The expanding world of oxidative protein folding

Hiroshi Kadokura, Jon Beckwith

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)


An ever-expanding and diverse collection of proteins and small molecules is involved in the pathways leading to protein disulphide bond formation. However, the origin of oxidative power for this process in the eukaryotic endoplasmic reticulum has remained mysterious. It has now been shown that in the yeast endoplasmic reticulum (ER), the catalyst Erv2p, a member of the Erv1p/ALR protein family, uses molecular oxygen directly to contribute oxidizing equivalents for disulphide bond information.

Original languageEnglish
Pages (from-to)E247-E249
JournalNature cell biology
Issue number11
Publication statusPublished - 2001 Nov
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology


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