The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. (Q41633923)

5 October 2017

title

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. (English)

1 reference

5 October 2017

Roseman AM

1 reference

5 October 2017

Chen S

1 reference

5 October 2017

White H

1 reference

5 October 2017

Braig K

1 reference

5 October 2017

Saibil HR

1 reference

5 October 2017

language of work or name

English

0 references

publication date

1 October 1996

1 reference

5 October 2017

1 reference

5 October 2017

1 reference

5 October 2017

1 reference

5 October 2017

page(s)

241-251

1 reference

Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure.

5 October 2017

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

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%2FS0092-8674%2800%2981342-2

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

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%2FS0092-8674%2800%2981342-2

7 January 2021

The chaperonin GroEL is destabilized by binding of ADP

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

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%2FS0092-8674%2800%2981342-2

7 January 2021

Residue lysine-34 in GroES modulates allosteric transitions in GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Characterization of a functionally important mobile domain of GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

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%2FS0092-8674%2800%2981342-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

The ribosome at improved resolution: new techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Three-dimensional reconstruction from random projections: orientational alignment via Radon transforms

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Structure of Lumbricus terrestris Hemoglobin at 30 Å Resolution Determined Using Angular Reconstitution

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

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%2FS0092-8674%2800%2981342-2

7 January 2021

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

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%2FS0092-8674%2800%2981342-2

7 January 2021

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

Allosteric control by ATP of non-folded protein binding to GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981342-2

7 January 2021

10.1016/S0092-8674(00)81342-2

Identifiers

DOI

1 reference

5 October 2017

1 reference