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Отдел биокинетики

Отдел биокинетики организован в 1965 г. выдающимся российским ученым, профессором, чл.-корр. АН СССР И.В. Березиным на основе всемирно известной российской школы химической кинетики, созданной лауреатом Нобелевской премии, акад. Н.Н. Семеновым, в качестве логического развития интереса ученых-химиков к биологическим объектам. И.В. Березин руководил отделом с 1965 по 1978 г., заведующие отделом в последующие годы – проф. С.Д. Варфоломеев (1978 - 2001 г.г.) и проф. В.К. Швядас (с 2001 г. по настоящее время).

Основные научные достижения отдела

Одно из приоритетных направлений - изучение кинетики и механизма действия ферментов семейства пенициллинацилаз. Для понимания механизма биокатализа, природы специфичности и стереоспецифичности действия, а также разработки новых подходов к биоинженерии ферментов внедрены методы молекулярного моделирования биокаталитических превращений. Исследованы кинетика и механизм реакций ферментативного ацильного переноса в водной среде, разработаны адекватные математические модели, позволяющие описать протекание реакций в широком диапазоне условий вплоть до высоких степеней превращения. Изучены реакции, протекающие как в гомогенном растворе, так и в гетерогенных системах "водный раствор-осадок", а также при минимальном содержании воды в реакционной смеси (твердофазные реакции). Изучена термодинамика реакций гидролиза-синтеза пенициллинов, цефалоспоринов, N-ацилированных аминов, аминокислот и их производных. Выявлены ключевые факторы, определяющие эффективность биокаталитического синтеза в водных средах. Исследованы неканонические превращения, катализируемые пенициллинацилазами и аминоацилазами. Развиты методы эффективного использования ферментов для получения физиологически активных соединений, а также в энантио- и региоселективном органическом синтезе. Достигнут существенный прогресс в развитии методов ферментативного синтеза пептидов, содержащих D-аминокислоты, при использовании ферментов для введения и снятия защитных групп в пептидном синтезе, в химикоэнзиматическом получении стереоизомерно чистых дикетопиперазинов. Созданы научные основы биокаталитических технологий синтеза новых бета-лактамных антибиотиков и получения индивидуальных энантиомеров аминосоединений. Проведены исследования механизма действия сульфатированных липидов на синтез лейкотриенов в нейтрофилах и на лейкоцит-эндотелиальные взаимодействия. Обнаружено, что сульфатированные галактоцереброзиды и сульфатированный холестерин (неопубликованные данные) являются агентами, вызывающими прикрепление нейтрофилов к коллагену и эндотелию. Исследована роль цитоскелета и динамики внутриклеточного кальция в нейтрофилах при действии на клетку сульфатированных галактоцереброзидов. Показано, что сульфатированный холестерин является агентом, вызывающим прикрепление нейтрофилов к эндотелиальным клеткам, активацию продукции супероксида в клетках, а также влияет на синтез лейкотриенов в нейтрофилах и при взаимодействии нейтрофилов с эндотелием и белками экстраклеточного матрикса. Предполагается, что сульфатированные липиды являются активными эндогенными регуляторами клеточного синтеза лейкотриенов, и что важным звеном такой регуляции является клеточная адгезия. Изучен синтез простагландинов и циклопентеноновых простагландинов, выброс арахидоновой и докозагексаеновой кислот при стимуляции астроцитов (глиальные клетки мозга) провоспалительными веществами (интерлейкин 1, фактор некроза опухоли альфа, тромбин, АТР, липополисахарид). Показано, что в регуляции синтеза простаноидов на астроцитах ключевая роль принадлежит докозагексаеновой кислоте, которая предотвращает синтез простаноидов даже на фоне значительной индукции простагландин Н синтазы. Впервые показано, что кальций независимая форма фосфолипазы А2, которая высвобождает докозагексаеновую кислоту из фосфолипидов мембран астроцитов, участвует в развитии воспалительных ответов клеток. Этот фермент предложено использовать для целевого поиска новых подходов к терапии воспалительных процессов в центральной нервной системе. Показано также, что циклопентеноновые простагландины группы А2 и группы Ж2 (15d-PGJ2) эффективно блокируют пролиферацию нормальных и трансформированных астроцитов, что может быть использовано при лечении астроцитозов, сопровождающих воспалительные процессы, и, возможно, ряда опухолевых заболеваний мозга. Проводятся исследования по выяснению механизма действия циклопентеноновых простагландинов и причин их различия во влиянии на первичные и трансформированные клетки. Научные достижения отдела отмечены: Ленинской премией 1982 г. (И.В. Березин, К. Мартинек), Государственными премиями 1984 г. (В.К. Швядас), 1984 г. (С.Д. Варфоломеев, А.А. Клесов), Премиями Ленинского Комсомола 1986 г. (П.В. Вржещ), 1988 г. (И.Н. Курочкин, Н.В. Породенко, М.Г. Сергеева), Премией Европейской академии для молодых ученых 2002 г. (М.И. Юшко).

Историческая справка

Основные результаты за сорок лет работы отдела достигнуты в изучении физико-химических основ биокатализа, специфичности, стереоспецифичности и хемоселективности ферментативных реакций, создании методов стабилизации и превращения ферментов в технологичные катализаторы, разработке научных основ инженерной энзимологии, создании и внедрении в медицинскую промышленность первых в стране промышленных процессов на основе иммобилизованных ферментов, разработке научных основ конверсии энергии биокаталитическими системами, открытии явления биоэлектрокатализа (открытие № 311 «Свойство ферментов участвовать в переносе электронов - биоэлектрокатализ»), исследовании биосинтеза и регуляторной роли простагландинов и лейкотриенов в животных клетках. Результаты исследований, выполненных в отделе биокинетики, вошли в циклы работ, отмеченых Ленинской премией в 1982 г. (И.В. Березин, К. Мартинек), двумя Государственными премиями СССР в 1984 г. (С.Д. Варфоломеев, А.А. Клесов и В.К. Швядас), а также рядом премий для молодых ученых. Создана всемирно известная научная школа, воспитанники которой успешно продолжают фундаментальные и прикладные исследования в как в России (С.Д. Варфоломеев, В.К. Швядас, Г.Ф. Судьина, А.Т. Варфоломеева, П.В. Вржещ, М.Г. Сергеева, Н.Ф. Казанская, А.В. Левашов, Н.И. Ларионова, С.О. Бачурин, А.П. Синицын, С.В. Калюжный, И.Н. Курочкин, А.В. Максименко, А.А. Карякин, С.С.Кормер, Д.А.Мироненко, Э.А.Колованов и др.), так и за рубежом: США (А.М. Клибанов, А.А. Клесов, А.Л. Марголин, А.М. Блинковский, М.Ю. Гололобов, О.Л. Барский, О.К. Мирзоева, В.В. Верхуша, М.М.Вешторт, М.В.Виноградова, А.В.Чельцов), Мексике (А.К. Яцимирский, А.Д. Варфоломеева), Швеции (С.В. Зайцев, И.Ю. Галаев, А.Е.Иванов), Канаде (А.В.Пшежецкий), ФРГ (В.Кошке), Литве (А.А.Пятраускас, Р.И.Диджяпетрис, Р.А.Паулюконис) и ряде других стран. Одной из отличительных характеристик отдела биокинетики является систематическая активная работа со студентами и аспирантами, его популярность среди молодежи. За последние годы в отделе выросли талантливые молодые ученые (М.И. Юшко, Д.Т. Гуранда, Г.Г. Чилов, Т.А. Щербакова, и др.), которые наряду с успешным проведением собственных исследований плодотворно работают с новым поколением студентов, интересующихся биокинетикой и биокатализом.

Международное сотрудничество

Отдел биокинетики ведет активное международное сотрудничество с Университетами Делфта и Гронингена (Нидерланды), Лундским университетом (Швеция), Королевским техническим университетом Стокгольма (Швеция), Университетом Отто-фон-Герике, г. Магдебург и Университетом г. Констанца (ФРГ), Мичиганским университетом (США), Институтом нефтехимии и биоорганической химии Украинской академии наук (Киев), а также с научными учреждениями России: кафедрой химической энзимологии химического факультета МГУ, факультетом биоинженерии и биоинформатики МГУ, НИВЦ МГУ, Институтом генетики и селекции промышленных микроорганизмов (Москва), Институтом элементоорганических соединений РАН (Москва), Институтом физиологически активных веществ РАН (Черноголовка).

Грантовая поддержка

Исследования поддержаны рядом грантов РФФИ, в т.ч. РФФИ-ГФЕН, Федеральной целевой научно-технической программой "Новейшие методы биоинженерии", Федеральной целевой программой "Интеграция науки и высшего образования", Междисциплинарным проектом МГУ, программами "Университеты России", INTAS.

Подразделения отдела

Все сотрудники отдела

Штатные сотрудники

Все статьи
  1. Shalaeva D.N., Galperin M.Y., Mulkidjanian A.Y. (2015) Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins. Biol. Direct, 10: . >>

  2. Mkrtchyan G., Aleshin V., Parkhomenko Y., Kaehne T., Di Salvo M.L., Parroni A., Contestabile R., Vovk A., Bettendorff L., Bunik V. (2015) Molecular mechanisms of the non-coenzyme action of thiamin in brain: biochemical, structural and pathway analysis. Sci Rep, 5: . >>

  3. Shalaeva D.N., Dibrova D.V., Galperin M.Y., Mulkidjanian A.Y. (2015) Modeling of interaction between cytochrome c and the WD domains of Apaf-1: bifurcated salt bridges underlying apoptosome assembly. Biol. Direct, 10: . >>

  4. Galkina S.I., Fedorova N.V., Serebryakova M.V., Arifulin E.A., Stadnichuk V.I., Gaponova T.V., Baratova L.A., Sud'ina G.F. (2015) Inhibition of the GTPase dynamin or actin depolymerisation initiates outward plasma membrane tubulation/vesiculation (cytoneme formation) in neutrophils. Biol. Cell, 107 (5): 144-158. >>

  5. Akparov V.K., Timofeev V.I., Khaliullin I.G., Svedas V., Chestukhina G.G., Kuranova I.P. (2015) Structural insights into the broad substrate specificity of carboxypeptidase T from Thermoactinomyces vulgaris. FEBS J., 282 (7): 1214-1224. >>

  6. Diaz-Munoz M.D., Bell S.E., Fairfax K., Monzon-Casanova E., Cunningham A.F., Gonzalez-Porta M., Andrews S.R., Bunik V.I., Zarnack K., Curk T., Heggermont W.A., Heymans S., Gibson G.E., Kontoyiannis D.L., Ule J., Turner M. (2015) The RNA-binding protein HuR is essential for the B cell antibody response. Nat. Immunol., 16 (4): 415-425. >>

  7. Shcherbakova T.A., Panin N.V., Suplatov D.A., Shapovalova I.V., Svedas V.K. (2015) The beta D484N mutant of penicillin acylase from Escherichia coli is more resistant to inactivation by substrates and can effectively perform peptide synthesis in aqueous medium. J. Mol. Catal. B-Enzym., 112: 66-68. >>

  8. Grigorenko B.L., Khrenova M.G., Nilov D.K., Nemukhin A.V., Svedas V.K. (2014) Catalytic Cycle of Penicillin Acylase from Escherichia coli: QM/MM Modeling of Chemical Transformations in the Enzyme Active Site upon Penicillin G Hydrolysis. ACS Catal., 4 (8): 2521-2529. >>

  9. Quinlan C.L., Goncalves R.L.S, Hey-Mogensen M., Yadava N., Bunik V.I., Brand M.D. (2014) The 2-Oxoacid Dehydrogenase Complexes in Mitochondria Can Produce Superoxide/Hydrogen Peroxide at Much Higher Rates Than Complex I. J. Biol. Chem., 289 (12): 8312-8325. >>

  10. Bunik V.I., Tylicki A., Lukashev N.V. (2013) Thiamin diphosphate-dependent enzymes: from enzymology to metabolic regulation, drug design and disease models. FEBS J., 280 (24): 6412-6442. >>

  11. Bunik V.I. (2013) Thiamin-dependent enzymes: new perspectives from the interface between chemistry and biology. FEBS J., 280 (24): 6373-6373. >>

  12. Galkina S.I., Fedorova N.V., Stadnichuk V.I., Sud'ina G.F. (2013) Membrane tubulovesicular extensions (cytonemes) Secretory and adhesive cellular organelles. Celll Adhes. Migr., 7 (2): 174-186. >>

  13. Araujo W.L., Trofimova L., Mkrtchyan G., Steinhauser D., Krall L., Graf A., Fernie A.R., Bunik V.I. (2013) On the role of the mitochondrial 2-oxoglutarate dehydrogenase complex in amino acid metabolism. Amino Acids, 44 (2): 683-700. >>

  14. Graf A., Trofimova L., Loshinskaja A., Mkrtchyan G., Strokina A., Lovat M., Tylicky A., Strumilo S., Bettendorff L., Bunik V.I. (2013) Up-regulation of 2-oxoglutarate dehydrogenase as a stress response. Int. J. Biochem. Cell Biol., 45 (1): 175-189. >>

  15. Novikov F.N., Stroganov O.V., Khaliullin I.G., Panin N.V., Shapovalova I.V., Chilov G.G., Svedas V.K. (2013) Molecular modeling of different substrate-binding modes and their role in penicillin acylase catalysis. FEBS J., 280 (1): 115-126. >>

  16. Suplatov D.A., Besenmatter W., Svedas V.K., Svendsen A. (2012) Bioinformatic analysis of alpha/beta-hydrolase fold enzymes reveals subfamily-specific positions responsible for discrimination of amidase and lipase activities. Protein Eng. Des. Sel., 25 (11): 689-697. >>

  17. Galkina S.I., Fedorova N.V., Serebryakova M.V., Romanova J.M., Golyshev S.A., Stadnichuk V.I., Baratova L.A., Sud'ina G.F., Klein T. (2012) Proteome analysis identified human neutrophil membrane tubulovesicular extensions (cytonemes, membrane tethers) as bactericide trafficking. Biochim. Biophys. Acta-Gen. Subj., 1820 (11): 1705-1714. >>

  18. Romanova N.N., Rybalko I.I., Tallo T.G., Zyk N.V., Svedas V.K. (2012) Synthesis of Schiff bases from 3-amino-3-arylpropionic acid esters in aqueous medium. Russ. J. Organ. Chem., 48 (6): 860-863. >>

  19. Guranda D.T., Ushakov G.A., Yolkin P.G., Svedas V.K. (2012) Thermodynamics of phenylacetamides synthesis: Linear free energy relationship with the pK of amine. J. Mol. Catal. B-Enzym., 74 (1): 48-53. >>

  20. Golenkina E.A., Galkina S.I., Romanova J.M., Lazarenko M.I., Sud'ina G.F. (2011) Involvement of red blood cells in the regulation of leukotriene synthesis in polymorphonuclear leucocytes upon interaction with Salmonella Typhimurium. Apmis, 119 (9): 635-642.

  21. Parkhomenko Y.M., Kudryavtsev P.A., Pylypchuk S.Y., Chekhivska L.I., Stepanenko S.P., Sergiichuk A.A., Bunik V.I. (2011) Chronic alcoholism in rats induces a compensatory response, preserving brain thiamine diphosphate, but the brain 2-oxo acid dehydrogenases are inactivated despite unchanged coenzyme levels. Journal of Neurochemistry, 117 (6): 1055-1065.

  22. Zakharenko A.L., Sukhanova M.V., Khodyreva S.N., Novikov F.N., Stroylov V.S., Nilov D.K., Chilov G.G., Svedas V.K., Lavrik O.I. (2011) Improved procedure of the search for poly(ADP-Ribose) polymerase-1 potential inhibitors with the use of the molecular docking approach. Molecular Biology, 45 (3): 517-521.

  23. Nilov D.K., Shabalin I.G., Popov V.O., Svedas V.K. (2011) Investigation of Formate Transport through the Substrate Channel of Formate Dehydrogenase by Steered Molecular Dynamics Simulations. Biochemistry-Moscow, 76 (2): 172-174.

  24. Bunik V.I. (2011) Metabolic Networking through Enzymatic Sensing, Signaling and Response to Homeostatic Fluctuations. Cellular Networks - Positioning, Performance Analysis, Reliability, Agassi Melikov (Ed.), : 377-405. >>

  25. Bunik V.I., Schloss J.V., Pinto J.T., Dudareva N., Cooper A.J. (2011) A survey of oxidative paracatalytic reactions catalyzed by enzymes that generate carbanionic intermediates: implications for ROS production, cancer etiology, and neurodegenerative diseases. Adv Enzymol Relat Areas Mol Biol, 77: 307-60.

  26. Tylicki A., Bunik V.I., Strumiеlo S. (2011) 2-Oxoglutarate dehydrogenase complex and its multipoint control. Postepy Biochem, 57 (3): 304-13.

  27. Chernorizov K.A., Elkina J.L., Semenyuk P.I., Svedas V.K., Muronetz V.I. (2010) Novel Inhibitors of Glyceraldehyde-3-phosphate Dehydrogenase: Covalent Modification of NAD-Binding Site by Aromatic Thiols. Biochemistry-Moscow, 75 (12): 1444-1449.

  28. Sokolov A.V., Golenkina E.A., Kostevich V.A., Vasilyev V.B., Sud'ina G.F. (2010) Interaction of Ceruloplasmin and 5-Lipoxygenase. Biochemistry-Moscow, 75 (12): 1464-1469.

  29. Trofimova L., Lovat M., Groznaya A., Efimova E., Dunaeva T., Maslova M., Graf A., Bunik V. (2010) Behavioral impact of the regulation of the brain 2-oxoglutarate dehydrogenase complex by synthetic phosphonate analog of 2-oxoglutarate: implications into the role of the complex in neurodegenerative diseases. Int J Alzheimers Dis, 2010: 749061.

  30. Zagryazhskaya A.N., Lindner S.C., Grishina Z.V., Galkina S.I., Steinhilber D., Sud'ina G.F. (2010) Nitric oxide mediates distinct effects of various LPS chemotypes on phagocytosis and leukotriene synthesis in human neutrophils. Cell Biology, 42 (6): 921-931.

  31. Van Der Merwe M.J., Osorio S., Arajo W.L., Balbo I., Nunes-Nesi A., Maximova E., Carrari F., Bunik V.I., Persson S., Fernie A.R. (2010) Tricarboxylic acid cycle activity regulates tomato root growth via effects on secondary cell wall production. Plant Physiol, 153 (2): 611-21.

  32. Gardossi L., Poulsen P.B., Ballesteros A., Hult K., Svedas V.K., Vasic-racki D., Carrea G., Magnusson A., Schmid A., Wohlgemuth R., Halling P.J. (2010) Guidelines for reporting of biocatalytic reactions. Trends in Biotechnology, 28 (4): 171-180.

  33. Graf A., Kabysheva M., Klimuk E., Trofimova L., Dunaeva T., Zundorf G., Kahlert S., Reiser G., Storozhevykh T., Pinelis V., Sokolova N., Bunik V. (2009) Role of 2-oxoglutarate dehydrogenase in brain pathologies involving glutamate neurotoxicity. Journal of Molecular Catalysis B-Enzymatic, 61 (1): 80-87.

  34. Bunik V.I., Fernie A.R. (2009) Metabolic control exerted by the 2-oxoglutarate dehydrogenase reaction: a cross-kingdom comparison of the crossroad between energy production and nitrogen assimilation. Biochemical Journal, 422: 405-421.

  35. Bunik V.I., Strumilo S. (2009) Regulation of Catalysis Within Cellular Network: Metabolic and Signaling Implications of the 2-Oxoglutarate Oxidative Decarboxylation. Current Chemical Biology, 3 (3): 279-290. >>

  36. Galkina S.I., Romanova J.M., Stadnichuk V.I., Molotkovsky J.G., Sud'ina G.F., Klein T. (2009) Nitric oxide-induced membrane tubulovesicular extensions (cytonemes) of human neutrophils catch and hold Salmonella enterica serovar Typhimurium at a distance from the cell surface. Fems Immunology and Medical Microbiology, 56 (2): 162-171.

  37. Kabysheva M.S., Storozhevykh T.P., Pinelis V.G., Bunik V.I. (2009) Synthetic regulators of the 2-oxoglutarate oxidative decarboxylation alleviate the glutamate excitotoxicity in cerebellar granule neurons. Biochemical Pharmacology, 77 (9): 1531-1540.

  38. Pchelintsev N.A., Youshko M.I., Svedas V.K. (2009) Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase. Journal of Molecular Catalysis B-Enzymatic, 56 (4): 202-207.

  39. Zundorf G., Kahlert S., Bunik V.I., Reiser G. (2009) Alpha-Ketoglutarate Dehydrogenase Contributes to Production of Reactive Oxygen Species in Glutamate-Stimulated Hippocampal Neurons in Situ. Neuroscience, 158 (2): 610-616.

  40. Bunik V.I., Kabysheva M.S., Klimuk E.I., Storozhevykh T.P., Pinelis V.G. (2009) Phosphono Analogues of 2-Oxoglutarate Protect Cerebellar Granule Neurons upon Glutamate Excitotoxicity. Natural Compounds and Their Role in Apoptotic Cell Signaling Pathways, 1171: 521-529.

  41. Arajo W.L., Nunes-Nesi A., Trenkamp S., Bunik V.I., Fernie A.R. (2008) Inhibition of 2-oxoglutarate dehydrogenase in potato tuber suggests the enzyme is limiting for respiration and confirms its importance in nitrogen assimilation. Plant Physiol, 148 (4): 1782-96.

  42. Bunik V., Kaehne T., Degtyarev D., Shcherbakova T., Reiser G. (2008) Novel isoenzyme of 2-oxoglutarate dehydrogenase is identified in brain, but not in heart. FEBS Journal, 275 (20): 4990-5006.

  43. Zagryagskaya A.N., Aleksandrov D.A., Pushkareva M.A., Galkina S.I., Grishina Z.V., Sud'ina G.F. (2008) Biosynthesis of leukotriene B4 in human polymorphonuclear leukocytes: regulation by cholesterol and other lipids. Journal of Immunotoxicology, 5 (4): 347-352.

  44. Trofimova L.K., Graf A.V., Klimuk E.I., Kabysheva M.S., Sokolova N.A., Bunik V.I. (2008) Phosphonate analogue of ketoglutarate increases activity of ketoglutarate dehydrogenasecomplex in situ and in vivo. European Neuropsychopharmacology, 18: S254-S255.

  45. Bunik V.I., Degtyarev D. (2008) Structure-function relationships in the 2-oxo acid dehydrogenase family: Substrate-specific signatures and functional predictions for the 2-oxoglutarate dehydrogenase-like proteins. Proteins-Structure Function and Bioinformatics, 71 (2): 874-890.

  46. Grinberg V.Y., Burova T.V., Grinberg N.V., Shcherbakova T.A., Guranda D.T., Chilov G.G., Svedas V.K. (2008) Thermodynamic and kinetic stability of penicillin acylase from Escherichia coli. Biochimica et Biophysica Acta-Proteins and Proteomics, 1784 (5): 736-746.

  47. Chernobrovkin M.G., Shapovalova E.N., Guranda D.T., Kudryavtsev P.A., Svedas V.K., Shpigun O.A. (2007) Chiral high-performance liquid chromatography analysis of alpha-amino acid mixtures using a novel SH reagent-N-R-mandelyl-L-cysteine and traditional enantiomeric thiols for precolumn derivatization. Journal of Chromatography A, 1175 (1): 89-95.

  48. Chilov G.G., Sidorova A.V., Svedas V.K. (2007) Quantum chemical studies of the catalytic mechanism of N-terminal nucleophile hydrolase. Biochemistry-Moscow, 72 (5): 495-500.

  49. Bunik V.I., Schloss J.V., Pinto J.T., Gibson G.E., Cooper A.J.L. (2007) Enzyme-catalyzed side reactions with molecular oxygen may contribute to cell signaling and neurodegenerative diseases. Neurochemical Research, 32 (4): 871-891.

  50. Galkina S.I., Sud'ina G.F., Klein T. (2006) Metabolic regulation of neutrophil spreading, membrane tubulovesicular extensions (cytonemes) formation and intracellular pH upon adhesion to fibronectin. Experimental Cell Research, 312 (13): 2568-2579.

  51. Bunik V.I., Raddatz G., Wanders R.J.A., Reiser G. (2006) Brain pyruvate and 2-oxoglutarate dehydrogenase complexes are mitochondrial targets of the CoA ester of the Refsum disease marker phytanic acid. FEBS Letters, 580 (14): 3551-3557.

  52. Pchelintsev N.A., Youshko M.I., Svedas V.K. (2006) A new method for spectrophotometric assay of activity of cross-linked penicillin acylase aggregates. Biochemistry-Moscow, 71 (3): 315-319.

  53. Santos S.S., Gibson G.E., Cooper A.J.L., Denton T.T., Thompson C.M., Bunik V.I., Alves P.M., Sonnewald U. (2006) Inhibitors of the alpha-ketoglutarate dehydrogenase complex alter [1-C-13] glucose and [U-C-13] glutamate metabolism in cerebellar granule neurons. Journal of Neuroscience Research, 83 (3): 450-458.

  54. Aleksandrov D.A., Zagryagskaya A.N., Pushkareva M.A., Bachschmid M., Peters-golden M., Werz O., Steinhilber D., Sud'ina G.F. (2006) Cholesterol and its anionic derivatives inhibit 5-lipoxygenase activation in polymorphonuclear leukocytes and MonoMac6 cells. FEBS Journal, 273 (3): 548-557.

  55. Guranda D.T., Kudryavtsev P.A., Khimiuk A.Y., Svedas V.K. (2005) Efficient enantiomeric analysis of primary amines and amino alcohols by high-performance liquid chromatography with precolumn derivatization using novel chiral SH-reagent N-(R)-mandelyl-(S)-cysteine. Journal of Chromatography A, 1095 (1): 89-93.

  56. Pertsovich S.I., Guranda D.T., Podchernyaev D.A., Yanenko A.S., Svedas V.K. (2005) Aliphatic amidase from Rhodococcus rhodochrous M8 is related to the nitrilase/cyanide hydratase family. Biochemistry-Moscow, 70 (11): 1280-1287.

  57. Bunik V.I., Denton T.T., xu H., Thompson C.M., Cooper A.J.L., Gibson G.E. (2005) Phosphonate analogues of alpha-ketoglutarate inhibit the activity of the alpha-ketoglutarate dehydrogenase complex isolated from brain and in cultured cells. Biochemistry, 44 (31): 10552-10561.

  58. Galkina S.I., Molotkovsky J.G., Ullrich V., Sud'ina G.F. (2005) Scanning electron microscopy study of neutrophil membrane tubulovesicular extensions (cytonemes) and their role in anchoring, aggregation and phagocytosis. The effect of nitric oxide. Experimental Cell Research, 304 (2): 620-629.

  59. Demina O.V., Varfolomeev S.D., Lukin A.Y., Laptev A.V., Shvets V.I., Khodonov A.A., Khitrina L.V., Gromov S.P., Vedernikov A.I., Barachevsky V.A., Strokach Y.P., Alfimov M.V., Lugtenburg J. (2005) Investigation of the spectral properties of the crowned retinals and bacteriorhodopsin analogs. Molecular Crystals and Liquid Crystals, 431: 509-514.

  60. Gibson G.E., Blass J.P., Beal M.F., Bunik V. (2005) The alpha-ketoglutarate-dehydrogenase complex - A mediator between mitochondria and oxidative stress in neurodegeneration. Molecular Neurobiology, 31 (1): 43-63.

  61. Guranda D.T., Volovik T.S., Svedas V.K. (2004) pH stability of penicillin acylase from Escherichia coli. Biochemistry-Moscow, 69 (12): 1386-1390.

  62. Shcherbakova T.A., Korennykh A.V., Van Langen L.M., Sheldon R.A., Svedas V.K. (2004) Use of high acyl donor concentrations leads to penicillin acylase inactivation in the course of peptide synthesis. Journal of Molecular Catalysis B-Enzymatic, 31 (1): 63-65.

  63. Guranda D.T., Khimiuk A.I., Van Langen L.M., Van Rantwijk F., Sheldon R.A., Svedas V.K. (2004) An 'easy-on, easy-off' protecting group for the enzymatic resolution of (+/-)-1-phenylethylamine in an aqueous medium. Tetrahedron-Asymmetry, 15 (18): 2901-2906.

  64. Galkina S.I., Dormeneva E.V., Bachschmid M., Pushkareva M.A., Sud'ina G.F., Ullrich V. (2004) Endothelium-leukocyte interactions under the influence of the superoxide-nitrogen monoxide system. Medical Science Monitor, 10 (9): BR307-BR316.

  65. Guranda D.T., Shapovalova I.V., Svedas V.K. (2004) A new N-acyl derivative of (S)-cysteine for quantitative determination of enantiomers of amino compounds by HPLC with a precolumn modification with o-phthalaldehyde. Russian Journal of Bioorganic Chemistry, 30 (5): 403-408.

  66. Youshko M.I., Van Langen L.M., Sheldon R.A., Svedas V.K. (2004) Application of aminoacylase I to the enantioselective resolution of alpha-amino acid esters and amides. Tetrahedron-Asymmetry, 15 (12): 1933-1936.

  67. Youshko M.I., Moody H.M., Bukhanov A.L., Boosten W.H.J., Svedas V.K. (2004) Penicillin acylase-catalyzed synthesis of beta-lactam antibiotics in highly condensed aqueous systems: Beneficial impact of kinetic substrate supersaturation. Biotechnology and Bioengineering, 85 (3): 323-329.

  68. Khimiuk A.Y., Korennykh A.V., Van Langen L.M., Van Rantwijk F., Sheldon R.A., Svedas V.K. (2003) Penicillin acylase-catalyzed peptide synthesis in aqueous medium: a chemo-enzymatic route to stereoisomerically pure diketopiperazines. Tetrahedron-Asymmetry, 14 (20): 3123-3128.

  69. Chilov G.G., Moody H.M., Boesten W.H.J., Svedas V.K. (2003) Resolution of (RS)-phenylglycinonitrile by penicillin acylase-catalyzed acylation in aqueous medium. Tetrahedron-Asymmetry, 14 (17): 2613-2617.

  70. Stroganov O.V., Chilov G.G., Svedas V.K. (2003) Force field parametrization for 6-aminopenicillanic acid. Journal of Molecular Structure-Theochem, 631: 117-125.

  71. Bunik V.I. (2003) 2-oxo acid dehydrogenase complexes in redox regulation - Role of the lipoate residues and thioredoxin. European Journal of Biochemistry, 270 (6): 1036-1042.

  72. Youshko M.I., Bukhanov A.L., Svedas V.K. (2003) Study of nucleophile binding in the penicillin acylase active center. Kinetic analysis. Biochemistry-Moscow, 68 (3): 334-338.

  73. Turutin D.V., Kubareva E.A., Pushkareva M.A., Ullrich V., Sud'ina G.F. (2003) Activation of NF-kappa B transcription factor in human neutrophils by sulphatides and L-selectin cross-linking. FEBS Letters, 536 (1): 241-245.

  74. Bunik V.I., Sievers C. (2002) Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species. European Journal of Biochemistry, 269 (20): 5004-5015.

  75. Youshko M.I., Chilov G.G., Shcherbakova T.A., Svedas V.K. (2002) Quantitative characterization of the nucleophile reactivity in penicillin acylase-catalyzed acyl transfer reactions. Biochimica et Biophysica Acta-Proteins and Proteomics, 1599 (1): 134-140.

  76. Youshko M.I., Svedas V.K. (2002) Penicillin acylase-catalyzed solid-state ampicillin synthesis. Catalysis, 344 (8): 894-898.

  77. Van Langen L.M., Janssen M.H.A., Oosthoek N.H.P., Pereira S.R.M., Svedas V.K., Van Rantwijk F., Sheldon R.A. (2002) Active site titration as a tool for the evaluation of immobilization procedures of penicillin acylase. Biotechnology and Bioengineering, 79 (2): 224-228.

  78. Youshko M.I., Van Langen L.M., de Vroom E., Van Rantwijk F., Sheldon R.A., Svedas V.K. (2002) Penicillin acylase-catalyzed ampicillin synthesis using a pH gradient: A new approach to optimization. Biotechnology and Bioengineering, 78 (5): 589-593.

  79. Chilov G.G., Svedas V.K. (2002) Enzymatic hydrolysis of beta-lactam antibiotics at low pH in a two-phase "aqueous solution water-immiscible organic solvent" system. Canadian Journal of Chemistry-Revue Canadienne de Chimie, 80 (6): 699-707.

  80. Sud'ina G.F., Brock T.G., Pushkareva M.A., Galkina S.I., Turutin D.V., Peters-golden M., Ullrich V. (2001) Sulphatides trigger polymorphonuclear granulocyte spreading on collagen-coated surfaces and inhibit subsequent activation of 5-lipoxygenase. Biochemical Journal, 359: 621-629.

  81. Guranda D.T., Van Langen L.M., Van Rantwijk F., Sheldon R.A., Svedas V.K. (2001) Highly efficient and enantioselective enzymatic acylation of amines in aqueous medium. Tetrahedron-Asymmetry, 12 (11): 1645-1650.

  82. Galkina S.I., Sud'ina G.F., Ullrich V. (2001) Inhibition of neutrophil spreading during adhesion to fibronectin reveals formation of long tubulovesicular cell extensions (cytonemes). Experimental Cell Research, 266 (2): 222-228.

  83. Youshko M.I., Van Langen L.M., de Vroom E., Van Rantwijk F., Sheldon R.A., Svedas V.K. (2001) Highly efficient synthesis of ampicillin in an "aqueous solution-precipitate" system: Repetitive addition of substrates in a semicontinuous process. Biotechnology and Bioengineering, 73 (5): 426-430.

  84. Youshko M.I., Svedas V.K. (2000) Kinetics of ampicillin synthesis catalyzed by penicillin acylase from E-coli in homogeneous and heterogeneous systems. Quantitative characterization of nucleophile reactivity and mathematical modeling of the process. Biochemistry-Moscow, 65 (12): 1367-1375.

  85. Van Langen L.M., Oosthoek N.H.P., Guranda D.T., Van Rantwijk F., Svedas V.K., Sheldon R.A. (2000) Penicillin acylase-catalyzed resolution of amines in aqueous organic solvents. Tetrahedron-Asymmetry, 11 (22): 4593-4600.

  86. Youshko M.I., Van Langen L.M., de Vroom E., Moody H.M., Van Rantwijk F., Sheldon R.A., Svedas V.K. (2000) Penicillin acylase-catalyzed synthesis of ampicillin in "aqueous solution-precipitate" systems. High substrate concentration and supersaturation effect. Journal of Molecular Catalysis B-Enzymatic, 10 (5): 509-515.

  87. Raddatz G., Kruft V., Bunik V. (2000) Structural determinants for the efficient and specific interaction of thioredoxin with 2-oxoacid dehydrogenase complexes. Applied Biochemistry and Biotechnology, 88 (1): 77-96.

  88. Bunik V., Westphal A.H., de Kok A. (2000) Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii - Evidence for the formation of a precatalytic complex with 2-oxoglutarate. European Journal of Biochemistry, 267 (12): 3583-3591.

  89. Shamolina T.A., Svedas V.K. (2000) Reactivation of heterodimer and individual subunits of penicillin acylase from E-coli after inactivation in urea. Biochemistry-Moscow, 65 (6): 672-676.

  90. Van Langen L.M., Van Rantwijk F., Svedas V.K., Sheldon R.A. (2000) Penicillin acylase-catalyzed peptide synthesis: a chemo-enzymatic route to stereoisomers of 3,6-diphenylpiperazine-2,5-dione. Tetrahedron-Asymmetry, 11 (5): 1077-1083.

  91. Bunik V. (2000) Increased catalytic performance of the 2-oxoacid dehydrogenase complexes in the presence of thioredoxin, a thiol-disulfide oxidoreductase. Journal of Molecular Catalysis B-Enzymatic, 8 (4): 165-174.

  92. Sud'ina G.F., Pushkareva M.A., Galkina S.I., Surkov S.A., Mehl M., Ullrich V. (1999) Effects of suramin on PMN interactions with different surfaces. Bioscience Reports, 19 (6): 547-558.

  93. Shamolina T.A., Drachev V.A., Svedas V.K. (1999) Activity of penicillin acylase from E-coli in the reversed-micelle system AOT-H2O-octane. Biochemistry-Moscow, 64 (10): 1186-1195.

  94. Youshko M.I., Sinev A.V., Svedas V.K. (1999) Stability and catalytic properties of penicillin acylase in systems with low water content. Biochemistry-Moscow, 64 (10): 1196-1199.

  95. Bunik V., Raddatz G., Lemaire S., Meyer Y., Jacquot J.P., Bisswanger H. (1999) Interaction of thioredoxins with target proteins: Role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes. Protein Science, 8 (1): 65-74.

  96. Mccartney R.G., Rice J.E., Sanderson S.J., Bunik V., Lindsay H., Lindsay J.G. (1998) Subunit interactions in the mammalian alpha-ketoglutarate dehydrogenase complex - Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamide dehydrogenase components. Journal of Biological Chemistry, 273 (37): 24158-24164.

  97. Youshko M.I., Shamolina T.A., Guranda D.F., Synev A.V., Svedas V.K. (1998) Specific substrates for spectrophotometric determination of penicillin acylase activity. Biochemistry-Moscow, 63 (9): 1104-1109.

  98. Soloshonok V.A., Soloshonok I.V., Kukhar V.P., Svedas V.K. (1998) Biomimetic transamination of alpha-alkyl beta-keto carboxylic esters. Chemoenzymatic approach to the stereochemically defined alpha-alkyl beta-fluoroalkyl beta-amino acids. Journal of Organic Chemistry, 63 (6): 1878-1884.

  99. Ilyina A.D., Zaitsev S.V., Grishina I.A., Varfolomeev S.D. (1998) Kinetics of homeostatic behavior of receptor-enzyme systems under the action of physiologically active compounds. Biosystems, 45 (1): 77-85.

  100. Sud'ina G.F., Galkina S.I., Margolis L.B., Ullrich V. (1998) Dependence of neutrophil activation on cell density and adhesion. Cell Adhesion and Communication, 5 (1): 27-37.

  101. Svedas V.K., Beltser A.I. (1998) Totally enzymatic synthesis of peptides - Penicillin acylase-catalyzed protection and deprotection of amino groups as important building blocks of this strategy. Enzyme Engineering Xiv, 864: 524-527.

  102. Ilyina A.D., Zaitsev S.V., Grishina I.A., Varfolomeev S.D. (1998) Kinetics of homeostatic behavior of receptor-enzyme systems under the action of physiologically active compounds. Biosystems, 45 (1): 77-85.

  103. Gurentsova O.I., Savchenko M.V., Sumbatyan N.V., Korshunova G.A., Svedas V.K. (1997) Detection of enantiomers of nucleoamino acids by HPLC with premodification with o-phthalic aldehyde. Bioorganicheskaya Khimiya, 23 (11): 877-881.

  104. Bunik V., Follmann H., Bisswanger H. (1997) Activation of mitochondrial 2-oxoacid dehydrogenases by thioredoxin. Biological Chemistry, 378 (10): 1125-1130.

  105. Bunik V.I., Pavlova O.G. (1997) Inhibition of pigeon breast muscle alpha-ketoglutarate dehydrogenase by structural analogs of alpha-ketoglutarate. Biochemistry-Moscow, 62 (9): 1012-1020.

  106. Bunik V.I., Pavlova O.G. (1997) Inactivation of alpha-ketoglutarate dehydrogenase during its enzymatic reaction. Biochemistry-Moscow, 62 (9): 973-982.

  107. Bunik V., Shoubnikova A., Bisswanger H., Follmann H. (1997) Characterization of thioredoxins by sodium dodecyl sulfate-slab gel electrophoresis and high performance capillary electrophoresis. Electrophoresis, 18 (5): 762-766.

  108. Raddatz G., Bunik V.I., Scior T., Bisswanger H. (1997) Homology modelling of a newly discovered thioredoxin protein and analysis of the force field and electrostatic properties. Journal of Molecular Modeling, 3 (8): 359-363.

  109. Elsliger M.A., Pshezhetsky A.V., Vinogradova M.V., Svedas V.K., Potier M. (1996) Comparative modeling of substrate binding in the S-1' subsite of serine carboxypeptidases from yeast, wheat, and human. Biochemistry, 35 (47): 14899-14909.

  110. Svedas V.K., Savchenko M.V., Beltser A.I., Guranda D.F. (1996) Enantioselective penicillin acylase-catalyzed reactions - Factors governing substrate and stereospecificity of the enzyme. Enzyme Engineering Xiii, 799: 659-669.

  111. Mirzoeva O.K., Sudina G.F., Pushkareva M.A., Varfolomeev S.D. (1995) Competitive inhibition of the 5-lipoxygenase-catalysed linoleate oxidation by arachidonic and 5-hydroperoxy-eicosatetraenoic acids. FEBS Letters, 377 (3): 306-308.

  112. Demina O.V., Vrzheshch P.V., Khodonov A.A., Kozlovskii V.I., Varfolomeev S.D. (1995) Synthesis of substituted pyridylisoxazoles and their 4,5-dihydro analogs - Novel inhibitors of thrombocyte aggregation. Bioorganicheskaya Khimiya, 21 (12): 933-940.

  113. Bunik V., Shoubnikova A., Loeffelhardt S., Bisswanger H., Borbe H.O., Follmann H. (1995) Using Lipoate Enantiomers and Thioredoxin to Study the Mechanism of the 2-Oxoacid-Dependent Dihydrolipoate Production by the 2-Oxoacid Dehydrogenase Complexes. FEBS Letters, 371 (2): 167-170.

  114. Soloshonok V.A., Fokina N.A., Rybakova A.V., Shishkina I.P., Galushko S.V., Sorochinsky A.E., Kukhar V.P., Savchenko M.V., Svedas V.K. (1995) Biocatalytic Approach to Enantiomerically Pure Beta-Amino Acids. Tetrahedron-Asymmetry, 6 (7): 1601-1610.

  115. Mirzoeva O.K., Sudina G.F., Pushkareva M.A., Korshunova G.A., Sumbatyan N.V., Varfolomeev S.D. (1995) Lipophilic Derivatives of Caffeic Acid As Lipoxygenase Inhibitors with Antioxidant Properties. Bioorganicheskaya Khimiya, 21 (2): 143-151.

  116. Efanov A.M., Koshkin A.A., Sazanov L.A., Borodulina O.I., Varfolomeev S.D., Zaitsev S.V. (1994) Inhibition of the Respiratory Burst in Mouse Macrophages by Ultra-Low Doses of An Opioid Peptide Is Consistent with A Possible Adaptation Mechanism. FEBS Letters, 355 (2): 114-116.

  117. Soloshonok V.A., Kirilenko A.G., Fokina N.A., Kukhar V.P., Galushko S.V., Svedas V.K., Resnati G. (1994) Chemoenzymatic Approach to the Synthesis of Each of the 4 Isomers of Alpha-Alkyl-Beta-Fluoroalkyl-Substituted Beta-Amino Acids. Tetrahedron-Asymmetry, 5 (7): 1225-1228.

  118. Soloshonok V.A., Kirilenko A.G., Fokina N.A., Shishkina I.P., Galushko S.V., Kukhar V.P., Svedas V.K., Kozlova E.V. (1994) Biocatalytic Resolution of Beta-Fluoroalkyl-Beta-Amino Acids. Tetrahedron-Asymmetry, 5 (6): 1119-1126.

  119. Bunik V., Follmann H. (1993) Thioredoxin Reduction Dependent on Alpha-Ketoacid Oxidation by Alpha-Ketoacid Dehydrogenase Complexes. FEBS Letters, 336 (2): 197-200.

  120. Mevkh A.T., Miroshnikov K.A., Igumnova N.D., Varfolomeev S.D. (1993) Prostaglandin-H Synthase - Chemical Modification of Histidine-Residues in Deferent Forms of the Enzyme with Diethyl Pyrocarbonate. Biochemistry-Moscow, 58 (10): 1154-1158.

  121. Solodenko V.A., Belik M.Y., Galushko S.V., Kukhar V.P., Kozlova E.V., Mironenko D.A., Svedas V.K. (1993) Enzymatic Preparation of Both L-Enantiomer and D-Enantiomer of Phosphonic and Phosphonous Analogs of Alanine Using Penicillin Acylase. Tetrahedron-Asymmetry, 4 (9): 1965-1968.

  122. Sudina G.F., Mirzoeva O.K., Pushkareva M.A., Korshunova G.A., Sumbatyan N.V., Varfolomeev S.D. (1993) Caffeic Acid Phenethyl Ester As A Lipoxygenase Inhibitor with Antioxidant Properties. FEBS Letters, 329 (1): 21-24.

  123. Bunik V.I., Pavlova O.G. (1993) Inactivation of Alpha-Ketoglutarate Dehydrogenase During Oxidative Decarboxylation of Alpha-Ketoadipic Acid. FEBS Letters, 323 (1): 166-170.

  124. Sergeeva M.G., Terentjeva I.V., Mevkh A.T., Varfolomeev S.D. (1993) Direct Influence of Morphine on the Release of Arachidonic-Acid and Its Metabolites. FEBS Letters, 323 (1): 163-165.

  125. Soloshonok V.A., Svedas V.K., Kukhar V.P., Kirilenko A.G., Rybakova A.V., Solodenko V.A., Fokina N.A., Kogut O.V., Galaev I.Y., Kozlova E.V., Shishkina I.P., Galushko S.V. (1993) An Enzymatic Entry to Enantiopure Beta-Amino Acids. Synlett, (5): 339-341.

  126. Mevkh A.T., Miroshnikov K.A., Igumnova N.D., Varfolomeev S.D. (1993) Prostaglandin-H Synthase - Inactivation of the Enzyme in the Course of Catalysis Is Accompanied by Fast and Dramatic Changes in Protein-Structure. FEBS Letters, 321 (2): 205-208.

  127. Kukhar V.P., Soloshonok V.A., Svedas V.K., Kotik N.V., Galaev I.Y., Kirilenko A.G., Kozlova E.V. (1993) Homochiral Organoelement Analogs of Natural Compounds .2. 3-Amino-4,4,4-Trifluorobutanoic Acid - Synthesis, Enzymatic Resolution and Determination of Absolute-Configurations of Enantiomers. Bioorganicheskaya Khimiya, 19 (4): 474-477.

  128. Soloshonok V.A., Galaev I.Y., Svedas V.K., Kozlova E.V., Kotik N.V., Shishkina I.P., Galushko S.V., Rozhenko A.B., Kukhar V.P. (1993) Homochiral Organoelement Analogs of Natural Compounds .1. Biocatalytic Methods for Production of Fluorine-Containing L-Phenylglycine and D-Phenylglycine on Preparative-Scale. Bioorganicheskaya Khimiya, 19 (4): 467-473.

  129. Soloshonok V.A., Svedas V.K., Kukhar V.P., Galaev I.Y., Kozlova E.V., Svistunova N.Y. (1993) Homochiral Organoelement Analogs of Natural Compounds .3. Biocatalytic Method for Production of Fluorosubstituted (R)-Phenylalanines and (S)-Phenylalanines, (S, R)-Phenylserines and (R, S)-Phenylserines. Bioorganicheskaya Khimiya, 19 (4): 478-483.

  130. Pshezhetsky A.V., Danilova R.A., Fedorova I.M., Sagimbaeva S.K., Pervushina S.V., Obuchova M.A., Svedas V.K., Ashmarin I.P. (1993) Influence of the Immunization Against Heterologous Alcohol-Dehydrogenase on Liver Alcohol-Dehydrogenase Isozymes and Alcohol-Abuse of Rats. European Journal of Biochemistry, 212 (3): 757-761.

  131. Zaitsev S.V., Ilina A.D., Klodt P.M., Varfolomeev S.D., Yukhananov R.Y. (1992) Heterogeneity of Mu-and Delta-Opioid Binding-Sites in Murine Cerebral-Cortex - Selective Increase in Affinity of Superhigh-Affinity Delta-Binding Sites After Long-Term Administration of Morphine. Biochemistry-Moscow, 57 (8): 859-862.

  132. Vrzheshch P.V., Tatarintsev A.V., Orlova E.V., Ershov D.E., Varfolomeev S.D. (1992) Kinetics of Merthiolate-Induced Aggregation of Human Platelets. Biochemistry-Moscow, 57 (3): 307-316.

  133. Zaitsev S.V., Koshkin A.A., Izumrudova I.I., Varfolomeev S.D. (1992) A Study of the Kinetics of the Interaction of Spiperone with Binding-Sites on Human Mononuclear-Cells - Existence of A Heterogeneous Population of Spiperone Binding-Sites. Journal of Neuroimmunology, 36 (2): 225-229.

  134. Kabanov A.V., Klyachko N.L., Nametkin S.N., Merker S., Zaroza A.V., Bunik V.I., Ivanov M.V., Levashov A.V. (1991) Engineering of Functional Supramacromolecular Complexes of Proteins (Enzymes) Using Reversed Micelles As Matrix Microreactors. Protein Engineering, 4 (8): 1009-1017.

  135. Kabanov A.V., Klyachko N.L., Nametkin S.N., Merker S., Zaroza A.V., Bunik V.I., Ivanov M.V., Levashov A.V. (1991) Engineering of Functional Supramacromolecular Complexes of Proteins (Enzymes) Using Reversed Micelles As Matrix Microreactors. Protein Engineering, 4 (8): 1009-1017.

  136. Galkina S.I., Budunova I.V., Sudjina G.F., Baibakov B.A., Margolis L.B. (1991) Intercellular Contacts and Intracellular Signaling. Biologicheskie Membrany, 8 (11): 1151-1152.

  137. Petrauskas A.A., Svedas V.K. (1991) Hydrophobicity of Beta-Lactam Antibiotics - Explanation and Prediction of Their Behavior in Various Partitioning Solvent Systems and Reversed-Phase Chromatography. Journal of Chromatography, 585 (1): 3-34.

  138. Petrauskas A.A., Svedas V.K. (1991) Hydrophobicity of Beta-Lactam Antibiotics - Explanation and Prediction of Their Behavior in Various Partitioning Solvent Systems and Reversed-Phase Chromatography. Journal of Chromatography, 585 (1): 3-34.

  139. Zaitsev S.V., Sazanov L.A., Koshkin A.A., Sudina G.F., Varfolomeev S.D. (1991) Respiratory Burst Inhibition in Human Neutrophils by Ultra-Low Doses of [D-Ala2]Methionine Enkephalinamide. FEBS Letters, 291 (1): 84-86.

  140. Solodenko V.A., Kasheva T.N., Kukhar V.P., Kozlova E.V., Mironenko D.A., Svedas V.K. (1991) Preparation of Optically-Active 1-Aminoalkylphosphonic Acids by Stereoselective Enzymatic-Hydrolysis of Racemic N-Acylated 1-Aminoalkylphosphonic Acids. Tetrahedron, 47 (24): 3989-3998.

  141. Bunik V.I., Buneeva O.A., Gomazkova V.S. (1991) Regulation of the Cooperative Properties of Alpha-Ketoglutarate Dehydrogenase by Means of Thiol-Disulfide Exchange. Biochemistry-Moscow, 56 (4): 470-479.

  142. Sudina G.F., Tatarintsev A.V., Koshkin A.A., Zaitsev S.V., Fedorov N.A., Varfolomeev S.D. (1991) The Role of Adhesive Interactions and Extracellular-Matrix Fibronectin from Human Polymorphonuclear Leukocytes in the Respiratory Burst. Biochimica et Biophysica Acta, 1091 (3): 257-260.

  143. Sudina G.F., Tatarintsev A.V., Koshkin A.A., Zaitsev S.V., Fedorov N.A., Varfolomeev S.D. (1991) The Role of Adhesive Interactions and Extracellular-Matrix Fibronectin from Human Polymorphonuclear Leukocytes in the Respiratory Burst. Biochimica et Biophysica Acta, 1091 (3): 257-260.

  144. Didziapetris R.J., Svedas V.K. (1991) Penicillin Acylase-Catalyzed Acyl Group Transfer to Amino-Acids, Their Esters and Peptides - A Kinetic-Study. Biomedica Biochimica Acta, 50 (10): S237-S242.

  145. Sudina G.F., Kobelkov G.M., Barskii O.A., Varfolomeev S.D. (1990) Kinetic Scheme of the Action of 5-Lipoxygenase from Human Neutrophils. Biochemistry-Moscow, 55 (10): 1341-1353.

  146. Sobirov M.M., Khalikov S.K., Zaitsev S.V., Saidov S.S., Varfolomeev S.D. (1990) Synthesis and Investigation of Opioid Activity of Bijunctional Neuropeptide Analogs Involving the Mu-Ligands and Delta-Ligands. Vestnik Moskovskogo Universiteta Seriya 2 Khimiya, 31 (3): 321-323.

  147. Gololobov M.Y., Schellenberger U., Schellenberger F., Jakubke H.D., Svedas V.K. (1990) Peptide-Synthesis Catalyzed by Proteases - Influence of Temperature on the Kinetics of Acyl Transfer Catalyzed by Papain. Biochemistry-Moscow, 55 (2): 251-256.

  148. Gololobov M.Y., Schellenberger U., Schellenberger F., Jakubke H.D., Svedas V.K. (1990) Peptide-Synthesis Catalyzed by Proteases - Influence of Temperature on the Kinetics of Acyl Transfer Catalyzed by Papain. Biochemistry-Moscow, 55 (2): 251-256.

  149. Bunik V.I., Buneeva O.A., Gomazkova V.S. (1990) Regulation of Alpha-Ketoglutarate Dehydrogenase Cooperative Properties in Substrate Binding by Thiol-Disulfide Exchange. Biochemistry International, 21 (5): 873-881.

  150. Bunik V.I., Romash O.G., Gomazkova V.S. (1990) Inactivation of Alpha-Ketoglutarate Dehydrogenase During Enzyme-Catalyzed Reaction. Biochemistry International, 22 (6): 967-976.

  151. Bunik V.I., Buneeva O.A., Gomazkova V.S. (1990) Regulation of Alpha-Ketoglutarate Dehydrogenase Cooperative Properties in Substrate Binding by Thiol-Disulfide Exchange. Biochemistry International, 21 (5): 873-881.

  152. Gololobov M.Y., Borisov I.L., Belikov V.M., Svedas V.K. (1988) Acyl Group Transfer by Proteases Forming Acyl Enzyme Intermediate - Kinetic-Model Analysis. Biotechnology and Bioengineering, 32 (7): 866-872.

  153. Sklyankina O.A., Kurochkin I.N., Keldysh P.L., Zaitsev S.V., Varfolomeev S.D. (1988) Kinetic-Model of the Interaction of Stable Gtp Analogs with the Opioid Receptor System. Biochemistry-Moscow, 53 (2): 171-178.

  154. Kurochkin I.N., Zaitsev S.V., Belousov A.S., Sklyankina O.A., Varfolomeev S.D. (1988) Physicochemical Investigation of A Heterogeneous Population of Opioid Receptors. Biochemistry-Moscow, 53 (1): 34-45.

  155. Bunik V.I., Gomazkova V.S. (1987) Functional-Role of Histidine-Residues of Alpha-Ketoglutarate Dehydrogenase. Biochemistry-Moscow, 52 (8): 1059-1069.

  156. Gomazkova V.S., Bunik V.I., Buneeva O.A. (1987) Form of Alpha-Ketoglutarate Dehydrogenase Exhibiting No Cooperative Properties During Substrate Binding. Biochemistry-Moscow, 52 (7): 987-991.

  157. Varfolomeev S.D. (1987) Desensitization As A Reflection of Receptor-Enzyme System in the Course of the Reaction - A Kinetic-Model of the Process. Biochemistry-Moscow, 52 (2): 276-286.

  158. Araujo W.L., Tohge T., Nunes-Nesi A., Daloso D.M., Nimick M., Krahnert I., Bunik V.I., Moorhead G.B.G, Fernie A.R. (0) Phosphonate analogs of 2-oxoglutarate perturb metabolism and gene expression in illuminated Arabidopsis leaves. Front. Plant Sci., 3: . >>

  159. Viryasova G.M., Galkina S.I., Gaponova T.V., Romanova J.M., Sud'ina G.F. (0) Regulation of 5-oxo-ETE synthesis by nitric oxide in human polymorphonuclear leucocytes upon their interaction with zymosan and Salmonella typhimurium. Biosci. Rep., 34: 207-216. >>

  160. Grishina Z.V., Viryasova G.M., Romanova Y.M., Sud'ina G.F. (0) Polymorphonuclear Leukocyte Apoptosis Is Accelerated by Sulfatides or Sulfatides-Treated Salmonella Typhimurium Bacteria. Biomed Res. Int., : . >>

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