(Q65002024)

3 July 2019

title

Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization. (English)

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3 July 2019

author name string

Semisotnov GV

1

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3 July 2019

Uversky VN

2

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3 July 2019

Sokolovsky IV

3

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3 July 2019

Gutin AM

4

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3 July 2019

Razgulyaev OI

5

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3 July 2019

Rodionova NA

6

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3 July 2019

publication date

1 June 1990

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3 July 2019

Journal of Molecular Biology

number of pages

8

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based on heuristic

inferred from page(s)

published in

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3 July 2019

volume

213

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3 July 2019

page(s)

561-568

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3 July 2019

issue

3

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3 July 2019

Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Cis-trans equilibrium and kinetic studies of acetyl-L-proline and glycyl-L-proline

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Possible implications of many proline residues for the kinetics of protein unfolding and refolding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

'Molten-globule' state accumulates in carbonic anhydrase folding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

The conformation around the peptide bond between the P1- and P2-positions is important for catalytic activity of some proline-specific proteases

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Conformational specificity of chymotrypsin toward proline-containing substrates.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Catalysis of protein folding by prolyl isomerase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Effect of proline residues on protein folding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Role of cis-trans isomerism of the peptide bond in protease specificity. Kinetic studies on small proline-containing peptides and on polyproline

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Catalysis of proline isomerization during protein-folding reactions

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Multiparameter kinetic study on the unfolding and refolding of bovine carbonic anhydrase B

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Swine pepsinogen folding intermediates are highly structured, motile molecules

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Sequential mechanism of refolding of carbonic anhydrase B.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

Acid denaturation of bovine carbonic anhydrase B.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980215-3

10.1016/S0022-2836(05)80215-3

7 January 2021

Identifiers

DOI

1 reference

3 July 2019

PubMed ID

2112610

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3 July 2019