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| http://purl.uniprot.org/citations/22482457 | http://www.w3.org/2000/01/rdf-schema#comment | "For both mammalian and fungal prion proteins, conformational templating drives the phenomenon of protein-only infectivity. The conformational conversion of a protein to its transmissible prion state is associated with changes to host cellular physiology. In mammals, this change is synonymous with disease, whereas in fungi no notable detrimental effect on the host is typically observed. Instead, fungal prions can serve as epigenetic regulators of inheritance in the form of partial loss-of-function phenotypes. In the presence of environmental challenges, the prion state [PRION(+)], with its resource for phenotypic plasticity, can be associated with a growth advantage. The growing number of yeast proteins that can switch to a heritable [PRION(+)] form represents diverse and metabolically penetrating cellular functions, suggesting that the [PRION(+)] state in yeast is a functional one, albeit rarely found in nature. In this chapter, we introduce the biochemical and genetic properties of fungal prions, many of which are shared by the mammalian prion protein PrP, and then outline the major contributions that studies on fungal prions have made to prion biology."xsd:string |
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| http://purl.uniprot.org/citations/22482457 | http://purl.uniprot.org/core/author | "Tuite M.F."xsd:string |
| http://purl.uniprot.org/citations/22482457 | http://purl.uniprot.org/core/author | "Staniforth G.L."xsd:string |
| http://purl.uniprot.org/citations/22482457 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22482457 | http://purl.uniprot.org/core/name | "Prog Mol Biol Transl Sci"xsd:string |
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| http://purl.uniprot.org/citations/22482457 | http://purl.uniprot.org/core/title | "Fungal prions."xsd:string |
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