Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding (Q27679694)

2

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Masaki Okumura

3

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Masatoshi Hagiwara

4

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Shoji Masui

5

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Ken-ichi Maegawa

6

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Masatoshi Saiki

7

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Tomohisa Horibe

8

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Mamoru Suzuki

9

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Kenji Inaba

Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported

10

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language of work or name

English

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publication date

2013

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published in

Scientific Reports

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volume

3

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page(s)

2456

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copyright license

start time

16 August 2013

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation

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Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum

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Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer

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Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene

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The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites

20 March 2017

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Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response

20 March 2017

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Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.

29 September 2017

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29 September 2017

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Multiple ways to make disulfides

29 September 2017

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Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin

29 September 2017

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Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins

29 September 2017

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Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation

29 September 2017

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Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum

29 September 2017

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Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation

29 September 2017

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A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells

29 September 2017

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Protein quality control in the early secretory pathway

29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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Structural basis for target protein recognition by the protein disulfide reductase thioredoxin

29 September 2017

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Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles

29 September 2017

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29 September 2017

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Formation and transfer of disulphide bonds in living cells

29 September 2017

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Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum

29 September 2017

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3744794

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3744794

Reexamination of the folding of BPTI: predominance of native intermediates.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3744794

Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).

29 September 2017

1 reference

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Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3744794

Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells

2 June 2018

1 reference

Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum

21 January 2018

1 reference

B- to plasma-cell terminal differentiation entails oxidative stress and profound reshaping of the antioxidant responses

21 January 2018

1 reference

Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

1 reference

Modulation of Cellular Disulfide-Bond Formation and the ER Redox Environment by Feedback Regulation of Ero1

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23949117

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Acceleration of disulfide-coupled protein folding using glutathione derivatives

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23949117

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

A kinetic explanation for the rearrangement pathway of BPTI folding

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23949117

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/SREP02456

1 reference

Dimensions Publication ID

1023128574

0 references

1 reference

1 reference

PubMed publication ID

23949117

1 reference