(Q48034329)

7 February 2018

title

The lid subdomain of DnaK is required for the stabilization of the substrate-binding site (English)

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7 February 2018

author

Arturo Muga

series ordinal

3

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7 February 2018

author name string

Fernando Moro

series ordinal

1

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7 February 2018

Vanesa Fernández-Sáiz

series ordinal

2

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7 February 2018

language of work or name

English

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publication date

25 February 2004

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7 February 2018

Journal of Biological Chemistry

number of pages

7

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based on heuristic

inferred from page(s)

published in

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7 February 2018

volume

279

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7 February 2018

issue

19

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7 February 2018

page(s)

19600-19606

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7 February 2018

Molecular chaperones in cellular protein folding

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1 reference

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

21 January 2018

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Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

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Structural insights into substrate binding by the molecular chaperone DnaK

21 January 2018

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

21 January 2018

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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

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Importance of the D and E Helices of the Molecular Chaperone DnaK for ATP Binding and Substrate Release

21 January 2018

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

21 January 2018

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Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1.

21 January 2018

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

21 January 2018

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Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy

21 January 2018

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Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling

21 January 2018

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

21 January 2018

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What vibrations tell us about proteins.

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Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study

21 January 2018

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Membrane binding induces destabilization of cytochrome c structure.

21 January 2018

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Secondary structure and temperature-induced unfolding and refolding of ribonuclease T1 in aqueous solution. A Fourier transform infrared spectroscopic study.

21 January 2018

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

21 January 2018

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The stability of proteins in extreme environments

21 January 2018

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The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator

21 January 2018

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Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

21 January 2018

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Catapult mechanism renders the chaperone action of Hsp70 unidirectional

21 January 2018

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The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system.

21 January 2018

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Redox-induced conformational changes in plastocyanin: an infrared study

21 January 2018

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Multistep mechanism of substrate binding determines chaperone activity of Hsp70

21 January 2018

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Evaluation of direct and cooperative contributions towards the strength of buried hydrogen bonds and salt bridges

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400921200

21 January 2018

Identifiers

DOI

10.1074/JBC.M400921200

1 reference

7 February 2018

1 reference

7 February 2018