(Q70870856)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8550566%20AND%20SRC:MED&resulttype=core&format=json

14 October 2019

title

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

1 reference

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14 October 2019

author name string

D L Gibbons

series ordinal

1

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14 October 2019

P M Horowitz

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8550566%20AND%20SRC:MED&resulttype=core&format=json

14 October 2019

language of work or name

English

0 references

publication date

1 January 1996

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8550566%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

14 October 2019

published in

1 reference

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14 October 2019

volume

271

1 reference

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14 October 2019

issue

1

1 reference

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14 October 2019

page(s)

238-243

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Protein folding in the cell

14 October 2019

cites work

1 reference

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

21 January 2018

1 reference

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

21 January 2018

1 reference

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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

1 reference

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

21 January 2018

1 reference

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Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.

21 January 2018

1 reference

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Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase.

21 January 2018

1 reference

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

21 January 2018

1 reference

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

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Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

21 January 2018

1 reference

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Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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Symmetric complexes of GroE chaperonins as part of the functional cycle

21 January 2018

1 reference

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

21 January 2018

1 reference

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Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

21 January 2018

1 reference

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Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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ATP induces large quaternary rearrangements in a cage-like chaperonin structure

21 January 2018

1 reference

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Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

21 January 2018

1 reference

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL14

21 January 2018

1 reference

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Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese

21 January 2018

1 reference

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The covalent and tertiary structure of bovine liver rhodanese

21 January 2018

1 reference

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GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

A new ultrasensitive method for the determination of proteolytic activity

21 January 2018

1 reference

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

Gas-phase sequencing after electroblotting on polyvinylidene difluoride membranes assigns correct molecular weights to myoglobin molecular weight markers

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

The chaperonin GroEL is destabilized by binding of ADP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.238

21 January 2018

Identifiers

DOI

10.1074/JBC.271.1.238

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8550566%20AND%20SRC:MED&resulttype=core&format=json

14 October 2019

1 reference