Mutant prion protein-mediated aggregation of normal prion protein in the endoplasmic reticulum: implications for prion propagation and neurotoxicity.

@article{Gu2003MutantPP,
  title={Mutant prion protein-mediated aggregation of normal prion protein in the endoplasmic reticulum: implications for prion propagation and neurotoxicity.},
  author={Yaping Gu and Susamma Verghese and Ravi Shankar Mishra and Xeumin Xu and Yongchang Shi and Neena Singh},
  journal={Journal of neurochemistry},
  year={2003},
  volume={84 1},
  pages={10-22}
}
Familial prion disorders are believed to result from spontaneous conversion of mutant prion protein (PrPM) to the pathogenic isoform (PrPSc). While most familial cases are heterozygous and thus express the normal (PrPC) and mutant alleles of PrP, the role of PrPC in the pathogenic process is unclear. Plaques from affected cases reveal a heterogeneous picture; in some cases only PrPM is detected, whereas in others both PrPC and PrPM are transformed to PrPSc. To understand if the coaggregation of… CONTINUE READING

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