Prion protein aggregation reverted by low temperature in transfected cells carrying a prion protein gene mutation.

@article{Singh1997PrionPA,
  title={Prion protein aggregation reverted by low temperature in transfected cells carrying a prion protein gene mutation.},
  author={Neena Singh and Gianluigi Zanusso and Shu Guang Chen and Hisashi Fujioka and S. Richardson and Pierluigi Gambetti and Robert Bob Petersen},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 45},
  pages={28461-70}
}
Prion diseases are characterized by the conversion of the normal cellular prion protein (PrPC), a glycoprotein that is anchored to the cell membrane by a glycosylphosphatidylinositol moiety, into an isoform that is protease-resistant (PrPres) and pathogenic. In inherited prion diseases, mutations in the prion protein (PrPM) engender the conversion of PrPM into PrPres. We developed a cell model of Gerstmann-Sträussler-Scheinker disease, a neurodegenerative condition characterized by PrPM… CONTINUE READING