Characterization of the F198S prion protein mutation: enhanced glycosylation and defective refolding.

@article{Zaidi2005CharacterizationOT,
  title={Characterization of the F198S prion protein mutation: enhanced glycosylation and defective refolding.},
  author={Syed I.A. Zaidi and Sandra L Richardson and Sabina Capellari and Li Song and Mark A. Smith and Bernardino Ghetti and M Ourey Sy and Pierluigi Gambetti and Robert Bob Petersen},
  journal={Journal of Alzheimer's disease : JAD},
  year={2005},
  volume={7 2},
  pages={159-71; discussion 173-80}
}
Prion diseases are associated with the accumulation of a misfolded, protease resistant form of the prion protein, PrPres. In humans there are a variety of different prion related diseases that are sporadic, inherited, or acquired by infection. Gerstmann-Straussler-Sheinker syndrome (GSS) is an inherited prion disease in which PrPres accumulates as amorphous… CONTINUE READING