Диссертация (1144259), страница 22
Текст из файла (страница 22)
// International Scientific Conference Science of the Future (17-20September 2014, Saint-Petersburg, Russia). – 2014, abstract onlinehttp://www.p220conf.ru/abstracts/download/2-life/334-v-zhemkov15. Zhemkov V.A., Vali S., Gagarskaya Y.A., Kulminskaya A.A., Vlasova O.L.,Bezprozvanny I.B., Kim M.W. Co-crystallization of streptavidin withbiotinylatedhuntingtin N17 domain. // Calcium 2014: From basics to bedside.Conference proceedings.
– 2014. – C. 516. Жемков В.А., Власова О.Л. Определение структуры N-концевогоучастка белка хантингтина в комплексе с пептоидным лигандом HNP1. // XLIIнаучно-практическая конференция с международным участием «Неделя наукиСПбГПУ». Cборник Института физики, нанотехнологий и телекоммуникаций.
–2013. – T.2. – С. 185-187.17. Жемков В.А., Дрожжина Т.А., Ким М.В., Вали Ш., Безпрозванный И.Б.Структура N-терминального конца хантингтина в комплексе с пептоидом HNP1. //Всероссийская конференция «Системно-технические решения проблемвизуализации в нейродегенерации». Сборник тезисов.
– 2013. – С. 4-8.- 125 -18. Drozhzhina T., Zhemkov V., Vali S., Jimin P., Grishin N., Bezprozvanny I.,Kim M.W. Structure of Huntingtin N-terminal region in complex with designed proteinligands. // 18th International Conference on Calcium Binding Proteins and CalciumFunction in Health and Disease. Conference proceedings. – 2013. – С. 20.- 126 -СПИСОК ЛИТЕРАТУРНЫХ ИСТОЧНИКОВ[1] Costa Mdo C., Paulson H. L. Toward understanding Machado-Joseph disease // ProgNeurobiol. -- 2012. -- May.
-- T. 97, № 2. -- C. 239-57.[2] Zoghbi H. Y., Orr H. T. Glutamine repeats and neurodegeneration // Annu RevNeurosci. -- 2000. -- T. 23. -- C. 217-47.[3] Ross C. A. Polyglutamine pathogenesis: emergence of unifying mechanisms forHuntington's disease and related disorders // Neuron. -- 2002.
-- Aug 29. -- T. 35, № 5. - C. 819-22.[4] La Spada A. R., Taylor J. P. Repeat expansion disease: progress and puzzles indisease pathogenesis // Nat Rev Genet. -- 2010. -- Apr. -- T. 11, № 4. -- C. 247-58.[5] Kim M. Pathogenic polyglutamine expansion length correlates with polarity of theflanking sequences // Mol Neurodegener. -- 2014. -- Nov 6. -- T. 9. -- C. 45.[6] Almeida B., Fernandes S., Abreu I. A., Macedo-Ribeiro S. Trinucleotide repeats: astructural perspective // Front Neurol. -- 2013.
-- T. 4. -- C. 76.[7] Nicastro G., Menon R. P., Masino L., Knowles P. P., McDonald N. Q., Pastore A.The solution structure of the Josephin domain of ataxin-3: structural determinants formolecular recognition // Proc Natl Acad Sci U S A. -- 2005. -- Jul 26. -- T. 102, № 30.
- C. 10493-8.[8] Mao Y., Senic-Matuglia F., Di Fiore P. P., Polo S., Hodsdon M. E., De Camilli P.Deubiquitinating function of ataxin-3: insights from the solution structure of theJosephin domain // Proc Natl Acad Sci U S A. -- 2005. -- Sep 6. -- T. 102, № 36. -- C.12700-5.[9] Satoh T., Sumiyoshi A., Yagi-Utsumi M., Sakata E., Sasakawa H., Kurimoto E.,Yamaguchi Y., Li W., Joazeiro C. A., Hirokawa T., Kato K.
Mode of substraterecognition by the Josephin domain of ataxin-3, which has an endo-type deubiquitinaseactivity // FEBS Lett. -- 2014. -- Nov 28. -- T. 588, № 23. -- C. 4422-30.[10] Weeks S. D., Grasty K. C., Hernandez-Cuebas L., Loll P. J. Crystal structure of aJosephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinatingactivity // J Biol Chem.
-- 2011. -- Feb 11. -- T. 286, № 6. -- C. 4555-65.[11] Song A. X., Zhou C. J., Peng Y., Gao X. C., Zhou Z. R., Fu Q. S., Hong J., Lin D.H., Hu H. Y. Structural transformation of the tandem ubiquitin-interacting motifs inataxin-3 and their cooperative interactions with ubiquitin chains // PLoS One.
-- 2010. -Oct 7. -- T. 5, № 10. -- C. e13202.[12] Masino L., Kelly G., Leonard K., Trottier Y., Pastore A. Solution structure ofpolyglutamine tracts in GST-polyglutamine fusion proteins // FEBS Lett. -- 2002. -- Feb27. -- T. 513, № 2-3. -- C. 267-72.[13] Kawaguchi Y., Okamoto T., Taniwaki M., Aizawa M., Inoue M., Katayama S.,Kawakami H., Nakamura S., Nishimura M., Akiguchi I., et al.
CAG expansions in anovel gene for Machado-Joseph disease at chromosome 14q32.1 // Nat Genet. -- 1994. - Nov. -- T. 8, № 3. -- C. 221-8.[14] Nicastro G., Todi S. V., Karaca E., Bonvin A. M., Paulson H. L., Pastore A.Understanding the role of the Josephin domain in the PolyUb binding and cleavageproperties of ataxin-3 // PLoS One. -- 2010. -- Aug 26. -- T. 5, № 8. -- C. e12430.- 127 -[15] Scaglione K. M., Zavodszky E., Todi S. V., Patury S., Xu P., Rodriguez-Lebron E.,Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J. E., Paulson H.
L. Ube2w andataxin-3 coordinately regulate the ubiquitin ligase CHIP // Mol Cell. -- 2011. -- Aug 19.-- T. 43, № 4. -- C. 599-612.[16] Warrick J. M., Morabito L. M., Bilen J., Gordesky-Gold B., Faust L. Z., Paulson H.L., Bonini N. M. Ataxin-3 suppresses polyglutamine neurodegeneration in Drosophilaby a ubiquitin-associated mechanism // Mol Cell. -- 2005. -- Apr 1. -- T. 18, № 1. -- C.37-48.[17] Sowa M. E., Bennett E. J., Gygi S.
P., Harper J. W. Defining the humandeubiquitinating enzyme interaction landscape // Cell. -- 2009. -- Jul 23. -- T. 138, № 2.-- C. 389-403.[18] Mazzucchelli S., De Palma A., Riva M., D'Urzo A., Pozzi C., Pastori V., ComelliF., Fusi P., Vanoni M., Tortora P., Mauri P., Regonesi M. E. Proteomic and biochemicalanalyses unveil tight interaction of ataxin-3 with tubulin // Int J Biochem Cell Biol. -2009.
-- Dec. -- T. 41, № 12. -- C. 2485-92.[19] Kristensen L. V., Oppermann F. S., Rauen M. J., Fog K., Schmidt T., Schmidt J.,Harmuth T., Hartmann-Petersen R., Thirstrup K. Mass spectrometry analyses of normaland polyglutamine expanded ataxin-3 reveal novel interaction partners involved inmitochondrial function // Neurochem Int. -- 2018. -- Jan.
-- T. 112. -- C. 5-17.[20] Boeddrich A., Gaumer S., Haacke A., Tzvetkov N., Albrecht M., Evert B. O.,Muller E. C., Lurz R., Breuer P., Schugardt N., Plassmann S., Xu K., Warrick J. M.,Suopanki J., Wullner U., Frank R., Hartl U. F., Bonini N. M., Wanker E.
E. Anarginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3fibrillogenesis // EMBO J. -- 2006. -- Apr 5. -- T. 25, № 7. -- C. 1547-58.[21] Durcan T. M., Kontogiannea M., Thorarinsdottir T., Fallon L., Williams A.
J.,Djarmati A., Fantaneanu T., Paulson H. L., Fon E. A. The Machado-Joseph diseaseassociated mutant form of ataxin-3 regulates parkin ubiquitination and stability // HumMol Genet. -- 2011. -- Jan 1. -- T. 20, № 1. -- C. 141-54.[22] Kuhlbrodt K., Janiesch P. C., Kevei E., Segref A., Barikbin R., Hoppe T. TheMachado-Joseph disease deubiquitylase ATX-3 couples longevity and proteostasis //Nat Cell Biol.
-- 2011. -- Mar. -- T. 13, № 3. -- C. 273-81.[23] Michalik A., Van Broeckhoven C. Pathogenesis of polyglutamine disorders:aggregation revisited // Hum Mol Genet. -- 2003. -- Oct 15. -- T. 12 Spec No 2. -- C.R173-86.[24] Seidel K., Siswanto S., Fredrich M., Bouzrou M., Brunt E. R., van Leeuwen F. W.,Kampinga H. H., Korf H. W., Rub U., den Dunnen W. F. Polyglutamine aggregation inHuntington's disease and spinocerebellar ataxia type 3: similar mechanisms in aggregateformation // Neuropathol Appl Neurobiol. -- 2016.
-- Feb. -- T. 42, № 2. -- C. 153-66.[25] Hoffner G., Djian P. Polyglutamine Aggregation in Huntington Disease: DoesStructure Determine Toxicity? // Mol Neurobiol. -- 2015. -- Dec. -- T. 52, № 3. -- C.1297-1314.[26] Hoffner G., Djian P. Monomeric, oligomeric and polymeric proteins in huntingtondisease and other diseases of polyglutamine expansion // Brain Sci. -- 2014. -- Mar 3. -T. 4, № 1. -- C. 91-122.- 128 -[27] Iuchi S., Hoffner G., Verbeke P., Djian P., Green H. Oligomeric and polymericaggregates formed by proteins containing expanded polyglutamine // Proc Natl AcadSci U S A. -- 2003.
-- Mar 4. -- T. 100, № 5. -- C. 2409-14.[28] Pelassa I., Fiumara F. Differential Occurrence of Interactions and InteractionDomains in Proteins Containing Homopolymeric Amino Acid Repeats // Front Genet. -2015. -- T. 6. -- C. 345.[29] Pelassa I., Cora D., Cesano F., Monje F. J., Montarolo P. G., Fiumara F.Association of polyalanine and polyglutamine coiled coils mediates expansion diseaserelated protein aggregation and dysfunction // Hum Mol Genet.
-- 2014. -- Jul 1. -- T.23, № 13. -- C. 3402-20.[30] Perez M. K., Paulson H. L., Pendse S. J., Saionz S. J., Bonini N. M., Pittman R. N.Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation// J Cell Biol. -- 1998. -- Dec 14. -- T. 143, № 6. -- C. 1457-70.[31] Masino L., Nicastro G., De Simone A., Calder L., Molloy J., Pastore A. TheJosephin domain determines the morphological and mechanical properties of ataxin-3fibrils // Biophys J. -- 2011. -- Apr 20.















