Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics (Q33231727)

24 July 2017

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

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24 July 2017

Jesus M Arizmendi

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Arturo Muga

object named as

Arturo Muga

5

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author name string

Vanesa Fernández-Sáiz

1

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24 July 2017

Fernando Moro

2

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24 July 2017

Sergio P Acebrón

4

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24 July 2017

language of work or name

English

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publication date

16 January 2006

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Journal of Biological Chemistry

24 July 2017

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24 July 2017

281

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24 July 2017

11

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24 July 2017

7479-7488

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Hsp70 chaperones: cellular functions and molecular mechanism

24 July 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Structural insights into substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Structural basis of interdomain communication in the Hsc70 chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

The lid subdomain of DnaK is required for the stabilization of the substrate-binding site.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Interdomain interaction through helices A and B of DnaK peptide binding domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Conformational properties of bacterial DnaK and yeast mitochondrial Hsp70. Role of the divergent C-terminal alpha-helical subdomain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Thermodynamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Destabilization of peptide binding and interdomain communication by an E543K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

The effect of mutating arginine-469 on the substrate binding and refolding activities of 70-kDa heat shock cognate protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Intragenic suppressors of Hsp70 mutants: interplay between the ATPase- and peptide-binding domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Influence of GrpE on DnaK-substrate interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Strength and co-operativity of contributions of surface salt bridges to protein stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

WHAT IF: a molecular modeling and drug design program

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M512744200

21 January 2018

Identifiers

DOI

10.1074/JBC.M512744200

1 reference

24 July 2017

1 reference