Disulfide bonds in ER protein folding and homeostasis.

@article{Feige2011DisulfideBI,
  title={Disulfide bonds in ER protein folding and homeostasis.},
  author={Matthias J Feige and Linda M Hendershot},
  journal={Current opinion in cell biology},
  year={2011},
  volume={23 2},
  pages={
          167-75
        }
}
Proteins that are expressed outside the cell must be synthesized, folded, and assembled in a way that ensures they can function in their designate location. Accordingly, these proteins are primarily synthesized in the endoplasmic reticulum (ER), which has developed a chemical environment more similar to that outside the cell. This organelle is equipped with a variety of molecular chaperones and folding enzymes that both assist the folding process, while at the same time exerting tight quality… CONTINUE READING
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