The ins and outs of a molecular chaperone machine. (Q47289550)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9584617%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

review article

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title

The ins and outs of a molecular chaperone machine (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9584617%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

0 references

2

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11 November 2019

author name string

A Richardson

series ordinal

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9584617%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

C Georgopoulos

series ordinal

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9584617%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

publication date

1 April 1998

1 reference

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11 November 2019

number of pages

6

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Trends in Biochemical Sciences

inferred from page(s)

published in

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11 November 2019

volume

23

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11 November 2019

issue

4

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11 November 2019

page(s)

138-143

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9584617%20AND%20SRC:MED&resulttype=core&format=json

The emergence of the chaperone machines

11 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

GroEL-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

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%2FS0968-0004%2898%2901193-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Temperature dependence of backbone dynamics in loops of human mitochondrial heat shock protein 10.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Conserved sequence motifs in bacterial and bacteriophage chaperonins

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Characterization of a functionally important mobile domain of GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Interplay of structure and disorder in cochaperonin mobile loops

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

GroES binding regulates GroEL chaperonin activity under heat shock

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

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%2FS0968-0004%2898%2901193-1

7 January 2021

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Protein folding Folding with a two-stroke motor

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

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

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

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%2FS0968-0004%2898%2901193-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Identification of GroEL as a constituent of an mRNA-protection complex in Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

An endosymbiont chaperonin is a novel type of histidine protein kinase.

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901193-1

7 January 2021

10.1016/S0968-0004(98)01193-1

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9584617%20AND%20SRC:MED&resulttype=core&format=json

release_gn5iddt2djbufiho5eglsknuwm

11 November 2019

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/gn5iddt2djbufiho5eglsknuwm

24 November 2022

mapped directly with Wikidata item

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