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- W616701050 abstract "The “ protein only ” hypothesis proposes that the prion is a conformational isoform of the normal host protein PrP C and that the abnormal conformer, when introduced into the organism, causes the conversion of PrP C into a likeness of itself. PrP C is encoded by a single-copy gene (Basler et al. 1986) located on chromosome 2 in mouse ( Prnp ) and on chromosome 20 ( PRNP ) in humans. A PrP gene has been found in all vertebrates examined (Wopfner et al. 1999), including birds (Wopfner et al. 1999), amphibians (Strumbo et al. 2001), and reptiles (Simonic et al. 2000); moreover, a PrP-like gene was identified in fugu fish (Suzuki et al. 2002). Maturation of the primary translation product results in removal of an amino-terminal signal sequence of 22 amino acids, replacement of 23 amino acids at the carboxyl terminus by a glycosylphosphatidylinositol (GPI) residue, and glycosylation at two asparagine residues. Mature PrP C comprises a highly flexible amino-terminal half, made up of octapeptide repeats, and a globular domain consisting of three α-helices, one short antiparallel β-sheet, and a single disulfide bond (Riek et al. 1996Riek et al. 1997; Donne et al. 1997). Cu ++ binds both to the octapeptide region and to histidines 96 and 111 of the PrP flexible tail (Sulkowski 1992; Hornshaw et al. 1995; Brown et al. 1997b; Jackson et al. 2001). PrP C is anchored to the outer surface of the cell membrane, in cholesterol-rich microdomains or caveolae (Vey et al. 1996; Naslavsky et al. 1997), and undergoes endocytosis and recycling (Shyng et al. 1993, 1995;..." @default.
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- W616701050 date "2004-01-01" @default.
- W616701050 modified "2023-09-24" @default.
- W616701050 title "8 Knockouts, Knockins, Transgenics, and Transplants in Prion Research" @default.
- W616701050 doi "https://doi.org/10.1101/087969693.41.373" @default.
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