Кафедра генетики и биотехнологии

Амилоиды, фолдинг белка, растительно-микробные взаимодействия, просвечивающая электронная микроскопия, генетика бактерий, вирулентность бактерий.

Belousov M.V., Kosolapova A.O., Fayoud H., Sulatsky M.I., Sulatskaya A.I., Romanenko M.N., Bobylev A.G., Antonets K.S., Nizhnikov A.A. OmpC and OmpF outer membrane proteins of Escherichia coli and Salmonella enterica form bona fide amyloids // International Journal of Molecular Sciences, 2023, V. 24(21), 15522 doi: 10.3390/ijms242115522
Sulatsky M.I., Belousov M.V., Kosolapova A.O., Mikhailova E.V., Romanenko M.N., Antonets K.S., Kuznetsova I.M., Turoverov K.K., Nizhnikov A.A., Sulatskaya A.I. Amyloid fibrils of Pisum sativum L. vicilin inhibit pathological aggregation of mammalian proteins // International Journal of Molecular Sciences, 2023, V. 24(16), 12932 doi: 10.3390/ijms241612932
Shikov A.E., Belousova M.E., Belousov M.V., Nizhnikov A.A., Antonets K.S. Salmonella-based biorodenticides: past applications and current contradictions // International Journal of Molecular Sciences, 2022, V. 23(23), 14595 doi: 10.3390/ijms232314595
Kosolapova A.O., Belousov M.V., Sulatsky M.I., Tsyganova A.V., Sulatskaya A.I., Bobylev A.G., Shtark O.Y., Tsyganov V.E., Volkov K.V., Zhukov V.A., Tikhonovich I.A., Nizhnikov A.A. RopB protein of Rhizobium leguminosarum bv. viciae adopts amyloid state during symbiotic interactions with pea (Pisum sativum L.) // Frontiers in Plant Science, 2022, 13, 1014699 doi: 10.3389/fpls.2022.1014699
Sokolov P.A., Rolich V.I., Vezo O.S., Belousov M.V., Bondarev S.A., Zhouravleva G.A., Kasyanenko N.A. Amyloid fibril length distribution from dynamic light scattering data // European Biophysics Journal, 2022, V. 51(4-5), P. 325-333. doi: 10.1007/s00249-022-01600-5
Kharkov B.B, Podkorytov I.S., Bondarev S.A., Belousov M.V., Salikov V.A., Zhouravleva G.A., Skrynnikov N.R. Role of rotational motion in diffusion NMR experiments on supramolecular assemblies: application to Sup35NM fibrils // Angewandte Chemie - International Edition, 2021. V. 60(28), 15441-15451. DOI: 10.1002/anie.202102408
Sulatskaya A.I., Kosolapova A.O., Bobylev A.G., Belousov M.V., Antonets K.S., Sulatsky M.I., Kuznetsova I.M., Turoverov K.K., Stepanenko O.V., Nizhnikov A.A. β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis // International Journal of Molecular Sciences, 2021, V. 22(21), 113616. DOI: 10.3390/ijms222111316
Danilov L.G., Moskalenko S.E., Matveenko A.G., Sukhanova X.V., Belousov M.V., Zhouravleva G.A., Bondarev S.A. The Human NUP58 Nucleoporin Can Form Amyloids In Vitro and In Vivo // Biomedicines, 2021, V. 9(10), 1451. DOI: 10.3390/biomedicines9101451
Antonets K.S., Belousov M.V., Sulatskaya A.I., Belousova M.E., Kosolapova A.O, Sulatsky M.I., Andreeva E.A., Zykin P.A., Malovichko Y.V., Shtark O.Y, Lykholay A.N, Volkov K.V., Kuznetsova I.M, Turoverov K.K., Kochetkova E.Y., Bobylev A.G., Usachev K.S., Demidov O.N., Tikhonovich I.A. and Nizhnikov A.A. Accumulation of storage proteins in plant seeds is mediated by amyloid formation // PLOS Biology, 2020. V. 18(7), e3000564. doi: 10.1371/journal.pbio.3000564
Kosolapova A.O., Antonets K.S., Belousov M.V., Nizhnikov A.A. Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions // International Journal of Molecular Sciences, 2020. V. 21(19), 7240. DOI: 10.3390/ijms21197240
Sulatskaya A.I., Bondarev S.A., Sulatsky M.I., Trubitsina N.P., Belousov M.V., Zhouravleva G.A., Llanos M., Kajava A.V., Kuznetsova I.M., Turoverov K.K. Point mutations affecting yeast prion propagation change the structure of its amyloid fibrils // Journal of Molecular Liquids, 2020, V. 314, 113618. doi: 10.1016/j.molliq.2020.113618
Drozdova P.B., Barbitoff Y.A., Belousov M.V., Skitchenko R.K., Rogoza T.M., Leclercq J., Kajava A.V., Matveenko A.G., Zhouravleva G.A., Bondarev S.A. Estimation of amyloid aggregate sizes with semi-denaturing detergent agarose gel electrophoresis and its limitations // Prion, 2020, V. 14(1), P. 118-128. doi: 10.1080/19336896.2020.1751574
Kosolapova A.O., Belousov M.V., Sulatskaya A.I., Belousova M.E., Sulatsky M.I., Antonets K.S., Volkov K.V., Lykholay A.N., Shtark O.Y., Vasileva E.N., Zhukov V.A., Ivanova A.N., Zykin P.A., Kuznetsova I.M., Turoverov K.K., Tikhonovich I.A. & Nizhnikov A.A. Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium Rhizobium leguminosarum // Biomolecules, 2019, V. 9(11), 694. DOI: 10.3390/biom9110694
Danilov L.G., Matveenko A.G., Ryzhkova V.E., Belousov M.V., Poleshuk O.I., Likholetova D.V., Sokolov P.A., Kasyanenko N.A., Kajava A.V., Zhouravleva G.A. & Bondarev S.A. Design of a new [PSI+]-no-more mutation in SUP35 with strong inhibitory effect on the [PSI+] prion propagation // Frontiers in Molecular Neuroscience, 2019, V. 12, 274. DOI: 10.3389/fnmol.2019.00274
Антонец К.С., Белоусов М.В., Белоусова М.Е., Нижников А.А. Транскрипционный регулятор Gln3 Saccharomyces cerevisiae демонстрирует прионоподобные свойства при сверхпродукции // Биохимия, 2019, Т. 84(4), С. 587-599. DOI: 10.1134/S0320972519040122 (Англоязычная версия: Antonets K.S., Belousov M.V., Belousova M.E., Nizhnikov A.A. The Gln3 transcriptional regulator of Saccharomyces cerevisiae manifests prion-like properties upon overproduction// Biochemistry (Moscow), 2019, V. 84(4), P. 441-451. DOI: 10.1134/S0006297919040126)
Belousov M.V., Bondarev S.A., Kosolapova A.O., Antonets K.S., Sulatskaya A.I., Sulatsky M.I., Zhouravleva G.A., Kuznetsova I.M., Turoverov K.K., Nizhnikov A.A. M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils // PLOS ONE, 2018, V. 13(1), e0191317. DOI: 10.1371/journal.pone.0191317
Sokolov P.A., Bondarev S.A., Belousov M.V., Zhouravleva G.A., Kasyanenko N.A. Sup35NMp Morphology Evaluation on Au, Si, Formvar and Mica Surfaces Using AFM, SEM and TEM // Journal of Structural Biology, 2018, V. 201(1), P. 5-14. DOI: 10.1016/j.jsb.2017.10.006
Сулацкий М.И., Сулацкая А.И., Родина Н.П., Белоусов М.В., Бондарев C.А., Журавлева Г.А., Туроверов К.К., Кузнецова И.М. Время жизни возбужденного состояния и анизотропия флуоресценции свободного и связанного с амилоидными фибриллами тиофлавина Т // Цитология, 2018, Т. 60(10), С. 838-841. DOI: 10.7868/S0041377118100168
Sokolov P.A., Belousov M.V., Bondarev S.A., Zhouravleva G.A., Kasyanenko N.A. FibrilJ: ImageJ plugin for fibrils' diameter and persistence length determination // Computer Physics Communications, 2017, V. 214, P. 199-206. DOI: 10.1016/j.cpc.2017.01.011
Бондарев С.А., Лихолетова Д.В., Белоусов М.В., Журавлева Г.А. Белок Rnq1 защищает прион [PSI+] от эффекта PNM мутации // Молекулярная биология, 2017, Т. 51(2), С. 367-371. DOI: 10.7868/S0026898417010050 (IF 0.29, Q4) (Англоязычная версия: Bondarev S.A., Likholetova D.V., Belousov M.V., Zhouravleva G.A. Rnq1 protein protects [PSI+] prion from effect of the PNM mutation // Molecular Biology, 2017, V. 51(2), P. 323-327. DOI: 10.1134/S0026893317010058)
Matveenko A.G., Drozdova P.B., Belousov M.V., Moskalenko S.E., Bondarev S.A., Barbitoff Yu.A., Nizhnikov A.A., Zhouravleva G.A. SFP1-mediated prion-dependent lethality is caused by increased Sup35 aggregation and alleviated by Sis1 // Genes to Cells, 2016, V. 21(10), P. 1290-1308. DOI 10.1111/gtc.12444
Матвеенко А.Г., Белоусов М.В., Бондарев С.А., Москаленко С.Е., Журавлева Г.А. Идентификация новых генов, влияющих на токсичность приона [PSI+] у дрожжей Saccharomyces cerevisiae // Молекулярная биология, 2016, Т. 50(5), С. 803-813. DOI: 10.7868/S0026898416050116 (IF 0.29, Q4) (Англоязычная версия: Matveenko A.G.; Belousov M.V.; Bondarev S.A.; Moskalenko S.E.; Zhouravleva G.A. Identification of new genes affecting [PSI+] prion toxicity in yeast Saccharomyces cerevisiae // Molecular Biology, 2016, V. 50(5), P. 710-718. DOI: 10.1134/S0026893316050113)
Sulatskaya A.I., Kuznetsova I.M., Belousov M.V., Bondarev S.A., Zhouravleva G.A., Turoverov K.K. Stoichiometry and affinity of Thioflavin T binding to Sup35p amyloid fibrils // PLOS ONE, 2016, 11(5), e0156314. DOI: 10.1371/journal.pone.0156314
Bondarev S.A., Zhouravleva G.A., Belousov M.V., Kajava A.V. Structure-based view on [PSI+] prion properties // Prion, 2015, 9(3), P. 190-199. DOI: 10.1080/19336896.2015.1044186

Кафедра генетики и биотехнологии - сотрудники