Область прикладного применения результатов научных исследований
медицина
биотехнология
Избранные публикации
1. Permyakov, E.A., Busel, E.P., and Burstein, E.A. Luminescence and state of indole derivatives in frozen watersalt solutions. Zhurnal strukturnoi khimii, (Moscow) vol. 12, N 1, p. 7986, 1971.
2. Yumakova, E.M., Atanasov, B.P., Burstein, E.A., and Permyakov E.A. pHinduced 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. 91103, 1975.
4. Burstein, E.A., Permyakov, E.A., Emelyanenko, V.I., Bushueva, T.L., and Pechere, J.F. Investigation of some physicochemical properties of parvalbumins by means of luminescence of their phenylalanine residues. Biochim. Biophys. Acta, vol. 400, N 1, p. 116, 1975.
5. BukolovaOrlova, T.G., Permyakov, E.A., Burstein, E.A., and Yukelson, L.Y. Reinterpretation of luminescence properties of neurotoxines from the venom of middleasian cobra Naja oxiana Eichw. Biochim. Biophys. Acta, vol. 439, N 2, p. 426431, 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. 149154, 1977.
7. Burstein, E.A., Permyakov, E.A., Yashin, V.A., Burkhanov, S.A., and FinazziAgro, A. The fine structure of luminescence spectra of azurin. Biochim. Biophys. Acta, vol. 491, N 1, p. 155159, 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. 163172, 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. 8393, 1977.
10. Burstein, E.A., Burkhanov, S.A., and Permyakov, E.A. On functional role of parvalbumins in regulation of Ca(II) in the contractionrelaxation cycle in vertebrata skeletal muscles. Biofizika (Moscow) vol. 22, N 5, p. 946948, 1977.
11. Permyakov, E.A. Cooperative freezing of internal mobility of proteins. In: Equilibrium Dynamics of Native Structure of Proteins. Pushchino, p. 8399, 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. 653657, 1978.
13. Burkhanov, S.A., Chaply, M.F., Permyakov, E.A., and Burstein, E.A. Contractionrelaxation of glycerized muscle fibers induced by pH changes in the presence of parvalbumins. Biofizika (Moscow) vol. 23, N 4, p. 734735, 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. 417422, 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. 307315, 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. 134135, 1981.
17. Permyakov, E.A., Yarmolenko, V.V., and Korystova, A.A. An evaluation of the Ca(II)binding constants of troponinC by means of intrinsic protein fluorescence. Studia Biophysica, vol. 83, N 1, p. 6370, 1981.
18. Permyakov, E.A., Yarmolenko, V.V., Kalinichenko, L.P., Morozova, L.A., and Burstein, E.A. Calcium binding to a-lactalbumin: structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes. Biochem. Biophys. Res. Commun. vol. 100, N 1, p. 191197, 1981.
19. Permyakov, E.A., Kalinichenko, L.P., Morozova, L.A., Yarmolenko, V.V., and Burstein, E.A. alactalbumin binds magnesium ions: study by means of intrinsic fluorescence technique. Biochem. Biophys. Res. Commun. vol. 102, N 1, p. 17, 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. 16601668, 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. 10591065, 1982.
22. Permyakov, E.A., Yarmolenko, V.V., Burstein, E.A., and Gerday, Ch. Intrinsic fluorescence spectra of a tryptophancontaining parvalbumin as a function of thermal, pH and urea denaturation. Biophys. Chemistry vol. 15, N 1, p. 1926, 1982.
23. Permyakov, E.A., Yarmolenko, V.V., Kalinichenko, L.P., Morozova, L.A., and Burstein, E.A. Calcium binding to alactalbumin from cow milk. Study by changes of intrinsic protein fluorescence. Biofizika (Moscow), vol. 27, N 3, p. 380385, 1982.
24. Permyakov, E.A., Kalinichenko, L.P., Morozova, L.A., Yarmolenko, V.V., and Burstein, E.A. Study of Mg(II) binding to alactalbumin by fluorescence spectroscopy method. Biofizika (Moscow), vol. 27, N 4, p. 578584, 1982.
25. Yarmolenko, V.V. Permyakov, E.A., Kalinichenko, L.P., Morozova, L.A., Burstein, E.A., and Vaitkus, V. Calcium ion binding to alactalbumin from cow milk. In: Proceedings of Lithuanian branch of AllUnion Inst. of Dairy Industry, vol. 16, p. 134140, 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 Cabinding proteins. Biofizika (Moscow), vol. 28, N 3, p. 393397, 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. 145152, 1983.
28. Morozova, L.A., Permyakov, E.A., and Burstein, E.A. Properties of alactalbumin as a metalbinding protein. In: PhysicoChemical Basis of Cell Functioning. Pushchino, p. 1621, 1983.
29. Permyakov, E.A., Medvedkin, V.N., Kalinichenko, L.P., and Burstein, E.A. Comparative study of physicochemical properties of two pike parvalbumins by means of their intrinsic tyrosyl and phenylalanyl fluorescence. Arch. Biochem. Biophys. vol. 227, N 1, p. 920, 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. 185191, 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. 8085, 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. 265271, 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. 719724, 1984.
34. Permyakov, E.A., Morozova, L.A., and Burstein, E.A. Cation binding effects on the pH, thermal and urea denaturation transitions in alactalbumin. Biophys. Chem. vol. 21, N 1, p. 2131, 1985.
35. Permyakov, E.A., Ostrovski, A.V., Burstein, E.A., Pleshanov, P.G., and Gerday, C. Parvalbumin conformers revealed by steadystate and timeresolved fluorescence spectroscopy. Arch. Biochem. Biophys. vol. 240, N 2, p. 781791, 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. 288295, 1985.
37. Permyakov, E.A. Parvalbumin and Related Calcium Binding Proteins. Nauka, Moscow, 1985.
38. 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. 14981500, 1985.
39. 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. 297305, 1986.
40. Permyakov, E.A., Kalinitschenko, L.P., Borissowa, M.A., and Oreschkin, E.F. Vergleichende Untersuchungen der Fluoreszenz von Fleisch und Eiweisen des Actomyosinkomplexes. Fleischwirtschaft, vol. 66, N 3, p. 406407, 1986.
41. Permyakov, E.A., and Kreimer, D.I. Effects of pH, temperature and Ca(II) content on the conformation of alactalbumin in a medium modeling physiological conditions. Gen. Phys. Biophys. vol. 5, N 4, p. 377390, 1986.
42. 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. 11111119, 1986.
43. Medvedkin, V.N., Mitin, Y.V., and Permyakov, E.A. Effects of Arg74 on formation of the structure of the Cterminal domain of pike parvalbumin III. Bioorg. Khimia, vol. 13, N 2, p. 177182, 1987.
44. 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. 11161125, 1987.
45. Medvedkin, V.N., Mitin, Y.V., and Permyakov, E.A. Preparation of analog of the fragment 74108 of pike parvalbumin III containing alanine residue in position 74 and of its acetylated derivative. Bioorg. Khimia, vol. 13, N 8, p. 10191023, 1987.
46. Permyakov, E.A. Muscle sarcoplasmic calciumbinding proteins. In: Structure and Functions of Proteins of Contractile Systems. Nauka, Leningrad, p. 159167, 1987.
47. Permyakov, E.A., Ostrovski, A.V., and Kalinichenko L.P. Stoppedflow kinetic studies of Ca(II) and Mg(II) dissociation in cod parvalbumin and bovine alactalbumin. Biophys. Chem., vol. 28, N 2, p. 225233, 1987.
48. 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.
49. 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.
50. 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.
51. Lakizova, I.Y., Elyakova, L.A., Emelyanenko, V.I., Permyakov, E.A., and Burstein, E.A. Comparative study of b 1,3glucanases of scallops by tryptophan fluorescence. Biofizika (Moscow) vol. 33, N 1, p. 3135, 1988.
52. Permyakov, E.A., Kreimer, D.I., Kalinichenko, L.P., and Shnyrov, V.L. Interactions of calcium binding proteins, parvalbumin and alactalbumin, with dipalmitoylphosphatidyl choline vesicles. Gen. Phys. Biophys. vol. 7, N 1, p. 95107, 1988.
53. 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. 5761, 1988.
54. Shnyrov, V.L., Freidina, N.A., and Permyakov, E.A. Study of pH and temperatureinduced transitions in Fprotein (phosphofructokinase) by spectroscopy and microcalorimetry methods. Biochim. Biophys. Acta, vol. 953, N 1, p. 128133, 1988.
55. Morozova, L.A., Gusev, N.B., Shnyrov, V.L., and Permyakov, E.A. Studies of physicochemical 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. 531540, 1988.
56. Permyakov, E.A., Ostrovski, A.V., and Kalinichenko, L.P. Kinetics of dissociation of complexes of alactalbumin with Ca(II) and Mg(II) ions. Biofizika (Moscow) vol. 33, N 3, p. 413416, 1988.
57. 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 lactalbumin with dipalmitoylphosphatidylcholine vesicles. Biofizika (Moscow) vol. 33, N 3, p. 465470, 1988.
58. 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 alactalbumin studied by timeresolved and steadystate fluorescence spectroscopy. Biophys. Chem. vol. 30, N 1, p. 105115, 1988.
59. 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. 984991, 1988.
60. Permyakov, E.A., and Tskhovrebova, L.A. Effects of temperature and pH on environment of tryptophan residues in aactinin. Biofizika (Moscow) vol. 33, N 5, p. 754757, 1988.
61. Permyakov, E.A., Morozova, L.A., Kalinichenko, L.P., and Derezhkov, V.Y. Interaction of alactalbumin with Cu(II). Biophys. Chem. vol. 32, N 1, p. 3742, 1988.
62. 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. 14971499, 1989.
63. 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. 7179, 1989.
64. 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. 627630, 1989.
65. 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. 693698, 1989.
66. Burstein, E.A., Nyamaa, D., BatErdene, 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. 1524, 1990.
67. Levitsky, D.I., Khvorov, N.V., Shnyrov, V.L., Vedenkina, N.S., Permyakov, E.A., and Poglazov, B.F. Domain structure of myosin subfragment1. Selective denaturation of the 50 kDa segment. FEBS Letters, vol. 264, N 2, p. 176178, 1990.
68. 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. 415420, 1990.
69. 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.6770, 1991.
70. 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. 563571, 1990.
71. Permyakov, E.A., Grishchenko, V.M., Kalinichenko, L.P., Orlov, N.Y., Kuwajima, K., and Sugai, S. Calciumregulated interactions of human alactalbumin with bee venom melittin. Biophys. Chem. vol. 39, p. 111117, 1991.
72. 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.
73. 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.
74. 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.
75. 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.
76. 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.
77. Permyakov, E.A., Shnyrov, V.L., Kalinichenko, L.P., Kuchar, A., Reyzer, I.L., and Berliner, L.J. Binding of Zn(II) ions to a-lactalbumin. J. Protein Chem., vol. 10, N. 6, p. 577-584, 1991.
78. 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.
79. 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.
80. 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.
81. Permyakov, E.A. Luminescent Spectroscopy of Proteins. CRC Press, Boca Raton, Ann Arbor, London, Tokyo, 164 p. 1993.
82. 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.
83. 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.
84. 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.
85. Permyakov, E.A. Calcium Binding Proteins. Moscow, Nauka, 190 p., 1993.
86. 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.
87. 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.
88. Permyakov, E.A., and Berliner, L.J. Co2+-binding to a-lactalbumin. J. Prot. Chem. vol. 13, N 3, p. 277-281, 1994.
89. 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.
90. 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.
91. 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.
92. 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.
93. 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.
94. 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.
95. Grishchenko, V.M., Kalinichenko, L.P., Deikus, G.Y., Veprintsev, D.B., Cawthern, K.M., Berliner, L.J., Permyakov, E.A. Interactions of a-lactalbumin with lipid vesicles studied by tryptophan fluorescence. Biochem. Mol. Biol. Internat. v. 38, N 3, p. 453-466, 1996.
96. 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.
97. Veprintsev, D.B., Permyakov, E.A., Kalinichenko, L.P., and Berliner, L.J. Pb2+ and Hg2+ binding to a-lactalbumin. Biochem. Mol. Biol. Internat. v. 39, N 6, p. 1255-1265, 1996.
98. 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.
99. 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.
100. 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-a-lactalbumins: evidence for a new intermediate state, FEBS Letters, v. 412, N 3, p. 625-628, 1997.
101. 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.
102. Cawthern,K.M., Narayan,M., Chaudhuri,D., Permyakov,E.A., and Berliner,L.J. Interactions of a-lactalbumin with fatty acids and spin label analogs. J. Biol. Chem. 1997, v. 272, N 49, p. 30812-30816.
103. Cawthern, K.M., Anderson, P.J., Permyakov, E.A., and Berliner, L.J. Interaction of N-acetylglucosamine-в(1-4)-galactosyltransferase with liposomes. Period. Biol., Vol. 100, Suppl. 2, p. 53-58, 1998.
104. 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: a-lactalbumin. Proteins, Vol. 37, N. 1, p. 65-72, 1999.
105. 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.
106. 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 б. Biochem. Biophys. Res. Commun. 267, 663-668, 2000.
107. Permyakov, E.A., and Berliner, L.J. a-Lactalbumin: structure and function. FEBS Letters, Vol. 473, N 3, p. 269-274, 2000.
108. 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.
109. Permyakov, S.E., Veprintsev, D.B., Brooks, C.L., Permyakov, E.A., and Berliner, L.J. Zinc binding in bovine a-lactalbumin: sequence homology may not be a predictor of subtle functional features. Proteins: Structure, Function, and Genetics, Vol. 40, p. 106-111, 2000.
110. 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.
111. 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.
112. 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.
113. 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.
114. Permyakov, S.E., Oberg, K.A., Cherskaya, A.M., Shavlovsky, M.M., Permyakov, E.A., and Uversky, V.N. Human a -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.
115. 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 a-lactalbumin: effects on the protein stability and cation binding. Protein Eng., Vol. 14, N. 10, p. 785-789, 2001.
116. Permyakov, E.A., and Freidin, A.A. Progress in the Russian biological instrumentation. Sci. Instrumentation Vol. 11, N. 3, p. 3-11, 2001.
117. 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 g subunit of retinal phosphodiesterase: a natively unfolded protein. J. Proteome Res. Vol. 1, p. 149-159, 2002.
118. Goers, J., Permyakov, S.E., Permyakov, E.A., Uversky, V.N., and Fink, A.L. Conformational prerequisites for a-lactalbumin fibrillation. Biochemistry, Vol. 41, p. 12546-12551, 2002.
119. 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
120. 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 a-lactalbumin disulfide bridges. Proteins: Structure, Function, and Genetics, Vol. 51, p. 498-503, 2003
121. Permyakov, S.E., Millett, I.S., Doniach, S., Permyakov, E.A., and Uversky, V.N. Natively unfolded C-terminal domain of caldesmon remains substantially unstructered after the effective binding to calmodulin. Proteins: Structure, Function, and Genetics, Vol. 53, p. 855-862. 2003
122. Permyakov, E.A., Permyakov, S.E., and Berliner, L.J. a-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.
123. Permyakov, E.A. The Method of Intrinsic Protein Luminescence. Moscow, Nauka, 189 p. 2003.
124. 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 a-lactalbumin to histones and basic poly-amino acids. Biochemistry, Vol. 43, N 19, p. 5575-5582, 2004.
Пермяков Евгений Анатольевич