S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration

@article{Uehara2006SNitrosylatedPI,
  title={S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration},
  author={T. Uehara and Tomohiro Nakamura and D. Yao and Zhong-Qing Shi and Z. Gu and Yuliang Ma and E. Masliah and Y. Nomura and S. Lipton},
  journal={Nature},
  year={2006},
  volume={441},
  pages={513-517}
}
Stress proteins located in the cytosol or endoplasmic reticulum (ER) maintain cell homeostasis and afford tolerance to severe insults. In neurodegenerative diseases, several chaperones ameliorate the accumulation of misfolded proteins triggered by oxidative or nitrosative stress, or of mutated gene products. Although severe ER stress can induce apoptosis, the ER withstands relatively mild insults through the expression of stress proteins or chaperones such as glucose-regulated protein (GRP) and… Expand
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The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in Neurodegeneration
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