(Q46720396)

English

Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine".

scientific article published on 23 September 2005

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine". (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

author name string

Ryo Iizuka

1

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Takao Yoshida

2

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Noriyuki Ishii

3

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Tamotsu Zako

4

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Kazunobu Takahashi

5

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Kosuke Maki

6

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Tomonao Inobe

7

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Kunihiro Kuwajima

8

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Masafumi Yohda

9

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

language of work or name

0 references

publication date

23 September 2005

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

280

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

48

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

40375-40383

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

The Hsp70 and Hsp60 chaperone machines

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

Cytoplasmic chaperonin containing TCP-1: structural and functional characterization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

The allosteric transition of GroEL induced by metal fluoride-ADP complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

Role of the -phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

A cytoplasmic chaperonin that catalyzes beta-actin folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

GroEL mediates protein folding with a two successive timer mechanism.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

Protein folding Folding with a two-stroke motor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506785200

21 January 2018

Identifiers

10.1074/JBC.M506785200

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16183634

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q46720396&oldid=917114217"