Abstract
Prions are composed largely, if not entirely, of an abnormal isoform of the prion protein (PrP) designated PrPSc. A protease resistant polypeptide, PrP 27–30, can be derived from PrPSc by limited proteolysis with retention of infectivity. Both PrPSc and the cellular isoform PrPC are encoded by a chromosomal gene; PrPSc is produced from the cellular isoform by a posttranslational process (for review see Prusiner, 1991).
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Riesner, D. et al. (1998). Biophysical Studies on Structure Structural Transitions and Infectivity of the Prion Protein. In: Morrison, D.R.O. (eds) Prions and Brain Diseases in Animals and Humans. NATO ASI Series, vol 295. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1896-3_23
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DOI: https://doi.org/10.1007/978-1-4899-1896-3_23
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