The expanding world of oxidative protein folding

Hiroshi Kadokura, Jon Beckwith

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

Abstract

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
Volume3
Issue number11
DOIs
Publication statusPublished - 2001 Nov
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology

Fingerprint Dive into the research topics of 'The expanding world of oxidative protein folding'. Together they form a unique fingerprint.

Cite this