10.1534/genetics.111.137760
Crossref journal-article
Oxford University Press (OUP)
Genetics (286)
Abstract

AbstractThe concept of a prion as an infectious self-propagating protein isoform was initially proposed to explain certain mammalian diseases. It is now clear that yeast also has heritable elements transmitted via protein. Indeed, the “protein only” model of prion transmission was first proven using a yeast prion. Typically, known prions are ordered cross-β aggregates (amyloids). Recently, there has been an explosion in the number of recognized prions in yeast. Yeast continues to lead the way in understanding cellular control of prion propagation, prion structure, mechanisms of de novo prion formation, specificity of prion transmission, and the biological roles of prions. This review summarizes what has been learned from yeast prions.

Bibliography

Liebman, S. W., & Chernoff, Y. O. (2012). Prions in Yeast. Genetics, 191(4), 1041–1072.

Authors 2
  1. Susan W Liebman (first)
  2. Yury O Chernoff (additional)
References 328 Referenced 351
  1. 10.1074/jbc.M110.183889 / J. Biol. Chem. / Molecular basis for transmission barrier and interference between closely related prion proteins in yeast by Afanasieva (2011)
  2. 10.1126/science.1080418 / Science / Asymmetric inheritance of oxidatively damaged proteins during cytokinesis by Aguilaniu (2003)
  3. 10.1038/nrd3050 / Nat. Rev. Drug Discov. / Protein aggregation diseases: pathogenicity and therapeutic perspectives by Aguzzi (2010)
  4. 10.1016/j.neuron.2009.12.016 / Neuron / The transcellular spread of cytosolic amyloids, prions, and prionoids by Aguzzi (2009)
  5. 10.1007/BF00341717 / Mol. Gen. Genet. / Genetic aspects of [URE3], a non-Mendelian, cytoplasmically inherited mutation in yeast by Aigle (1975)
  6. 10.1134/S0026893306050104 / Mol. Biol. (Mosk.) / [Phenotypic manifestation of epigenetic determinant [ISP+] in Saccharomyces serevisiae depends on combination of mutations in SUP35 and SUP45 genes]. In Russian by Aksenova (2006)
  7. 10.1016/j.cell.2009.02.044 / Cell / A systematic survey identifies prions and illuminates sequence features of prionogenic proteins by Alberti (2009)
  8. 10.1016/S0076-6879(10)70030-6 / Methods Enzymol. / Biochemical, cell biological, and genetic assays to analyze amyloid and prion aggregation in yeast by Alberti (2010)
  9. 10.1534/genetics.104.037168 / Genetics / Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+] by Allen (2005)
  10. 10.1074/jbc.M609597200 / J. Biol. Chem. / Effects of ubiquitin system alterations on the formation and loss of a yeast prion by Allen (2007)
  11. 10.1016/S0076-6879(06)12003-0 / Methods Enzymol. / Analysis of amyloid aggregates using agarose gel electrophoresis by Bagriantsev (2006)
  12. 10.1091/mbc.e08-01-0078 / Mol. Biol. Cell / Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition by Bagriantsev (2008)
  13. 10.1074/jbc.M406612200 / J. Biol. Chem. / The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms by Bai (2004)
  14. 10.1093/genetics/153.1.81 / Genetics / Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae by Bailleul (1999)
  15. 10.3727/000000001783992650 / Gene Expr. / An antiprion effect of the anticytoskeletal drug latrunculin A in yeast by Bailleul-Winslett (2000)
  16. 10.1016/j.jmb.2009.03.036 / J. Mol. Biol. / Heterologous prion interactions are altered by mutations in the prion protein Rnq1p by Bardill (2009)
  17. 10.1534/genetics.111.136655 / Genetics / [PSI+] prion transmission barriers protect Saccharomyces cerevisiae from infection: intraspecies’ species barriers by Bateman (2012)
  18. 10.1091/mbc.e03-01-0007 / Mol. Biol. Cell / Conservation of the prion properties of Ure2p through evolution by Baudin-Baillieu (2003)
  19. 10.1073/pnas.082097899 / Proc. Natl. Acad. Sci. USA / Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein by Baxa (2002)
  20. 10.1074/jbc.M306004200 / J. Biol. Chem. / Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber by Baxa (2003)
  21. 10.1016/j.jmb.2004.03.033 / J. Mol. Biol. / The N-terminal prion domain of Ure2p converts from an unfolded to a thermally resistant conformation upon filament formation by Baxa (2004)
  22. 10.1016/j.jsb.2005.02.007 / J. Struct. Biol. / Filaments of the Ure2p prion protein have a cross-beta core structure by Baxa (2005)
  23. 10.1021/bi700826b / Biochemistry / Characterization of beta-sheet structure in Ure2p1–89 yeast prion fibrils by solid-state nuclear magnetic resonance by Baxa (2007)
  24. 10.1111/j.1365-2958.2010.07466.x / Mol. Microbiol. / In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone by Baxa (2011)
  25. 10.4161/pri.4.2.11963 / Prion / Prions: en route from structural models to structures by Bockmann (2010)
  26. 10.1006/jmbi.1995.0438 / J. Mol. Biol. / The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae by Bonetti (1995)
  27. 10.1093/emboj/20.23.6683 / EMBO J. / Yeast prion protein derivative defective in aggregate shearing and production of new ‘seeds’ by Borchsenius (2001)
  28. 10.1007/s00294-005-0035-0 / Curr. Genet. / Prion variant maintained only at high levels of the Hsp104 disaggregase by Borchsenius (2006)
  29. 10.1016/S0969-2126(00)00553-0 / Structure / Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae by Bousset (2001)
  30. 10.1021/bi011007b / Biochemistry / Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds by Bousset (2001)
  31. 10.1093/emboj/cdf303 / EMBO J. / The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro by Bousset (2002)
  32. 10.1016/S1631-0691(02)01385-9 / C. R. Biol. / Structure and assembly properties of the yeast prion Ure2p by Bousset (2002)
  33. 10.1016/S1047-8477(02)00606-8 / J. Struct. Biol. / The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils by Bousset (2003)
  34. 10.1021/bi049828e / Biochemistry / Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p by Bousset (2004)
  35. 10.1371/journal.pone.0009760 / PLoS One / Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural context by Bousset (2010)
  36. 10.1038/sj.emboj.7600772 / EMBO J. / Prion generation in vitro: amyloid of Ure2p is infectious by Brachmann (2005)
  37. 10.1016/j.ymeth.2006.04.008 / Methods / Reporter assay systems for [URE3] detection and analysis by Brachmann (2006)
  38. 10.1093/genetics/165.4.1675 / Genetics / Destabilizing interactions among [PSI+] and [PIN+] yeast prion variants by Bradley (2003)
  39. 10.1073/pnas.152330699 / Proc. Natl. Acad. Sci. USA / Interactions among prions and prion “strains” in yeast by Bradley (2002)
  40. 10.1101/gad.1839109 / Genes Dev. / A heritable switch in carbon source utilization driven by an unusual yeast prion by Brown (2009)
  41. 10.1016/j.semcdb.2011.03.005 / Semin. Cell Dev. Biol. / Sequence specificity and fidelity of prion transmission in yeast by Bruce (2011)
  42. 10.1099/0022-1317-68-1-79 / J. Gen. Virol. / Biological evidence that scrapie agent has an independent genome by Bruce (1987)
  43. 10.1073/pnas.0701392104 / Proc. Natl. Acad. Sci. USA / Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride by Byrne (2007)
  44. 10.1371/journal.pone.0004670 / PLoS ONE / The number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae by Byrne (2009)
  45. 10.1016/j.bpj.2011.06.016 / Biophys. J. / Physical properties of polymorphic yeast prion amyloid fibers by Castro (2011)
  46. 10.1007/s002940000180 / Curr. Genet. / Ssb1 chaperone is a [PSI+] prion-curing factor by Chacinska (2001)
  47. 10.1021/bi050724t / Biochemistry / Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10–39 of the yeast prion protein Ure2p by Chan (2005)
  48. 10.1073/pnas.0802215105 / Proc. Natl. Acad. Sci. USA / Strain-specific sequences required for yeast [PSI+] prion propagation by Chang (2008)
  49. 10.1073/pnas.0611158104 / Proc. Natl. Acad. Sci. USA / Prion species barrier between the closely related yeast proteins is detected despite coaggregation by Chen (2007)
  50. 10.1073/pnas.0907821106 / Proc. Natl. Acad. Sci. USA / Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy by Chen (2009)
  51. 10.1111/j.1365-2958.2010.07177.x / Mol. Microbiol. / Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission by Chen (2010)
  52. 10.1093/protein/gzq100 / Protein Eng. Des. Sel. / Deletion of a Ure2 C-terminal prion-inhibiting region promotes the rate of fibril seed formation and alters interaction with Hsp40 by Chen (2011)
  53. 10.1016/S1383-5742(00)00060-0 / Mutat. Res. / Mutation processes at the protein level: Is Lamarck back? by Chernoff (2001)
  54. 10.1016/j.cbpa.2004.09.002 / Curr. Opin. Chem. Biol. / Amyloidogenic domains, prions and structural inheritance: Rudiments of early life or recent acquisition? by Chernoff (2004)
  55. {'key': '2022011219172284000_bib54', 'first-page': '257', 'article-title': 'Cellular control of prion formation and propagation in yeast', 'volume-title': 'Prions and Prion Diseases: Current Perspectives', 'author': 'Chernoff', 'year': '2004'} / Prions and Prion Diseases: Current Perspectives / Cellular control of prion formation and propagation in yeast by Chernoff (2004)
  56. 10.1016/j.febslet.2007.04.075 / FEBS Lett. / Stress and prions: lessons from the yeast model by Chernoff (2007)
  57. 10.1073/pnas.0806234105 / Proc. Natl. Acad. Sci. USA / Identity determinants of infectious proteins by Chernoff (2008)
  58. 10.1002/yea.320080702 / Yeast / Dosage-dependent translational suppression in yeast Saccharomyces cerevisiae by Chernoff (1992)
  59. 10.1007/BF00351802 / Curr. Genet. / Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae by Chernoff (1993)
  60. 10.1126/science.7754373 / Science / Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+] by Chernoff (1995)
  61. 10.1128/MCB.19.12.8103 / Mol. Cell. Biol. / Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone Ssb in formation, stability, and toxicity of the [PSI] prion by Chernoff (1999)
  62. 10.1046/j.1365-2958.2000.01761.x / Mol. Microbiol. / Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein by Chernoff (2000)
  63. 10.1074/jbc.M310283200 / J. Biol. Chem. / Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool by Chernova (2003)
  64. 10.1016/j.molcel.2011.07.001 / Mol. Cell / Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton by Chernova (2011)
  65. 10.1038/35065632 / Nature / Conformational diversity in a yeast prion dictates its seeding specificity by Chien (2001)
  66. 10.1038/nchembio.131 / Nat. Chem. Biol. / Amyloid formation by globular proteins under native conditions by Chiti (2009)
  67. 10.1128/EC.00353-08 / Eukaryot. Cell / Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae by Choe (2009)
  68. 10.1101/cshperspect.a006833 / Cold Spring Harb. Perspect. Biol. / Prions by Colby (2011)
  69. 10.1016/S0140-6736(06)68930-7 / Lancet / Kuru in the 21st century: an acquired human prion disease with very long incubation periods by Collinge (2006)
  70. 10.1073/pnas.73.10.3651 / Proc. Natl. Acad. Sci. USA / A mutant of Saccharomyces cerevisiae defective for nuclear fusion by Conde (1976)
  71. 10.1073/pnas.94.18.9773 / Proc. Natl. Acad. Sci. USA / The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog by Coustou (1997)
  72. 10.1038/hdy.1965.65 / Heredity / Ψ, a cytoplasmic suppressor of super-suppression in yeast by Cox (1965)
  73. {'key': '2022011219172284000_bib72', 'first-page': '219', 'article-title': 'Psi phenomena in yeast', 'volume-title': 'The Early Days of Yeast Genetics', 'author': 'Cox', 'year': '1993'} / The Early Days of Yeast Genetics / Psi phenomena in yeast by Cox (1993)
  74. 10.1016/S0960-9822(00)00167-6 / Curr. Biol. / Cytoplasmic inheritance. Prion-like factors in yeast by Cox (1994)
  75. 10.1093/genetics/165.1.23 / Genetics / Analysis of the generation and segregation of propagons: entities that propagate the [PSI+] prion in yeast by Cox (2003)
  76. 10.1002/yea.320040302 / Yeast / The psi factor of yeast: a problem in inheritance by Cox (1988)
  77. 10.4161/pri.1.3.4839 / Prion / Prion stability by Cox (2007)
  78. 10.1046/j.1365-2443.2003.00661.x / Genes Cells / [PHI+], a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104 by Crist (2003)
  79. 10.1128/MCB.05338-11 / Mol. Cell. Biol. / A small, glutamine-free domain propagates the [SWI+] prion in budding yeast by Crow (2011)
  80. 10.1093/genetics/128.3.513 / Genetics / Interaction of the yeast omnipotent suppressors SUP1(SUP45) and SUP2(SUP35) with non-Mendelian factors by Dagkesamanskaya (1991)
  81. 10.1016/S0092-8674(00)81467-1 / Cell / A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion by DePace (1998)
  82. 10.1126/science.1197785 / Science / A size threshold limits prion transmission and establishes phenotypic diversity by Derdowski (2010)
  83. 10.4161/pri.1.3.4837 / Prion / Prion-prion interactions by Derkatch (2007)
  84. 10.1093/genetics/144.4.1375 / Genetics / Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae by Derkatch (1996)
  85. 10.1093/genetics/147.2.507 / Genetics / Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae by Derkatch (1997)
  86. 10.1007/s002940050433 / Curr. Genet. / The PNM2 mutation in the prion protein domain of SUP35 has distinct effects on different variants of the [PSI+] prion in yeast by Derkatch (1999)
  87. 10.1093/emboj/19.9.1942 / EMBO J. / Dependence and independence of [PSI+] and [PIN+]: A two-prion system in yeast? by Derkatch (2000)
  88. 10.1016/S0092-8674(01)00427-5 / Cell / Prions affect the appearance of other prions: the story of [PIN+] by Derkatch (2001)
  89. 10.1073/pnas.0404968101 / Proc. Natl. Acad. Sci. USA / Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro by Derkatch (2004)
  90. 10.1073/pnas.0504599102 / Proc. Natl. Acad. Sci. USA / Strain-specific morphologies of yeast prion amyloid fibrils by Diaz-Avalos (2005)
  91. 10.1016/0021-9975(68)90005-4 / J. Comp. Pathol. / Identification of a gene which controls the incubation period of some strains of scrapie agent in mice by Dickinson (1968)
  92. 10.1038/nsmb.2031 / Nat. Struct. Mol. Biol. / Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation by DiSalvo (2011)
  93. 10.1093/genetics/137.3.659 / Genetics / The dominant PNM2− mutation which eliminates the ψ factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene by Doel (1994)
  94. 10.1074/jbc.M704952200 / J. Biol. Chem. / Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions by Dong (2007)
  95. 10.1073/pnas.0802593105 / Proc. Natl. Acad. Sci. USA / Chaperone-dependent amyloid assembly protects cells from prion toxicity by Douglas (2008)
  96. 10.1038/ng.112 / Nat. Genet. / Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae by Du (2008)
  97. 10.1128/MCB.00225-10 / Mol. Cell. Biol. / Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function by Du (2010)
  98. 10.4161/pri.18071 / Prion / Polyglutamine misfolding in yeast: toxic and protective aggregation by Duennwald (2011)
  99. 10.1093/emboj/18.7.1974 / EMBO J. / Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism by Eaglestone (1999)
  100. 10.1073/pnas.162349599 / Proc. Natl. Acad. Sci. USA / Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein by Edskes (2002)
  101. 10.1073/pnas.96.4.1498 / Proc. Natl. Acad. Sci. USA / The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments by Edskes (1999)
  102. 10.1534/genetics.108.099929 / Genetics / Prion variants and species barriers among Saccharomyces Ure2 proteins by Edskes (2009)
  103. 10.1021/bi200142x / Biochemistry / Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel beta-sheet structure by Engel (2011)
  104. 10.1101/gad.439307 / Genes Dev. / Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p by Erjavec (2007)
  105. 10.1534/genetics.107.077982 / Genetics / The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion by Fan (2007)
  106. 10.1074/jbc.M506917200 / J. Biol. Chem. / Structure of the prion Ure2p in protein fibrils assembled in vitro by Fay (2005)
  107. 10.1016/j.jmb.2005.12.011 / J. Mol. Biol. / Packing of the prion Ure2p in protein fibrils probed by fluorescence X-ray near-edge structure spectroscopy at sulfur K-edge by Fayard (2006)
  108. 10.1093/embo-reports/kvf011 / EMBO Rep. / The [URE3] phenotype: evidence for a soluble prion in yeast by Fernandez-Bellot (2002)
  109. 10.1046/j.1365-2958.2001.02478.x / Mol. Microbiol. / The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation by Ferreira (2001)
  110. 10.1016/j.jmb.2011.02.025 / J. Mol. Biol. / Radically different amyloid conformations dictate the seeding specificity of a chimeric Sup35 prion by Foo (2011)
  111. 10.1016/j.tibs.2007.03.003 / Trends Biochem. Sci. / Functional amyloid: from bacteria to humans by Fowler (2007)
  112. 10.1128/MCB.26.2.617-629.2006 / Mol. Cell. Biol. / Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast by Ganusova (2006)
  113. 10.1073/pnas.0913280107 / Proc. Natl. Acad. Sci. USA / Conversion of a yeast prion protein to an infectious form in bacteria by Garrity (2010)
  114. 10.1038/nrmicro1127 / Nat. Rev. Microbiol. / Amyloids: a functional coat for microorganisms by Gebbink (2005)
  115. 10.1091/mbc.e04-08-0715 / Mol. Biol. Cell / Stress granule assembly is mediated by prion-like aggregation of TIA-1 by Gilks (2004)
  116. 10.1016/S0092-8674(00)81223-4 / Cell / Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins by Glover (1998)
  117. 10.2174/092986609788490087 / Protein Pept. Lett. / Remodeling of protein aggregates by Hsp104 by Glover (2009)
  118. 10.1016/S0092-8674(00)80264-0 / Cell / Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae by Glover (1997)
  119. 10.1371/journal.pone.0009642 / PLoS ONE / Pathogenic polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis by Goehler (2010)
  120. 10.1074/jbc.M500390200 / J. Biol. Chem. / Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model by Gokhale (2005)
  121. 10.1371/journal.pgen.1002634 / PLoS Genet. / Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast by Gong (2012)
  122. 10.1074/jbc.M312403200 / J. Biol. Chem. / The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104 by Grimminger (2004)
  123. 10.1371/journal.pgen.1000517 / PLoS Genet. / Complex adaptations can drive the evolution of the capacitor [PSI], even with realistic rates of yeast sex by Griswold (2009)
  124. 10.1126/science.1191081 / Science / Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits by Halfmann (2010)
  125. 10.1016/j.molcel.2011.05.013 / Mol. Cell / Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins by Halfmann (2011)
  126. 10.1038/nature10875 / Nature / Prions are a common mechanism for phenotypic inheritance in wild yeasts by Halfmann (2012)
  127. 10.1073/pnas.1019368108 / Proc. Natl. Acad. Sci. USA / Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB) by Heinrich (2011)
  128. 10.1074/jbc.M111.302869 / J. Biol. Chem. / Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104) by Helsen (2012)
  129. 10.1073/pnas.0808934105 / Proc. Natl. Acad. Sci. USA / Specificity of the J-protein Sis1 in the propagation of 3 yeast prions by Higurashi (2008)
  130. 10.1371/journal.pgen.1001309 / PLoS Genet. / [SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity by Hines (2011)
  131. 10.1002/yea.1857 / Yeast / A new colour assay for [URE3] prion in a genetic background used to score for the [PSI] prion by Hong (2011)
  132. 10.1074/jbc.C300300200 / J. Biol. Chem. / Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation by Hosoda (2003)
  133. 10.1534/genetics.106.056820 / Genetics / N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression by Hung (2006)
  134. 10.2174/138920308784534041 / Curr. Protein Pept. Sci. / Natural protective amyloids by Iconomidou (2008)
  135. {'key': '2022011219172284000_bib134', 'first-page': '1022', 'article-title': 'Ambiguity of translation: A eukaryotic version?', 'volume': '30', 'author': 'Inge-Vechtomov', 'year': '1994', 'journal-title': 'Genetika'} / Genetika / Ambiguity of translation: A eukaryotic version? by Inge-Vechtomov (1994)
  136. 10.4161/pri.1.4.5059 / Prion / Biological roles of prion domains by Inge-Vechtomov (2007)
  137. 10.1074/jbc.M408159200 / J. Biol. Chem. / Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it by Inoue (2004)
  138. 10.1017/S1355838298971874 / RNA / The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast by Ito (1998)
  139. 10.1093/genetics/159.2.527 / Genetics / Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae by Jensen (2001)
  140. 10.1128/MCB.24.9.3928-3937.2004 / Mol. Cell. Biol. / Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding by Jones (2004)
  141. 10.1111/j.1420-9101.2008.01515.x / J. Evol. Biol. / Effects of the [PSI+] prion on rates of adaptation in yeast by Joseph (2008)
  142. 10.1007/s002840010251 / Curr. Microbiol. / Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions by Jung (2001)
  143. 10.1093/genetics/156.2.559 / Genetics / A role for cytosolic Hsp70 in yeast [PSI+] prion propagation and [PSI+] as a cellular stress by Jung (2000)
  144. 10.1073/pnas.152333299 / Proc. Natl. Acad. Sci. USA / Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance by Jung (2002)
  145. 10.1111/j.1365-2958.2011.07719.x / Mol. Microbiol. / A mutation within the C-terminal domain of Sup35p that affects [PSI+] prion propagation by Kabani (2011)
  146. 10.1371/journal.pgen.1000824 / PLoS Genet. / Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1 by Kadnar (2010)
  147. 10.1038/nature07195 / Nature / Misfolded proteins partition between two distinct quality control compartments by Kaganovich (2008)
  148. 10.1083/jcb.201002149 / J. Cell Biol. / In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells by Kawai-Noma (2010)
  149. 10.4161/pri.1.2.4533 / Prion / Prion-dependent lethality of sup45 mutants in Saccharomyces cerevisiae by Kiktev (2007)
  150. 10.1134/S1607672911030021 / Dokl. Biochem. Biophys. / Identification of genes influencing synthetic lethality of genetic and epigenetic alterations in translation termination factors in yeast by Kiktev (2011)
  151. 10.1247/csf.28.187 / Cell Struct. Funct. / Analysis of yeast prion aggregates with amyloid-staining compound in vivo by Kimura (2003)
  152. 10.1006/jmbi.2001.4542 / J. Mol. Biol. / Supporting the structural basis of prion strains: induction and identification of [PSI] variants by King (2001)
  153. 10.1038/nature02391 / Nature / Protein-only transmission of three yeast prion strains by King (2004)
  154. 10.1073/pnas.94.13.6618 / Proc. Natl. Acad. Sci. USA / Prion-inducing domain 2–114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments by King (1997)
  155. 10.1534/genetics.111.129460 / Genetics / Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity by Kirkland (2011)
  156. 10.1016/j.bbrc.2004.01.117 / Biochem. Biophys. Res. Commun. / β-Helix is a likely core structure of yeast prion Sup35 amyloid fibers by Kishimoto (2004)
  157. 10.1002/yea.700 / Yeast / [Psi+] prion generation in yeast: characterization of the ‘strain’ difference by Kochneva-Pervukhova (2001)
  158. 10.1371/journal.pone.0029832 / PLoS ONE / Amyloid-mediated sequestration of essential proteins contributes to mutant Huntingtin toxicity in yeast by Kochneva-Pervukhova (2012)
  159. 10.1016/S1097-2765(04)00206-0 / Mol. Cell / Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe by Kong (2004)
  160. 10.1038/nature03679 / Nature / Structural insights into a yeast prion illuminate nucleation and strain diversity by Krishnan (2005)
  161. 10.1091/mbc.e07-02-0128 / Mol. Biol. Cell / Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae by Kryndushkin (2007)
  162. 10.1074/jbc.M307996200 / J. Biol. Chem. / Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104 by Kryndushkin (2003)
  163. 10.1038/emboj.2008.198 / EMBO J. / Curing of the [URE3] prion by Btn2p, a Batten disease-related protein by Kryndushkin (2008)
  164. 10.1016/j.jmb.2011.03.067 / J. Mol. Biol. / The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-beta structure: evidence from solid-state NMR by Kryndushkin (2011)
  165. 10.1534/genetics.111.127779 / Genetics / Molecular chaperone Hsp104 can promote yeast prion strain generation by Kryndushkin (2011)
  166. 10.1038/sj.emboj.7600985 / EMBO J. / Molecular chaperones and the assembly of the prion Sup35p, an in vitro study by Krzewska (2006)
  167. 10.1074/jbc.M608110200 / J. Biol. Chem. / Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain by Krzewska (2007)
  168. 10.1111/j.1365-2958.2007.05629.x / Mol. Microbiol. / Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation by Kurahashi (2007)
  169. 10.1128/MCB.01900-07 / Mol. Cell. Biol. / A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates by Kurahashi (2008)
  170. 10.1111/j.1365-2443.2011.01511.x / Genes Cells / [PSI+] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast by Kurahashi (2011)
  171. 10.1016/S0092-8674(00)81216-7 / Cell / Structure and replication of yeast prions by Kushnirov (1998)
  172. 10.1093/emboj/19.3.324 / EMBO J. / Prion properties of the Sup35 protein of yeast Pichia methanolica by Kushnirov (2000)
  173. 10.1016/S0960-9822(00)00802-2 / Curr. Biol. / Chaperones that cure yeast artificial [PSI+] and their prion-specific effects by Kushnirov (2000)
  174. 10.1128/jb.106.2.519-522.1971 / J. Bacteriol. / Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast by Lacroute (1971)
  175. 10.1534/genetics.109.110213 / Genetics / The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system by Lancaster (2010)
  176. 10.3109/02656739509022483 / Int. J. Hyperthermia / Heat shock proteins, thermotolerance, and their relevance to clinical hyperthermia by Li (1995)
  177. 10.1126/science.287.5453.661 / Science / Creating a protein-based element of inheritance by Li (2000)
  178. 10.1073/pnas.152318899 / Proc. Natl. Acad. Sci. USA / Progress toward an ultimate proof of the prion hypothesis by Liebman (2002)
  179. 10.1016/j.ymeth.2006.04.010 / Methods / Biochemical and genetic methods for characterization of [PIN+] prions in yeast by Liebman (2006)
  180. 10.1371/journal.pgen.1002297 / PLoS Genet. / Inter-allelic prion propagation reveals conformational relationships among a multitude of [PSI] strains by Lin (2011)
  181. 10.1016/j.cell.2009.12.031 / Cell / The polarisome is required for segregation and retrograde transport of protein aggregates by Liu (2010)
  182. 10.1016/j.cell.2011.11.018 / Cell / Segregation of protein aggregates involves actin and the polarity machinery by Liu (2011)
  183. 10.1038/23048 / Nature / Oligopeptide-repeat expansions modulate ‘protein-only’ inheritance in yeast by Liu (1999)
  184. 10.1073/pnas.252652099 / Proc. Natl. Acad. Sci. USA / Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+] by Liu (2002)
  185. 10.1016/j.bbrc.2006.11.143 / Biochem. Biophys. Res. Commun. / Effects of randomizing the Sup35NM prion domain sequence on formation of amyloid fibrils in vitro by Liu (2007)
  186. 10.1016/j.jmb.2009.09.016 / J. Mol. Biol. / Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules by Loquet (2009)
  187. 10.1128/MCB.19.6.4516 / Mol. Cell. Biol. / Two prion-inducing regions of Ure2p are nonoverlapping by Maddelein (1999)
  188. 10.1073/pnas.072199199 / Proc. Natl. Acad. Sci. USA / Amyloid aggregates of the HET-s prion protein are infectious by Maddelein (2002)
  189. 10.1126/science.1173155 / Science / Functional amyloids as natural storage of peptide hormones in pituitary secretory granules by Maji (2009)
  190. 10.1371/journal.pgen.1001386 / PLoS Genet. / Prion formation and polyglutamine aggregation are controlled by two classes of genes by Manogaran (2011)
  191. 10.1089/088282403322017875 / Viral Immunol. / Transmissible encephalopathies: speculations and realities by Manuelidis (2003)
  192. 10.1534/genetics.105.051649 / Genetics / Cryptic genetic variation is enriched for potential adaptations by Masel (2006)
  193. 10.1111/j.0014-3820.2003.tb00358.x / Evolution / The evolution of the evolvability properties of the yeast prion [PSI+] by Masel (2003)
  194. 10.1126/science.270.5233.93 / Science / Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells by Masison (1995)
  195. 10.4161/pri.18005 / Prion / Modeling Huntington disease in yeast: perspectives and future directions by Mason (2011)
  196. 10.1016/j.jmb.2009.04.063 / J. Mol. Biol. / Ssa1 overexpression and [PIN+] variants cure [PSI+] by dilution of aggregates by Mathur (2009)
  197. 10.1091/mbc.e09-11-0927 / Mol. Biol. Cell / Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s]y, in yeast by Mathur (2010)
  198. 10.1073/pnas.1102762108 / Proc. Natl. Acad. Sci. USA / Suicidal [PSI+] is a lethal yeast prion by McGlinchey (2011)
  199. 10.1083/jcb.200112104 / J. Cell Biol. / Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1 by Meriin (2002)
  200. 10.1128/MCB.23.21.7554-7565.2003 / Mol. Cell. Biol. / Aggregation of expanded polyglutamine domain in yeast leads to defects in endocytosis by Meriin (2003)
  201. 10.1073/pnas.97.22.11910 / Proc. Natl. Acad. Sci. USA / A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions by Michelitsch (2000)
  202. 10.1073/pnas.1011342108 / Proc. Natl. Acad. Sci. USA / Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy by Mizuno (2011)
  203. {'key': '2022011219172284000_bib201', 'first-page': '187', 'article-title': 'Species barriers in prion diseases: brief review', 'author': 'Moore', 'year': '2005', 'journal-title': 'Arch. Virol.'} / Arch. Virol. / Species barriers in prion diseases: brief review by Moore (2005)
  204. 10.1002/yea.1742 / Yeast / Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI+] prion but not for prion propagation by Moosavi (2010)
  205. 10.1128/MCB.20.23.8916-8922.2000 / Mol. Cell. Biol. / [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p by Moriyama (2000)
  206. 10.1016/S1097-2765(01)00259-3 / Mol. Cell / Yeast [PSI+] “prions” that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state by Nakayashiki (2001)
  207. 10.1073/pnas.0504882102 / Proc. Natl. Acad. Sci. USA / Yeast prions [URE3] and [PSI+] are diseases by Nakayashiki (2005)
  208. {'key': '2022011219172284000_bib206', 'author': 'Namy', 'year': '2008'} by Namy (2008)
  209. 10.1038/nature03680 / Nature / Structure of the cross-beta spine of amyloid-like fibrils by Nelson (2005)
  210. 10.1128/MCB.22.15.5593-5605.2002 / Mol. Cell. Biol. / Guanidine hydrochloride inhibits the generation of prion “seeds” but not prion protein aggregation in yeast by Ness (2002)
  211. 10.1128/MCB.19.2.1325 / Mol. Cell. Biol. / Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing by Newnam (1999)
  212. 10.1016/j.jmb.2011.02.034 / J. Mol. Biol. / Destabilization and recovery of a yeast prion after mild heat shock by Newnam (2011)
  213. 10.1074/jbc.M111.269092 / J. Biol. Chem. / Hierarchical organization in the amyloid core of yeast prion protein ure2 by Ngo (2011)
  214. 10.1016/S0092-8674(01)00440-8 / Cell / Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI+] prion by Osherovich (2001)
  215. 10.1016/S1534-5807(02)00118-1 / Dev. Cell / The utility of prions by Osherovich (2002)
  216. 10.1371/journal.pbio.0020086 / PLoS Biol. / Dissection and design of yeast prions by Osherovich (2004)
  217. 10.1093/emboj/20.9.2111 / EMBO J. / Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions by Parham (2001)
  218. 10.1534/genetics.105.054221 / Genetics / De novo appearance and “strain” formation of yeast prion [PSI+] are regulated by the heat-shock transcription factor by Park (2006)
  219. 10.1016/j.jmb.2006.10.069 / J. Mol. Biol. / “Prion-proof” for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132–405) induces [PIN+] by Patel (2007)
  220. 10.1038/ncb1843 / Nat. Cell Biol. / The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion by Patel (2009)
  221. 10.1126/science.273.5275.622 / Science / Support for the prion hypothesis for inheritance of a phenotypic trait in yeast by Patino (1996)
  222. 10.1002/j.1460-2075.1996.tb00675.x / EMBO J. / Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor by Paushkin (1996)
  223. 10.1126/science.6801762 / Science / Novel proteinaceous infectious particles cause scrapie by Prusiner (1982)
  224. 10.1016/0092-8674(90)90134-Z / Cell / Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication by Prusiner (1990)
  225. 10.1016/j.jmb.2007.04.018 / J. Mol. Biol. / Hydrogen/deuterium exchange mass spectrometric analysis of conformational changes accompanying the assembly of the yeast prion Ure2p into protein fibrils by Redeker (2007)
  226. 10.4161/pri.17749 / Prion / Modulation and elimination of yeast prions by protein chaperones and co-chaperones by Reidy (2011)
  227. 10.1099/00221287-148-4-1049 / Microbiology / The Candida albicans Sup35p protein (CaSup35p): function, prion-like behaviour and an associated polyglutamine length polymorphism by Resende (2002)
  228. 10.1046/j.1365-2958.2003.03608.x / Mol. Microbiol. / Prion protein gene polymorphisms in Saccharomyces cerevisiae by Resende (2003)
  229. 10.4161/pri.1.4.5058 / Prion / Chaperone effects on prion and nonprion aggregates by Rikhvanov (2007)
  230. 10.1074/jbc.M408792200 / J. Biol. Chem. / The [URE3] yeast prion results from protein aggregates that differ from amyloid filaments formed in vitro by Ripaud (2004)
  231. 10.1038/nature03793 / Nature / Correlation of structural elements and infectivity of the HET-s prion by Ritter (2005)
  232. 10.1101/gad.1115803 / Genes Dev. / Heritable activity: a prion that propagates by covalent autoactivation by Roberts (2003)
  233. 10.1002/yea.1062 / Yeast / [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast by Roberts (2004)
  234. 10.1073/pnas.1005949107 / Proc. Natl. Acad. Sci. USA / Non-Mendelian determinant [ISP+] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1 by Rogoza (2010)
  235. 10.2174/092986609788490078 / Protein Pept. Lett. / Hsp104 and prion propagation by Romanova (2009)
  236. 10.4161/pri.2.4.7490 / Prion / The elaborate structure of spider silk: structure and function of a natural high performance fiber by Romer (2008)
  237. 10.1128/MCB.24.16.7206-7213.2004 / Mol. Cell. Biol. / Scrambled prion domains form prions and amyloid by Ross (2004)
  238. 10.1073/pnas.0506136102 / Proc. Natl. Acad. Sci. USA / Primary sequence independence for prion formation by Ross (2005)
  239. 10.1038/ncb1105-1039 / Nat. Cell Biol. / Prion domains: sequences, structures and interactions by Ross (2005)
  240. {'key': '2022011219172284000_bib238', 'author': 'Sadlish', 'year': '2008'} by Sadlish (2008)
  241. 10.1111/j.1567-1364.2010.00700.x / FEMS Yeast Res. / Yeast prions: Could they be exaptations? The URE2/[URE3] system in Kluyveromyces lactis by Safadi (2011)
  242. 10.1007/s00294-010-0314-2 / Curr. Genet. / [NSI+]: a novel non-Mendelian nonsense suppressor determinant in Saccharomyces cerevisiae by Saifitdinova (2010)
  243. 10.1074/jbc.M410150200 / J. Biol. Chem. / Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids by Salnikova (2005)
  244. 10.1016/S0092-8674(00)81565-2 / Cell / Molecular basis of a yeast prion species barrier by Santoso (2000)
  245. 10.1038/nature03981 / Nature / Prion protein remodelling confers an immediate phenotypic switch by Satpute-Krishnan (2005)
  246. 10.1371/journal.pbio.0050024 / PLoS Biol. / Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance by Satpute-Krishnan (2007)
  247. 10.4161/pri.1.2.4666 / Prion / A short history of small s: a prion of the fungus Podospora anserina by Saupe (2007)
  248. {'key': '2022011219172284000_bib246', 'author': 'Saupe', 'year': '2011'} by Saupe (2011)
  249. 10.1038/nature05695 / Nature / Atomic structures of amyloid cross-beta spines reveal varied steric zippers by Sawaya (2007)
  250. 10.1002/yea.1515 / Yeast / Yeast genome evolution: the origin of the species by Scannell (2007)
  251. 10.1073/pnas.96.8.4604 / Proc. Natl. Acad. Sci. USA / Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington’s disease pathology by Scherzinger (1999)
  252. 10.1110/ps.9.3.440 / Protein Sci. / The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein by Schlumpberger (2000)
  253. 10.1128/MCB.21.20.7035-7046.2001 / Mol. Cell. Biol. / Induction of distinct [URE3] yeast prion strains by Schlumpberger (2001)
  254. 10.1128/MCB.22.11.3590-3598.2002 / Mol. Cell. Biol. / Antagonistic interactions between yeast [PSI+] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p by Schwimmer (2002)
  255. 10.1074/jbc.M611464200 / J. Biol. Chem. / Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked beta-solenoid model of HET-s prion fibrils by Sen (2007)
  256. 10.1371/journal.pone.0006939 / PLoS ONE / The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion by Senechal (2009)
  257. 10.1534/genetics.108.089458 / Genetics / Functionally redundant isoforms of a yeast Hsp70 chaperone subfamily have different antiprion effects by Sharma (2008)
  258. 10.1073/pnas.1107421108 / Proc. Natl. Acad. Sci. USA / Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p by Sharma (2011)
  259. 10.1534/genetics.108.098699 / Genetics / Curing of yeast [URE3] prion by the Hsp40 cochaperone Ydj1p is mediated by Hsp70 by Sharma (2009)
  260. 10.1073/pnas.0609638103 / Proc. Natl. Acad. Sci. USA / Amyloid of the prion domain of Sup35p has an in-register parallel {beta}-sheet structure by Shewmaker (2006)
  261. 10.1021/bi7024589 / Biochemistry / Amyloids of shuffled prion domains that form prions have a parallel in-register beta-sheet structure by Shewmaker (2008)
  262. 10.1021/bi900345q / Biochemistry / Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration by Shewmaker (2009)
  263. 10.1074/jbc.M109.007054 / J. Biol. Chem. / The functional curli amyloid is not based on in-register parallel beta-sheet structure by Shewmaker (2009)
  264. 10.4161/pri.3.4.10388 / Prion / Localization of prion-destabilizing mutations in the N-terminal non-prion domain of Rnq1 in Saccharomyces cerevisiae by Shibata (2009)
  265. 10.1534/genetics.105.048660 / Genetics / The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants by Shkundina (2006)
  266. 10.1039/c004550k / Mol. Biosyst. / Emergence and natural selection of drug-resistant prions by Shorter (2010)
  267. 10.1126/science.1098007 / Science / Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers by Shorter (2004)
  268. 10.1016/j.molcel.2006.05.042 / Mol. Cell / Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities by Shorter (2006)
  269. 10.1016/S0092-8674(03)01020-1 / Cell / A neuronal isoform of the aplysia CPEB has prion-like properties by Si (2003)
  270. 10.1016/j.cell.2010.01.008 / Cell / Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation by Si (2010)
  271. 10.1073/pnas.1000347107 / Proc. Natl. Acad. Sci. USA / Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast by Sideri (2010)
  272. {'key': '2022011219172284000_bib270', 'author': 'Sideri', 'year': '2011'} by Sideri (2011)
  273. 10.1016/S1097-2765(00)80412-8 / Mol. Cell / Rnq1: an epigenetic modifier of protein function in yeast by Sondheimer (2000)
  274. 10.1093/emboj/20.10.2435 / EMBO J. / The role of Sis1 in the maintenance of the [RNQ+] prion by Sondheimer (2001)
  275. 10.1126/science.289.5479.595 / Science / Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein by Sparrer (2000)
  276. 10.1083/jcb.153.6.1327 / J. Cell Biol. / Prion filament networks in [URE3] cells of Saccharomyces cerevisiae by Speransky (2001)
  277. 10.4161/pri.18213 / Prion / The [RNQ+] prion: A model of both functional and pathological amyloid by Stein (2011)
  278. 10.1126/science.1219491 / Science / A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress by Suzuki (2012)
  279. 10.1534/genetics.105.043489 / Genetics / The [URE3] prion is not conserved among Saccharomyces species by Talarek (2005)
  280. 10.1038/nature02392 / Nature / Conformational variations in an infectious protein determine prion strain differences by Tanaka (2004)
  281. 10.1016/j.cell.2005.03.008 / Cell / Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins by Tanaka (2005)
  282. 10.1038/nature04922 / Nature / The physical basis of how prion conformations determine strain phenotypes by Tanaka (2006)
  283. 10.1016/j.molcel.2007.05.027 / Mol. Cell / A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast by Taneja (2007)
  284. 10.1128/MCB.02127-06 / Mol. Cell. Biol. / Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability by Tank (2007)
  285. 10.1093/genetics/137.3.671 / Genetics / The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae by Ter-Avanesyan (1994)
  286. 10.1111/j.1365-2958.2008.06135.x / Mol. Microbiol. / Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation by Tessarz (2008)
  287. 10.1128/MCB.00201-09 / Mol. Cell. Biol. / The yeast AAA+ chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins by Tessarz (2009)
  288. 10.1038/nature05848 / Nature / Prion recognition elements govern nucleation, strain specificity and species barriers by Tessier (2007)
  289. 10.1038/nsmb.1617 / Nat. Struct. Mol. Biol. / Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+] by Tessier (2009)
  290. 10.1016/j.molcel.2008.11.003 / Mol. Cell / In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104 by Tipton (2008)
  291. 10.1128/MCB.01140-09 / Mol. Cell. Biol. / Compositional determinants of prion formation in yeast by Toombs (2010)
  292. 10.1371/journal.pone.0021953 / PLoS ONE / [PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain by Toombs (2011)
  293. 10.1038/nature06108 / Nature / The structural basis of yeast prion strain variants by Toyama (2007)
  294. 10.1038/35035005 / Nature / A yeast prion provides a mechanism for genetic variation and phenotypic diversity by True (2000)
  295. 10.1038/nature02885 / Nature / Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits by True (2004)
  296. 10.1016/S0021-9258(19)68961-1 / J. Biol. Chem. / An homologous in vitro assay for yeast nonsense suppressors by Tuite (1981)
  297. 10.1021/bi9002666 / Biochemistry / Evidence for novel beta-sheet structures in Iowa mutant beta-amyloid fibrils by Tycko (2009)
  298. 10.1371/journal.pbio.0060294 / PLoS Biol. / Prion switching in response to environmental stress by Tyedmers (2008)
  299. {'key': '2022011219172284000_bib296', 'author': 'Tyedmers', 'year': '2010'} by Tyedmers (2010)
  300. 10.1073/pnas.98.4.1459 / Proc. Natl. Acad. Sci. USA / The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p by Umland (2001)
  301. 10.1093/emboj/20.22.6236 / EMBO J. / Strains of [PSI+] are distinguished by their efficiencies of prion-mediated conformational conversion by Uptain (2001)
  302. 10.1021/ja068633m / J. Am. Chem. Soc. / Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p by van der Wel (2007)
  303. 10.1021/ja104213j / J. Am. Chem. Soc. / Atomic-resolution three-dimensional structure of HET-s(218–289) amyloid fibrils by solid-state NMR spectroscopy by Van Melckebeke (2010)
  304. 10.1038/nsmb.2030 / Nat. Struct. Mol. Biol. / Strain conformation, primary structure and the propagation of the yeast prion [PSI+] by Verges (2011)
  305. 10.1186/1741-7007-7-26 / BMC Biol. / Heterologous cross-seeding mimics cross-species prion conversion in a yeast model by Vishveshwara (2009)
  306. 10.1074/jbc.M609269200 / J. Biol. Chem. / Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM by Vitrenko (2007)
  307. 10.1093/genetics/160.1.25 / Genetics / Novel non-Mendelian determinant involved in the control of translation accuracy in Saccharomyces cerevisiae by Volkov (2002)
  308. 10.1083/jcb.152.5.923 / J. Cell Biol. / The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins by Walenta (2001)
  309. 10.1073/pnas.0801934105 / Proc. Natl. Acad. Sci. USA / Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs by Wang (2008)
  310. 10.1016/j.jsb.2011.03.008 / J. Struct. Biol. / The fibrils of Ure2p homologs from Saccharomyces cerevisiae and Saccharoymyces paradoxus have similar cross-beta structure in both dried and hydrated forms by Wang (2011)
  311. 10.1126/science.1151839 / Science / Amyloid fibrils of the HET-s(218–289) prion form a beta solenoid with a triangular hydrophobic core by Wasmer (2008)
  312. 10.1016/j.jmb.2009.09.015 / J. Mol. Biol. / The molecular organization of the fungal prion HET-s in its amyloid form by Wasmer (2009)
  313. 10.1128/MCB.21.14.4656-4669.2001 / Mol. Cell. Biol. / Mechanism of prion loss after Hsp104 inactivation in yeast by Wegrzyn (2001)
  314. 10.1016/j.cell.2004.11.027 / Cell / Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB by Weibezahn (2004)
  315. 10.1126/science.7909170 / Science / [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae by Wickner (1994)
  316. {'key': '2022011219172284000_bib313', 'author': 'Wickner', 'year': '1997'} by Wickner (1997)
  317. 10.1073/pnas.0712032105 / Proc. Natl. Acad. Sci. USA / Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure by Wickner (2008)
  318. 10.1002/bies.20821 / Bioessays / Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures by Wickner (2008)
  319. 10.1111/j.1567-1364.2010.00666.x / FEMS Yeast Res. / Prion amyloid structure explains templating: how proteins can be genes by Wickner (2010)
  320. 10.1016/j.semcdb.2011.02.021 / Semin. Cell Dev. Biol. / Prion diseases of yeast: amyloid structure and biology by Wickner (2011)
  321. {'key': '2022011219172284000_bib318', 'first-page': '1322', 'article-title': '[Prionization of the Pichia methanolica SUP35 gene product in the yeast Saccharomyces cerevisiae]. In Russian', 'volume': '36', 'author': 'Zadorskii', 'year': '2000', 'journal-title': 'Genetika'} / Genetika / [Prionization of the Pichia methanolica SUP35 gene product in the yeast Saccharomyces cerevisiae]. In Russian by Zadorskii (2000)
  322. 10.1007/BF01734159 / Mol. Cell. Biochem. / Cytoduction as a new tool in studying the cytoplasmic heredity in yeast by Zakharov (1977)
  323. 10.1128/EC.5.2.217-225.2006 / Eukaryot. Cell / The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans by Zenthon (2006)
  324. 10.1074/jbc.M901189200 / J. Biol. Chem. / Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils by Zhang (2009)
  325. 10.1016/j.jmb.2008.09.047 / J. Mol. Biol. / “Restoration” of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2 by Zhang (2008)
  326. 10.1016/j.cell.2011.11.002 / Cell / Motility and segregation of Hsp104-associated protein aggregates in budding yeast by Zhou (2011)
  327. 10.1046/j.1365-2958.2001.02224.x / Mol. Microbiol. / The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI+] and [PIN+] by Zhou (2001)
  328. 10.1093/emboj/18.5.1182 / EMBO J. / The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion- like form of release factor eRF3 by Zhou (1999)
Dates
Type When
Created 13 years ago (Aug. 9, 2012, 9:23 a.m.)
Deposited 1 year, 4 months ago (April 28, 2024, 4:42 a.m.)
Indexed 3 weeks, 3 days ago (Aug. 5, 2025, 8:54 a.m.)
Issued 13 years ago (Aug. 1, 2012)
Published 13 years ago (Aug. 1, 2012)
Published Online 13 years ago (Aug. 1, 2012)
Published Print 13 years ago (Aug. 1, 2012)
Funders 0

None

@article{Liebman_2012, title={Prions in Yeast}, volume={191}, ISSN={1943-2631}, url={http://dx.doi.org/10.1534/genetics.111.137760}, DOI={10.1534/genetics.111.137760}, number={4}, journal={Genetics}, publisher={Oxford University Press (OUP)}, author={Liebman, Susan W and Chernoff, Yury O}, year={2012}, month=aug, pages={1041–1072} }