(Q34081455)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

review article

1 reference

title

Molecular basis for interactions of the DnaK chaperone with substrates (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

0 references

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

author name string

Mayer MP

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

Rüdiger S

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

publication date

1 September 2000

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

volume

381

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

issue

9-10

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

page(s)

877-885

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11076019%20AND%20SRC:MED&resulttype=core&format=json

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

2 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

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/10.1515%2FBC.2000.109

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

In vivo observation of polypeptide flux through the bacterial chaperonin system.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Catapult mechanism renders the chaperone action of Hsp70 unidirectional

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat shock protein induction.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Specificity of DnaK-peptide binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Role of the J-domain in the cooperation of Hsp40 with Hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Protein disaggregation mediated by heat-shock protein Hsp104.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Structural insights into substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Interaction of Hsp70 chaperones with substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Functional interaction of the auxilin J domain with the nucleotide- and substrate-binding modules of Hsc70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

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/10.1515%2FBC.2000.109

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109

Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2000.109