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[Head of Laboratory ] [Scientific Staff] [General description of the Laboratory] [Area of Research in the Laboratory] [The Main Achievements] [Unique or Rare Approaches] [Scientific Connections] [Grant Support] [Selected Publications]


LABORATORY OF MOLECULAR ORGANIZATION OF BIOLOGICAL STRUCTURES

Head of Laboratory:

    Professor Dmitrii I. Levitsky,
    Dr. Biol. Sci., Professor of Biochemistry
    Born: 11 December 1951
    tel.:  +7(495)-952-1384
    e-mail: Levitsky@inbi.ras.ru

    Education:
    M.S. – 1976, Moscow State University (School of Biology, Department of Molecular Biology); Ph.D. – 1981, Moscow State University; Doctor of Biological Sciences (Biochemistry) – 1992, A.N.Bach Institute of Biochemistry, Russian Academy of Science; Professor of Biochemistry – 2001, A.N.Bach Institute of Biochemistry, Russian Academy of Sciences.

    Institutional Affiliations
    :
    1976–1988: Junior Research Associate (1976-1982), Scientist (1982-1988), A.N.Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry (from 1991 – A.N.Belozersky Institute of Physico-Chemical Biology), Moscow State University; 1988-1992: Senior Scientist, A.N.Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia; 1992–1997: Leader Scientist, Head of Research Group, A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia; 1997–2008: Head Scientist, A.N.Belozersky Institute of Physico-Chemical Biology, Moscow State University; 2001–present: Head of Laboratory, A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
    Area of Expertise: Myosin, actin and tropomyosin structure and functions, thermal unfolding of proteins, differential scanning calorimetry.

    Honors: 1990 – Prize of the Academy of Sciences of the USSR.

    List of Selected Publications (from 1995 only; the papers published in English are only cited) :
    1. Bobkov, A.A. and Levitsky, D.I. (1995) Differential scanning calorimetric study of the complexes of myosin subfragment 1 with nucleoside diphosphates and vanadate or beryllium fluoride. Biochemistry 34, 9708-9713.
    2. Gopal, D., Bobkov, A.A., Schwonek, J.P., Sanders, C.R., Ikebe, M., Levitsky, D.I., and Burke, M. (1995) Structural basis of actomyosin chemo-mechanical transduction by non-nucleoside triphosphate analogues. Biochemistry 34, 12178-12184.
    3. Ponomarev, M.A., Timofeev, V.P., and Levitsky, D.I. (1995) The difference between ADP-beryllium fluoride and ADP-aluminum fluoride complexes of the spin-labeled myosin subfragment 1. FEBS Letters 371, 261-263.
    4. Nikolaeva, O.P., Orlov, V.N., Dedova, I.V., Drachev, V.A., and Levitsky, D.I. (1996) Interaction of myosin subfragment 1 with F-actin studied by differential scanning calorimetry. Biochemistry and Molecular Biology International 40, 653-661.
    5. Golitsina, N.L., Bobkov, A.A., Dedova, I.V., Pavlov, D.A., Nikolaeva, O.P., Orlov V.N., and Levitsky, D.I. (1996) Differential scanning calorimetric study of the complexes of modified myosin subfragment 1 with ADP and vanadate or beryllium fluoride. J. Muscle Res. and Cell Motility 17, 475-485.
    6. Gopal, D., Pavlov, D.A., Levitsky, D.I., Ikebe, M., and Burke, M. (1996) Chemomechanical transduction in the actomyosin molecular motor by 2’,3’-dideoxydidehydro-ATP and characterization of its interaction with myosin subfragment 1 in the presence and absence of actin. Biochemistry 35, 10149-10157.
    7. Levitsky, D. I., Ponomarev, M. A., Geeves, M. A., Shnyrov, V. L., and Manstein, D. J. (1998) Differential scanning calorimetric study of the thermal unfolding of the motor domain fragments of Dictyostelium discoideum myosin II. Europ. J. Biochem. 251, 275-280.
    8. Levitsky, D.I., Nikolaeva, O.P., Orlov, V.N., Pavlov, D.A., Ponomarev, M.A., and Rostkova, E.V. (1998) Differential scanning calorimetric studies on myosin and actin (review). Biochemistry (Moscow) 63, 322-333.
    9. Pavlov, D. A., Sobieszek, A., and Levitsky, D. I. (1998) Calorimetric studies of the thermal unfolding of smooth muscle myosin fragments and their complexes with ADP and phosphate analogs. Biochemistry (Moscow) 63, 952-962.
    10. Orlov, V. N., Rostkova, E. V., Nikolaeva, O. P., Drachev, V. A., Gusev, N. B., and Levitsky, D. I. (1998) Thermally induced chain exchange of smooth muscle tropomyosin dimers studied by differential scanning calorimetry. FEBS Letters 433, 241-244.
    11. Bobkova, E. A., Bobkov, A. A., Levitsky, D. I., and Reisler, E. (1999) Effects of SH1 and SH2 modifications on myosin: similarities and differences. Biophys. J. 76, 1001-1007.
    12. Rostkova, E.V., Moiseeva, L.N., Teplova, M.V., Nikolaeva, O.P., and Levitsky, D.I. (1999) Use of stable analogs of myosin ATPase intermediates for kinetic studies of the “weak” binding of myosin heads to F-actin. Biochemistry (Moscow) 64, 875-882.
    13. Levitsky, D.I., Rostkova, E.V., Orlov, V.N., Nikolaeva, O.P., Moiseeva, L.N., Teplova, M.V., and Gusev, N.B. (2000) Complexes of smooth muscle tropomyosin with F-actin studied by differential scanning calorimetry. Europ. J. Biochem. 267, 1869-1877.
    14. Ponomarev, M.A., Furch, M., Levitsky, D.I., and Manstein, D.J. (2000) Charge changes in loop 2 affect the thermal unfolding of the myosin motor domain bound to F-actin. Biochemistry 39, 4527-4532.
    15. Kaspieva, O.V., Nikolaeva, O.P., Orlov, V.N., Ponomarev, M.A., Drachev, V.A., and Levitsky, D.I. (2001) Changes in the thermal unfolding of p-phenylenedimaleimide-modified myosin subfragment 1 induced by its “weak” binding to F-actin. FEBS Lett. 489, 144-148.
    16. Nikolaeva, O. P., Orlov, V. N., Bobkov, A. A., and Levitsky, D. I. (2002) Differential scanning calorimetric study of myosin subfragment 1 with tryptic cleavage at the N-terminal region of the heavy chain. Eur. J. Biochem. 269, 5678-5688.
    17. Tsiavaliaris, G., Fujita-Becker, S., Batra, R., Levitsky, D. I., Kull, F. J., Geeves, M. A., and Manstein, D. J. (2002) Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium. EMBO Reports 3, 1099-1105.
    18. Levitsky, D. I. (2004) Structural and functional studies of muscle proteins by using differential scanning calorimetry. In: “The Nature of Biological Systems as Revealed by Thermal Methods” (Denes Lorinczy, Ed.), Kluwer Acad. Publ., Dordrecht/Boston/London, 2004, p. 127-158.
    19. Dedova, I.V., Nikolaeva. O.P., Mikhailova, V.V., dos Remedios, C.G., and Levitsky, D.I. (2004) Two opposite effects of cofilin on the thermal unfolding of F-actin: a differential scanning calorimetric study. Biophysical Chemistry 110, 119-128.
    20. Kremneva, E., Boussouf, S., Nikolaeva, O., Maytum, R., Geeves, M.A., and Levitsky, D.I. (2004) Effects of two familial hypertrophic cardiomyopathy mutations in α-tropomyosin, Asp175Asn and Glu180Gly, on the thermal unfolding of actin-bound tropomyosin. Biophys. J. 87, 3922-3933.
    21. Levitsky, D.I. (2004) Actomyosin systems of biological motility (review) Biochemistry (Moscow) 69, 1177–1189.
    22. Pivovarova, A.V., Mikhailova, V.V., Chernik, I.S., Chebotareva, N.A., Levitsky, D.I., and Gusev, N.B. (2005) Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin. Biochem. Biophys. Res. Commun. 331, 1548–1553.
    23. Kremneva, E., Nikolaeva, O., Maytum, R., Arutyunyan, A.M., Geeves, M.A., and Levitsky, D.I. (2006) Thermal unfolding of smooth muscle and non-muscle tropomyosin α-homodimers with alternatively spliced exons. FEBS Journal 273, 588–600.
    24. Mirza M., Robinson P., Kremneva E., Copeland O., Nikolaeva O., Watkins H, Levitsky D., Redwood C., El-Mezgueldi M., and Marston S. (2007) “The effect of mutations in α-tropomyosin (E40K and E54K) that cause familial dilated cardiomyopathy on the regulatory mechanism of cardiac muscle thin filaments” J. Biol. Chem., v. 282, ¹ 18, p. 13487–13497.
    25. Pivovarova A.V., Chebotareva N.A., Chernik I.S., Gusev N.B., and Levitsky D.I. (2007) “Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin”. FEBS Journal, v. 274, ¹ 22, p. 5937–5948.
    26. Markov D.I., Pivovarova A.V., Chernik I.S., Gusev N.B., and Levitsky D.I. (2008) “Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation”. FEBS Lett., v. 582, ¹ 10, p. 1407–1412.
    27. Levitsky, D.I., Pivovarova, A.V., Mikhailova, V.V., and Nikolaeva O.P. (2008) “Thermal unfolding and aggregation of actin. Stabilization and destabilization of actin filaments”. FEBS Journal, v. 275, ¹ 17, p. 4280–4295.
    28. Nevzorov I., Redwood C. and Levitsky D. (2008) “Stability of two β-tropomyosin isoforms: effects of mutation Arg91Gly”. J. Muscle Res. Cell Motil., v. 29, p. 173–176.
    29. Kazakov A.S., Markov D.I., Gusev N.B., Levitsky D.I. (2009) “Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22”. Biophysical Chemistry, v. 145, No. 2–3, p. 79–85.
    30. Pivovarova, A.V., Khaitlina, S.Yu., Levitsky, D.I. (2010) “Specific cleavage of the DNase-I binding loop dramatically decreases the thermal stability of actin”, FEBS Journal, v. 277, No. 18, p. 3812-3822.

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Scientific Staff:

    Natalia A. CHEBOTAREVA, Dr. Biol. Sci., Leading Research Fellow
    BellaYa. GURVITS, Dr. Biol. Sci., Leading Research Fellow
    Iraida E. ANDREEVA, Ph.D., Senior Research Fellow
    Tatyana B. ERONINA, Ph.D., Senior Research Fellow
    Valentina F. MAKEEVA, Ph.D., Senior Research Fellow
    Elena V. KREMNEVA, Ph.D., Research Fellow
    Anastasiya V. PIVOVAROVA, Ph.D., Research Fellow
    Valeria V. MIKHAILOVA, Ph.D., Junior Research Fellow
    Vita A. SHTEIN-MARGOLINA, Ph.D., Senior Research Fellow
    Sergei Yu. KLEIMENOV, Ph.D., Senior Research Fellow
    Ilya A. NEVZOROV, Junior Research Fellow
    Svetlana G. ROMAN(BAZHINA), Junior Research Fellow
    Denis I. MARKOV, Post-Graduate Student
    Zoya M. BUMAGINA, Post-Graduate Student
    Natalia V. ARTEMOVA, Post-Graduate Student

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General description of the Laboratory:
    The founder of this Laboratory was well-known Russian scientist, academician Vladimir A. Engelhardt. He was the first who discovered the ability of myosin, the main muscle protein, to hydrolyze ATP. This work published in “Nature” in 1939 has initiated a new scientific direction – mechanochemistry of muscle contraction, and predetermined the whole posterior progress of muscle biochemistry. From 1977 to 2001 the Head of the Laboratory was Professor Boris F. Poglazov (1930–2001), the Corresponding Member of Russian Academy of Sciences. In 1988 he was elected the Director of the Bach Institute of Biochemistry. Boris F. Poglazov played an important role in development of muscle biochemistry and in studies on biological motility. Starting his scientific activities from studies on structure and properties of muscle myosin in the course of diploma work and following preparation of the PhD thesis under the supervision of Vladimir A. Engelhardt, later on he attempted, for the first time in the world, to find myosin in non-muscle cells and tissues. He was the first scientist in the world who has found myosin in non-muscle tissues of animals, as well as myosin-like proteins in higher plants and algae, and has proposed from this finding that myosin is the main “motile” protein not only in muscles, but also in all eucaryotic cells. These innovatory works of Professor Poglazov were reflected in his monograph “Structure and Functions of Contractile Proteins” published in Russian in 1965 and in English by “Academic Press” (N. Y.) in 1966. A hypothesis advanced many years ago by Professor Boris F. Poglazov, on the presence of myosin-like proteins in all eucaryotic cells, was very audacious and unusual for that time, but later on it was completely corroborated. At present there are no doubts that just ATP-dependent interaction of myosin with actin is a universal molecular mechanism providing a number of various events of motility in living cells. When Professor Poglazov died in 2001, Professor Dmitrii I. Levitsky was chosen to head the Laboratory.
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Area of Research in the Laboratory:
    Structural and functional studies of myosin, actin, and tropomyosin – the main proteins of muscles and many other systems of biological motility. The use of the method of differential scanning calorimetry (DSC) for studies on the thermal unfolding of these proteins and for probing structural changes that occur in these proteins during their functioning.
    Structure, regulation of activity, and denaturation of key energy-providing enzymes of skeletal muscle – glycogen phosphorylase b and kinase phosphorylase. Effects of molecular crowding on structural and functional properties of these enzymes.
    Protein folding and stability; enzymatic catalysis of the folding process; immunologically active thermostable peptides/neuropeptides that participate in the protein folding; new biochemical mechanisms of adaptation of an organism to the heat shock and other types of stresses. Investigation of a mechanism of acting of low molecular weight chaperones (small heat shock proteins).
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The Main Achievements:
    A new approach has been developed for probing and following investigation of structural changes that occur in muscle proteins (myosin heads, actin, tropomyosin) in the course of their functioning. This approach is based on detailed studies, using the method of differential scanning calorimetry (DSC), of the character of thermal unfolding of muscle proteins and its changes upon modeling the processes naturally occurring during muscle contraction. It has been shown using this approach that during ATPase reaction myosin heads undergo to global conformational changes, which are accompanied by significant changes in the domain structure of the protein. We have also found significant conformational changes of myosin heads and tropomyosin induced by interaction of these proteins with actin filaments.
    We have also developed a new approach for studying the mechanism of the thermal unfolding of tropomyosin (Tm) bound to F-actin. This approach includes combined studies of the thermal unfolding of actin-bound Tm using differential scanning calorimetry (DSC) and the thermally induced dissociation of the Tm–F-actin complexes investigated by measuring temperature dependences of light scattering. We applied this approach for studying the thermal unfolding of a great number of Tm species in their actin-bound state (muscle and non-muscle Tm isoforms of different length, as well as various mutant constructs of Tm expressed in E. coli). As a result, a mechanism of the thermal unfolding of actin-bound Tm has been proposed. According to this mechanism, the character of the thermal unfolding of actin-bound Tm is mainly determined by dissociation of the Tm–F-actin complexes. Another achievement of our work was that we applied the above described approach to examine the effects of two familial hypertrophic cardiomyopathy mutations in Tm, D175N and E180G, on the thermal unfolding of actin-bound Tm, and showed that Tm carrying mutation E180G dissociates from F-actin and denatures at temperature lower than that for wild type Tm and Tm with mutation D175N, but close to the temperature in the heart. Thus, under conditions similar to physiological (e. g. when the body temperature increases by only few degrees as a reaction to fever or vigorous muscle activity) the mutation E180G may cause dissociation of Tm from F-actin and its following denaturation. These results could explain for the first time why the mutation E180G leading to severe cardiac hypertrophy and death is much more disruptive than the mutation D175N that causes only a mild hypertrophy.
    It has also been shown that low-molecular-weight chaperones (small heat shock proteins, α-crystallin) effectively prevent aggregation of thermally denatured F-actin, but they do not affect the thermal unfolding of F-actin. These results provide for the first time the answer to one of the key questions on the molecular mechanism of action of small heat shock proteins, namely they affect only the heat-induced aggregation of a target protein, with no influence on the thermal denaturation preceding aggregation.
    The method for continuous recording of activity of phosphorylase kinase has been developed. A model of the functional complex between phosphorylase b and phosphorylase kinase on the glycogen particles has been proposed. A mechanism of thermal denaturation and renaturation of glycogen phosphorylase b has been studied.
    The systematic research of the influence of molecular crowding on the key enzymes of the glycogen metabolism has been carried out. The crowding condition in vitro was imitated by high concentration of osmolytes. The effects of the crowding on association and conformation of the enzymes, as well as on their interaction with glycogen and protein-protein interactions have been demonstrated. It has been shown upon studies on chemical and thermal denaturation of phosphorylase b that osmolytes protect the protein from denaturation but they promote aggregation of unfolded protein due to the effect of molecular crowding.
    It has been demonstrated for the first time that stress-induced cytokine, macrophage migration inhibitory factor (MIF), shows chaperone-like properties in preventing the thermally induced aggregation of model target proteins.
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Unique or Rare Approaches Developed in the Laboratory (on the base of own equipment):
    Differential Scanning Calorimetry (DSC) . This method allows the thermal denaturation of proteins to be studied in detail. We have two differential adiabatic scanning microcalorimeters DASM-4M (Institute for Biological Instrumentation of Russian Academy of Sciences, Pushchino, Russia)
    Analysis of Temperature Dependences of Light Scattering. This approach allows to investigate the dissociation of protein complexes and the heat-induced aggregation of proteins at a constant heating rate, i. e. under the same conditions as for DSC experiments. This approach allows comparing the processes of aggregation or dissociation with that of the thermal denaturation. These experiments are performed on a Cary Eclipse fluorescence spectrophotometer (Varian) equipped with temperature controller and thermoprobes.
    Ultracentrifugation of Microprobes. This approach allows fast high-speed centrifugation of microprobes (100–150 ?l) with following analysis of the protein content in pellets and supernatants by SDS-PAGE. The approach is mainly used for studies of the interaction of various actin-binding proteins with F-actin filaments. These experiments are performed on the Airfuge (Beckman) which allows achieving the rotor speed of 180,000 during only several tens of seconds.
    Analytical Ultracentrifugation. This approach is applied for detailed studies of oligomeric states of proteins, interaction between macromolecules, and protein-ligand interactions under normal conditions or under conditions of molecular crowding. The experiments are carried out on Beckman model E analytical ultracentrifuge equipped with a photoelectric scanner and personal computer, as well as with a unique software for data collecting.
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Inter-institutional and International Scientific Connections:
    Moscow State University (A.N. Belozersky Institute of Physico-Chemical Biology; Department of Biochemistry, School of Biology; Department of Biophysics, School of Physics);
    University of Kent at Canterbury, Canterbury, United Kingdom (Department of Biosciences, Prof. M.A. Geeves), National Heart and Lung Institute, Imperial College, London, United Kingdom (Prof. Steven Marston), and Department of Cardiovascular Medicine, University of Oxford, Oxford, United Kingdom (Dr. Charles Redwood) – collaboration with Prof. Dmitrii Levitsky’s scientific team on structural and functional studies on tropomyosin .
    University of Nottingham, Sutton Bonington, United Kingdom (National Centre for Macromolecular Hydrodynamics, Prof. S.E. Harding – collaboration with Dr. N.A. Chebotareva on hydrodynamic studies of macromolecules under thermodynamically non-ideal conditions).
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Grant Support:
    1990–1992: International Science Cooperation Grant from the US National Science Foundation and Russian Academy of Sciences; 1993–1995: Two-years Cooperation grant from Fogarty International Center, NIH; 1994–1996: International Science Foundation (ISF) two-years research grant; 1994–present: Three-years research grants from Russian Foundation for Basic Research (RFBR); 1999–2001: Three years joint grant from the International Association for the Promotion of Cooperation with the Scientists from the New Independent States of the former Soviet Union (INTAS) and RFBR (Grant Coordinator – Prof. M.A. Geeves); 2002–2005: The Wellcome Trust (Grant Coordinator – Prof. M.A. Geeves, Canterbury, UK); 2003–2005: Grant of the Program for the Support of Scientific Schools in Russia; 2002–2007, 2008–2012: Grant of the Program “Molecular and Cell Biology” of Russian Academy of Sciences (Principal Investigator – Prof. Boris I. Kurganov).
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Selected Publications for last 5 years:

    1. Pivovarova, A.V., Mikhailova, V.V., Chernik, I.S., Chebotareva, N.A., Levitsky, D.I., Gusev, N.B. “Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin”. Biochem. Biophys. Res. Commun. (2005), v. 331, p. 1548–1553.
    2. Chebotareva N.A., Kurganov B.I., Harding S.E., Winzor D.J. "Effect of osmolytes on the interaction of flavin adenine dinucleotide with muscle glycogen phosphorylase b" Biophysical Chemistry (2005), v. 113, p. 61–66.
    3. Chebotareva N.A., Meremyanin A.V., Makeeva V.F., Kurganov B.I. “Self-association of phosphorylase kinase under molecular crowding conditions”. Progr. Colloid Polym. Sci., (2006), v. 131, p. 83-92.
    4. Kremneva E., Nikolaeva O., Maytum R., Arutyunyan A.M., Geeves, M.A. and Levitsky D.I. “Thermal unfolding of smooth muscle and non-muscle tropomyosin alpha-homodimers with alternatively spliced exons”. FEBS Journal (2006) v. 273, p. 588–600.
    5. Golub, N., Meremyanin, A., Markossian, K., Eronina, T., Chebotareva, N., Asryants, R., Muronets, V., Kurganov, B. Evidence for the formation of start aggregates as an initial stage of protein aggregation, FEBS Letters , (2007) v. 581, p. 4223-4227.
    6. Pivovarova A.V., Chebotareva N.A., Chernik I.S., Gusev N.B., and Levitsky D.I. “Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin”. FEBS Journal , (2007) v. 274, ¹ 22, p. 5937–5948.
    7. Markov D.I., Pivovarova A.V., Chernik I.S., Gusev N.B., and Levitsky D.I. “Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation”. FEBS Lett., (2008) v. 582, ¹ 10, p. 1407–1412.
    8. Meremyanin, A.V., Eronina, T.B., Chebotareva, N.A., Kurganov, B.I. “Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: mechanism of protein action of alpha-crystallin”. Biopolymers, (2008) v. 89, No. 2, p. 124-134.
    9. Chebotareva N.A., Meremyanin, A.V., Makeeva V.F., Livanova N.B., Kurganov B.I. Cooperative self-association of phosphorylase kinase from rabbit skeletal muscle. Biophysical Chemistry , (2008) v. 133, p. 45-53.
    10. Artemova N.V., Kasakov A.S., Bumagina Z.M., Lyutova E.M., Gurvits B.Ya. “Protein aggregates as depots for the release of biologically active compounds”. Biochemical and Biophysical Research Communications , (2008) v. 377, ¹ 2, p. 596–599.
    11. Levitsky, D.I., Pivovarova, A.V., Mikhailova, V.V., and Nikolaeva O.P. “Thermal unfolding and aggregation of actin. Stabilization and destabilization of actin filaments”. FEBS Journal (2008) v. 275, ¹ 17, p. 4280–4295.
    12. Kazakov A.S., Markov D.I., Gusev N.B., Levitsky D.I. “Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22”. Biophysical Chemistry, (2009) v. 145, No. 2–3, p. 79–85.
    13. Eronina, T.B., Chebotareva, N.A., Bazhina, S.G., Makeeva, V.F., Kleymenov, S.Y., Kurganov, B.I. “Effect of proline on thermal inactivation, denaturation and aggregation of glycogen phosphorylase b from rabbit skeletal muscle”. Biophysical Chemistry, (2009) v. 141, No. 1, p. 66-74.
    14. Pivovarova, A.V., Khaitlina, S.Yu., Levitsky, D.I. “Specific cleavage of the DNase-I binding loop dramatically decreases the thermal stability of actin”, FEBS Journal, (2010) v. 277, No. 18, p. 3812-3822.
    15. Chebotareva, N.A., Makeeva, V.F., Bazhina, S.G., Eronina, T.B., Gusev, N.B., Kurganov, B.I. “Interaction of Hsp27 with native phosphorylase kinase under crowding conditions”. Macromolecular Bioscience, (2010) v. 10, No. 7, p. 783-789.
    16. Bumagina, Z.M., Gurvits, B.Ya., Artemova, N.V., Muranov, K.O., Kurganov, B.I. “Mechanism of suppression of dithiothreitol-induced aggregation of bovine alpha-lactalbumin by alpha-crystallin” Biophysical Chemistry, (2010) v. 146, No. 2-3, p. 108-117.
    17. Artemova, N.V., Bumagina, Z.M., Kasakov, A.S., Shubin, V.V., Gurvits, B.Ya. “Opioid peptides derived from food proteins suppress aggregation and promote reactivation of partly unfolded stressed proteins”. Peptides, (2010) v. 31, No. 2, p. 332-338.
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Last review: 29 September, 2010
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