(Q45254051)

11 December 2017

Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch (English)

1 reference

11 December 2017

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Tong-Jin Zhao

1

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11 December 2017

Wen-Bin Ou

2

1 reference

11 December 2017

Qiang Xie

3

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11 December 2017

Yang Liu

4

1 reference

11 December 2017

Yong-Bin Yan

5

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11 December 2017

Hai-Meng Zhou

6

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11 December 2017

language of work or name

English

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publication date

5 February 2005

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Journal of Biological Chemistry

11 December 2017

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11 December 2017

280

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11 December 2017

14

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11 December 2017

13470-13476

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The protein disulphide-isomerase family: unravelling a string of folds

11 December 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Protein disulfide isomerases exploit synergy between catalytic and specific binding domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Chaperone-like activity of peptidyl-prolyl cis-trans isomerase during creatine kinase refolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Aggregation of creatine kinase during refolding and chaperonin-mediated folding of creatine kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Dependence of the anti-chaperone activity of protein disulphide isomerase on its chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Protein disulfide isomerase as an enzyme and a chaperone in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

Dimerization and oligomerization of the chaperone calreticulin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M413882200

21 January 2018

Identifiers

DOI

10.1074/JBC.M413882200

1 reference

11 December 2017

1 reference