(Q71018406)

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

15 October 2019

title

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

1 reference

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

15 October 2019

author name string

J S Weissman

1

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15 October 2019

H S Rye

2

1 reference

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15 October 2019

W A Fenton

3

1 reference

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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

0 references

1 reference

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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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Global analysis of biochemical and biophysical data

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7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

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7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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7 January 2021

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

1 reference

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7 January 2021

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

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7 January 2021

Understanding, improving and using green fluorescent proteins

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7 January 2021

Molecular chaperones. Opening and closing the Anfinsen cage

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7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

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7 January 2021

Protein folding in the cell

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Molecular chaperone functions of heat-shock proteins

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7 January 2021

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

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7 January 2021

Measurement of protein-binding phenomena by gel filtration

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7 January 2021

Nature and consequences of GroEL-protein interactions.

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Characterization of a functionally important mobile domain of GroES.

1 reference

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7 January 2021

Biochemical Characterization of Symmetric GroEL-GroES Complexes

1 reference

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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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7 January 2021

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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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Specificity in chaperonin-mediated protein folding

1 reference

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7 January 2021

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

1 reference

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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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981293-3

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981293-3

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981293-3

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981293-3

7 January 2021

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

1 reference

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7 January 2021

10.1016/S0092-8674(00)81293-3

Identifiers

DOI

1 reference

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

15 October 2019

1 reference