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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">vestich</journal-id><journal-title-group><journal-title xml:lang="ru">Известия Национальной академии наук Беларуси. Серия химических наук</journal-title><trans-title-group xml:lang="en"><trans-title>Proceedings of the National Academy of Sciences of Belarus, Chemical Series</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1561-8331</issn><issn pub-type="epub">2524-2342</issn><publisher><publisher-name>The Republican Unitary Enterprise Publishing House "Belaruskaya Navuka"</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.29235/1561-8331-2022-58-1-105-128</article-id><article-id custom-type="elpub" pub-id-type="custom">vestich-711</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>ОБЗОРЫ</subject></subj-group></article-categories><title-group><article-title>Роль пуриновых и пиримидиновых нуклеозидов и их производных в реакциях, катализируемых панкреатической фосфолипазой А2</article-title><trans-title-group xml:lang="en"><trans-title>Role of purine and pyrimidine nucleosides and their derivatives in reactions catalyzed by pancreatic phospholipase A2</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Литвинко</surname><given-names>Н. М.</given-names></name><name name-style="western" xml:lang="en"><surname>Litvinko</surname><given-names>N. M.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Литвинко Наталья Михайловна – доктор химических наук, доцент, заведующая лабораторией</p><p>ул. Купревича, 5/2, 220141, Минск</p></bio><bio xml:lang="en"><p>Litvinko Natalia M. – D. Sc. (Chemistry), Associate Professor, Head of the laboratory</p><p>5/2, Kuprevich Str., 220141, Minsk</p></bio><email xlink:type="simple">al_h@mail.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Институт биоорганической химии Национальной академии наук Беларуси</institution></aff><aff xml:lang="en"><institution>Institute of Bioorganic Chemistry of the National Academy of Sciences of Belarus</institution></aff></aff-alternatives><pub-date pub-type="collection"><year>2022</year></pub-date><pub-date pub-type="epub"><day>11</day><month>03</month><year>2022</year></pub-date><volume>58</volume><issue>1</issue><fpage>105</fpage><lpage>128</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Литвинко Н.М., 2022</copyright-statement><copyright-year>2022</copyright-year><copyright-holder xml:lang="ru">Литвинко Н.М.</copyright-holder><copyright-holder xml:lang="en">Litvinko N.M.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://vestichem.belnauka.by/jour/article/view/711">https://vestichem.belnauka.by/jour/article/view/711</self-uri><abstract><p>Представлен обзор результатов изучения взаимосвязи в системе «нуклеозиды–фосфолипаза А2», которая играет определяющую роль в метаболизме фосфолипидов и их производных – простагландинов, тромбоксанов и лейкотриенов как важнейших внутриклеточных мессенджеров. Рассмотрено влияние нуклеозидов на активность секреторной ФЛА2 и метаболизм липонуклеозидов, представляющих интерес в качестве специфических средств доставки нуклеозидных лекарств. Результаты этих исследований рассмотрены с точки зрения фармакологического потенциала липонуклеозидов как новых форм известных лекарственных препаратов.</p></abstract><trans-abstract xml:lang="en"><p>A review of the results of studying the relationship in the system “nucleosides–phospholipase A2”, which plays a decisive role in the metabolism of phospholipids and their derivatives – prostaglandins, thromboxanes and leukotrienes as the most important intracellular messengers, is presented. The review considers the effect of nucleosides on the activity of secretory PLA2 and the metabolism of liponucleosides, which are of interest as specific delivery vehicles for nucleoside drugs. The results of these studies are considered from the point of view of the pharmacological potential of liponucleosides as new forms of known drugs.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>нуклеозиды</kwd><kwd>фосфолипазы А2</kwd><kwd>липонуклеозиды</kwd><kwd>гидролиз фосфолипидов</kwd></kwd-group><kwd-group xml:lang="en"><kwd>nucleosides</kwd><kwd>phospholipases A2</kwd><kwd>liponucleosides</kwd><kwd>hydrolysis of phospholipids</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Брокерхофф, X. Липолитические ферменты / X. Брокерхофф, Р. Дженсен. – М.: Мир, 1978. – 330c.</mixed-citation><mixed-citation xml:lang="en">Brockerhoff H., Jensen R. G. Lipolytic enzymes. New York, Academic Press, 1974. 330 p. https://doi.org/10.1016/B978-0-12-134550-1.X5001-1</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Mouchlis, V. D. Phospholipase A2 catalysis and lipid mediator lipidomics / V. D. Mouchlis, E. A. Dennis // Biochim. Biophys. Acta. Mol. Cell. Biol. Lipids. – 2019. – Vol. 1864(6). – P. 766–771. https://doi.org/10.1016/j.bbalip.2018.08.010</mixed-citation><mixed-citation xml:lang="en">Mouchlis V. D., Dennis E. A. Phospholipase A2 catalysis and lipid mediator lipidomics. Biochimica et Biophysica Acta (BBA) – Molecular and Cell Biology of Lipids. 2019, vol. 1864, no. 6, pp. 766–771. https://doi.org/10.1016/j.bbalip.2018.08.010</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Zimmermann, H. Extracellular ATP and other nucleotides–ubiquitous triggers of intercellular messenger release / Н. Zimmermann // Purinergic. Signal. – 2016 – Vol. 12(1). – P. 25–57. https://doi.org/10.1007/s11302-015-9483-2</mixed-citation><mixed-citation xml:lang="en">Zimmermann H. Extracellular ATP and other nucleotides–ubiquitous triggers of intercellular messenger release. Purinergic. Signal. 2016, vol. 12, no. 1, pp. 25–57. https://doi.org/10.1007/s11302-015-9483-2</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Nucleoside conjugates. Synthesis and biological activity of anti-HIV7 nucleoside conjugates of ether and thioether phospholipids / С. I. Hong [et al.] // J. Med. Chem. – 1996. – Vol. 39, N 9. – P. 1771–1777. https://doi.org/10.1021/jm950620o</mixed-citation><mixed-citation xml:lang="en">Hong С. I., Nechaev A., Kirisits A. J., Vig R., West C. R., Manouilov K. K., Chu C. K. Nucleoside conjugates. Synthesis and biological activity of anti-HIV7 nucleoside conjugates of ether and thioether phospholipids. Journal of Medicinal Chemistry, 1996, vol. 39, no. 9, pp. 1771–1777. https://doi.org/10.1021/jm950620o</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Фармакокинетические свойства и энзиматический гидролиз диацилглицерофосфатных производных флударабина / И. А. Цибульская [и др.] // Докл. Нац. акад. наук Беларуси. – 2016. – Т. 60, № 1. – С. 65–71.</mixed-citation><mixed-citation xml:lang="en">Tsybulskaya I. A., Kulak T .I., Buravskaya T. N., Golubeva M. B., Shabunya P. S., Fatykhova S. A., Kurman P. V., Kalinichenko E. N. Pharmacokinetic properties and the enzymatic hydrolysis of diacylglyce-rophosphate fludarabine derivatives. Doklady Natsional`noi akademii nauk belarusi = Dokladyof the National Academy of Sciences of Belarus, 2016, vol. 60, no. 1, pp. 65–71 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Synthesis of phospholipid_ribavirin conjugates / I. A. Oleynikova [et al.] // Helv. Chim. Acta. – 2013. – Vol. 96, N 3. – Р. 463–472. https://doi.org/10.1002/hlca.201200203</mixed-citation><mixed-citation xml:lang="en">Oleynikova I. A., Kulak T. I., Bolibrukh D. A., Kalinichenko E. N. Synthesis of phospholipid_ribavirin conjugates. Helvetica Chimica Acta, 2013, vol. 96, no. 3. 46, pp. 463–472. https://doi.org/10.1002/hlca.201200203</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Lipid conjugates of antiretroviral agents. I. Azidothymidine-monophosphate-diglyceride: anti-HIV7 activity, physical properties, and interaction with plasma proteins / J. M. Steim [et al.] // Biochem. Biophys. Res. Conimun. – 1990. – Vol. 171, N I. – P.451–457. https://doi.org/10.1016/0006-291x(90)91414-n</mixed-citation><mixed-citation xml:lang="en">Steim J. M., Neto C. C., Sarin P. S., Sun D. K., Sehgal R. K., Turcotte J. G. Lipid conjugates of antiretroviral agents. I. Azidothymidine-monophosphate-diglyceride: anti-HIV7 activity, physical properties, and interaction with plasma proteins. Biochemical and Biophysical Research Communications, 1990, vol. 171, no. I, pp. 451–457. https://doi.org/10.1016/0006-291x(90)91414-n</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Hostetler, К. Y Phosphatidylazidothymidine. Mechanism of antiretroviral action in CEM cells / K. Y. Hostetler, D. A. Carson, D. D. Richman // Biol. Chem. – 1991. – Vol. 266, N 18. – P. 11714–11717. https://doi.org/10.1016/s0021-9258(18)99015-0</mixed-citation><mixed-citation xml:lang="en">Hostetler К. Y., Carson D. A., Richman D. D. Phosphatidylazidothymidine. Mechanism of antiretroviral action in CEM cells. Journal of Biological Chemistry, 1991, vol. 266, no. 18, pp. 11714–11717. https://doi.org/10.1016/s0021-9258(18)99015-0</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Cellular metabolism in lymphocytes of a novel thioether-phospholtpid-AZT conjugate with anti-HIV-1 activity / G. L. Kucera [et al.] // Antiviral Res. – 2001. – Vol. 50, N 2. – P. 129–137. https://doi.org/10.1016/s0166-3542(01)00137-1</mixed-citation><mixed-citation xml:lang="en">Kucera G. L., Goff C., Iyer N., Morrisnatschke S., Ishaq K., Wyrick S., Fleming R., Kucera L. Cellular metabolism in lymphocytes of a novel thioether-phospholtpid-AZT conjugate with anti-HIV-1 activity. Antiviral Research, 2001, vol. 50, no. 2, pp. 129–137. https://doi.org/10.1016/s0166-3542(01)00137-1</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Химико-энзиматическая модификация компонентов нуклеиновых кислот и биохимическое моделирование как научно-практическая основа поиска, создания и производства противовирусных и противоопухолевых лекарственных средств / Е. Н. Калиниченко [и др.] // Вестн. ФФИ. – 2006. – № 3. – С. 32–57.</mixed-citation><mixed-citation xml:lang="en">Kalinichenko E. N., Mikhailopulo I. А.,, Litvinko N. М., Zinchenko A. I., Petrov P. T. Chemical-enzymatic modification of nucleic acid components and biochemical modeling as a scientific and practical basis for the search, creation and production of antiviral and antitumor drugs. Vestnik Fonda fundamental’nykh issledovanii = Bulletin of the foundation for fundamental research, 2006, no. 3, pp. 32–57 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Владимиров, В. Г. Острый панкреатит. Экспериментально-клинические исследования / В. Г. Владимиров, В. И. Сергиенко. – М.: Медицина, 1986. – 240 с.</mixed-citation><mixed-citation xml:lang="en">Vladimirov V. G., Sergienko V. I. Acute pancreatitis. Experimental clinical research. Moscow, Meditsina Publ., 1986. 240 p. (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Various secretory phospholipase A2 enzymes are expressed in rheumatoid arthritis and augment prostaglandin production in cultured synovial cells / S. Masuda [et al.] // Febs J. – 2005. – Vol. 272, N 3. – P. 655–672. https://doi.org/10.1111/j.1742-4658.2004.04489.x</mixed-citation><mixed-citation xml:lang="en">Masuda S., Murakami M., Komiyama K., Ishihara M., Ishikawa Y., Ishii T., Kudo I. Various secretory phospholipase A2 enzymes are expressed in rheumatoid arthritis and augment prostaglandin production in cultured synovial cells. FEBS Journal , 2005, vol. 272, no. 3, pp. 655–672. https://doi.org/10.1111/j.1742-4658.2004.04489.x</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Phospholipase A2 enzymes / I. Kudo [et al.] // Prostaglandins Other Lipid. Mediat. – 2002. – Vol. 68–69. – P. 3–58. https://doi.org/10.1016/s0090-6980(02)00020-5</mixed-citation><mixed-citation xml:lang="en">Kudo I., Murakami M. Phospholipase A2 enzymes. Prostaglandins &amp; Other Lipid Mediators, 2002, vol. 68–69, pp. 3–58. https://doi.org/10.1016/s0090-6980(02)00020-5</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Identification of a 27 bp 5’-flanking region element responsible for the lowlevel constitutive expression of the human cytosolic phospholipase A2 gene / A. Miyashita [et al.] // Nucleic. Acids. Res. – 1995. – Vol. 23, N 2. – P. 293–301. https://doi.org/10.1093/nar/23.2.293</mixed-citation><mixed-citation xml:lang="en">Miyashita A., Crystal R. G., Hay J. G. Identification of a 27 bp 5’-flanking region element responsible for the low level constitutive expression of the human cytosolic phospholipase A2 gene. Nucleic Acids Research, 1995, vol. 23, no. 2, pp. 293– 301. https://doi.org/10.1093/nar/23.2.293</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Lambeau, G. Receptors for a growing family of secreted phospholipases A2 / G. Lambeau, M. Lazdunski // Trends. Pharmacol. Sci. – 1999. – Vol. 20, N 4. – P. 162–170. https://doi.org/10.1016/s0165-6147(99)01300-0</mixed-citation><mixed-citation xml:lang="en">Lambeau G., Lazdunski M. Receptors for a growing family of secreted phospholipases A2. Trends in Pharmacological Sciences, 1999, vol. 20, no. 4, pp. 162–170. https://doi.org/10.1016/s0165-6147(99)01300-0</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Studies on a mechanism by which cytosolic phospholipase A2 regulates the expression and function of type IIA secretory phospholipase A2 / H. Kuwata [et al.] // J. Immunol. – 2000. – Vol. 165, N 7. – P. 4024–4031. https://doi.org/10.4049/jimmunol.165.7.4024</mixed-citation><mixed-citation xml:lang="en">Kuwata H., Yamamoto S., Miyazaki Y., Shimbara S., Nakatani Y., Suzuki H., Ueda N., Yamamoto S., Murakami M., Kudo I. Studies on a mechanism by which cytosolic phospholipaseA2 regulates the expression and function of type IIA secretory phospholipase A2. The Journal of Immunology, 2000, vol. 165, no. 7, pp. 4024–4031. https://doi.org/10.4049/jimmunol.165.7.4024</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Regulation of cytosolic phospholipase A2 in rat endometrial stromal cells: the role of epidermal growth factor / B. M. Bany [et al.] // Mol. Reprod. Dev. – 1999. – Vol. 52,N 4. – P. 335–340. https://doi.org/10.1002/(sici)1098-2795(199904)52:4&lt;335::aid-mrd1&gt;3.0.co;2-f</mixed-citation><mixed-citation xml:lang="en">Bany B. M., Schultz G. A., Kennedy T. G. Regulation of cytosolic phospholipase A2 in rat endometrial stromal cells: the role of epidermal growth factor. Molecular Reproduction and Development, 1999, vol. 52, no. 4, pp. 335–340. https://doi.org/10.1002/(sici)1098-2795(199904)52:4&lt;335::aid-mrd1&gt;3.0.co;2-f</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Verheij, H. M. Structure and function of phospholipase A2 / H. M. Verheij, A. J. Slotboom, G. H. de Haas // Rev. Physiol. Biochem. Pharmacol. – 1981. – Vol. 91. – P. 91–203.</mixed-citation><mixed-citation xml:lang="en">Verheij H. M., Slotboom A. J., de Haas G. H. Structure and function of phospholipase A2. Reviews of physiology, biochemistry and pharmacology, 1981, vol. 91, pp. 91–203.</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Group II phospholipase A2 mRNA synthesis is stimulated by two distinct mechanisms in rat vascular smooth muscle cells / T. Nakano [et al.] // FEBS Lett. – 1990. –Vol. 261, N 1. – P. 171–174. https://doi.org/10.1016/0014-5793(90)80663-4</mixed-citation><mixed-citation xml:lang="en">Nakano T., Ohara O., Teraoka H., Arita H. Group II phospholipase A2 mRNA synthesis is stimulated by two distinct mechanisms in rat vascular smooth muscle cells. FEBS Letters, 1990, vol. 261, no. 1, pp. 171–174. https://doi.org/10.1016/0014-5793(90)80663-4</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Potential benefits and risks of omega-3 fatty acids supplementation to patients with COVID-19 / M. M. Rogero [et al.] // Free Radical Biology and Medicine. – 2020. – Vol. 156. – P. 190–199. https://doi.org/10.1016/j.freeradbiomed.2020.07.005</mixed-citation><mixed-citation xml:lang="en">Rogero M. M., de C. Leão M., Santana T. M., de M. B. Pimentel M. B., Carlini G. C. G., da Silveira T. F. F., Gonçalves R. C., Castro I. A. Potential benefits and risks of omega-3 fatty acids supplementation to patients with COVID-19. Free Radical Biology and Medicine, 2020, vol. 156, pp. 190–199. http:doi.org/10.1016/j.freeradbiomed.2020.07.005</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Large-Scale Plasma Analysis Revealed New Mechanisms and Molecules Associated with the Host Response to SARS-CoV-2 / E. Barberis [et al.] // Int. J. Mol. Sci. – 2020. – Vol. 21. – Р. 8623–8648. https://doi.org/10.3390/ijms21228623</mixed-citation><mixed-citation xml:lang="en">Barberis E., Timo S., Amede E., Vanella V. V., Puricelli Ch., Cappellano G., Raineri D., Cittone M. G., Rizzi E., Pedrinelli A. R., Vassia V., Casciaro F. G., Priora S., Nerici I., Galbiati A., Hayden E., Falasca M., Vaschetto R., Sainaghi P. P., Dianzani U., Rolla R., Chiocchett A., Baldanzi G., Marengo E., Manfredi M. Large-Scale Plasma Analysis Revealed New Mechanisms and Molecules Associated with the Host Response to SARS-CoV-2. International Journal of Molecular Sciences, 2020, vol. 21, pp. 8623–8648. https://doi.org/10.3390/ijms21228623</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Литвинко, Н. М. Ингибирование фосфолипаз А2 и С / Н. М. Литвинко // Вес. Нац. акад. навук Беларусі. Сер. хім. навук. – 2005. – № 4. – С. 113–124.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. М. Inhibition of phospholipases А2andС. Vestsi Natsyyanal’nai akademii navuk Belarusi. Seryya khimichnykh navuk = Proceedings of the National Academy of Sciences of Belarus. Chemical series, 2005, no. 4, pp. 113–124 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Литвинко, Н. М. Анионный центр панкреатической фосфолипазы А2 свиньи / Н. М. Литвинко, Ю. И. Хургин, Е. Д. Каверзнева // Биохимия. – 1977. – T. 42, № 1. – С. 85–94.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. M., Khurgin Yu. I., Kaverzneva E. D. Anionic center of porcine pancreatic phospholipase A2. Biochemistry (Moscow), 1977, vol. 42, no. 1, pp. 85–94 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Small-molecule inhibitors as potential therapeutics and as tools to understand the role of phospholipases A2 / A. Nikolaou [et al.] // Biochimica et Biophysica Acta (BBA) – Molecular and Cell Biology of Lipids. – 2019. – Vol. 1864, N6. – P. 941–956. https://doi.org/10.1016/j.bbalip.2018.08.009</mixed-citation><mixed-citation xml:lang="en">Nikolaou A., Kokotou M. G., Vasilakaki S., Kokotos G. Small-molecule inhibitors as potential therapeutics and as tools to understand the role of phospholipases A2. Biochimica et Biophysica Acta (BBA) – Molecular and Cell Biology of Lipids, 2019, vol. 1864, no. 6, pp. 941–956. https://doi.org/10.1016/j.bbalip.2018.08.009</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Synthesis of new secretory phospholipase A2-inhibitory indole containing isoxazole derivatives as anti-inflammatory and anticancer agents / S. R. Pedada [et al.] // Eur. J. Med. Chem. – 2016. – Vol. 112 – P. 289–297. https://doi.org/10.1016/j.ejmech.2016.02.025</mixed-citation><mixed-citation xml:lang="en">Pedada S. R. Yarla N. S., Tambade P. J., Dhananjaya B. L., Bishayee A., Arunasree K. M., Philip G. H., Dharmapuri G., Aliev G., Putta S., Rangaiah G. Synthesis of new secretory phospholipase A2-inhibitory indole containing isoxazole derivatives as anti-inflammatory and anticancer agents. European Journal of Medicinal Chemistry, 2016, vol. 112, pp. 289–297. https://doi.org/10.1016/j.ejmech.2016.02.025</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Discovery of AZD2716: a novel secreted phospholipase A2 (sPLA2) inhibitor for the treatment of coronary artery disease / F. Giordanetto [et al.] // ACS Med. Chem. Lett. – 2016. – Vol. 7, N 10. – P. 884–889. https://doi.org/10.1021/acsmedchemlett.6b00188</mixed-citation><mixed-citation xml:lang="en">Giordanetto F., Pettersen D., Starke I., Nordberg P., Dahlström M., Knerr L., Selmi N., Rosengren B., Larsson L-O., Sandmark J., Castaldo M., Dekker N., Karlsson U., Hurt-Camejo E. Discovery of AZD2716: a novel secreted phospholipase A2 (sPLA2) inhibitor for the treatment of coronary artery disease. ACS Medicinal Chemistry Letters, 2016, vol. 7, no. 10, pp. 884–889. https://doi.org/10.1021/acsmedchemlett.6b00188</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Development of a potent 2-oxoamide inhibitor of secreted phospholipase A2 guided by molecular docking calculations and molecular dynamics simulations / S. Vasilakaki [et al.] // Bioorg. Med. Chem. – 2016. Vol. 24, N. 8. – P. 1683–1695. https://doi.org/10.1016/j.bmc.2016.02.040</mixed-citation><mixed-citation xml:lang="en">Vasilakaki S., Barbayianni E., Leonis G., Papadopoulos M. G., Mavromoustakos T., Gelb M. H., Kokotos G. Development of a potent 2-oxoamide inhibitor of secreted phospholipase A2 guided by molecular docking calculations and molecular dynamics simulations. Bioorganic &amp; Medicinal Chemistry, 2016, vol. 24, no. 8, pp. 1683–1695. https://doi.org/10.1016/j.bmc.2016.02.040</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Inhibitors of secreted phospholipase A2 suppress the release of PGE2 in renal mesangial cells / S. Vasilakaki [et al.] // Bioorg. Med. Chem. – 2016. Vol. 24, N 13. – P. 3029–3034. https://doi.org/10.1016/j.bmc.2016.05.017</mixed-citation><mixed-citation xml:lang="en">Vasilakaki S., Barbayianni E., Magriot, V., Pastukhov O., Constantinou-Kokotou V., Huwiler A., Kokotos G. Inhibitors of secreted phospholipase A2 suppress the release of PGE2 in renal mesangial cells. Bioorganic &amp; medicinal chemistry, 2016, vol. 24, no. 13, pp. 3029–3034. https://doi.org/10.1016/j.bmc.2016.05.017</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">New quinoxalinone inhibitors targeting secreted phospholipase A2 and α-glucosidase / F. Alasmary [et al.] // J. Enzyme Inhib. Med. Chem. – 2017. – Vol. 32, N 1. – P. 1143–1151. https://doi.org/10.1080/14756366.2017.1363743</mixed-citation><mixed-citation xml:lang="en">Alasmary F., Alnahdi F. S., Ben Bacha A., El-Araby A. M., Moubayed N., Alafeefy A. M., El-Araby M. E. New quinoxalinone inhibitors targeting secreted phospholipase A2 and α-glucosidase. Journal of enzyme inhibition and medicinal chemistry, 2017, vol. 32, no. 1, pp. 1143–1151. https://doi.org/10.1080/14756366.2017.1363743</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Dimethyl ester of bilirubin exhibits anti-inflammatory activity through inhibition of secretory phospholipase A2, lipoxygenase and cyclooxygenase / V. Joshi [et al.] // Arch. Biochem. Biophys. – 2016. – Vol. 598. – P. 28–39. https://doi.org/10.1016/j.abb.2016.04.003</mixed-citation><mixed-citation xml:lang="en">Joshi V., Umashankara M., Ramakrishnan C., Nanjaraj Urs A. N., Suvilesh K. N., Velmurugan D., Rangappa K. S., Vishwanath B. S. Dimethyl ester of bilirubin exhibits anti-inflammatory activity through inhibition of secretory phospholipase A2, lipoxygenase and cyclooxygenase. Archives of biochemistry and biophysics, 2016, vol. 598, pp. 28–39. https://doi.org/10.1016/j.abb.2016.04.003</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Celastrol modulates inflammation through inhibition of the catalytic activity of mediators of arachidonic acid pathway: secretory phospholipase A2 group IIA, 5-lipoxygenase and cyclooxygenase-2 / V. Joshi [et al.] // Pharmacol. Res. – 2016. – Vol. 113. – P. 265–275. https://doi.org/10.1016/j.phrs.2016.08.035</mixed-citation><mixed-citation xml:lang="en">Joshi V., Venkatesha S. H., Ramakrishnan C., Nanjaraj Urs A. N., Hiremath V., Moudgil K. D., Velmurugan D., Vishwanath B. S. Celastrol modulates inflammation through inhibition of the catalytic activity of mediators of arachidonic acid pathway: secretory phospholipase A2 group IIA, 5-lipoxygenase and cyclooxygenase-2. Pharmacological Research, 2016, vol. 113, pp. 265–275. https://doi.org/10.1016/j.phrs.2016.08.035</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Inhibitory effect of sulforaphane on secretory group IIA phospholipase A2 / Y. Lee [et al.] // Int. J. Pharmacol. – 2018. – Vol. 14. – P. 187–193. https://doi.org/10.3923/ijp.2018.187.193</mixed-citation><mixed-citation xml:lang="en">Lee Y., Lee W., Kim J., Bae J-S. Inhibitory effect of sulforaphane on secretory group IIA phospholipase A2. International Journal of Pharmacology, 2018, vol. 14, pp. 187–193. https://doi.org/10.3923/ijp.2018.187.193</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Inhibition of secretory phospholipase A2. 1-Design, synthesis and structure–activity relationship studies starting from 4-tetradecyloxybenzamidine to obtain specific inhibitors of group II sPLA2s / L. Assogbaa [et al.] // European Journal of Medicinal Chemistry. – 2005. – Vol. 40, N 9. – P. 850–861. https://doi.org/10.1016/j.ejmech.2005.03.027</mixed-citation><mixed-citation xml:lang="en">Assogbaa L., Ahamada-Himidia A., Meddad-Bel Habicha N., Aouna D., Bouklia L., Massicota F., Mounierc C. M., Hueta J., Lamouri A., Ombetta J.-E., Godfroid J.-J., Donga, C.-Z., Heymans F. Inhibition of secretory phospholipase A2. 1-Design, synthesis and structure–activity relationship studies starting from 4-tetradecyloxybenzamidine to obtain specific inhibitors of group II sPLA2s. European Journal of Medicinal Chemistry, 2005, vol. 40, no. 9, pp. 850–861. https://doi.org/10.1016/j.ejmech.2005.03.027</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Взаимосвязь между действием аналогов простагландинов на активность фосфолипазы А2 и их биологической активностью/ Н. М. Литвинко [и др.] // Вес. Нац. акад. навук Беларусі. Сер. хім. навук. –1998. – № 4. С. 101–113.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. М., Kuchuro S. V., Zheldakova T. A., Lis L. G., Filich E. R., Kuzmitskii B. B., Shulyak V. N. A correlation between prostaglandin analogs effect on phospholipase A2 and their biological activity. Vestsi Natsyyanal’nai akademii navuk Belarusi. Seryya khimichnykh navuk = Proceedings of the National Academy of Sciences of Belarus. Chemical series, 1998, no. 4, pp. 101–113 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">3,5-дизамещенные производные тиотетроновой кислоты – новые ингибиторы секреторных фосфолипаз А2 / С. В. Кучуро [и др.] // Докл. Нац. акад. наук Беларуси. – 2004. – Т. 48, № 1. – С. 65-69.</mixed-citation><mixed-citation xml:lang="en">Kuchuro S. V., Rakhuba G. N., Rubinov D. B., Zheldakova T. A., Babitskaya S. V., Litvinko N. M. 3,5-disubstituted thiotetronic acid derivatives – new inhibitors of secretor phospholipases A2. Doklady Natsional`noi akademii nauk belarusi = Dokladyof the National Academy of Sciences of Belarus, 2004, vol. 48, no. 1, pp. 65–69 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Compositions and methods for inhibition of phospholipase A2 mediated inflammation: Pat. US 7745489B2 / E. Dennis, T. Yaksh, K. K. Lucas, C. Svensson, D. A. Six, G. Kokotos, V. Constantinou-Kokotou. – Publ. date 29.06.2010.</mixed-citation><mixed-citation xml:lang="en">Dennis E., Yaksh T., Lucas K. K., Svensson C., Six D. A., Kokotos G., Constantinou-Kokotou V. Compositions and methods for inhibition of phospholipase A2 mediated inflammation. Patent USA, no. 7745489B2, 2010.</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Inhibitors of phospholipase enzymes: Pat. US20030153751A1 / J. Seehra, N. Kaila, J. Mckew, F. Lovering, J. Bemis, Y. Xiang. – Publ. date 14.08.2003.</mixed-citation><mixed-citation xml:lang="en">Seehra J. S., Kaila N., Mckew J. S., Lovering F., Bemis J. E., Xiang Y. Phospholipase inhibitors. Patent USA, no. 20030153751A1, 2003.</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Small-molecule inhibitors as potential therapeutics and as tools to understand the role of phospholipase A2 / A. Nicolaou [et al.] // BBA – Molecular and Cell Biology of Lipids. – 2019. – Vol. 1864, N 6. – P. 941–956. https://doi.org/10.1016/j.bbalip.2018.08.009</mixed-citation><mixed-citation xml:lang="en">Nicolaou A., Kokotou M. G., Vasilakaki S. G., Kokotos. Small-molecule inhibitors as potential therapeutics and as tools to understand the role of phospholipase A2. BBA –Molecular and Cell Biology of Lipids, 2019, vol. 1864, no. 6, pp. 941– 956. https://doi.org/10.1016/j.bbalip.2018.08.009</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Development of potent and selective inhibitors for group VIA calcium-independent phospholipase A2 guided by molecular dynamics and structure-activity relationships / V. D. Mouchlis [et al.] // J. Med. Chem. – 2016. Vol. 59, N. 9. – P. 4403–4414. https://doi.org/10.1021/acs.jmedchem.6b00377</mixed-citation><mixed-citation xml:lang="en">Mouchlis V. D., Limnios D., Kokotou M. G., Barbayianni E., Kokotos G., McCammon J. A., Dennis E. A. Development of potent and selective inhibitors for group VIA calcium-independent phospholipase A2 guided by molecular dynamics and structure-activity relationships. Journal of medicinal chemistry, 2016, vol. 59, no. 9, pp. 4403–4414. https://doi.org/10.1021/acs.jmedchem.6b00377</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Mouchlis, V. D. Phospholipase A2 catalysis and lipid mediator lipidomics / V. D. Mouchlis, E. A. Dennis // BBA – Molecular and Cell Biology of Lipids. – 2018. – Vol. 1864, N. 6. – P. 766–771. https://doi.org/10.1016/j.bbalip.2018.08.010</mixed-citation><mixed-citation xml:lang="en">Mouchlis V. D., Dennis E. A. Phospholipase A2 catalysis and lipid mediator lipidomics. BBA – Molecular and Cell Biology of Lipids, 2018, vol. 1864, no. 6, pp. 766-771. https://doi:10.1016/j.bbalip.2018.08.010</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Скрининг действия фосфатных аналогов ацикловира на реакцию липолиза с участием панкреатической ФЛА2 / Н. М. Литвинко [и др.] // Современное состояние и перспективы развития микробиологии и биотехнологии : сб. материалов междунар. науч. конф. – Минск, 2008. – Т. 2. – С. 17–19.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. M., Kuchuro S. V., Gerlovsky D. O., Kalinichenko E. N., Farina A. V. Screening of the effect of acyclovir phosphate analogues on the lipolytic reaction with pancreatic PLA2 participation. Sovremennoe sostoyanie i perspektivy razvitiya mikrobiologi i biotekhnologii: sb. materialov mezhdunar. nauch. konf. [Current state and prospects for the development of microbiology and biotechnology: collection of materials of the international. scientific. conf.]. Minsk, 2008, vol. 2, pp. 17–19 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Действие фосфолипаз на химерные субстраты, созданные на основе фосфолипидов и компонентов нуклеиновых кислот / Н. М. Литвинко [и др.] // Докл. Нац. акад. наук Беларуси. – 2005. – Т. 49, № 4, – С. 70–73.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. M., Kuchuro S. V., Rakhuba G. N., Skorostetskaya L. A., Kalinichenko E. N., Zhernosek E. V. Effect of phospholipases on chimeric substrates based on phospholipids and nucleic acid components. Doklady Natsional`noi akademii nauk belarusi = Dokladyof the National Academy of Sciences of Belarus, 2005, vol. 49, no. 4, pp. 70–73 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Nuclear translocation of cytosolic phospholipase A2 is induced by ATP depletion / A. M. Sheridan [et al.] // J. Biol. Chem. – 2001. – Vol. 276, N 32. – Р. 29899–29905. https://doi.org/10.1074/jbc.m103758200</mixed-citation><mixed-citation xml:lang="en">Sheridan A. M., Sapirstein A., Lemieux N., Martin B. D., Kim D. K., Bonventre, J. V. Nuclear translocation of cytosolic phospholipase A2 is induced by ATP depletion. Journal of Biological Chemistry, 2001, vol. 276, no. 32, pp. 29899– 29905. https://doi.org/10.1074/jbc.m103758200</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Lykidis, A. Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant / A. Lykidis, I. Baburina, S. Jackowski // J. Biol. Chem. – 1999. – Vol. – 274, N 38. – P. 26992–27001. https://doi.org/10.1074/jbc.274.38.26992</mixed-citation><mixed-citation xml:lang="en">Lykidis A., Baburina I., Jackowski S. Distribution of CTP: phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant. Journal of Biological Chemistry, 1999, vol. 274, no. 38, pp. 26992–27001. https://doi.org/10.1074/jbc.274.38.26992</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Baburina, I. Cellular responses to excess phospholipids / I. Baburina, S. Jackowski // J. Biol. Chem. – 1999. – Vol. 274, N 14. – P. 9400–9408. https://doi.org/10.1074/jbc.274.14.9400</mixed-citation><mixed-citation xml:lang="en">Baburina I., Jackowski S. Cellular responses to excess phospholipids. Journal of Biological Chemistry, 1999, vol. 274, no. 14, pp. 9400–9408. https://doi.org/10.1074/jbc.274.14.9400</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">CDP-choline significantly restores phosphatidylcholine levels by differentially affecting phospholipase A2 and CTP: phosphocholine cytidylyltransferase after stroke / R. M. Adibhatla [et al.] // J. Biol. Chem. – 2006. – Vol. 281, N 10. – P. 6718–6725. https://doi.org/10.1074/jbc.M512112200</mixed-citation><mixed-citation xml:lang="en">Adibhatla R. M., Hatcher J. F., Larsen E. C., Chen X., Sun D., Tsao F. H. CDP-choline significantly restores phosphatidylcholine levels by differentially affecting phospholipase A2 and CTP: phosphocholine cytidylyltransferase after stroke. Journal of Biological Chemistry, 2006, vol. 281, no. 10, pp. 6718–6725. https://doi.org/10.1074/jbc.M512112200</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">McHowat, J. Thrombin activates a membrane-associated calcium-independent PLA2 in ventricular myocytes / J. McHowat, M. H. Creer // Am. J. Physiol. – 1998. – Vol. 274, N 2, Pt 1. – P. 447–454. https://doi.org/10.1152/ajpcell.1998.274.2.C447</mixed-citation><mixed-citation xml:lang="en">McHowat J., Creer M. H. Thrombin activates a membrane-associated calcium-independent PLA2 in ventricular myocytes. American Journal of Physiology-Cell Physiology, 1998, vol. 274, no. 2, pt 1, pp. 447–454. https://doi.org/10.1152/ajpcell.1998.274.2.C447</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Hazen, S. L. ATP-dependent regulation of rabbit myocardial cytosolic calcium-independent phospholipase A2 / S. L. Hazen, R. W. Gross // J. Biol. Chem. – 1991. – Vol. 266, N 22. – P. 14526–14534. https://doi.org/10.1016/S0021-9258(18)98718-1</mixed-citation><mixed-citation xml:lang="en">Hazen S. L., Gross R. W. ATP-dependent regulation of rabbit myocardial cytosolic calcium-independent phospholipase A2. Journal of Biological Chemistry, 1991, vol. 266, no. 22, pp. 14526–14534. https://doi.org/10.1016/S0021-9258(18)98718-1</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Hazen, S. L. Human myocardial cytosolic Ca(2+)-independent phospholipase A2 is modulated by ATP. Concordant ATP-induced alterations in enzyme kinetics and mechanism-based inhibition / S. L. Hazen, R. W. Gross // Biochem. J. – 1991. – Vol. 280, N. 3. – P. 581–587. https://doi.org/10.1042/bj2800581</mixed-citation><mixed-citation xml:lang="en">Hazen S. L., Gross R. W. Human myocardial cytosolic Ca(2+)-independent phospholipase A2 is modulated by ATP. Concordant ATP-induced alterations in enzyme kinetics and mechanism-based inhibition. Biochemical Journal, 1991, vol. 28, no. 3, pp. 581–587. https://doi.org/10.1042/bj2800581</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Ackermann, E. J. Inhibition of macrophage Ca(2+)-independent phospholipase A2 by bromoenol lactone and trifluoromethyl ketones / E. J. Ackermann, K. Conde-Frieboes, E. A. Dennis // J. Biol. Chem. – 1995. – Vol. 270, N 1. – P. 445–450. https://doi.org/10.1074/jbc.270.1.445</mixed-citation><mixed-citation xml:lang="en">Ackermann E. J., Conde-Frieboes K., Dennis E. A. Inhibition of macrophage Ca(2+)-independent phospholipase A2 by bromoenol lactone and trifluoromethyl ketones. Journal of Biological Chemistry, 1995, vol. 270, no. 1, pp. 445–450. https://doi.org/10.1074/jbc.270.1.445</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Ackermann, E. J. Ca(2+)-independent cytosolic phospholipase A2 from macrophage-like P388D1 cells. Isolation and characterization / E. J. Ackermann, E. S. Kempner, E. A. Dennis // J. Biol. Chem. – 1994. – Vol. 269, N 12. – P. 9227–9233. https://doi.org/10.1016/S0021-9258(17)37098-9</mixed-citation><mixed-citation xml:lang="en">Ackermann E. J., Kempner E. S., Dennis E. A. Ca(2+)-independent cytosolic phospholipase A2 from macrophage-like P388D1 cells. Isolation and characterization. Journal of Biological Chemistry, 1994, vol. 269, no. 12, pp. 9227–9233. https://doi.org/10.1016/S0021-9258(17)37098-9</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Литвинко, Н. М. Комплексообразование фосфолипазы А2 с фрагментами нуклеиновых кислот и способы их устранения / Н. М. Литвинко, А. П. Дрожденюк // Прикладная биохимия и микробиология. – 1996. – Т. 32, № 6. – С. 650–655.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. M., Drozhdenok A. P. Complexation of phospholipase A2 with nucleic acid fragments and methods for their elimination. Prikladnaya biokhimiya i mikrobiologiya [Applied Biochemistry and Microbiology], 1996, vol. 32, no. 6, pp. 650–655 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Способ определения эффекторных свойств физиологически активных соединений: пат. BY 5752 / Н. М. Литвинко, С. В. Кучуро, Т. А. Желдакова, Е. Р. Филич. – Опубл. 07.01.2004.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. М., Kuchuro S. V., Zheldakova Т. А., Filich Е. R. Method for determining the effector properties of physiologically active compounds. Patent BY, no. 5752, 2004 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Активность ФЛА2 в присутствии модифицированных аналогов нуклеозидов / А. В. Лях [и др.] // Биотехнологии микроорганизмов: материалы междунар. науч.-практ. конф. посвящ. Ю. К. Фомичеву, Минск, 27–29 ноября 2019 г. – Минск, 2019. – С. 368–370.</mixed-citation><mixed-citation xml:lang="en">Lyakh A. V., Litvinko N. M., Mikhailopulo I. A., Gerlovsky D. O. PLA2 Activity in the Presence of Modified Nucleoside Analogs. Materialy Mezhdunarodnoi nauchno-prakticheskoi konferentsii «Biotekhnologii mikroorganizmov», posvyashchennoi professoru Yu. K. Fomichevu (1929–2015) [Materials of the International Scientific and Practical Conference “Biotechnology of Microorganisms” dedicated to Professor Yu. K. Fomichev (1929–2015)]. Minsk, 2019, pp. 368–370 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">Влияние производных рибавирина на катализ липолитических реакций / Н. М. Литвинко [и др.] // Молекулярные, мембранные и клеточные основы функционирования биосистем: сб. науч. тр. IX съезда Бел. общ. объед. фотобиологов и биофизиков, 23–25 июня 2010 г. – Минск, 2010. – С. 240–242.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. M., Gerlovsky D. O., Kuchuro S. V., Kalinichenko E. N., Kulak T. I., Oleinikova I. A. Effect of ribavirin derivatives on catalysis of lipolytic reactions. Molekulyarnye, membrannye i kletochnye osnovy funktsionirovaniya biosistem: sbornik nauchnykh trudov IX s’ezda Belorusskogo obshchestvennogo ob’edineniya fotobiologov i biofizikov, 23–25 iyunya 2010 g. [Molecular, membrane and cellular bases of the functioning of biosystems: collection of scientific papers of the IX Congress of the Belarusian Public Association of Photobiologists and Biophysicists, June 23–25, 2010]. Minsk, 2010, pp. 240–242 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Ремеева, Е. А. Ферментативный синтез транс-зеатин рибозида и определение его эффекторных свойств в отношении фосфолипазы А2 / Е. А. Ремеева, Ю. Н. Артемьева // Молодежь в науке – 2020: тез. докл. XVII Междунар. конф. молодых ученых. – Минск, 2020. – С. 542 – 545.</mixed-citation><mixed-citation xml:lang="en">Remeeva Е. А., Artsemyeva J. N Enzymatic synthesis of trans-zeatin riboside and determination of its effector properties in relation to phospholipase А2. Molodezh’ v nauke – 2020: tez. dokl. XVII Mezhdunar. konf. molodykh uchenykh [Youth in science: Book of abstracts, XVII Int. conf. young scientists]. Minsk, 2020, pp. 542–545 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Drenichev, M. S. Cytokinin nucleosides-natural compounds with a unique spectrum of biological activities / M. S. Drenichev, V. E. Oslovsky, S. N. Mikhailov // Current topics in medicinal chemistry. – 2016. – Vol. 16, N 23. – P. 2562– 2576. https://doi.org/10.2174/1568026616666160414123717</mixed-citation><mixed-citation xml:lang="en">Drenichev M. S., Oslovsky V. E., Mikhailov S. N. Cytokinin nucleosides-natural compounds with a unique spectrum of biological activities. Current topics in medicinal chemistry, 2016, vol. 16, no. 23, pp. 2562–2576. https://doi.org/10.2174/1568026616666160414123717</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Возможное участие цианобактерий в формировании гормональной системы растений / Г. В. Шевченко [и др.] // Физиология растений. – 2014. – Т. 96, № 3. – C. 170–176.</mixed-citation><mixed-citation xml:lang="en">Shevchenko G. V., Karavaiko N. N., Selivankina S. Y., Zubkova N. K., Kupriyanova E. V., Los D. A., Kusnetsov V. V., Kulaeva O. N. Possible involvement of cyanobacteria in the formation of plant hormonal system. Fiziologiya rastenii = Russian Journal of Plant Physiology, 2014, vol. 61, no. 2, pp. 170–176 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Натуральный trans-зеатин-рибозид 98 % Мин Цитокинин [Электронный ресурс]. – Режим доступа: https:// offer.alibaba.com/product. – Дата доступа: 08.06.2020.</mixed-citation><mixed-citation xml:lang="en">Natural trans-zeatin-riboside 98% Min Cytokinin. Available at: https://offer.alibaba.com/product. (accessed 08 June 2020) (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Изучение действия уридина на панкреатическую ФЛА2 методом дифференциальной спектроскопии / Л. А. Скоростецкая [и др.] // Молекулярные, мембранные и клеточные основы функционирования биосистем: сб. тр. XlV съезда Бел. общ. объед. фотобиологов и биофизиков. – Минск: БГУ, 2019. – С. 43.</mixed-citation><mixed-citation xml:lang="en">Skorostetskaya L. A., Gerlovsky D. O., Remeeva E. A., Artsemyeva J. N., Vasilevskaya E. D., Birichevskaya L. L., Vinter M. A., Zinchenko A. I., Mikhailopulo I. A., Litvinko N. M. Study of the action of uridine on pancreatic PLA2 by differential spectroscopy. Molekulyarnye, membrannye i kletochnye osnovy funktsionirovaniya biosistem: sb. tr. XlV s”ezda Bel. obshch. ob”ed. fotobiologov i biofizikov [Molecular, membrane and cellular bases of the functioning of biosystems: collection of articles. XIV Congress of the Belarusian Public Association of Photobiologists and Biophysicists]. Minsk, Belarusian State University, 2020, pp. 43 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Deems, R. A. Kinetic analysis of phospholipase A2 activity toward mixed micelles and its implications for the study of lipolytic enzymes / R. A. Deems, B. R. Eaton, E. A. Dennis // J. Biol. Chem. – 1975. – Vol. 250, N 23. – P. 9013–9020. https://doi.org/10.1016/S0021-9258(19)40687-X</mixed-citation><mixed-citation xml:lang="en">Deems R. A., Eaton B. R., Dennis E. A. Kinetic analysis of phospholipase A2 activity toward mixed micelles and its implications for the study of lipolytic enzymes. Journal of Biological Chemistry, 1975, vol. 250, no. 23, pp. 9013–9020. https://doi.org/10.1016/S0021-9258(19)40687-X</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Chemical Modification of the alpha–Amino Group in Snake Venom Phospholipases A2. A Comparison of the Interaction of Pancreatic and Venom Phospholipases with Lipid–Water Interfaces / H. M. Verheij [еt al.] // J. Biochemistry. – 1981. – Vol. 20, N 3. – P. 94–99. https://doi.org/10.1021/bi00504a016</mixed-citation><mixed-citation xml:lang="en">Verheij H. M., Egmond M. R., De Haas G. H. Chemical Modification of the alpha–Amino Group in Snake Venom Phospholipases A2. A Comparison of the Interaction of Pancreatic and Venom Phospholipases with Lipid–Water Interfaces. Biochemistry, 1981, vol. 20, no. 3, pp. 94–99. https://doi.org/10.1021/bi00504a016</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Литвинко, Н. М. Ингибирование фосфолипазы А2 производными виразола / Н. М. Литвинко // Докл. Нац. акад. наук Беларуси. – 2021. – Т.65, № 3. – С. 309–319. https://doi.org/10.29235/1561-8323-2021-65-3-309-319</mixed-citation><mixed-citation xml:lang="en">Litvinko N. М. Inhibition of phospholipase A2 by virazole derivatives. Doklady Natsional`noi akademii nauk belarusi = Dokladyof the National Academy of Sciences of Belarus, 2021, vol. 65, no. 3, pp. 309–319 (in Russian). https://doi.org/10.29235/1561-8323-2021-65-3-309-319</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">Литвинко, Н. М. Активность фосфолипаз А2 и С при биохимическом моделировании / Н. М. Литвинко. – Минск: Технопринт, 2003. – 350 с.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. М. Activity of phospholipases A2 and C in biochemical modeling. Minsk, Technoprint Publ., 2003. 350 p. (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Расщепление фосфатидилнуклеозидов под действием фосфолипаз / Т. И. Новожилова [и др.] // Биоорганическая химия. – 2000. –Т. 26, № 3. – С. 238–240.</mixed-citation><mixed-citation xml:lang="en">Novozhilova T. I., Malkin S. I., Kozhukhov V. I., Kruglyak Yu. L., Kurochkin V. K. Decomposition of phosphatidylnucleosides under the action of phospholipases. Bioorganicheskaya khimiya = Russian Journal of Bioorganic Chemistry, 2000, vol. 26, no. 3, pp. 238–240 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Cинтез конъюгатов фосфатидовой кислоты с модифицированными компонентами нуклеиновых кислот и их чувствительность к действию фосфолипазы А2 / Е. В. Жерносек [и др.] // Химические реактивы, реагенты и процессы малотоннажной химии: XVIII Междунар. науч.-технич. конф. – Минск, 2005. – С. 33.</mixed-citation><mixed-citation xml:lang="en">ZhernosekЕ. V., Kalinichenko E. N., Litvinko N. М., Kuchuro S. V., Rakhuba G. N. Synthesis of conjugates of phosphatidic acid with modified components of nucleic acids and their sensitivity to the action of phospholipase A2. Khimicheskie reaktivy, reagenty i protsessy malotonnazhnoi khimii: XVIII Mezhdunar. nauch.-tekhnich. konf. [Chemical reagents, reagents and low-tonnage chemistry processes; XVIII Int. scientific and technical conf.]. Minsk, 2005, pp. 33 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Синтез 2’,3’-дидезоксицитидин-5’-монофосфат-фосфатидилэтаноламина – фосфорамидата и его взаимодействие с фосфолипазой А2 / Е. Н. Калиниченко [и др.] // Химия и биологическая активность азотсодержащих гетероциклов: сб. тр. 3-й междунар. конф. – Черноголовка, 2006. – C.</mixed-citation><mixed-citation xml:lang="en">Kalinichenko E. N., Zhernosek Е. V., Litvinko N. М., Kuchuro S. V., Rakhuba G. N. Synthesis of 2’, 3’-dideoxycytidine-5’-monophosphate-phosphatidylethanolamine – phosphoramidate and its interaction with phospholipase A2. Khimiya i biologicheskaya aktivnost’ azotsoderzhashchikh geterotsiklov: sb. tr. 3-i mezhdunar. konf. [Chemistry and Biological Activity of Nitrogen-Containing Heterocycles: 3rd Intern. conf.]. Chernogolovka, 2006 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Лекарственные формы новых поколений и их устойчивость / Н. М. Литвинко [и др.] // Сахаровские чтения 2006 г.: экологические проблемы ХХI века; сб. тр. 6-й междунар. науч. конф. – Минск, 2006. – C.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. М., Kuchuro S. V., Rakhuba G. N., Kalinichenko E. N., Zhernosek Е. V. Pharmaceutical drug forms of new generations and their sustainability. Sakharovskie chteniya 2006 g.: ekologicheskie problemy KhKhI veka: sb. tr. 6-i mezhdunar. nauch. konf. [Sakharov Readings 2006: Environmental Problems of the XXI Century: 6th Int. scientific. conf.]. Minsk, 2006 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Влияние модификации этаноламинового фрагмента субстрата на активность панкреатической фосфолипазы А2 / Н. М. Литвинко [и др.] // Вес. Нац. акад. нвук Беларусi. Сер. хім. навук. – 2006. – № 3. – С. 79–82.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. М., Kuchuro S. V., Rakhuba G. N., Kalinichenko Е. N., Zhernosek Е. V. Effect of modification of the ethanolamine fragment of the substrate on the activity of pancreatic phospholipase А2. Vestsi Natsyyanal’nai akademii navuk Belarusi. Seryya khimichnykh navuk = Proceedings of the National Academy of Sciences of Belarus. Chemical series, 2006, no. 3, pp. 79–82 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Модифицированный 2’,3’-дидезоксиуридином фосфолипид, фармацевтическая композиция и противоядие к действию яда кобры: пат. BY 11904 / Н. М. Литвинко, Е. Н. Калиниченко, Е. В. Жерносек, С. В. Кучуро. – Опубл. 30.06.2009.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. М., Kalinichenko Е. N., Zhernosek Е. V., Kuchuro S. V. Phospholipid modified by 2 ‘, 3’-dideoxyuridine, pharmaceutical composition and antidote to the action of cobra venom. Patent BY, no. 11904, 2009 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Конъюгат фосфолипида с модифицированным нуклеозидом, фармацевтическая композиция и средство, повышающее устойчивость к действию панкреатической фосфолипазы А2: пат. BY 11905 / Н. М. Литвинко, Е. Н. Калиниченко, Е. В. Жерносек, С. В. Кучуро. – Опубл. 30.06.2009.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. М., Kalinichenko Е. N., Zhernosek Е. V., Kuchuro S. V. Conjugate of a phospholipid with a modified nucleoside, a pharmaceutical composition and an agent that increases resistance to the action of pancreatic phospholipase А2. Patent BY, no. 11905, 2009 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Устойчивость диацилглицерофосфатных производных нуклеозидов по отношению к панкреатической ФЛА2 / Д. О. Герловский [и др.] // Белорусские лекарства: материалы конф. – Минск, 2019. – С. 38–41.</mixed-citation><mixed-citation xml:lang="en">Gerlovsky D. О., Remeeva Е. А., Artsemyeva J. N., Vasilevskaya E. D., Birichevskaya L. L., Vinter М. А., Zinchenko A. I., Mikhailopulo I. А., Litvinko N. М. Stability of diacylglycerophosphate derivatives of nucleosides in relation to pancreatic PLA2. Belorusskie lekarstva: materialy konf. [Belarusian medicines: conference materials]. Minsk, 2019, pp. 38–41 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit73"><label>73</label><citation-alternatives><mixed-citation xml:lang="ru">Активность фосфолипазы А2 по отношению к фосфолипидным коньюгатам / Е. А. Ремеева [и др.] // Молодежь в науке – 2019: тез. докл. XVI Междунар. конф. молодых ученых, г. Минск, 14-17 октября 2019 г. – Минск: НАН Беларуси. – 2019. – С. 556–558.</mixed-citation><mixed-citation xml:lang="en">Remeeva Е. А., Artsemyeva J. N., Vasilevskaya E. D., Vinter М. А. Phospholipase A2 activity towards phospholipid conjugates. Molodezh’ v nauke – 2019: tez. dokl. XVI Mezhdunar. konf. molodykh uchenykh, g. Minsk, 14–17 oktyabrya 2019 g. [Youth in Science - 2019: Abstracts of the XVI International Conference of Young Scientists, Minsk, October 14–17, 2019]. Minsk, NAS of Belarus, 2019, pp. 556–558 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit74"><label>74</label><citation-alternatives><mixed-citation xml:lang="ru">The enzymatic synthesis of Phospholipide-Nucleoside conjugates and study of their substrate activity for the digestive phospholipase A2 / N. M. Litvinko [еt al.] // Journal of Nanotechnoligy: Nanomedicine &amp; Nanobiotechnology. – 2020. – Vol. 7. – P. 55–56.</mixed-citation><mixed-citation xml:lang="en">Litvinko N. M., Remeeva E. A., Artsemyeva J. N., Zinchenko A. I., Gerlovsky D. O., Birichevskaya L. L., Pavluchenko N. I., Mikhailopulo I. A. The enzymatic synthesis of Phospholipide-Nucleoside conjugates and study of their substrate activity for the digestive phospholipase A2. Journal of Nanotechnoligy: Nanomedicine &amp; Nanobiotechnology, 2020, vol. 7, pp. 55–56.</mixed-citation></citation-alternatives></ref><ref id="cit75"><label>75</label><citation-alternatives><mixed-citation xml:lang="ru">Гидролиз фосфатидилбривудина под действием панкреатической ФЛА2 / Д. О. Герловский [и др.] // Молекулярные, мембранные и клеточные основы функционирования биосистем : тез. докл. междунар. науч. конф., Четырнадцатого съезда Белорус. обществ. об-ния фотобиологов и биофизиков, Беларусь, Минск, 17–19 июня 2020 г. – Минск: БГУ, 2019. – С. 207.</mixed-citation><mixed-citation xml:lang="en">Gerlovsky D. О., Remeeva Е. А., Artsemyeva J. N., Vasilevskaya E. D., Birichevskaya L. L., Vinter М. А., Zinchenko A. I., Mikhailopulo I. А., Litvinko N. М. Hydrolysis of phosphatidylbrivudine under the action of pancreatic PLA2. Molekulyarnye, membrannye i kletochnye osnovy funktsionirovaniya biosistem : tez. dokl. mezhdunar. nauch. konf., Chetyrnadtsatogo s”ezda Belorus. obshchestv. ob-niya fotobiologov i biofizikov, Belarus’, Minsk, 17–19 iyunya 2020 g. [Molecular, Membrane and Cellular Basis for the Functioning of Biosystems: abstract. report intl. scientific Conf., Fourteenth Congress Belorus. societies. Society of Photobiologists and Biophysicists, Belarus, Minsk, June 17–19, 2020]. Minsk, Belarusian State University, 2019, pp. 207 (in Russian)</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
