The [URE3] yeast prion results from protein aggregates that differ from amyloid filaments formed in vitro

Journal of Biological Chemistry

Volumn 279, Issue 49, 2004, Pages 50962-50968

  Ripaud, Leslie ^a   Maillet, Laurent ^a   Immel Torterotot, Françoise ^a   Durand, Fabien ^a   Cullin, Christophe ^a  

^a Institut de Biochimie et Genetique Cellulaires   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; CELLS; STRAIN; YEAST;

NITROGEN CATABOLITE REPRESSION; PROTEASE; PROTEOLYSIS; VITRO;

PROTEINS;

AMYLOID; ANAZOLENE SODIUM; FUNGAL PROTEIN; PROTEIN URE2P; PROTEIN URE3; PROTEINASE; UNCLASSIFIED DRUG; UREA;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; IN VITRO STUDY; NONHUMAN; PRION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DEGRADATION; SPECIES DIFFERENCE; STAINING; WESTERN BLOTTING; WILD TYPE; YEAST;

AMYLOID; BLOTTING, WESTERN; CLONING, MOLECULAR; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPEPTIDASE K; ESCHERICHIA COLI; MICROSCOPY, ELECTRON; OPEN READING FRAMES; PEPTIDES; PLASMIDS; PRIONS; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TEMPERATURE; TIME FACTORS; UREA;

EID: 10944222210     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M408792200     Document Type: Article

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