Autori: Surewicz WK, Jones EM, Apetri AC.

Editorial: American Chemical Society, Acc Chem Res. (review), 39(9), p.654-62, 2006.

Rezumat:

Self-perpetuating conformational conversion of the cellular prion protein PrP(C) into the beta-sheet-rich „scrapie” conformer (PrP(Sc)) is believed to be the central molecular event in pathogenesis of a group of diseases known as transmissible spongiform encephalopathies. Recent advances provide growing support for the notion that a misfolded protein alone might act as an infectious agent. Furthermore, findings regarding the mechanism of prion protein structural rearrangement, the role of folding intermediates in conformational conversion, and „conformational adaptability” in the propagation of prion amyloids in vitro yield molecular-level insight into such phenomena as inherited prion diseases, prion transmission barriers, and prion strains.

Cuvinte cheie: prion diseases, conversion mechanism, amyloid fibers

URL: http://pubs.acs.org/cgi-bin/article.cgi/achre4/2006/39/i09/pdf/ar050226c.pdf