(Q54560154)

31 May 2018

title

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

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31 May 2018

4

Hartl FU

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31 May 2018

Ewalt KL

1

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31 May 2018

Hendrick JP

series ordinal

2

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31 May 2018

Houry WA

series ordinal

3

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31 May 2018

language of work or name

English

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publication date

1 August 1997

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31 May 2018

published in

Cell

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31 May 2018

volume

90

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31 May 2018

page(s)

491-500

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31 May 2018

issue

3

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31 May 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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1 reference

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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

Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL.

1 reference

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7 January 2021

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

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7 January 2021

Proteins as molecular chaperones.

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7 January 2021

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

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7 January 2021

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

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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

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

1 reference

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7 January 2021

Truncated staphylococcal nuclease is compact but disordered

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7 January 2021

Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms

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7 January 2021

Successive action of Escherichia coli chaperones in vivo.

1 reference

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7 January 2021

Role of the major heat shock proteins as molecular chaperones

1 reference

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7 January 2021

Host participation in bacteriophage lambda head assembly

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7 January 2021

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

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7 January 2021

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

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7 January 2021

A new periplasmic protein of Escherichia coli which is synthesized in spheroplasts but not in intact cells

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7 January 2021

Molecular chaperones in cellular protein folding

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

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

1 reference

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7 January 2021

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

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7 January 2021

Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle

1 reference

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7 January 2021

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

1 reference

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7 January 2021

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1 reference

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7 January 2021

The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol.

1 reference

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7 January 2021

Ribosomes and ribosomal RNA as chaperones for folding of proteins.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

Chaperonin-mediated folding of actin and tubulin

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

1 reference

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7 January 2021

The effect of macromolecular crowding on chaperonin-mediated protein folding

1 reference

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

Functional interaction of heat shock protein GroEL with an RNase E-like activity in Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

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%2980509-7

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%2980509-7

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2980509-7

7 January 2021

10.1016/S0092-8674(00)80509-7

Identifiers

DOI

1 reference

31 May 2018

release_co4fuunt6nd4nntkqsdbuqj45q

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/co4fuunt6nd4nntkqsdbuqj45q

24 November 2022

mapped directly with Wikidata item

PubMed ID

9267029

1 reference

31 May 2018