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Trends in Biochemical Sciences|November 21, 2017
How Are Proteins Reduced in the Endoplasmic Reticulum?Lars Ellgaard, Carolyn S Sevier, Neil J BulleidTrends in Biochemical Sciences|July 23, 2011
Multiple ways to make disulfidesNeil J Bulleid, Lars EllgaardAntioxidants & Redox Signaling|December 7, 2011
Erv2 and quiescin sulfhydryl oxidases: Erv-domain enzymes associated with the secretory pathwayCarolyn S SevierCold Spring Harbor Perspectives in Biology|November 6, 2012
Disulfide bond formation in the mammalian endoplasmic reticulumNeil J BulleidNature Structural & Molecular Biology|October 6, 2012
Solving the mystery of procollagen chain selectivityNeil J BulleidThe Journal of Biological Chemistry|February 12, 2016
Formation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative StressJie Wang, Carolyn S SevierMolecular Membrane Biology|July 10, 2003
Protein folding and translocation across the endoplasmic reticulum membraneEileithyia Swanton, Neil J BulleidThe Journal of Biological Chemistry|July 16, 2004
Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathwaySeema Chakravarthi, Neil J BulleidAnnual Review of Biochemistry|April 19, 2011
Protein folding and modification in the mammalian endoplasmic reticulumIneke Braakman, Neil J BulleidPageof 13