title: Mammalian prion proteins.
abstract: The past two years have seen the extension of our knowledge on the cellular prion protein structure with new NMR data on both the hamster and human proteins. In addition, the folding dynamics of two cellular prion proteins have been elucidated. There are now several examples of recombinant prion proteins that are able to adopt different conformations in solution and recent work on the molecular basis of prion strains has done much to consolidate the protein-only hypothesis. Important advances in relating disease to structure have also been made through the identification of the minimal prion protein fragment that is capable of conferring susceptibility to and propagation of the scrapie agent.
authors.affiliation: Department of Neurogenetics, Medical Research Council Prion Unit, Imperial College School of Medicine at St. Mary's, Norfolk Place Paddington, London, W2 1PG, UK.
authors.forename: G S
authors.initials: GS
authors.lastname: Jackson
authors.forename: A R
authors.initials: AR
authors.lastname: Clarke
mesh_terms: D000818:Animals; D001704:Biopolymers; D016923:Cell Death; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D007562:Creutzfeldt-Jakob Syndrome / Q000209:etiology / Q000378:metabolism; D016643:Encephalopathy, Bovine Spongiform / Q000209:etiology / Q000378:metabolism / Q000635:transmission; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008322:Mammals / Q000235:genetics / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D018621:PrPC Proteins / Q000737:chemistry / Q000378:metabolism; D018620:PrPSc Proteins / Q000737:chemistry / Q000378:metabolism; D017096:Prion Diseases / Q000209:etiology / Q000378:metabolism; D011328:Prions / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D001704:Biopolymers; D018621:PrPC Proteins; D018620:PrPSc Proteins; D011328:Prions