eugene-a-permyakov
Eugene A Permyakov
Professor of Biophysics

Pushchino State Institute of Natural Sciences
Pushchino, Moscow region, Russia
Phone: +7(495)624-57-49, Fax: +7(4967)33-05-22
E-mail: epermyak@yandex.ru

Education

High School Ivanovo, USSR 1964
Graduate Equivalent of Masters degree in science Moscow Institute of Physics and Technology 1970
Ph.D. Biophysics Moscow Institute of Physics and Technology 1976
Doctor of Sciences Biophysics Moscow State University 1988

Biography

Dr. Permyakov obtained a doctorate (Ph.D.) in physics and mathematics from the Moscow Institute of Physics and Technology and defended a doctor dissertation (Doctor of Sciences) in biology in Moscow State University. Previously he worked in the Institute of Theoretical and Experimental Biophysics (Russia), Ohio State University (USA) and Denver University (USA). Currently Dr. Permyakov is a director of the Institute for Biological Instrumentation (Russia). He has published 10 monographs and more than 160 articles. 


Research Interest

  • Metal Binding Proteins
  • Protein Physics
  • Luminescence (Fluorescence, Phosphorescence)
  • Spectroscopy of Proteins
  • Scanning and Titration Calorimetry of Proteins.

Scientific Activities

Employment History
1970-1990 Institute of Biological Physics, USSR Academy of Sciences, Pushchino, Moscow region 142292, USSR; junior researcher, senior researcher. Development of intrinsic protein luminescence method. Photophysics and protein physics. Fast intramolecular dynamics of proteins. Studies of structural, physico-chemical and functional properties of calcium-binding proteins (parvalbumins, a-lactalbumin, calmodulin, troponin C, and so on).
1990-1991 Department of Chemistry, The Ohio State University, Columbus, Ohio 43210 USA; visiting researcher in the lab of Prof. L.J.Berliner. Zn2+ binding to a-lactalbumin and effects of the Zn2+ binding on lactose synthase activity.
1993 Department of Chemistry, The Ohio State University, Columbus, Ohio 43210 USA; visiting researcher in the lab of Prof. L.J. Berliner. Interactions of a-lactalbumin and galactosyltransferase with lipids; intermediate states of a-lactalbumin.
1994-2004 Short visits (for one to two months) to the lab of Prof. L.J. Berliner in Department of Chemistry, The Ohio State University, Columbus, Ohio, USA; Denver University, Denver, Colorado, USA and to the lab of Prof. A. Fink in Depatrment of Chemistry and Biochemistry, University of California in Santa Cruz, Santa Cruz, California, USA. Studies of physico-chemical properties of metal binding proteins, lectureship.
1991-1996 Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow region 142292, Russia. Leading researcher. Physico-chemical properties of calcium binding proteins. Low temperature luminescence of proteins.
1994 - present time Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow region 142292, Russia. Director. Manager of the Laboratory of New Methods in Biology. Professor of Biophysics. Kinetics of peptide synthesis in solution. Microcalorimetry and luminescence spectroscopy. Physico-chemical and functional properties of Ca-binding proteins. Development of new instruments for physico-chemical biology. Lectures for undergraduate and postgraduate students.
2003 – present time The dean of the Faculty of Biomedical Engineering of the Pushchino State Institute of Natural Sciences. Lectureship in physico-chemical biology.
2000 – 2016 Vice-President of the Pushchino Research Center of the Russian Academy of Sciences.
Professional Activities

Membership in Scientific societies and organizations: Member of Russian Biochemical Society.


Publications

  1. Permyakov, E.A., Busel, E.P., and Burstein, E.A. Luminescence and state of indole derivatives in frozen water-salt solutions. J. Struct. Chem. (Moscow) vol. 12, N 1, p. 79-86, 1971.
  2. Yumakova, E.M., Atanasov, B.P., Burstein, E.A., and Permyakov E.A. pH-induced conformational changes of native state of myoglobin derivatives. Spectrofluorimetric study. In "Conformational Changes of Biopolymers in Solution" Nauka, Moscow, 1973.
  3. Permyakov, E.A., and Burstein, E.A. Relaxation processes in frozen aqueous solutions of proteins. Temperature dependence of fluorescence parameters. Studia Biophysica, vol. 51, N 1, p. 91-103, 1975.
  4. Burstein, E.A., Permyakov, E.A., Emelyanenko, V.I., Bushueva, T.L., and Pechere, J.F. Investigation of some physico-chemical properties of parvalbumins by means of luminescence of their phenylalanine residues. Biochim. Biophys. Acta, vol. 400, N 1, p. 1-16, 1975.
  5. Bukolova-Orlova, T.G., Permyakov, E.A., Burstein, E.A., and Yukelson, L.Y. Reinterpretation of luminescence properties of neurotoxines from the venom of middle-asian cobra Naja oxiana Eichw. Biochim. Biophys. Acta, vol. 439, N 2, p. 426-431, 1976.
  6. Permyakov, E.A., Burstein, E.A., Sawada, Y., and Yamazaki, Y. Luminescence of phenylalanine residues in superoxide dismutase from green pea. Biochim. Biophys. Acta, vol. 491, N 1, p. 149-154, 1977.
  7. Burstein, E.A., Permyakov, E.A., Yashin, V.A., Burkhanov, S.A., and Finazzi-Agro, A. The fine structure of luminescence spectra of azurin. Biochim. Biophys. Acta, vol. 491, N 1, p. 155-159, 1977.
  8. Permyakov, E.A., and Burstein, E.A. Relaxation processes in frozen aqueous protein solutions. Effects of water isotopic composition and of chromophore localization on relaxation freezing. Studia Biophysica, vol. 64, N 1, p. 163-172, 1977.
  9. Permyakov, E.A., and Burstein, E.A. Fast relaxation processes in protein powders. Effect of water content on the temperature dependence of protein fluorescence spectrum position. Studia Biophysica, vol. 64, N 1, p. 83-93, 1977.
  10. Burstein, E.A., Burkhanov, S.A., and Permyakov, E.A. On functional role of parvalbumins in regulation of Ca(II) in the contraction-relaxation cycle in vertebrata skeletal muscles. Biofizika (Moscow) vol. 22, N 5, p. 946-948, 1977.
  11. Permyakov, E.A. Cooperative freezing of internal mobility of proteins. In: Equilibrium Dynamics of Native Structure of Proteins. Pushchino, p. 83-99, 1977.
  12. Burstein, E.A., Bushueva, T.L., and Permyakov, E.A. Study of equilibrium structural mobility of macromolecules by characteristics of protein chromophores luminescence. Zhurnal Prikladnoi Spektroskopii, vol. 28, N 4, p. 653-657, 1978.
  13. Burkhanov, S.A., Chaply, M.F., Permyakov, E.A., and Burstein, E.A. Contraction-relaxation of glycerized muscle fibers induced by pH changes in the presence of parvalbumins. Biofizika (Moscow) vol. 23, N 4, p. 734-735, 1978.
  14. Permyakov, E.A., Yarmolenko, V.V., Emelyanenko, V.I., Burstein, E.A., Gerday, C., and Closset, J. Studies of calcium ions binding to whiting parvalbumin by means of changes in parameters of intrinsic protein fluorescence. Biofizika (Moscow) vol. 25, N 3, p. 417-422, 1988.
  15. Permyakov, E.A., Yarmolenko, V.V., Emelyanenko, V.I., Burstein, E.A., Gerday, C., and Closset, J. Fluorescence studies of the calcium binding to whiting (Gadus merlangus) parvalbumin. Eur. J. Biochem. vol. 109, N 1, p. 307-315, 1980.
  16. Permyakov, E.A., and Yarmolenko, V.V. Possible artifacts upon the pH measurements in water solutions of Ca(II)-binding systems.Biofizika (Moscow) vol. 26, N 1, p. 134-135, 1981.
  17. Permyakov, E.A., Yarmolenko, V.V., and Korystova, A.A. An evaluation of the Ca(II)-binding constants of troponin-C by means of intrinsic protein fluorescence. Studia Biophysica, vol. 83, N 1, p. 63-70, 1981.
  18. Permyakov, E.A., Yarmolenko, V.V., Kalinichenko, L.P., Morozova, L.A., and Burstein, E.A. Calcium binding to -lactalbumin: structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes. Biochem. Biophys. Res. Commun. vol. 100, N 1, p. 191-197, 1981.
  19. Permyakov, E.A., Kalinichenko, L.P., Morozova, L.A., Yarmolenko, V.V., and Burstein, E.A. -lactalbumin binds magnesium ions: study by means of intrinsic fluorescence technique. Biochem. Biophys. Res. Commun. vol. 102, N 1, p. 1-7, 1981.
  20. Permyakov, E.A., Yarmolenko, V.V., Kalinichenko, L.P., and Burstein, E.A. Evaluation of constants of Ca(II) ion binding to proteins by changes of their intrinsic tyrosine and phenylalanine fluorescence. Bioorganicheskaia khimia (Moscow), vol. 7, N 11, p. 1660-1668, 1981.
  21. Permyakov, E.A., Kalinichenko, L.P., Yarmolenko, V.V., Burstein, E.A., and Gerday, C. Binding of nucleotides to parvalbumins. Biochem. Biophys. Res. Commun. Vol. 105, N 3, p. 1059-1065, 1982.
  22. Permyakov, E.A., Yarmolenko, V.V., Burstein, E.A., and Gerday, Ch. Intrinsic fluorescence spectra of a tryptophan-containing parvalbumin as a function of thermal, pH and urea denaturation. Biophys. Chemistry vol. 15, N 1, p. 19-26, 1982.
  23. Permyakov, E.A., Yarmolenko, V.V., Kalinichenko, L.P., Morozova, L.A., and Burstein, E.A. Calcium binding to -lactalbumin from cow milk. Study by changes of intrinsic protein fluorescence. Biofizika (Moscow), vol. 27, N 3, p. 380-385, 1982.
  24. Permyakov, E.A., Kalinichenko, L.P., Morozova, L.A., Yarmolenko, V.V., and Burstein, E.A. Study of Mg(II) binding to -lactalbumin by fluorescence spectroscopy method. Biofizika (Moscow), vol. 27, N 4, p. 578-584, 1982.
  25. Yarmolenko, V.V. Permyakov, E.A., Kalinichenko, L.P., Morozova, L.A., Burstein, E.A., and Vaitkus, V. Calcium ion binding to -lactalbumin from cow milk. In: Proceedings of Lithuanian branch of All-Union Inst. of Dairy Industry, vol. 16, p. 134-140, Mokslas, Vilnius, 1982.
  26. Permyakov, E.A., Burstein, E.A., Emelyanenko, V.I., Aleksandrov, Y.M., Glagolev, K.V., Makhov, V.N., Syreishchikova, T.N., and Yakimenko, M.N. Effects of calcium binding on decay time of intrinsic fluorescence of Ca-binding proteins. Biofizika (Moscow), vol. 28, N 3, p. 393-397, 1983.
  27. Permyakov, E.A., and Shnyrov, V.L. A spectrofluorimetric study of the environment of tryptophans in bacteriorhodopsin. Biophys. Chem. vol. 18, N 1, p. 145-152, 1983.
  28. Morozova, L.A., Permyakov, E.A., and Burstein, E.A. Properties of -lactalbumin as a metal-binding protein. In: Physico-Chemical Basis of Cell Functioning. Pushchino, p. 16-21, 1983.
  29. Permyakov, E.A., Medvedkin, V.N., Kalinichenko, L.P., and Burstein, E.A. Comparative study of physico-chemical properties of two pike parvalbumins by means of their intrinsic tyrosyl and phenylalanyl fluorescence. Arch. Biochem. Biophys. vol. 227, N 1, p. 9-20, 1983.
  30. Permyakov, E.A., Kalinichenko, L.P., Medvedkin, V.N., Burstein, E.A., and Gerday, C. Sodium and potassium binding to parvalbumins measured by means of intrinsic protein fluorescence. Biochim. Biophys. Acta, vol. 749, N 1, p. 185-191, 1983.
  31. Permyakov, E.A., and Burstein, E.A. Evaluation of parameters of binding of low molecular mass compounds to proteins by luminescence method. In: Luminescence Analysis in Medical and Biological Studies. Riga, p. 80-85, 1983.
  32. Permyakov, E.A., and Burstein, E.A. Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence. Biophys. Chem. vol. 19, N 3, p. 265-271, 1984.
  33. Zakharova, N.I., Permyakov, E.A., Fabian, M., Kononenko, A.A., Chamorovski, S.K., Burstein, E.A., and Rubin, A.B. On protein fluorescence of photosynthetic reaction centers from Rhodopseudomonas sphaeroides. Mol. Biologia (Moscow), vol. 18, N 3, p. 719-724, 1984.
  34. Permyakov, E.A., Morozova, L.A., and Burstein, E.A. Cation binding effects on the pH, thermal and urea denaturation transitions in -lactalbumin. Biophys. Chem. vol. 21, N 1, p. 21-31, 1985.
  35. Permyakov, E.A., Ostrovski, A.V., Burstein, E.A., Pleshanov, P.G., and Gerday, C. Parvalbumin conformers revealed by steady-state and time-resolved fluorescence spectroscopy. Arch. Biochem. Biophys. vol. 240, N 2, p. 781-791, 1985.
  36. Permyakov, E.A., Shnyrov, V.L., Kalinichenko, L.P., and Orlov, N.Y. Effects of cation binding on the thermal transitions in calmodulin. Biochim. Biophys. Acta, vol. 830, N 2, p. 288-295, 1985.
  37. Oreschkin, E.F., Borissowa, M.A., Permjakow, E.A., Burstein, E.A., und Schnyrow, V.L. Untersuchungen fur Warmedenaturierung von Fleisch mittels Eiweiseigenfluoreszenz und Mikrokalorimetrie. Fleischwirtschaft, vol. 65, N 12, p. 1498-1500, 1985.
  38. Oreshkin, E.F., Borisova, M.A., Tchubarova, G.S., Gorbatov, V.M., Permyakov, E.A., Shnyrov, V.L., and Burstein, E.A. Conformational changes in the muscle proteins of cured beef during heating. Meat Science, vol. 16, N 4, p. 297-305, 1986.
  39. Permyakov, E.A., Kalinitschenko, L.P., Borissowa, M.A., and Oreschkin, E.F. Vergleichende Untersuchungen der Fluoreszenz von Fleisch und Eiweisen des Actomyosin-komplexes. Fleischwirtschaft, vol. 66, N 3, p. 406-407, 1986.
  40. Permyakov, E.A., and Kreimer, D.I. Effects of pH, temperature and Ca(II) content on the conformation of -lactalbumin in a medium modeling physiological conditions. Gen. Phys. Biophys. vol. 5, N 4, p. 377-390, 1986.
  41. Shnyrov, V.L., Salia, C.H., Zhadan, G.G., and Permyakov, E.A. Thermal transitions in rat erythrocyte ghosts. Biomed. Biochim. Acta vol. 45, N 9, p. 1111-1119, 1986.
  42. Medvedkin, V.N., Mitin, Y.V., and Permyakov, E.A. Effects of Arg-74 on formation of the structure of the C-terminal domain of pike parvalbumin III. Bioorg. Khimia, vol. 13, N 2, p. 177-182, 1987.
  43. Kube, D., Shnyrov, V.L., Permyakov, E.A., Ivanov, M.V., and Nagradova, N.K. Interrelationship between thermostability of tetrameric molecule of lactatdehydrogenase from pork muscle and filling of its active sites by ligands. Biokhimia, vol. 52, N 7, p. 1116-1125, 1987.
  44. Medvedkin, V.N., Mitin, Y.V., and Permyakov, E.A. Preparation of analog of the fragment 74-108 of pike parvalbumin III containing alanine residue in position 74 and of its acetylated derivative. Bioorg. Khimia, vol. 13, N 8, p. 1019-1023, 1987.
  45. Permyakov, E.A. Muscle sarcoplasmic calcium-binding proteins. In: Structure and Functions of Proteins of Contractile Systems. Nauka, Leningrad, p. 159-167, 1987.
  46. Permyakov, E.A., Ostrovski, A.V., and Kalinichenko L.P. Stopped-flow kinetic studies of Ca(II) and Mg(II) dissociation in cod parvalbumin and bovine -lactalbumin. Biophys. Chem., vol. 28, N 2, p. 225-233, 1987.
  47. Permyakov, E.A., Murakami, K., and Berliner, L.J. On experimental artifacts in the use of metal ion chelators for the determination of the cation binding constants of -lactalbumin. A reply. J. Biol. Chem. vol. 268, N 7, p. 3196-3198, 1987.
  48. Permyakov, E.A., Ostrovsky, A.V., Kalinichenko, L.P., Deikus, G.Y. Kinetics of dissociation of complexes of parvalbumin with calcium and magnesium ions. Mol. Biol. (Moscow) vol. 21, N 4, 1987.
  49. Muronets, V.I., Ashmarina, L.I., Permyakov, E.A., and Nagradova N.K. Fluorimetric study of immobilized yest D-glyceraldehyde-3-phosphatedehydrogenase and its subunits. The binding of NAD+. Proceedings of the USSR Academy of Sci., vol. 293, N 3, p. 732-736, 1987.
  50. Lakizova, I.Y., Elyakova, L.A., Emelyanenko, V.I., Permyakov, E.A., and Burstein, E.A. Comparative study of  -1,3-glucanases of scallops by tryptophan fluorescence. Biofizika (Moscow) vol. 33, N 1, p. 31-35, 1988.
  51. Permyakov, E.A., Kreimer, D.I., Kalinichenko, L.P., and Shnyrov, V.L. Interactions of calcium binding proteins, parvalbumin and -lactalbumin, with dipalmitoylphosphatidyl choline vesicles. Gen. Phys. Biophys. vol. 7, N 1, p. 95-107, 1988.
  52. Salia, C.K., Zhadan, G.G., Permyakov, E.A., and Shnyrov, V.L. Effects of pH and concentration of buffer solution on thermal denaturation of rat erythrocyte ghosts. Proc. Acad. Sci. Georgian SSR (Tbilisi) vol. 14, N 1, p. 57-61, 1988.
  53. Shnyrov, V.L., Freidina, N.A., and Permyakov, E.A. Study of pH- and temperature-induced transitions in F-protein (phosphofructokinase) by spectroscopy and microcalorimetry methods. Biochim. Biophys. Acta, vol. 953, N 1, p. 128-133, 1988.
  54. Morozova, L.A., Gusev, N.B., Shnyrov, V.L., and Permyakov, E.A. Studies of physico-chemical properties of troponins I and T from cardiac and skeletal muscles by intrinsic protein fluorescence and calorimetry methods. Biokhimia (Moscow), vol. 53, N 4, p. 531-540, 1988.
  55. Permyakov, E.A., Ostrovski, A.V., and Kalinichenko, L.P. Kinetics of dissociation of complexes of -lactalbumin with Ca(II) and Mg(II) ions. Biofizika (Moscow) vol. 33, N 3, p. 413-416, 1988.
  56. Permyakov, E.A., Kreimer, D.I., Kalinichenko, L.P., and Shnyrov, V.L. Effects of calcium and magnesium ions on interactions of calcium binding proteins parvalbumin and α-lactalbumin with dipalmitoylphosphatidylcholine vesicles. Biofizika (Moscow) vol. 33, N 3, p. 465-470, 1988.
  57. Ostrovsky, A.V., Kalinichenko, L.P., Emelyanenko, V.I., Klimanov, A.V., and Permyakov, E.A. Environment of tryptophan residues in various conformational states of -lactalbumin studied by time-resolved and steady-state fluorescence spectroscopy. Biophys. Chem. vol. 30, N 1, p. 105-115, 1988.
  58. Permyakov, E.A., Kalinichenko, L.P., Morozova, L.A., Derezhkov, V.Y., Bagelova, Y., and Antalik, M. Interactions of copper and zinc cations with calcium binding proteins. Mol. Biologia (Moscow) vol. 22, N 4, p. 984-991, 1988.
  59. Permyakov, E.A., and Tskhovrebova, L.A. Effects of temperature and pH on environment of tryptophan residues in -actinin. Biofizika (Moscow) vol. 33, N 5, p. 754-757, 1988.
  60. Permyakov, E.A., Morozova, L.A., Kalinichenko, L.P., and Derezhkov, V.Y. Interaction of -lactalbumin with Cu(II). Biophys. Chem. vol. 32, N 1, p. 37-42, 1988.
  61. Shnyrov, V.L., Levitski, D.I., Vedenkina, N.S., Nikolaeva, O.P., Khvorov, N.V., Permyakov, E.A., and Poglazov, B.F. Domain structure of myosin subfragment 1. Dokl. Akadmii Nauk SSSR (Moscow) vol. 304, N 6, p. 1497-1499, 1989.
  62. Permyakov, E.A., Kreimer, D.I., Kalinichenko, L.P., Orlova, A.A., and Shnyrov, V.L. Interaction of parvalbumins with model phospholipid vesicles. Cell Calcium, vol. 10, N 2, p. 71-79, 1989.
  63. Oreschkin, E.F., Borissowa, M.A., Permjakow, E.A., and Burstein, E.A. Konformationsveranderungen des Muskeleiweises wahrend der Reifung und ihre Beriechung zum Wasserbindungsvermogen von Schweinefleisch. Fleischwirtschaft, vol. 69, N 4, p. 627-630, 1989.
  64. Permyakov, E.A., Medvedkin, V.N., Korneichuk, G.A., Kostrzhevskaia, E.G., and Murzin, A.G. Binding of melittin to parvalbumin inhibited by Ca(II) ions. New function for parvalbumin. Mol. Biologia (Moscow) vol. 23, N 3, p. 693-698, 1989.
  65. Burstein, E.A., Nyamaa, D., Bat-Erdene, O., Enkhzaya, D., Burgetbazar, B., Emelyanenko, V.I., and Permyakov, E.A. An interaction of albumin from camel serum with fraxetin. Studia Biophysica, vol. 135, N 1, p. 15-24, 1990.
  66. Levitsky, D.I., Khvorov, N.V., Shnyrov, V.L., Vedenkina, N.S., Permyakov, E.A., and Poglazov, B.F. Domain structure of myosin subfragment-1. Selective denaturation of the 50 kDa segment. FEBS Letters, vol. 264, N 2, p. 176-178, 1990.
  67. Shnyrov, V.L., Vedenkina, N.S., Ostrovski, A.V., Permyakov, E.A., Golitsyna, N.L., and Levitski, D.I. Study of the thermal denaturation of myosin rod by microcalorimetry and intrinsic fluorescence methods. Biofizika (Moscow), vol. 35, N 3, p. 415-420, 1990.
  68. Permyakov, E.A., Medvedkin, V.N., Mitin, Y.V., and Kretsinger, R.H., Noncovalent complex between domain AB and domains CD*EF of parvalbumin. Biochim. Biophys. Acta, vol. 1076, p.67-70, 1991.
  69. Musatov, A., Permyakov, E.A., Bagelova, J., Morozova, L., and Shnyrov, V.L. Some aspects of fluorescence and microcalorimetric studies of cytochrome C oxidase. Biochem. Int. vol. 21, p. 563-571, 1990.
  70. Permyakov, E.A., Grishchenko, V.M., Kalinichenko, L.P., Orlov, N.Y., Kuwajima, K., and Sugai, S. Calcium-regulated interactions of human -lactalbumin with bee venom melittin. Biophys. Chem. vol. 39, p. 111-117, 1991.
  71. Vedenkina, N.S., Abramyan, A.A., Bagdasaryan, Z.N., Shnyrov, V.L. and Permyakov, E.A. The binding of copper and zinc ions to aminoacylase from Aspergillus oryzae. Biokhimia (Moscow) vol. 56, N 3, p. 500-507, 1991.
  72. Czurylo, E.A., Emelyanenko, V.I., Permyakov, E.A., and Dabrowska, R. Spectrofluorimetric studies on C-terminal 34 kDa fragment of caldesmon. Biophys. Chem. vol. 40, N 2, p. 181-188, 1991.
  73. Morozova, L.A., Shnyrov, V.L., Gusev, N.B., and Permyakov, E.A. Thermal transitions in cardiac troponin and its subunits. In NATO ASI Series, vol. H 56, Cellular Regulation by Protein Phosphorylation, Edited by L.M.G. Heilmeyer, Jr. Springer Verlag, Berlin, Heidelberg, p. 67-71, 1991.
  74. Levitsky, D.I., Khvorov, N.V., Shnyrov, V.L., Bukatina, A.E., Vedenkina, N.S., Permyakov, E.A., and Poglazov, B.F. Nucleotide-induced changes in domain structure of myosin subfragment 1. In Muscle and Motility (ed. G. Marshal, U. Carraro) Intercept Ltd, London, p. 311-315, 1990.
  75. Levitsky, D.I., Nikolaeva, O.P., Vedenkina, N.S., Shnyrov, V.L., Golitsina, N.L., Khvorov, N.V., Permyakov, E.A., and Poglazov, B.F. The effect of alkali light chains on the thermal stability of myosin subfragment 1. Biomed. Sci., vol. 2, N 2, p. 140-146, 1991.
  76. Permyakov, E.A., Shnyrov, V.L., Kalinichenko, L.P., Kuchar, A., Reyzer, I.L., and Berliner, L.J. Binding of Zn(II) ions to -lactalbumin. J. Protein Chem., vol. 10, N. 6, p. 577-584, 1991.
  77. Hirai, Y., Permyakov, E.A., and Berliner, L.J. Proteolytic digestion of -lactalbumin: physiological implications. J. Protein Chem., vol. 11, N 1, p. 51-57, 1992.
  78. Permyakov, E.A., Kalinichenko, L.P., Derezhkov, V.Y., Antalik, M., Meinholtz, D.C., and Berliner, L.J. Interaction of cupric ion with parvalbumin. Biophys. Chem., vol. 42, N 1, p. 189-194, 1992.
  79. Bakunina, I.Y., Sova, V.V., Elyakova, L.A., Makaryeva, T.N., Stonik, V.A., Permyakov, E.A., and Emelyanenko, V.I. Effects of polyhydroxysteroid sulfates on endo- and exoglucanases. Biokhimia (Moscow), vol. 56, N 8, 1397-1405, 1991.
  80. Levitsky, D.I., Shnyrov, V.L., Khvorov, N.V., Bukatina, A.E., Vedenkina, N.S., Permyakov, E.A., Nikolaeva, O.P., and Poglazov, B.F. Effects of nucleotide binding on thermal transitions and domain structure of myosin subfragment 1. Eur. J. Biochem. vol. 209, p. 829-835, 1992.
  81. Shnyrov, V.L., Lubsandorzhieva, V.C., Zhadan, G.G., and Permyakov, E.A. Multi-stage nature of the thermal denaturation process in collagen. Biochem. Int. vol. 26, N 1, p. 211-217, 1992.
  82. Leontiev, V.V., Uversky, V.N., Permyakov, E.A., and Murzin, A.G. Introduction of Ca2+-binding amino acid sequence into the T4 lysozyme. Biochim. Biophys. Acta vol. 1162, N 1-2, p. 84-88, 1993.
  83. Permyakov, E.A., Reyzer, I.L., and Berliner, L.J. Effects of Zn(II) on galactosyl transferase activity. J. Prot. Chem. vol. 12, N 5, p. 633-638, 1993.
  84. Medvedkin, V.N., Permyakov, E.A., Uversky, V.N., Gripas', A.F., and Mitin, Yu.V. A quartz reactor-cuvette for fluorescent monitoring of the solid phase peptide synthesis. Bioorg. Chem. (in Russian) vol. 20, N 6, p. 635-643, 1994.
  85. Permyakov, E.A., and Berliner, L.J. Co2+-binding to -lactalbumin. J. Prot. Chem. vol. 13, N 3, p. 277-281, 1994.
  86. Permyakov, E.A., Medvedkin, V.N., Klimenko, L.V., Mitin, Y.V., and Permyakov, S.E. Kinetics of peptide synthesis studied by fluorescence of fluorophenyl esters. Int. J. Peptide Protein Res. vol. 44, N 1, p. 472-476, 1994.
  87. Permyakov, E.A., Deikus, G.Y. Analytical description of electron-vibrational spectra of proteins. Mol. Biol. (Moscow) vol. 29, N 1, p. 159-167, 1995.
  88. Permyakov, E.A., Deikus, G.Y. Monitoring conformational changes in proteins by means of low temperature fluorescence and phosphorescence spectroscopy. Mol. Biol. (Moscow) vol. 29, N 2, p. 339-344, 1995.
  89. Vedenkina, N.S., Kalinichenko, L.P., and Permyakov, E.A. Effects of falloidin on stability of F- and G-actin. Mol. Biol. (Moscow) vol. 29, N 3, p. 597-602, 1995.
  90. Medvedkin, V.N., Permyakov, E.A., Klimenko, L.V., Mitin, Y.V., Matsushima, N., Nakayama, S. and Kretsinger, R. Interactions of (AlaAlaLysPro)n and (LysLysSerPro)n with DNA. Proposed coiled coil of AlgR3 and AlgP from Pseudomonas Aeruginosa. Prot. Eng. v. 8, N 1, p. 63-70, 1995.
  91. Medvedkin, V.N., Zabolotskikh, V.F., Permyakov, E.A., Mitin, Y.V., Sorokina, M.N., and Klimenko, L.V. p-sulfotetrafluorophenyl hydrophobic active esters of amino acids in peptide synthesis. Bioorg. Chimia. (Moscow) v. 21, N 9, p. 684-690, 1995.
  92. Grishchenko, V.M., Kalinichenko, L.P., Deikus, G.Y., Veprintsev, D.B., Cawthern, K.M., Berliner, L.J., Permyakov, E.A. Interactions of -lactalbumin with lipid vesicles studied by tryptophan fluorescence. Biochem. Mol. Biol. Internat. v. 38, N 3, p. 453-466, 1996.
  93. Cawthern, K.M., Permyakov, E.A., and Berliner, L.J. Membrane-bound states of -lactalbumin: implications for the protein stability and conformation. Protein Sci. v. 5, N 7, p. 1394-1405, 1996.
  94. Veprintsev, D.B., Permyakov, E.A., Kalinichenko, L.P., and Berliner, L.J. Pb2+ and Hg2+ binding to -lactalbumin. Biochem. Mol. Biol. Internat. v. 39, N 6, p. 1255-1265, 1996.
  95. Todorova, R.T., Rogov, V.V., Vasilenko, K.S., and Permyakov, E.A. Study of tyrosine-containing mutants of ribosomal protein L7/L12 from Escherichia coli. Biophys. Chem. v. 62, N 1-3, p. 39-46, 1996.
  96. Permyakov, E.A., Veprintsev, D.B., Deikus, G.Y., Permyakov, S.E., Kalinichenko, L.P., Grishchenko, V.M., and Brooks, C.L. pH-induced transition and Zn2+-binding properties of bovine prolactin. FEBS Letters v. 405, N 3, p. 273-276, 1997.
  97. Veprintsev, D.B., Permyakov, S.E., Permyakov, E.A., Rogov, V.V., Cawthern, K.M., and Berliner, L.J. Cooperative thermal transitions of bovine and human apo--lactalbumins: evidence for a new intermediate state, FEBS Letters, v. 412, N 3, p. 625-628, 1997.
  98. Shnyrov,V.L., Sanchez-Ruiz,J.M., Boiko, B.N., Zhadan, G.G., and Permyakov, E.A. Applications of scanning microcalorimetry in biophysics and biochemistry. Thermochim. Acta, v. 302, N. 1-2, p. 165-180, 1997.
  99. Cawthern,K.M., Narayan,M., Chaudhuri,D., Permyakov,E.A., and Berliner,L.J. Interactions of -lactalbumin with fatty acids and spin label analogs. J. Biol. Chem. 1997, v. 272, N 49, p. 30812-30816.
  100. Cawthern, K.M., Anderson, P.J., Permyakov, E.A., and Berliner, L.J. Interaction of N-acetylglucosamine-β(1-4)-galactosyltransferase with liposomes. Period. Biol., Vol. 100, Suppl. 2, p. 53-58, 1998.
  101. Veprintsev, D.B., Narayan, M., Permyakov, S.E., Uversky, V.N., Brooks, C.L., Cherskaya, A.M., Permyakov, E.A., and Berliner, L.J. Fine tuning of the N-terminus of a calcium binding protein: -lactalbumin. Proteins, Vol. 37, N. 1, p. 65-72, 1999.
  102. Permyakov, S.E., Senin, I.I., Uversky, V.N., Cherskaya, A.M., Shulga-Moskoy, S.V., Zinchenko, L.V., Alexeev, A.M., Zargarov, A.A., Lipkin, V.M., Philippov, P.P., and Permyakov, E.A. Site-directed amino acid substitutions in the Ca2+-binding sites of recoverin. I. Mechanism of sequential filling of the Ca2+-binding sites. Bioorg. Chem. (Moscow) Vol. 25, N 10, p. 749-753, 1999.
  103. Uversky, V.N., Gillespie, J.R., Millett, I.S., Khodyakova, A.V., Vasilenko, R.N., Vasiliev, A.M., Rodionov, I.L., Kozlovskaya, G.D., Dolgikh, D.A., Fink, A.L., Doniach, S., Permyakov, E.A., Abramov, V.M. Zn2+-mediated structure formation and compaction of the “natively unfolded” human prothymosin α. Biochem. Biophys. Res. Commun. 267, 663-668, 2000.
  104. Permyakov, E.A., and Berliner, L.J. -Lactalbumin: structure and function. FEBS Letters, Vol. 473, N 3, p. 269-274, 2000.
  105. Uversky, V.N., Permyakov, S.E., Senin, I.I., Cherskaya, A.M., Shulga-Moskoy, S.V., Zinchenko, L.V., Alexeev, A.M., Zargarov, A.A., Lipkin, V.M., Philippov, P.P., and Permyakov, E.A. Site-directed amino acid substitutions in the Ca2+-binding sites of recoverin. II. Unusual behavior of the protein upon interaction with Ca2+ ions. Bioorg. Chem. (Moscow) Vol. 26, N 3, p. 173-178, 2000.
  106. Permyakov, S.E., Veprintsev, D.B., Brooks, C.L., Permyakov, E.A., and Berliner, L.J. Zinc binding in bovine -lactalbumin: sequence homology may not be a predictor of subtle functional features. Proteins: Structure, Function, and Genetics, Vol. 40, p. 106-111, 2000.
  107. Permyakov, S.E., Uversky, V.N., Cherskaya, A.M., Shulga-Moskoy, S.V., Zinchenko, L.V., Alexeev, A.M., Zargarov, A.A., Senin, I.I., Lipkin, V.M., Philippov, P.P., and Permyakov, E.A. Site-directed amino acid substitutions in the Ca2+-binding sites of recoverin. III A mutant with the forth reconstructed Ca2+-binding site. Bioorg. Chem. (Moscow) Vol. 26, N 4, p. 285-289, 2000.
  108. Permyakov, S.E., Cherskaya, A.M., Senin, I.I., Zargarov, A.A., Shulga-Moskoy, S.V., Alexeev, A.M., Zinchenko, L.V., Lipkin, V.M., Philippov, P.P., Uversky, V.N., and Permyakov, E.A. Effects of mutations in the calcium-binding sites of recoverin on its calcium affinity: evidence for successive filling of the calcium binding sites. Protein Eng. Vol. 13, N 11, p. 783-790, 2000.
  109. Permyakov, S.E., and Permyakov, E.A. Use of protein engineering methods for studies of calcium-binding proteins. Biofizika (Moscow) Vol. 45, N 6, p. 990-1006, 2000.
  110. Permyakov, E.A., Permyakov, S.E., and Medvedkin, V.N. Kinetics and mechanism of synthesis of peptides in solution. Bioorg. Chem. (Moscow) Vol. 28, N 1, p. 11-15, 2001.
  111. Permyakov, S.E., Oberg, K.A., Cherskaya, A.M., Shavlovsky, M.M., Permyakov, E.A., and Uversky, V.N. Human  -fetoprotein as a Zn2+-binding protein. Tight cation binding is not accompanied by global changes in protein structure and stability. Biochim. Biophys. Acta, V. 62064, p. 1-10, 2001.
  112. Permyakov, S.E., Uversky, V.N., Veprintsev, D.B., Cherskaya, A.M., Brooks, C.L., Permyakov, E.A., and Berliner, L.J. Mutating aspartate in the calcium-binding site of -lactalbumin: effects on the protein stability and cation binding. Protein Eng., Vol. 14, N. 10, p. 785-789, 2001.
  113. Permyakov, E.A., and Freidin, A.A. Progress in the Russian biological instrumentation. Sci. Instrumentation Vol. 11, N. 3, p. 3-11, 2001.
  114. Uversky, V.N., Permyakov, S.E., Zagranichny, V.E., Rodionov, I.L., Fink, A.L., Cherskaya, A.M., Wasserman, L.A., and Permyakov, E.A. Effect of zinc and temperature on the conformation of the  subunit of retinal phosphodiesterase: a natively unfolded protein. J. Proteome Res. Vol. 1, p. 149-159, 2002.
  115. Goers, J., Permyakov, S.E., Permyakov, E.A., Uversky, V.N., and Fink, A.L. Conformational prerequisites for -lactalbumin fibrillation. Biochemistry, Vol. 41, p. 12546-12551, 2002.
  116. Permyakov, S.E., Cherskaya, A.M., Wasserman, L.A., Khokhlova, T.I., Senin, I.I., Zargarov, A.A., Zinchenko, D.V., Zernii, E.Y., Lipkin V.M., Philippov, P.P., Uversky, V.V., and Permyakov, E.A. Recoverin is a zinc-binding protein. J. Proteome Res. Vol. 2, p. 51-57, 2003.
  117. Permyakov, E.A., Permyakov, S.E., Deikus, G.Y., Morozova-Roche, L.A., Grishchenko, V.M., Kalinichenko, L.P., and Uversky, V.N. Ultraviolet illumination-induced reduction of -lactalbumin disulfide bridges. Proteins: Structure, Function, and Genetics, Vol. 51, p. 498-503, 2003.
  118. Permyakov, S.E., Millett, I.S., Doniach, S., Permyakov, E.A., and Uversky, V.N. Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. Proteins: Structure, Function, and Genetics, Vol. 53, p. 855-862, 2003.
  119. Permyakov, E.A., Permyakov, S.E., and Berliner, L.J. -Lactalbumin: Ca2+ binding protein with multiple functions. In Protein Structures: Kaleidoscope of Structural Properties and Functions, Research Singpost, Kerala, India, Ed. V.N. Uversky, p. 457-497, 2003.
  120. Permyakov, S.E., Pershikova, I.V., Khokhlova, T.I., Uversky, V.N., and Permyakov, E.A. No need to be HAMLET or BAMLET to interact with histones: binding of monomeric -lactalbumin to histones and basic poly-amino acids. Biochemistry, Vol. 43, N 19, p. 5575-5582, 2004.
  121. Permyakov, S.E., Pershikova, I.V., Zhadan, A.P., Goers, J., Bakunts, A.G., Uversky, V.N., Berliner, L.J., and Permyakov, E.A. Conversion of human -lactalbumin to an apo-like state in the complexes with basic poly-amino acids: toward understanding of the molecular mechanism of antitumor action of HAMLET. J. Proteome Res. Vol 4, N 2, p. 564-569, 2005.
  122. Permyakov, E.A. Innovation activity in Pushchino Research Center of RAS. Innovations (Moscow) Vol. 3, N 80, 25-29, 2005.
  123. Permyakov, E.A. The use of nanotechnologies in molecular and cellular biophysics. Nanotechnics, Vol. 2, p. 78-83, 2005.
  124. Permyakov, S.E., Makhatadze, G.I., Owenius, R., Uversky, V.N., Brooks, C.L., Permyakov, E.A., and Berliner, L.J. How to improve nature: study of the electrostatic properties of the surface of α-lactalbumin. Protein Eng. Design and Selection, Vol. 18, N 9, p. 425-433, 2005.
  125. Permyakov, S.E., Khokhlova, T.I., Nazipova, A.A., Zhadan, A.P., Morozova-Roche L.A., and Permyakov, E.A. Calcium-binding and temperature induced transitions in equine lysozyme: new insights from the pCa-temperature "phase diagrams". Proteins Vol. 65, N 4, p. 984-998, 2006.
  126. Permyakov, S.E., and Permyakov, E.A. The use of the free metal – temperature ‘phase diagrams’ for studies of single site metal binding proteins. Protein J. Vol. 26, N 1, p. 1-12, 2006.
  127. Weiergraber, O.H., Senin, I.I., Zernii, E.Y., Churumova, V.A., Kovaleva, N.A., Nazipova, A.A., Permyakov, S.E., Permyakov, E.A., Philippov, P.P., Granzin, J., and Koch, K.W. Tuning of a neuronal calcium sensor. J. Biol. Chem. Vol. 281, N 49, p. 37594-37602, 2006.
  128. Permyakov, E.A. The use of physical methods in studies of neuronal calcium sensor proteins. In Neuronal Calcium Sensor Proteins, Eds. P. Philippov, K. Koch, Nova Science Publishers, p. 331-349, 2006.
  129. Permyakov, S.E., Nazipova, A.A., Denesyuk, A.I., Bakunts, A.G., Zinchenko, D.V., Lipkin, V.M., Uversky, V.N., and Permyakov, E.A. Recoverin as a redox-sensitive protein. J. Proteome Res. Vol. 6, p. 1855-1863, 2007.
  130. Permyakov, E.A. Tryptophan phosphorescence of proteins. In Methods in Protein Structure and Stability Analysis. Part A. Luminescence Spectroscopy and Circular Dichroism. Nova Biomedical Books, New York, V.N. Uversky & E.A. Permyakov, eds. p. 201-236, 2007.
  131. Permyakov, E.A. Studies of metal binding proteins by intrinsic luminescence method. In Methods in Protein Structure and Stability Analysis. Part A. Luminescence Spectroscopy and Circular Dichroism. Nova Biomedical Books, New York, V.N. Uversky & E.A. Permyakov, eds. p. 257-288, 2007.
  132. Permyakov, S.E., Bakunts, A.G., Denesyuk, A.I., Knyazeva, E.L., Uversky, V.N., and Permyakov, E.A. Apo-parvalbumin as an intrinsically disordered protein. Proteins, Vol. 72, p. 822-836, 2008.
  133. Permyakov, E.A. The use of protein engineering methods for studies of calcium binding proteins. In Methods in Protein Structure and Stability Analysis. Part D. NMR and EPR Spectroscopies, Mass-Spectrometry and Protein Imaging. Nova Science Publishers, New York, V.N. Uversky & E.A. Permyakov, eds. 319-350, 2008.
  134. Permyakov, S.E., Karnoup A.S., Bakunts, A.G., and Permyakov, E.A. Sequence microheterogeneity of parvalbumin pI 5.0 of pike: A mass spectrometric study. Biochim. Biophys. Acta, 2008, 1794, 129-136.
  135. Permyakov, E.A., and Kretsinger, R.H. Cell Signaling, Beyond Cytosolic Calcium in Eukaryotes. J. Inorg. Biochem. 2009, 103, 77-86.
  136. Knyazeva, E.L., Grishchenko, V.M., Fadeev, R.S., Akatov, V.S., Permyakov, S.E., and Permyakov, E.A. Who Is Mr. HAMLET? Interaction of human α-lactalbumin with monomeric oleic acid. Biochemistry, 2008, 47, 49, 13127-13137.
  137. Zherelova, O.M., Kataev, A.A., Grishchenko, V.M., Knyazeva, E.L., Permyakov, S.E., and Permyakov, E.A. Interaction of antitumor α-lactalbumin-oleic acid complexes with artificial and natural membranes. J. Bioenerg. Biomembr. 2009, 41, 3, 229-237.
  138. Permyakov, S.E., Bakunts, A.G., Permyakova, M.E., Denesyuk, A.I., Uversky, V.N., and Permyakov, E.A. Metal-controlled interdomain cooperativity in parvalbumins. Cell Calcium, 2009, 46, 163-175.
  139. Permyakov, S.E., Khokhlova, T.I., Uversky, V.N., and Permyakov, E.A. Analysis of Ca2+/Mg2+ selectivity in α-lactalbumin and Ca2+-binding lysozyme reveals a distinct Mg2+-specific site in lysozyme. Proteins, 2010, 78, 2609-2624.
  140. Permyakov, E.A., Uversky, V.N. Fluorescence spectroscopy of intrinsically disordered proteins. In: Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA., 2010, pp. 323-344.
  141. Zernii, E., Komolov, K., Permyakov, S., Kolpakova, T., Dell Orco, D., Poetzsch, A., Knyazeva, E., Grigoriev, I., Permyakov, E., Senin, I., Philippov, P., and Koch, K.W. Involvement of recoverin C-terminal segment in recognition of the target enzyme rhodopsin kinase. Biochem. J. 2011, 435, 2, 441-450;; PMID: 21299498.
  142. Permyakov, S.E., Zernii, E.Y., Knyazeva, E.L., Denesyuk, A.I., Nazipova, A.A., Kolpakova, T.V., Zinchenko, D.V., Philippov, P.P., Permyakov, E.A., Senin, I.I. Oxidation mimicking substitution of conservative cysteine in recoverin suppresses its membrane association. Amino Acids, 2011, PMID: 21344177.
  143. Permyakov, S.E., Ismailov, R.G., Xue, B., Denesyuk, A.I., Uversky, V.N., and Permyakov, E.A. Intrinsic disorder in S100 proteins. Mol. BioSyst. 2011, 7, 2164–2180; DOI: 10.1039/C0MB00305K.
  144. Permyakov, S.E., Knyazeva, E.L., Leonteva, M.V., Fadeev, R.S., Chekanov, A.V., Zhadan, A.P., Håkansson, A.P., Akatov, V.S., and Permyakov, E.A. A novel method for preparation of HAMLET-like protein complexes. Biochimie, 2011, 93, 1495-1501; PMID: 21596091.
  145. Permyakov, E.A., and Uversky, V.N. The use of protein engineering methods for studies of calcium binding proteins. In Protein Engineering: Design, Selection and Applications, Nova Science Publishers, Sheehan, M., ed., New York (2011) 163-204.
  146. Permyakov, S.E., Knyazeva, E.L., Khasanova, L.M., Fadeev, R.S., Zhadan, A.P., Roche-Hakansson, H., Håkansson, A.P., Akatov, V.S., and Permyakov, E.A. Oleic acid is a key cytotoxic component of HAMLET-like complexes. Biol Chem. 2012, 393, 85-92; PMID: 22124270.
  147. Permyakov, S.E., Vologzhannikova, A.A., Emelyanenko, V.I., Knyazeva, E.L., Kazakov, A.S., Lapteva, Y.S., Permyakova, M.E., Zhadan, A.P., and Permyakov, E.A. The impact of alpha-N-acetylation on structural and functional status of parvalbumin. Cell Calcium (2012) 52, 5, 366-376.
  148. Permyakov, E.A. The use of UV-Vis absorption spectroscopy for studies of natively disordered proteins. Methods Mol. Biol. (2012) 895, 421-433.
  149. Nemashkalova, E.L., Kazakov, A.S., Khasanova, L.M., Permyakov, E.A., and Permyakov, S.E. Structural characterization of more potent alternatives to HAMLET, a tumoricidal complex of α-lactalbumin and oleic acid. Biochemistry (2013) DOI: 10.1021/bi400643s.
  150. Permyakov, S.E., Kazakov, A.S., Avkhacheva, N.V., and Permyakov, E.A. Parvalbumin as a metal-dependent antioxidant. Cell Calcium (2014) 55, 5, 261-268 dx.doi.org 10.1016 j.ceca.2014. 03.001.
  151. Denessiouk, K., Permyakov, S., Denesyuk, A., Permyakov, E., and Johnson, M.S. Two structural motifs within canonical EF-hand calcium binding domains identify five different classes of calcium buffers and sensors. PLoS ONE (2014) 9(10): e109287. doi:10.1371/journal.pone.0109287.
  152. Kaspersen, J.D., Pedersen, J.N., Hansted, J.G., Nielsen, S.B., Sakthivel, S., Wilhelm, K., Nemashkalova, E.L., Permyakov, S.E., Permyakov, E.A., Pinto Oliveira, C.L., Morozova-Roche, L.A., Otzen, D.E., Pedersen, J.S. Generic Structures of Cytotoxic Liprotides: Nano-Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins. Chembiochem 15, 18, 2693-2702. doi: 10.1002/cbic.201402407.
  153. Breydo L., Sales, A.E., Ferreira, L., Fedotoff, O., Shevelyova, M.P., Permyakov, S.E., Kroeck, K.G., Permyakov, E.A., Zaslavsky, B.Y., Uversky, V.N. Analyzing the effect of TMAO on proteins in crowded solutions. Arch. Biochem. Biophys. 2015 570, 66-74. hdx.doi.org/10.1016/j.abb.2015.02.021.
  154. Zernii, E.Y., Nazipova, A.A., Gancharova, O.S., Kazakov, A.S., Serebryakova, M.V., Zinchenko, D.V., Tikhomirova, N.K., Senin, I.I., Philippov, P.P., Permyakov, E.A., Permyakov, S.E. Light-induced disulfide dimerization of recoverin under ex vivo and in vivo conditions, Free Radical Biology and Medicine, 2015 83, 283–295.
  155. Lomonosova, A.V., Ovchinnikova, E.V., Kazakov, A.S., Denesyuk, A.I., Sofin, A.D., Mikhailov, R.V., Ulitin, A.B., Mirzabekov, T.A., Permyakov, E.A., Permyakov, S.E. Extremophilic 50S Ribosomal RNA-binding Protein L35Ae as a Basis for Engineering of an Alternative Protein Scaffold. PloS ONE, 10, 8, e0134906. doi: 10.1371/journal.pone.0134906, 2015.
  156. Permyakov, S.E., Permyakov, E.A., Uversky, V.N. Intrinsically disordered caldesmon binds calmodulin via the “buttons on a string” mechanism. Peer J.. 2015,,3:e1265 https://dx.doi.org/10.7717/pe
  157. Kazakov, A.S., Sokolov, A.S., Rastrygina, V.A., Solovyev, V.V., Ismailov, R.G., Mikhailov, R.V., Ulitin, A.B., Yakovenko, A.R., Mirzabekov, T.A., Permyakov, E.A., Permyakov, S.E. (2015) High-affinity interaction between interleukin-11 and S100P protein. Biochem Biophys Res Commun. pii: S0006-291X(15)30894-9. doi: 10.1016/j.bbrc.2015.11.024.
  158. Kazakov, A.S., Sokolov, A.S., Vologzhannikova, A.A. Permyakova, M.E., Khorn, P.A., Ismailov, R.G., Denessiouk, K.A., Denesyuk, A.I., Rastrygina, V.A., Baksheeva, V.E., Zernii, E.Yu., Zinchenko, D.V., Glazatov, V.V., Uversky, V.N., Mirzabekov, T.A., Permyakov, E.A., Permyakov, S.E. (2015) Interleukin-11 binds specific EF-hand proteins via their conserved structural motif. J. Biomolecular Structure and Dynamics. 8, 1-14; DOI: 10.1080/07391102.2015.1132392.
  159. Permyakov EA, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Uversky VN (2016) Disorder in milk proteins: α-lactalbumin. Part A. Structural properties and conformational behavior. Current Protein & Peptide Science, 17, 4, 352-367.
  160. Uversky VN, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Permyakov EA (2016) Disorder in milk proteins: α-lactalbumin. Part B. A multifunctional whey protein acting as an oligomeric molten globule “oil container” in the anti-tumorogenic drugs, liprotides. Current Proetin Peptide Science 17, 6, 612-628.
  161. Permyakov EA, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Uversky VN (2016) Disorder in milk proteins: α-lactalbumin. Part C. Perularities of metal binding. Current Protein Peptide Science 17, 8, 735-745.
  162. Kazakov AS, Sokolov AS, Vologzhannikova AA Permyakova ME, Khorn PA, Ismailov RG, Denessiouk KA, Denesyuk AI, Rastrygina VA, Baksheeva VE, Zernii EYu, Zinchenko DV, Glazatov VV, Uversky VN, Mirzabekov TA, Permyakov EA, Permyakov SE (2016) Interleukin-11 binds specific EF-hand proteins via their conserved structural motif. J Biomol Structure and Dynamics 8, 1-14 DOI: 10.1080/07391102.2015.1132392.
  163. Permyakov EA, Uversky VN, Permyakov SE (2016) Interleukin-11: a multifunctional cytokine with intrinsically disordered region. Cell Biochem Biophys 74, 3, 285-296.
  164. Sokolov AS, Kazakov AS, Solovyov VV, Ismailov RG, Uversky VN, Lapteva YS, Mikhailov RV, Pavlova EV, Terletskaya IO, Ermolina LV, Permyakov SE, Permyakov EA (2016) Expression, purification and characterization of interleukin-11 orthologues. Molecules 21, 1632, doi: 10.3390/molecules 21121632.
  165. Permyakov EA, Uversky VN, Permyakov SE (2016) Parvalbumin as a pleomorphic protein. Current Protein Peptide Science, 18, 8, 780-794. PMID: 27964700.
  166. Denesyuk AI, Permyakov SE, Johnson MS, Permyakov EA, Denessiouk K (2017) Novel calcium recognition constructions in proteins: Calcium blade and EF-hand zone. Biochem Biophys. Res. Commun. 483, 3, 958-963 doi: 10.1016/j.bbrc.2017.01.040.
  167. Lomonosova AV, Ulitin AB, Kazakov AS, Mirzabekov TA, Permyakov EA, Permyakov SE (2017) Derivative of extremophilic 50S ribosomal Protein L35Ae as an alternative protein scaffold. PLoS ONE, doi:10.1371/ journal.pone.0170349.
  168. Litus EA, Permyakov SE, Uversky VN, Permyakov EA (2017) Intrinsically Disordered Regions in Serum Albumin: What Are They For? Cell Biochem Biophys. doi:10.1007/s12013-017-0785-6
  169. Nemashkalova EL, Permyakov EA, Permyakov SE, Litus EA (2017) Modulation of linoleic acid-binding properties of human serum albumin by divalent metal cations. Biometals DOI 10.1007/s10534-017-0010-5.
Books
  1. Permyakov EA Parvalbumin and Related Calcium Binding Proteins. Nauka, Moscow, 1985, 191 p.
  2. Permyakov EA Calcium Binding Proteins. Nauka, Moscow, 1993, 190 p.
  3. Permyakov EA Luminescent Spectroscopy of Proteins. CRC Press, Boca Raton, Ann Arbor, London, Tokyo, 1993, 164 p.
  4. Permyakov EA The Method of Intrinsic Protein Luminescence. Nauka, Moscow, 2003, 189 p.
  5. Permyakov EA α-Lactalbumin. Nova Science Publishers, New York, 2005, 136 p.
  6. Permyakov EA Parvalbumin. Nova Science Publishers, New York, 2006, 196 p.
  7. Permyakov EA Metalloproteomics. A John Wiley & Sons, Inc., Hoboken, New Jersey, 2009, 786 p.
  8. Permyakov EA and Kretsinger RH Calcium Binding Proteins. A John Wiley & Sons, Inc., Hoboken, New Jersey, 2011, 573 p.
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  10. Permyakov EA, Morozova LA and Berliner LJ Calcium Binding Lysozymes. Nova Science Publishers, New York, 2012.
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