(Q35676893)

English

Sequential action of ATP-dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins

scientific article published on 13 October 2008

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scholarly article

1 reference

Europe PubMed Central

9 August 2017

Sequential action of ATP-dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins (English)

1 reference

Europe PubMed Central

9 August 2017

José María Valpuesta

8

object named as

José M Valpuesta

1 reference

Europe PubMed Central

9 August 2017

object named as

Toshihiko Oka

9

0 references

object named as

Muhamad Sahlan

6

0 references

object named as

Noriyuki Ishii

11

0 references

object named as

Masafumi Yohda

13

0 references

author name string

Taro Kanzaki

1

1 reference

Europe PubMed Central

9 August 2017

Ryo Iizuka

2

1 reference

Europe PubMed Central

9 August 2017

Kazunobu Takahashi

3

1 reference

Europe PubMed Central

9 August 2017

Kosuke Maki

4

1 reference

Europe PubMed Central

9 August 2017

Rie Masuda

5

1 reference

Europe PubMed Central

9 August 2017

Hugo Yébenes

7

1 reference

Europe PubMed Central

9 August 2017

Masahiro Furutani

10

1 reference

Europe PubMed Central

9 August 2017

Kunihiro Kuwajima

12

1 reference

Europe PubMed Central

9 August 2017

language of work or name

0 references

publication date

13 October 2008

1 reference

Europe PubMed Central

9 August 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

9 August 2017

283

1 reference

Europe PubMed Central

9 August 2017

34773-34784

1 reference

Europe PubMed Central

9 August 2017

50

1 reference

Europe PubMed Central

9 August 2017

Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

The changing landscape of protein allostery

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 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://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

The Hsp70 and Hsp60 chaperone machines

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 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://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 2018

The 60 kDa heat shock proteins in the hyperthermophilic archaeon Sulfolobus shibatae.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259901

12 July 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.M805303200

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.M805303200

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.M805303200

21 January 2018

Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M805303200

21 January 2018

Cooperativity in the thermosome.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M805303200

21 January 2018

Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M805303200

21 January 2018

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M805303200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M805303200

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.M805303200

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.M805303200

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.M805303200

21 January 2018

Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M805303200

21 January 2018

An engineered chaperonin caging a guest protein: Structural insights and potential as a protein expression tool

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M805303200

21 January 2018

Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M805303200

21 January 2018

Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M805303200

21 January 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/18854314

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Dynamics of group II chaperonin and prefoldin probed by 13C NMR spectroscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/18854314

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL

1 reference

https://pubmed.ncbi.nlm.nih.gov/18854314

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M805303200

1 reference

Europe PubMed Central

9 August 2017

1 reference

Europe PubMed Central

9 August 2017

1 reference

Europe PubMed Central

9 August 2017

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