Molecular chaperones. Opening and closing the Anfinsen cage. (Q54027466)

23 May 2018

title

Molecular chaperones. Opening and closing the Anfinsen cage. (English)

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23 May 2018

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Ellis RJ

1

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23 May 2018

language of work or name

English

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publication date

1 July 1994

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23 May 2018

number of pages

3

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inferred from page(s)

published in

Current Biology

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23 May 2018

volume

4

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23 May 2018

issue

7

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23 May 2018

page(s)

633-635

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23 May 2018

ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

cites work

1 reference

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7 January 2021

Principles that govern the folding of protein chains

1 reference

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7 January 2021

Molecular chaperones in protein folding: the art of avoiding sticky situations

1 reference

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7 January 2021

Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.

1 reference

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7 January 2021

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

1 reference

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7 January 2021

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

Proper and improper folding of proteins in the cellular environment

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.

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7 January 2021

Molecular chaperones: the plant connection.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2800%2900140-8

7 January 2021

10.1016/S0960-9822(00)00140-8

Identifiers

DOI

1 reference

23 May 2018

PubMed ID

7953542

1 reference

23 May 2018