8 Purification of GroEL with low fluorescence background (Q74420349)

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10 November 2019

title

Purification of GroEL with low fluorescence background (English)

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10 November 2019

8 Purification of GroEL with low fluorescence background (English)

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10.1016/S0076-6879(98)90010-6

DOI

https://api.crossref.org/works/10.1016/S0076-6879(98)90010-6

16 December 2024

3

C Frieden

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10 November 2019

author name string

A. C. Clark

series ordinal

1

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16 December 2024

R. Ramanathan

series ordinal

2

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16 December 2024

publication date

1 January 1998

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10 November 2019

1998

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National Center for Biotechnology Information

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16 December 2024

language of work or name

English

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National Center for Biotechnology Information

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16 December 2024

published in

Methods in Enzymology

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10 November 2019

volume

290

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10 November 2019

page(s)

100-118

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

10 November 2019

cites work

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The role of molecular chaperones in protein folding

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Residues in chaperonin GroEL required for polypeptide binding and release

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Revisiting the Anfinsen cage

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Molecular chaperones in protein folding and translocation

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A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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

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

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

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

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

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The effect of carboxyl-terminal mutagenesis of Gt alpha on rhodopsin and guanine nucleotide binding

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

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GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps

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7 January 2021

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

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7 January 2021

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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7 January 2021

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

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7 January 2021

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry

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7 January 2021

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

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

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7 January 2021

The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli. Evidence for the existence of an unfolding intermediate state.

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7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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7 January 2021

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

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7 January 2021

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

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7 January 2021

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

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7 January 2021

10.1016/S0076-6879(98)90010-6

Identifiers

DOI

1 reference

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10 November 2019

1 reference