{"id":14,"date":"2022-11-09T14:01:35","date_gmt":"2022-11-09T11:01:35","guid":{"rendered":"http:\/\/bioproteom.protres.ru\/mainw\/?page_id=14"},"modified":"2022-11-10T11:19:36","modified_gmt":"2022-11-10T08:19:36","slug":"list-of-scientific-papers-of-o-v-galzitskaya","status":"publish","type":"page","link":"http:\/\/bioproteom.protres.ru\/mainw\/en\/papers\/list-of-scientific-papers-of-o-v-galzitskaya\/","title":{"rendered":"List of scientific papers of O.V. Galzitskaya"},"content":{"rendered":"
    \n
  1. M. Gutin and O.V.Galzitskaia<\/strong>, Helix-coil transition in the simplest model of large native RNA. I. Consideration of only native helices. Biofizika, 38(1), 84-92, Russian (1993)<\/strong><\/li>\n
  2. M. Gutin and O.V.Galzitskaia<\/strong>, Helix-coil transition in the simplest models of large native RNA. II. Consideration of nonspecific interactions. Biofizika, 38(1), 93-98, Russian (1993)<\/strong><\/li>\n
  3. V. Galzitskaia<\/strong>, B.A. Reva and A.V. Finkelstein, Attainment of an energy minimum by a protein chain does not require a complete sorting of conformations: a computerized experiment and phenomenological theory. Mol Biol (Mosk)., 28(6), 1412-1427 (1994)<\/strong><\/li>\n
  4. V. Galzitskaia<\/strong> and A.V. Finkelstein, Self-organization of protein chain accelerates upon stabilization of its native conformation. Numerical experiment. Mol Biol (Mosk)., 29(2), 181-186 (1995)<\/strong><\/li>\n
  5. V. Galzitskaya<\/strong> and A.V. Finkelstein, Folding of chains with random and edited sequences: similarities and differences. Protein Eng., 8(9), 883-892 (1995)<\/strong><\/li>\n
  6. V. Finkelstein and O.V. Galzitskaia<\/strong>, Turning speed and stability of a native structure in «random» and «edited» chains. Mol Biol (Mosk)., 30(1), 145-155 (1996)<\/strong><\/li>\n
  7. V. Galzitskaya<\/strong> and A.V. Finkelstein, Computer simulation of secondary structure folding of random and \u201cedited\u201d RNA chains. J.Chem. Phys.,105(1), 319-325 (1996)<\/strong><\/li>\n
  8. V. Galzitskaya<\/strong> and A.V. Finkelstein, A theoretical study of the dependence of rate of winding of RNA-like heteropolymers on the length of the chain. Mol Biol (Mosk)., 31(3), 478-487 (1997)<\/strong><\/li>\n
  9. V. Galzitskaya<\/strong>, Effect of the energy of distant contacts on the time of finding the native structure for RNA-like heteropolymers. Mol Biol (Mosk)., 31(3), 488-491 (1997)<\/strong><\/li>\n
  10. N. Serdiuk, O.V. Galzitskaia<\/strong> and A.A. Timchenko, Roughness of the globular protein surface. Biofizika (Russian), 42(6), 1197-207 (1997)<\/strong><\/li>\n
  11. V. Galzitskaia<\/strong>, Geometrical factor and physical reasons for its influence on the kinetic and thermodynamic properties of RNA-like heteropolymers. Fold Des., 2(3), 193-201 (1997)<\/strong><\/li>\n
  12. A. Timchenko, O.V. Galzitskaya<\/strong> and I.N. Serdyuk, Roughness of the globular protein surface: analysis of high resolution X-ray data. Proteins, 28(2), 194-201 (1997)<\/strong><\/li>\n
  13. A. Timchenko, O.V. Galzitskaya<\/strong> and I.N. Serdyuk, Roughness of the globular protein surface. JINR Rapid Communications, 4(90), 59-63 (1998)<\/strong><\/li>\n
  14. V. Galzitskaya<\/strong> and A.V. Finkelstein, Folding rate dependence on the chain length of RNA-like heteropolymers. Fold Des., 3(2), 69-78 (1998)<\/strong><\/li>\n
  15. N. Uversky, S. Winter, O.V. Galzitskaya<\/strong>, L. Kittler and G. Lober, Hyperphosphorylation induces structural modification of tau-protein. FEBS Lett., 439(1-2), 21-25 (1998)<\/strong><\/li>\n
  16. V. Galzitskaya<\/strong> and A.V. Finkelstein, A theoretical search for folding\/unfolding nuclei in three-dimensional protein structures. Proc Natl Acad Sci U S A., 96(20), 11299-11304 (1999)<\/strong><\/li>\n
  17. N. Uversky, O.V. Galzitskaya<\/strong>, S. Winter, L. Kittler and G. Lober, Effect of hyperphosphorylation on structure of TAU protein. Tsitologiia (Russian), 41(6), 540-9 (1999)<\/strong><\/li>\n
  18. V. Skugarev, O.V. Galzitskaia<\/strong> and AV. Finkelstein, Search for folding nuclei in the spatial structure of proteins. Mol Biol (Mosk)., 33(6), 1016-1026 (1999)<\/strong><\/li>\n
  19. Galzitskaya<\/strong> and A. Caflisch, Solution conformation of phakellistatin 8 investigated by molecular dynamics simulations. J Mol Graph Model., 17(1), 19-27 (1999)<\/strong><\/li>\n
  20. V. Galzitskaya<\/strong>, A.V. Skoogarev, D.N. Ivankov and A.V. Finkelstein, Folding nuclei in 3D protein structures. Proceedings of the Pacific Symposium on Biocomputong, 131-142 (2000)<\/strong><\/li>\n
  21. V. Galzitskaya<\/strong>, A.K. Surin and H. Nakamura, Optimal region of average side-chain entropy for fast protein folding. Protein Sci., 9(3), 580-586 (2000)<\/strong><\/li>\n
  22. V. Galzitskaya<\/strong>, J. Higo, M. Kuroda and H. Nakamura, b-hairpin folds by molecular dynamics simulations. Chemical Physics Letters, 326, 421-429 (2000)<\/strong><\/li>\n
  23. Higo, O.V. Galzitskaya<\/strong>, S. Ono and H. Nakamura, Energy landscape of a b-hairpin peptide in explicit water studied by multicanonical molecular dynamics. Chemical Physics Letters, 337, 169-175 (2001)<\/strong><\/li>\n
  24. V. Galzitskaia<\/strong>, D.N. Ivankov and A.V. Finkelstein, Folding nuclei in proteins. FEBS Lett., 489(2-3), 113-118 (2001)<\/strong><\/li>\n
  25. V. Galzitskaya<\/strong>, D.N. Ivankov and A.V. Finkelstein, The state of art in steps of protein folding. Summer School «The prediction and mechanism of protein folding: from topology to intermediate states». (Chomilier,J., Labesse, G, and Sadoc, J.-F., eds.) Institute d’etudes scientifiques de Cargese, 8-19 (2001)<\/strong><\/li>\n
  26. V. Galzitskaya<\/strong>, D.N. Ivankov and A.V. Finkelstein, Nucleation and folding rate in proteins. Mol Biol (Mosk)., 35(4), 708-717 (2001)<\/strong><\/li>\n
  27. V. Galzitskaya<\/strong>, J. Higo and A.V. Finkelstein, a-helix and b-hairpin folding from experiment, analytical theory and molecular dynamics simulations. Current Protein and Peptide Science, 3(2), 191-200 (2002)<\/strong><\/li>\n
  28. V. Galzitskaya<\/strong>, Sensitivity of folding pathway to the details of amino-acid sequence. Mol. Biol. (Russian), 36(3), 386-390 (2002)<\/strong><\/li>\n
  29. V. Galzitskaya<\/strong>, b-Hairpin Folding. Mol. Biol. (Russian), 36(5), 755-760 (2002)<\/strong><\/li>\n
  30. Ikeda, O.V. Galzitskaya<\/strong>, H. Nakamura and J. Higo, b-hairpin, a-helices, and the intermediates among the secondary structures in the energy landscape of a peptide from a distal b-hairpin of SH3 domain. J.Comp. Chem., 24(3), 310-318 (2003)<\/strong><\/li>\n
  31. V. Galzitskaya<\/strong>, S.O. Garbuzynskiy, D.N. Ivankov and A.V. Finkelstein, Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics. Proteins, 51 (2), 162-166 (2003)<\/strong><\/li>\n
  32. V. Galzitskaya<\/strong> and B.S. Melnik, Prediction of protein domain boundaries from sequence alone. Protein Science, 12(4), 696-701 (2003)<\/strong><\/li>\n
  33. O. Garbuzynskiy, A.V. Finkelstein and O.V. Galzitskaya<\/strong>, Outlining folding nuclei in globular proteins. J. Mol. Biol., 336(2), 509-525 (2004)<\/strong><\/li>\n
  34. V. Finkelstein and O.V. Galzitskaya<\/strong>, Physics of protein folding. Physics of Life Reviews, 1, 23-56 (2004)<\/strong><\/li>\n
  35. O. Garbuzynskiy, M.Yu. Lobanov and O.V. Galzitskaya<\/strong>, To be folded or to be unfolded? Protein Science, 13(11), 2871-2877 (2004)<\/strong><\/li>\n
  36. Suzuki, O.V. Galzitskaya<\/strong>, D. Mitomo and J. Higo, General dynamic properties of Ab12-36 <\/sub>amyloid peptide involved in\u00a0 Alzheimer\u2019s disease from unfolding simulation. Eur. J. Biochem., 136(5), 583-594 (2004<\/strong>)<\/li>\n
  37. V. Marchenkov, I.V. Sokolovskii, N.V. Kotova, O.V. Galzitskaya<\/strong>, E.S. Bochkareva, A.S. Girshovich and G.V. Semisotnov. The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure. Biofizika (Russian), 49(6), 987-994 (2004)<\/strong><\/li>\n
  38. S. Melnik, S.O. Garbuzynskiy, M.Yu. Lobanov and O.V. Galzitskaya<\/strong>. The difference between protein structures obtained by X-ray analysis and nuclear magnetic resonance. Molecular Biology (Russian), 39(1), 113-122 (2005)<\/strong><\/li>\n
  39. V. Finkelstein, D.N. Ivankov and O.V. Galzitskaya<\/strong>, Prediction folding rates and folding nuclei in globular proteins on the basis of theory of their folding. Progress in biological chemistry. Russian, 45, 3-36 (2005)<\/strong><\/li>\n
  40. V. Galzitskaya<\/strong>, S.O. Garbuzynskiy and A.V. Finkelstein, Theoretical study of protein folding: outlining folding nuclei and estimation of protein folding rates. Journal of Physics: Condensed Matter. 17, S1539-S1551 (2005)<\/strong><\/li>\n
  41. O. Garbuzynskiy, B.S. Melnik, M.Yu.Lobanov, A.V. Finkelstein and O.V. Galzitskaya<\/strong>, Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures? Proteins, 60(1), 139-147 (2005)<\/strong><\/li>\n
  42. O. Garbuzynskiy, A.V. Finkelstein and O.V. Galzitskaya<\/strong>, On prediction of folding nuclei in globular proteins. Molecular Biology (Russia), 39(6), 1032-1041 (2005)<\/strong><\/li>\n
  43. V. Galzitskaya<\/strong>, N.V. Dovidchenko, M.Yu. Lobanov and S.O. Garbuzynskiy Prediction of protein domain boundaries from statistics of appearance of amino acid residues. Molecular Biology (Russia), 40(1), 111-121 (2006)<\/strong><\/li>\n
  44. V. Galzitskaya<\/strong>, S.O. Garbuzynskiy and M.Yu. Lobanov, Prediction of natively unfolded regions in protein chains. Molecular Biology (Russia), 40(2) 341-348 (2006)<\/strong><\/li>\n
  45. V. Galzitskaya<\/strong> and S.O. Garbuzynskiy, Entropy capacity determines protein folding. Proteins, 63(1), 144-154 (2006)<\/strong><\/li>\n
  46. V. Galzitskaya<\/strong>, S.O. Garbuzynskiy and M.Yu. Lobanov, Is it possible to predict amyloidogenic regions from sequence alone? Journal of Bioinformatics and Computational Biology (JBCB), 4(2), 373-88 (2006)<\/strong><\/li>\n
  47. V. Galzitskaya<\/strong> and S.O. Garbuzynskiy, Optimal relationship between average conformational entropy and average energy of residue interaction for fast protein folding. Biofizika (Russia), 51(4), 622-632 (2006)<\/strong><\/li>\n
  48. S. Bogatyreva, A.V. Finkelstein and O.V. Galzitskaya<\/strong>, Trend of amino acid compositions of different taxa. Journal of Bioinformatics and Computational Biology (JBCB), 4(2), 597-608 (2006)<\/strong><\/li>\n
  49. V. Galzitskaya<\/strong>, S.O. Garbuzynskiy and M.Yu. Lobanov, A search of amyloidogenic regions in protein chain. Molecular Biology (Russia), 40(5) 910-918 (2006)<\/strong><\/li>\n
  50. V. Galzitskaya<\/strong>, Identification of beta-aggregate sites in protein chain. Molecular Biology (Russia), 40(6) 931-936 (2006)<\/strong><\/li>\n
  51. V. Galzitskaya<\/strong>, S.O. Garbuzynskiy and M.Yu. Lobanov, FoldUnfold: web server for the prediction of disordered regions in protein chain. Bioinformatics, 22(23), 2948-2949 (2006)<\/strong><\/li>\n
  52. V. Galzitskaya<\/strong>, S.O. Garbuzynskiy and M.Yu. Lobanov, Prediction of Amyloidogenic and Disordered Regions in Protein Chain. PLoS Computational Biology, 2(12), e177 (2006)<\/strong><\/li>\n
  53. M. Savitski, F. Kjeldsen, M.L. Nielsen, S.O. Garbuzynskiy, O.V. Galzitskaya<\/strong>, A.K. Surin and R.A. Zubarev<\/a>, Backbone Carbonyl Group Basicities Are Related to Gas-Phase Fragmentation of Peptides and Protein Folding. Angew Chem Int Ed Engl. 46(9), 1481-1484 (2007)<\/strong><\/li>\n
  54. V. Dovidchenko, M.Yu. Lobanov and O.V. Galzitskaya<\/strong>, Prediction of number and position of domain boundaries in multi-domain proteins by use of amino acid sequence alone. Current Protein and Peptide Science, 8(2), 189-195 (2007)<\/strong><\/li>\n
  55. V. Galzitskaya<\/strong>, S.O. Garbuzynskiy and M.Yu. Lobanov, Expected packing density allows predicting both amyloidogenic and disordered regions in protein chain. Journal of Physics: Condensed Matter. 19(28), 285225 (2007)<\/strong><\/li>\n
  56. \u0410.V. Glyakina, \u041c.Yu. Lobanov and O.V. Galzitskaya<\/strong>, Search for structural factors responsible for the stability of proteins from thermophilic organisms. Molecular Biology, Russia, 41(4), 681-687 (2007)<\/strong><\/li>\n
  57. N. Serdyuk and O.V. Galzitskaya<\/strong>, Disodered regions in elongation factors EF1A in the three seperkingdoms of life. Molecular Biology, Russia, 41(6), 1042-1055 (2007)<\/strong><\/li>\n
  58. \u0410.V. Glyakina, S.O. Garbuzynskiy, \u041c.Yu. Lobanov and O.V. Galzitskaya<\/strong>, Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms. Bioinformatics, 23(17), 2231-2238 (2007)<\/strong><\/li>\n
  59. V. Finkelstein, D.N. Ivankov, S.O. Garbuzynskiy and O.V. Galzitskaya<\/strong>, Understanding the folding rates and folding nuclei of globular proteins. Current Protein and Peptide Science, 8(6) 521-536 (2007)<\/strong><\/li>\n
  60. V. Galzitskaya<\/strong>, D.C. Reifsnyder, N.S. Bogatyreva, D.N. Ivankov and S.O. Garbuzynskiy, More Compact Protein Globules Exhibit Slower Folding Rates. Proteins, 70(2), 329-332 (2008)<\/strong><\/li>\n
  61. V. Finkelstein, D.N. Ivankov, S.O. Garbuzynskiy and O.V. Galzitskaya<\/strong>, Protein structure and its folding rate. In: Applied Optimization: Mathematical Modelling of Biosystems (Editors: R.P. Mondaini, P.M. Pardalos). Springer Verlag (Heidelberg), XII, v.102, pp. 273-301 (2008)<\/strong><\/li>\n
  62. V. Galzitskaya<\/strong>, N.S. Bogatyreva and D.N. Ivankov, Compactness determines protein folding type. J Bioinform Comput Biol. 6(4), 667-680 (2008)<\/strong><\/li>\n
  63. V. Galzitskaya<\/strong>, Search for folding initiation sites from amino acid sequence. J Bioinform Comput Biol. 6(4), 681-691 (2008)<\/strong><\/li>\n
  64. V. Dovidchenko and O.V. Galzitskaya<\/strong>, Prediction of status residue to be protected or not protected from hydrogen exchange using amino acid sequence only. The Open Biochemistry Journal, 2, 77-80 (2008)<\/strong><\/li>\n
  65. Yu. Lobanov, N.S. Bogatyreva and O.V. Galzitskaya<\/strong>, Radius of gyration as an indicator of protein structure compactness. Molecular Biology, Russia, 42(4), 623-628 (2008)<\/strong><\/li>\n
  66. V. Dovidchenko, N.S. Bogatyreva and O.V. Galzitskaya<\/strong>, Prediction of loop regions in protein sequence. J Bioinform Comput Biol. 6(5), 1035-1047 (2008)<\/strong><\/li>\n
  67. I. Deruysheva, O.V. Galzitskaya<\/strong> and I.N. Serduyk, Prediction of short loops in the proteins with internal disorder. Molecular Biology (Russia), 42 (6), 1067—1078 (2008)<\/strong><\/li>\n
  68. V. Finkelstein, D.N. Ivankov, S.O. Garbuzynskiy and O.V. Galzitskaya<\/strong>, Protein structure and its folding rate. In: Applied Optimization: Mathematical Modelling of Biosystems (Editors: R.P. Mondaini, P.M. Pardalos). Springer Verlag (Heidelberg), XII, v.102, pp. 273-301 (2008<\/strong>)<\/li>\n
  69. V. Glyakina, O.V. Galzitskaya<\/strong> and N.K. Balabaev, Molecular dynamics of protein unfolding under the external forces. Bulletin of Tver University, 8(68), 109-119 (2008)<\/strong><\/li>\n
  70. V. Galzitskaya<\/strong>, E.I. Deryusheva and I.N. Serdyuk, Phylogenetic Analysis of the Loops in Elongation Factors EF1A: Stronger Support for the Grouping of Animal and Fungi. Journal of Computer Science and System Biology. 1, 073-080 (2008)<\/strong><\/li>\n
  71. S. Bogatyreva, D. N. Ivankov, M. Yu. Lobanov, O.V. Galzitskaya<\/strong>, \u0421onnection of shape of globular proteins with their folding and unfolding rates. Mathematical biology and bioinformatics (Russia), 3(2), 69-78, (2008)<\/strong><\/li>\n
  72. Yu. Lobanov, N.S. Bogatyreva, O.V. Galzitskaya<\/strong>, Radius of gyration as an indicator of protein structure compactness. Molecular Biology, 42(4), 623-628 (2008)<\/strong><\/li>\n
  73. S. Kalebina, T.A. Plotnikova, A.A. Gorkovskii, I.O. Selyakh, O.V. Galzitskaya<\/strong>, E.E. Bezsonov, G. Gellissen and I.S. Kulaev, Amyloid-like properties of Saccharomyces cerevisiae cell wall glucantransferase Bgl2p: prediction and experimental evidences. Prion, 2(2), 91-96, (2008)<\/strong><\/li>\n
  74. V. Galzitskaya<\/strong>, Do amyloidogenic regions intersect with folding nuclei of native structure? Proceedings from Computational biophysics to system biology (CBSB08), pp.219-221. 19-21 May, 2008b, Julich, Germany, (2008)<\/strong><\/li>\n
  75. V. Galzitskaya<\/strong>, S.O. Garbuzynskiy, Folding and aggregation features of proteins, Nova Science Publishers, Inc. In: Protein Misfolding, Editors: Cian B. O’Doherty and Adam C. Byrne, pp.99-112, (2008) <\/strong><\/li>\n
  76. V. Galzitskaya<\/strong>, The same or different amino acid residues are responsible for protein folding and misfolding? Biochemistry (Moscow), 74(2), 229-237, (2009)<\/strong><\/li>\n
  77. Fong, B. Shoemaker, S.O. Garbuzynskiy, M.Yu. Lobanov, O.V. Galzitskaya<\/strong> and A. Panchenko, Intrinsic disorder in proteins and their complexes: a large-scale view. PLoS Comput Biol. 5(3), e1000316, (2009)<\/strong><\/li>\n
  78. V. Galzitskaya<\/strong> and S.O. Garbuzynskiy, Comparison of \u03a6-values and folding time predictions by using Monte-Carlo and Dynamic Programming approaches. Chapter in the book, «Computational Biology: New Research». pp. 277-314, (2009)<\/strong><\/li>\n
  79. V. Glyakina, N.K. Balabaev and O.V. Galzitskaya<\/strong>, Comparison of Transition States Obtained upon Modeling of Unfolding of Immunoglobulin-Binding Domains of Proteins L and G Caused by External Action with Transition States Obtained in the Absence of Force Probed by Experiments. Biochemistry (Moscow), 74(3), 316-328, (2009)<\/strong><\/li>\n
  80. V. Glyakina, N. K. Balabaev, and O. V. Galzitskaya<\/strong>, Mechanical unfolding of proteins L and G with constant force: Similarities and differences. .J Chem. Phys. 131, 045102 (2009)<\/strong><\/li>\n
  81. N. Ivankov, N. S. Bogatyreva, M. Yu. Lobanov, O. V. Galzitskaya<\/strong>. Coupling between Properties of the Protein Shape and the Rate of Protein Folding. PLoS ONE 4(8): e6476 (2009)<\/strong><\/li>\n
  82. V. Glyakina, N. K. Balabaev, and O. V. Galzitskaya<\/strong>, Multiple Unfolding Intermediates Obtained by Molecular Dynamic Simulations under Stretching for Immunoglobulin-Binding Domain of Protein G. Open Biochemistry, 3, 66-77, (2009)<\/strong><\/li>\n
  83. V. Dovidchenko, M.Yu., Lobanov, S.O. Garbuzynskiy, and O.V. Galzitskaya<\/strong>, Prediction of amino acid residues protected from hydrogen-deuterium exchange in a protein chain. Biochemistry (Moscow), 74(8), 1091-1102, (2009)<\/strong><\/li>\n
  84. V. Galzitskaya<\/strong>, Influence of flexible loops on the rate of protein folding, Current Topics in Peptide & Protein Research, V.9, pages 71-82, (2009)<\/strong><\/li>\n
  85. V. Glyakina, N. K. Balabaev, and O. V. Galzitskaya<\/strong>, Two-, Three-, and Four-State Events Occur in the Mechanical Unfolding of Small Protein L Using Molecular Dynamics Simulations. Protein and Peptide Letters, 17, 92-103 (2010)<\/strong><\/li>\n
  86. Yu. Lobanov, B. A. Shoemaker, S. O. Garbuzynskiy, J. H. Fong, A. R. Panchenko, O. V. Galzitskaya<\/strong>, ComSin: Database of protein structures in bound (Complex) and unbound (Single) states in relation to their intrinsic disorder. Nucleic Acids Research, D283-D287 (2010)<\/strong><\/li>\n
  87. Yu. Lobanov, S.O. Garbuzynskiy, O.V. Galzitskaya<\/strong>, Statistical analysis of unstructured amino acid residues in protein structures. Biochemistry (Moscow), 75(2), 192-200 (2010)<\/strong><\/li>\n
  88. B. Mamonova, A.V. Glyakina, M.G. Kurnikova, O.V. Galzitskaya<\/strong>, Flexibility and mobility in Mesophilic and thermophilic homologous proteins from Molecular Dynamics and FoldUnfold Method. J Bioinform Comput Biol., 8(3), 377-394 (2010)<\/strong><\/li>\n
  89. V. Glyakina, O.V. Galzitskaya<\/strong>, A comparative analysis of folding pathways of thermophilic and mesophilic proteins by Monte Carlo simulations. J Bioinform Comput Biol., 8(3), 395\u2013411 (2010)<\/strong><\/li>\n
  90. V. Galzitskaya<\/strong>, Estimation of protein folding rate from Monte Carlo simulations and entropy capacity. Current Protein and Peptide Science, 11 (7), 523-537, (2010)<\/strong><\/li>\n
  91. V. Galzitskaya<\/strong>. Is the protein folding rate dependent on the number of folding stages? Modeling of protein folding with ferredoxin-like fold. Biochemistry (Moscow), 75(6), 807-818, (2010)<\/strong><\/li>\n
  92. v. Maltsev and O.V. Galzitskaya<\/strong>, Formation and participation of nano-amyloids in pathogenesis of alzheimer\u2019s disease and other amyloidogenic diseases. Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry, 4(3), 228\u2013236 (2010)<\/strong><\/li>\n
  93. O. Garbuzynskiy, M. Yu. Lobanov and O. V. Galzitskaya<\/strong>. FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence. Bioinformatics, 26, 326-332, (2010)<\/strong><\/li>\n
  94. V. Glyakina, O.V. Galzitskaya<\/strong>. Influence of organization of native structure on its folding: modeling of the folding of alpha-helical proteins. Biochemistry (Moscow), 75(8), 1098-1110, (2010)<\/strong><\/li>\n
  95. V. Galzitskaya<\/strong>. Influence of Conformational Entropy on the Protein Folding Rate. Entropy, 12(4), 961-982, (<\/strong>2010<\/strong>)<\/strong><\/li>\n
  96. V. Galzitskaya<\/strong>. Modelling of Protein Folding and Prediction of Rate based on Nucleation Mechanism. Nova Science Publishers, Inc. ISBN: 978-1-61728-990-3 In: protein Folding Editor: Eric C. Walters, pp.151-185 (2011)<\/strong><\/li>\n
  97. V. Glyakina, O. V. Galzitskaya<\/strong>, N. K. Balabaev. Investigation of mechanical properties of immunoglobulin-binding properties of proteins L and G by molecular dynamics simulations. 2, 73-81, (2010)<\/strong><\/li>\n
  98. . Yu. Lobanov, E. I. Furletova, N. S. Bogatyreva, M. A. Roytberg, O. V. Galzitskaya<\/strong>. Library of Disordered Patterns in 3D Protein Structures. PLoS Computational Biology. 6 (10), e1000958 (2010)<\/strong><\/li>\n
  99. Yu. Lobanov and O.V. Galzitskaya<\/strong>. Statistical analysis and prediction of disordered residues in protein structures. Mathematical biology and bioinformatics, 5, 124-137 (2010)<\/strong><\/li>\n
  100. Galzitskaya<\/strong>V., Lobanov M.Yu., Finkelstein A.V. (2011) Cunning simplicity of a stoichiometry driven protein folding thesis. J. Biomol. Struct. Dyn., 28 (4), 595-598 (2011)<\/strong><\/li>\n
  101. V. Galzitskaya<\/strong>, N.S. Bogatyreva, A.V. Glyakina. Bacterial proteins fold faster than eukaryotic proteins with simple folding kinetics, Biochemistry (Moscow), 76(2), 225-235 (2011)<\/strong><\/li>\n
  102. B. Pereyaslavets, M.V. Baranov, E.I. Leonova, O.V. Galzitskaya<\/strong>. Prediction of folding\/unfolding nuclei for tRNA molecules. Biochemistry (Moscow). 76(2), 299-308 (2011)<\/strong><\/li>\n
  103. Yu. Lobanov and O. V. Galzitskaya<\/strong>. The Ising model for prediction of disordered residues from protein sequence alone. Physical biology. Phys. Biol., 8 035004 (2011)<\/strong><\/li>\n
  104. Galzitskaya<\/strong>V. Misfolded Species Involved Regions Which Are Involved in an Early Folding Nucleus. Nova Science Publishers, Inc. ISBN: 978-1-61728-990-3 In: Protein Structure Editor: Lauren M. Haggerty, pp. 1-30, chapter 1 (2011<\/strong>)<\/li>\n
  105. Dovidchenko N.V., Galzitskaya<\/strong>V. Modeling of amyloid fibril formation. Biochemistry, 76(3), 449-458 (2011)<\/strong><\/li>\n
  106. Galzitskaya<\/strong>V. Regions which are responsible for swapping are also responsible for folding and misfolding. The Open Biochemistry Journal, 5, 27-36 (2011)<\/strong><\/li>\n
  107. Maltsev A.V., S. Bystryak, and Galzitskaya<\/strong>V. Role of amyloid beta-peptide in neurodegenerative diseases. Ageing Research Reviews, 10(4), 440-452 (2011)<\/strong><\/li>\n
  108. Yu. Lobanov and O.V. Galzitskaya<\/strong>. Disordered Patterns in Clustered Protein Data Bank and in eukaryotic and bacterial Proteomes. PLOS ONE, 6(11), e27142 (2011<\/strong>)<\/li>\n
  109. V. Glyakina, N.S. Bogatyreva, O.V. Galzitskaya<\/strong>. Accessible surfaces of beta proteins increase with increasing protein molecular mass more rapidly than those of other proteins, PLOS ONE, 6(12), 28464 (2011<\/strong>)<\/li>\n
  110. Yu. Lobanov, N. S. Bogatyreva, and O. V. Galzitskaya<\/strong>, Occurrence of Six Amino Acid Motifs in Three Eukaryotic Proteomes. Molecular Biology, 46, 168\u2013173 (2012<\/strong>).<\/li>\n
  111. I. Leonova, M.V. Baranov, O.V. Galzitskaya<\/strong> Formation of RNA spatial structures. Molecular Biology, 46, 34\u201346 (2012<\/strong>).<\/li>\n
  112. Yu. Lobanov and O.V. Galzitskaya<\/strong>. Occurrence of disordered patterns and homorepeats in eukaryotic and bacterial proteomes. Mol. BioSyst., 8 (1), 327 \u2013 337 (2012)<\/strong><\/li>\n
  113. Selivanova OM, Galzitskaya<\/strong> Structural polymorphism and possible pathways of amyloid fibril formation on the example of insulin protein. Biochemistry (Mosc). 77: 1237-1247 (2012)<\/strong>.<\/li>\n
  114. Suvorina MY, Surin AK, Dovidchenko NV, Lobanov MY, Galzitskaya<\/strong> Comparison of experimental and theoretical data on hydrogen-deuterium exchange for ten globular proteins. Biochemistry (Mosc). 77(6):616-23. doi: 10.1134\/S0006297912060089. (2012<\/strong>).<\/li>\n
  115. V. Galzitskaya<\/strong> and A.V. Glyakina. Nucleation-based prediction of the protein folding rate and its correlation with the folding nucleus size. Proteins: Structure, Function, and Bioinformatics, 80 (12): 2711-2727 (2012<\/strong>).<\/li>\n
  116. Michail Yu. Lobanov, Igor V. Sokolovskiy and Oxana V. Galzitskaya<\/strong> IsUnstruct: Prediction of the Residue Status to Be Ordered or Disordered in the Protein Chain by a method based on the Ising model. Journal of Biomolecular Structure & Dynamics, 31(10), 1034-1043 (2013<\/strong>).<\/li>\n
  117. Stanislav O. Fedechkin, Jacob Brockerman, Elizabeth J. Luna, Michail Yu. Lobanov, Oxana V. Galzitskaya<\/strong>, Serge L. Smirnov. An N-terminal, 830-residue Intrinsically Disordered Region of the Cytoskeleton-regulatory Protein Supervillin Contains Myosin II- and F-actin- Binding Sites. Journal of Biomolecular Structure & Dynamics, 31(10), 1150-1159 (201<\/strong>3<\/strong>).<\/li>\n
  118. Leonova EI, Galzitskaya<\/strong> OV Comparative characteristics of the structure and function for syndecan-1 from animal organisms. Mol Biol (Mosk). 47(3):505-12. Russian. (2013<\/strong>).<\/li>\n
  119. Bezsonov E.E., Groenning M., Galzitskaya<\/strong>V., Gorkovskii A.A., Semisotnov G.V., Selyakh I.O., Ziganshin R.H., Rekstina V.V., Kudryashova I.B., Kuznetsov S.A., Kulaev I.S. Kalebina T.S. Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation. Prion, 7(2), 175-84 (2013<\/strong>).<\/li>\n
  120. Mal’tsev AV, Davidchenko NV, Uteshev VK, Sokolik VV, Shtang OM, Iakushun MA, Sokolova NM, Suprin AK, Galzitskaia<\/strong> Intensive Protein Synthesis in Neurons and Phosphorylation of Beta Amyloid Precursor Protein and Tau Protein are Triggering Factorsof Neuronal Amyloidosis and Alzheimer\u2019s Disease. Biomed Khim.; 59(2):144-70. Review. Russian. (2013<\/strong>).<\/li>\n
  121. Maltsev A.V., Dovidchenko N.V., Uteshev V.K., Sokolik V.V., Shtang O.M., Yakushin M.A., Sokolova N.M., Surin A.K., and Galzitskaya<\/strong>V. (2013<\/strong>) Intensive Protein Synthesis in Neurons and Phosphorylation of Beta Amyloid Precursor Protein and Tau Protein are Triggering Factors of Neuronal Amyloidosis and Alzheimer\u2019s Disease. Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry, 7(4), 278\u2013293<\/li>\n
  122. Mamonova T.B., Glyakina A.V., Galzitskaya<\/strong>V., Kurnikova M.G. Stability and rigidity\/flexibility — two sides of the same coin? BBA — Proteins and Proteomics, V. 1834 (5), 854-866 (2013<\/strong>).<\/li>\n
  123. Lobanov M.Yu., Suvorina M.Yu., Dovidchenko N.V., Sokolovskiy I.V., Surin A. K. and Galzitskaya<\/strong> V. A novel web server predicts amino acid residue protection against hydrogen-deuterium exchange. Bioinformatics, 29(11), 1375-1381 (2013<\/strong>).<\/li>\n
  124. Glyakina A.V., Pereyaslavets L.B., Galzitskaya<\/strong>V. Right- and left-handed three-helix proteins: Experimental and simulation analysis of differences in folding and structure. Proteins, 81, 1527-1541, doi: 10.1002\/prot.24301 (2013<\/strong>).<\/li>\n
  125. Leonova EI, Galzitskaya<\/strong> Structure and functions of syndecans in vertebrates. Biochemistry (Mosc). 2013 Oct;78(10):1071-85. doi: 10.1134\/S0006297913100015. (2013)<\/strong>.<\/li>\n
  126. Glyakina AV, Balabaev NK, Galzitskaya<\/strong> Experimental and theoretical studies of mechanical unfolding of different proteins. Biochemistry (Mosc). 2013 Nov;78(11):1216-27. doi: 10.1134\/S0006297913110023. (2013<\/strong>)<\/li>\n
  127. Glyakina A.V., Likhachev I.V., Balabaev N.K., Galzitskaya<\/strong>V. Right- and left-handed three-helix proteins: II. Similarity and Differences in Mechanical Unfolding of Proteins. Proteins. 82:90\u2013102, Jul 20. doi: 10.1002\/prot.24373. (2014<\/strong>)<\/li>\n
  128. Finkelstein A.V., Ivankov D.N., Garbuzynskiy S.O. and Galzitskaya<\/strong>V. Understanding the folding rates and folding nuclei of globular proteins. In eBook Series «Frontiers in Protein and Peptide Sciences», V.1 B.M. Dunn, ed.). Bentham eBooks (Oak Park, IL, USA), 2014, pp.91-138. (2014<\/strong>)<\/li>\n
  129. Lobanov M.Y., Sokolovskiy I.V., Galzitskaya<\/strong>V. HRaP: database of occurrence of HomoRepeats and patterns in proteomes. Nucleic Acids Res., PMID: 24150944. Jan 1;42(1):D273-278. doi: 10.1093\/nar\/gkt927. (2014<\/strong>)<\/strong><\/li>\n
  130. Maltsev A.V., Santockyte R., Bystryak S., Galzitskaya<\/strong>V. Activation of neuronal defence mechanisms in response to pathogenic factors triggering induction of amyloidosis in Alzheimer\u2019s disease. Journal of Alzheimer’s Disease. 40, 19-32 (2014<\/strong>).<\/li>\n
  131. Syutkin A.S., Pyatibratov M.G., Galzitskaya<\/strong>V., Rodr\u00edguez-Valera F. and Fedorov O. V. Haloarcula marismortui archaellin genes as ecoparalogs. Extremophiles. 18(2):341-9. DOI: 10.1007\/s00792-013-0619-4 (2014<\/strong>)<\/li>\n
  132. Dovidchenko N.V., Finkelstein A.V., Galzitskaya<\/strong>, O.V. How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. I. Modeling the amyloid protofibril formation \/\/ The Journal of Physical Chemistry. 118(5):1189-97. (2014<\/strong>)<\/li>\n
  133. Selivanova OM, Suvorina MY, Dovidchenko NV, Eliseeva IA, Surin AK, Finkelstein AV, Schmatchenko VV, Galzitskaya<\/strong> How to Determine the Size of Folding Nuclei of Protofibrils from the Concentration Dependence of the Rate and Lag-Time of Aggregation. II. Experimental Application for Insulin and LysPro Insulin: Aggregation Morphology, Kinetics, and Sizes of Nuclei. J Phys Chem B. 118(5):1198-206. doi: 10.1021\/jp4083568. (2014<\/strong>)<\/li>\n
  134. Galzitskaya<\/strong>V., Pereyaslavets L.B., and Glyakina A.V. Folding of Right- and Left-Handed Three-Helix Proteins. Israel Journal of Chemistry, 54<\/strong>, 1126-1136. (2014<\/strong>)<\/li>\n
  135. Dovidchenko NV, Leonova EI, Galzitskaya<\/strong> Mechanisms of amyloid fibrilformation. Biochemistry (Mosc). 2014 Dec;79(13):1515-27. (2014)<\/strong><\/li>\n
  136. I. Leonova, O.V. Galzitskaya<\/strong>, The role of syndecan-2 in amyloid plaque formation. Molecular Biology (Russian), 49, Issue 1, pp 77-85 (2015)<\/strong>.<\/li>\n
  137. Glyakina A.V., Likhachev IV, Balabaev N.K., Galzitskaya<\/strong>V., Mechanical stability analysis of the protein L immunoglobulin-binding domain by full alanine screening using molecular dynamics simulations. Biotechnol J. Mar;10(3):386-94. (2015)<\/strong><\/li>\n
  138. Pereyaslavets L.B., Glyakina A.V., Dovidchenko N.V., Sokolovskiy I.V., and Galzitskaya<\/strong>V. What handedness and angles between helices has the studied three-helical protein domain? Bioinformatics; 31(6):963-5. (2015)<\/strong><\/li>\n
  139. Leonova EI, Galzitskaya<\/strong> Cell communication using intrinsically disordered proteins: what can syndecans say? J Biomol Struct Dyn. 33(5):1037-50. (<\/strong>2015<\/strong>)<\/strong><\/li>\n
  140. Finkelstein AV, Dovidchenko NV, Selivanova OM, Suvorina MY, Surin AK, Galzitskaya<\/strong> Determination of the size of the primary and secondary folding nuclei of protofibrils from the concentration dependence of the rate and the lag-time of their formation. In: Physical Biology of Proteins and Peptides: Theory, Simulation and Experiment (eds.:Olivares-Quiroz L., Jard\u00f3n-Valadez H.E., Guzm\u00e1n-L\u00f3pez O.). New York: Springer, 47-66. (<\/strong>2015<\/strong>)<\/strong><\/li>\n
  141. Dovidchenko N.V. and Galzitskaya<\/strong>V. Computational approaches to identification of aggregation sites and the mechanism of amyloid growth, Springer International Publishing Switzerland O. Gursky (ed.), Lipids in Protein Misfolding, Advances in Experimental Medicine and Biology 855: 213-39, DOI 10.1007\/978-3-319-17344-3_9. (<\/strong>2015<\/strong>)<\/strong><\/li>\n
  142. Elena I. Leonova, Oxana V. Galzitskaya<\/strong>, Role of syndecans in lipid metabolism and in human disease. Springer International Publishing Switzerland O. Gursky (ed.), Lipids in Protein Misfolding, Advances in Experimental Medicine and Biology 855:241-58, DOI 10.1007\/978-3-319-17344-3_10. (<\/strong>2015<\/strong>)<\/strong><\/li>\n
  143. V. Galzitskaya<\/strong> and M.Yu. Lobanov, Phyloproteomic analysis of 11780 six-residues-long motifs occurrences. BioMed Research International; 208346. doi: 10.1155\/2015\/208346. (2015)<\/strong><\/li>\n
  144. Lobanov, M.Y.; Galzitskaya<\/strong>, O.V. How Common Is Disorder? Occurrence of Disordered Residues in Four Domains of Life. Int. J. Mol. Sci., 16, 19490-19507. (<\/strong>2015<\/strong>)<\/strong><\/li>\n
  145. Pereyaslavets LB, Sokolovsky IV, Galzitskaya<\/strong> FoldNucleus: web server for the prediction of RNA and protein folding nuclei from their 3D structures. Bioinformatics. 31, 3374-3376. PubMed PMID: 26104744 (<\/strong>2015<\/strong>)<\/strong><\/li>\n
  146. Galzitskaya<\/strong> Reversible and Irreversible Aggregation of Proteins from the FET Family: Influence of Repeats in Protein Chain on Its Aggregation Capacity. Curr Protein Pept Sci., 17(4), 319-331. (<\/strong>2016<\/strong>)<\/strong><\/li>\n
  147. Galzitskaya<\/strong> Repeats are one of the main characteristics of RNA-binding proteins with prion-like domains. Mol Biosyst. 11(8):2210-8. (<\/strong>2015<\/strong>)<\/strong><\/li>\n
  148. Galzitskaya<\/strong> OV, Dovidchenko NV, Selivanova OM, Suvorina MY, Surin AK, Finkelstein AV. 171 Determination of the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of their formation. J Biomol Struct Dyn. 33 Suppl 1:112. (2015)<\/strong><\/li>\n
  149. Galzitskaya<\/strong> OV, Lobanov M. 170 Influence of homo-repeats on functions and aggregation propensities of protein chains. J Biomol Struct Dyn. 33 Suppl 1:111-2. (2015)<\/strong><\/li>\n
  150. Pereyaslavets L.B., Galzitskaya<\/strong>, O.V. Theoretical Search for RNA Folding Nuclei, Entropy, 17, 7827-7847. (2015)<\/strong><\/li>\n
  151. Suvorina M.Y., Selivanova O.M., Grigorashvili E.I., Nikulin A.D., Marchenkov V. V, Surin A.K., Galzitskaya<\/strong> V. Studies of Polymorphism of Amyloid-\u03b2 42 Peptide from Different Suppliers. J. Alzheimer\u2019s Dis., 47, 583\u2013593. (2015)<\/strong><\/li>\n
  152. Galzitskaya<\/strong>V. What is necessary to be prion-like domain? Atlas of Science, December 5, http:\/\/atlasofscience.org\/what-is-necessary-to-be\/<\/a> (2015)<\/strong><\/li>\n
  153. Galzitskaya<\/strong>V. Is it possible reversible and irreversible aggregation of proteins? Atlas of Science, December 23, http:\/\/atlasofscience.org\/is-it-possible-reversible-and\/<\/a> (2015)<\/strong><\/li>\n
  154. Galzitskaya<\/strong>V., Leonova E.I., Dovidchenko N.V. Possible mechanisms of amyloid growth Atlas of Science March 25, http:\/\/atlasofscience.org\/possible-mechanisms-of-amyloid-growth\/<\/a> (2016)<\/strong><\/li>\n
  155. Shilyaev N.G., Selivanova O.M., Galzitskaya<\/strong>V. Search for conserved amino acid residues of the alpha-crystallin proteins of vertebrate. Journal of Bioinformatics and Computational Biology. Apr;14(2):1641004, (2016)<\/strong>.<\/li>\n
  156. Bobylev AG, Galzitskaya<\/strong> OV, Fadeev RS, Bobyleva LG, Yurshenas DA, Molochkov NV, Dovidchenko NV, Selivanova OM, Penkov NV, Podlubnaya ZA, Vikhlyantsev IM. Smooth muscle titin forms in vitro amyloid aggregates. Bioscience Reports; 36(3). pii: e00334., DOI: 10.1042\/BSR20160066, PMID: 27129292 (2016)<\/strong><\/li>\n
  157. Oxana V. Galzitskaya<\/strong>, Nikita V. Dovidchenko, Olga M. Selivanova Kinetics of amyloid formation by different proteins and peptides: polymorphism and sizes of folding nuclei of fibrils. Book: in «Exploring New Findings on Amyloidosis», :Fernandez-Escamilla A.M.). Croatia: InTech, pp.143-163. ISBN 978-953-51-4716-9. (2016)<\/strong><\/li>\n
  158. Lobanov M, Klus P, Sokolovsky I, Tartaglia GG, Galzitskaya<\/strong> Non-random distribution of homo-repeats: links with biological functions and human diseases, Scientific Reports, 6:26941. doi: 10.1038\/srep26941. (2016)<\/strong><\/li>\n
  159. Dovidchenko, N.V., Glyakina, A.V., Selivanova, O.M., Grigorashvili, E.I., Suvorina, M.Y., Dzhus, U.F., Mikhailina, A.O., Shiliaev, N.G., Marchenkov, V.V., Surin, A.K., and Galzitskaya<\/strong>, O.V. One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of A\u03b240 and A\u03b242, J. Struct. Biol., 194, 404-414. doi: 10.1016\/j.jsb.2016.03.020 (2016)<\/strong><\/li>\n
  160. Galzitskaya<\/strong>V. Influence of Repeats in the Protein Chain on Its Aggregation Capacity for ALS-associated Proteins. Book: In: UPDATE ON AMYOTROPHIC LATERAL SCLEROSIS (eds.: Sibat H.F., Ibanez-Valdes L.F.). Croatia: InTech, pp. 101-120. ISBN 978-953-51-2600-3. (2016)<\/strong><\/li>\n
  161. Grigorashvili, O. M. Selivanova, N. V. Dovidchenko, U. F. Dzhus, A. O. Mikhailina, M. Yu. Suvorina, V. V. Marchenkov, A. K. Surin, O. V. Galzitskaya<\/strong>, Vol. 81, No. 5, pp. 710-720. ISSN 0006-2979, Biochemistry (Moscow), Vol. 81, No. 5, pp. 538-547. (2016)<\/strong><\/li>\n
  162. Galzitskaya<\/strong> To be folded, to be unfolded or to be aggregated? F1000 Research 5:817 (slide presentation) (doi: 10.7490\/f1000research.1111826.1) (2016)<\/strong><\/li>\n
  163. M. Selivanova, E. Yu. Gorbunova, L. G. Mustaeva, E. I. Grigorashvili, M. Yu. Suvorina, A. K. Surin and O. V. Galzitskaya<\/strong>, PEPTIDE A\u03b2(16\u201325) FORMS NANOFILMS IN THE PROCESS OF ITS AGGREGATION. Biochemistry (Moscow), 81, 755-761. (2016)<\/strong><\/li>\n
  164. K. Surin, E. I. Grigorashvili, M. Yu. Suvorina, O. M. Selivanova, and O. V. Galzitskaya<\/strong>, DETERMINATION OF REGIONS INVOLVED IN AMYLOID FIBRIL FORMATION FOR A\u03b2(1\u201340) PEPTIDE. Biochemistry (Moscow), 81, 762-769. (2016)<\/strong><\/li>\n
  165. Selivanova, OM; Grigorashvili, EI; Suvorina, MY; Dzhus, UF; Nikulin, AD; Marchenkov, VV; Surin, AK; Galzitskaya<\/strong>, OV. X-ray diffraction and electron microscopy data for amyloid formation of A\u03b240 and A\u03b242; Data in Brief PMID: 27294177;8:108-13. doi: 10.1016\/j.dib.2016.05.020. (2016)<\/strong><\/li>\n
  166. Selivanova OM, Surin AK, Marchenkov VV, Dzhus UF, Grigorashvili EI, Suvorina MY, Glyakina AV, Dovidchenko NV, Galzitskaya OV<\/strong>. The Mechanism Underlying Amyloid Polymorphism is Opened for Alzheimer\u2019s Disease Amyloid-\u03b2 Peptide J. of Alzheimer’s disease, 54<\/strong>, 821-830. doi: 10.3233\/JAD-160405 http:\/\/www.j-alz.com\/vol54-2, PMID: 27567850., http:\/\/www.j-alz.com\/vol54-2<\/a> (2016)<\/strong><\/li>\n
  167. Dovidchenko NV, Selivanova OM., Galzitskaya<\/strong> One of the mechanisms of amyloid fibrils formation based on the sizes of folding nuclei of A\u03b240 and A\u03b242. Atlas of Science http:\/\/atlasofscience.org\/one-of-the-mechanisms-of-amyloid-fibrils-formation-based-on-the-sizes-of-folding-nuclei-of-a%CE%B240-and-a%CE%B242\/<\/a> (2016)<\/strong><\/li>\n
  168. Selivanova, O.M. Grigorashvili, E.I. Suvorina, M.Y. Dzhus, U.F. Nikulin, A.D. Marchenkov, V.V. Surin, A.K. Galzitskaya<\/strong>, O.V. X-ray diffraction and electron microscopy data for amyloid formation of A\u03b240 and A\u03b242; Data in Brief, PMID: 27294177; 8:108-13. (2016)<\/strong><\/li>\n
  169. Selivanova O.M., Glyakina A.V., Gorbunova E.Yu., Mustaeva L.G., Suvorina M.Yu., Grigorashvili E.I., Nikulin A.D., Dovidchenko N.V., Rekstina V.V, Kalebina T.S., Surin A.K., Galzitskaya<\/strong>V. Structural model of amyloid fibrils for amyloidogenic peptide from Bgl2p — glucantransferase of S. cerevisiae cell wall and its modifying analogue. New morphology of amyloid fibrils. Biochim Biophys Acta. 1864(11):1489-1499. doi: 10.1016\/j.bbapap.2016.08.002.(2016)<\/strong><\/li>\n
  170. Glyakina A.V., Balabaev N.K., Galzitskaya<\/strong>V. Dataset of the molecular dynamics simulations of bilayers consisting of short amyloidogenic peptide VDSWNVLVAG from Bgl2p-glucantransferase of S. cerevisiae cell wall. Data in Brief. DIB1121, 9, 597-601 10.1016\/j.dib.2016.09.043<\/a>, 10.1016\/j.dib.2016.09.043. (2016)<\/strong><\/li>\n
  171. Deryusheva EI, Machulin AV, Selivanova OM, Galzitskaya<\/strong> Taxonomic distribution, repeats, and functions of the S1 domain-containing proteins as members of the OB-fold family. Proteins. 85(4):602-613. (201<\/strong>7<\/strong>)<\/strong><\/li>\n
  172. Fontanillas E, Galzitskaya<\/strong> OV, Lecompte O, Lobanov MY, Tanguy A, Mary J, Girguis PR, Hourdez S, Jollivet D. Proteome evolution of deep-sea hydrothermal vent alvinellid polychaetes supports the ancestry of thermophily and subsequent adaptation to cold in some lineages. Genome Biol Evol. 9(2):279-296. doi: 10.1093\/gbe\/evw298. (2017)<\/strong><\/li>\n
  173. Selivanova OM, Suvorina MY, Surin AK, Dovidchenko NV, Galzitskaya<\/strong> Insulin and LysPro Insulin: What is Common and Different in Their Behaviour? Curr Protein Pept Sci. 18(1):57-64 (2017)<\/strong><\/li>\n
  174. Tikhomirova TS, Selivanova OM, Galzitskaya<\/strong> \u03b1-Crystallins Are Small Heat Shock Proteins: Functional and Structural Properties. Biochemistry (Mosc). Feb;82(2):106-121. doi: 10.1134\/S0006297917020031. Review. PubMed PMID: 28320295. (2017)<\/strong><\/li>\n
  175. Finkelstein AV, Badretdin AJ, Galzitskaya<\/strong> OV, Ivankov DN, Bogatyreva NS, Garbuzynskiy SO. There and back again: Two views on the protein folding puzzle. Phys Life Rev. 56-71. doi: 10.1016\/j.plrev.2017.01.025. Review. PubMed PMID: 28190683. IF=13.840 (2017)<\/strong><\/li>\n
  176. Olga M. Selivanova, Oxana V. Galzitskaya<\/strong> Unusual structure of aggregates formed by the fragment of \u0410\u03b2(16-25) peptide http:\/\/atlasofscience.org\/unusual-structure-of-aggregates-formed-by-the-fragment-of-%D0%B0%CE%B216-25-peptide\/#more-20667<\/a> (2017)<\/strong><\/li>\n
  177. Nikita V. Dovidchenko, Olga M. Selivanova, Oxana V. Galzitskaya<\/strong> Determination of the size of folding nuclei of fibrils formed from A\u03b2(1-40) peptide http:\/\/atlasofscience.org\/determination-of-the-size-of-folding-nuclei-of-fibrils-formed-from-a%CE%B21-40-peptide\/<\/a> (2017)<\/strong><\/li>\n
  178. Leonova E.I., Solonin A.S., Galzitskaya<\/strong>V., Shaykhutdinova E.R., Lobanov A.V., Murashev A.N. Expression of sdc1 gene in aortic arch and the serum concentration of \u00absoluble\u00bb \u0421D138 in ApoE knockout mice, Pathogenesis, \u21161, pp.34-39. (2017)<\/strong><\/li>\n
  179. Olga M. Selivanova, Alexey K. Surin, Tatyana S. Kalebina, Oxana V. Galzitskaya<\/strong>, New morphology of amyloid fibrils. http:\/\/atlasofscience.org\/new-morphology-of-amyloid-fibrils\/#more-21199<\/a> (2017)<\/strong><\/li>\n
  180. Alexey K. Surin, Oxana V. Galzitskaya<\/strong>, Determination of regions involved in amyloid fibril formation for A\u03b2(1-40) peptide, https:\/\/atlasofscience.org\/determination-of-regions-involved-in-amyloid-fibril-formation-for-a%CE%B21-40-peptide\/<\/a> (2017)<\/strong><\/li>\n
  181. Leonova I., Sadovnikova E.S., Shaykhutdinova E.R., Galzitskaya<\/strong> O.V., Murashev A.N., <\/sub>Solonin A.S. Hepatic and aortic arch expression and serum levels of syndecan-1 in ApoE-\/- mice. The Open Biochemistry Journal, 2017, 11:77-93. doi: 10.2174\/1874091X01711010077. eCollection 2017. (2017)<\/strong><\/li>\n
  182. Galzitskaya OV<\/strong>, Selivanova OM. Rosetta Stone for Amyloid Fibrils: The Key Role of Ring-Like Oligomers in Amyloidogenesis. Journal of Alzheimer\u2019s Disease, 59(3):785-795. doi: 10.3233\/JAD-170230. (201<\/strong>7<\/strong>)<\/strong><\/li>\n
  183. Glyakina AV, Likhachev IV, Balabaev NK, Galzitskaya<\/strong> Comparative mechanical unfolding studies of spectrin domains R15, R16 and R17. J Struct Biol. 201(2):162-170. doi: 10.1016\/j.jsb.2017.12.003. PMID: 29221897 (201<\/strong>8<\/strong>)<\/strong><\/li>\n
  184. Finkelstein A.V., Badretdin A.J., Galzitskaya<\/strong>V., Ivankov D.N., Bogatyreva N.S., Garbuzynskiy S.O. Two views on the protein folding puzzle. In: Trends in Biomathematics: Modeling, Optimization and Computational Problems (Mondiani R.P., Ed.), Springer Nature Switzerland AG, Bazel, 2018, pp.391-412. (<\/strong>2018<\/strong>)<\/strong><\/li>\n
  185. Selivanova OM, Surin AK, Ryzhykau YL, Glyakina AV, Suvorina MY, Kuklin AI, Rogachevsky VV, Galzitskaya<\/strong> To Be Fibrils or To Be Nanofilms? Oligomers Are Building Blocks for Fibril and Nanofilm Formation of Fragments of A\u03b2 Peptide. Langmuir. 34(6):2332-2343. doi: 10.1021\/acs.langmuir.7b03393. Epub 2018 Jan 30. PubMed PMID: 29338255. (2018<\/strong>)<\/strong><\/li>\n
  186. Finkelstein AV, Dovidchenko NV, Galzitskaya<\/strong> What is Responsible for Atypical Dependence of the Rate of Amyloid Formation on Protein Concentration: Fibril-Catalyzed Initiation of New Fibrils or Competition with Oligomers? J Phys Chem Lett. 2018 Feb 12:1002-1006. doi: 10.1021\/acs.jpclett.7b03442. PubMed PMID: 29412673. (201<\/strong>8<\/strong>)<\/strong><\/li>\n
  187. Selivanova OM, Grishin SY, Glyakina AV, Sadgyan AS, Ushakova NI, Galzitskaya<\/strong> Analysis of Insulin Analogs and the Strategy of Their Further Development. Biochemistry (Moscow), 83(1), S146-S162 doi 10.1134\/S0006297918140122, http:\/\/link.springer.com\/article\/10.1134\/S0006297918140122<\/a> (201<\/strong>8<\/strong>)<\/strong><\/li>\n
  188. Galzitskaya<\/strong> OV, Galushko EI, Selivanova OM. Studies of the Process of Amyloid Formation by A\u03b2 Peptide. Biochemistry (Moscow), 83(1), S62-S80, doi 10.1134\/S0006297918140079, http:\/\/link.springer.com\/article\/10.1134\/S0006297918140079<\/a> (201<\/strong>8<\/strong>)<\/strong><\/li>\n
  189. Selivanova O.M., Rogachevsky V.V., Surin A.K., Galzitskaya<\/strong>V., Molecular mechanism of amyloid formation by Abeta peptide: review of own works, Biomedical Chemistry, 64, 94-109. (201<\/strong>8<\/strong>)<\/strong><\/li>\n
  190. Deryusheva E, Machulin A, Nemashkalova E, Glyakina A, Galzitskaya<\/strong> Search for Functional Flexible Regions in the G-protein Family: New Reading of the FoldUnfold Program. Protein Pept Lett. 25(6):589-598. doi: 10.2174\/0929866525666180621143957. PubMed PMID: 29929460. (201<\/strong>8<\/strong>)<\/strong><\/li>\n
  191. Galzitskaya<\/strong> OV, Lobanov MY. Proteome-scale understanding of relationship between homo-repeat enrichments and protein aggregation properties. PLoS One. 2018 Nov 6;13(11):e0206941. doi: 10.1371\/journal.pone.0206941. eCollection 2018. PubMed PMID: 30399196; PubMed Central PMCID: PMC6219797. (201<\/strong>8<\/strong>)<\/strong><\/li>\n
  192. Galzitskaya<\/strong> OV, Surin AK, Glyakina AV, Rogachevsky VV, Selivanova OM. Should the Treatment of Amyloidosis Be Personified? Molecular Mechanism of Amyloid Formation by A\u03b2 Peptide and Its Fragments. J Alzheimers Dis Rep. 2(1):181-199. doi: 10.3233\/ADR-180063. PubMed PMID: 30480261; PubMed Central PMCID: PMC6218156. (201<\/strong>8<\/strong>)<\/strong><\/li>\n
  193. Olga M. Selivanova, Oxana V. Galzitskaya<\/strong> Some questions remain unanswered for alpha-Crystallin. http:\/\/atlasofscience.org\/some-questions-remain-unanswered-for-alpha-crystallin\/#more-24585<\/a> (2018<\/strong>)<\/strong><\/li>\n
  194. Tikhomirova TS, Galzitskaya<\/strong> [Functionally Significant Amino Acid Motifs of Heat Shock Proteins: Structural and Bioinformatics Analyses of Hsp60\/Hsp10 in Five Classes of Chordata]. Mol Biol (Mosk). 52(5):879-897. doi:10.1134\/S0026898418050130. Russian. PubMed PMID: 30363062. (201<\/strong>8<\/strong>)<\/strong><\/li>\n
  195. Glyakina AV, Strizhov NI, Karpov MV, Dovidchenko NV, Matkarimov BT, Isaeva LV, Efimova VS, Rubtsov MA, Novikova LA, Donova MV, Galzitskaya<\/strong> Ile351, Leu355 and Ile461 residues are essential for catalytic activity of bovine cytochrome P450scc (CYP11A1). Steroids. 143:80-90. doi: 10.1016\/j.steroids.2019.01.002. (<\/strong>201<\/strong>9)<\/strong><\/li>\n
  196. Litus EA, Kazakov AS, Sokolov AS, Nemashkalova EL, Galushko EI, Dzhus UF, Marchenkov VV, Galzitskaya<\/strong> OV, Permyakov EA, Permyakov SE. The binding of monomeric amyloid \u03b2 peptide to serum albumin is affected by major plasma unsaturated fatty acids. Biochem Biophys Res Commun.; 510(2):248-253. doi: 10.1016\/j.bbrc.2019.01.081. (201<\/strong>9<\/strong>)<\/strong><\/li>\n
  197. Galzitskaya<\/strong> New mechanism of amyloid fibril formation. Curr Protein Pept Sci. 20(6):630-640. doi: 10.2174\/1389203720666190125160937. (201<\/strong>9<\/strong>)<\/strong><\/li>\n
  198. Galzitskaya<\/strong> OV, Novikov GS, Dovidchenko NV, Lobanov MY. Is there codon usage bias for poly-Q stretches in the human proteome? J Bioinform Comput Biol. 17(1):1950010. doi: 10.1142\/S0219720019500100. PubMed PMID: 30866735. (201<\/strong>9<\/strong>)<\/strong><\/li>\n
  199. Surin AK, Grishin SY, Galzitskaya<\/strong> Identification of Amyloidogenic Regions in the Spine of Insulin Fibrils. Biochemistry (Mosc).; 84(1):47-55. doi: 10.1134\/S0006297919010061. PubMed PMID: 30927525. (201<\/strong>9<\/strong>)<\/strong><\/li>\n
  200. Machulin A, Deryusheva E, Lobanov M, Galzitskaya<\/strong> Int J Mol Sci.; 20(10). pii: E2377. doi: 10.3390\/ijms20102377. (201<\/strong>9<\/strong>)<\/strong><\/li>\n
  201. Deryusheva E.I., Machulin A.V., Matyunin M.A., Galzitskaya <\/strong>V. Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure. Molecules. 24(20). pii: E3681. doi: 10.3390\/molecules24203681 (2019)<\/strong><\/li>\n
  202. Machulin AV, Deryusheva EI, Selivanova OM, Galzitskaya <\/strong> The number of domains in the ribosomal protein S1 as a hallmark of the phylogenetic grouping of bacteria. PLoS One. 14(8):e0221370. doi:10.1371\/journal.pone.0221370. (2019)<\/strong><\/li>\n
  203. Galzitskaya<\/strong> OV, Oligomers are promising targets for drug development in the treatment of proteinopathies. Frontiers in Molecular Neuroscience, doi: 10.3389\/fnmol.2019.00319 (2019)<\/strong><\/li>\n
  204. Galzitskaya<\/strong> OV, Novikov GS. [An Overlap between Splicing Sites in RNA and Homo-Repeats in Human Proteins]. Mol Biol (Mosk). 53(3):524-528. doi: 10.1134\/S0026898419030066. Russian. PubMed PMID: 31184618. (2020)<\/strong><\/li>\n
  205. Galzitskaya O.V.<\/strong>, Grishin S.Y., Dzhus U.F., Selivanova O.M., Glyakina A.V., Deryusheva E.I., Machulin A.V., Suvorina M.Y., Surin, A.K. Identification of amyloidogenic regions in S1 ribosomal proteins from Thermus thermophilus and Mycoplasma mobile. FEBS Open Bio, P-27-053, DOI:10.1002\/2211-5463.12675 (2019)<\/strong><\/li>\n
  206. Grishin SY, Dzhus UF, Selivanova OM, Balobanov VA, Surin AK, Galzitskaya OV<\/strong>. Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable Fragment. Biochemistry (Mosc). 85(3):344-354. doi: 10.1134\/S0006297920030104. (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  207. Grishin SY, Deryusheva EI, Machulin AV, Selivanova OM, Glyakina AV, Gorbunova EY, Mustaeva LG, Azev VN, Rekstina VV, Kalebina TS, Surin AK, Galzitskaya OV.<\/strong> Amyloidogenic Propensities of Ribosomal S1 Proteins: Bioinformatics Screening and Ex-perimental Checking. Int J Mol Sci. 21(15):5199. doi: 10.3390\/ijms21155199. (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  208. Kurpe SR, Grishin SY, Surin AK, Selivanova OM, Fadeev RS, Dzhus UF, Gorbunova EY, Mustaeva LG, Azev VN, Galzitskaya OV.<\/strong> Antimicrobial and Amyloidogenic Activi-ty of Peptides Synthesized on the Basis of the Ribosomal S1 Protein from Thermus Thermophilus. Int J Mol Sci. 21(17):6382. doi: 10.3390\/ijms21176382. (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  209. Lobanov MY, Likhachev IV, Galzitskaya OV<\/strong>. Disordered Residues and Patterns in the Protein Data Bank. Molecules. 25(7):1522. doi: 10.3390\/molecules25071522. (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  210. Sobolev E, Zolotarev S, Giewekemeyer K, Bielecki J, Okamoto K, Reddy HKN., Andreasson J, Ayyer K, Barak I, Bari S, Barty A, Bean R, Bobkov S, Chapman HN, Chojnowski G, Daurer BJ, Dorner K, Ekeberg T, Fluckiger L, Galzitskaya O<\/strong>, Gelisio L, Hauf S, Hogue BG, Horke DA, Hosseinizadeh A, Ilyin V, Jung C, Kim C, Kim Y, Kirian RA, Kirkwood H, Kulyk O, Kupper J, Letrun R, Loh ND, Lorenzen K, Messerschmidt M, Muhlig K, Ourmazd A, Raab N, Rode AV, Rose M, Round A, Sato T, Schubert R, Schwander P, Sellberg JA, Sikorski M, Silenzi A, Song CY, Spence JCH, Stern S, Sztuk-Dambietz J, Teslyuk A, Timneanu N, Trebbin M, Uetrecht C, Weinhausen B, Williams GJ, Xavier PL, Xu C, Vartanyants IA, Lamzin VS, Mancuso A, Maia FRNC. Megahertz single-particle imaging at the European XFEL. Communications physics. 2020, 3(1):97. DOI: 10.1038\/s42005-020-0362-y. (2020)<\/strong><\/li>\n
  211. Slizen MV, Galzitskaya OV.<\/strong> Comparative Analysis of Proteomes of a Number of Noso-comial Pathogens by KEGG Modules and KEGG Pathways. Int J Mol Sci. 21(21):7839. doi: 10.3390\/ijms21217839. (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  212. \u041a\u0443\u0440\u043f\u0435 \u0421\u0420, \u0413\u0440\u0438\u0448\u0438\u043d \u0421\u042e, \u0421\u0435\u043b\u0438\u0432\u0430\u043d\u043e\u0432\u0430 \u041e\u041c, \u0421\u0443\u0440\u0438\u043d \u0410\u041a, \u0413\u0430\u043b\u0437\u0438\u0442\u0441\u043a\u0430\u044f \u041e\u0412<\/strong>. A\u043d\u0442\u0438\u0431\u0430\u043a\u0442\u0435\u0440\u0438\u0430\u043b\u044c\u043d\u044b\u0435 \u044d\u0444\u0444\u0435\u043a\u0442\u044b \u043f\u0435\u043f\u0442\u0438\u0434\u043e\u0432, \u0441\u0438\u043d\u0442\u0435\u0437\u0438\u0440\u043e\u0432\u0430\u043d\u043d\u044b\u0445 \u043d\u0430 \u043e\u0441\u043d\u043e\u0432\u0435 \u043f\u043e\u0441\u043b\u0435\u0434\u043e\u0432\u0430\u0442\u0435\u043b\u044c\u043d\u043e\u0441\u0442\u0438 \u0440\u0438\u0431\u043e\u0441\u043e\u043c\u043d\u043e\u0433\u043e \u0431\u0435\u043b\u043a\u0430 S1 \u0438\u0437 Thermus Thermophilus. \u0410\u043a\u0442\u0443\u0430\u043b\u044c\u043d\u0430\u044f \u0431\u0438\u043e\u0442\u0435\u0445\u043d\u043e\u043b\u043e\u0433\u0438\u044f. 3(34):372-376. (2020<\/strong>)<\/strong><\/li>\n
  213. \u0414\u0435\u0440\u044e\u0448\u0435\u0432\u0430 \u0415\u0418, \u041c\u0430\u0447\u0443\u043b\u0438\u043d \u0410\u0412, \u0421\u0435\u043b\u0438\u0432\u0430\u043d\u043e\u0432\u0430 \u041e\u041c, \u0413\u0440\u0438\u0448\u0438\u043d \u0421\u042e, \u0413\u043b\u044f\u043a\u0438\u043d\u0430 \u0410\u0412, \u0421\u0443\u0440\u0438\u043d \u0410\u041a, \u0413\u0430\u043b\u0437\u0438\u0442\u0441\u043a\u0430\u044f<\/strong> \u041e\u0412. \u0418\u0437\u0443\u0447\u0435\u043d\u0438\u0435 \u0444\u0438\u0431\u0440\u0438\u043b\u043b\u043e\u043e\u0431\u0440\u0430\u0437\u043e\u0432\u0430\u043d\u0438\u044f \u0430\u043c\u0438\u043b\u043e\u0438\u0434\u043e\u0433\u0435\u043d\u043d\u044b\u0445 \u0443\u0447\u0430\u0441\u0442\u043a\u043e\u0432 \u0440\u0438\u0431\u043e\u0441\u043e\u043c\u043d\u044b\u0445 \u0431\u0435\u043b\u043a\u043e\u0432 S1. \u0414\u043e\u043a\u043b\u0430\u0434\u044b \u041c\u0435\u0436\u0434\u0443\u043d\u0430\u0440\u043e\u0434\u043d\u043e\u0439 \u043a\u043e\u043d\u0444\u0435\u0440\u0435\u043d\u0446\u0438\u0438 «\u041c\u0430\u0442\u0435\u043c\u0430\u0442\u0438\u0447\u0435\u0441\u043a\u0430\u044f \u0431\u0438\u043e\u043b\u043e\u0433\u0438\u044f \u0438 \u0431\u0438\u043e\u0438\u043d\u0444\u043e\u0440\u043c\u0430\u0442\u0438\u043a\u0430». \u041f\u043e\u0434 \u0440\u0435\u0434. \u0412.\u0414. \u041b\u0430\u0445\u043d\u043e. \u041f\u0443\u0449\u0438\u043d\u043e: \u0418\u041c\u041f\u0411 \u0420\u0410\u041d, \u0442\u043e\u043c 8, \u0441\u0442\u0430\u0442\u044c\u044f \u2116 e13. doi: 10.17537\/icmbb20.19. (2020)<\/strong><\/li>\n
  214. Surin AK, Grishin SYu, Galzitskaya <\/strong> Determination of amyloid core regions of insulin analogues fibrils. Prion. 14(1): 149\u2013162. doi: 10.1080\/19336896.2020.1776062. (2020<\/strong>)<\/strong><\/li>\n
  215. Glyakina A.V., Surin A.K, Grishin S.Yu., Selivanova O.M., Suvorina M.Yu., Bobyleva L.G., Vikhlyantsev I.M., Galzitskaya<\/strong>V. New Model for Stacking Monomers in Fila-mentous Actin from Skeletal Muscles of Oryctolagus cuniculus. Int J Mol Sci. 21(21): 8319. doi: 10.3390\/ijms21218319. (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  216. Glyakina A.V., Galzitskaya<\/strong>V. How Quickly Do Proteins Fold and Unfold, and What Structural Parameters Correlate with These Values? Biomolecules. 10(2): 197. doi: 10.3390\/biom10020197. (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  217. Selivanova OM, Galzitskaya<\/strong> Structural and Functional Peculiarities of \u03b1-Crystallin. Biology (Basel) 9(4): 85. doi: 10.3390\/biology9040085. (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  218. Glyakina A.V., Galzitskaya <\/strong>V. Bioinformatics Analysis of Actin Molecules: Why Quantity Does Not Translate Into Quality? Front. Genet., 11: 617763 doi: 10.3389\/fgene.2020.617763. (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  219. Bobylev AG, Yakupova EI, Bobyleva LG, Galzitskaya OV<\/strong>, Nikulin AD, Shumeyko SA, Yurshenas DA, Vikhlyantsev IM. Changes in Titin Structure during Its Aggregation. Mol Biol (Mosk). 54(4):643-652. doi: 10.31857\/S0026898420040047. (2020<\/strong>)<\/strong><\/li>\n
  220. Martins PM, Navarro S, Silva A, Pinto MF, S\u00e1rk\u00e1ny Z, Figueiredo F, Pereira PJB, Pinhei-ro F, Bednarikova Z, Burdukiewicz M, Galzitskaya<\/strong> OV, Gazova Z, Gomes CM, Pastore A, Serpell LC, Skrabana R, Smirnovas V, Ziaunys M, Otzen DE, Ventura S, Macedo-Ribeiro S. MIRRAGGE — Minimum Information Required for Reproducible AGGrega-tion Experiments. Front Mol Neurosci 13: 582488. DOI: 10.3389\/fnmol.2020.582488 (<\/strong>2020<\/strong>)<\/strong><\/li>\n
  221. Kurpe S.R., Grishin S.Yu., Surin A.K., Panfilov A.V., Slizen M.V., Chowdhury S.D., Galzitskaya<\/strong>V. Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimi-crobial Peptides Be Used Against SARS-CoV-2? INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 21, 9552. https:\/\/doi.org\/10.3390\/ijms21249552 (2020)<\/strong><\/li>\n
  222. V. LikhachevN. K. Balabaev, O.V. Galzitskaya.<\/strong> Elastic and Non-elastic Properties of Cadherin Ectodomain: Comparison with Mechanical System, https:\/\/link.springer.com\/chapter\/10.1007\/978-3-030-16621-2_52<\/a> International Conference on Computer Science, Engineering and Education Applications ICCSEEA 2019: Advances in Computer Science for Engineering and Education II pp 555-566 (2020)<\/strong><\/li>\n
  223. Deryusheva E, Machulin A, Matyunin M, Galzitskaya<\/strong> Sequence and evolutionary analysis of bacterial ribosomal S1 proteins. Proteins. 89(9):1111-1124. doi: 10.1002\/prot.26084. (<\/strong>2021<\/strong>)<\/strong><\/li>\n
  224. Grishin SY, Dzhus UF, Glukhov AS, Selivanova OM, Surin AK, Galzitskaya<\/strong> Identification of Amyloidogenic Regions in Pseudomonas aeruginosa Ribosomal S1 Protein. Int J Mol Sci. 22(14):7291. doi: 10.3390\/ijms22147291. (2021)<\/strong><\/li>\n
  225. Galzitskaya<\/strong> Exploring Amyloidogenicity of Peptides From Ribosomal S1 Protein to Develop Novel AMPs. Front Mol Biosci. 2021 Aug 19;8:705069. doi: 10.3389\/fmolb.2021.705069. eCollection (2021)<\/strong>.<\/li>\n
  226. Kurpe SR, Grishin SY, Glyakina AV, Slizen MV, Panfilov AV, Kochetov AP, Surin AK, Kobyakova MI, Fadeev RS, Galzitskaya<\/strong> Biomed Khim. 67(3):231-243. doi: 10.18097\/PBMC20216703231. (<\/strong>2021<\/strong>)<\/strong><\/li>\n
  227. Grishin SY, Domnin PA, Kravchenko SV, Azev VN, Mustaeva LG, Gorbunova EY, Kobyakova MI, Surin AK, Makarova MA, Kurpe SR, Fadeev RS, Vasilchenko AS, Firstova VV, Ermolaeva SA, Galzitskaya<\/strong> Is It Possible to Create Antimicrobial Peptides Based on the Amyloidogenic Sequence of Ribosomal S1 Protein of P. aeruginosa? Int J Mol Sci.;22(18):9776. doi: 10.3390\/ijms22189776. (2021)<\/strong><\/li>\n
  228. Lobanov M.Yu., Pereyaslavets L.B., Likhachev I.V., Matkarimov B.T., Galzitskaya <\/strong>V. Is there an advantageous arrangement of aromatic residues in proteins? Statistical analysis of aromatic interactions in globular proteins. Computational and Structural Biotechnology Journal 19 5960\u20135968 https:\/\/doi.org\/10.1016\/j.csbj.2021.10.036<\/a> (2021)<\/strong><\/li>\n
  229. Galzitskaya<\/strong>V., Selivanova O.M., Gorbunova E.Y., Mustaeva L.G., Azev V.N., Surin A.K. Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides. Nanomaterials (Basel).;11(11):3129. doi: 10.3390\/nano11113129. (<\/strong>2021<\/strong>)<\/strong><\/li>\n
  230. Necci M, Piovesan D, CAID Predictors (including Galzitskaya O<\/strong>); DisProt Curators; Tosatto SCE. Critical assessment of protein intrinsic disorder prediction. Nature Methods;18(5):472-481. doi: 10.1038\/s41592-021-01117-3. (2021)<\/strong><\/li>\n
  231. Deryusheva EI, Machulin AV, Galzitskaya<\/strong> Structural, Functional, and Evolutionary Characteristics of Proteins with Repeats. Mol Biol (Mosk) 55(5):748-771. doi: 10.31857\/S0026898421050037. (2021)<\/strong><\/li>\n
  232. Bobyleva LG, Shumeyko SA, Yakupova EI, Surin AK, Galzitskaya<\/strong> OV, Kihara H, Timchenko AA, Timchenko MA, Penkov NV, Nikulin AD, Suvorina MY, Molochkov NV, Lobanov MY, Fadeev RS, Vikhlyantsev IM, Bobylev AG. Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro. Int J Mol Sci.;22(2):731. doi: 10.3390\/ijms22020731. (2021)<\/strong><\/li>\n
  233. Glyakina AV, Pavlov CD, Sopova JV, Gainetdinov RR, Leonova EI, Galzitskaya OV<\/strong>. Search for Structural Basis of Interactions of Biogenic Amines with Human TAAR1 and TAAR6 Receptors. Int J Mol Sci. 2021 Dec 25;23(1):209. doi: 10.3390\/ijms23010209. PMID: 35008636. (2021)<\/strong><\/li>\n
  234. Tikhomirova TS, Matyunin MA,Lobanov MY, Galzitskaya OV<\/strong>. In-depth analysis of amino acidand nucleotide sequences of Hsp60: How conserved is this protein? Proteins. 2022;1-23. doi:10.1002\/prot.26294 (2022)<\/strong><\/li>\n
  235. Glyakina A.V., Balabaev N.K., and Galzitskaya<\/strong>V. Determination of the Most Stable Packing of Peptides From Ribosomal S1 Protein, Protein Bgl2p and Abeta peptide in beta-layers during Molecular Dynamics Simulations. (2022)<\/strong> Methods Mol Biol.; 2340:221-233. doi: 10.1007\/978-1-0716-1546-1_11.<\/li>\n
  236. Kravchenko SV, Domnin PA, Grishin SY, Panfilov AV, Azev VN, Mustaeva LG, Gorbunova EY, Kobyakova MI, Surin AK, Glyakina AV, Fadeev RS, Ermolaeva SA, Galzitskaya OV<\/strong>. Multiple Antimicrobial Effects of Hybrid Peptides Synthesized Based on the Sequence of Ribosomal S1 Protein from Staphylococcus aureus. Int J Mol Sci. 2022 Jan 4;23(1):524. doi: 10.3390\/ijms23010524. PMID: 35008951. (2022)<\/strong><\/li>\n
  237. Galzitskaya OV<\/strong>, Selivanova OM, Dzhus UF, Marchenkov VV, Suvorina MY, Surin AK. Influence of Chaperones on Amyloid Formation of \u0410\u03b2 Peptide. Curr Protein Pept Sci. 2022 Jan 27. doi: 10.2174\/1389203723666220127152545. Epub ahead of print. PMID: 35086445. (2022)<\/strong><\/li>\n
  238. Galzitskaya OV<\/strong>, Kurpe SR, Panfilov AV, Glyakina AV, Grishin SY, Kochetov AP, Deruysheva EI, Machulin AV, Kravchenko SV, Domnin PA, Surin AK, Azev VN and Ermolaeva SA. Amyloidogenic Peptides: New Class of Antimicrobial Peptides with the Novel Mechanism of Activity. Int J Mol Sci. (2022) <\/strong>23(10):5463. doi: 10.3390\/ijms23105463.<\/li>\n
  239. Likhachev IV, Balabaev NK, Galzitskaya OV. <\/strong>Is It Possible to Find an Antimicrobial Peptide That Passes the Membrane Bilayer with Minimal Force Resistance? An Attempt at a Predictive Approach by Molecular Dynamics Simulation. (2022) <\/strong>Int J Mol Sci;23(11):5997. doi: 10.3390\/ijms23115997.<\/li>\n
  240. Kogan GL, Mikhaleva EA, Olenkina OM, Ryazansky SS, Galzitskaya OV<\/strong>, Abramov YA, Leinsoo TA, Akulenko NV, Lavrov SA, Gvozdev VA. Extended disordered regions of ribosome-associated NAC proteins paralogs belong only to the germline in Drosophila melanogaster. (2022)<\/strong> Sci Rep.;12(1):11191. doi: 10.1038\/s41598-022-15233-3.<\/li>\n
  241. Kachkin DV, Volkov KV, Sopova JV, Bobylev AG, Fedotov SA, Inge-Vechtomov SG, Galzitskaya OV<\/strong>, Chernoff YO, Rubel AA, Aksenova AY. Human RAD51 Protein Forms Amyloid-like Aggregates In Vitro. (2022) Int J Mol Sci. 23(19):11657. doi: 10.3390\/ijms231911657.<\/li>\n
  242. Aksenova, A.Y.; Likhachev, I.V.; Grishin, S.Y.; Galzitskaya, O.V.<\/strong> The Increased Amyloidogenicity of Spike RBD and pH-Dependent Binding to ACE2 May Contribute to the Transmissibility and Pathogenic Properties of SARS-CoV-2 Omicron as Suggested by In Silico Study. J. Mol. Sci.<\/em> 2022<\/strong>, 23<\/em>, 13502. https:\/\/doi.org\/10.3390\/ijms232113502<\/li>\n<\/ol>\n

     <\/p>\n","protected":false},"excerpt":{"rendered":"

    M. Gutin and O.V.Galzitskaia, Helix-coil transition in the simplest model of large native RNA. I. Consideration of only native helices. Biofizika, 38(1), 84-92, Russian (1993) M. Gutin and O.V.Galzitskaia, Helix-coil transition in the simplest models of large native RNA. II. Consideration of nonspecific interactions. Biofizika, 38(1), 93-98, Russian (1993) V. Galzitskaia, B.A. Reva and A.V. … Read More «List of scientific papers of O.V. Galzitskaya»<\/span> »<\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"parent":44,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-14","page","type-page","status-publish","hentry"],"jetpack_sharing_enabled":true,"_links":{"self":[{"href":"http:\/\/bioproteom.protres.ru\/mainw\/wp-json\/wp\/v2\/pages\/14","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/bioproteom.protres.ru\/mainw\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/bioproteom.protres.ru\/mainw\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/bioproteom.protres.ru\/mainw\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"http:\/\/bioproteom.protres.ru\/mainw\/wp-json\/wp\/v2\/comments?post=14"}],"version-history":[{"count":3,"href":"http:\/\/bioproteom.protres.ru\/mainw\/wp-json\/wp\/v2\/pages\/14\/revisions"}],"predecessor-version":[{"id":21,"href":"http:\/\/bioproteom.protres.ru\/mainw\/wp-json\/wp\/v2\/pages\/14\/revisions\/21"}],"up":[{"embeddable":true,"href":"http:\/\/bioproteom.protres.ru\/mainw\/wp-json\/wp\/v2\/pages\/44"}],"wp:attachment":[{"href":"http:\/\/bioproteom.protres.ru\/mainw\/wp-json\/wp\/v2\/media?parent=14"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}