Tricia R. Serio
Affiliations: | University of Massachusetts, Amherst, Amherst, MA |
Area:
Genetics, Molecular BiologyGoogle:
"Tricia Serio"Parents
Sign in to add mentor| Susan L. Lindquist | grad student | (FlyTree) | |
| I. George Miller | grad student | Yale |
Children
Sign in to add trainee| Afua Adusei | grad student | U Mass Amherst | |
| Teal Brechtel | grad student | University of Arizona | |
| Suzanne DiSalvo | grad student | Brown | |
| Xuezhen Ge | grad student | University of Arizona | |
| William Holmes | grad student | Brown | |
| Courtney Klaips | grad student | Brown | |
| Christine Langlois | grad student | Brown | |
| Jennifer Norton | grad student | University of Arizona | |
| Fen Pei | grad student | University of Arizona | |
| Janice Villali | grad student | Brown | |
| Prasanna Satpute-Krishnan | grad student | 2007 | Brown |
| Martina Strbuncelj | grad student | 2009 | Brown |
| Aaron M. Derdowski | post-doc | Brown (Microtree) | |
| Wes Naeimi | post-doc | U Mass Amherst | |
| John A. Pezza | post-doc | U Mass Amherst | |
| Nicole E. Seah | research scientist | U Mass Amherst (Chemistry Tree) |
BETA: Related publications
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Publications
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| Naeimi WR, Serio TR. (2022) Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures. Viruses. 14 |
| Villali J, Dark J, Brechtel TM, et al. (2020) Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast. Nature Structural & Molecular Biology |
| Serio TR. (2018) [PIN+]ing down the mechanism of prion appearance. Fems Yeast Research. 18 |
| Pei F, DiSalvo S, Sindi SS, et al. (2017) A dominant-negative mutant inhibits multiple prion variants through a common mechanism. Plos Genetics. 13: e1007085 |
| Banks HT, Flores KB, Langlois CR, et al. (2017) Estimating the rate of prion aggregate amplification in yeast with a generation and structured population model Inverse Problems in Science and Engineering. 26: 257-279 |
| Langlois CR, Pei F, Sindi SS, et al. (2016) Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo. Plos Genetics. 12: e1006417 |
| Klaips CL, Hochstrasser ML, Langlois CR, et al. (2015) Correction: Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing. Elife. 4: e06494 |
| Klaips CL, Hochstrasser ML, Langlois CR, et al. (2014) Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing. Elife. 3 |
| Pezza JA, Villali J, Sindi SS, et al. (2014) Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype. Nature Communications. 5: 4384 |
| Holmes WM, Mannakee BK, Gutenkunst RN, et al. (2014) Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding. Nature Communications. 5: 4383 |