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Tricia R. Serio - Publications

Affiliations: 
University of Massachusetts, Amherst, Amherst, MA 
Area:
Genetics, Molecular Biology
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33 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2024 Norton J, Seah N, Santiago F, Sindi SS, Serio TR. Multiple aspects of amyloid dynamics integrate to establish prion variant dominance in yeast. Frontiers in Molecular Neuroscience. 17: 1439442. PMID 39139213 DOI: 10.3389/fnmol.2024.1439442  0.82
2022 Naeimi WR, Serio TR. Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures. Viruses. 14. PMID 35893700 DOI: 10.3390/v14081635  0.392
2020 Villali J, Dark J, Brechtel TM, Pei F, Sindi SS, Serio TR. Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast. Nature Structural & Molecular Biology. PMID 32367069 DOI: 10.1038/S41594-020-0416-6  0.773
2018 Serio TR. [PIN+]ing down the mechanism of prion appearance. Fems Yeast Research. 18. PMID 29718197 DOI: 10.1093/Femsyr/Foy026  0.619
2017 Pei F, DiSalvo S, Sindi SS, Serio TR. A dominant-negative mutant inhibits multiple prion variants through a common mechanism. Plos Genetics. 13: e1007085. PMID 29084237 DOI: 10.1371/Journal.Pgen.1007085  0.819
2017 Banks HT, Flores KB, Langlois CR, Serio TR, Sindi SS. 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. DOI: 10.1080/17415977.2017.1316498  0.777
2016 Langlois CR, Pei F, Sindi SS, Serio TR. Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo. Plos Genetics. 12: e1006417. PMID 27814358 DOI: 10.1371/Journal.Pgen.1006417  0.831
2015 Klaips CL, Hochstrasser ML, Langlois CR, Serio TR. Correction: Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing. Elife. 4: e06494. PMID 25626954 DOI: 10.7554/Elife.06494  0.742
2014 Klaips CL, Hochstrasser ML, Langlois CR, Serio TR. Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing. Elife. 3. PMID 25490068 DOI: 10.7554/Elife.04288  0.811
2014 Pezza JA, Villali J, Sindi SS, Serio TR. Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype. Nature Communications. 5: 4384. PMID 25023996 DOI: 10.1038/Ncomms5384  0.828
2014 Holmes WM, Mannakee BK, Gutenkunst RN, Serio TR. Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding. Nature Communications. 5: 4383. PMID 25023910 DOI: 10.1038/Ncomms5383  0.699
2014 Holmes WM, Klaips CL, Serio TR. Defining the limits: Protein aggregation and toxicity in vivo Critical Reviews in Biochemistry and Molecular Biology. 49: 294-303. PMID 24766537 DOI: 10.3109/10409238.2014.914151  0.84
2014 Brodsky JL, Merz A, Serio T. Organelle and proteome quality control mechanisms: how cells are able to keep calm and carry on. Molecular Biology of the Cell. 25: 733-4. PMID 24626847 DOI: 10.1091/Mbc.E13-11-0672  0.522
2011 DiSalvo S, Serio TR. Insights into prion biology: integrating a protein misfolding pathway with its cellular environment. Prion. 5: 76-83. PMID 21654204 DOI: 10.4161/Pri.5.2.16413  0.869
2011 DiSalvo S, Derdowski A, Pezza JA, Serio TR. Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation. Nature Structural & Molecular Biology. 18: 486-92. PMID 21423195 DOI: 10.1038/Nsmb.2031  0.807
2011 Tuite MF, Serio TR. Conformational conversion and prion disease: authors' reply Nature Reviews Molecular Cell Biology. 12: 273-273. DOI: 10.1038/Nrm3007-C2  0.409
2010 Tuite MF, Serio TR. The prion hypothesis: from biological anomaly to basic regulatory mechanism. Nature Reviews. Molecular Cell Biology. 11: 823-33. PMID 21081963 DOI: 10.1038/Nrm3007  0.412
2010 Derdowski A, Sindi SS, Klaips CL, DiSalvo S, Serio TR. A size threshold limits prion transmission and establishes phenotypic diversity. Science (New York, N.Y.). 330: 680-3. PMID 21030659 DOI: 10.1126/Science.1197785  0.797
2009 Sindi SS, Serio TR. Prion dynamics and the quest for the genetic determinant in protein-only inheritance. Current Opinion in Microbiology. 12: 623-30. PMID 19864176 DOI: 10.1016/J.Mib.2009.09.003  0.512
2009 Pezza JA, Langseth SX, Raupp Yamamoto R, Doris SM, Ulin SP, Salomon AR, Serio TR. The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype. Molecular Biology of the Cell. 20: 1068-80. PMID 19073888 DOI: 10.1091/Mbc.E08-04-0436  0.832
2007 Pezza JA, Serio TR. Prion propagation: the role of protein dynamics. Prion. 1: 36-43. PMID 19164914 DOI: 10.4161/Pri.1.1.3992  0.791
2007 Satpute-Krishnan P, Langseth SX, Serio TR. Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance. Plos Biology. 5: e24. PMID 17253904 DOI: 10.1371/Journal.Pbio.0050024  0.839
2005 Satpute-Krishnan P, Serio TR. Prion protein remodelling confers an immediate phenotypic switch. Nature. 437: 262-5. PMID 16148935 DOI: 10.1038/Nature03981  0.849
2001 Serio TR, Lindquist SL. The yeast prion [PSI+]: molecular insights and functional consequences. Advances in Protein Chemistry. 59: 391-412. PMID 11868278 DOI: 10.1016/S0065-3233(01)59012-9  0.641
2001 Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Lindquist SL. Self-perpetuating changes in Sup35 protein conformation as a mechanism of heredity in yeast. Biochemical Society Symposium. 35-43. PMID 11573346 DOI: 10.1042/Bst028A050C  0.729
2001 Serio TR, Lindquist SL. [PSI+], SUP35, and chaperones. Advances in Protein Chemistry. 57: 335-66. PMID 11447696 DOI: 10.1016/S0065-3233(01)57027-8  0.661
2000 Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Serpell L, Arnsdorf MF, Lindquist SL. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science (New York, N.Y.). 289: 1317-21. PMID 10958771 DOI: 10.1126/Science.289.5483.1317  0.695
2000 Serio TR, Lindquist SL. Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends in Cell Biology. 10: 98-105. PMID 10675903 DOI: 10.1016/S0962-8924(99)01711-0  0.66
2000 Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Lindquist SL. Self-Perpetuating Changes in Sup35 Protein Conformation as A mechanism of Heredity in Yeast Biochemical Society Transactions. 28: A50-A50. DOI: 10.1042/bst028a050c  0.397
1999 Serio TR, Lindquist SL. [PSI+]: an epigenetic modulator of translation termination efficiency. Annual Review of Cell and Developmental Biology. 15: 661-703. PMID 10611975 DOI: 10.1146/Annurev.Cellbio.15.1.661  0.634
1999 Serio TR, Cashikar AG, Moslehi JJ, Kowal AS, Lindquist SL. Yeast prion [psi +] and its determinant, Sup35p. Methods in Enzymology. 309: 649-73. PMID 10507053 DOI: 10.1016/S0076-6879(99)09043-6  0.614
1998 Lindquist S, DebBurman SK, Glover JR, Kowal AS, Liu JJ, Schirmer EC, Serio TR. Amyloid fibres of Sup35 support a prion-like mechanism of inheritance in yeast. Biochemical Society Transactions. 26: 486-90. PMID 9765901 DOI: 10.1042/Bst0260486  0.806
1996 Serio TR, Angelont A, Kolman JL, Gradoville L, Sun R, Katz DA, Van Grunsven W, Middeldorp J, Miller G. Two 21-kilodalton components of the Epstein-Barr virus capsid antigen complex and their relationship to ZEBRA-associated protein p21 (ZAP21) Journal of Virology. 70: 8047-8054. PMID 8892929 DOI: 10.1128/Jvi.70.11.8047-8054.1996  0.317
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