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

Journal of Virology

Volumn 88, Issue 5, 2014, Pages 2690-2703

  Coleman, Bradley M ^a,b   Harrison, Christopher F ^a,b,d   Guo, Belinda ^a,b   Masters, Colin L ^c   Barnham, Kevin J ^a,b,c   Lawson, Victoria A ^a,c   Hill, Andrew F ^a,b,c  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

^c FLOREY INSTITUTE OF NEUROSCIENCE AND MENTAL HEALTH   (Australia)

^d UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; PRION PROTEIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BIOASSAY; CELL LINE; CELL LYSATE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; GENE CONVERSION; GENE MUTATION; HYDROPHOBICITY; LETHALITY; MOUSE; MUTATIONAL ANALYSIS; NONHUMAN; PHYSICAL CHEMISTRY; PRION DISEASE; PRION GENE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BRAIN; CELL LINE; CODON; GENE EXPRESSION; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MICE; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE HYDROLASES; PRION DISEASES; PRIONS; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEOLYSIS; PRPC PROTEINS; PRPSC PROTEINS; SEQUENCE ALIGNMENT;

EID: 84896722245     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02720-13     Document Type: Article

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