Macromolecular crowding converts the human recombinant PrPC to the soluble neurotoxic beta-oligomers.

@article{Huang2010MacromolecularCC,
  title={Macromolecular crowding converts the human recombinant PrPC to the soluble neurotoxic beta-oligomers.},
  author={Liqin Huang and Rui Jin and Jiarui Li and Kan Luo and Tao Huang and Di Wu and Wenxi Wang and Rui Chen and Gengfu Xiao},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2010},
  volume={24 9},
  pages={3536-43}
}
Prion diseases are fatal neurodegenerative disorders and are linked with the conversion of the cellular isoform of the prion protein (PrP(C)) into the abnormal beta-sheet-rich isoform. It is widely accepted that the soluble oligomers of beta-PrP are neurotoxic and that they are more pathologically significant. To unravel the molecular mechanism under the conversion process, it is critical to identify the factors that can promote the conversion from PrP(C) to the beta-oligomers. By recording… CONTINUE READING

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