Федеральное государственное бюджетное учреждение науки
 ИНСТИТУТ БИОЛОГИИ РАЗВИТИЯ им. Н.К. Кольцова РАН
Koltzov Institute of Developmental Biology of Russian Academy of Sciences
Close

Почта ИБР РАН


Логин:
(e.mail полностью)

Пароль:

Лаборатория БИОХИМИИ ПРОЦЕССОВ ОНТОГЕНЕЗА

Публикации за 2022 г.

  1. Карпов Н.С., Ерохов П.А., Шарова Н.П., Астахова Т.М. Каким образом развитие тонкого кишечника крысы связано с изменениями в пуле протеасом?//Онтогенез. 2022. Т. 53. № 1. С. 46-57. DOI: 10.31857/s0475145022010049. – R. – Karpov N.S., Erokhov P.A., Sharova N. P., Astakhova T.M.1 How Is the Development of the Rat's Small Intestine Related to Changes in the Proteasome Pool?//Russian Journal of Developmental Biology. 2022. Vol. 53. Is. 1. P. 41-50. DOI: 10.1134/S1062360422010040. – Q4.
  2. Шмакова А.А., Шмакова О.П., Карпухина А.А., Васецкий Е.С.1 CRISPR/Cas: История и перспективы//Онтогенез. 2022. Т. 53. № 4. С. 287–300. DOI: 10.31857/S0475145022040073. – R. – Shmakova A.A., Shmakova O.P., Karpukhina A.A., Vassetzky Y.S.1 CRISPR/Cas: History and Perspectives//Russian Journal of Developmental Biology. 2022. Vol. 53. P. 272-282. DOI: 10.1134/S1062360422040075 – Q4.
  3. Шмакова А.А., Климович П.С., Рысенкова К.Д., Попов В.С., Горбунова А.С., Карпухина А.А., Карагяур М.Н., Рубина К.А., Семина Е.В. Переоценка роли рецептора урокиназы UPAR в онкологии: подавление экспрессии UPAR снижает пролиферацию, но вызывает химиорезистентность, дормантность и метастазирование в клетках нейробластомы//Вопросы онкологии. 2022. Т. 68. № S3. С. 353-355.
  4. Boguslavsky D.V., Sharova N.P., Sharov K.S. Public Policy Measures to Increase Anti-SARS-CoV-2 Vaccination Rate in Russia//International Journal of Environmental Research and Public Health. 2022. Vol. 19(6). Art. no. 3387. DOI: 10.3390/ijerph19063387. – Q1.
  5. Boguslavsky D.V., Sharova N.P., Sharov K.S. Evolutionary Challenges to Humanity Caused by Uncontrolled Carbon Emissions: The Stockholm Paradigm//Int. J. Environ. Res. Public Health. 2022. Vol. 19. Art.no 16920. DOI: 10.3390/ijerph192416920. — Q1.
  6. Boguslavsky D.V., Sharov K.S., Sharova N.P. Counteracting conspiracy ideas as a measure of increasing propensity for COVID-19 vaccine uptake in Russian society//Journal of Global Health. 2022. Vol. 12. Art. no 03013. DOI: 10.7189/jogh.12.03013. – Q1.
  7. Boguslavsky D.V., Sharov K.S., Sharova N.P. Using Alternative Sources of Energy for Decarbonization: A Piece of
  8. Canoy R.J., Shmakova A., Karpukhina A., Shepelev M., Germini D., Vassetzky Y.2 Factors That Affect the Formation of Chromosomal Translocations in Cells//Cancers. 2022. 14(20). Art. no. 5110. DOI: 10.3390/cancers14205110 – Q1
  9. Gordeeva O., Gordeev A., Erokhov P.1 Archetypal Architecture Construction, Patterning, and Scaling Invariance in a 3D Embryoid Body Differentiation Model//Front Cell Dev Biol. 2022. Vol. 10. Art. no 852071. DOI: 10.3389/fcell.2022.852071. eCollection 2022. – Q1.
  10. Johnson S., Karpova Y., Guo D., Ghatak A., Markov D., Tulin A.V. PARG suppresses tumorigenesis and downregulates genes controlling angiogenesis, inflammatory response, and immune cell recruitment//BMC Cancer. 2022. Vol. 22. Is. 1. Art no 557 DOI: 10.1186/s12885-022-09651-9. – Q2.
  11. Кarpova Y., Johnsona S.J., Bordet G., Guo D., Ghatak A., Markov D.A., Tulin A.V. Upregulation of PARG in prostate cancer cells suppresses their malignant behavior and downregulates tumor-promoting genes//Biomedicine & Pharmacotherapy. 2022. Vol. 153. Art. no 113504. DOI: 10.1016/j.biopha.2022.113504. – Q1.
  12. Kiseleva E., Serbina O., Karpukhina A., Mouly V., Vassetzky Y. S. Interaction between mesenchymal stem cells and myoblasts in the context of facioscapulohumeral muscular dystrophy contributes to the disease phenotype//Journal of Cellular Physiology. 2022. P. 1–10. DOI: 10.1002/jcp.30789. – Q1.
  13. Krajewski W.A. Histone Modifications, Internucleosome Dynamics, and DNA Stresses: How They Cooperate to “Functionalize” Nucleosomes//Frontiers in Genetics. 2022. Vol. 1328. Art no 873398. DOI: 10.3389/fgene.2022.873398. – Q1.
  14. Kurnaeva M.A., Zalevsky O., Arifulin E.A., Lisitsyna O.M, Tvorogova A.V., Shubina M.Y., Bourenkov G.P., Tikhomirova M.A., Potashnikova D.M., Kachalova A.I., Musinova Y.R., Golovin A.V., Vassetzky Y.S., Sheval E.V. Molecular coevolution of nuclear and nucleolar localization signals inside the basic domain of HIV-1 Tat//Journal of Virology. 2022. Vol. 96. Is. 1. Art. no. e01505-21. DOI: 10.1128/JVI.01505-21. – Q1.**.
  15. Morozov A., Astakhova T., Erokhov P., Karpov V. The ATP/Mg2+ Balance Affects the Degradation of Short Fluorogenic Substrates by the 20S Proteasome//Methods and Protocols. 2022. Vol. 5. Is. 1. Art. no. 15. DOI:10.3390/mps5010015. – Q.
  16. Sengupta Bh., Huynh M., Smith Ch.B., McGinty R.K., Krajewski W., Lee T.-H. The Effects of Histone H2B Ubiquitylations on the Nucleosome Structure and Internucleosomal Interactions//Biochemistry. 2022. Vol. 61. Is. 20. P. 2198–2205. DOI: 10.1021/acs.biochem.2c00422. – Q3.
  17. Shmakova A., Lomov N., Viushkov V., Tsfasman T., Kozhevnikova Y., Sokolova D., Pokrovsky V., Syrkina M., Germini D., Rubtsov M.,Vassetzky Y.S.2 Cell models with inducible oncogenic translocations allow to evaluate the potential of drugs to favor secondary translocations//Cancer Communications. 2022. DOI: 10.1002/cac2.12370. – Q1.
  18. Shmakova A.A., Klimovich P.S., Rysenkova K.D., Popov V.S., Gorbunova A.S., Karpukhina A.A., Karagyaur M.N., Rubina K.A., Tkachuk V.A., Semina E.V. Urokinase Receptor uPAR Downregulation in Neuroblastoma Leads to Dormancy, Chemoresistance and Metastasis//Cancers. 2022. Vol. 14(4). Art. no. 994. DOI: 10.3390/cancers14040994. – Q1.
  19. Shmakova A., Vassetzky Y.2 lncRNA: a new danger for genome integrity//International Journal of Cancer. 2022. DOI: 10.1002/ijc.34397. – Q1.
  20. Valyaeva A.A., Tikhomirova M.A., Bogomazova A.N., Snigiryova G.P., Penin A.A., Logacheva M.D., Arifulin E.A., Shmakova A.A., Zharikova A.A., Potashnikova D.M., Germini D., Kachakova A.I., Saidova A.A., Musinova Y.R., Mironov A.A., Vassetzky Y.S., Sheval E.V. Ectopic expression of HIV-1 Tat modifies gene expression in cultured B cells: possible implications for development of B-cell lymphomas in HIV-1-infected patients//PeerJ. 2022. DOI: 10.7717/peerj.13986. hal-03796238.
  21. Vassetzky Y.S., Mège R.D. SETDB1 fuels the lung cancer phenotype by modulating epigenome, 3D genome organization and chromatin mechanical properties//Nucleic Acids Research. 2022. Vol. 50. Is 8. P. 4389 – 4413. DOI: 10.1093/nar/gkac234. – Q1
  22. Viushkov V.S., Lomov N.A., Rubtsov M.A., Vassetzky Y.S. Visualizing the Genome: Experimental Approaches for Live-Cell Chromatin Imaging//Cells. 2022. Vol. 11. Is. 24. Art. no. 4086. DOI: 10.3390/cells11244086. – Q2.
  23. Zakharova V.V., Magnitov M.D., Del Maestro L., Ulianov S.V., Glentis A., Uyanik B., Williart A., Karpukhina A., Demidov O., Joliot V.,Vassetzky Y.S., Mège R.D. SETDB1 fuels the lung cancer phenotype by modulating epigenome, 3D genome organization and chromatin mechanical properties//Nucleic Acids Research. 2022. Vol. 50. Is 8. P. 4389 – 4413. DOI: 10.1093/nar/gkac234. – Q1.

Публикации за 2021 г.

Публикации в отечественных журналах
  1. Игнатюк В.М., Извольская М.С., Захарова Л.А. Стресс при беременности и нарушения развития нейроэндокринной, иммунной и репродуктивной систем у потомства в пренатальном и постнатальном онтогенезе: от эксперимента к разработке подходов сохранения здоровья у человека//Акушерство и гинекология. 2021. № 8. С. 69-74. DOI: 10. 8565/aig.2021.8.69-74. – R. – Ignatyuk V.M., Izvolskaya M.S., Zakharova L.A. Stress during pregnancy and developmental abnormalities of the neuroendocrine, immune, and reproductive systems in offspring during prenatal and postnatal ontogenesis: From the experiment to the elaboration of approaches to preserving human health//Akusherstvo i Ginekologiya (Russian Federation). 2021. Vol. 8. P. 69-74. DOI:10. 8565/aig.2021.8.69-74. – S.
  2. Кравчук О.И., Бураков А.В., Горностаев Н.Г., Михайлов К.В., Адамейко К.И., Финошин А.Д., Георгиев А.А., Михайлов В.С., Ерюкова Ю.Э., Рубиновский Г.А., Заиц Д.В., Газизова Г.Р., Гусев О.А., Шагимарданова Е.И., Люпина Ю.В. . Деацетилазы гистонов в процессе реагрегации клеток губки Halisarca dujardinii//Онтогенез. 2021. Т. 52. № 5. С. 367-383. DOI: 10.31857/S0475145021050050. – R. – Kravchuk O.I., Burakov A.V., Gornostaev N.G., Mikhailov K.V., Adameyko K.I., Finoshin A.D., Georgiev A.A., Mikhailov V.S., Yeryukova Y.E., Rubinovsky G.A., Zayts D.V., Gazizova G.R., Gusev O.A., Shagimardanova E.I., Lyupina Y.V. Histone deacetylases in the process of Halisarca dujardini cell reaggregation//Russian Journal of Developmental Biology. 2021. Vol. 52. № 5. P. 319–333. DOI: 10. 134/S1062360421050052. – Q4
Публикации в зарубежных журналах
  1. Adameyko K.I., Burakov A.V., Finoshin A.D., Mikhailov K.V., Kravchuk O.I., Kozlova O.S., Gornostaev N.G., Cherkasov A.V., Erokhov P.A., Indeykina M.I., Bugrova A.E., Kononikhin A.S., Moiseenko A.V., Sokolova O.S., Bonchuk A.N., Zhegalova I.V., Georgiev A.A., Mikhailov V.S., Gogoleva N.E., Gazizova G.R., Shagimardanova E.I., Gusev O.A., Lyupina Yu.V. Conservative and Atypical Ferritins of Sponges//International Journal of Molecular Sciences. 2021. Vol. 22. Is. 16. Art no. 8635. DOI: 10.3390/ijms22168635. – Q1.
  2. Akbay B., Germini D., Bissenbaev A.K., Musinova Y.R., Sheval E.V., Vassetzky Y., Dokudovskaya S. Hiv-1 tat activates akt/mtorc1 pathway and aicda expression by downregulating its transcriptional inhibitors in b cells//International Journal of Molecular Sciences. 2021. Vol. 22. Is. 4. Art. no 1588. P. 1-12. DOI: 10.3390/ijms22041588. – Q1
  3. Belkina E.G., Lazebny O.E., Gornostaev N.G., Mikhailov V.S., Danilenkova L.V., Besedina N.G., Bragina J.V., Kamyshev N.G., Sokolov V. V., Kravchuk O.I. Influence of the quick-to-court gene deletion on courtship behaviour of Drosophila melanogaster//Journal Genetics. 2021. Vol. 100. Art. no 37. DOI: 10. 007/s12041-021-01284-4. – Q4.
  4. Boguslavsky D.V., Sharova N.P., Sharov K.S. Cryptocurrency as epidemijlogically safe means of transactions: Diminishing risk of SARS-CoV-2 spread//Mathematics. 2021. Vol. 9. Art. no 3263. DOI: 10.3390/math9243263. – Q1.
  5. Erokhov P.A., Kulikov A.M., Karpova Y.D., Rodoman G.V., Sumedi I.R., Goncharov A.L., Razbirin D.V., Gorelova V.S., Sharova N.P., Astakhova T.M. Proteasomes in Patient Rectal Cancer and Different Intestine Locations: Where Does Proteasome Pool Change?//Cancers. 2021. Vol. 13 P. 1108. DOI: 10.3390/cancers13051108. – Q1.
  6. Izvolskaia M., Ignatiuk V., Ismailova A., Sharova V., Zakharova L. IgG modulation in male mice with reproductive failure after prenatal inflammation//Reproduction (Cambridge, England). 2021. Vol. 161. Is. 6. P. 669-679. DOI: 10. 530/REP-20-0386. – Q2.
  7. Karpova Y., Guo D., Makhov P., Haines A.M., Markov D.A., Kolenko V., Tulin A.V. Poly(ADP)-Ribosylation Inhibition: A Promising Approach for Clear Cell Renal Cell Carcinoma Therapy//Cancers. 2021. Vol. 13. Is. 19 Art. No 4973. DOI: 10.3390/cancers13194973 – Q1.
  8. Karpukhinа A., Galkin I., Ma Y., Dib C., Zinovkin R., Pletjushkina O., Chernyak B., Popova E, Vassetzky Y.S. Analysis of genes regulated by DUX4 via oxidative stress reveals potential therapeutic targets for treatment of facioscapulohumeral dystrophy//Redox Biology. 2021. Vol. 43. Art. No 102008. DOI: 10. 016/j.redox.2021. 02008. – Q1.
  9. Karpukhina A., Tiukacheva E., Dib C., Vassetzky Y.S. Control of DUX4 Expression in Facioscapulohumeral Muscular Dystrophy and Cancer//Trends in Molecular Medicine. 2021. Vol. 27. Is. 6. P. 588-601. DOI: 10. 016/j.molmed.2021.03.008. – Q1.
  10. Kurnaeva M.A., Zalevsky O., Arifulin E.A., Lisitsyna O.M, Tvorogova A.V., Shubina M.Y., Bourenkov G.P., Tikhomirova M.A., Potashnikova D.M., Kachalova A.I., Musinova Y.R., Golovin A.V., Vassetzky Y.S., Sheval E.V. Molecular coevolution of nuclear and nucleolar localization signals inside the basic domain of HIV-1 Tat // J. Virol. 2021. DOI: 10. 128/JVI.01505-21 - Q1.
  11. Maltsev A., Funikov S., Burov A., Spasskaya D., Ignatyuk V., Astakhova T., Lyupina Y., Deikin A., Tutyaeva V., Bal N., Karpov V., Morozov A. Immunoproteasome Inhibitor ONX-0914 Affects Long-Term Potentiation in Murine Hippocampus//Journal of Neuroimmune Pharmacology. 2021. DOI: 10. 007/s11481-020-09973-0. – Q2.
  12. Naimark E., Kirpotin D., Boeva N., Gmoshinskiy V., Kalinina M., Lyupina Yu., Markov A., Nikitin M., Shokurov A., Volkov D. Taphonomic experiments imply a possible link between the evolution of multicellularity and the fossilization potential of soft-bodied organisms//Ecology and Evolution. 2021. Vol. 11. Is. 2. P. 1037 1056. DOI: 1002/ece3.7120. – Q2.*
  13. Ulianov S.V., Zakharova V.V., Galitsyna A.A., Kos P.I., Polovnikov K.E., Flyamer I.M., Mikhaleva E.A., Khrameeva E.E., Germini D., Logacheva M.D., Gavrilov A.A., Gorsky A.S., Nechaev S.K., Gelfand M.S., Vassetzky Y.S., Chertovich A.V., Shevelyov Y.Y., Razin S.V. Order and stochasticity in the folding of individual Drosophila genomes//Nature Communications. 2021. Vol. 12. Is. 1. Art. N 41. DOI: 10. 038/s41467-020-20292-z. – Q1.
  14. Vagapova E., Burov A., Spasskaya D., Lebedev T., Astakhova T., Spirin P., Prassolov V., Karpov V., Morozov A. Immunoproteasome Activity and Content Determine Hematopoietic Cell Sensitivity to ONX-0914 and to the Infection of Cells with Lentiviruses//Cells. 2021. Vol. 10. Is. 5. Art. no 1185. DOI: 10.3390/cells10051185. – Q2.
  15. Zakharova L., Sharova V., Izvolskaia M. Mechanisms of reciprocal regulation of gonadotropin-releasing hormone (GnRH)-producing and immune systems: The role of GnRH, cytokines and their receptors in early ontogenesis in normal and pathological conditions//International Journal of Molecular Sciences. 2021. Vol. 22. Is. 1. Art. N 114. P. 1-24. DOI: 10.3390/ijms22010114. – Q1.
Тезисы конференций в журналах, индексируемых в Web of Science
  1. Adameyko K.I., Finoshin A.D., Lyupina Y.V., Kravchuk O.I., Shagimardanova E.I., Gazizova G.R., Gusev O.A. Regulation of ferritin and globin genes in cold-water sea sponges Halisarca dujardini and Halichondria panicea and its role during reaggregation//FEBS OPEN BIO. 2021. Vol. 11. N 1. P-01. -46. P. 120-120. Meeting Abstract . WOS:000668898600348. – 111 RIVER ST, HOBOKEN 07030-5774, NJ USA 2211-5463. JUL 2021. This work was funded by RFBR, project number. 20-04-60561\20
  2. Bal N., Maltsev A., Funikov S., Burov A., Spasskaya D., Ignatyuk V., Astakhova T., Lyupina Y., Deikin A., Karpov V., Morozov A. Immunoproteasomes participate in long-term potentiation in murine hippocampus//FEBS OPEN BIO. 2021. Vol. 11. N 1. P-03. -39. P. 211-211. Meeting Abstract. WOS:000668898601026. – 111 RIVER ST, HOBOKEN 07030-5774, NJ USA 2211-5463. JUL 2021. The study was supported by the Russian Science Foundation grant #18-74-10095.
  3. Funikov S., Teterina E., Spasskaya D., Burov A., Astakhova T., Erokhov P., Revtovich S., Tutyaeva V., Deikin A., Ustugov A., Karpov V., Morozov A. Perturbations in the proteasome pool accompany pathology progression in FUS transgenic mice//FEBS OPEN BIO. 2021. Vol. 11. N 1. P-08.4-22. P. 469-469. Meeting Abstract. WOS:000668898602166. – 111 RIVER ST, HOBOKEN 07030-5774, NJ USA 2211-5463. JUL 2021. The study was supported by the Russian Science Foundation grant #18-7410095.
  4. Ignatiuk V. IgG modulation of reproductive disorders in male mice induced by proinflammatory cytokines in prenatal period//FEBS OPEN BIO. 2021. Vol. 11. N 1. P-08.3-53. P. 408-408. Meeting Abstract. WOS: 000668898602136. – 111 RIVER ST, HOBOKEN 07030-5774, NJ USA 2211-5463. JUL 2021. The reported study was funded by RFBR, project number 19-34-90006.
  5. Morozov A., Astakhova T., Burov A., Erokhov P., Karpov V. Modulation of the 20S proteasome activity by the interplay between ATP and Mg2+ ions//FEBS OPEN BIO. 2021. Vol. 11. N 1. P-02.3-14. P. 165-165. Meeting Abstract. WOS:000668898600481. – 111 RIVER ST, HOBOKEN 07030-5774, NJ USA 2211-5463. JUL 2021.
  6. Serbina O., Kiseleva E., Vassetzky Y. MSCS are key players in muscle fibrosis development in facioscapulohumeral dystrophy//CYTOTHERAPY. 2021. Vol. 23. N 5. S 144. S53-S54. Meeting Abstract. WOS: 000650965900066. – THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND 1465-3249 1477-2566. MAY 2021. The work was conducted under the IDB RAS Government basic research program in 2021 N 0088-2021-0016.
  7. Serbina O., Kiseleva E., Vassetzky Y. Myoblasts and MSCs influence to each other's proliferative and differentiation status in the in vitro model of the Facioscapulohumeral muscular dystrophy (FSHD)//FEBS OPEN BIO. 2021. Vol. 11. N 1. P-06.4-04. P. 335-335. Meeting Abstract. WOS:000668898601383. – 111 RIVER ST, HOBOKEN 07030-5774, NJ USA 2211-5463. JUL 2021. The work was conducted under the IDB RAS Government basic research program in 2021 No 0088-2021-0016.

Публикации за 2020 г.

  1. Адамейко К.И.1, Кравчук О.И.1, Финошин А.Д.1, Бончук А.Н., Георгиев А.А., Михайлов В.С.1, Горностаев Н.Г.1, Михайлов К.В., Бачева А.В., Индейкина М.И., Бугрова А.Е., Газизова Г.Р., Козлова О.С., Гусев О.А., Шагимарданова Е.И., Люпина Ю.В.1 Структура нейроглобина холодноводной губки Halisarca dujardinii//Молекулярная биология. – 2020. – Т. 54. – № 3. – С. 474-479. DOI: 10.31857/S0026898420030039. – Adameyko K.I.1, Kravchuk O.I.1, Finoshin A.D.1, (...),Mikhailov V.S.1, Gornostaev N.G.1, (…), Shagimardanova E.I., Lyupina Y.V.1. Structure of Neuroglobin from Cold-Water Sponge Halisarca dujardinii//Molecular Biology. – 2020. – Vol. 54(3). – P. 416-420. DOI: 10.1134/S0026893320030036. – Q4.
  2. Астахова Т.М.1, Моисеева Е.В., Шарова Н.П.1 Особенности пула протеасом в спонтанно возникающих злокачественных опухолях молочной железы мышей//Онтогенез. – 2020. – Т. 51. – № 5. – С. 379-385. – Astakhova T.M.11, Moiseeva E.V., Sharova N.P.1 Features of the Proteasome Pool in Spontaneously Occurring Malignant Tumors of the Mammary Gland in Mice//Russian Journal of Developmental Biology. – 2020. – Vol. 51. – No. 5. – P. 317-322. DOI: 10.1134/S1062360420050021. – Q4
  3. Белкина Е.Г.1, Лазебный О.Е.1, Кравчук О.И.1 Влияние гена Quick-to-court на некоторые аспекты брачного поведения у Drosophila melanogaster//Генетика. – 2020. – Т. 56. – № 2. – С. 181-187. DOI: 10.31857/S0016675820020022. – Belkina E.G.1, Lazebny O.E.1, Kravchuk O.I.1 The Influence of quick-to-court Gene on Some Aspects of Mating Behavior in Drosophila melanogaster//Russian Journal of Genetics. – 2020. – Vol. 56. – Is. 2. – P. 177-182. DOI: 10.1134/S1022795420020027. – Q4
  4. Карпухина А.А.4, Васецкий Е.С.2 Экспрессия активатора зиготического генома DUX4 в соматических клетках приводит к развитию наследственных и онкологических заболеваний//Онтогенез. – 2020. – Т. 51. – № 3. – Р. 210 – 217. DOI: 10.31857/S0475145020030076. – Karpukhina A.4, Vassetzky Y.2 DUX4, a Zygotic Genome Activator, Is Involved in Oncogenesis and Genetic Diseases//Russian Journal of Developmental Biology. – 2020. – Vol. 51. – Is. 3. – P. 176-182. DOI: 10.1134/S1062360420030078. – Q4.
  5. Лифанцева Н.В.1, Конеева Ц.О.1, Воронова С.Н.1, Луценко Г.В. , Захарова Л.А.1, Мельникова В.И.1 Экспрессия и роль серотонинового рецептора 1а типа в эмбриональном тимусе крыс//Онтогенез. – 2020. – Т. 51. – № 5. – С. 338-350. DOI: 10.31857/S0475145020050055. – R. Lifantseva N.V.1, Koneeva Ts.O.1, Voronova S.N.1, Lutsenko G.V., Zakharova L.A.1, Melnikova V.I.1 Expression and the Role of Type 1A Serotonin Receptor in Rats' Embryonic Thymus//Russian Journal of Developmental Biology. – 2020. – Vol. 51. – No. 5. – P. 283-293. DOI: 10.1134/S1062360420050021. – Q4.
  6. Akbay B., Shmakova A., Vassetzky Y.S.3, Dokudovskaya S. Modulation of mTORC1 signaling pathway by HIV-1//Cells. – 2020. – Vol. 9. – Is. 5. – P. 1090. DOI: 10.3390/cells9051090. – Q2
  7. Canoy R.J., Andre F., Shmakova A., Wiels J., Lipinski M., Vassetzky Y.2, Germini D. Easy and robust electrotransfection protocol for efficient ectopic gene expression and genome editing in human B cells//Gene Therapy. – 2020. DOI: 10.1038/s41434-020-00194-x. – Q1.
  8. Finoshin A.D.1, Adameyko K.I.1, Mikhailov K.V., Kravchuk O.I.1, Georgiev A.A., Gornostaev N.G.1, Kosevich I.A., Mikhailov V.S.1, Gazizova G.R., Shagimardanova E.I., Gusev O.A., Lyupina Y.V.1 Iron metabolic pathways in the processes of sponge plasticity//Plos One. – 2020. – Vol. 15. – Is. 2. P. e0228722. DOI: 10.1371/journal.pone.0228722. – Q2.
  9. Germini D., Sall F.B., Shmakova A., Wiels J., Dokudovskaya S., Drouet E., Vassetzky Y.2 Oncogenic properties of the ebv zebra protein//Cancers. – 2020. – Vol. 12. – Is. 6. – № Art. 1479. – P. 1-26. DOI: 10.3390/cancers12061479. – Q1.
  10. Izvolskaia M.S.1, Sharova V.S.1, Zakharova L.A.1 Perinatal inflammation reprograms neuroendocrine, immune, and reproductive functions: Profile of cytokine biomarkers//Inflammation. – 2020. Vol. 43. – Is. 4. – P. 1175-1183. DOI: 10.1007/s10753-020-01220-1. – Q3
  11. Kondakova I.V., Shashova E.E., Sidenko E.A., Astakhova T.M.1, Zakharova L.A.1, Sharova N.P.1 Estrogen Receptors and Ubiquitin Proteasome System: Mutual Regulation//Biomolecules. – 2020. – Vol. 10. – P. 500. DOI: 10.3390/biom10040500. – Q2.
  12. Krajewski W.A.1 "Direct" and "Indirect" Effects of Histone Modifications: Modulation of Sterical Bulk as a Novel Source of Functionality//Bioessays. – 2020. – Vol. 42(1). – Art. No 1900136. DOI: 10.1002/bies.201900136. – Q1. *
  13. Krajewski W.A.1 The intrinsic stability of H2B-ubiquitylated nucleosomes and their in vitro assembly/disassembly by histone chaperone NAP1//Biochimica et Biophysica Acta – General Subjects. – 2020. – Vol. 1864(3). – Art. no 129497. DOI: 10.1016/j.bbagen.2019.129497. – Q2
  14. Murugina N.E., Budikhina A.S., Dagil Y.A., Maximchik P.V., Balyasova L.S., Murugin V.V., Melnikov M.V., Sharova V.S.1, Nikolaeva A.M., Chkadua G.Z., Pinegin B.V., Pashenkov M.V. Glycolytic reprogramming of macrophages activated by NOD1 and TLR4 agonists: No association with proinflammatory cytokine production in normoxia//Journal of Biological Chemistry. – 2020. – Vol. 295. – Is. 10. – P. 3099-3114. DOI: 10.1074/jbc.RA119.010589. – Q2.
  15. Naimark E., Kirpotin D., Boeva N., Gmoshinskiy V., Kalinina M., Lyupina Yu.1, Markov A., Nikitin M., Shokurov A., Volkov D. Taphonomic experiments imply a possible link between the evolution of multicellularity and the fossilization potential of soft-bodied organisms//Ecology and Evolution. – 2020. DOI: 1002/ece3.7120. – Q2.
  16. Shmakova A., Germini D., Vassetzky Y.3 HIV-1, HAART and cancer: A complex relationship//International Journal of CanceR. 2020. – Vol. 146. – Is. 10. – P. 2666-2679. DOI: 10.1002/ijc.32730. – Q1.
  17. Valyaeva A.A., Zharikova A.A., Kasianov A.S., Vassetzky Y.S.2, Sheval E.V. Expression of SARS-CoV-2 entry factors in lung epithelial stem cells and its potential implications for COVID-19//Scientific Reports. – 2020. – Vol. 10. – Is. 1. – Art. No 17772. DOI: 10.1038/s41598-020-74598-5. – Q1.
  18. Sorokin D.V., Arifulin E.A., Vassetzky Y.S.2, Sheval E.V. Live-Cell Imaging and Analysis of Nuclear Body Mobility//Methods in molecular biology (Clifton, N.J.) – 2020. – Vol. 2175. – P. 1-9. DOI: 10.1007/978-1-0716-0763-3_1. ISBN 978-1-4939-9748-0; 978-1-4939-9747-3.

Публикации за 2019 г.

  1. Астахова Т.М., Божок Г.А., Алабедалькарим Н.М., Карпова Я.Д., Люпина Ю.В., Ушакова Е.М., Легач Е.И., Бондаренко Т.П., Шарова Н.П. Экспрессия протеасом в гетеротопических аллотрансплантатах яичников крыс Вистар и Август при индукции донорспецифической толерантности // Онтогенез. 2019. Т. 50. № 5. С. 332-339. DOI: 10.1134/S0475145019050021. (РИНЦ) – Astakhova T.M., Bozhok G.A., Alabedal’karim N.M., Karpova Ya.D., Lyupina Yu.V., Ushakova E.M., Legach E.I., Bondarenko T.P., Sharova N.P. Proteasome expression in ovarian heterotopic allografts of Wistar and August rats under induction of donor specific tolerance // Russian Journal of Developmental Biology. 2019. V. 50. No. 5. P. 261-267. DOI: 10.1134/S1062360419050023. (WoS, Scopus) – Q4.
  2. Морозов А.В., Буров А.В., Астахова Т.М., Спасская Д.С., Маргулис Б.А., Карпов В.Л. Динамика функциональной активности и экспрессии субъединиц протеасом в условиях адаптации клетки к тепловому шоку // Молекулярная биология. 2019. Т. 53. № 4. С. 638-647. DOI: 10.1134/S0026898419040086. (РИНЦ) – Morozov A.V., Burov A.V., Astakhova T.M., Spasskaya D.S., Margulis B.A., Karpov V.L. Dynamics of the Functional Activity and Expression of Proteasome Subunits during Cellular Adaptation to Heat Shock // Molecular Biology. 2019. V. 53. Is. 4. P. 571-579. DOI: 10.1134/S0026893319040071. (WoS, Scopus). – Q4
  3. Dib C., Zakharova V., Popova E., (...), Lipinski M., Vassetzky Y.S. DUX4 Pathological Expression: Causes and Consequences in Cancer // Trends in Cancer. 2019. DOI: 10.1016/j.trecan.2019.03.001. (WoS, Scopus) – Q1
  4. Gorbacheva M., Valyaeva A., Potashnikova D., Arifulin E., Vassetzky Y., Musinova Y. HIV-1 Tat induces cell type-specific expression of host genes in B-cells // FEBS OPEN BIO. 2019. V. 9. Is. 1. P-35-157. P 368. WOS:000486972406001. (WoS) – Q4.
  5. Gorbacheva M., Valyaeva A., Potashnikova D., (..), Vassetzky Y., Musinova Y. M-3. HIV 1 tat induces cell type specific expression of host genes in B cells // Biopolymers and Cell. 2019. V. 35(3). P. 225-226. DOI: 10.7124/bc.0009F0. (Scopus).
  6. Ignatiuk V.M., Izvolskaya M.S., Sharova V.S., Voronova S.N., Zakharova L.A. Disruptions in the reproductive system of female rats after prenatal lipopolysaccharide-induced immunological stress: role of sex steroids // Stress-the International Journal on the Biology of Stress. 2019. V. 22. Is. 1, P. 133-141. DOI: 10.1080/10253890.2018.1508440. (WoS, Scopus) – Q2.
  7. Iarovaia O.V., Minina E.P., Sheval E.V., Onichtchouk D., Dokudovskaya S., Razin S.V., Vassetzky Y.S. Nucleolus: A Central Hub for Nuclear Functions // Trends in Cell Biology. 2019. DOI: 10.1016/j.tcb.2019.04.003. (WoS, Scopus) – Q1.
  8. Izvolskaia M.S., Sharova V.S., Ignatiuk V.M., Voronova S.N., Zakharova L.A. Abolition of prenatal lipopolysaccharide-induced reproductive disorders in rat male offspring by fulvestrant // Andrologia. 2019. V. 51. e13204. DOI: 10.1111/and.13204. (WoS, Scopus) – Q3
  9. Krajewski W.A. "Direct" and "Indirect" Effects of Histone Modifications: Modulation of Sterical Bulk as a Novel Source of Functionality // Bioessays. 2019. Art. 1900136. DOI: 10.1002/bies.201900136. (WoS, Scopus) – Q1.
  10. Krajewski W.A. Ubiquitylation: How Nucleosomes Use Histones to Evict Histones Iarovaia O.V., Minina E.P., Sheval E.V., Onichtchouk D., Dokudovskaya S., Razin S.V., Vassetzky Y.S. Nucleolus: a central hub for nuclear functions // Trends in Cell Biology. – 2019. – V. 29. Is. 8. – P. 647-659. DOI: 10.1016/j.tcb.2019.04.003. (WoS, Scopus) – Q1.
  11. Krajewski W.A., Vassiliev O.L. Analysis of histone ubiquitylation by MSL1/MSL2 proteins in vitro // Archives of Biochemistry and Biophysics. 2019. V. 666. Is. 15. P. 22-30. DOI: 10.1016/j.abb.2019.03.015. (WoS, Scopus) – Q2.
  12. Kravchuk O.I., Lyupina Y.V., Erokhov P.A., Finoshin A.D., Adameyko K.I., Mishyna M.Yu, Moiseenko A.V., Sokolova O.S., Orlova O.V., Beljelarskaya S.N., Serebryakova M.V., Indeykina M.I., Bugrova A.E., Kononikhin A.S., Mikhailov V.S. Characterization of the 20S proteasome of the lepidopteran, Spodoptera frugiperda // Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics. 2019. V. 1867. Is. 9. P. 840-853. DOI: 10.1016/j.bbapap.2019.06.010. (WoS, Scopus) – Q2 – Q3.
  13. Kurnaeva M.A., Sheval E.V., Musinova Y.R., Vassetzky Y.S. Tat basic domain: A "Swiss army knife" of HIV-1 Tat? // Reviews in Medical Virology. 2019. e2031. DOI: 10.1002/rmv.2031. (WoS, Scopus) – Q1.
  14. Melnikova V.I., Lifantseva N.V., Voronova S.N., Zakharova L.A. Gonadotropin-Releasing Hormone in Regulation of Thymic Development in Rats: Profile of Thymic Cytokines // International journal of molecular sciences. 2019. V. 20(16). DOI: 10.3390/ijms20164033. (WoS, Scopus) – Q2.
  15. Sall F.B., El A.R., Markozashvili D., Tsfasman T., Oksenhendler E., Lipinski M., Vassetzky Y., Germini D. HIV-1 Tat protein induces aberrant activation of AICDA in human B-lymphocytes from peripheral blood // Journal of Cellular Physiology. 2019. V. 234. Is. 9. P. 15678-15685. DOI: 10.1002/jcp.28219. (WoS, Scopus) – Q1-Q2.
  16. Shmakova A., Germini D., Vassetzky Y. HIV-1, HAART and cancer: A complex relationship // International Journal of Cancer. 2019. DOI: 10.1002/ijc.32730. (WoS, Scopus). – Q1
  17. Shmakova A.A., Germini D., Vassetzky Y.S. S-4. Exploring the features of burkitt’s lymphoma-associated t(8;14) translocations generated via a CRISPR/cas9-based system // Biopolymers and Cell. 2019. V. 35(3). P. 232-233. DOI: 10.7124/bc.0009F8. (Scopus).
  18. Syrkina M., Viushkov V., Potashnikova D., Veiko V., Vassetzky Y., Rubtsov M. From an increase in the number of tandem repeats through the decrease of sialylation to the downregulation of MUC1 expression level // Journal of Cellular Biochemistry. 2019. V. 120(3). P. 4472-4484. DOI: 10.1002/jcb.27735. (WoS, Scopus) – Q2-Q3.
  19. Syrkina M.S., Vassetzky Y.S., Rubtsov M.A. MUC1 story: Great expectations, disappointments and the renaissance // Current Medicinal Chemistry. 2019. V. 26(3). P. 554-563. DOI: 10.2174/0929867324666170817151954. (WoS, Scopus) – Q2.

Публикации за 2018 г.

  1. Bozhok G.A., Alabedal’karim N.M., Legach E.I., Lyupina Yu.V., Sharova N.P., Karpova Ya.D. Changes in the Expression of Immune Proteasomes in the Liver after the Induction of Portal Tolerance Depending on Donor-Recipient Differences in Rats // Bulletin of Experimental Biology and Medicine. 2018. V. 164. No. 5. Р. 641-644. DOI: 10.1007/s10517-018-4049-2). (WoS, Scopus)
  2. Sall F.B., Germini D., Kovina A., Ribrag V., Wiels J., Toure A.O., Iarovaia O.V., Lipinski M., Vassetzky Y. Влияние факторов окружающей среды на организацию ядра и трансформацию В-лимфоцитов человека // Биохимия. 2018. Т. 83. № 4. С. 556–565. (РИНЦ). (Sall F.B., Germini D., Kovina A.P., Ribrag V., Wiels J., Toure A.O., Iarovaia O.V., Lipinski M., Vassetzky Y. Effect of Environmental Factors on Nuclear Organization and Transformation of Human B Lymphocytes // Biochemistry (Moscow).2018. V. 83. N 4. P. 402-410. DОI: 10.1134/S0006297918040119.) (WoS, Scopus).
  3. Арифулин Е.А., Мусинова Я.Р., Васецкий Е.С., Шеваль Е.В. Подвижность компонентов клеточного ядра и функционирование генома // Биохимия. 2018. Т. 83. № 4. С. 629–641. (РИНЦ). (Arifulin E.A., Musinova Y.R., Vassetzky Y.S., Sheval E.V. Mobility of Nuclear Components and Genome Functioning (Review) // Biochemistry (Moscow).V. 83. Is. 6. 1 June 2018. P. 690-700. DOI: 10.1134/S0006297918060068). (WoS, Scopus)
  4. Карпова Я.Д., Люпина Ю.В., Алабедалькарим Н.М., Легач Е.И., Божок Г.А., Шарова Н.П. Изменение содержания мононуклеарных клеток печени, экспрессирующих иммунные протеасомы, при трансплантации ткани яичников в зависимости от донор-реципиентных различий у крыс // Бюллетень экспериментальной биологии и медицины. 2018. № 6. С. 732–736 (РИНЦ) (Karpova Y.D., Lyupina Y.V., Alabedal’karim N.M., Legach E.I., Bozhok G.A., Sharova N.P. Changes in the Content of Mononuclear Liver Cells Expressing Immune Proteasomes after Transplantation of Ovarian Tissues Depending on Donor–Recipient Differences in Rats // Bulletin of Experimental Biology and Medicine. V. 165. Is. 6. 2018. P. 772-776. DOI: 10.1007/s10517-018-4263-y (WoS, Scopus).
  5. Колегова Е.С., Кондакова И.В., Завьялов А.А., Добродеев А.Ю., Шарова Н.П. Функционирование протеасом при лимфогенном метастазировании немелкоклеточного рака легкого // Бюллетень экспериментальной биологии и медицины. 2018. Т. 165. № 4. С. 481-484. (РИНЦ) (Kolegova E.S., Kondakova I.V., Zav'yalov A.A., Dobrodeev A.Y., Sharova N.P. Functioning of Proteasomes in Lymphogenic Metastasizing of Non-Small-Cell Lung Cancer // Bulletin of Experimental Biology and Medicine. 2018. V. 165. Is. 4. P. 486-489. DOI: 10.1007/s10517-018-4200-0). (WoS, Scopus).
  6. Кравчук О.И., Лавров А.И., Финошин А.Д., Горностаев Н.Г., Георгиев А.А., Абатурова С.Б., Михайлов В.С., Люпина Ю.В. Роль эпибионтов бактерий рода Pseudoalteromonas и клеточных протеасом в адаптивной пластичности морских холодноводных губок // Доклады Академии наук. 2018. Т.479. № 2. С. 225-227. DOI: 10.7868/S0869565218080248. (РИНЦ) (Kravchuk O.I., Lavrov A.I., Finoshin A.D., Gornostaev N.G., Georgiev A.A., Abaturova S.B., Mikhailov V.S., Lyupina Yu.V. The Role of Epibionts of Bacteria of the Genus Pseudoalteromonas and Cellular Proteasomes in the Adaptive Plasticity of Marine Cold-Water Sponges // Doklady Biochemistry and Biophysics. 2018. V. 479. N 1. P. 77-79. DOI: 10.1134/S1607672918020072. (WoS, Scopus)
  7. Arifulin E.А., Sorokin D.V., Tvorogova А.V., Кurnаеvа M.А., Musinova Y.R., Zhironkina O.A., Golyshev S.А., Abramchuk S.S., Vassetzky Y.S., Sheval Е.V. Heterochromatin restricts the mobility of nuсlеаr bodies // Chromosoma. 2018. V. 127. N 4. P. 529-537. DOI: 10.1007/s00412-018-0683-8). (WoS, Scopus)
  8. Astakhova T.M., Morozov A.V., Erokhov P.A., Mikhailovskaya M.I., Akopov S.B., Chupikova N.I., Safarov R.R, Sharova N.P. Combined Effect of Bortezomib and Menadione Sodium Bisulfite on Proteasomes of Tumor Cells: The Dramatic Decrease of Bortezomib Toxicity in a Preclinical Trial // Cancers. 2018. V. 10. No. 351. doi:10.3390/cancers10100351.(WoS, Scopus)
  9. Dagil Y.A., Sharova V.S., Pinegin B.V., Pashenkov M.V. A cell-based test system for the assessment of pharmacokinetics of NOD1 and NOD2 receptor agonists // International Immunopharmacology. 2018. V. 63. P. 94-100. DOI: 10.1016/j.intimp.2018.07.037. (WoS, Scopus).
  10. Germini D., Tsfasman T., Zakharova V.V., Sjakste N., Lipinski M., Vassetzky Y.S. A comparison of techniques to evaluate the effectiveness of genome editing // Trends in Biotechnology. 2018. V 36. N. 2. Р. 147-159. DOI: 10.1016/j.tibtech.2017.10.008. (WoS, Scopus
  11. Izvolskaia M., Sharova V., Zakharova L. Prenatal Programming of Neuroendocrine System Development by Lipopolysaccharide: Long-Term Effects // Int. J.Mol. Sci. 2018. V. 19(11), 3695. DOI: 10.3390/ijms19113695. (WoS, Scopus).
  12. Krajewski W.A., Li J.B., Dou Y.L. Effects of histone H2B ubiquitylation on the nucleosome structure and dynamics // Nucleic Acids Research. V. 46. Is. 15. P. 7631-7642. DOI: 10.1093/nar/gky526. (WoS, Scopus).
  13. Krajewski W.A. Effects of DNA Superhelical Stress on the Stability of H2B-Ubiquitylated Nucleosomes // Journal of Molecular Biology. 2018. pii: S0022-2836(18)30656-9. DOI: 10.1016/j.jmb.2018.09.014. (WoS, Scopus
  14. Latyeva O., Kiseleva E., Vassetzky Y. Applying of immortalized myoblasts for the study of the cellular mechanisms of the muscle tissue replacement by connective tissue in the in vitro model of facioscapulohumeral muscular dystrophy (FSHD) // FEBS OPEN BIO. 2018. V. 8. P. 153-153. WOS:000437674102149. (WoS, Scopus).
  15. Lyupina Yu.V., Erokhov P.A. , Kravchuk O.I., Finoshin A.D., Abaturova S.B., Orlova O.V., Beljelarskaya S.N., Kostyuchenko M.V., Mikhailov V.S. Essential function of VCP/p97 ininfection cycle of the nucleopolyhedrovirus AcMNPV in Spodoptera frugiperda Sf9 cells // Virus Research. 2018. V. 253. P. 68–76. DOI: 10.1016/j.virusres.2018.06.001. (WoS, Scopus).
  16. Polesskaya O., Kananykhina E., Roy-Engel A.M., Nazarenko O., Kulemzina I., Baranova A., Vassetsky Y., Myakishev-Rempel M. The role of Alu-derived RNAs in Alzheimer's and other neurodegenerative conditions // Medical Hypotheses. 2018. V. 115. P. 29-34. DOI: 10.1016/j.mehy.2018.03.008. (WoS, Scopus).
  17. Spasskaya D., Astakhova T., Karpov V., Morozov A. Novel unspecific proteasome regulatory mechanism: evidences in favor // FEBS OPEN BIO. 2018. V. 8. P. 417-417. WOS:000437674105022. ((WoS, Scopus)).
  18. Yurinskaya M., Morozov A., Astakhova T., Vinokurov M., Karpov V., Evgen'ev M. Cytoprotective effects of hydrogen sulfide and its influence on proteasome activity // FEBS OPEN BIO. 2018. V. 8. P. 404-404. WOS:000437674104294. (WoS, Scopus).

Публикации за 2017 г.

  1. Morozov A. V., Astakhova T.M., Garbuz D.G., Krasnov G.S., Bobkova N. V., Zatsepina O.G., Karpov V.L., Evgen'ev M.B.Interplay between recombinant Hsp70 and proteasomes: proteasome activity modulation and ubiquitin-independent cleavage of Hsp70 // Cell Stress Chaperones. 2017. V. 22.No. 5.P. 687–697. Doi: 10. 1007/s12192-017-0792-y.
  2. Stankevicins L., Barat A., Dessen P., Vassetzky Y., de Moura Gallo C. V.The microRNA-205-5p is correlated to metastatic potential of 21T series: A breast cancer progression model // PLOS ONE. 2017. V. 12.No. 3:e0173756. DOI:10. 1371/journal.pone. 0173756.
  3. Germini D., Tsfasman T., Zakharova V. V., Sjakste N., Lipinski M., Vassetzky Y.S. A comparison of techniques to evaluate the effectiveness of genome editing // Trends in Biotechnology. 2017 Nov 17.pii: S0167-7799(17)30272-X. Doi: 10. 1016/j.tibtech. 2017. 10. 008.
  4. Syrkina M.S., Vassetzky Y.S., Rubtsov M.A.MUC1 Story: Great Expectations, Disappointments and the Renaissance // Current Med.Chem. 2017. DOI: 10. 2174/0929867324666170817151954.
  5. Syrkina M.S., Maslakova A.A., Potashnikova D.M., Veiko V.P., Vassetzky Y.S., Rubtsov M.A. Dual role of the extracellular domain of human mucin MUC1 in metastasis // J.Cell.Biochem. 2017. V. 118.No. 11.P. 4002–4011. DOI: 10. 1002/jcb. 26056.
  6. Bou Saada Y., Zakharova V., Chernyak B., Dib C., Carnac G., Dokudovskaya S., Vassetzky Y.S. Control of DNA integrity in skeletal muscle under physiological and pathological conditions // Cell.Mol.Life Sci.Published on line 25 April 2017. DOI 10. 1007/s00018-017-2530-0.
  7. Erokhov P.A., Lyupina Yu. V., Radchenko A.S., Kolacheva A.A., Nikishina Yu.O., Sharova N.P.Detection of active proteasome structures in brain extracts: Proteasome features of August rat brain with violations in monoamine metabolism // Oncotarget. 2017. V. 8.P. 70941–70957. Doi: 10. 18632/oncotarget. 20208.
  8. Kiprowska M.J., Stepanova A., Todaro D.R., Galkin A., Haas A., Wilson S.M., Figueiredo-Pereira M.E.Neurotoxic mechanisms by which the USP14 inhibitor IU1 depletes ubiquitinated proteins and Tau in rat cerebral cortical neurons: Relevance to Alzheimer's disease // Biochimica et BiophysicaActa - Molecular Basis of Disease. 2017. V. 1863.N 6.P. 1157-1170. DOI: 10. 1016/j.bbadis. 2017. 03. 017.
  9. Карпова Я.Д., Устиченко В.Д., Алабедалькарим Н.М., Степанова А.А., Люпина Ю.В., Богуславский К.И., Божок Г.А., Шарова Н.П.. Изменение содержания иммунопротеасом и макрофагов в печени крыс при индукции донор-специфической толерантности // Acta Naturae. 2017.Т. 9. №3(34).С. 35–44.
    (Karpova Y. D., Ustichenko V. D., Alabedal'karim N.M., Stepanova A.A., Lyupina Y. V., Boguslavski K.I., Bozhok G.A., Sharova N.P Change in the Content of Immunoproteasomes and Macrophages in Rat Liver At the Induction of Donor-Specific Tolerance // Acta Naturae. 2017. V. 9.No. 3.P. 71–80.)
  10. Ereskovsky A. V., Lavrov A.I, Bolshakov F. V., Tokina D.B.Regeneration in White Sea sponge Leucosolenia complicata (Porifera, Calcarea) // Invertebrate Zoology. 2017. V. 14.No. 2.P. 108–113. Doi: 10. 15298/invertzool. 14. 2. 02.
  11. Карпова Я.Д., Божок Г.А., Алабедалькарим Н.М., Люпина Ю.В., Астахова Т.М., Легач Е.И., Шарова Н.П. Протеасомы и трансплантология: современное состояние проблемы и поиски перспективных направлений // Известия РАН.Серия биологическая. 2017, № 3, С. 218-227. DOI: 10. 7868/S0002332917030043.
    (Karpova Ya. D., Bozhok G.A., Alabedal’karim N.M., Lyupinao Yu. V., Astakhova T.M., Legach E.I., and Sharova N.P. Proteasomes and Transplantology: Current State of the Problem and the Search for Promising Trends // Biology Bulletin. 2017, Vol. 44.No. 3.pp. 237–244. DOI: 10. 1134/S1062359017030049).
  12. Астахова Т.М., Иванова Э.В., Родоман Г.В., Сумеди И.Р., Афанасьев С.Г., Гончаров А.Л., Кондакова И.В., Шарова Н.П. Влияние неоадъювантной химиолучевой терапии на пул протеасом рака прямой кишки // Бюллетень экспериментальной биологии и медицины. 2017.Т. 164. № 8.С. 220–223.
    (Astakhova T.M., Ivanova E. V., Rodoman G. V., Sumedi I.R., Afanas'ev S.G., Goncharov A.L., Kondakova I. V., Sharova N.P. Effect of Neoadjuvant Chemoradiation Therapy on Proteasome Pool in Rectal Cancer // Bull.Exp.Biol.Med. 2017. V. 164.No. 2.P. 191–194. Doi: 10. 1007/s10517-017-3955-z.)
  13. Божок Г.А., Алабедалькарим Н.М., Легач Е.И., Люпина Ю.В., Шарова Н.П., Карпова Я.Д. Изменение экспрессии иммунных протеасом в печени при индукции портальной толерантности в зависимости от донор-реципиентных различий у крыс // Бюллетень экспериментальной биологии и медицины. 2017.Т. 164. № 11.С. 594–598. DOI нет.ИФ (РИНЦ) 0, 634.
    (Bozhok G.A., Alabedal’karim N.M., Legach E.I., Lyupina Yu. V., Sharova N.P., Karpova Ya. D. Change of immune proteasome expressuin in the liver under induction of portal tolerance in the dependence on donor-recipient distinctions in rats // Bull.Exp.Biol.Med. 2018. V. 164.No. 5.Р. 541-644. Doi: 10. 1007/s10517-018-4049-2.)

Публикации за 2016 г.

  1. Lyupina Yu. V., Zatsepina O.G., Serebryakova M. V., Erokhov P.A., Abaturova S.B., Kravchuk O.I., Orlova O. V., Beljelarskaya S.N., Lavrov A.I., Sokolova O.S., Mikhailov V.S. Proteomics of the 26S proteasome in Spodoptera frugiperda cells infected with the nucleopolyhedrovirus, AcMNPV // Biochimica et Biophysica Acta (Proteins and Proteomics). 2016. V. 1864.P. 738–746. DOI: 10. 1016/j.bbapap. 2016. 02. 021.
  2. Savitsky M., Kim M., Kravchuk O., and Schwartz Yu.B. Distinct Roles of Chromatin Insulator Proteins in Control of the Drosophila Bithorax Complex // Genetics. 2016. V. 202.P. 601–617. DOI: 10. 1534/genetics. 115. 179309.
  3. Степанова А.А., Люпина Ю.В., Шарова Н.П., Ерохов П.А. Нативная структура иммунных протеасом печени крысы // Доклады Академии наук (Биохимия, Биофизика, Молекулярная биология). 2016.Т. 468. № 3.С. 339–341. DOI: 10. 7868/S0869565216150251 (Stepanova A.A., Lyupina Yu. V., Sharova N.P., Erokhov P.A.Native Structure of Rat Liver Immune Proteasomes // Doklady Biochemistry and Biophysics. 2016. V. 468.P. 200-202). DOI: 10. 1134/S160767291603011X
  4. Krajewski W.A. On the role of internucleosomal interactions and intrinsic nucleosome dynamics in chromatin function // Biochemistry and Biophysics Reports. 2016. V. 5.P. 492–501. DOI: 57-59. 10. 1016/j.bbrep. 2016. 02. 009.
  5. Krajewski W.A. A composite agarose-polyacrylamide matrix as 2D hard support for solid-phase protein assays // Analytical Biochemistry. 2016. V. 497.P. 57–59. DOI: 10. 1016/j.ab. 2015. 11. 023
  6. Krajewski W.A.Mobilization of hyperacetylated mononucleosomes by purified yeast ISW2 in vitro // Archives of Biochemistry and Biophysics. 2016. V. 591.P. 1-6. DOI: 10. 1016/j.abb. 2015. 12. 002
  7. Markozashvili D., Pichugin A., Barat A., Camara-Clayette V., Vasilyeva N., Lelièvre H., Kraus-Berthier L., Depil S., Ribrag V., Vassetzky Y.S. Histone deacetylase inhibitor abexinostat affects chromatin organization and gene transcription in mantle cell lymphoma cells // Gene. 2016. DOI: 10. 1016/j.gene. 2016. 01. 017.
  8. Bou Saada Y., Dib C., Dmitirev P., Hamade A., Carnac G., Laoudj-Chenivesse D., Lipinski M., Vassetzky, Y.S. Facioscapulohumeral dystrophy myoblasts efficiently repair moderate levels of oxidative DNA damage // Histochem.Cell Biol. 2016. DOI: 10. 1007/s00418-016-1410-2.
  9. Stepanova A., Shurubor Ye., Valsecchi F., Manfredi G., Galkin A. Differential susceptibility of mitochondrial complex II to inhibition by oxaloacetate in brain and heart // Biochim.Biophys.Acta (Bioenergetics). 2016. V. 1857.P. 1561-1568. DOI: 10. 1016/j.bbabio. 2016. 06. 002.ISSN 0005-2728
  10. Kravchuk O., Kim M., Klepikov P.Parshikov A., Georgiev P., Savitsky M. Transvection in Drosophila: trans-interaction between yellow enhancers and promoter is strongly suppressed by a cis-promoter only in certain genomic regions // Chromosoma. 2016. DOI:10. 1007/s00412-016-0605-6.
  11. Morozov A. V., Kulikova A.A., Astakhova T.M., Mitkevich V.A., Burnysheva K.M., Adzhubei A.A., Erokhov P.A., Evgen’ev M.B., Sharova N.P., Karpov V.L., Makarov A.A. Amyloid-b increases activity of proteasomes capped with 19S and 11S regulators // J.Alzheimer Dis. 2016. V. 54.No 2.P. 763-776. DOI: 10. 3233/JAD-160491.
  12. Dmitirev P., Kiseleva E., Kharchenko O., Ivashkin E., Pichugin A., Dessen P., Robert T., Lazar V., Coppée F., Belayew A., Carnac G., Laoudj-Chenivesse D., Lipinski M., Vasiliev A., Vassetzky Y.S. // DUX4 controls migration of mesenchymal stem cells through the CXCR4-SDF1 axis.Oncotarget. 2016. DOI: 10. 18632/oncotarget. 11368.
  13. Становова М.В., Ерохов П.А., Горностаев Н.Г., Михайлов В.С., Люпина Ю.В. Роль протеасом в неспецифическом иммунном ответе у морских аннелид // ДАН.Биохимия, биофизика, молекулярная биология. 2016.Т. 471, № 4.С. 472-474
  14. Мальцев Д.И., Ямскова В.П., Ильина А.П., Березин Б.Б., Ямсков И.А.. Биорегулятор из печени крыс // Прикладная биохимия и микробиология. 2016, 52 (3): 1-4. DOI: 10. 7868/S055510 9916030119 (Перевод Maltsev D.I., Yamskova V.P., Il’ina A.P., Beresin B.B., Yamskov I.A.Bioregulator from rat liver tissue // Appl.Biochem.Microbiol., 2016, 52: 342. DOI: 10. 1134/S000368381603011X.).
  15. Налобин Д.С., Краснов М.С., Алипкина С.И., Сырчина М.С., Ямскова В.П., Ямсков И.А.Влияние биорегуляторов, выделенных из печени крысы и сыворотки крови, на состояние печени мыши при роллерном органотипическом культивировании после CCl4 индуцированного фиброза // Клеточные технологии в биологии и медицине. 2016. № 2.с. 126-131. DOI:10. 1007/s10517-016-3468-1 (Перевод: Nalobin D.S., Krasnov M.S., Alipkina S.I., Syrchina M.S., Yamskova V.P., Yamskov I.A.// Effect of Bioregulators Isolated from Rat Liver and Blood Serum on the State of Murine Liver in Roller Organotypic Culture after CCl4-Induced Fibrosis // Bull Exp Biol Med. 2016. 161: 604-609. Doi:10. 1007/s10517-016-3468-1).
  16. Шайxалиев А.И., Кpаcнов М.C., Ильина А.П., Ямcкова О.В., Pыбакова Е.Ю., Cвентcкая Н.В., Белецкий Б.И., Ямcкова В.П., Ямcков И.А.Влияние химической природы имплантационных материалов на протекание регенеративных процессов в костном ложе // Биофизика. 2016.Т. 61. №4. С. 813-822. DOI:10. 1134/s0006350916040199 (Перевод: Shaihaliev A.I., Krasnov M.S., Il’ina A.P., Yamskova O. V., Rybakova E.Yu., Sventskaya N. V., Beletsky B.I., Yamskova V.P., Yamskov I.A.// The effect of the chemical nature of implant materials on regeneration processes in an implant site // BIOPHYSICS. 2016. V. 61.P. 687-695. doi:10. 1134/S0006350916040199).

Публикации за 2015 г.

  1. Alexey Belogurov Jr., Ekaterina Kuzina, Anna Kudriaeva, Alexey Kononikhin, Sergey Kovalchuk, Yelena Surina, Ivan Smirnov, Yakov Lomakin, Anna Bacheva, Alexey Stepanov, Yaroslava Karpova, Yulia Lyupina, Oleg Kharybin, Dobroslav Melamed, Natalia Ponomarenko, Natalia Sharova, Eugene Nikolaev, and Alexander Gabibov. Ubiquitin-independent proteosomal degradation of myelin basic protein contributes to development of neurodegenerative autoimmunity // The FASEB Journal. fj.14-259333. Published online January 29, 2015. 29(5):1901-13.
  2. Бродский В.Я., Шарова Н.П., Мальченко Л.А., Конченко Д.C., Дубовая Т.К., Звездина Н.Д. Блокирование активности протеасом нарушает ритм синтеза белка – маркера прямых межклеточных взаимодействий // Онтогенез. 2015. Т. 46. № 1. С. 44-52.
  3. Anna Stepanova, Alba Valls, Alexander Galkin. Effect of monovalent cations on the kinetics of hypoxic conformational change of mitochondrial complex I // Biochimica et Biophysica Acta, 2015, 1847, Р. 1085-1092.
  4. Н.Л. Рендаков, Л.А. Лысенко, Ю.В. Люпина, Н.П. Шарова, Н.Б. Сельверова, Н.Н. Немова. Роль лизосомальных протеиназ и эстрадиола в нейродегенерации, индуцированной бета-амилоидом. Доклады Академии Наук. Биология. 2015, Т. 463, № 1, С. 112-115.
  5. Кравчук О.И., Михайлов В.С., Савицкий М.Ю. Простой и эффективный метод получения направленных делеций в геноме дрозофилы // Генетика, 2015, том 51, № 11, с. 1325–1329.
  6. Krajewski WA. A simple and cost-effective solid-phase protein nano-assay using polyacrylamide-coated glass plates // Analytical Biochemistry, 2015, 470, 78–83.
  7. Налобин Д.С., Мальцев Д.И., Ильина А.П., Краснов М.С., Алипкина С.И., Сырчина М.С., Рыбакова Е.Ю., Ямскова В.П., Ямсков И.А. Исследование влияния биорегуляторов, выделенных из печени и сыворотки крови млекопитающих, на развитие фиброза печени мыши // Фундаментальные исследования. 2015. № 7 (часть 1), стр. 48-56.
  8. Куликова О.Г., Мальцев Д.И., Ильина А.П., Бурдина А.В., Ямскова В.П., Ямсков И.А. Биологически активные пептиды, выделенные из укропа пахучего Anethum graveolens L. // Прикладная биохимия и микробиология, 2015, Т.51, №3, с.362-366.
  9. O.G. Kulikova, D.I. Maltsev, A. P. Ilyina, V. P. Yamskova, I. A. Yamskov. Hepatoprotective Activity of Plant Peptides // American Journal of Plant Sciences, 2015, 6, 848-855.
  10. O.G. Kulikova, A.P. Ilyina, V.P. Yamskova, I.A. Yamskov. Composition of Bioregulators Obtained from Garlic, Allium sativum L. // Journal of Nature Science and Sustainable Technology. Nova Science Publishers, 2015, V.11, I.4.
  11. O.G. Kulikova, D.I. Maltsev, A.P. Ilyina, A.O. Roshchin, V.P. Yamskova, I.A. Yamskov. Peptides of Plant Origin Exerting Hepatoprotective Properties // Journal of Nature Science and Sustainable Technology. Nova Science Publishers, 2015, V.11, I.4.
  12. Богданов В.В., Березин Б.Б., Ильина А.П., Ямскова В.П., Ямсков И.А. Биологически активные пептиды гепатопанкреаса камчатского краба // Прикладная биохимия и микробиология. 2015, том 51, № 4, с. 1–7.

Основные публикации предыдущих лет

  1. Zbarsky I.B. Biochemical properties of the tumour cells. Progress in Modern Biology, 1961, vol. 52, pp. 164-178. [Russ.].
  2. Zbarsky I.B., Yermolaeva L.P. and Khrushchov N.G. Characteristics of base composition of the nucleolar-associated chromatin. Proc. of the USSR Academy of Sciences, 1964, vol. 157, pp. 175-177. [Russ.].
  3. Zbarsky I.B., Perevoshchikova K.A. and Delektorskaya L.N. Isolation of animal cell nuclear envelopes Proc. of the USSR Academy of Sciences, 1967, vol. 177, pp. 445-447. [Russ.].
  4. Zbarsky I.B., Dmitrieva N.P. and Yermolaeva L.P. On the structure of Tumour Cell Nuclei. Exp. Cell Res., 1968, vol. 27, pp. 573-576.
  5. Zbarsky I.B. Structure and function of the nuclear envelope. Progress in Modern Biology, 1969, vol. 67, pp. 323-331. [Russ.].
  6. Zbarsky I.B., Perevoshchikova K.A., Delektorskaya L.N. and Delektorsky V. V. Isolation and Biochemical Characterization of the Nuclear Envelope. Nature, 1969, vol. 221, pp. 257-259.
  7. Zbarsky I.B. Nuclear Envelope Isolation. In "Methods in Cell Physiology". Acad. Press, New York, 1972, vol. 5, pp. 167-198.
  8. Zbarsky I.B. Nuclear Envelope. In " Structure and Function of Biological Membranes". "Nauka", Moscow, 1975, pp.26-44. [Russ.].
  9. Zbarsky I.B. An Enzyme Profile of the Nuclear Envelope. Intern. Review of Cytology, 1978, vol. 54, pp. 295-360.
  10. Zbarsky I.B. Characterization of the Nuclear Matrix of Rat Liver and Hepatoma 27. In "Macromolecules in the Functioning Cell", Plenum Press, New York, 1979, pp.15-29.
  11. Zbarsky I.B. Nuclear Matrix and its Characteristics in Normal and Tumour Cells. In "Problems of Developmental Biology", "MIR" Publ., Moscow, 1981, pp. 7-45.
  12. Kuzmina S.N., Buldyaeva T. V., Troitskaya L.P., Zbarsky I.B. Characterization and Fractionation of Rat Liver Nuclear Matrix. Eur. J. Cell Biol., 1981, vol. 25, pp. 225-232.
  13. Zbarsky I.B., Peskin A. V. and Koen Ya.M. Some Features of Nucleo-Cytoplasmic RNA Transport from Isolated Nuclei. Molec. Biol. Rep., 1981, vol. 7, pp. 26-30.
  14. Engelhardt P., Plagens U., Zbarsky I.B. and Filatova L.S. Granules 25-30 nm in Diameter - a Basic Constituent of the Nuclear Matrix, Chromosome Scaffold and Nuclear Envelope. Proc Natl. Acad. Sci. USA, 1982, vol. 78, pp. 6937-6940.
  15. Luchnik A.N. Eukaryote chromosome structure: foundation of the bineme model. J. Theor. Biol., 1982, 99, 135-157.
  16. Mikhailov V.S., Gulyamov D.B. Changes in DNA polymerase alpha, beta, gamma activities during early development of the teleost fish Misgurnus fossilis (loach). Eur. J. Biochem., 1983, 135, 303-306.
  17. Peskin A. V., Zbarsky I.B. Qualitative and Quantitative Characteristics of Enzyme Generation of Superoxide Radicals by Tumour Intracellular Membrabes. Herald of the USSR Academy of Medical Sciences, 1984, No. 8, pp. 32-35. [Russ.].
  18. Mikhailov V.S., Ataeva J.O., Marlyev K.A., Kullyev P.K. Changes in DNA polymerase activities in pupae of the silkworm Bombyx mori after infection with nuclear polyhedrosis virus. J. Gen. Virol., 1986, 67, 175-179.
  19. Mikhailov V.S., Marlyev K.A., Ataeva J.O., Kullyev P.K., Atrazhev A.M. Characterization of 3'-5' exonuclease associated with DNA polymerase of silkworm nuclear polyhedros virus. Nucl. Acids Res., 1986, 14, 3841-3857.
  20. Збарский И. Б. Организация клеточного ядра. - М.: Медицина, 1988.
  21. Mikhailov V.S., Ataeva J.O., Marlyev K.A., Atrazhev A.M. Selective inhibition of 3’-5’ exonuclease activity of Escherichia coli DNA polymerase l by fluoride ion. Molecularnaya Biologiya (Moscow), 1989, 23(1), 306-314.
  22. Georgiev, G.P., Vassetzky, Y.S., Luchnick, A.N., Chernokhvostov, V. V., Razin S. V. Nuclear skeleton, DNA domains and control of replication and transcription. Eur. J. Biochem. 1991, 200:613-624.
  23. Mikhailov V.S., Ataeva J.O., Voronova S.N., Bronstein I.B. Synthesis on double-stranded circular DNA catalyzed by complex of DNA polymerase alpha-primase from silkworm cells. Molecularnaya Biologiya (Moscow), 1991, 25(2), 531-540.
  24. Збарский И. Б., Кузьмина С.Н. Скелетные структуры клеточного ядра. - М.: Наука, 1991.
  25. Zemskov E.A., Abramova E.B., Mikhailov V.S. Virus-induced phosphoproteins in silkworm pupae infected with nuclear polyhedrosis virus. Biokhimiya (Moscow), 1991, 56(12), 2207-2217.
  26. Zemskov E.A., Abramova E.B., Mikhailov V.S. Induction of virus-specific protein kinase in silkworm Bombix mori after infection with nuclear polyhedrosis virus. // Dokl. Akad. Nauk (Moscow), 1991, 321(6), 1277-1281.
  27. Zemskov E.A., Voronova S.N., Bazarnova T.M., Abramova E.B., Filatova L.S., Buldyaeva T. V., Kullyev P.K., Mikhailov V.S. Protein synthesis in silkworm pupae infected with the nuclear polyhedrosis virus. // Biokhimiya (Moscow), 1991, 56(9), 1620-1631.
  28. Mikhailov V.S., Zemskov E.A., Abramova E.B. Protein synthesis in pupae of the silkworm Bombyx mori after infection with nuclear polyhedrosis virus: resistance to viral infection acquired during pupal period. // J. Gen. Virol., 1992, 73(12), 3195-3202.
  29. Podust V., Mikhailov V.S., Georgaki A., Hubscher U. DNA polymerase delta and epsilon holoenzymes from calf thymus. Chromosoma, 1992, 102, 133-141.
  30. Sharova N.P., Eliseeva E. D., and Mikhailov V.S. Changes in the activity of two forms of DNA polymerase alpha during embryogenesis of the teleost fish Misgurnus fossilis L. // Biochemistry (Moscow), 1992, 57(6), 644-649
  31. Zemskov E.A., Abramova E.B., Mikhailov V.S. Induction of a novel protein kinase in pupae of the silkworm Bombyx mori after infection with nuclear polyhedrosis virus. // J. Gen. Virol., 1992, 73(12), 3231-3234.
  32. Filatova L.S., Zbarsky I.B. Immunochemical Identification of Some High Molecular Weight Proteins in Tumour Cell Nuclear Matrix. // Bulletin of Exp. Biol. Med., 1993, vol. 116, No. 10, pp. 418-420. [Russ.].
  33. Sharova N.P., Eliseeva E. D., and Mikhailov V.S. Interrelationship between two forms of DNA polymerase alpha from eggs of the teleost fish Misgurnus fossilis L. (Loach). Biochemistry (Moscow), 1993, 58(12), 1453-1462
  34. Akopov S.B., Bazrnova T.M., Zemskov E.A., Abramova E.B., Mikhailov V.S. Induction of virus-specific proteins in cultured silkworm cells BmN after infection with nuclear polyhedrosis virus. // Biokhimiya (Moscow), 1994, 59(1), 23-30.
  35. Peskin A. V., Stolyarov S. D. Estimation of oxidative stress for environmental assessment. // Izvestiya Akad. Nauk (Moscow), 1994, 21(4), 588-595.
  36. Luchnik A.N., Slesinger M., Vetrova L.N. Experimental evidence for the binemic structure of human chromosomes. // Biochem. Molec. Biol. Int., 1995, 36(4), 723-732.
  37. Sharova N.P. and Mikhailov V.S. DNA polymerase alpha in early development of the teleost fish Misgurnus fossilis L. (Loach). Biochemistry (Moscow), 1995, 60(9), 1125-1131
  38. Luchnik A.N., Slesinger M., Vetrova L.N. Experimental evidence in favour of the binemic structure of human chromosome. // Radiat. Biol., Radiat. Ecol. (Moscow), 1996, 36(6), 798-804.
  39. Mikhailov V.S., Bogenhagen D.F. Effects of Xenopus laevis mitochondrial single-stranded DNA-binding protein on primer-template binding and 3'-5' exonuclease activity of DNA polymerase gamma. // J. Biol. Chem., 1996, 271(31), 18939-18946.
  40. Mikhailov V.S., Bogenhagen D.F. Termination within oligo(dT) tracts in template DNA by DNA polymerase gamma occurs with formation of a triplex structure and is relieved by mitochondrial single-stranded DNA-binding protein.// J. Biol. Chem., 1996, 271(48), 30774-30780.
  41. Peskin A. V., Stolyarov S. D. Comparison of Cu, Zn-superoxide dismutases of clawed frogs Xenopus. // Biokhimiya (Moscow), 1997, 62(7), 905-907.
  42. Zemskov E.A., Abramova E.B. Effect of “Decreasing of sensitivity” to heparin of casein kinase ll type (CK ll) in early development of loach Misgurnus fossilis L. // Germ cells and early development, 1997, 235-236.
  43. Bazarnova T.M., Buldyaeva T. V., Filatova L.S., Akopov S.B., Zbarsky I.B. Phosphorylation and Biosynthesis of High Molecular Weight Phosphoproteins of Tumour Nuclear Matrix. Cell Research, 1998, vol.8, pp. 195-207.
  44. Mikhailov V.S., Mikhailova A.L., Iwanaga M., Gomi S., Maeda S. Bombyx mori nucleopolyhedrovirus encodes a DNA-binding protein capable of destabilizing duplex DNA. // J. Virol., 1998, 72(4), 3107-3116.
  45. Zemskov E.A., Abramova E.B., Klyachko O.S., Ozernyuk N. D., Mikhailov V.S. Casein kinase activity during early development of loach (Misgurnus fossilis L.). // Izvestiya Akad. Nauk (Moscow), 1998, N 2, 230-234.
  46. Mikhailov V.S. Eukaryotic DNA polymerases. Molecularnaya Biologiya (Moscow), 1999, 33(4), 498-510.
  47. Okano K., Mikhailov V.S., Maeda S. Colocalization of baculovirus IE-1 and two DNA-binding proteins, DBP and LEF-3, to viral replication factories. J. Virol., 1999, 73(1), 110-119.
  48. Luchnik A.N. A common link in the mechanism of self-maintenance of malignant growth: The syndrome of the non-healing wound. // Ontogenez (Moscow), 2000, 31(3), 227-231.
  49. Vassetzky, Y.S., Lemaitre, J.-M., and Michali, M. (2000) Specification of Chromatin Domains and Regulation of Replication and Transcription During Development. Crit. Rev. Eukar. Gene Expr. 10:31-38.
  50. Vassetzky, Y.S., Hair, A., and Michali, M. (2000) Rearrangement of chromatin domains during development in Xenopus. Genes and Dev., 14: 1541-1552.
  51. Vassetzky, Y.S., Bogdanova, A., and Razin, S. (2000) Analysis of the chicken DNA fragments that contain structural sites of attachment to the nuclear matrix: DNA-matrix interactions and replication. J. Cell. Biochem., 79: 1-14.
  52. Sharova N.P., Abramova E.B., Dmitrieva S.B., Dimitrova D. D., and Mikhailov V.S. Preferential interaction of loach DNA polymerase delta with DNA duplexes containing single-stranded gaps. // FEBS Lett., 2000, 486(1), 14-18.
  53. Sharova N.P., Dimitrova D. D., Abramova E.B., Dmitrieva S.B., and Mikhailov V.S. Identification of DNA Polymerase delta in Eggs of a Teleost Fish (Loach). // Biochemistry (Moscow), 2001, 66(2), 225-231.
  54. Sharova N.P., Abramova E.B., Dmitrieva S.B., Dimitrova D. D., Mikhailov V.S. Interaction of Loach DNA Polymerase Delta with DNA Duplexes with Single-Strand Gaps. Biochemistry (Moscow), 2001, 66(4), 402-409.
  55. Demeret, C., Vassetzky, Y.S., Mechali, M. Chromatin remodelling and DNA replication: from nucleosomes to loop domains. Oncogene, 2001, 20:3086-3093.
  56. Lemaitre, J.M., Vassetzky, Y.S., and Mechali, M. Ananlysis of chromatin assembly, chromatin domains, and DNA replication using Xenopus systems. in "Mapping protein/DNA interactions by cross-linking and immuno-FISH methods", ed. by G. Cavalli and V. Orlando. 2001, INSERM.
  57. Mikhailov V.S., Rohrmann G.F. The baculovirus replication factor LEF-1 is a DNA primase. Journal of Virology. 2002, 76 (5), 2287-2297.
  58. Abramova E.B., Sharova N.P., Karpov V.L. The proteasoma: destroy to live. Mol. Biol. (Moscow). 2002, 36, 761-776.
  59. Krajewski, W.A. Histone Acetylation Status and DNA Sequence Modulate ATP-dependent Nucleosome Repositioning. J. Biol. Chem. 2002, 277, 14509-14513.
  60. Sharova N.P., Abramova E.B., Dmitrieva S.B., Mikhailov V.S. Specific features of repair DNA polymerases in embryogenesis of the loach. Ontogenesis (Moscow). 2002. 33(5). 380-384.
  61. Nakamura T., Mori T., Krajewski W., Rozovskaia T., Wassell R., Mazo A., Croce C., Canaani E. The ALL-1 protein is a histone methyltransferase and assembles a supercomplex of proteins involved in transcriptional regulation. Mol. Cell. 2002, 10, 1119-1128.
  62. Sharova N.P., Abramova E.B. Initiation of DNA Replication in Eukaryotes Is an Intriguing Cascade of Protein Interactions. Biokhimia (Moscow), 2002, 67 (11), 1474-1482.
  63. Mikhailov V.S., Rohrmann G.F. Binding of the baculovirus very late expression factor 1 (VLF-1) to different DNA structures. BMC Mol. Biol. 2002. 3 (14). 1-11.
  64. Mikhailov V.S., Okano K., Rohrmann G.F. Alkaline nuclease possesses a 5'->3' exonuclease activity and associates with the DNA-binding protein LEF-3. Journal of Virology, 2003, v. 77, No. 4, 2436-2444.
  65. Mikhailov V.S. Baculovirus genome replication. Molecular biology (Moscow), 2003, v. 37, N 2, 288-299.
  66. Abramova E.B., Karpov V.L. Proteasome: destroing for creation. Priroda (Moscow), 2003, N 7, 36-45.
  67. Васецкий Е.С. Прикрепление петель ДНК к искусственной матрице не определяет положение участка начала репликации в раннем развитии шпорцевой лягушки. Онтогенез, 2003, т. 34, с. 213-217.
  68. Петров А., Лаудж Д. и Васецкий Е. Генетика и эпигенетика лице-лопаточно-бедренной прогрессирующей мышечной дистрофии Ландузи-Дежерина. Генетика, 2003, т. 39. С. 147-151.
  69. Girard-Reydet, C., Gregoire D., Vassetzky, Y., and Mechali M. (2004) DNA replication initiates at domains overlapping with nuclear matrix attachment regions in the Xenopus and mouse c-myc promoter, Gene, 332: 129-138.
  70. Goldman, I.L., Razin S. V., and Vassetzky, Y.S. (2004) Effect of microinjection time and loop anchorage regions (LARs) on expression of beta-galactosidase gene injected into one-cell rabbit embryos. J. Cell. Biochem., 15: 1171-1179.
  71. Mikhailov V.S, Okano K, Rohrmann G.F. Specificity of the endonuclease activity of the Baculovirus alkaline nuclease for single-stranded DNA. Journal of Biological Chemistry, 2004, vol. 279, N 15, 14734-45.
  72. Абрамова Е.Б., Астахова Т.М., Ерохов П.А., Шарова Н.П. Множественность форм протеасомы и некоторые подходы к их разделению // Известия АН. Серия биологическая. -2004. -№ 2. -С. 150-156.
  73. Краевский В.А., Лагарькова М.А., Аузио Х. "Исследование структурных перестроек фибрилл хроматина с помощью интеркаляции бромистого этидия и дифосфата хлороквина." Биофизика (2004) 49(3), 457-467.
  74. Шарова Н.П., Абрамова Е.Б. Повреждение и починка ДНК или "На всякую прореху найдется заплата" // Природа. -2004. -№ 11. -С. 3-12.
  75. Ротанова Т.В., Абрамова Е.Б., Шарова Н.П. От парадокса - к Нобелевской премии. // Биологические мембраны. 2005. Т. 22. № 2. С. 146-151.
  76. Абрамова Е.Б., Астахова Т.М., Шарова Н.П. Изменение активности и состава протеасом в постнатальном развитии крысы // Онтогенез. 2005. Т. 36. № 3. С. 1-6.
  77. Шарова Н.П. Как клетка восстанавливает поврежденную ДНК? // Биохимия. 2005. Т. 70. № 3. С. 141-159.
  78. Mikhailov V.S., Okano K., Rohrmann G.F. The redox state of the baculovirus single-stranded DNA-binding protein LEF-3 regulates its DNA binding, unwinding, and annealing activities. J. Biol. Chem., 2005, 280(33), 29444-29453.
  79. Krajewski, W.A., Nakamura, T., Mazo, A., Canaani, E. A motif within SET-domain proteins binds single stranded nucleic acids, transcribed and supercoiled DNAs, and can interfere with assembly of nucleosomes. Molecular and Cellular Biology. 2005, 25, 1891-1899.
  80. Lemaitre JM, Danis E, Pasero P, Vassetzky Y, Mechali M. Lemaitre JM, Danis E, Pasero P, Vassetzky Y, Mechali M. Mitotic remodeling of the replicon and chromosome structure. Cell. 2005 123(5):787-801.
  81. Borunova V, Iarovaia OV, Vassetzky YS, Razin SV. The upstream area of the chicken alpha-globin gene domain is transcribed in both directions in the same cells. FEBS Lett. 2005 579(21):4746-50.
  82. Okano K, Vanarsdall AL, Mikhailov VS, Rohrmann GF. Conserved molecular systems of the Baculoviridae. Virology, 2006, v. 344, N 1, 77-87.
  83. Mikhailov V.S., Okano K., Rohrmann G.F. Structural and functional analysis of the baculovirus single-stranded DNA-binding protein LEF-3. Virology, 2006, v. 346, N 2, 469-478.
  84. Астахова Т.М., Шарова Н.П. Исключение иммунных протеасом из асцитной карциномы Krebs-II мыши // Известия РАН. Серия биологическая. 2006. № 3. С. 275-283.
  85. Шарова Н.П. Иммунные протеасомы и иммунитет // Онтогенез. 2006. Т. 37. № 3. С. 171-178.
  86. Шарова Н.П., Астахова Т.М., Бондарева Л.А., Дмитриева С.Б., Ерохов П.А. Особенности формирования пулов протеасом в селезенке и печени крысы в постнатальном развитии // Биохимия. 2006. Т. 71. Вып. 9. С. 1278-1286.
  87. Petrov, A. Pirozhkova, I., Carnac, G., Laoudj, D., Lipinski, M., and Vassetzky, Y.S., Chromatin loop domain organization within the 4q35 locus in facioscapulohumeral dystrophy patients versus normal human myoblasts. Proc. Natl. Acad. Sci. USA, 2006, 103:6982-6987
  88. Iarovaia OV, Borounova V, Vassetzky, YS, Razin SV. An unusual extended DNA loop attachment region is located in the human dystrophin gene. J Cell Physiol. 2006, 209: 515-521.
  89. Panova I.G., Sharova N.P., Dmitrieva S.B., Poltavtseva R.A., Sukhikh G.T., Tatikolov A.S. Use of a cyanine dye as a probe for albumin and collagen in the extracellular matrix // Analytical Biochemistry. 2007. V. 361. P. 183-189.
  90. Шарова Н.П., Астахова Т.М., Бондарева Л.А., Дмитриева С.Б., Столяров С.Д. Формирование иммунных протеасом и развитие иммунной системы в онтогенезе млекопитающих // Онтогенез. 2007. Т. 38. № 5. С. 323-329.
  91. Шарова Н.П., Строева О.Г., Ерохов П.А., Дмитриева С.Б., Усова Т.А. Изменение активности протеасом in vivo под влиянием окислительного стресса и пара-аминобензойной кислоты у зародышей вьюна // Доклады Академии наук. 2007. Т. 415. № 4. С. 562-565.
  92. Vanarsdall AL, Mikhailov VS, Rohrmann GF. Characterization of a baculovirus lacking the DBP (DNA-binding protein) gene. Virology. 2007, 364(2), 475-485.
  93. Vanarsdall AL, Mikhailov VS, Rohrmann GF. Baculovirus DNA replication and processing. Curr Drug Targets. 2007, 8(10), 1096-102.
  94. Eivazova, E., Vassetzky, Y.S., Aune, T (2007) Selective matrix attachment regions in T helper cell subsets support loop conformation in the Ifng gene. Genes and Immunity, 8: 35-43.
  95. Razin, S. V., Iarovaia, O;, Sjakste, N., Sjakste, T., Bagdoniene, L., Rynditch, A. V., Eivazova, E.R., Lipinski, M., and Vassetzky, Y.S. (2007) Chromatin domains and regulation of transcription. J. Mol. Biol, 369:597-607.
  96. Мельникова В.И., Карпова Я.Д., Афанасьева М.А., Захарова Л.А. Шарова Н.П. Иммунные протеасомы в формирующейся селезенке крысы // Известия РАН. Серия биологическая. 2008. № 2. C. 163-168.
  97. Шарова Н.П., Мельникова В.И., Хегай И.И., Карпова Я.Д., Дмитриева С.Б., Астахова Т.М., Афанасьева М.А., Попова Н.А., Иванова Л.Н., Захарова Л.А. Особенности экспрессии протеасом в клетках опухоли Walker 256 после их трансплантации крысам Brattleboro с генетическим дефектом синтеза вазопрессина // Докл. РАН. 2008. Т. 419, № 6. C. 833-837.
  98. Мельникова В.И., Афанасьева М.А., Дмитриева С.Б., Карпова Я.Д., Шарова Н.П., Захарова Л.А. Иммунные протеасомы в развивающемся тимусе крысы // Биохимия. 2008. Т. 73. № 4. C. 553-561.
  99. Астахова Т.М, Шарова Н.П. Особенности экспрессии протеасом в злокачественно трансформированных клетках // Известия Национальной Академии Наук Беларуси. Серия медицинских наук. 2008. № 1. С. 98-105.
  100. Шарова Н.П., Астахова Т.М., Дмитриева С.Б., Мельникова В.И., Афанасьева М.А., Карпова Я.Д., Захарова Л.А. Роль иммунных протеасом в молекулярных механизмах становления иммунитета. Известия Национальной Академии Наук Беларуси. Серия медицинских наук. 2008. № 1. С. 106-111.
  101. Шарова Н.П. Протеасомы в судьбе злокачественной опухоли. Природа. 2008. № 5. С. 20-26.
  102. Sharova N., Zakharova L.A. Multiple forms of proteasomes and their role in tumor fate. Recent Patents on Endocrine, Metabolic & Immune Drug Discovery. 2008. V.2. No. 3. P. 152-161.
  103. Panova I.G., Sharova N.P., Dmitrieva S.B., Levin P.P., Tatikolov A.S. Characterization of the composition of the aqueous humor and the vitreous body of the eye of the frog Rana temporaria L. Comp. Biochem. Physiol. Part A (Mol. Integr. Physiol.). 2008. V. 151. No. 4. P. 676-681.
  104. W. Krajewski (2008) Evidence for the nucleosome-disruption process regulated by phosphorylation of 120 kDa protein complex in Drosophila embryo cell-free system. Biochimie, 90, 534-541
  105. Petrov A., Allinne J., Pirozhkova, I., Laoudj, D., Lipinski, M., and Vassetzky, Y.S., (2008) Nuclear matrix attachment site in the 4q35 locus has an enhancer-blocking activity: implications for the facioscapulohumeral dystrophy. Genome Research (Impact Factor: 10.325), 18:39-45
  106. Bielskene K, Bagdoniene L., Juodka B., Muiznieks I., Sjakste T., Lipinski M., Vassetzky Y.S. and Sjakste N (2008) Transcription- and apoptosis-dependent long-range distribution of the tight DNA-protein complexes in the chicken alpha globin gene. DNA Cell Biol, 27:615-621.
  107. Mikhailov VS, Vanarsdall AL, Rohrmann G.F. Isolation and characterization of the Autographa californica multiple nucleopolyhedrovirus. Virology, 2008, 370(2):415-429.
  108. Sharova N.P., Zakharova L.A., Astakhova T.M., Karpova Ya. D., Melnikova V.I., Dmitrieva S.B., Lyupina Yu. V., Erokhov P.A. New approach to study of T cellular immunity development: Parallel investigation of lymphoid organ formation and changes in immune proteasome amount in rat early ontogenesis. Cell. Immunol. 2009, V. 256. P. 47-55.
  109. Mikhailov V.S., Rohrmann G.F. Characterization of short-lived intermediates produced during replication of baculovirus DNA. Virus Research, 2009, 145(1), 106-111.
  110. Iarovaia, O., V. Borounova, et al. (2009). In embryonic chicken erythrocytes actively transcribed alpha globin genes are not associated with the nuclear matrix. J. Cell Biochem, 106: 170-178.
  111. Dmitriev P., Lipinski, M. and Vassetzky, Y (2009) Pearls in the junk: dissecting the molecular pathogenesis of facioscapulohumeral muscular dystrophy. Neuromuscular Disorder, 19: 17-20.
  112. Gavrilov A., Eivazova E. R., Pirozhkova I., Lipinski M., Razin S. V., Vassetzky Y. S. (2009) Chromosome conformation capture (3C) and its ChIP-based modifications; Methods in Molecular Biology, 567:171-188.
  113. Eivazova E. R., Gavrilov A., Pirozhkova I., Petrov A., Iarovaia O. V., Razin S. V., Lipinski M., Vassetzky Y. S. (2009) Interaction in vivo between the two matrix attachment regions flanking a single chromatin loop. J. Mol.Biol., 386: 929-937.
  114. Klochkov, D.B., Gavrilov, A. V., Vassetzky, Y.S., Razin S. V. (2009) Early replication timing of the chicken α-globin gene domain correlates with its open chromatin state in cells of different lineages. Genomics, 93:481-486.
  115. Афанасьева М.А., Захарова Л.А., Хегай И.И., Шарова Н.П., Попова Н.А., Иванова Л.Н., Мельникова В.И. Восстановление экспрессии молекулы ГКГ класса I в опухоли Walker 256 в динамике роста у крыс Brattleboro // Доклады РАН. 2010, Т. 430, № 2, С. 1-3. 
  116. Спирина Л.В., Кондакова И.В., Чойнзонов Е.Л., Шарова Н.П., Чижевская С.Ю., Шишкин Д.А. Активность и субъединичный состав протеасом в плоскоклеточных карциномах головы и шеи // Бюллетень экспериментальной биологии и медицины. 2010. Т. 149, № 1, С. 89-92. 
  117. Т.М. Астахова, Г.В. Делоне, Ю.В. Люпина, Е.Б. Абрамова, И.В. Урываева, Н.П. Шарова. Изменение пула протеасом в процессе злокачественной трансформации клеток печени мыши //Acta Naturae. 2010. № 3. С. 109-114. 
  118. Л.В. Спирина, И.В. Кондакова, Е.А. Усынин, Н.П. Шарова. Активность протеасом и их субъединичный состав при раке почки и мочевого пузыря // Онкоурология. 2010. № 3. С. 12-15. 
  119. G. Panova, A. S. Tatikolov, N. P. Sharova. Use of a cyanine dye probe to estimate the composition of the vitreous body after enzymatic treatment. Ophthalmic Technologies XX, edited by F. Manns, P. G. Soderberg, A. Ho. Proc. of SPIE. 2010. Vol. 7550. P. 75501W1-75501W7. 
  120. Sjakste, N., Bagdoniene, L., Gutcaits, A., Labeikyte, D., Bielskene, K., Trapina I., Muiznieks, I., Vassetzky, Y., Sjakste, T. Proteins Tightly Bound to DNA: New Data and Old Problems // Biochemistry (Moscow). 2010. V. 75. No. 10. P. 1240-1251. 
  121. V. Melnikova, N. Sharova, E. Maslova, S. Voronova, L. Zakharova. Ontogenesis of Rat Immune System: proteasome expression in different cell populations of the developing thymus // Cell. Immunol. 2010. М. 266. Р. 83-89.
  122. Lyupina YV, Dmitrieva SB, Timokhova AV, Beljelarskaya SN, Zatsepina OG, Evgen'ev MB, Mikhailov VS. An important role of the heat shock response in infected cells for replication of baculoviruses // Virology. 2010. 406. V. 2. P. 336-341.
  123. Krajewski, W.A., Reese, J.C. SET domains of histone methyltransferases recognize ISWI-remodeled nucleosomal species // Mol. Cell. Biol. 2010. V. 30. P. 552–564. 
  124. Krajewski, W.A., Vassiliev, O.L. Histone acetylation facilitates association of nucleosomes with SET domain of ALL-1 methyltransferase in vitro // Biochem. Biophys. Res. Comm. 2010. V. 397. P. 112-116.
  125. Krajewski, W.A., Vassiliev, O.L. The Saccharomyces cerevisiae Swi/Snf complex can catalyze formation of dimeric nucleosome structures in vitro // Biochemistry (US). 2010. V. 49. P. 6531–6540. 
  126. Barro, M., Carnac, G., Flavier, S., Mercier, J, Vassetzky, Y. and Laoudj-Chenivesse, D. Primary myoblasts derived from the facioscapulohumeral dystrophy patients are hypersensitive to oxidative stress and show defects upon terminal differentiation // J. Cell. Mol. Med. 2010. V. 14. P. 275-289.
  127. Rijnkels, M., Kabotyansky E., Montazer-Torbati M.B., Hue Beauvais C, Vassetzky, Y.S., Rosen J.M., Devinoy, E. The epigenetic landscape of mammary gland development and functional differentiation // Journal of Mammary Gland Biology and Neoplasia. 2010. V. 15. P. 85–100.
  128. Божок Г.А., Карпова Я.Д., Люпина Ю.В., Легач Е.И., Богомягкова Ю.В., Бондаренко Т.П., Шарова Н.П. Возможная роль протеасом печени в реализации механизмов трансплантационной толерантности // Вестник трансплантологии и искусственных органов. 2011. Т. XIII. № 3. С. 73-81.
  129. Карпова Я.Д., Божок Г.А., Люпина Ю. В., Легач Е.И., Астахова Т.М., Степанова А.А., Бондаренко Т.П., Шарова Н.П. Изменение функции протеасом после индукции донор-специфической толерантности у крыс при аллотрансплантации ткани яичника // Известия РАН. Сер. Биол. 2012, в печати.
  130. Шарова Н.П., Астахова Т.М., Карпова Я.Д., Абатурова С.Б., Люпина Ю.В., Богомягкова Ю.В., Абрамова Е.Б., Ерохов П.А. Множественные формы протеасом как мишени противоопухолевых лекарств нового поколения // Онкохирургия. 2011. Т. 3. № 2. С. 37-42.
  131. Krajewski W.A., Vassiliev O.L. Interaction of SET domains with histones and nucleic acid structures in active chromatin // Clinical Epigenetics. 2011. V. 2. P. 17–25.
  132. Krajewski, W.A., Vassiliev O.L., “Remodeling of nucleosome-dimer particles with yIsw2 promotes their association with ALL-1 SET domain in vitro”, Biochemistry, in press, ID: bi-2011-01645c
  133. Lyupina Y. V., Zatsepina O.G., Timokhova A. V., Orlova O. V., Kostyuchenko M. V., Beljelarskaya S.N., Evgen'ev M.B., Mikhailov V.S. // New insights into the induction of the heat shock proteins in baculovirus infected insect cells. Virology 2011. V. 421, № 1, P. 34–41.
  134. Sharova N.P., Astakhova T.M., Karpova Ya. D., Lyupina Yu. V., Alekhin A.I., Goncharov N.G., Sumedi I.R., Cherner V.A., Rodoman G. V., Kuznetsov N.A., Erokhov P.A. Changes in proteasome pool in human papillary thyroid carcinoma development // Cent. Eur. J. Biol. 2011. V. 6. No 4. P. 486-496.
  135. Zakharova L.A., Khegai I.I., Sharova N.P., Melnikova V.I., Karpova Y. D., Astakhova T.M., Popova N.A., Ivanova L.N. Pattern of MHC class I and immune proteasome expression in Walker 256 tumor during growth and regression in Brattleboro rats with the hereditary defect of arginine-vasopressin synthesis // Cell. Immunol. 2011. V. 271. P. 385-391.
  136. Krajewski W.A., Vassiliev OL., Remodeling of nucleosome-dimer particles with yIsw2 promotes their association with ALL-1 SET domain in vitro. Biochemistry, 2012, 51, 4354−4363.
  137. Морозов А.В., Морозов В.А., Астахова Т.М., Тимофеев А.В., Карпов В.Л. ДНК-вакцина, кодирующая альфа-фетопротеин и сигнал деградации орнитиндекарбоксилазы, существенно замедляет рост перевиваемой гепатоцеллюлярной карциномы у мышей // Мол. Биол. 2012. Т. 46. №3. С. 434-451.
  138. Спирина Л.В., Кондакова И.В., Коваль В.Д., Коломиец Л.А., Чернышова А.Л., Чойнзонов Е.Л., Шарова Н.П. Активность протеасом и их субъединичный состав в ткани рака эндометрия: связь с клинико-морфологическими параметрами. Бюлл.Эксп. Биол. Мед. 2012. Т. 153. № 4. С. 491-494. 49.
  139. Карпова Я.Д., Божок Г.А., Люпина Ю.В., Легач Е.И., Астахова Т.М., Степанова А.А., Бондаренко Т.П., Шарова Н.П. Изменение функции протеасом после индукции донор-специфической толерантности у крыс при аллотрансплантации ткани яичника. Известия РАН. Сер. Биол. 2012. № 3. С. 296-302.
  140. Люпина Ю.В., Богатырев М.Е., Орлова А.Ш., Марюхнич Е.В., Казанский Д.Б., Шарова Н.П.. Протеасомы в головном мозгу мышей, нокаутных по β2-микроглобулину // Биохимия. 2013. Т. 78. Вып. 10. С. 1436-1447.
  141. Lyupina Y. V., Abaturova S.B., Erokhov P.A., Orlova O. V., Beljelarskaya S.N., Mikhailov V.S. Proteotoxic stress induced by Autographa californica nucleopolyhedrovirus infection of Spodoptera frugiperda Sf9 cells. Virology. 2013; 436(1):49-58.
  142. Krajewski W.A. Comparison of the Isw1a, Isw1b, and Isw2 nucleosome disrupting activities, Biochemistry. 2013, 52, 6940-6949.
  143. Шашова Е.Е., Астахова Т.М., Плеханова А.С., Богомягкова Ю.В., Люпина Ю.В., Сумеди И.Р., Слонимская Е.М., Ерохов П.А., Абрамова Е.Б., Родоман Г.В., Кузнецов Н.А., Кондакова И.В., Шарова Н.П., Чойнзонов Е.Л. Изменение химотрипсинподобной активности протеасом в развитии карцином молочной и щитовидной желез человека // Бюлл. Эксп. Биол. Мед. 2013 г. Т.155. № 8. С. 209-211.
  144. Карпова Я.Д., Люпина Ю.В., Астахова Т.М. Степанова А.А., Ерохов П.А., Абрамова Е.Б., Шарова Н.П. Иммунные протеасомы в развитии иммунной системы крысы. Биоорганическая химия. 2013 г. Т. 39, № 4. С 400-410.
  145. Krajewski W.A., Isw1a does not have strict limitations on the length of extranucleosomal DNAs for mobilization of nucleosomes assembled with HeLa cell histones, Journal of Biomolecular Structure and Dynamics, 2014, 32, 523-531.
  146. Krajewski W.A., Yeast Isw1a and Isw1b exhibit similar nucleosome mobilization capacities for mononucleosomes, but differently mobilize dinucleosome templates. Archives of Biochemistry and Biophysics, 2014, 546, 72-80.
  147. Lyupina Y. V., Orlova O. V., Abaturova S.B., Beljelarskaya S.N., Lavrov A.N., Mikhailov V.S. Egress of budded virions of Autographa californica nucleopolyhedrovirus does not require activity of Spodoptera frugiperda HSP/HSC70 chaperones. Virus Res. 2014; 192:1-5.
  148. Shashova E.E., Lyupina Yu. V., Glushchenko S.A., Slonimskaya E.M., Savenkova O. V., Kulikov A.M., Gornostaev N.G., Kondakova I. V., Sharova N.P. Proteasome Functioning in Breast Cancer: Connection with Clinical-Pathological Factors // Plos One. Published: October 17, 2014, DOI: 10.1371/journal.pone.0109933.
  149. Степанова А.А., Карпова Я.Д., Божок Г.А., Устиченко В.Д., Люпина Ю.В., Легач Е.И., Вагида М.С., Казанский Д.Б., Бондаренко Т.П., Шарова Н.П. Протеасомы при аллотрансплантации ткани щитовидной железы в условиях индукции донорспецифической толерантности у крыс // Биоорганическая химия. 2014 г. Т. 40. № 1. С. 42-54.
  150. Люпина Ю.В., Орлова А.Ш., Горностаев Н.Г., Карпова Я.Д., Михайлов В.С., Шарова Н.П. Пластичность нервной и иммунной систем у различных организмов: возможная роль протеасом // Журнал общей биологии. 2014. Т.75. № 1. C. 3-24
  151. Шарова Н.П., Сумеди И.Р., Астахова Т.М., Плеханова А.С., Люпина Ю.В., Шашова Е.Е., Кондакова И.В., Родоман Г.В. Диагностика рака щитовидной железы: ограничения существующих методов и перспективы будущих разработок. Известия Ран. Сер. Биол. 2014. №4. С. 348-354
  152. Орлова А.Ш., Люпина Ю.В., Абатурова С.Б., Шарова Н.П. Особенности экспрессии иммунных протеасом в развитии центральной нервной системы у крыс. Биоорганическая химия. 2014 г. Т. 40. № 6. С. 703-711.
  153. Luchnik AN. DNA conformational transitions induced by supercoiling control transcription in chromatin. Gene Regul Syst Bio. 2014 Mar 12;8:89-96. doi: 10.4137/GRSB.S13756. eCollection 2014.




Поделиться ссылкой: