Wild-type Shadoo proteins convert to amyloid-like forms under native conditions

Journal of Neurochemistry

Volumn 113, Issue 1, 2010, Pages 92-104

  Daude, Nathalie ^a   Ng, Vivian ^b   Watts, Joel C ^b   Genovesi, Sacha ^a   Glaves, John Paul ^c   Wohlgemuth, Serene ^a   Schmitt Ulms, Gerold ^b   Young, Howard ^c   McLaurin, Joanne ^b   Fraser, Paul E ^b   Westaway, David ^a,c  

^a UNIVERSITY OF ALBERTA   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Fibrils; Hydrophobic domain; Misfolding; Prions; Protease resistant

Indexed keywords

AMYLOID; ARGININE; CARBOHYDRATE; CONGO RED; DODECYL SULFATE SODIUM; GLYCOPROTEIN; MUTANT PROTEIN; PROTEIN SHADOO; PROTEINASE K; RECOMBINANT PROTEIN; THIOFLAVINE; UNCLASSIFIED DRUG;

ACIDIFICATION; AMINO ACID SEQUENCE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DNA POLYMORPHISM; ELECTRON MICROSCOPY; GENE DELETION; GENE INSERTION; HYDROPHOBICITY; MOUSE; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; TANDEM REPEAT; WILD TYPE;

AMINO ACID SEQUENCE; AMYLOID; ANIMALS; CONGO RED; CULTURE MEDIA, CONDITIONED; ENDOPEPTIDASE K; MICE; MICROSCOPY, ELECTRON, TRANSMISSION; NERVE TISSUE PROTEINS; NEUROBLASTOMA; PEPTIDE FRAGMENTS; PRIONS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PRPC PROTEINS; SHEEP; TRANSFECTION;

OVIS ARIES;

EID: 77749264931     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.06575.x     Document Type: Article

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