title: Mammalian prions: tracking the infectious entities.
abstract: Protein misfolding is central to the pathogenesis of several neurodegenerative disorders. Among these disorders, prion diseases are unique because they are transmissible. The conversion of the host-encoded GPI-anchored PrP protein into a structurally altered form is crucially associated with the infectious and neurotoxic properties of the resulting abnormal PrP. Many lines of evidence indicate that distinct aggregated forms with different size and protease resistance are produced during prion multiplication. The recent isolation of various subsets of abnormal PrP, along with the improved biochemical tools and infectivity detection assays have shed light on the diversity of abnormal PrP protein and may give insights into the features of the more infectious subsets of abnormal PrP.
authors: UMR INRA ENVT 1225, Interactions Hôte Agent Pathogène, Ecole Nationale Vétérinaire de Toulouse, France.
authors: Jimmy
authors: J
authors: Savistchenko
authors: Zaira E
authors: ZE
authors: Arellano-Anaya
authors: Olivier
authors: O
authors: Andréoletti
authors: Didier
authors: D
authors: Vilette
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