(Q43633780)

25 November 2017

title

The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivation (English)

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25 November 2017

Bhattacharyya AM

1

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25 November 2017

Horowitz PM

series ordinal

2

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25 November 2017

language of work or name

English

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publication date

7 June 2001

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Journal of Biological Chemistry

25 November 2017

published in

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25 November 2017

volume

276

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25 November 2017

issue

31

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25 November 2017

page(s)

28739-28743

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On-pathway versus off-pathway folding intermediates

25 November 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M102500200

Folding and association of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

The covalent and tertiary structure of bovine liver rhodanese

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

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.M102500200

Measurement of protein using bicinchoninic acid

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

Why are enzymes less active in organic solvents than in water?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

Rhodanese folding is controlled by the partitioning of its folding intermediates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

Productive and nonproductive intermediates in the folding of denatured rhodanese

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

Alteration around the active site of rhodanese during urea-induced denaturation and its implications for folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

Domain separation precedes global unfolding of rhodanese

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M102500200

21 January 2018

Identifiers

DOI

10.1074/JBC.M102500200

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25 November 2017

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