Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality.

Coleman, Bradley M; Harrison, Christopher F; Guo, Belinda; Masters, Colin L; Barnham, Kevin J; Lawson, Victoria A; Hill, Andrew F

Coleman, Bradley M; Harrison, Christopher F; Guo, Belinda; Masters, Colin L; Barnham, Kevin J; Lawson, Victoria A; Hill, Andrew F.

Affiliation

Coleman BM; Department of Biochemistry & Molecular Biology, The University of Melbourne, Parkville, Victoria, Australia.

J Virol ; 88(5): 2690-703, 2014 Mar.

Article in En | MEDLINE | ID: mdl-24352465

Subject(s)

Mutation; Prions/genetics; Prions/metabolism; Protein Interaction Domains and Motifs; Amino Acid Sequence; Amino Acid Substitution; Animals; Brain/metabolism; Brain/pathology; Cell Line; Codon; Gene Expression; Humans; Hydrophobic and Hydrophilic Interactions; Mice; Molecular Sequence Data; Peptide Hydrolases/metabolism; PrPC Proteins/chemistry; PrPC Proteins/genetics; PrPC Proteins/metabolism; PrPSc Proteins/chemistry; PrPSc Proteins/genetics; PrPSc Proteins/metabolism; Prion Diseases/genetics; Prion Diseases/metabolism; Prion Diseases/pathology; Prions/chemistry; Proteolysis; Sequence Alignment

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Full text: 1 Database: MEDLINE Main subject: Prions / Protein Interaction Domains and Motifs / Mutation Type of study: Diagnostic_studies / Prognostic_studies Limits: Animals / Humans Language: En Journal: J Virol Year: 2014 Type: Article Affiliation country: Australia

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