Protein folding in vivo: unraveling complex pathways (Q34434336)

2 August 2017

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title

Protein folding in vivo: unraveling complex pathways (English)

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2 August 2017

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Johnson JL

1

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PubMed ID

9244293

2 August 2017

Craig EA

series ordinal

2

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PubMed ID

9244293

2 August 2017

language of work or name

English

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publication date

1 July 1997

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2 August 2017

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2 August 2017

90

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2 August 2017

201-204

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2 August 2017

2

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Hold 'em and fold 'em: chaperones and signal transduction

2 August 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

Chaperone function of Hsp90-associated proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

A cyclophilin function in Hsp90-dependent signal transduction

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

GroEL-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

Functional specificity among Hsp70 molecular chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

Chaperones get Hip. Protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980327-X

7 January 2021

10.1016/S0092-8674(00)80327-X

Identifiers

DOI

1 reference

2 August 2017

1 reference

PubMed ID

9244293