(Q40499272)

21 September 2017

1 reference

title

GroEL structure: a new chapter on assisted folding (English)

1 reference

21 September 2017

Lorimer GH

1

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21 September 2017

1 December 1994

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21 September 2017

1 reference

21 September 2017

2

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21 September 2017

12

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21 September 2017

1125-1128

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

21 September 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Molecular chaperones. Opening and closing the Anfinsen cage.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Symmetric complexes of GroE chaperonins as part of the functional cycle

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

A polypeptide bound by the chaperonin groEL is localized within a central cavity

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2894%2900114-6

7 January 2021

10.1016/S0969-2126(94)00114-6

Identifiers

DOI

1 reference

21 September 2017

1 reference

PubMed ID

7704522