| Literature DB >> 30710020 |
Abstract
Yeast prions have become important models for the study of the basic mechanisms underlying human amyloid diseases. Yeast prions are pathogenic (unlike the [Het-s] prion of Podospora anserina), and most are amyloid-based with the same in-register parallel β-sheet architecture as most of the disease-causing human amyloids studied. Normal yeast cells eliminate the large majority of prion variants arising, and several anti-prion/anti-amyloid systems that eliminate them have been identified. It is likely that mammalian cells also have anti-amyloid systems, which may be useful in the same way humoral, cellular, and innate immune systems are used to treat or prevent bacterial and viral infections.Entities:
Keywords: Btn2; Cur1; Hsp104; Siw14; Upf proteins; [PSI+]; [URE3]; amyloid; chaperone; in-register parallel; innate immunity; inositol phosphate; prion
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Year: 2019 PMID: 30710020 PMCID: PMC6364766 DOI: 10.1074/jbc.TM118.004168
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157