{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Koritzinsky M"],"funding":["Dutch Research Council (NWO)","Canadian Institutes of Health Research"],"pagination":["615-27"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3840938"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["203(4)"],"pubmed_abstract":["Most proteins destined for the extracellular space require disulfide bonds for folding and stability. Disulfide bonds are introduced co- and post-translationally in endoplasmic reticulum (ER) cargo in a redox relay that requires a terminal electron acceptor. Oxygen can serve as the electron acceptor in vitro, but its role in vivo remains unknown. Hypoxia causes ER stress, suggesting a role for oxygen in protein folding. Here we demonstrate the existence of two phases of disulfide bond formation in living mammalian cells, with differential requirements for oxygen. Disulfide bonds introduced rapidly during protein synthesis can occur without oxygen, whereas those introduced during post-translational folding or isomerization are oxygen dependent. Other protein maturation processes in the secr"],"journal":["The Journal of cell biology"],"pubmed_title":["Two phases of disulfide bond formation have differing requirements for oxygen."],"pmcid":["PMC3840938"],"funding_grant_id":["916.56.015","700.54.013"],"pubmed_authors":["Harding NJ","Braakman I","Koritzinsky M","Levitin F","Wouters BG","van den Beucken T","Boutros PC","Rumantir RA","Chu KC"],"additional_accession":[]},"is_claimable":false,"name":"Two phases of disulfide bond formation have differing requirements for oxygen.","description":"Most proteins destined for the extracellular space require disulfide bonds for folding and stability. Disulfide bonds are introduced co- and post-translationally in endoplasmic reticulum (ER) cargo in a redox relay that requires a terminal electron acceptor. Oxygen can serve as the electron acceptor in vitro, but its role in vivo remains unknown. Hypoxia causes ER stress, suggesting a role for oxygen in protein folding. Here we demonstrate the existence of two phases of disulfide bond formation in living mammalian cells, with differential requirements for oxygen. Disulfide bonds introduced rapidly during protein synthesis can occur without oxygen, whereas those introduced during post-translational folding or isomerization are oxygen dependent. Other protein maturation processes in the secr","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Nov","modification":"2026-04-17T11:25:40.442Z","creation":"2026-04-07T14:24:00.619Z"},"accession":"S-EPMC3840938","cross_references":{"pubmed":["24247433"],"doi":["10.1083/jcb.201307185"]}}