(Q54559767)

31 May 2018

title

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL (English)

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14 November 2024

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H. S. Rye

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S. G. Burston

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W. A. Fenton

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J. M. Beechem

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Z. Xu

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P. B. Sigler

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A. L. Horwich

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language of work or name

English

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publication date

1 August 1997

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31 May 2018

21 August 1997

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National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9285593

full work available at URL

14 November 2024

https://www.nature.com/articles/42047.pdf

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https://www.nature.com/articles/42047.pdf

14 November 2024

1 reference

https://www.nature.com/articles/42047

14 November 2024

1 reference

http://www.nature.com/doifinder/10.1038/42047

14 November 2024

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14 November 2024

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31 May 2018

volume

388

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31 May 2018

issue

6644

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31 May 2018

page(s)

792-798

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31 May 2018

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

cites work

1 reference

7 January 2021

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

1 reference

7 January 2021

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

1 reference

7 January 2021

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

1 reference

7 January 2021

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

1 reference

7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1 reference

7 January 2021

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

1 reference

7 January 2021

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

1 reference

7 January 2021

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

1 reference

7 January 2021

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

1 reference

7 January 2021

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1 reference

7 January 2021

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

1 reference

7 January 2021

Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction

1 reference

7 January 2021

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

1 reference

7 January 2021

Resolution of multiphasic reactions by the combination of fluorescence total-intensity and anisotropy stopped-flow kinetic experiments

1 reference

7 January 2021

Sequential Domain Unfolding in Phosphoglycerate Kinase: Fluorescence Intensity and Anisotropy Stopped-Flow Kinetics of Several Tryptophan Mutants

1 reference

7 January 2021

The use of fluorescence methods to monitor unfolding transitions in proteins

1 reference

7 January 2021

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

1 reference

7 January 2021

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

1 reference

7 January 2021

Release of both native and non-native proteins from a cis-only GroEL ternary complex

1 reference

7 January 2021

The sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain

1 reference

7 January 2021

Molecular chaperones in cellular protein folding

1 reference

7 January 2021

GroEL-mediated protein folding

1 reference

7 January 2021

Identifiers

DOI

10.1038/42047

1 reference

31 May 2018

Dimensions Publication ID

1037404000

0 references

1 reference

31 May 2018