(Q73316715)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10617586%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

title

Productive and nonproductive intermediates in the folding of denatured rhodanese (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10617586%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

author name string

M Panda

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10617586%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

B M Gorovits

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10617586%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

P M Horowitz

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10617586%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

language of work or name

English

0 references

publication date

1 January 2000

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10617586%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

3 November 2019

published in

1 reference

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3 November 2019

volume

275

1 reference

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3 November 2019

issue

1

1 reference

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3 November 2019

page(s)

63-70

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10617586%20AND%20SRC:MED&resulttype=core&format=json

On-pathway versus off-pathway folding intermediates

3 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

Rhodanese folding is controlled by the partitioning of its folding intermediates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

The covalent and tertiary structure of bovine liver rhodanese

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

The molten globule protein conformation probed by disulphide bonds

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

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.275.1.63

Pressure-induced reversible dissociation of enolase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

Pressure denaturation of proteins: evaluation of compressibility effects

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

Refolding and aggregation of bovine carbonic anhydrase B: quasi-elastic light scattering analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

Determining molecular weight distributions of antigen-antibody complex by quasi-elastic light scattering

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

Control of aggregation in protein refolding: the temperature-leap tactic

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.1.63

21 January 2018

Identifiers

DOI

10.1074/JBC.275.1.63

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10617586%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

1 reference