(Q43790536)

26 November 2017

title

GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation (English)

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26 November 2017

Girish C Melkani

1

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26 November 2017

Gustavo Zardeneta

series ordinal

2

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26 November 2017

Jose A Mendoza

series ordinal

3

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26 November 2017

language of work or name

English

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publication date

1 June 2002

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Biochemical and Biophysical Research Communications

26 November 2017

published in

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26 November 2017

volume

294

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26 November 2017

issue

4

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26 November 2017

page(s)

893-899

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Chaperone-assisted protein folding.

26 November 2017

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900575-2

GroEL-mediated protein folding

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

7 January 2021

1 reference

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Protein-catalysed protein folding.

7 January 2021

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Basis of Substrate Binding by the Chaperonin GroEL†

7 January 2021

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The hydrophobic nature of GroEL-substrate binding

7 January 2021

1 reference

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Rhodanese conformational changes permit oxidation to give disulfides that form in a kinetically determined sequence

7 January 2021

1 reference

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Partitioning of rhodanese onto GroEL. Chaperonin binds a reversibly oxidized form derived from the native protein.

7 January 2021

1 reference

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Purification of bovine liver rhodanese by low-pH column chromatography

7 January 2021

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The covalent and tertiary structure of bovine liver rhodanese

7 January 2021

1 reference

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Purification of GroEL with low fluorescence background

7 January 2021

1 reference

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

7 January 2021

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.

7 January 2021

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

7 January 2021

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

7 January 2021

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Modified method of silver staining of proteins in polyacrylamide gels

7 January 2021

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alpha-Crystallin facilitates the reactivation of hydrogen peroxide-inactivated rhodanese

7 January 2021

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Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding

7 January 2021

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Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.

7 January 2021

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The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases

7 January 2021

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

7 January 2021

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Physical characterization of a reactivatable liposome-bound rhodanese folding intermediate

7 January 2021

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

7 January 2021

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GroEL-assisted refolding of adrenodoxin during chemical cluster insertion

7 January 2021

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Active site structural features for chemically modified forms of rhodanese

7 January 2021

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Enhanced hydrogen peroxide sensitivity and altered stress protein expression in iron-starved Mycobacterium smegmatis

7 January 2021

1 reference

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10.1016/S0006-291X(02)00575-2

7 January 2021

Identifiers

DOI

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26 November 2017

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