(Q36820063)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23584019%20AND%20SRC:MED&resulttype=core&format=json

28 February 2020

title

GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP (English)

1 reference

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28 February 2020

1 reference

2

1 reference

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28 February 2020

Andrija Finka

5

1 reference

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28 February 2020

author name string

Smriti Priya

1

1 reference

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28 February 2020

Vishal Sood

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23584019%20AND%20SRC:MED&resulttype=core&format=json

28 February 2020

Rayees U H Mattoo

4

1 reference

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28 February 2020

Abdussalam Azem

6

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23584019%20AND%20SRC:MED&resulttype=core&format=json

28 February 2020

Paolo De Los Rios

7

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23584019%20AND%20SRC:MED&resulttype=core&format=json

28 February 2020

Pierre Goloubinoff

8

1 reference

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28 February 2020

language of work or name

English

0 references

publication date

12 April 2013

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23584019%20AND%20SRC:MED&resulttype=core&format=json

Proceedings of the National Academy of Sciences of the United States of America

28 February 2020

published in

1 reference

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28 February 2020

volume

110

1 reference

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28 February 2020

issue

18

1 reference

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28 February 2020

page(s)

7199-7204

1 reference

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Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis

28 February 2020

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Chaperonins: two rings for folding

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Disaggregating chaperones: an unfolding story.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

GroEL stimulates protein folding through forced unfolding

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Allosteric regulation of chaperonins.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Protein folding and misfolding

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Review: allostery in chaperonins

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Minimal and optimal mechanisms for GroE-mediated protein folding

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Residues in chaperonin GroEL required for polypeptide binding and release

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Protein stability and protein folding

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase

27 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate

27 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

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

5 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex.

5 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

5 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Characterization of a functionally important mobile domain of GroES.

5 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

5 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3645539

Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli

5 September 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.1219867110

Biophysical Characterization of Two Different Stable Misfolded Monomeric Polypeptides That Are Chaperone-Amenable Substrates

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.1219867110

Identification of in vivo substrates of the chaperonin GroEL

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.1219867110

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

21 January 2018

1 reference

12 December 2020

Symmetric complexes of GroE chaperonins as part of the functional cycle

1 reference

12 December 2020

Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding

1 reference

12 December 2020

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

1 reference

12 December 2020

Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity

1 reference

12 December 2020

GroE facilitates refolding of citrate synthase by suppressing aggregation

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.1219867110

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23584019%20AND%20SRC:MED&resulttype=core&format=json

28 February 2020

0 references

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23584019%20AND%20SRC:MED&resulttype=core&format=json

28 February 2020

PubMed publication ID

23584019

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23584019%20AND%20SRC:MED&resulttype=core&format=json