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SELECTED PUBLICATIONS
Nicklow, E.E. and Sevier, C.S. 2020. Activity of the yeast cytoplasmic Hsp70 nucleotide exchange factor Fes1 is regulated by reversible methionine oxidation, J. Biol. Chem., 295:552-569.
Siegenthaler, K.D., and Sevier, C.S. 2019. Working together: redox signaling between the endoplasmic reticulum and mitochondria, Chem. Res. Toxic. 32:342-344.
Sevier, C.S. 2018. Redox regulation of Hsp70 chaperone function in the endoplasmic reticulum, in Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering, Feige M.J. (Ed), Royal Society of Chemistry. (Book Chapter)
O’Donnell, J.P., Marsh, H.M., Sondermann, H., and Sevier, C.S. 2018. Disrupted hydrogen bond network and impaired ATPase activity in an Hsc70 cysteine mutant, Biochemistry, 57:1073-1086.
Ellgaard, L., Sevier, C.S., and Bulleid, N.J. 2018. How are proteins reduced in the endoplasmic reticulum? Trends Biochem. Sci., 43:32-43. (Review Article)
Siegenthaler, K.D., Pareja, K.A., Wang, J., and Sevier, C.S. 2017. An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP, eLife, 6:e24141.
Xu, M., Marsh, H.M., and Sevier, C.S. 2016. A conserved cysteine within the ATPase domain of the endoplasmic reticulum chaperone BiP is necessary for a complete complement of BiP activities, J. Mol. Biol., 428:4168-4184.
Wang, J., and Sevier, C.S. 2016. Formation and reversibility of BiP cysteine oxidation facilitate cell survival during and post oxidative stress, J. Biol. Chem., 291:7541-7157.
Wang, J., Pareja, K.A., Kaiser, C.A., and Sevier, C.S. 2014. Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress, eLife, 3:e03496.
Sevier, C.S. 2012. Erv2 and quiescin sulfhydryl oxidases: Erv-domain proteins associated with the secretory pathway, Antioxid. Redox Signal., 16:800-808. (Review Article)