(Q34543463)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27783598%20AND%20SRC:MED&resulttype=core&format=json

26 March 2020

title

Alternative modes of client binding enable functional plasticity of Hsp70 (English)

1 reference

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26 March 2020

1

1 reference

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26 March 2020

David P Minde

3

1 reference

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26 March 2020

Matthias P. Mayer

7

1 reference

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26 March 2020

Günter Kramer

8

1 reference

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26 March 2020

Bernd Bukau

9

1 reference

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26 March 2020

5

Roman Kityk

1 reference

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26 March 2020

6

Beate Zachmann-Brand

1 reference

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26 March 2020

4

Anne S Wentink

1 reference

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26 March 2020

author name string

Sergey Bezrukavnikov

2

1 reference

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26 March 2020

Sander J Tans

10

1 reference

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26 March 2020

language of work or name

English

0 references

publication date

26 October 2016

1 reference

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26 March 2020

number of pages

4

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inferred from page(s)

published in

Nature

1 reference

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26 March 2020

volume

539

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26 March 2020

issue

7629

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26 March 2020

page(s)

448-451

1 reference

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https://scigraph.springernature.com/pub.10.1038/nature20137

26 March 2020

exact match

0 references

cites work

Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.

1 reference

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The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

21 January 2018

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Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles

21 January 2018

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

21 January 2018

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Hsp70 chaperones: cellular functions and molecular mechanism

21 January 2018

1 reference

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

21 January 2018

1 reference

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Cellular strategies for controlling protein aggregation

21 January 2018

1 reference

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Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Mechanics of Hsp70 chaperones enables differential interaction with client proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Direct observation of chaperone-induced changes in a protein folding pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Reshaping of the conformational search of a protein by the chaperone trigger factor.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Stretching DNA with optical tweezers

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Real-time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Replication initiator protein RepE of mini-F plasmid: functional differentiation between monomers (initiator) and dimers (autogenous repressor).

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Action of the Hsp70 chaperone system observed with single proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Hsp90 as a capacitor for morphological evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

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/10.1038%2FNATURE20137

Gymnastics of molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE20137

The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171.

21 January 2018

1 reference

12 December 2020

Multistep mechanism of substrate binding determines chaperone activity of Hsp70

1 reference

12 December 2020

A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.

1 reference

12 December 2020

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

1 reference

12 December 2020