Chaperone substrates inside the cell (Q33899375)

29 July 2017

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title

Chaperone substrates inside the cell (English)

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29 July 2017

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Ellis RJ

1

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PubMed ID

10782086

29 July 2017

language of work or name

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1 May 2000

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29 July 2017

3

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Trends in Biochemical Sciences

inferred from page(s)

published in

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29 July 2017

25

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29 July 2017

5

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29 July 2017

210-212

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Identification of in vivo substrates of the chaperonin GroEL

29 July 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

PapD-like chaperones and pilus biogenesis

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

Effects of macromolecular crowding on protein folding and aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

Principles of protein folding in the cellular environment

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

The Hsp70 and Hsp60 chaperone machines

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

Roles of molecular chaperones in cytoplasmic protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

Structural and mechanistic consequences of polypeptide binding by GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2901576-0

7 January 2021

10.1016/S0968-0004(00)01576-0

Identifiers

DOI

1 reference

29 July 2017

1 reference

PubMed ID

10782086