(Q28262765)

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Allostery in the Hsp70 chaperone proteins

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

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

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

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

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Hsp70 chaperones: cellular functions and molecular mechanism

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393–507) in complex with the peptide NRLLLTG

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Molecular chaperones in the cytosol: from nascent chain to folded protein

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Structural insights into substrate binding by the molecular chaperone DnaK

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Structural analysis of substrate binding by the molecular chaperone DnaK

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Allostery in Hsp70 chaperones is transduced by subdomain rotations

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Hsp70 chaperone dynamics and molecular mechanism

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Allostery and the Monod-Wyman-Changeux model after 50 years

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Quaternary dynamics and plasticity underlie small heat shock protein chaperone function

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Hsp70 chaperone machines.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

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

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

An interdomain sector mediating allostery in Hsp70 molecular chaperones

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Hsp70 chaperone systems: diversity of cellular functions and mechanism of action

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Interaction of Hsp70 chaperones with substrates

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4460500

Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes

2 June 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1506692112

Energetics of nucleotide-induced DnaK conformational states

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1506692112

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1506692112

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1506692112

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1506692112

Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1506692112

Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/26038563

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/26038563

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.1506692112

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

5008486

ADS bibcode

2015PNAS..112E2865Z

0 references

OpenCitations bibliographic resource ID

5008486

1 reference