(Q28213524)

1

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Catherine McLellan

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Deborah A Raynes

3

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Vince Guerriero

4

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Jeffrey L Brodsky

Roles of molecular chaperones in cytoplasmic protein folding

5

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language of work or name

English

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publication date

6 November 2002

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published in

FEBS Letters

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volume

531

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issue

2

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page(s)

339-42

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cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Folding of newly translated proteins in vivo: the role of molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

The action of molecular chaperones in the early secretory pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

The J-domain family and the recruitment of chaperone power

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

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/10.1016%2FS0014-5793%2802%2903570-6

Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

GrpE accelerates peptide binding and release from the high affinity state of DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Molecular chaperone targeting and regulation by BAG family proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Species-specific elements in the large T-antigen J domain are required for cellular transformation and DNA replication by simian virus 40

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

Mitochondrial Hsp70 Ssc1: role in protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6

The role of ATP in the functional cycle of the DnaK chaperone system

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903570-6