(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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31 May 2018

author name string

Rye HS

1

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31 May 2018

Burston SG

2

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31 May 2018

Fenton WA

3

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31 May 2018

Beechem JM

4

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31 May 2018

Xu Z

5

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31 May 2018

Sigler PB

6

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31 May 2018

Horwich AL

7

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31 May 2018

language of work or name

English

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publication date

1 August 1997

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31 May 2018

published in

Nature

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31 May 2018

volume

388

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31 May 2018

page(s)

792-798

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31 May 2018

issue

6644

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31 May 2018

https://scigraph.springernature.com/pub.10.1038/42047

exact match

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cites work

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

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

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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

7 January 2021

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

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7 January 2021

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

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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

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31 May 2018

Dimensions Publication ID

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31 May 2018