(Q54648101)

2 June 2018

title

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

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2 June 2018

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4

Hartl FU

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2 June 2018

Martin J

1

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2 June 2018

Mayhew M

series ordinal

2

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2 June 2018

Langer T

series ordinal

3

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2 June 2018

publication date

1 November 1993

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language of work or name

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2 June 2018

volume

366

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issue

6452

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2 June 2018

page(s)

228-233

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2 June 2018

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7 January 2021

Protein folding in the cell

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7 January 2021

Molecular chaperone functions of heat-shock proteins

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7 January 2021

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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7 January 2021

Purification and properties of groE, a host protein involved in bacteriophage assembly

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7 January 2021

Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly

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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

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

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7 January 2021

Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60.

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7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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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

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

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7 January 2021

GroE facilitates refolding of citrate synthase by suppressing aggregation

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7 January 2021

Characterization of a functionally important mobile domain of GroES.

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7 January 2021

Binding of chaperonins.

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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

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

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7 January 2021

Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.

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7 January 2021

The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable.

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7 January 2021

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

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7 January 2021

Unfolding protein folding

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7 January 2021

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

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7 January 2021

Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes

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7 January 2021

Renaturation of citrate synthase: influence of denaturant and folding assistants

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7 January 2021

Identifiers

DOI

10.1038/366228A0

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2 June 2018

Dimensions Publication ID

1048865531

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2 June 2018