Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro.

@article{Dear2007EffectsOP,
  title={Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro.},
  author={D. V. Anderson Dear and Duncan S Young and Jurate Kazlauskaite and Filip Meersman and David Oxley and Judith M. Webster and Teresa T. J. Pinheiro and A. Christina Gill and Igor Bronstein and Christopher Robin Lowe},
  journal={Biochimica et biophysica acta},
  year={2007},
  volume={1774 7},
  pages={792-802}
}
Prion diseases, or transmissible spongiform encephalopathies (TSEs) are typically characterised by CNS accumulation of PrP(Sc), an aberrant conformer of a normal cellular protein PrP(C). It is thought PrP(Sc) is itself infectious and the causative agent of such diseases. To date, no chemical modifications of PrP(Sc), or a sub-population thereof, have been reported. In this study we have investigated whether chemical modification of amino acids within PrP might cause this protein to exhibit… CONTINUE READING