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• W2013112316 abstract "The protein-remodeling factor Hsp104 governs inheritance of [ PSI + ], a yeast prion formed by self-perpetuating amyloid conformers of the translation termination factor Sup35. Perplexingly, either excess or insufficient Hsp104 eliminates [ PSI + ]. In vitro, at low concentrations, Hsp104 catalyzed the formation of oligomeric intermediates that proved critical for the nucleation of Sup 35 fibrillization de novo and displayed a conformation common among amyloidogenic polypeptides. At higher Hsp104 concentrations, amyloidogenic oligomerization and contingent fibrillization were abolished. Hsp104 also disassembled mature fibers in a manner that initially exposed new surfaces for conformational replication but eventually exterminated prion conformers. These Hsp104 activities differed in their reaction mechanism and can explain [ PSI + ] inheritance patterns." @default.
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• W2013112316 date "2004-06-18" @default.
• W2013112316 modified "2023-09-23" @default.
• W2013112316 title "Hsp104 Catalyzes Formation and Elimination of Self-Replicating Sup35 Prion Conformers" @default.
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• W2013112316 doi "https://doi.org/10.1126/science.1098007" @default.
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