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- W2023595610 endingPage "803" @default.
- W2023595610 startingPage "789" @default.
- W2023595610 abstract "Prions are infectious proteins. Several prions have been identified in fungi where they behave as non-Mendelian cytoplasmic genetic elements. Most of these prions propagate as self-perpetuating amyloid aggregates thus providing an example of structural heredity. In yeast, prion propagation requires the Hsp104 disaggregase presumably to sheer amyloid assemblies and generate more fiber ends. Recent work in yeast shows that amyloid structure polymorphism underlies the prion strain phenomenon and influences species barriers. Structural models for the amyloid form of several fungal prion proteins are now available. All propose a cross β-organization with parallel β-sheets. Whether or not some of the fungal prions might be beneficial to their host is still a debated issue." @default.
- W2023595610 created "2016-06-24" @default.
- W2023595610 creator A5051607758 @default.
- W2023595610 creator A5076009017 @default.
- W2023595610 date "2006-12-01" @default.
- W2023595610 modified "2023-09-27" @default.
- W2023595610 title "Prion proteins as genetic material in fungi" @default.
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