Prions are the greatest protein misfolding problem, and yeast has several solutions von Wickner, Reed B, Edskes, Herman K, Wu, Songsong, Gregg, Kristen

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Prions of fungi: inherited structures and biological roles von Wickner, Reed B, Edskes, Herman K, Shewmaker, Frank, Nakayashiki, Toru

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Prion Variants of Yeast are Numerous, Mutable, and Segregate on Growth, Affecting Prion Pathogenesis, Transmission Barriers, and Sensitivity to Anti-Prion Systems von Wickner, Reed B, Son, Moonil, Edskes, Herman K

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Yeast prions [URE3] and [PSI+] are diseases von Nakayashiki, T, Kurtzman, C.P, Edskes, H.K, Wickner, R.B

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Anti-Prion Systems Block Prion Transmission, Attenuate Prion Generation, Cure Most Prions as They Arise and Limit Prion-Induced Pathology in Saccharomyces cerevisiae von Wickner, Reed B., Edskes, Herman K., Son, Moonil, Wu, Songsong

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Primary sequence independence for prion formation von Ross, E.D, Edskes, H.K, Terry, M.J, Wickner, R.B

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Yeast killer elements hold their hosts hostage von Wickner, Reed B, Edskes, Herman K

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Human proteins curing yeast prions von Wu, Songsong, Edskes, Herman K, Wickner, Reed B

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Interactions among Prions and Prion "Strains" in Yeast von Bradley, Michael E., Edskes, Herman K., Hong, Joo Y., Wickner, Reed B., Liebman, Susan W.

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The [URE3] Prion in Candida von Edskes, Herman K, Wickner, Reed B

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Hermes Transposon Mutagenesis Shows [URE3] Prion Pathology Prevented by a Ubiquitin-Targeting Protein: Evidence for Carbon/Nitrogen Assimilation Cross Talk and a Second Function fo... von Edskes, Herman K, Mukhamedova, Maryam, Edskes, Bouke K, Wickner, Reed B

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Yeast prions: proteins templating conformation and an anti-prion system von Wickner, Reed B, Edskes, Herman K, Bateman, David A, Gorkovskiy, Anton, Dayani, Yaron, Bezsonov, Evgeny E, Mukhamedova, Maryam

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Yeast prions: structure, biology, and prion-handling systems von Wickner, Reed B, Shewmaker, Frank P, Bateman, David A, Edskes, Herman K, Gorkovskiy, Anton, Dayani, Yaron, Bezsonov, Evgeny E

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Innate immunity to yeast prions: Btn2p and Cur1p curing of the [URE3] prion is prevented by 60S ribosomal protein deficiency or ubiquitin/proteasome system overactivity von Bezsonov, Evgeny E, Edskes, Herman K, Wickner, Reed B

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[PSI+] prion propagation is controlled by inositol polyphosphates von Wickner, Reed B., Kelly, Amy C., Bezsonov, Evgeny E., Edskes, Herman K.

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Yeast Prions Compared to Functional Prions and Amyloids von Wickner, Reed B., Edskes, Herman K., Son, Moonil, Bezsonov, Evgeny E., DeWilde, Morgan, Ducatez, Mathieu

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How Do Yeast Cells Contend with Prions? von Wickner, Reed B, Edskes, Herman K, Son, Moonil, Wu, Songsong, Niznikiewicz, Madaleine

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Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip von Wickner, Reed B., Edskes, Herman K., Son, Moonil, Wu, Songsong, Niznikiewicz, Madaleine

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The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments von Edskes, H.K. (NIH, Bethesda, MD.), Gray, V.T, Wickner, R.B

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Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae von Edskes, Herman K, Stroobant, Emily E, DeWilde, Morgan P, Bezsonov, Evgeny E, Wickner, Reed B

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