Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells.

@article{Lehmann1997BlockadeOG,
  title={Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells.},
  author={Sylvain Lehmann and David A Harris},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 34},
  pages={
          21479-87
        }
}
The conformational conversion of the prion protein, a sialoglycoprotein containing two N-linked oligosaccharide chains, from its normal form (PrPC) to a pathogenic form (PrPSc) is the central causative event in prion diseases. Although PrPSc can be generated in the absence of glycosylation, there is evidence that oligosaccharide chains may modulate the efficiency of the conversion process, and may also serve as molecular markers of diverse prion strains. In addition, mutational inactivation of… CONTINUE READING
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Alzheimer’s Disease: Biology, Diagnosis and Therapeutics

D. A. Harris, S. Lehmann
1997
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