Multiple ways to make disulfides

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Multiple ways to make disulfides

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Multiple ways to make disulfides. / Bulleid, Neil J; Ellgaard, Lars.

I: Trends in Biochemical Sciences, Bind 36, Nr. 9, 2011, s. 485-92.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Bulleid, NJ & Ellgaard, L 2011, 'Multiple ways to make disulfides', Trends in Biochemical Sciences, bind 36, nr. 9, s. 485-92. https://doi.org/10.1016/j.tibs.2011.05.004

APA

Bulleid, N. J., & Ellgaard, L. (2011). Multiple ways to make disulfides. Trends in Biochemical Sciences, 36(9), 485-92. https://doi.org/10.1016/j.tibs.2011.05.004

Vancouver

Bulleid NJ, Ellgaard L. Multiple ways to make disulfides. Trends in Biochemical Sciences. 2011;36(9):485-92. https://doi.org/10.1016/j.tibs.2011.05.004

Author

Bulleid, Neil J ; Ellgaard, Lars. / Multiple ways to make disulfides. I: Trends in Biochemical Sciences. 2011 ; Bind 36, Nr. 9. s. 485-92.

Bibtex

@article{5bb547c78c8d4105839d1f69e9e4f4c6,

title = "Multiple ways to make disulfides",

abstract = "Our concept of how disulfides form in proteins entering the secretory pathway has changed dramatically in recent years. The discovery of endoplasmic reticulum (ER) oxidoreductin 1 (ERO1) was followed by the demonstration that this enzyme couples oxygen reduction to de novo formation of disulfides. However, mammals deficient in ERO1 survive and form disulfides, which suggests the presence of alternative pathways. It has recently been shown that peroxiredoxin 4 is involved in peroxide removal and disulfide formation. Other less well-characterized pathways involving quiescin sulfhydryl oxidase, ER-localized protein disulfide isomerase peroxidases and vitamin K epoxide reductase might all contribute to disulfide formation. Here we discuss these various pathways for disulfide formation in the mammalian ER and highlight the central role played by glutathione in regulating this process.",

keywords = "Animals, Cysteine, Disulfides, Endoplasmic Reticulum, Glutathione, Humans, Hydrogen Peroxide, Mammals, Membrane Glycoproteins, Mixed Function Oxygenases, Oxidation-Reduction, Oxidoreductases, Oxidoreductases Acting on Sulfur Group Donors, Peroxides, Peroxiredoxins, Protein Disulfide-Isomerases, Protein Folding, Yeasts",

author = "Bulleid, {Neil J} and Lars Ellgaard",

year = "2011",

doi = "10.1016/j.tibs.2011.05.004",

language = "English",

volume = "36",

pages = "485--92",

journal = "Trends in Biochemical Sciences",

issn = "0968-0004",

publisher = "Elsevier",

number = "9",

}

RIS

TY - JOUR

T1 - Multiple ways to make disulfides

AU - Bulleid, Neil J

AU - Ellgaard, Lars

PY - 2011

Y1 - 2011

N2 - Our concept of how disulfides form in proteins entering the secretory pathway has changed dramatically in recent years. The discovery of endoplasmic reticulum (ER) oxidoreductin 1 (ERO1) was followed by the demonstration that this enzyme couples oxygen reduction to de novo formation of disulfides. However, mammals deficient in ERO1 survive and form disulfides, which suggests the presence of alternative pathways. It has recently been shown that peroxiredoxin 4 is involved in peroxide removal and disulfide formation. Other less well-characterized pathways involving quiescin sulfhydryl oxidase, ER-localized protein disulfide isomerase peroxidases and vitamin K epoxide reductase might all contribute to disulfide formation. Here we discuss these various pathways for disulfide formation in the mammalian ER and highlight the central role played by glutathione in regulating this process.

AB - Our concept of how disulfides form in proteins entering the secretory pathway has changed dramatically in recent years. The discovery of endoplasmic reticulum (ER) oxidoreductin 1 (ERO1) was followed by the demonstration that this enzyme couples oxygen reduction to de novo formation of disulfides. However, mammals deficient in ERO1 survive and form disulfides, which suggests the presence of alternative pathways. It has recently been shown that peroxiredoxin 4 is involved in peroxide removal and disulfide formation. Other less well-characterized pathways involving quiescin sulfhydryl oxidase, ER-localized protein disulfide isomerase peroxidases and vitamin K epoxide reductase might all contribute to disulfide formation. Here we discuss these various pathways for disulfide formation in the mammalian ER and highlight the central role played by glutathione in regulating this process.

KW - Animals

KW - Cysteine

KW - Disulfides

KW - Endoplasmic Reticulum

KW - Glutathione

KW - Humans

KW - Hydrogen Peroxide

KW - Mammals

KW - Membrane Glycoproteins

KW - Mixed Function Oxygenases

KW - Oxidation-Reduction

KW - Oxidoreductases

KW - Oxidoreductases Acting on Sulfur Group Donors

KW - Peroxides

KW - Peroxiredoxins

KW - Protein Disulfide-Isomerases

KW - Protein Folding

KW - Yeasts

U2 - 10.1016/j.tibs.2011.05.004

DO - 10.1016/j.tibs.2011.05.004

M3 - Journal article

C2 - 21778060

VL - 36

SP - 485

EP - 492

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

SN - 0968-0004

IS - 9

ER -

ID: 37816672