Prions as Protein-Based Genetic Elements
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References (184)
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Structure of the Globular Region of the Prion Protein Ure2 from the Yeast Saccharomyces cerevisiae
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Genetic Study of Interactions Between the Cytoskeletal Assembly Protein Sla1 and Prion-Forming Domain of the Release Factor Sup35 (eRF3) in Saccharomyces cerevisiae
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Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions
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The HET-s Prion Protein of the Filamentous Fungus Podospora anserina Aggregates in Vitro into Amyloid-like Fibrils
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Two Prion-Inducing Regions of Ure2p Are Nonoverlapping
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Self-assembly properties of a model RING domain
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The C‐terminus of eRF1 defines a functionally important domain for translation termination inSaccharomyces cerevisiae
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Equilibrium folding properties of the yeast prion protein determinant Ure2 1 1Edited by J. Karn
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The prion domain of yeast Ure2P induces autocatalytic formation of amyloid fibers by a recombinant fusion protein
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The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele
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The Utility of Prions
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A protein required for prion generation: [URE3] induction requires the Ras-regulated Mks1 protein
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