(Q38556889)

4 September 2017

title

Conformational changes at the nucleotide binding of GroEL induced by binding of protein substrates. Luminescence studies (English)

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4 September 2017

Churchich JE

1

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4 September 2017

language of work or name

English

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publication date

1 August 1997

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Journal of Biological Chemistry

4 September 2017

published in

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4 September 2017

volume

272

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4 September 2017

issue

32

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4 September 2017

page(s)

19645-19648

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Two-dimensional crystals of the molecular chaperone GroEL reveal structural plasticity.

4 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Binding of a fluorescent nucleotide analog to Hsc70. The effect of peptide protein interactions on the luminescence properties of the probe

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

A rapid and sensitive radiometric assay for adenosine triphosphatase activity using Cerenkov radiation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Refolding and recognition of mitochondrial malate dehydrogenase by Escherichia coli chaperonins cpn 60 (groEL) and cpn10 (groES)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Ligand-induced conformational changes in the apical domain of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Ligand-induced conformational changes of GroEL are dependent on the bound substrate polypeptide

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Intrinsic Fluorescence Studies of the Chaperonin GroEL Containing Single Tyr → Trp Replacements Reveal Ligand-induced Conformational Changes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Refolding and reassociation of glycerol dehydrogenase from Bacillus stearothermophilus in the absence and presence of GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as subtrates for various enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

Symmetric complexes of GroE chaperonins as part of the functional cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.32.19645

21 January 2018

Identifiers

DOI

10.1074/JBC.272.32.19645

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4 September 2017

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