Ligand-induced conformational changes of GroEL are dependent on the bound substrate polypeptide (Q71143789)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8663187%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

title

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

1 reference

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16 October 2019

author name string

J A Mendoza

series ordinal

1

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16 October 2019

G D Campo

series ordinal

2

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16 October 2019

language of work or name

English

0 references

publication date

1 July 1996

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Journal of Biological Chemistry

16 October 2019

published in

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16 October 2019

volume

271

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16 October 2019

issue

27

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16 October 2019

page(s)

16344-16349

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Protein folding in the cell

16 October 2019

cites work

1 reference

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Molecular chaperone functions of heat-shock proteins

21 January 2018

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

21 January 2018

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

21 January 2018

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Chaperonins and protein folding: unity and disunity of mechanisms

21 January 2018

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Unfolding protein folding

21 January 2018

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

21 January 2018

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Effect of divalent cations on the molecular structure of the GroEL oligomer.

21 January 2018

1 reference

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

21 January 2018

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

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Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

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

21 January 2018

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GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

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Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

1 reference

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Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP.

21 January 2018

1 reference

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

21 January 2018

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Purification of thiosulfate sulfurtransferase by selective immobilization on blue agarose

21 January 2018

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The covalent and tertiary structure of bovine liver rhodanese

21 January 2018

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The preparation and properties of two new chromogenic substrates of trypsin

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

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Modified method of silver staining of proteins in polyacrylamide gels

21 January 2018

1 reference

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Mutation Ala2-->Ser destabilizes intersubunit interactions in the molecular chaperone GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.27.16344

Photoincorporation of 4,4'-bis(1-anilino-8-naphthalenesulfonic acid) into the apical domain of GroEL: specific information from a nonspecific probe

21 January 2018

1 reference

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High hydrostatic pressure induces the dissociation of cpn60 tetradecamers and reveals a plasticity of the monomers.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.27.16344

21 January 2018

Identifiers

DOI

10.1074/JBC.271.27.16344

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8663187%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

1 reference