Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants

@inproceedings{Tsunoda2014IntactPF,
  title={Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants},
  author={Satoshi Tsunoda and Edward Avezov and Alisa F Zyryanova and Tasuku Konno and Leonardo Mendes-Silva and Eduardo Pinho Melo and Heather P Harding and David Ron},
  booktitle={eLife},
  year={2014}
}
Protein folding homeostasis in the endoplasmic reticulum (ER) requires efficient protein thiol oxidation, but also relies on a parallel reductive process to edit disulfides during the maturation or degradation of secreted proteins. To critically examine the widely held assumption that reduced ER glutathione fuels disulfide reduction, we expressed a modified form of a cytosolic glutathione-degrading enzyme, ChaC1, in the ER lumen. ChaC1(CtoS) purged the ER of glutathione eliciting the expected… CONTINUE READING
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Modulation of

  • CS Sevier, H Qu, N Heldman, E Gross, D Fass, CA Kaiser
  • CELLULAR
  • 2007
Highly Influential
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  • HG Hansen, JD Schmidt, +7 authors L. Ellgaard
  • The Journal of Biological Chemistry 287:39513…
  • 2012
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