(Q40832423)

English

Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57.

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Europe PubMed Central

PubMed publication ID

24 September 2017

Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57. (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

author name string

Pirneskoski A

1

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Ruddock LW

2

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Klappa P

3

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Freedman RB

4

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Kivirikko KI

5

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Koivunen P

6

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

language of work or name

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publication date

29 December 2000

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

276

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

14

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

11287-11293

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Prolyl 4-hydroxylases and their protein disulfide isomerase subunit

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Collagens: molecular biology, diseases, and potentials for therapy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

The role of protein disulphide isomerase in the microsomal triacylglycerol transfer protein does not reside in its isomerase activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide binding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Protein disulphide isomerase: building bridges in protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Assignment of 1H, 13C and 15N resonances of the a' domain of protein disulfide isomerase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

The structure in solution of the b domain of protein disulfide isomerase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Interactions between protein disulphide isomerase and peptides

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

10 Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010656200

21 January 2018

Identifiers

10.1074/JBC.M010656200

1 reference

https://api.fatcat.wiki/v0/release/k2lgv7avuvbjdamjd7ujmy3c7q

30 July 2022

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release_k2lgv7avuvbjdamjd7ujmy3c7q

1 reference

https://api.fatcat.wiki/v0/release/k2lgv7avuvbjdamjd7ujmy3c7q

30 July 2022

based on heuristic

mapped directly with Wikidata item

PubMed publication ID

1 reference

https://api.fatcat.wiki/v0/release/k2lgv7avuvbjdamjd7ujmy3c7q

30 July 2022

based on heuristic

mapped directly with Wikidata item

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