title: Structuring the puzzle of prion propagation.
abstract: Of all the prion proteins identified to date, the agent responsible for transmissible spongiform encephalopathies is one of the least characterized. Nevertheless, recent advances in the prion field should lead to important progress in our knowledge of mammalian prions. First, the demonstration that PrP aggregates generated in vitro infect animals and cause neuronal death is a considerable breakthrough. Second, new structural data provide direct insight into the structure of the infectious agent. Third, the study of yeast prions unveiled what might be the structural basis for the strain phenomena in transmissible spongiform encephalopathies.
authors.affiliation: Laboratoire d'Enzymologie et Biochimie Structurales, UPR 9063, Centre National de la Recherche Scientifique, Bâtiment 34, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France. feghiai@nimr.mrc.ac.uk
authors.forename: Frédéric
authors.initials: F
authors.lastname: Eghiaian
mesh_terms: D000818:Animals; D019281:Dimerization; D051379:Mice; D008958:Models, Molecular; D018621:PrPC Proteins / Q000737:chemistry / Q000378:metabolism*; D018620:PrPSc Proteins / Q000737:chemistry / Q000378:metabolism*; D017096:Prion Diseases / Q000378:metabolism*; D011328:Prions / Q000378:metabolism; D011487:Protein Conformation; D015003:Yeasts / Q000378:metabolism
chemical_list: D018621:PrPC Proteins; D018620:PrPSc Proteins; D011328:Prions