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- W2009603911 startingPage "2047" @default.
- W2009603911 abstract "Prions are self-propagating infectious protein isoforms. A growing number of prions have been identified in yeast, each resulting from the conversion of soluble proteins into an insoluble amyloid form. These yeast prions have served as a powerful model system for studying the causes and consequences of prion aggregation. Remarkably, a number of human proteins containing prion-like domains, defined as domains with compositional similarity to yeast prion domains, have recently been linked to various human degenerative diseases, including amyotrophic lateral sclerosis. This suggests that the lessons learned from yeast prions may help in understanding these human diseases. In this review, we examine what has been learned about the amino acid sequence basis for prion aggregation in yeast, and how this information has been used to develop methods to predict aggregation propensity. We then discuss how this information is being applied to understand human disease, and the challenges involved in applying yeast prediction methods to higher organisms." @default.
- W2009603911 created "2016-06-24" @default.
- W2009603911 creator A5067205503 @default.
- W2009603911 creator A5087578611 @default.
- W2009603911 date "2014-01-04" @default.
- W2009603911 modified "2023-10-16" @default.
- W2009603911 title "Yeast prions and human prion-like proteins: sequence features and prediction methods" @default.
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