(Q44772724)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14978026%20AND%20SRC:MED&resulttype=core&format=json

24 November 2019

title

Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin (English)

1 reference

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24 November 2019

0 references

3

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24 November 2019

Masafumi Yohda

7

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24 November 2019

author name string

Ryo Iizuka

1

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24 November 2019

Sena So

2

1 reference

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24 November 2019

Takao Yoshida

4

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24 November 2019

Tamotsu Zako

5

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24 November 2019

Kunihiro Kuwajima

6

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24 November 2019

language of work or name

English

0 references

publication date

20 February 2004

1 reference

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Journal of Biological Chemistry

24 November 2019

published in

1 reference

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24 November 2019

volume

279

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24 November 2019

issue

18

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24 November 2019

page(s)

18834-18839

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The Hsp70 and Hsp60 chaperone machines

24 November 2019

cites work

1 reference

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

21 January 2018

1 reference

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The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol.

21 January 2018

1 reference

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Group II chaperonins: new TRiC(k)s and turns of a protein folding machine

21 January 2018

1 reference

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

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Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

21 January 2018

1 reference

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

21 January 2018

1 reference

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ATP-induced structural change of the thermosome is temperature-dependent

21 January 2018

1 reference

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The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin

21 January 2018

1 reference

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Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

ATP binding is critical for the conformational change from an open to closed state in archaeal group II chaperonin.

21 January 2018

1 reference

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Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin

21 January 2018

1 reference

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Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1.

21 January 2018

1 reference

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Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Glycine at the 65th position plays an essential role in ATP-dependent protein folding by Archael group II chaperonin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations

21 January 2018

1 reference

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Gene duplication and gene conversion shape the evolution of archaeal chaperonins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Natural chaperonin of the hyperthermophilic archaeum, Thermococcus strain KS-1: a hetero-oligomeric chaperonin with variable subunit composition

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Group II chaperonin in an open conformation examined by electron tomography

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

Gene duplication and the evolution of group II chaperonins: implications for structure and function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400839200

21 January 2018

Identifiers

DOI

10.1074/JBC.M400839200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14978026%20AND%20SRC:MED&resulttype=core&format=json

24 November 2019

1 reference