Indexed keywords
AMYLOID PROTEIN;
TRANSLATION TERMINATION FACTOR;
HEREDITY;
IN VITRO STUDY;
MUTATION;
NONSENSE MUTATION;
NOTE;
PRION;
PRIORITY JOURNAL;
PROTEIN AGGREGATION;
PROTEIN DEPLETION;
PROTEIN DOMAIN;
PROTEIN EXPRESSION;
PROTEIN STRUCTURE;
SACCHAROMYCES CEREVISIAE;
SEQUENCE ANALYSIS;
TRANSLATION REGULATION;
AMINO ACID SEQUENCE;
CYTOPLASM;
FUNGAL PROTEINS;
GENE EXPRESSION REGULATION, FUNGAL;
HUMANS;
MOLECULAR SEQUENCE DATA;
MUTATION;
PRION DISEASES;
PRIONS;
SACCHAROMYCES CEREVISIAE;
SACCHAROMYCES CEREVISIAE PROTEINS;
SACCHAROMYCES CEREVISIAE;
1
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Prion-inducing domain 2–114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
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Evidence for a prion analog in S. cerevisiae: the [URE3] non-Mendelian genetic element as an altered URE2 protein
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The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [PSI+] in the yeast Saccharomyces cerevisiae
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Multicopy SUP35 gene induces de novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae
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The dominant PNM2− mutation which eliminates the Y factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene
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A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
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Oligopeptide-repeat expansions modulate ‘protein-only’ inheritance in yeast
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Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
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Mechanism of inhibition of [PSI+] prion determinant propagation by a mutation of the N-terminus of the yeast Sup35 protein
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Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells
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In vitro propagation of the prion-like state of yeast Sup35 protein
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Trinucleotide repeat length instability and age of onset in Huntington’s disease
M. Duyao Trinucleotide repeat length instability and age of onset in Huntington’s disease Nat. Genet. 4 1993 387 392
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