Article
Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.
Proceedings of the National Academy of Sciences of the United States of America - 31 Aug 2004
Derkatch Irina L, Uptain Susan M, Outeiro Tiago F, Krishnan Rajaraman, Lindquist Susan L, Liebman Susan W
Abstract excerpt
Prions are infectious protein conformations that are generally ordered protein aggregates. In the absence of prions, newly synthesized molecules of these same proteins usually maintain a conventional soluble conformation. However, prions occasionally arise even without a homologous prion template. The conformational switch that results in the de novo appearance of yeast prions with glutamine/aspargine (Q/N)-rich...
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