Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction (Q71018406)

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15 October 2019

title

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

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15 October 2019

author name string

J S Weissman

1

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15 October 2019

H S Rye

2

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15 October 2019

W A Fenton

3

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15 October 2019

J M Beechem

4

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15 October 2019

A L Horwich

5

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15 October 2019

publication date

1 February 1996

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15 October 2019

language of work or name

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15 October 2019

volume

84

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15 October 2019

issue

3

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15 October 2019

page(s)

481-490

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To fold or not to fold....

15 October 2019

cites work

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7 January 2021

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

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Global analysis of biochemical and biophysical data

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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

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The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding

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Understanding, improving and using green fluorescent proteins

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Molecular chaperones. Opening and closing the Anfinsen cage

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Residues in chaperonin GroEL required for polypeptide binding and release

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Protein folding in the cell

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

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Molecular chaperone functions of heat-shock proteins

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Measurement of protein-binding phenomena by gel filtration

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Nature and consequences of GroEL-protein interactions

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

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Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding.

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7 January 2021

Characterization of a functionally important mobile domain of GroES.

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7 January 2021

Biochemical Characterization of Symmetric GroEL-GroES Complexes

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7 January 2021

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

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7 January 2021

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

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Proton nuclear magnetic resonance and fluorescence spectroscopic studies of segmental mobility in aequorin and a green fluorescent protein from aequorea forskalea

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Resolution of multiphasic reactions by the combination of fluorescence total-intensity and anisotropy stopped-flow kinetic experiments

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Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.

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Yeast TATA binding protein interaction with DNA: fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics

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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

The interaction of epidermal growth factor with its receptor in A431 cell membranes: a stopped-flow fluorescence anisotropy study

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7 January 2021

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

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

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Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin

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7 January 2021

Specificity in chaperonin-mediated protein folding

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7 January 2021

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7 January 2021

The Single-Ring Thermoanaerobacter brockii Chaperonin 60 (Tbr-EL7) Dimerizes to Tbr-EL14.cntdot.Tbr-ES7 under Protein Folding Conditions

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7 January 2021

Reversible denaturation of Aequorea green-fluorescent protein: physical separation and characterization of the renatured protein

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7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

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7 January 2021

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

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7 January 2021

Does compactness induce secondary structure in proteins? A study of poly-alanine chains computed by distance geometry

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7 January 2021

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8608602%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

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