GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle. (Q54536818)

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13 December 2019

title

GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle (English)

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13 December 2019

5

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13 December 2019

author name string

Takuya Miyazaki

1

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13 December 2019

Tatsunari Yoshimi

2

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13 December 2019

Yoshinobu Furutsu

3

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13 December 2019

Kunihiro Hongo

4

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13 December 2019

Masaaki Kanemori

6

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13 December 2019

Yasushi Kawata

7

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13 December 2019

language of work or name

English

0 references

publication date

10 October 2002

1 reference

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Journal of Biological Chemistry

13 December 2019

number of pages

8

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based on heuristic

inferred from page(s)

published in

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13 December 2019

volume

277

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13 December 2019

issue

52

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13 December 2019

page(s)

50621-50628

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Molecular chaperones in the cytosol: from nascent chain to folded protein

13 December 2019

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

GroEL-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Functional communications between the apical and equatorial domains of GroEL through the intermediate domain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Coupling between protein folding and allostery in the GroE chaperonin system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Requirement for GroEL/GroES-dependent protein folding under nonpermissive conditions of macromolecular crowding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli. Evidence for the existence of an unfolding intermediate state.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Effects of reduced levels of GroE chaperones on protein metabolism: enhanced synthesis of heat shock proteins during steady-state growth of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Mutation Ala2-->Ser destabilizes intersubunit interactions in the molecular chaperone GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

In vivo and in vitro function of GroEL mutants with impaired allosteric properties

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

On the relationship between the Hill coefficients for steady-state and transient kinetic data: a criterion for concerted transitions in allosteric proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Dissociation of the GroEL-GroES asymmetric complex is accelerated by increased cooperativity in ATP binding to the GroEL ring distal to GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

The effect of macromolecular crowding on chaperonin-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Macromolecular crowding: an important but neglected aspect of the intracellular environment

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

Identification of in vivo substrates of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209183200

21 January 2018

Identifiers

DOI

10.1074/JBC.M209183200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12377767%20AND%20SRC:MED&resulttype=core&format=json

release_ez3l5vs3m5eknevedcostocnfq

13 December 2019

Fatcat ID

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Fatcat

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mapped directly with Wikidata item

24 November 2022

based on heuristic

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