Yeast prions, mammalian amyloidoses, and the problem of proteomic networks |
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Authors: | A. P. Galkin L. N. Mironova G. A. Zhuravleva S. G. Inge-Vechtomov |
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Affiliation: | (1) Department of Genetics and Breeding, St. Petersburg State University, St. Petersburg, 199034, Russia;(2) St. Petersburg Branch, Vavilov Institute of General Genetics, Russian Academy of Sciences, St. Petersburg, 199034, Russia |
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Abstract: | ![]() Prion proteins are infective amyloids and cause several neurodegenerative diseases in humans and animals. In yeasts, prions are detected as the cytoplasmic heritable determinants of a protein nature. Yeast prion [PSI], which results from a conformational rearrangement and oligomerization of translation termination factor eRF3, is used as an example to consider the structural-functional relationships in a potentially prion molecule, specifics of its evolution, and interactions with other prions, which form so-called prion networks. In addition, the review considers the results of modeling mammalian prion diseases and other amyloidoses in yeast cells. A hypothesis of proteomic networks is proposed by analogy with prion networks, involving interactions of different amyloids in mammals. |
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