Prions
Author(s) -
Dmitry Kryndushkin,
Herman K. Edskes,
Frank Shewmaker,
Reed B. Wickner
Publication year - 2017
Publication title -
cold spring harbor protocols
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.674
H-Index - 51
eISSN - 1940-3402
pISSN - 1559-6095
DOI - 10.1101/pdb.top077586
Subject(s) - computer science , computational biology , biology
Infectious proteins (prions) are usually self-templating filamentous protein polymers (amyloids). Yeast prions are genes composed of protein and, like the multiple alleles of DNA-based genes, can have an array of “variants,” each a distinct self-propagating amyloid conformation. Like the lethal mammalian prions and amyloid diseases, yeast prions may be lethal, or only mildly detrimental, and show an array of phenotypes depending on the protein involved and the prion variant. Yeast prions are models for both rare mammalian prion diseases and for several very common amyloidoses such as Alzheimer’s disease, type 2 diabetes, and Parkinson’s disease. Here, we describe their detection and characterization using genetic, cell biological, biochemical, and physical methods.
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