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Science  20 Dec 1996:
Vol. 274, Issue 5295, pp. 1983
DOI: 10.1126/science.274.5295.1983e

Prion proteins, the suspected causative agent of several inherited and infectious forms of spongiform encephalopathy in animals and humans, are abnormal conformers of host proteins. The normal host form (PrPC) has a high alpha -helical content, whereas the prion form (PrPSc) is composed mainly of beta sheets and can assume different isoforms that have protease-resistant fragments of different sizes. Telling et al. (p. 2079; see the news story by Grady, p. 2010) show that extracts from brains of human patients with prion-associated diseases could induce neurodegeneration in transgenic mice that express the human form of PrP. Moreover, the protease-resistant fragments were of the size characteristic for the human disease. These results indicate that the presence of the PrpSc form redirects folding of the PrP protein and may help to explain how different strains of these proteins could arise and propagate.

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