Protein folding in the central cavity of the GroEL-GroES chaperonin complex (Q34062238)

30 July 2017

title

Protein folding in the central cavity of the GroEL-GroES chaperonin complex (English)

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30 July 2017

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Hartl FU

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30 July 2017

Mayhew M

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30 July 2017

da Silva AC

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30 July 2017

Martin J

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30 July 2017

Erdjument-Bromage H

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30 July 2017

Tempst P

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30 July 2017

language of work or name

English

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publication date

1 February 1996

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30 July 2017

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30 July 2017

volume

379

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30 July 2017

issue

6564

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30 July 2017

page(s)

420-426

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

30 July 2017

cites work

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7 January 2021

Molecular chaperone functions of heat-shock proteins

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7 January 2021

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

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7 January 2021

Unfolding protein folding

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7 January 2021

A polypeptide bound by the chaperonin groEL is localized within a central cavity

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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

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

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7 January 2021

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

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7 January 2021

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

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7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

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7 January 2021

Binding of chaperonins.

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7 January 2021

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

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7 January 2021

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

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

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

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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The role of molecular chaperones in protein folding

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Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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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

ATP induces large quaternary rearrangements in a cage-like chaperonin structure

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7 January 2021

Refolding of barnase in the presence of GroE

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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

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

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7 January 2021

Folding of dihydrofolate reductase from Escherichia coli.

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7 January 2021

Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites

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7 January 2021

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

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7 January 2021

Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60

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7 January 2021

Measurement of protein-binding phenomena by gel filtration

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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.

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7 January 2021

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7 January 2021

Understanding how proteins fold: the lysozyme story so far.

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7 January 2021

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

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7 January 2021

Protein folding. Secrets of a double-doughnut.

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7 January 2021

Characterization of a functionally important mobile domain of GroES.

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7 January 2021

Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

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7 January 2021

(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL.

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7 January 2021

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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7 January 2021

Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

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7 January 2021

Identifiers

DOI

10.1038/379420A0

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Dimensions Publication ID

30 July 2017

1015415554

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