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

2 August 2017

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title

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

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2 August 2017

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Saibil HR

1

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2 August 2017

Horwich AL

series ordinal

2

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2 August 2017

Fenton WA

series ordinal

3

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2 August 2017

publication date

1 January 2001

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Advances in Protein Chemistry

2 August 2017

published in

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2 August 2017

volume

59

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2 August 2017

page(s)

45-72

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

2 August 2017

cites work

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7 January 2021

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

1 reference

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7 January 2021

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

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7 January 2021

Folding of malate dehydrogenase inside the GroEL-GroES cavity

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

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7 January 2021

GroEL-mediated protein folding

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7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

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7 January 2021

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

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7 January 2021

Folding intermediates of β-lactamase recognized by GroEL

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7 January 2021

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

1 reference

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7 January 2021

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

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7 January 2021

Analysis of GroE-assisted folding under nonpermissive conditions

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7 January 2021

GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase

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7 January 2021

Mechanisms of protein folding

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Identification of in vivo substrates of the chaperonin GroEL

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7 January 2021

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

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

7 January 2021

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

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7 January 2021

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

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

7 January 2021

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

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

7 January 2021

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

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

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7 January 2021

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

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7 January 2021

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

1 reference

7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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

7 January 2021

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

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

7 January 2021

Structure and function in GroEL-mediated protein folding

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

7 January 2021

Chaperonin function: folding by forced unfolding

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

7 January 2021

Identification of substrate binding site of GroEL minichaperone in solution

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

7 January 2021

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

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7 January 2021

Basis of Substrate Binding by the Chaperonin GroEL†

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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

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

7 January 2021

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

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

7 January 2021

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

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

7 January 2021

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

10.1016/S0065-3233(01)59002-6

Identifiers

DOI

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2 August 2017

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