Trehalose impairs aggregation of PrPSc molecules and protects prion-infected cells against oxidative damage.

@article{Branger2008TrehaloseIA,
  title={Trehalose impairs aggregation of PrPSc molecules and protects prion-infected cells against oxidative damage.},
  author={Florence B{\'e}ranger and Carole A Crozet and Andrew Simon Goldsborough and Sylvain Lehmann},
  journal={Biochemical and biophysical research communications},
  year={2008},
  volume={374 1},
  pages={
          44-8
        }
}
Neurodegenerative disorders such as Alzheimer's, Huntington's, and prion diseases are characterized by abnormal protein deposits in the brain of affected patients. In prion diseases, a key event in the pathogenesis is the conversion of the normal prion protein (PrP(c)) into abnormal protease resistant PrP(Sc) deposits, a phenomenon associated with a higher sensitivity to oxidative stress in vitro. In cellular models of Alzheimer and Huntington diseases, the disaccharide trehalose has been shown… CONTINUE READING
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