E
Evgeny E. Bezsonov
Researcher at National Institutes of Health
Publications - 27
Citations - 330
Evgeny E. Bezsonov is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 7, co-authored 11 publications receiving 234 citations.
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Journal ArticleDOI
Yeast Prions: Structure, Biology, and Prion-Handling Systems
Reed B. Wickner,Frank Shewmaker,David A. Bateman,Herman K. Edskes,Anton Gorkovskiy,Yaron Dayani,Evgeny E. Bezsonov +6 more
TL;DR: The mechanism of faithful templating of protein conformation, the biological roles of these prions, and their interactions with cellular chaperones, the Btn2 and Cur1 aggregate-handling systems, and other cellular factors governing prion generation and propagation are reviewed.
Journal ArticleDOI
Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants.
TL;DR: It is found that most [URE3] variants generated in a btn2 cur1 double mutant are cured by restoring normal levels of Btn2p and Cur1p, with both proteins needed for efficient curing.
Journal ArticleDOI
[PSI+] prion propagation is controlled by inositol polyphosphates
TL;DR: It is shown that certain inositol polyphosphates and pyrophosphates promote the propagation of the [PSI+] prion and that an inositl pyroph phosphate pyphosphatase has an antiprion effect.
Journal ArticleDOI
Yeast Prions Compared to Functional Prions and Amyloids.
Reed B. Wickner,Herman K. Edskes,Moonil Son,Evgeny E. Bezsonov,Morgan Dewilde,Mathieu Ducatez +5 more
TL;DR: Amyloid-based yeast prions are rare in wild strains, arise sporadically, have an array of prion variants for a single prion protein sequence, have a folded in-register parallel β-sheet amyloid architecture, are detrimental to their hosts, arouse a stress response in the host, and are subject to curing by various host anti-prion systems.
Book ChapterDOI
Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology
TL;DR: The beneficial [Het-s] prion of Podospora anserina poses an important contrast in its structure, biology, and evolution to the yeast prions characterized thus far.