Диссертация (Влияние мутаций в прионизующем домене белка sup35 на свойства приона [PSI+] дрожжей Saccharomyces cerevisiae), страница 20
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Файл "Диссертация" внутри архива находится в папке "Влияние мутаций в прионизующем домене белка sup35 на свойства приона [PSI+] дрожжей Saccharomyces cerevisiae". PDF-файл из архива "Влияние мутаций в прионизующем домене белка sup35 на свойства приона [PSI+] дрожжей Saccharomyces cerevisiae", который расположен в категории "". Всё это находится в предмете "биология" из Аспирантура и докторантура, которые можно найти в файловом архиве СПбГУ. Не смотря на прямую связь этого архива с СПбГУ, его также можно найти и в других разделах. , а ещё этот архив представляет собой кандидатскую диссертацию, поэтому ещё представлен в разделе всех диссертаций на соискание учёной степени кандидата биологических наук.
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Biol. 2012. Т. 4. № 9. С. a012286.52. DePace A.H., Santoso A., Hillner P., Weissman J.S. A critical role for amino-terminalglutamine/asparagine repeats in the formation and propagation of a yeast prion // Cell. 1998. Т. 93.№ 7. С. 1241–52.53. DePace A.H., Weissman J.S. Origins and kinetic consequences of diversity in Sup35 yeastprion fibers // Nat.
Struct. Biol. 2002. Т. 9. № 5. С. 389–96.54. Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W. Prions affect the appearance of otherprions: the story of [PIN(+)] // Cell. 2001. Т. 106. № 2. С. 171–182.55. Derkatch I.L., Bradley M.E., Zhou P., Chernoff Y.O., Liebman S.W. Genetic and environmentalfactors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae // Genetics.1997.
Т. 147. С. 507–519.56. Derkatch I.L., Bradley M.E., Zhou P., Liebman S.W. The PNM2 mutation in the prion proteindomain of SUP35 has distinct effects on different variants of the [PSI+] prion in yeast // Curr. Genet.1999. Т. 35. № 2. С. 59–67.57. Derkatch I.L., Chernoff Y.O., Kushnirov V. V., Inge-vcchtomov S.G., Liebman S.W. Genesisand variability of [PSI] prion factor in Saccharomyces cerevisiae // Genetics. 1996. Т. 144.
С. 1375–1386.58. Derkatch I.L., Uptain S.M., Outeiro T.F., Krishnan R., Lindquist S.L., Liebman S.W. Effects ofQ/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast andaggregation of Sup35 in vitro // Proc. Natl. Acad. Sci. U. S. A. 2004. Т. 101. № 35. С. 12934–9.59. Dever T.E., Green R. The elongation, termination, and recycling phases of translation ineukaryotes // Cold Spring Harb. Perspect. Biol. 2012. Т.
4. № 7. С. a013706.60. Diaz-Avalos R., King C., Wall J., Simon M., Caspar D.L.D. Strain-specific morphologies ofyeast prion amyloid fibrils // Proc. Natl. Acad. Sci. USA. 2005. Т. 102. № 29. С. 10165–10170.61. Diener T.O., McKinley M.P., Prusiner S.B. Viroids and prions // Proc. Natl. Acad. Sci. U. S. A.1982. Т. 79. № 17. С. 5220–4.62. DiSalvo S., Derdowski A., Pezza J.
A., Serio T.R. Dominant prion mutants induce curingthrough pathways that promote chaperone-mediated disaggregation // Nat. Struct. Mol. Biol. 2011. Т.18. № 4. С. 486–492.63. Doel S.M., Mccready S.J., Nierras C.R., Cox B.S. The dominant PNM2 mutation whicheliminates the PSI factor of Saccharomyces cerevisiae is the result of missense mutation in theSUP35 gene // Genetics.
1994. Т. 137. С. 659–670.64. Du Z., Park K.-W., Yu H., Fan Q., Li L. Newly identified prion linked to the chromatinremodeling factor Swi1 in Saccharomyces cerevisiae // Nat. Genet. 2008. Т. 40. № 4. С. 460–5.65. Eaglestone S.S., Cox B.S., Tuite M.F. Translation termination efficiency can be regulated inSaccharomyces cerevisiae by environmental stress through a prion-mediated mechanism // EMBO J.1999. Т. 18. № 7. С.
1974–81.66. Eaglestone S.S., Ruddock L.W., Cox B.S., Tuite M.F. Guanidine hydrochloride blocks a criticalstep in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae // Proc.Natl. Acad. Sci. U. S. A. 2000. Т. 97. № 1. С. 240–244.67. Edgeworth J.A., Gros N., Alden J., Joiner S., Wadsworth J.D.F., Linehan J., Brandner S.,Jackson G.S., Weissmann C., Collinge J.
Spontaneous generation of mammalian prions // Proc. Natl.Acad. Sci. U. S. A. 2010. Т. 107. № 32. С. 14402–6.10968. Eyler D.E., Wehner K. A., Green R. Eukaryotic release factor 3 is required for multipleturnovers of peptide release catalysis by eukaryotic release factor 1 // J. Biol. Chem. 2013. Т. 288. №41. С. 29530–8.69. Ferreira P.C., Ness F., Edwards S.R., Cox B.S., Tuite M.F. The elimination of the yeast [PSI+]prion by guanidine hydrochloride is the result of Hsp104 inactivation // Mol. Microbiol.
2001. Т. 40.№ 6. С. 1357–69.70. Fisher R.A. On the interpretation of χ2 from contingency tables, and the calculation of P // J. R.Stat. Soc. 1922. Т. 85. № 1. С. 87–94.71. Fitzpatrick D. A., O’Brien J., Moran C., Hasin N., Kenny E., Cormican P., Gates A., MorrisD.W., Jones G.W. Assessment of inactivating stop codon mutations in forty Saccharomycescerevisiae strains: implications for [PSI] prion-mediated phenotypes // PLoS One.
2011. Т. 6. № 12.С. e28684.72. Foo C.K., Ohhashi Y., Kelly M.J.S., Tanaka M., Weissman J.S. Radically different amyloidconformations dictate the seeding specificity of a chimeric Sup35 prion // J. Mol. Biol. 2011. Т. 408.№ 1. С. 1–8.73. Fowler D.M., Koulov A. V, Alory-Jost C., Marks M.S., Balch W.E., Kelly J.W.
Functionalamyloid formation within mammalian tissue // PLoS Biol. 2006. Т. 4. № 1. С. e6.74. Fowler D.M., Koulov A. V, Balch W.E., Kelly J.W. Functional amyloid--from bacteria tohumans // Trends Biochem. Sci. 2007. Т. 32. № 5. С. 217–24.75. Frolova L., Goff X. Le, Rasmussen H.H., Cheperegin S., Drugeon G., Kress M., Arman I.,Haenni A.L., Celis J.E., Philippe M. A highly conserved eukaryotic protein family possessingproperties of polypeptide chain release factor // Nature.
1994. Т. 372. № 6507. С. 701–3.76. Gajdusek D.C., Zigas V. Degenerative disease of the central nervous system in New Guinea;the endemic occurrence of kuru in the native population // N. Engl. J. Med. 1957. Т. 257. № 20. С.974–8.77. Ganusova E.E., Ozolins L.N., Bhagat S., Newnam G.P., Wegrzyn R.D., Sherman M.Y.,Chernoff Y.O. Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton inyeast // Mol. Cell.
Biol. 2006. Т. 26. № 2. С. 617–29.78. Gibbs C.J., Gajdusek D.C., Latarjet R. Unusual resistance to ionizing radiation of the viruses ofkuru, Creutzfeldt-Jakob disease, and scrapie // Proc. Natl. Acad. Sci. U. S. A. 1978. Т. 75. № 12. С.6268–70.79. Gilks N., Kedersha N., Ayodele M., Shen L., Stoecklin G., Dember L.M., Anderson P.
Stressgranule assembly is mediated by prion-like aggregation of TIA-1 // Mol. Biol. Cell. 2004. Т. 15. С.5383–5398.80. Gill S.C., Hippel P.H. Calculation of protein extinction coefficients from amino acid sequencedata // Anal. Biochem. 1989. Т. 182. № 2. С. 319–26.81. Glover J.R., Kowal A. S., Schirmer E.C., Patino M.M., Liu J.J., Lindquist S. Self-seeded fibersformed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae //Cell. 1997. Т. 89. № 5.
С. 811–9.82.Griffith J.S. Self-replication and scrapie // Nature. 1967. Т. 215. № 5105. С. 1043–4.83. Grishin A. V, Rothenberg M., Downs M.A., Blumer K.J. Mot3, a Zn finger transcription factorthat modulates gene expression and attenuates mating pheromone signaling in Saccharomycescerevisiae // Genetics. 1998. Т. 149. С. 879–892.84.Hadlow W.J. Letter to editor // Lancet. 1959.
Т. 2. С. 289–290.11085. Halfmann R., Jarosz D.F., Jones S.K., Chang A., Lancaster A.K., Lindquist S. Prions are acommon mechanism for phenotypic inheritance in wild yeasts // Nature. 2012b. Т. 482. № 7385. С.363–368.86. Halfmann R., Lindquist S. Screening for amyloid aggregation by semi-denaturing detergentagarose gel electrophoresis // NIH Public Access. 2009. Т. 17. № 2008.
С. 1–4.87. Halfmann R., Wright J.R., Alberti S., Lindquist S., Rexach M. Prion formation by a yeastGLFG nucleoporin // Prion. 2012a. Т. 6. № 4. С. 1–9.88. Helsen C.W., Glover J.R. Insight into molecular basis of curing of [PSI+] prion byoverexpression of 104-kDa heat shock protein (Hsp104) // J. Biol. Chem. 2012. Т.
287. № 1. С. 542–556.89. Higurashi T., Hines J.K., Sahi C., Aron R., Craig E. A. Specificity of the J-protein Sis1 in thepropagation of 3 yeast prions // Proc. Natl. Acad. Sci. U. S. A. 2008. Т. 105. № 43. С. 16596–601.90. Holmes D.L., Lancaster A.K., Lindquist S., Halfmann R. heritable remodeling of yeastmulticellularity by an environmentally responsive prion // Cell. 2013.
Т. 153. № 1. С. 153–165.91. Hosoda N., Kobayashi T., Uchida N., Funakoshi Y., Kikuchi Y., Hoshino S., Katada T.Translation termination factor eRF3 mediates mRNA decay through the regulation ofdeadenylation // J. Biol. Chem. 2003. Т. 278. № 40. С. 38287–91.92. Hou F., Sun L., Zheng H., Skaug B., Jiang Q.-X., Chen Z.J. MAVS forms functional prion-likeaggregates to activate and propagate antiviral innate immune response // Cell. 2011.
