WWW.KONF.X-PDF.RU
- , ,
 


Pages:     | 1 |   ...   | 5 | 6 ||

SACCHAROMYCES CEREVISIAE ...

-- [ 7 ] --

226. Saifitdinova A.F., Nizhnikov A.A., Lada A.G., Rubel A.A, Magomedova Z.M., Ignatova V.V., Inge-Vechtomov S.G., Galkin A.P. [NSI+]: a novel nonMendelian nonsense suppressor determinant in Saccharomyces cerevisiae. // Curr Genet. 2010. Vol. 56, 5. P. 467 - 478.

227. Sipe J.D., Cohen A.S. Review: history of the amyloid fibril. // J Struct Biol.

- 2000. - Vol. 130. 2-3. P. 88-98.

228. Sipe J.D., Benson M.D., Buxbaum J.N., Ikeda S., Merlini G. et al.

Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis. // Amyloid. 2014. Vol. 21. . P. 221 224.

229. Sambrook J., Fritsch E.F., Maniatis T. Molecular cloning. A laboratory manual // New York: Cold Spring Harbor Lab. Press. 1989. 1626 p.

230. Sarantseva S., Timoshenko S., Bolshakova O., Karaseva E., Rodin D. et al.

Apolipoprotein E-mimetics inhibit neurodegeneration and restore cognitive functions in a transgenic Drosophila model of Alzheimer's disease. // PLoS One.

2009. Vol. 4, 12. - e8191.

231. Saupe S.J. The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility. // Semin Cell Dev Biol. 2011. V. 22, 5. - P.

460 - 468.

232. Schilling G., Becher M.W., Sharp A.H., Jinnah H.A., Duan K. et al.

Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. // Hum Mol Genet. 1999. Vol. 8. P. 397 407.

233. Schwarze-Eicker K., Keyvani K., Gortz N., Westaway D., Sachser N., Paulus W. Prion protein (PrPc) promotes beta-amyloid plaque formation // Neurobiol. Aging. - 2005. - V. 26, 8. - P. 1177 - 1182.

234. Schwimmer C., Masison D.C. Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p. // Mol Cell Biol. 2002. Vol. 22, 11. P. 3590 Selkoe D.J. Alzheimer's disease. // Cold Spring Harb Perspect Biol. 2011.

235.

- Vol. 3, 7. - pii: a004457.

236. Serio T.R., Cashikar A.G., Kowal A.S., Sawicki G.J., Moslehi J.J. et al. // Nucleated conformational conversion and the replication of conformational information by a prion determinant. // Science. 2000. Vol. 289. P. 1317 Sherman F., Fink G.R., Hinks J.B. Methods in Yeast Genetics. // Cold Spring Harbor Lab Press, New-York. - 1986.

238. Shewmaker F., McGlinchey R.P., Wickner R.B. Structural insights into functional and pathological amyloid. // J Biol Chem. 2011. Vol. 286, 19. P. 16533 - 16540.

239. Si K., Choi Y., White-Grindley E., MajumdarA., Kandel E. Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation. // Cell. - 2010. V. 140, 3. - P. 421 - 435.

240. Sikorski R.S., Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. // Genetics. 1989. Vol. 122. P. 19-27.

241. Snow A.D., Sekiguchi R., Nochlin D., Fraser P., Kimata K. et al. An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A beta-amyloid in rat brain. // Neuron. 1994. Vol. 12, 1. P. 219 - 234.

242. Sondheimer N. and Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast // Mol. Cell. - 2000. - Vol. 5. - P. 163 - 172.

243. Sondheimer N, Lopez N, Craig EA, Lindquist S. The role of Sis1 in the maintenance of the [RNQ+] prion. // EMBO J. 2001. Vol. 20, 10. P.

2435 - 2442.

244. Speransky V.V., Taylor K.L., Edskes H.K., Wickner R.B., Steven A.C.

Prion filament networks in [URE3] cells of Saccharomyces cerevisiae // J. 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 lateral sclerosis show enhanced formation of aggregates in vitro. // Proc Natl Acad Sci USA. // 2003. Vol. 100. P. 7021 - 7026

246. Sugiyama S., Tanaka M. Self-propagating amyloid as a critical regulator for 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 possible fragment size. // J Mol Biol. 2008. V. 376, 4. P. 1155-1167.

248. Suzuki G., Shimazu N., Tanaka M. A yeast prion, Mod5, promotes acquired 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 analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. // Nat Methods. 2013. Vol. 10, 7. P. 676-82.

250. Syed AK, Boles BR. Fold modulating function: bacterial toxins to functional amyloids. // Front Microbiol. 2014. V. 5: 401.

251. Tanaka M., Weissman J.S. An efficient protein transformation protocol for introducing prions into yeast. // Methods Enzymol. 2006 Vol. 412. P. 185 Taneja V., Maddelein M.L., Talarek N., Saupe S.J., Liebman S.W. A nonQ/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast // Mol Cell. 2007. - Vol. 27. - P. 67-77.

253. Taylor K.L., Cheng N., Williams R.W., Steven A.C., Wickner R.B. Prion domain initiation of amyloid formation in vitro from native Ure2p // Science. 1999. Vol. 283. 5406. P. 13391343.

254. 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 protein enciphering and propagating prion diversity // Science. - 1996. - Vol. 274. - P.

2079-2082.

255. Terashima H., Hamada K., Kitada K. The localization change of Ybr078w/Ecm33, a yeast GPI-associated protein, from the plasma membrane to the cell wall, affecting the cellular function. // FEMS Microbiol Lett. 2003. Vol.

218, 1. P. 175 - 180.

256. Ter-Avanesyan M.D., Kushnirov V.V., Dagkesamanskaya A.R., Didichenko S.A., Chernoff Y.O., Inge-Vechtomov S.G., Smirnov V.N. Deletion analysis of the SUP35 gene of the yeast Sacchoromyces cerevisiae reveals two non-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., Smirnov V.N. The SUP35 omnipotent suppressor gene is involved in the maintenance of the 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., Melki R. Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2 // J. Biol. Chem. - 1999. - Vol. 274. - P. 13666-13674.

259. Tkach J.M., Yimit A., Lee A.Y., Riffle M., Costanzo M. et al. Dissecting DNA damage response pathways by analysing protein localization and abundance changes 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 activity rhythms and sleep in mice devoid of prion protein // Nature. 1996. Vol. 380. P. 639642.

261. Tuite M., Mundy, C.R., Cox, B.S. Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae // Genetics. 1981. Vol. 98. P. 691711.

262. Urakov V.N., Vishnevskaya A.B., Alexandrov I.M., Kushnirov V.V., Smirnov V.N. et al. Interdependence of amyloid formation in yeast: implications for 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., TerAvanesyan M.D. Elongation factor eEF1B modulates functions of the release factors 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., Bockmann A., 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, Their Receptor Molecules, and Innovative Approaches for TSE Therapy // Cell. Mol.

Neurobiol. 2007. Vol. 27. 1. P. 107128.

266. Vishveshwara N., Bradley M.E., Liebman S.W. Sequestration of essential proteins causes prion associated toxicity in yeast. // Mol Microbiol. 2009. Vol. 73, 6. P. 1101 - 1114.

267. Vitrenko Y.A., Gracheva E.O., Richmond J.E., Liebman S.W.

Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM. // J Biol Chem. 2007. Vol. 282, 3. P. 1779 Vogel J.L., Parsell D.A., Lindquist S. Heat-shock proteins Hsp104 and Hsp70 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 Exp Neurol. 1998. Vol. 57. - P 369 384.

270. Wang Y., Meriin A.B., Costello C.E., Sherman M.Y. Characterization of proteins associated with polyglutamine aggregates: a novel approach towards isolation 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., Meier B.H. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core // Science. - 2008. - Vol. 319. - P. 1523 - 1526.

272. Weingarten M. D., Lockwood A. H., Hwo S. Y., Kirschner M. W. A protein factor essential for microtubule assembly. // Proc. Natl. Acad. Sci.

U.S.A. 1975. Vol. 72. P. 18581862.

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 prion analog 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 of yeast 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., Brachmann A., 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 explains templating: 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. The yeast 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. et al. Amyloid diseases of yeast: prions are proteins acting as genes. // Essays Biochem. 2014. Vol. 56. P. 193 - 205.

282. Winderickx J., Delay C., De Vos A., Klinger H., Pellens K. et al. Protein folding diseases and neurodegeneration: lessons learned from yeast. // Biochimica et 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 cerevisiae regulates G2/M transitions during the mitotic cell cycle and DNA-damage response. The SFP1 gene product of Saccharomyces cerevisiae regulates G2/M transitions 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 of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity. // Mol Microbiol. 2014. Vol. 93, 5. P. 1043 - 1056.

286. Zakharov I.A., Yarovoy B.P. Cytoduction as a new tool in studying the cytoplasmic 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-Vechtomov S.G. et al. Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. // EMBO J. 1995. Vol. 14.

P. 4065 - 4072.

, .

. .

.. -, . . , .. , , :

. , . , . , . , . , . , . , . , . . .

.. .. .



Pages:     | 1 |   ...   | 5 | 6 ||
 

:

( . ) 03.02.14 : ..., .. 1. ...

(OVIBOS MOSCHATUS ZIMMERMANN, 1780) 03.02.08 : . . ., . . 2015 .. 1. -...

, BRCA1/2 14.03.09 , : .. 2015 .. 3 .. 5 I....

13.00.01 , : , ,...

BRUCELLA ABORTUS 19 BA, FRANCISELLA TULARENSIS 15 , YERSINIA PESTIS EV 03.02.03 :...

06.02.03 : , ...

03.01.00 : -. , , ... .. ...







 
<<     |    
2016 www.konf.x-pdf.ru - - , ,

, .
, , , , 1-2 .