Диссертация (1145920), страница 21
Текст из файла (страница 21)
V.10. (3). P. 182–206.182. Nizhnikova a, Antonets K.S., Inge-Vechtomov S.G. Amyloids: frompathogenesis to function // Biochem. 2015. V. 80. (9). P. 1127–1144.183. Norrby E. Prions and protein-folding diseases // J. Intern. Med. 2011. V. 270.(1). P. 1–14.184. Oesch B., Westaway D., Wälchli M., McKinley M.P., Kent S.B., Aebersold R.,Barry R.A., Tempst P., Teplow D.B., Hood L.E.
A cellular gene encodes scrapiePrP 27-30 protein. // Cell. 1985. V. 40. (4). P. 735–46.185. Oh J., Kim J.-G., Jeon E., Yoo C.-H., Moon J.S., Rhee S., Hwang I.Amyloidogenesis of type III-dependent harpins from plant pathogenic bacteria. //J. Biol. Chem. 2007. V. 282. (18). P.
13601–9.186. Olanow C.W., McNaught K. Parkinson’s disease, proteins, and prions:Milestones // Mov. Disord. 2011. V. 26. (6). P. 1056–1071.187. Oma Y., Kino Y., Sasagawa N., Ishiura S. Intracellular Localization ofHomopolymeric Amino Acid-containing Proteins Expressed in Mammalian Cells// J. Biol. Chem. 2004.
V. 279. (20). P. 21217–21222.188. Orlowska-Matuszewska G., Wawrzycka D. A novel phenotype of eight sporesasci in deletants of the prion-like Rnq1p in Saccharomyces cerevisiae // Biochem.Biophys. Res. Commun. 2006. V. 340. (1). P. 190–193.189. Osherovich L.Z., Cox B.S., Tuite M.F., Weissman J.S. Dissection and designof yeast prions. // PLoS Biol. 2004. V. 2. (4).
P. E86.190. Osherovich L.Z., Weissman J.S. Multiple Gln/Asn-rich prion domains confersusceptibility to induction of the yeast [PSI(+)] prion. // Cell. 2001. V. 106. (2).P. 183–94.127191. Ouchi E., Nomura N., Watabe S., Seiji K., Sato J. Clinical significance ofCongo red test // Tohoku J. Exp. Med.
1976. V. 118 Suppl. P. 191–198.192. Palmer E., Wilhelm J.M., Sherman F. Variation of phenotypic suppression dueto the psi+ and psi- extrachromosomal determinants in yeast. // J. Mol. Biol. 1979.V. 128. (1). P. 107–10.193. Paravastu A.K., Leapman R.D., Yau W.-M., Tycko R. Molecular structuralbasis for polymorphism in Alzheimer’s beta-amyloid fibrils. // Proc. Natl. Acad.Sci. U. S.
A. 2008. V. 105. (47). P. 18349–54.194. Patel A.J., Honoré E. Properties and modulation of mammalian 2P domain K+channels. // Trends Neurosci. 2001. V. 24. (6). P. 339–46.195. Patel B.K., Gavin-Smyth J., Liebman S.W. The yeast global transcriptional corepressor protein Cyc8 can propagate as a prion. // Nat. Cell Biol. 2009. V. 11.(3). P.
344–349.196. Pauly P.C., Harris D.A. Copper stimulates endocytosis of the prion protein. //J. Biol. Chem. 1998. V. 273. (50). P. 33107–10.197. Peretz D., Supattapone S., Giles K., Vergara J., Freyman Y., Lessard P., SafarJ.G., Glidden D. V., McCulloch C., Nguyen H.-O.B., Scott M., DeArmond S.J.,Prusiner S.B. Inactivation of Prions by Acidic Sodium Dodecyl Sulfate // J. Virol.2006. V. 80. (1). P. 322–331.198. Petkova A.T., Ishii Y., Balbach J.J., Antzutkin O.N., Leapman R.D., DelaglioF., Tycko R. A structural model for Alzheimer’s beta -amyloid fibrils based onexperimental constraints from solid state NMR. // Proc.
Natl. Acad. Sci. U. S. A.2002. V. 99. (26). P. 16742–7.199. Petkova A.T., Yau W.-M., Tycko R. Experimental constraints on quaternarystructure in Alzheimer’s beta-amyloid fibrils. // Biochemistry. 2006. V. 45. (2).P. 498–512.200. Picken M.M. Immunoglobulin light and heavy chain amyloidosis AL/AH: renalpathology and differential diagnosis. // Contrib. Nephrol. 2007. V. 153.
P. 135–55.128201. Polymeropoulos M.H., Lavedan C., Leroy E., Ide S.E., Dehejia A., Dutra A.,Pike B., Root H., Rubenstein J., Boyer R., Stenroos E.S., Chandrasekharappa S.,Athanassiadou A., Papapetropoulos T., Johnson W.G., Lazzarini A.M., DuvoisinR.C., Iorio G. Di, Golbe L.I., Nussbaum R.L. Mutation in the alpha-synucleingene identified in families with Parkinson’s disease. // Science. 1997. V. 276.(5321).
P. 2045–7.202. Poulopoulos M., Levy O.A., Alcalay R.N. The neuropathology of geneticParkinson’s disease. // Mov. Disord. 2012. V. 27. (7). P. 831–42.203. Pras M., Schubert M., Zucker-Franklin D., Rimon A., Franklin E.C. Thecharacterization of soluble amyloid prepared in water. // J. Clin.
Invest. 1968. V.47. (4). P. 924–933.204. Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. // Science.1982. V. 216. (4542). P. 136–44.205. Prusiner S.B., Scott M.R. Genetics of prions. // Annu. Rev. Genet. 1997. V. 31.P. 139–75.206. Radovanovic I., Braun N., Giger O.T., Mertz K., Miele G., Prinz M., NavarroB., Aguzzi A. Truncated prion protein and Doppel are myelinotoxic in the absenceof oligodendrocytic PrPC. // J. Neurosci. 2005.
V. 25. (19). P. 4879–88.207. Reidy M., Masison D.C. Modulation and elimination of yeast prions by proteinchaperones and co-chaperones. // Prion. 2011. V. 5. (4). P. 245–9.208. Reitz C., Brayne C., Mayeux R. Epidemiology of Alzheimer disease // Nat.Rev. Neurol. 2011. V. 7. (3). P. 137–152.209. Revesz T., Holton J.L., Doshi B., Anderton B.H., Scaravilli F., Plant G.T.Cytoskeletal pathology in familial cerebral amyloid angiopathy (British type)with non-neuritic amyloid plaque formation.
// Acta Neuropathol. 1999. V. 97.(2). P. 170–6.210. Riedel M., Goldbaum O., Richter-Landsberg C. α-Synuclein Promotes theRecruitment of Tau to Protein Inclusions in Oligodendroglial Cells: Effects ofOxidative and Proteolytic Stress // J. Mol. Neurosci. 2009. V. 39. (1–2). P. 226–234.129211. Riek R. The Three-Dimensional Structures of Amyloids. // Cold Spring Harb.Perspect. Biol. 2016.212. Roberts B.T., Wickner R.B. Heritable activity: a prion that propagates bycovalent autoactivation. // Genes Dev. 2003. V. 17. (17).
P. 2083–7.213. Rogoza T., Goginashvili A., Rodionova S., Ivanov M., Viktorovskaya O.,Rubel A., Volkov K., Mironova L. Non-Mendelian determinant [ISP+] in yeast isa nuclear-residing prion form of the global transcriptional regulator Sfp1.
// Proc.Natl. Acad. Sci. U. S. A. 2010. V. 107. (23). P. 10573–7.214. Rokitansky C. von. Handbuch der Speciellen Pathologischen Anatomica.Vienna: Braumuller und Seidel, 1842.215. Rose M.D., Winstone F., Hieter P. Methods in yeast genetics.
: CSHL Press.,1990. 198 p.216. Rowczenio D., Dogan A., Theis J.D., Vrana J.A., Lachmann H.J., WechalekarA.D., Gilbertson J.A., Hunt T., Gibbs S.D.J., Sattianayagam P.T., Pinney J.H.,Hawkins P.N., Gillmore J.D. Amyloidogenicity and Clinical PhenotypeAssociated with Five Novel Mutations in Apolipoprotein A-I // Am. J. Pathol.2011. V. 179.
(4). P. 1978–1987.217. Rubel A. a, Ryzhova T. a, Antonets K.S., Chernoff Y.O., Galkin A.Identification of PrP sequences essential for the interaction between the PrPpolymers and Aβ peptide in a yeast-based assay. // Prion. 2013. V. 7. (6). P. 1–8.218. Saifitdinova A.F., Nizhnikov A.A., Lada A.G., Rubel A.A., MagomedovaZ.M., Ignatova V. V., Inge-Vechtomov S.G., Galkin A.P. [NSI +]: a novel nonMendelian nonsense suppressor determinant in Saccharomyces cerevisiae // Curr.Genet.
2010. V. 56. (5). P. 467–478.219. Sakai M., Austin J., Witmer F., Trueb L. Studies of corpora amylacea. I.Isolation and preliminary characterization by chemical and histochemicaltechniques. // Arch. Neurol. 1969. V. 21. (5). P. 526–44.220. Sambrook J., Fritsch E.F., Maniatis T. Molecular cloning: a laboratory manual., 1989. 626 p.130221.
Saunders H.M., Bottomley S.P. Multi-domain misfolding: understanding theaggregation pathway of polyglutamine proteins // Protein Eng. Des. Sel. 2009. V.22. (8). P. 447–451.222. Schilling G., Becher M.W., Sharp A.H., Jinnah H.A., Duan K., Kotzuk J.A.,Slunt H.H., Ratovitski T., Cooper J.K., Jenkins N.A., Copeland N.G., Price D.L.,Ross C.A., Borchelt D.R. Intranuclear inclusions and neuritic aggregates intransgenic mice expressing a mutant N-terminal fragment of huntingtin.
// Hum.Mol. Genet. 1999. V. 8. (3). P. 397–407.223. Schleiden M.J. Einige Bermerkungen ueber den vegetabilischen Faserstoff undsein Verhaeltnis zum Staerkemehl. // Ann. Phys. 1838. V. 43. P. 397–397.224. Schneider K., Fangerau H., Michaelsen B., Raab W.H.M. The early history ofthe transmissible spongiform encephalopathies exemplified by scrapie // BrainRes. Bull. 2008. V. 77. (6). P. 343–355.225. Schwarz P. New patho-anatomic observations on amyloidosis in the aged.Fluorescence microscopic observations // Proc. Symp.
on Amyloidosis . In E.Mandema et al. (Ed.). Amsterdam: Excerpta Medica, 1967. P. 400–417.226. Schwimmer C., Masison D.C. Antagonistic interactions between yeast [PSI(+)]and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p butnot by Ssa2p. // Mol. Cell. Biol. 2002. V. 22. (11). P. 3590–8.227. Selkoe D.J., Abraham C.R., Podlisny M.B., Duffy L.K. Isolation of lowmolecular-weight proteins from amyloid plaque fibers in Alzheimer’s disease.
![](https://s.studizba.com/z.php?f=/templates/si/i/noavatar.png&w=100&h=100&t=1"){kind=avatar}
