Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide binding. (Q52539029)

2 May 2018

title

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

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2 May 2018

author name string

Klappa P

1

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2 May 2018

Koivunen P

2

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2 May 2018

Pirneskoski A

3

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2 May 2018

Karvonen P

4

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2 May 2018

Ruddock LW

5

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2 May 2018

Kivirikko KI

6

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2 May 2018

Freedman RB

7

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2 May 2018

language of work or name

English

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publication date

1 May 2000

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2 May 2018

Journal of Biological Chemistry

number of pages

6

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based on heuristic

inferred from page(s)

published in

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2 May 2018

volume

275

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2 May 2018

issue

18

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2 May 2018

page(s)

13213-13218

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2 May 2018

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

cites work

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

Prolyl 4-hydroxylases and their protein disulfide isomerase subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

The membrane proteins TRAMp and sec61 alpha p may be involved in post-translational transport of presecretory proteins into mammalian microsomes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

Mechanisms and catalysts of disulfide bond formation in proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

A pancreas-specific glycosylated protein disulphide-isomerase binds to misfolded proteins and peptides with an interaction inhibited by oestrogens

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

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/JBC.275.18.13213

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/JBC.275.18.13213

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

Protein disulfide-isomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

Interactions Between Protein Disulphide Isomerase and Peptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.275.18.13213

21 January 2018

Identifiers

DOI

10.1074/JBC.275.18.13213

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2 May 2018

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2 May 2018