Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding (Q34545652)

From Wikidata

Jump to navigation Jump to search

The printable version is no longer supported and may have rendering errors. Please update your browser bookmarks and please use the default browser print function instead.

scientific article

Language	Label	Description	Also known as
English	Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding	scientific article

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

1 reference

Europe PubMed Central

Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

protein folding

0 references

author name string

Saibil HR

1

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Horwich AL

2

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Fenton WA

3

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

publication date

1 January 2001

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Advances in Protein Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

59

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

45-72

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60)

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Folding of malate dehydrogenase inside the GroEL-GroES cavity

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Protein folding in the cell: competing models of chaperonin function.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

In vivo observation of polypeptide flux through the bacterial chaperonin system.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

GroEL-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Two conformational states of β-lactamase bound to GroEL: a biophysical characterization 1 1Edited by A. R. Fersht

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Folding intermediates of β-lactamase recognized by GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Identification of the binding surface on beta-lactamase for GroEL by limited proteolysis and MALDI-mass spectrometry

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Intrinsic Fluorescence Studies of the Chaperonin GroEL Containing Single Tyr → Trp Replacements Reveal Ligand-induced Conformational Changes

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Analysis of GroE-assisted folding under nonpermissive conditions

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Mechanisms of protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Identification of in vivo substrates of the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformation

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Secondary structure forming propensity coupled with amphiphilicity is an optimal motif in a peptide or protein for association with chaperonin 60 (GroEL)

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Interaction with GroEL destabilises non-amphiphilic secondary structure in a peptide

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Structure and function in GroEL-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Chaperonin function: folding by forced unfolding

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Identification of substrate binding site of GroEL minichaperone in solution

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Basis of Substrate Binding by the Chaperonin GroEL†

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Structural basis of allosteric changes in the GroEL mutant Arg197-->Ala

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Allosteric control by ATP of non-folded protein binding to GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959002-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/S0065-3233(01)59002-6

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

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=Q34545652&oldid=1966705859"