Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle. (Q35676628)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18567585%20AND%20SRC:MED&resulttype=core&format=json

9 January 2020

title

Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle (English)

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9 January 2020

4

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9 January 2020

Takashi Funatsu

7

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9 January 2020

author name string

Tomoya Sameshima

1

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9 January 2020

Taro Ueno

2

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9 January 2020

Ryo Iizuka

3

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9 January 2020

Naofumi Terada

5

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9 January 2020

Kohki Okabe

6

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9 January 2020

language of work or name

English

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publication date

20 June 2008

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9 January 2020

number of pages

9

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Journal of Biological Chemistry

inferred from page(s)

published in

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9 January 2020

volume

283

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9 January 2020

issue

35

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9 January 2020

page(s)

23765-23773

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Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.

9 January 2020

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

GroEL-GroES-mediated protein folding

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Protein measurement with the Folin phenol reagent

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 -> Ala.

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Structure and function of the GroE chaperone

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

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

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

ATP-bound states of GroEL captured by cryo-electron microscopy

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Application of fluorescence resonance energy transfer to the GroEL-GroES chaperonin reaction

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

The Hsp70 and Hsp60 chaperone machines

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Catalysis of protein folding by symmetric chaperone complexes

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

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

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Aluminofluoride and beryllofluoride complexes: a new phosphate analogs in enzymology

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Positive cooperativity in the functioning of molecular chaperone GroEL

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3259762

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

27 July 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

Catalysis, commitment and encapsulation during GroE-mediated folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

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.M802541200

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.M802541200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

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.M802541200

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

GroEL mediates protein folding with a two successive timer mechanism.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

Single-molecule observation of protein-protein interactions in the chaperonin system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M802541200

Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding

21 January 2018

1 reference

12 December 2020

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

1 reference

12 December 2020

Symmetric complexes of GroE chaperonins as part of the functional cycle

1 reference

12 December 2020

Fluorescence detection of symmetric GroEL14(GroES7)2 heterooligomers involved in protein release during the chaperonin cycle

1 reference

12 December 2020

GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps

1 reference

12 December 2020

Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides

1 reference

12 December 2020

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

1 reference

12 December 2020

Identifiers

DOI

10.1074/JBC.M802541200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18567585%20AND%20SRC:MED&resulttype=core&format=json

9 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18567585%20AND%20SRC:MED&resulttype=core&format=json

9 January 2020

1 reference