(Q36671475)

English

The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains

scholarly article

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains (English)

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

molecular chaperones

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molecular machine

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author name string

Yongbo Zhang

1

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

Erik R P Zuiderweg

2

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

language of work or name

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publication date

1 July 2004

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

number of pages

6

1 reference

based on heuristic

inferred from page(s)

Proceedings of the National Academy of Sciences of the United States of America

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

101

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

28

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

10272-10277

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Quaternary structure of hemoglobin in solution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Weak alignment offers new NMR opportunities to study protein structure and dynamics.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Dynamic remodeling of transcription complexes by molecular chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Hsp70 chaperone machines.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

NMR structures of biomolecules using field oriented media and residual dipolar couplings

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Structural insights into substrate binding by the molecular chaperone DnaK

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Posttranslational quality control: folding, refolding, and degrading proteins.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Transverse-relaxation-optimized (TROSY) gradient-enhanced triple-resonance NMR spectroscopy

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Structure of a new crystal form of human Hsp70 ATPase domain

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

The Hsp70 and Hsp60 chaperone machines

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Structural analysis of substrate binding by the molecular chaperone DnaK

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

30 September 2017

Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

28 June 2018

BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

28 June 2018

New techniques in structural NMR--anisotropic interactions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

28 June 2018

Automated analysis of protein NMR assignments using methods from artificial intelligence.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

28 June 2018

Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

20 September 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=478562

20 September 2018

Identifiers

10.1073/PNAS.0401313101

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

2004PNAS..10110272Z

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

ResearchGate publication ID

0 references

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