Монографии
- Мархасин В.С., Кацнельсон Л.Б., Никитина Л.В., Проценко Ю.Л., Руткевич С.М., Соловьева О.Э., Ясников Г.П. Биомеханика неоднородного миокарда. Екатеринбург, РАН. Уральское отделение, 1999, 253 с.
- Мархасин В.С., Изаков В.Я., Ясников Г.П., Белоусов В.С., Проценко Ю.Л., Введение в основы биомеханики пассивного миокарда. Москва, Наука, 2000. -207 с.
- Кобелев А.В., Смолюк Л.Т., Кобелева Р.М., Проценко Ю.Л. Нелинейные вязкоупругие свойства биологических тканей. Екатеринбург, РИО УрО РАН, 2012. 216 с.
Статьи
- Khokhlova A, Myachina T, Butova X, Volzhaninov D, Berg V, Kochurova A, Kuznetsov D, Mukhlunina E, Kopylova G, Shchepkin D. (2021) The different effects of estrogen deficiency on contractile function of atrial and ventricular myocardium. Biophys. Res. Commun. 541: 30-35. DOI: 10.1016/j.bbrc.2020.12.102. IF 2.985
- Gonchar AD, Kopylova GK, Kochurova AM, Berg VY, Shchepkin DV, Koubasova NA, Tsaturyan AK, Kleymenov SY, Matyushenko AM, Levitsky DI. (2021) Effects of myopathy-causing mutations R91P and R245G in the TPM3 gene on structural and functional properties of slow skeletal muscle tropomyosin. Biophys. Res. Commun. 534: 8-13. DOI: 10.1016/j.bbrc.2020.11.103. IF 2.985
- Lookin O., Butova X., Protsenko Y. (2021). The role of pacing rate in the modulation of mechano-induced immediate and delayed changes in the force and Ca-transient of cardiac muscle. Biophys. Mol. Biol. 159:34-45 DOI: 10.1016/j.pbiomolbio.2020.05.005
- Klinova S.V.; Katsnelson B.A.; Minigalieva I.A.; Gerzen O.P.; Balakin A.A.; Lisin R.V.; Butova K.A.; Nabiev S.R.; Lookin O.N.; Katsnelson L.B ... Nikitina L.V.; Protsenko Y.L. (2021). Cardioinotropic Effects in Subchronic Intoxication of Rats with Lead and/or Cadmium Oxide Nanoparticles. J. Mol. Sci.. 22, 3466. DOI: 10.3390/ijms22073466 IF 4.556 Q1
- Matyushenko A.M., V.V. Nefedova, D.V. Shchepkin, V. Kopylova, V.Y. Berg, A.V. Pivovarova, S.Y. Kleymenov, S.Y. Bershitsky, D.I. Levitsky. (2020). Mechanisms of disturbance of the contractile function of slow skeletal muscles induced by myopathic mutations in the tropomyosinTPM3gene. FASEB J., DOI: 10.1096/fj.202001318R. IF 4.966
- Marchenko M.A., Nefedova V.V., Yampolskaya D.S., Kopylova G.V., Shchepkin D.V., Bershitsky S.Y., Koubassova N.A., Tsaturyan A.K., Levitsky D.I., Matyushenko AM. (2020) Role of A134 and E218 amino acid residues in tropomyosin flexibility and functioning. International Journal of Molecular Sciences. 21(22):E8720. DOI: 10.3390/ijms21228720 IF 4.556
- MatyushenkoM., D.V. Shchepkin, G.V. Kopylova, S.Y. Bershitsky, D.I. Levitsky. (2020). Unique functional properties of slow skeletal muscle tropomyosin. Biochimie 174:1-8. DOI: 10.1016/j.biochi.2020.03.013. IF 3.413
- ShchepkinV., S.R. Nabiev, L.V. Nikitina, A.M. Kochurova, V.Y. Berg, S.Y. Bershitsky, G.V. Kopylova. (2020). Myosin from the ventricle is more sensitive to omecamtiv mecarbil than myosin from the atrium. Biochem. Biophys. Res. Commun. 528.4:658-663. DOI: 10.1016/j.bbrc.2020.05.108. IF 2.985
- Katsnelson B.A., S.V. Klinova, O.P. Gerzen, A.A. Balakin, O.N. Lookin, R.V. Lisin, S.R. Nabiev, L.I. Privalova, I.A. Minigalieva, V.G.Panov L.B. Katsnelson, L.V. Nikitina, D.A. Kuznetsov, Y.L. Protsenko. (2020). Force-velocity characteristics of isolated myocardium preparations from rats exposed to subchronic intoxication with lead and cadmium acting separately or in combination. Food Chem. Toxicol. 144:111641. DOI: 1016/j.fct.2020.111641 IF 4.6 Q1
- Lookin O. (2020). The use of Ca-transient to evaluate Ca2+ utilization by myofilaments in living cardiac muscle. Exp. Pharmacol. Physiol. 47.11:1824-1833. DOI: 10.1111/1440-1681.13376)
- Balakin A.A., Lukin O.N., Kuznetsov D.A., Protsenko Y.L. (2020). The intracellular calcium kinetics and action potential in the ventricular myocardium of spontaneously hypertensive ISIAH rats. Biophysics 3:487-494 DOI: 10.1134/S0006350920030021
- Protsenko Y.L., S.V. Klinova, O.P. Gerzen, L.I. Privalova, I.A. Minigalieva, A.A. Balakin, O.N. Lookin, R.V. Lisin, K.A. Butova S.R. Nabiev, L.B. Katsnelson, L.V. Nikitina, B.A. Katsnelson. (2020). Changes in rat myocardium contractility under subchronic intoxication with lead and cadmium salts administered alone or in combination. Toxicology Reports 7:433–442. DOI: 1016/j.toxrep.2020.03.001 S
- Matyushenko A.M., Shchepkin D.V., Susorov D.S., Nefedova V.V., Kopylova G.V., Berg V.Y., Kleymenov S.Y., Levitsky D.I. (2019) Structural and functional properties of alpha-beta-heterodimers of tropomyosin with myopathic mutations Q147P and K49del in the beta-chain. Biophys. Res. Commun. 508.3:934-939. DOI: 10.1016/j.bbrc.2017.06.043. IF 2.985
- Matyushenko A.M., N.A. Koubassova, D.V. Shchepkin, G.V. Kopylova, S.R. Nabiev, L.V. Nikitina, S.Y. Bershitsky, D.I. Levitsky, A.K. Tsaturyan. (2019). The effects of cardiomyopathy-associated mutations in the head-to-tail overlap junction of α-tropomyosin on its properties and interaction with actin. J. Biol. Macromol. DOI: 10.1016/j.ijbiomac.2018.09.105. IF 3.909
- Bershitsky Y., D.S. Logvinova, D.V. Shchepkin, G.V. Kopylova, A.M. Matyushenko. (2019). Myopathic mutations in the β-chain of tropomyosin differently affect the structural and functional properties of ββ- and αβ-dimers. FASEB J. DOI: 10.1096/fj.201800755R. IF 5.498
- Protsenko Y.L., B.A. Katsnelson, S.V. Klinova, O.N. Lookin, A.A. Balakin, L.V. Nikitina, O.P. Gerzen, S.R. Nabiev, I.A. Minigalieva, L.I. Privalova, V.B. Gurvich, M.P. Sutunkova, L.B. Katsnelson. (2019). Further analysis of rat myocardium contractility changes associated with a subchronic lead intoxication. Food Chem. Toxicol. 125:233–241. DOI: 1016/j.fct.2018.12.054 IF 4.6 Q1
- Lookin O., Protsenko Y. (2019). Length-dependent activation of contractility and Ca-transient kinetics in auxotonically contracting isolated rat ventricular cardiomyocytes. Physiol. 10:1473. DOI: 10.3389/fphys.2019.01473)
- Myachina T.A., Butova X.A., Lookin O.N. (2019). Development and program implementation of an algorithm to estimate the mean sarcomere length of a cardiomyocyte. Biophysics 5:732–737. DOI: 10.1134/S0006350919050178
- Protsenko Y.L., Katsnelson B.A., Klinova S.V., Lookin O.N., Balakin A.A., Nikitina L.V., Gerzen O.P., Nabiev S.R., Minigalieva I.A., Privalova L.I., Gurvich V.B., Sutunkova M.P., Katsnelson L.B. (2019). Further analysis of rat myocardium contractility changes associated with a subchronic lead intoxication. Food Chem. Toxicol. 125: 233-241. DOI: 10.1016/j.fct.2018.12.054 IF 4.6
- Lookin O., Protsenko Y. (2019). The lack of slow force response in failing rat myocardium: role of stretch-induced modulation of Ca-TnC kinetics. J. Physiol. Sci., 2:345-357 DOI: 10.1007/s12576-018-0651-3
- Koubassova N.A., S.Y. Bershitsky, A.K. Tsaturyan. (2018). Effects of an Interchain Disulfide Bond on Tropomyosin Structure: A Molecular Dynamics Study. J. Mol. Sci.; 19.11. DOI: 10.3390/ijms19113376. IF 3.687
- Matyushenko A.M., D.V. Shchepkin, G.V. Kopylova, S.Y. Bershitsky, N.A. Koubassova, A.K. Tsaturyan, D.I. Levitsky. (2018). Functional role of the core gap in the middle part of tropomyosin. FEBS J. DOI: 10.1111/febs.14369. IF 3.902
- Protsenko Y.L., B.A. Katsnelson, S.V. Klinova, O.N. Lookin, A.A. Balakin, L.V. Nikitina, O.P. Gerzen, I.A. Minigalieva, L.I. Privalova, V.B. Gurvich, M.P. Sutunkova, L.B. Katsnelson. (2018). Effects of subchronic lead intoxication of rats on the myocardium contractility. Food Chem. Toxicol. 120:378–389. DOI: 1016/j.fct.2018.07.034 IF 4.6 Q1
- Lookin O., Balakin A., Protsenko Y. (2018). Inhibition of AT1 receptors by losartan affects myocardial slow force response in healthy but not in monocrotaline-treated young rats. Physiol. Biophys. 37.2:153-162. DOI: 10.4149/gpb_2017025
- Balakin A., Kuznetsov D., Protsenko Y. (2018). The phenomena of mechanical interaction of segments of hypertrophied myocardium. Prog. Biophys. Mol. Biol. 133:20-26. DOI: 10.1016/j.pbiomolbio.2017.10.002
- Protsenko Y.L., Kuznetsov D.A., Lisin R.V., Lukin O.N., Balakin A.A. (2018). Effect of calcium on slow force responses in isolated right ventricle preparations of healthy and hypertrophied myocardium in male and female rats. Exp. Biol. Med. 165.3:285-288 DOI: 10.1007/s10517-018-4158-y
- Lookin O.N., Protsenko Y.L. (2018). Deficiency of length-dependent activation of contraction in the cardiac muscle of rats with heart failure: assessment of the muscle strip and single cell levels. Biophysics 3:441-448 DOI: 10.1134/S0006350918030132
- Lookin O., Protsenko Y. (2018). The deficiency in slow force response to sudden stretch in failing rat myocardium is associated with altered stretch-dependent modulation of Ca-TnC kinetics. Eur. Heart J. 39(Suppl_1):ehy564.P940. DOI: 10.1093/eurheartj/ehy564.P940
- Shchepkin D.V., L.V. Nikitina, S.Y. Bershitsky, G.V. Kopylova. (2017). The isoforms of α-actin and myosin affect the Ca2+ regulation of the actin-myosin interaction in the heart. Biophys. Res. Commun. 490.2:324-9. DOI: 10.1016/j.bbrc.2017.06.043. IF 2.466
- Shchepkin D.V., S.R. Nabiev, G.V. Kopylova, A.M. Matyushenko, D.I. Levitsky, S.Y. Bershitsky, A.K. Tsaturyan (2017). Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin. Muscle Res. Cell Motil. DOI 10.1007/s10974-017-9472-x. IF 2.071
- Bershitsky S.Y., N.A. Koubassova, M.A. Ferenczi, G.V. Kopylova, T. Narayanan, A.K. Tsaturyan (2017). The closed state of the thin filament is not occupied in fully activated skeletal muscle. J. 112.7:1455–61. DOI: 10.1016/j.bpj.2017.02.017. IF 3.656
- Matyushenko A.M., D.V. Shchepkin, G.V. Kopylova, K.E. Popruga, N.V. Artemova, A.V. Pivovarova, S.Y. Bershitsky, D.I. Levitsky (2017). Structural and Functional Effects of Cardiomyopathy-Causing Mutations in the Troponin T-Binding Region of Cardiac Tropomyosin. Biochemistry 1:250-9. DOI: 10.1021/acs.biochem.6b00994. IF 2.98
- Matyushenko A.M., N.V. Artemova, D.V. Shchepkin, G.V. Kopylova, S.R. Nabiev, L.V. Nikitina, D.I. Levitsky, S.Y. Bershitsky (2017). The interchain disulfide cross-linking of tropomyosin alters its regulatory properties and interaction with actin filament. Biophys. Res. Commun. 482:305-9. DOI: 10.1016/j.bbrc.2016.11.059. IF 2.371
- Protsenko Y.L., Balakin A.A., Kuznetsov D.A., Kursanov A.G., Lisin R.V., Mukhlynina E.A., Lookin O.N. (2017). Contractility of right ventricular myocardium in male and female rats during physiological and pathological hypertrophy. Exp. Biol. Med. 162.3:303-305. DOI: 10.1007/s10517-017-3600-x
- Peyronnet R., Bollensdorff C., Capel R.A., Rog-Zielinska E.A., Woods C.E., Charo D.N., Lookin O., Fajardo G., Hoe M., Quertermous T., Ashley E.A., Kohl P. (2017). Load-dependent effects of apelin on murine cardiomyocytes. Biophys. Mol. Biol. 130(Part B):333-343 (doi: 10.1016/j.pbiomolbio.2017.09.013)
- Kopylova G.V., S.N. Nabiev, L.V. Nikitina, D.V. Shchepkin, Y. Bershitsky (2016). The properties of the actin-myosin interaction in the heart muscle depend on the isoforms of myosin but not of α-actin. Biochem. Biophys. Res. Commun. 476.4:648-53. DOI: 10.1016/j.bbrc.2016.06.013. IF 2.371
- Koubassova N.A., S.Y. Bershitsky, M.A. Ferenczi,·T. Narayanan, A.K. Tsaturyan (2016) Tropomyosin movement is described by a quantitative high-resolution model of X-ray diffraction of contracting muscle. Biophys. J. 46:335–42. DOI: 10.1007/s00249-016-1174-6. IF 1.472
- Nabiev S.R., D.A. Ovsyannikov, G.V. Kopylova, D.V. Shchepkin, A.M. Matyushenko, N.A. Koubassova, D.I. Levitsky, A.K. Tsaturyan, S.Y. Bershitsky (2015). Stabilizing the Central Part of Tropomyosin Increases the Bending Stiffness of the Thin Filament. J., 109.2:373-9. DOI: 10.1016/j.bpj.2015.06.006. IF 3.972
- Nabiev S.R., D.A. Ovsyannikov, A.K. Tsaturyan and S.Y. Bershitsky (2015). The lifetime of the actomyosin complex in vitro under load corresponding to stretch of contracting muscle. Biophys. J. 44.6:457-63. DOI: 10.1007/s00249-015-1048-3. IF 2.474
- Lookin O.N., Protsenko Y.L. (2016). The kinetics of cytosolic calcium in the right ventricular myocardium of guinea pigs and rats. Biophysics 1:119-132 DOI: 10.1134/S0006350916010140
- Lookin O., Kuznetsov D., Protsenko Y. (2015). Sex differences in stretch-dependent effects on tension and Ca2+ transient of rat trabeculae in monocrotaline pulmonary hypertension. J. Physiol. Sci. 65:89-98. DOI: 10.1007/s12576-014-0341-8
- Lookin O., Balakin A., Kuznetsov D., Protsenko Y. (2015). The length-dependent activation of contraction is equally impaired in impuberal male and female rats in monocrotaline-induced right ventricular failure. Clin. Exp. Pharmacol. Physiol. 11:1198-1206. DOI: 10.1111/1440-1681.12471)
- Matyushenko A.M., Artemova N.V., Shchepkin D.V., Kopylova G.V., Bershitsky Y., Tsaturyan A.K., Sluchanko N.N., Levitsky D.I. (2014). Structural and functional effects of two stabilizing substitutions, D137L and G126R, in the middle part of α-tropomyosin molecule. FEBS J. 281, 2004-16. DOI: 10.1111/febs.12756. IF 4.001
- Ferenczi M.A., S.Y. Bershitsky, N.A. Koubassova, G.V. Kopylova, M. Fernandez, T. Narayanan, A.K. Tsaturyan (2014). Why muscle is an efficient shock absorber. PLoS One. DOI: 10.1371/journal.pone.0085739. IF 534
- Markhasin V.S., Balakin A., Katsnelson L.B., Konovalov P., Lookin O., Protsenko Y., Solovyova O. (2012). Slow force response and auto-regulation of contractility in heterogeneous myocardium. Biophys. Mol. Biol. 110:305-318. DOI: 10.1016/j.pbiomolbio.2012.08.011
- Tsaturyan A.K., S.Y. Bershitsky, N.A. Koubassova, M. Fernandez,T. Narayanan and M.A. Ferenczi. (2011). The fraction of myosin motors that participate in isometric contraction of rabbit muscle fibers at near-physiological temperature. J., 101:404-410. IF 3.653
- Markhasin V.S., Balakin A.A., Protsenko Y.L., Solovyova O. (2011). Activation sequence of cardiac muscle in simplified experimental models: relevance for cardiac mechano electric coupling», Ch. 21 in Cardiac Mechano-Electric Coupling & Arrhythmias 2nd edition, eds. Dr's Kohl, Sachs and Franz, pp 153-159
- Bollensdorff C., Lookin O., Kohl P. (2011). Assessment of contractility in intact ventricular cardiomyocytes using the dimensionless ‘Frank–Starling Gain’ index. Pflugers Arch. 1:39-48. DOI: 10.1007/s00424-011-0964-z
- Katsnelson L.B., Solovyova O., Balakin A., Lookin O., Konovalov P., Protsenko Y., Sulman T., Markhasin V.S. (2011). Contribution of mechanical factors to arrhythmogenesis in calcium overloaded cardiomyocytes: model predictions and experiments. Biophys. Mol. Biol. 107:81-89. DOI: 10.1016/j.pbiomolbio.2011.06.001
- Shchepkin D.V., G.V. Kopylova, L.V. Nikitina, L.B. Katsnelson, S.Y. Bershitsky. (2010). Effects of cardiac myosin binding protein-C on the regulation of interaction of cardiac myosin with thin filament in an in vitro motility assay. Biophys. Res. Commun. 401:159-163. IF 2.595
- Bershitsky S.Y., N.A. Koubassova, P.M. Bennett, M.A. Ferenczi, D.A. Shestakov and A.K. Tsaturyan. (2010). Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle. J. 99.6:1827-1834. IF 4.218
- Bershitsky S.Y., M.A. Ferenczi, N.A. Koubassova and A.K. Tsaturyan. (2009). Insight into the actin-myosin motor from x-ray diffraction on muscle. Front. Biosci. 14:3188-3213. IF 3.736
- Koubassova N.A., S.Y. Bershitsky, M.A. Ferenczi and A.K. Tsaturyan. Direct modeling of X-ray diffraction pattern from contracting skeletal muscle. (2008). J. 95.6:2880-94. IF 4.683
- Solovyova O., Katsnelson L.B., Kohl P., Konovalov P., Lookin O., Moskvin A.S., Vikulova N., Protsenko Y.L., Markhasin V. (2006). Activation sequence as a key mechanism of functional self-organization of myocardium. Philosophical Transactions The Royal Soc. A, 364:1367-1383. DOI: 10.1098/rsta.2006.1777
- Ferenczi M.A., Bershitsky S.Y., Koubassova N., Siththanandan V., Helsby W.I., Panine P., Roessle M., Narayanan T. and Tsaturyan A.K. (2005). The ‘roll and lock’ mechanism of force generation in muscle. Structure 1:131-141. IF 5.543
- Tsaturyan A.K., Koubassova N., Ferenczi M.A., Narayanan T., Roessle M. and Bershitsky S.Y. (2005). Strong binding of myosin heads stretches and twists the actin helix. J. 88.3, 1902-1910. IF 4.507
- Protsenko Y.L., Routkevitch S.M., Gur’ev V.Y., Katsnelson L.B., Solovyova O., Lookin O.N., Balakin A.A., Kohl P., Markhasin V.S. (2005). Hybrid duplex – a novel method to study the contractile function of heterogeneous myocardium. American J. Physiol. - Heart Circ. Physiol. 289:H2733-2746. DOI: 10.1152/ajpheart.00306.2005
- Bennett P.M., Tsaturyan A.K. and Bershitsky S.Y. (2002). Rapid cryofixation of rabbit muscle fibres after a temperature jump. Microscopy, 206.2:152–160, 2002. IF 2.15
- Bershitsky S.Y. and Tsaturyan A.K. (2002). The elementary force generation process probed by temperature and length perturbations in muscle fibres from the rabbit. Physiol., 540.3:971-988. IF 4.476
- Tsaturyan A.K., Bershitsky S.Y., Burns R., He Z.-H. and Ferenczi M.A. (1999.) Structural responses to the photolytic release of ATP in frog muscle fibres observed by time-resolved X-ray diffraction. J Physiol. 520:681-696. IF 4.552
- Tsaturyan, A. K., Bershitsky, S. Y., Burns, R. and Ferenczi, M. A. (1999). Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers. J. 77:354-372. IF 4.58
- Bershitsky S.Y., Tsaturyan A.K., Bershitskaya O.N., Mashanov, G.I., Brown, P., Burns, R., Ferenczi M.A. (1997) Muscle force is generated by myosin heads stereospecifically attached to actin Nature 388:186-190. IF 27.368.
- Bershitsky, S.Y., A.K. Tsaturyan, O.N. Bershitskaya, G.I. Mashanov, P. Brown, M. Webb and M.A. Ferenczi (1996) Mechanical and structural properties underlying contraction of skeletal muscle fibers after partial 1-ethyl-3[3-(dimethylamino)propyl]carbodiimide cross-linking. J. 71:1462-1474. IF 4.713
- Bershitsky, S.Y. and A.K. Tsaturyan (1995) Force generation and work production by covalently cross-linked actin-myosin cross-bridges in rabbit muscle fibers. J. 69:1011-1021. IF 4.325
- Bershitsky, S.Y. and A.K. Tsaturyan (1992). Tension responses to Joule temperature jump in skinned rabbit muscle fibres. Physiol. 447:425-448. IF 4.843
Патенты
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