January 2018

Automated computation of low-energy pathways for complex rearrangements in proteins: application to the conformational switch of Ras p21.

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PCBI.1003379

21 January 2018

Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PCBI.1003379

21 January 2018

The GROMOS Biomolecular Simulation Program Package

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PCBI.1003379

21 January 2018

Molecular dynamics with coupling to an external bath

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PCBI.1003379

21 January 2018

Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication

1 reference

https://pubmed.ncbi.nlm.nih.gov/24348227

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker

1 reference

https://pubmed.ncbi.nlm.nih.gov/24348227

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The role of ATP in the functional cycle of the DnaK chaperone system

1 reference

https://pubmed.ncbi.nlm.nih.gov/24348227

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Free energy landscape of a biomolecule in dihedral principal component space: sampling convergence and correspondence between structures and minima

1 reference

https://pubmed.ncbi.nlm.nih.gov/24348227

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Similarities between principal components of protein dynamics and random diffusion

1 reference

https://pubmed.ncbi.nlm.nih.gov/24348227

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Conformational dynamics of full-length inducible human Hsp70 derived from microsecond molecular dynamics simulations in explicit solvent

1 reference

https://pubmed.ncbi.nlm.nih.gov/24348227

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Two-state allosteric behavior in a single-domain signaling protein

1 reference

https://pubmed.ncbi.nlm.nih.gov/24348227

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Full correlation analysis of conformational protein dynamics

1 reference

https://pubmed.ncbi.nlm.nih.gov/24348227

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1371/JOURNAL.PCBI.1003379

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

DBLP publication ID

journals/ploscb/NicolaiDS13

1 reference

DBLP Dataset 2021-01-02

28 January 2021

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

ResearchGate publication ID

0 references

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