Диссертация (1144700), страница 32
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Cell.Biol. - 2001. - Vol. 153. - P. 1327-1336.245.Stathopulos P.B., Rumfeldt J., Scholz G.A., Irani R.A., Frey H.E. et al.Cu/Zn superoxide dismutase mutants associated with amyotrophic lateralsclerosis show enhanced formation of aggregates in vitro. // Proc Natl Acad SciUSA. // 2003. – Vol. 100. – P. 7021 - 7026246.Sugiyama S., Tanaka M.
Self-propagating amyloid as a critical regulatorfor diverse cellular functions. // J Biochem. – 2014. – V. 155, №6. –P. 345-351.247.Sun Y, Makarava N, Lee CI, Laksanalamai P, Robb FT, Baskakov IV.Conformational stability of PrP amyloid fibrils controls their smallest possiblefragment size.
// J Mol Biol. – 2008. V. 376, №4. – P. 1155-1167.248.Suzuki G., Shimazu N., Tanaka M. A yeast prion, Mod5, promotesacquired drug resistance and cell survival under environmental stress. // Science.– 2012. – Vol. 336. – P. 355 - 359.249.Swaney D.L., Beltrao P., Starita L., Guo A., Rush J. et al. Global analysisof phosphorylation and ubiquitylation cross-talk in protein degradation. // NatMethods. – 2013. – Vol. 10, № 7. – P. 676-82.250.Syed AK, Boles BR. Fold modulating function: bacterial toxins tofunctional amyloids. // Front Microbiol.
– 2014. – V. 5: 401.251.Tanaka M., Weissman J.S. An efficient protein transformation protocol forintroducing prions into yeast. // Methods Enzymol. – 2006 – Vol. 412. – P. 185 200.252.Taneja V., Maddelein M.L., Talarek N., Saupe S.J., Liebman S.W. A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion inyeast // Mol Cell. – 2007. - Vol.
27. - P. 67-77.253.Taylor K.L., Cheng N., Williams R.W., Steven A.C., Wickner R.B. Priondomain initiation of amyloid formation in vitro from native Ure2p // Science. –1999. – Vol. 283. – №5406. – P. 1339–1343.201254.Telling G.C., Parchi P., DeArmond S.J., Cortelli P., Montagna P. et al.Evidence for the conformation of the pathologic isoform of the prion proteinenciphering and propagating prion diversity // Science.
- 1996. - Vol. 274. - P.2079-2082.255.Terashima H., Hamada K., Kitada K. The localization change ofYbr078w/Ecm33, a yeast GPI-associated protein, from the plasma membrane tothe cell wall, affecting the cellular function. // FEMS Microbiol Lett. – 2003. Vol.218, № 1.
– P. 175 - 180.256.Ter-AvanesyanM.D.,KushnirovV.V.,DagkesamanskayaA.R.,Didichenko S.A., Chernoff Y.O., Inge-Vechtomov S.G., Smirnov V.N. Deletionanalysis of the SUP35 gene of the yeast Sacchoromyces cerevisiae reveals twonon-overlapping functional regions in the encoded protein // Mol. Microbiol. –1993.
– Vol. 7. – P. 683 – 692.257.Ter-Avanesyan M.D., Dagkesamanskaya A.R., Kushnirov V.V., SmirnovV.N. The SUP35 omnipotent suppressor gene is involved in the maintenance ofthe non-Mendelian determinant [PSI+] in the yeast Sacchoromyces cerevisiae //Genetics.
– 1994. – Vol. 137. – P. 671 – 676.258.Thual C., Komar A.A., Bousset L., Fernandez-Bellot E., Cullin C., MelkiR. Structural characterization of Saccharomyces cerevisiae prion-like proteinUre2 // J. Biol. Chem. - 1999. - Vol. 274. - P. 13666-13674.259.Tkach J.M., Yimit A., Lee A.Y., Riffle M., Costanzo M. et al. DissectingDNA damage response pathways by analysing protein localization and abundancechanges during DNA replication stress. // Nat Cell Biol. – 2012.
– Vol. 14, № 9. –P. 966 - 976.260.Tobler I., Gaus S.E., Deboer T., Achermann P., Fischer M., Rulicke T.,Moser M., Oesch B., McBride P.A., Manson J.C. Altered circadian activityrhythms and sleep in mice devoid of prion protein // Nature. – 1996. – Vol. 380. –P. 639–642.202261.Tuite M., Mundy, C.R., Cox, B.S. Agents that cause a high frequency ofgenetic change from [psi+] to [psi-] in Saccharomyces cerevisiae // Genetics.
–1981. – Vol. 98. – P. 691–711.262.Urakov V.N., Vishnevskaya A.B., Alexandrov I.M., Kushnirov V.V.,Smirnov V.N. et al. Interdependence of amyloid formation in yeast: implicationsfor polyglutamine disorders and biological functions. // Prion. – 2010. – Vol. 4. –P. 45-52.263.Valouev I.A., Fominov G.V., Sokolova E.E., Smirnov V.N., Ter-Avanesyan M.D.
Elongation factor eEF1B modulates functions of the releasefactors eRF1 and eRF3 and the efficiency of translation termination in yeast. //BMC Mol Biol. – 2009. – V. 10: 60.264.Van Melckebeke H., Wasmer C., Lange A., Ab E., Loquet A., BockmannA., Meier B.H. Atomic-resolution three-dimensional structure of HET-s(218-289)amyloid fibrils by solid-state NMR spectroscopy. // J Am Chem Soc. – 2010. Vol. 132, №39. - P. 13765-13775.265.Vana K., Zuber C., Nikles D., Weiss S. Novel Aspects of Prions, TheirReceptor Molecules, and Innovative Approaches for TSE Therapy // Cell.
Mol.Neurobiol. – 2007. – Vol. 27. – №1. – P. 107–128.266.Vishveshwara N., Bradley M.E., Liebman S.W. Sequestration of essentialproteins causes prion associated toxicity in yeast. // Mol Microbiol. – 2009. –Vol. 73, № 6. – P. 1101 - 1114.267.VitrenkoY.A.,GrachevaE.O.,RichmondJ.E.,LiebmanS.W.Visualization of aggregation of the Rnq1 prion domain and cross-seedinginteractions with Sup35NM.
// J Biol Chem. – 2007. – Vol. 282, № 3. – P. 1779 1787.268.Vogel J.L., Parsell D.A., Lindquist S. Heat-shock proteins Hsp104 andHsp70 reactivate mRNA splicing after heat inactivation. // Curr Biol. – 1995. –Vol. 5, № 3. – P. 306 - 317.269.Vonsattel J.P., DiFiglia M. Huntington disease. // J Neuropathol ExpNeurol. – 1998. – Vol. 57. - P 369 – 384.203270.Wang Y., Meriin A.B., Costello C.E., Sherman M.Y.
Characterization ofproteins associated with polyglutamine aggregates: a novel approach towardsisolation of aggregates from protein conformation disorders. // Prion. – 2007. Vol. 1. – P. 128 - 135.271.Wasmer C., Lange A., Van Melckebeke H., Siemer A.B., Riek R., MeierB.H. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with atriangular hydrophobic core // Science. - 2008. - Vol.
319. - P. 1523 - 1526.272.Weingarten M. D., Lockwood A. H., Hwo S. Y., Kirschner M. W. Aprotein factor essential for microtubule assembly. // Proc. Natl. Acad. Sci.U.S.A. – 1975. – Vol. 72. – P. 1858–1862.273.Westermark G.T., Westermark P. Serum amyloid A and protein AA:molecular mechanisms of a transmissible amyloidosis. // FEBS Lett. – 2009. –Vol. 583, № 16. – P. 2685 – 2690.274.Wickner R.B. [URE3] as an altered URE2 protein: evidence for a prionanalog in Saccharomyces cerevisiae. // Science.
– 1994. – V. 264, №5158. - P.566 - 569.275.Wickner R.B. A new prion controls fungal cell fusion incompatibility. //Proc Natl Acad Sci U S A. – 1997. Vol. 94, № 19. – P. 10012 - 10024.276.Wickner R.B., Edskes H.K., Maddelein M.L., Taylor K.L., Moriyama H.Prions of yeast and fungi.
Proteins as genetic material. // J Biol Chem. – 1999. –V. – 274, №2. – P. 555 - 558.277.Wickner R.B., Edskes H.K., Roberts B.T., Pierce M., Baxa U. Prions ofyeast as epigenetic phenomena: high protein "copy number" inducing protein"silencing". // Adv Genet. – 2002. – Vol. 46. – P.
485 - 525.278.Wickner R.B., Edskes H.K., Ross E.D., Pierce M.M., Baxa U., BrachmannA., Shewmaker F. Prion genetics: new rules for a new kind of gene // Annu. Rev.Genet. - 2004. - Vol. 38. - P. 681-707.279.Wickner RB.., Shewmaker F, Edskes H., Kryndushkin D., Nemecek J,McGlinchey R, Bateman D, Winchester CL. Prion amyloid structure explains204templating: how proteins can be genes. // FEMS Yeast Res. – 2010. - Vol.
8. – P.980-991.280.Wickner R.B., Edskes H.K., Bateman D., Kelly A.C., Gorkovskiy A. Theyeast prions [PSI+] and [URE3] are molecular degenerative diseases. // Prion.2011. – Vol. 4. – P. 258 – 262.281.Wickner R.B., Edskes H.K., Bateman D.A., Kelly A.C., Gorkovskiy A. etal. Amyloid diseases of yeast: prions are proteins acting as genes. // EssaysBiochem.
– 2014. – Vol. 56. – P. 193 - 205.282.Winderickx J., Delay C., De Vos A., Klinger H., Pellens K. et al. Proteinfolding diseases and neurodegeneration: lessons learned from yeast. // Biochimicaet Biophysica Acta. – 2008. – Vol. 1783. P. 1381 - 1395.283.Winklhofer K.F., Tatzelt J., Haass C. The two faces of protein misfolding:gain- and loss-of-function in neurodegenerative diseases.
// EMBO J. – 2008. –V. 27, №2. – P. 336 - 349.284.Xu Z., Norris D. The SFP1 gene product of Saccharomyces cerevisiaeregulates G2/M transitions during the mitotic cell cycle and DNA-damageresponse. The SFP1 gene product of Saccharomyces cerevisiae regulates G2/Mtransitions during the mitotic cell cycle and DNA-damage response. // Genetics.
–1998. Vol. 150, № 4. – P. 1419 - 1428.285.Yang Z., Stone D.E., Liebman S.W. Prion-promoted phosphorylation ofheterologous amyloid is coupled with ubiquitin-proteasome system inhibition andtoxicity. // Mol Microbiol. – 2014. – Vol.
93, № 5. – P. 1043 - 1056.286.Zakharov I.A., Yarovoy B.P. Cytoduction as a new tool in studying thecytoplasmic heredity in yeast. //Mol Cell Biochem. – 1977. Vol. 14, № 1-3. - P.15 – 18.287.Zhouravleva G.A., Frovola L., Le Goff X., Le Guellec R., Inge-VechtomovS.G. et al. Termination of translation in eukaryotes is governed by two interactingpolypeptide chain release factors, eRF1 and eRF3. // EMBO J. – 1995. – Vol. 14.– P.
4065 - 4072.205БЛАГОДАРНОСТИЯ хочу поблагодарить коллектив кафедры генетики и в особенности сотрудниковлабораторий генетики животных и физиологической генетики, где мнепосчастливилось работать.БлагодарюруководителейисотрудниковЦКП«Хромас»и«Развитиямолекулярных и клеточных технологий». Без них эта работа не могла бысостояться.Личную благодарность я хочу высказать С.Г. Инге-Вечтомову, А. Ф. Смирнову,П.А.
Зыкину, а также людям, принимавшим непосредственное участие в этойработе:А. Рубелю, О. Цапониной, А. Лада, З. Магомедовой, А. Сайфитдиновой,А. Нижникову, К. Антонцу, Т. Рыжовой, С. Задорскому и К. Волкову.Я благодарен своей супруге С.А. Галкиной и маме Е.А.
Галкиной за помощь иподдержку..