All publications

List of publications

2021

  1. Efimova, V. S, Isaeva, L. V, Orekhov, P. S, Bozdaganyan, M. E, Rubtsov, M. A and Novikova, L. A. Using a viral 2A peptide-based strategy to reconstruct the bovine P450scc steroidogenic system in S. cerevisiae. In Journal of Biotechnology, 325, 2021. [doi..
  2. Yudenko, A., Smolentseva, A., Maslov, I., Semenov, O., Goncharov, I. M, Nazarenko, V. V, Maliar, N. L, Borshchevskiy, V., Gordeliy, V., Remeeva, A. and Gushchin, I. Rational Design of a Split Flavin-Based Fluorescent Reporter. In ACS Synthetic Biology, 10 (1): 72-83, 2021. [doi..
  3. Ryzhykau, Y. L., Orekhov, P. S., Rulev, M. I., Vlasov, A. V., Melnikov, I. A., Volkov, D. A., Nikolaev, M. Yu., Zabelskii, D. V., Murugova, T. N., Chupin, V. V., Rogachev, A. V., Gruzinov, A. Yu., Svergun, D. I., Brennich, M. E., Gushchin, I. Yu., Soler-Lopez, M., Bothe, A., B\"uldt, G., Leonard, G., Engelhard, M., Kuklin, A. I. and Gordeliy, V. I. Molecular model of a sensor of two-component signaling system. In Scientific Reports, 11 (1): 10774, 2021. [doi..
  4. Volkova, M., Atamas, A., Tsarenko, A., Rogachev, A. and Guskov, A. Cation Transporters of Candida albicans—New Targets to Fight Candidiasis?. In Biomolecules, 11 (4): 584, 2021. [doi..
  5. Varaksa, T., Bukhdruker, S., Grabovec, I., Marin, E., Kavaleuski, A., Gusach, A., Kovalev, K., Maslov, I., Luginina, A., Zabelskii, D., Astashkin, R., Shevtsov, M., Smolskaya, S., Kavaleuskaya, A., Shabunya, P., Baranovsky, A., Dolgopalets, V., Charnou, Y., Savachka, A., Litvinovskaya, R., Hurski, A., Shevchenko, E., Rogachev, A., Mishin, A., Gordeliy, V., Gabrielian, A., Hurt, D. E., Nikonenko, B., Majorov, K., Apt, A., Rosenthal, A., Gilep, A., Borshchevskiy, V. and Strushkevich, N. Metabolic Fate of Human Immunoactive Sterols in Mycobacterium tuberculosis. In Journal of Molecular Biology, 433 (4), 2021. [doi..
  6. Zhang, H., Luginina, A., Mishin, A., Baidya, M., Shukla, A. K. and Cherezov, V. Structural insights into ligand recognition and activation of angiotensin receptors. In Trends in Pharmacological Sciences, 42 (7): 577-587, 2021. [doi..
  7. Arkhipova, V., Fu, H., Hoorens, M. W. H., Trinco, G., Lameijer, L. N., Marin, E., Feringa, B. L., Poelarends, G. J., Szymanski, W., Slotboom, D. J. and Guskov, A. Structural Aspects of Photopharmacology: Insight into the Binding of Photoswitchable and Photocaged Inhibitors to the Glutamate Transporter Homologue. In Journal of the American Chemical Society, 143 (3): 1513-1520, 2021. [doi..
  8. Mineev, K. S., Goncharuk, S. A., Goncharuk, M. V., Povarova, N. V., Sokolov, A. I., Baleeva, N. S., Smirnov, A. Yu., Myasnyanko, I. N., Ruchkin, D. A., Bukhdruker, S., Remeeva, A., Mishin, A., Borshchevskiy, V., Gordeliy, V., Arseniev, A. S., Gorbachev, D. A., Gavrikov, A. S., Mishin, A. S. and Baranov, M. S. NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids. In Chemical Science, 12 (19): 6719-6725, 2021. [doi..
  9. Trinco, G., Arkhipova, V., Garaeva, A. A., Hutter, C. A. J., Seeger, M. A., Guskov, A. and Slotboom, D. J. Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk. In Communications Biology, 4 (1): 751, 2021. [doi..

2020

  1. Lobysheva, N V, Nesterov, S V, Skorobogatova, Yu. A and Lobyshev, V I. The Functional Activity of Mitochondria in Deuterium Depleted Water. In Biophysics, 65 (2), 2020. [doi..
  2. Manukhov, I V, Zavilgelsky, G B and Gnuchikh, E.Y. Biosensors for the Determination of Promoters and Chaperones Activity in Bacillus subtilis Cells. In Biotekhnologiya, 36 (6), 2020. [doi..
  3. Shibaev, A. V, Ospennikov, A. S, Kuklin, A. I, Arkharova, N. A, Orekhov, A. S and Philippova, O. E. Structure, rheological and responsive properties of a new mixed viscoelastic surfactant system. In Colloids and Surfaces A: Physicochemical and Engineering Aspects, 586: 124284, 2020. [doi..
  4. Artykulnyi, O P, Shibaev, A V, Avdeev, M M, Ivankov, O I, Bulavin, L A, Petrenko, V I and Philippova, O E. Structural investigations of poly(ethylene glycol)-dodecylbenzenesulfonic acid complexes in aqueous solutions. In Journal of Molecular Liquids, 308, 2020. [doi..
  5. Remeeva, A., Nazarenko, V. V., Goncharov, I. M., Yudenko, A., Smolentseva, A., Semenov, O., Kovalev, K., G\"ulbahar, C., Schwaneberg, U., Davari, M. D., Gordeliy, V. and Gushchin, I. Effects of Proline Substitutions on the Thermostable LOV Domain from Chloroflexus aggregans. In Crystals, 10 (4), 2020. [doi..
  6. Sharaevskaya, A Y, Popov, P A and Osokin, S A. Численное моделирование распространения магнитостатических волн в связанных магнонных кристаллах меандрового типа. In Izvestiya VUZ. Applied Nonlinear Dynamics, 28 (4), 2020. [doi..
  7. Napolskiy, F., Avdeev, M., Yerdauletov, M., Ivankov, O., Bocharova, S., Ryzhenkova, S., Kaparova, B., Mironovich, K., Burlyaev, D. and Krivchenko, V. On the Use of Carbon Nanotubes in Prototyping the High Energy Density Li‐ion Batteries. In Energy Technology, 8 (6), 2020. [doi..
  8. Aliper, A. M., Bozdaganyan, M. E., Sarkisova, V. A., Veviorsky, A. P., Ozerov, I. V., Orekhov, P. S., Korzinkin, M. B., Moskalev, A., Zhavoronkov, A. and Osipov, A. N. Radioprotectors.org: an open database of known and predicted radioprotectors. In Aging, 12 (15), 2020. [doi..
  9. Kovalev, K, Volkov, D, Astashkin, R, Alekseev, A, Gushchin, I, Haro-Moreno, J M, Chizhov, I, Siletsky, S, Mamedov, M, Rogachev, A, Balandin, T, Borshchevskiy, V, Popov, A, Bourenkov, G, Bamberg, E, Rodriguez-Valera, F, B\"uldt, G and Gordeliy, V. High-resolution structural insights into the heliorhodopsin family. In Proceedings of the National Academy of Sciences, 117 (8): 4131-4141, 2020. [doi..
  10. Tomchuk, O. V, Ryukhtin, V., Ivankov, O., A., Ya. V., Aleksenskii, A. E, Bulavin, L. A, Aksenov, V. L and Avdeev, M. V. SANS analysis of aqueous dispersions of Eu- and Gd-grafted nanodiamond particles. In Fullerenes, Nanotubes and Carbon Nanostructures, 28 (4), 2020. [doi..
  11. KOVALENKO, M. G, KOLESNICHENKO, K. A and KUDRYAVTSEVA, A. A. Revealing the specific status of Mellicta distans Higgins, 1955, stat. n. (Lepidoptera, Nymphalidae) with morphological and molecular characters. In Zootaxa, 4853 (3), 2020. [doi..
  12. Safin, A R, Nikitov, S A, Kirilyuk, A I, Kalyabin, D V, Sadovnikov, A V, Stremoukhov, P A, Logunov, M V and Popov, P A. Excitation of Terahertz Magnons in Antiferromagnetic Nanostructures: Theory and Experiment. In Journal of Experimental and Theoretical Physics, 131 (1), 2020. [doi..
  13. Gushchin, I., Orekhov, P., Melnikov, I., Polovinkin, V., Yuzhakova, A. and Gordeliy, V. Sensor Histidine Kinase NarQ Activates via Helical Rotation, Diagonal Scissoring, and Eventually Piston-Like Shifts. In International Journal of Molecular Sciences, 21 (9), 2020. [doi..
  14. Bosak, A., Dideikin, A., Dubois, M., Ivankov, O., Lychagin, E., Muzychka, A., Nekhaev, G., Nesvizhevsky, V., Nezvanov, A., Schweins, R., Strelkov, A., Vul', A. and Zhernenkov, K. Fluorination of Diamond Nanoparticles in Slow Neutron Reflectors Does Not Destroy Their Crystalline Cores and Clustering While Decreasing Neutron Losses. In Materials, 13 (15), 2020. [doi..
  15. \vZelinská, K., Gallová, J., Huláková, S., Uhríková, D. and Ivankov, O. Solubilisation of model membrane by DDAO surfactant – partitioning, permeabilisation and liposome-micelle transition. In General physiology and biophysics, 39 (02), 2020. [doi..
  16. Lubova, K. I, Chugunov, A. O, Volynsky, P. E, Trofimov, Y. A, Korolkova, Y. V, Mosharova, I. V, Kozlov, S. A, Andreev, Y. A and Efremov, R. G. Probing temperature and capsaicin-induced activation of TRPV1 channel via computationally guided point mutations in its pore and TRP domains. In International Journal of Biological Macromolecules, 158, 2020. [doi..
  17. Zalygin, A., Solovyeva, D., Vaskan, I., Henry, S., Schaefer, M., Volynsky, P., Tuzikov, A., Korchagina, E., Ryzhov, I., Nizovtsev, A., Mochalov, K., Efremov, R., Shtykova, E., Oleinikov, V. and Bovin, N. Structure of Supramers Formed by the Amphiphile Biotin‐CMG‐DOPE. In ChemistryOpen, 9 (6), 2020. [doi..
  18. Britikov, V. V, Britikova, E. V, Urban, A. S, Lesovoy, D. M, Le, T. B. T., C., Van P., Usanov, S. A, Arseniev, A. S and Bocharov, E. V. Backbone and side-chain chemical shift assignments for the ribosome-inactivating protein trichobakin (TBK). In Biomolecular NMR Assignments, 14 (1), 2020. [doi..
  19. Vladoiu, R., Mandes, A., Dinca, V., Balasoiu, M., Soloviov, D. and Turchenko, V. Synthesis and Characterization of Complex Nanostructured Thin Films Based on Titanium for Industrial Applications. In Materials, 13 (2): 399, 2020. [doi..
  20. Zabelskii, D., Alekseev, A., Kovalev, K., Rankovic, V., Balandin, T., Soloviov, D., Bratanov, D., Savelyeva, E., Podolyak, E., Volkov, D., Vaganova, S., Astashkin, R., Chizhov, I., Yutin, N., Rulev, M., Popov, A., Eria-Oliveira, A., Rokitskaya, T., Mager, T., Antonenko, Y., Rosselli, R., Armeev, G., Shaitan, K., Vivaudou, M., B\"uldt, G., Rogachev, A., Rodriguez-Valera, F., Kirpichnikov, M., Moser, T., Offenh\"ausser, A., Willbold, D., Koonin, E., Bamberg, E. and Gordeliy, V. Viral rhodopsins 1 are an unique family of light-gated cation channels. In Nature Communications, 11 (1), 2020. [doi..
  21. Kholina, E G, Kovalenko, I B, Bozdaganyan, M E, Strakhovskaya, M G and Orekhov, P S. Cationic Antiseptics Facilitate Pore Formation in Model Bacterial Membranes. In The Journal of Physical Chemistry B, 124 (39), 2020. [doi..
  22. Lunin, A. V, Sokolov, I. L, Zelepukin, I. V, Zubarev, I. V, Yakovtseva, M. N, Mochalova, E. N, Rozenberg, J. M, Nikitin, M. P and Kolychev, E. L. Spindle-like MRI-active europium-doped iron oxide nanoparticles with shape-induced cytotoxicity from simple and facile ferrihydrite crystallization procedure. In RSC Advances, 10 (12), 2020. [doi..
  23. G\"oller, P. C., Haro-Moreno, J. M., Rodriguez-Valera, F., Loessner, M. J. and Gómez-Sanz, E. Uncovering a hidden diversity: optimized protocols for the extraction of dsDNA bacteriophages from soil. In Microbiome, 8 (1), 2020. [doi..
  24. Zemskaya, T. I., Cabello-Yeves, P. J., Pavlova, O. N. and Rodriguez-Valera, F. Microorganisms of Lake Baikal—the deepest and most ancient lake on Earth. In Applied Microbiology and Biotechnology, 104 (14), 2020. [doi..
  25. Sosorev, A., Dominskiy, D., Chernyshov, I. and Efremov, R. Tuning of Molecular Electrostatic Potential Enables Efficient Charge Transport in Crystalline Azaacenes: A Computational Study. In International Journal of Molecular Sciences, 21 (16), 2020. [doi..
  26. Haro‐Moreno, J. M, Rodriguez‐Valera, F., Rosselli, R., Martinez‐Hernandez, F., Roda‐Garcia, J. J, Gomez, M. L., Fornas, O., Martinez‐Garcia, M. and López‐Pérez, M. Ecogenomics of the SAR11 clade. In Environmental Microbiology, 22 (5), 2020. [doi..
  27. López-Pérez, M., Haro-Moreno, J. M, Coutinho, F. H., Martinez-Garcia, M. and Rodriguez-Valera, F. The Evolutionary Success of the Marine Bacterium SAR11 Analyzed through a Metagenomic Perspective. In mSystems, 5 (5), 2020. [doi..
  28. Marin, E., Luginina, A., Gusach, A., Kovalev, K., Bukhdruker, S., Khorn, P., Polovinkin, V., Lyapina, E., Rogachev, A., Gordeliy, V., Mishin, A., Cherezov, V. and Borshchevskiy, V. Small-wedge synchrotron and serial XFEL datasets for Cysteinyl leukotriene GPCRs. In Scientific Data, 7 (1): 388, 2020. [doi..
  29. Nesterov, S V, Yaguzhinsky, L S, Podoprigora, G I and Nartsissov, Ya. R. Amino Acids as Regulators of Cell Metabolism. In Biochemistry (Moscow), 85 (4), 2020. [doi..
  30. Dubovskii, P. V, Ignatova, A. A, Feofanov, A. V, Utkin, Y. N and Efremov, R. G. Antibacterial activity of cardiotoxin-like basic polypeptide from cobra venom. In Bioorganic & Medicinal Chemistry Letters, 30 (3), 2020. [doi..
  31. Bogorodskiy, A. O, Bolkhovitina, E. L, Gensch, T., Troyanova, N. I, Mishin, A. V, Okhrimenko, I. S, Braun, A., Spies, E., Gordeliy, V. I, Sapozhnikov, A. M, Borshchevskiy, V. I and Shevchenko, M. A. Murine Intraepithelial Dendritic Cells Interact With Phagocytic Cells During Aspergillus fumigatus-Induced Inflammation. In Frontiers in Immunology, 11 (February): 1-15, 2020. [doi..
  32. Albrecht, C., Appert-Collin, A., Bagnard, D., Blaise, S., Romier-Crouzet, B., Efremov, R. G, Sartelet, H., Duca, L., Maurice, P. and Bennasroune, A. Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?. In Frontiers in Oncology, 10, 2020. [doi..
  33. Kozlovskii, I. and Popov, P. Spatiotemporal identification of druggable binding sites using deep learning. In Communications Biology, 3 (1), 2020. [doi..
  34. Gigolaev, A. M, Kuzmenkov, A. I, Peigneur, S., Tabakmakher, V. M, Pinheiro-Junior, E. L, Chugunov, A. O, Efremov, R. G, Tytgat, J. and Vassilevski, A. A. Tuning Scorpion Toxin Selectivity: Switching From KV1.1 to KV1.3. In Frontiers in Pharmacology, 11, 2020. [doi..
  35. Kovalev, K., Astashkin, R., Gushchin, I., Orekhov, P., Volkov, D., Zinovev, E., Marin, E., Rulev, M., Alekseev, A., Royant, A., Carpentier, P., Vaganova, S., Zabelskii, D., Baeken, C., Sergeev, I., Balandin, T., Bourenkov, G., Carpena, X., Boer, R., Maliar, N., Borshchevskiy, V., B\"uldt, G., Bamberg, E. and Gordeliy, V. Molecular mechanism of light-driven sodium pumping. In Nature Communications, 11 (1), 2020. [doi..
  36. Kudryavtseva, A A, Okhrimenko, I S, Didina, V S, Zavilgelsky, G B and Manukhov, I V. Antirestriction Protein ArdB (R64) Interacts with DNA. In Biochemistry (Moscow), 85 (3), 2020. [doi..
  37. Karlov, D. S, Sosnin, S., Fedorov, M. V and Popov, P. graphDelta: MPNN Scoring Function for the Affinity Prediction of Protein–Ligand Complexes. In ACS Omega, 5 (10), 2020. [doi..
  38. Buslaev, P., Mustafin, K. and Gushchin, I. Principal component analysis highlights the influence of temperature, curvature and cholesterol on conformational dynamics of lipids. In Biochimica et Biophysica Acta (BBA) - Biomembranes, 1862 (7), 2020. [doi..
  39. Colbasevici, A., Voskoboynikova, N., Orekhov, P. S., Bozdaganyan, M. E., Karlova, M. G., Sokolova, O. S., Klare, J. P., Mulkidjanian, A. Y., Shaitan, K. V. and Steinhoff, H. Lipid dynamics in nanoparticles formed by maleic acid-containing copolymers: EPR spectroscopy and molecular dynamics simulations. In Biochimica et Biophysica Acta (BBA) - Biomembranes, 1862 (5), 2020. [doi..
  40. Murugova, T., Ivankov, O., Ermakova, E., Kondela, T., Hrubov\vcák, P., Skoi, V., Kuklin, A. and Ku\vcerka, N. Structural changes introduced by cholesterol and melatonin to the model membranes mimicking preclinical conformational diseases. In General physiology and biophysics, 39 (02), 2020. [doi..
  41. Bukhdruker, S., Varaksa, T., Grabovec, I., Marin, E., Shabunya, P., Kadukova, M., Grudinin, S., Kavaleuski, A., Gusach, A., Gilep, A., Borshchevskiy, V. and Strushkevich, N. Hydroxylation of Antitubercular Drug Candidate, SQ109, by Mycobacterial Cytochrome P450. In International Journal of Molecular Sciences, 21 (20): 7683, 2020. [doi..
  42. Tomchuk, A. A, Shershakova, N. N, Andreev, S. M, Turetskiy, E. A, Ivankov, O. I, Kyzyma, O. A, Tomchuk, O. V and Avdeev, M. V. C 60 and C 60 -arginine aqueous solutions: In vitro toxicity and structural study. In Fullerenes, Nanotubes and Carbon Nanostructures, 28 (4), 2020. [doi..
  43. Nabiyev, A A, Olejniczak, A, Pawlukojc, A, Balasoiu, M, Bunoiu, M, Maharramov, A M, Nuriyev, M A, Ismayilova, R S, Azhibekov, A K, Kabyshev, A M, Ivankov, O I, Vlase, T, Linnik, D S, Shukurova, A A, Ivanshina, O Yu, Turchenko, V A and Kuklin, A I. Nano-ZrO2 filled high-density polyethylene composites: Structure, thermal properties, and the influence $\gamma$-irradiation. In Polymer Degradation and Stability, 171, 2020. [doi..
  44. Rempel, S., Gati, C., Nijland, M., Thangaratnarajah, C., Karyolaimos, A., W., de G. J., Guskov, A. and Slotboom, D. J. A mycobacterial ABC transporter mediates the uptake of hydrophilic compounds. In Nature, 580 (7803), 2020. [doi..
  45. Stetsenko, A. and Guskov, A. Cation permeability in CorA family of proteins. In Scientific Reports, 10 (1), 2020. [doi..
  46. Bolmatov, D., Soloviov, D., Zhernenkov, M., Zav'yalov, D., Mamontov, E., Suvorov, A., Cai, Y. Q and Katsaras, J. Molecular Picture of the Transient Nature of Lipid Rafts. In Langmuir, 36 (18), 2020. [doi..
  47. Tomchuk, O V, Avdeev, M V, Dideikin, A T, Vul', A.Ya., Aleksenskii, A E, Kirilenko, D A, Ivankov, O I, Soloviov, D V, Kuklin, A I, Garamus, V M, Kulvelis, Yu.V., Aksenov, V L and Bulavin, L A. Revealing the structure of composite nanodiamond–graphene oxide aqueous dispersions by small-angle scattering. In Diamond and Related Materials, 103: 107670, 2020. [doi..
  48. Panina, I., Krylov, N., Nolde, D., Efremov, R. and Chugunov, A. Environmental and dynamic effects explain how nisin captures membrane-bound lipid II. In Scientific Reports, 10 (1), 2020. [doi..
  49. Tomchuk, O V, Bulavin, L A, Pipich, V, Ryukhtin, V, Ivankov, O I, Aksenov, V L and Avdeev, M V. Fractal aggregation in silica sols in basic tetraethoxysilane/ethanol/water solutions by small-angle neutron scattering. In Journal of Molecular Liquids, 304, 2020. [doi..
  50. Alleva, C, Kovalev, K, Astashkin, R, Berndt, M I, Baeken, C, Balandin, T, Gordeliy, V, Fahlke, Ch. and Machtens, J.-P. Na + -dependent gate dynamics and electrostatic attraction ensure substrate coupling in glutamate transporters. In Science Advances, 6 (47), 2020. [doi..
  51. Vlasov, A. V., Maliar, N. L., Bazhenov, S. V., Nikelshparg, E. I., Brazhe, N. A., Vlasova, A. D., Osipov, S. D., Sudarev, V. V., Ryzhykau, Y. L., Bogorodskiy, A. O., Zinovev, E. V., Rogachev, A. V., Manukhov, I. V., Borshchevskiy, V. I., Kuklin, A. I., Pokorný, J., Sosnovtseva, O., Maksimov, G. V. and Gordeliy, V. I. Raman Scattering: From Structural Biology to Medical Applications. In Crystals, 10 (1), 2020. [doi..
  52. Cabello‐Yeves, P. J, Zemskaya, T. I, Zakharenko, A. S, Sakirko, M. V, Ivanov, V. G, Ghai, R. and Rodriguez‐Valera, F. Microbiome of the deep Lake Baikal, a unique oxic bathypelagic habitat. In Limnology and Oceanography, 65 (7), 2020. [doi..
  53. Dubach, V. R.A. and Guskov, A. The Resolution in X-ray Crystallography and Single-Particle Cryogenic Electron Microscopy. In Crystals, 10 (7), 2020. [doi..
  54. Tugaeva, K. V, Remeeva, A., Gushchin, I., Cooley, R. B and Sluchanko, N. N. Design, expression, purification and crystallization of human 14-3-3$\zeta$ protein chimera with phosphopeptide from proapoptotic protein BAD. In Protein Expression and Purification, 175, 2020. [doi..
  55. \Ludzik, K., Woloszczuk, S., Zajçc, W., Jazdzewska, M., Rogachev, A., Kuklin, A. I., Zawisza, A. and Jóźwiak, M. Can the Isothermal Calorimetric Curve Shapes Suggest the Structural Changes in Micellar Aggregates?. In International Journal of Molecular Sciences, 21 (16), 2020. [doi..
  56. Bulavin, L A, Mikhailov, A E, Kuzmichev, P K, Chupin, V V, Borshchevskiy, V I, Chizhov, I V and Soloviov, D V. Influence of Cholesterol Concentration on Bacteriorhodopsin Photocycle. In Ukrainian Journal of Physics, 65 (9): 778, 2020. [doi..
  57. Gusach, A., Maslov, I., Luginina, A., Borshchevskiy, V., Mishin, A. and Cherezov, V. Beyond structure: emerging approaches to study GPCR dynamics. In Current Opinion in Structural Biology, 63: 18-25, 2020. [doi..
  58. Molchanov, V S, Efremova, M A, Orekhov, A S, Arkharova, N A, Rogachev, A V and Philippova, O E. Soft nanocomposites based on nanoclay particles and mixed wormlike micelles of surfactants. In Journal of Molecular Liquids, 314, 2020. [doi..
  59. Nagornyi, A V, Shlapa, Yu.Yu., Avdeev, M V, Solopan, S O, Belous, A G, Shulenina, A V, Ivankov, O I and Bulavin, L A. Structural characterization of aqueous magnetic fluids with nanomagnetite of different origin stabilized by sodium oleate. In Journal of Molecular Liquids, 312, 2020. [doi..
  60. Gonzalez-Serrano, R., Dunne, M., Rosselli, R., Martin-Cuadrado, A., Grosboillot, V., Zinsli, L. V., Roda-Garcia, J. J., Loessner, M. J. and Rodriguez-Valera, F. Alteromonas Myovirus V22 Represents a New Genus of Marine Bacteriophages Requiring a Tail Fiber Chaperone for Host Recognition. In mSystems, 5 (3), 2020. [doi..
  61. Kessenikh, A., Gnuchikh, E., Bazhenov, S., Bermeshev, M., Pevgov, V., Samoilov, V., Shorunov, S., Maksimov, A., Yaguzhinsky, L. and Manukhov, I. Genotoxic effect of 2,2'-bis(bicyclo[2.2.1] heptane) on bacterial cells. In PLOS ONE, 15 (8), 2020. [doi..
  62. Kadukova, M., Chupin, V. and Grudinin, S. Docking rigid macrocycles using Convex-PL, AutoDock Vina, and RDKit in the D3R Grand Challenge 4. In Journal of Computer-Aided Molecular Design, 34 (2), 2020. [doi..
  63. Kwiatkowski, A. L, Molchanov, V. S, Kuklin, A. I and Philippova, O. E. Opposite effect of salt on branched wormlike surfactant micelles with and without embedded polymer. In Journal of Molecular Liquids, 311, 2020. [doi..
  64. Maliar, N, Okhrimenko, I S, Petrovskaya, L E, Alekseev, A A, Kovalev, K V, Soloviov, D V, Popov, P A, Rokitskaya, T I, Antonenko, Y N, Zabelskii, D V, Dolgikh, D A, Kirpichnikov, M P and Gordeliy, V I. Novel pH-Sensitive Microbial Rhodopsin from Sphingomonas paucimobilis. In Doklady Biochemistry and Biophysics, 495 (1), 2020. [doi..
  65. Кудрявцева, А.А., Охрименко, И.С., Дидина, В.С., Завильгельский, Г.Б. and Манухов, И.В. Антирестрикционный белок ArdB (R64) взаимодействует с ДНК. In Биохимия, 85 (3), 2020. [doi..
  66. Gushchin, I., Melnikov, I., Polovinkin, V., Ishchenko, A. and Gordeliy, V. Crystal Structure of a Proteolytic Fragment of the Sensor Histidine Kinase NarQ. In Crystals, 10 (3), 2020. [doi..
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  68. Soloviov, D., Cai, Y. Q, Bolmatov, D., Suvorov, A., Zhernenkov, K., Zav'yalov, D., Bosak, A., Uchiyama, H. and Zhernenkov, M. Functional lipid pairs as building blocks of phase-separated membranes. In Proceedings of the National Academy of Sciences, 117 (9), 2020. [doi..
  69. Zaragoza-Solas, A., Rodriguez-Valera, F. and López-Pérez, M. Metagenome Mining Reveals Hidden Genomic Diversity of Pelagimyophages in Aquatic Environments. In mSystems, 5 (1), 2020. [doi..
  70. A., Di C., Dzhembekova, N., Cabello-Yeves, P. J, Eckert, E. M, Slabakova, V., Slabakova, N., Peneva, E., Bertoni, R., Corno, G., Salcher, M. M, Kamburska, L., Bertoni, F., Rodriguez-Valera, F., Moncheva, S. and Callieri, C. Genomic Comparison and Spatial Distribution of Different Synechococcus Phylotypes in the Black Sea. In Frontiers in Microbiology, 11, 2020. [doi..
  71. Kuznetsov, A. S, Zamaletdinov, M. F, Bershatsky, Y. V, Urban, A. S, Bocharova, O. V, Bennasroune, A., Maurice, P., Bocharov, E. V and Efremov, R. G. Dimeric states of transmembrane domains of insulin and IGF-1R receptors: Structures and possible role in activation. In Biochimica et Biophysica Acta (BBA) - Biomembranes, 1862 (11), 2020. [doi..
  72. Popov, P A, Safin, A R, Kirilyuk, A, Nikitov, S A, Lisenkov, I, Tyberkevich, V and Slavin, A. Voltage-Controlled Anisotropy and Current-Induced Magnetization Dynamics in Antiferromagnetic-Piezoelectric Layered Heterostructures. In Physical Review Applied, 13 (4), 2020. [doi..
  73. Agapova, Y. K., Altukhov, D. A., Timofeev, V. I., Stroylov, V. S., Mityanov, V. S., Korzhenevskiy, D. A., Vlaskina, A. V., Smirnova, E. V., Bocharov, E. V. and Rakitina, T. V. Structure-based inhibitors targeting the alpha-helical domain of the Spiroplasma melliferum histone-like HU protein. In Scientific Reports, 10 (1), 2020. [doi..
  74. Belozerova, O. A, Osmakov, D. I, Vladimirov, A., Koshelev, S. G, Chugunov, A. O, Andreev, Y. A, Palikov, V. A, Palikova, Y. A, Shaykhutdinova, E. R, Gvozd, A. N, Dyachenko, I. A, Efremov, R. G, Kublitski, V. S and Kozlov, S. A. Sevanol and Its Analogues: Chemical Synthesis, Biological Effects and Molecular Docking. In Pharmaceuticals, 13 (8), 2020. [doi..
  75. Ivankov, O. I, Ermakova, E. V, Murugova, T. N, Badreeva, D. R, Dushanov, E., Kondela, T., Kholmurodov, K., Kuklin, A. I and Ku\vcerka, N. Interactions in the model membranes mimicking preclinical conformational diseases. [doi..
  76. Arkhipova, V., Guskov, A. and Slotboom, D. J. Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment. In Nature Communications, 11 (1), 2020. [doi..
  77. Lysenko, S N, Lebedev, A V, Astaf'eva, S A, Yakusheva, D E, Balasoiu, M, Kuklin, A I, Kovalev, Yu S and Turchenko, V A. Preparation and magneto-optical behavior of ferrofluids with anisometric particles. In Physica Scripta, 95 (4), 2020. [doi..
  78. Chilom, C. G, Sandu, N., Bălăşoiu, M., Yaroslavtsev, R. N, Stolyar, S. V and Rogachev, A. V. Ferrihydrite nanoparticles insights: Structural characterization, lactate dehydrogenase binding and virtual screening assay. In International Journal of Biological Macromolecules, 164, 2020. [doi..
  79. Gnuchikh, E Yu., Manukhov, I V and Zavilgelsky, G B. DnaK Chaperone Takes Part in Folding but Not in Refolding of Thermal Inactivated Proteins in Bacillus subtilis. In Russian Journal of Genetics, 56 (9), 2020. [doi..
  80. Maliar, N., Kovalev, K., Baeken, C., Balandin, T., Astashkin, R., Rulev, M., Alekseev, A., Ilyinsky, N., Rogachev, A., Chupin, V., Dolgikh, D., Kirpichnikov, M. and Gordeliy, V. Crystal Structure of the N112A Mutant of the Light-Driven Sodium Pump KR2. In Crystals, 10 (6), 2020. [doi..
  81. Avetisyan, A., Balasanyants, S., Simonyan, R., Koroev, D., Kamynina, A., Zinovkin, R., Bobkova, N. and Volpina, O. Synthetic fragment (60–76) of RAGE improves brain mitochondria function in olfactory bulbectomized mice. In Neurochemistry International, 140, 2020. [doi..
  82. Konovalov, O. V, Novikova, N. N, Kovalchuk, M. V, Yalovega, G. E, Topunov, A. F, Kosmachevskaya, O. V, Yurieva, E. A, Rogachev, A. V, Trigub, A. L, Kremennaya, M. A, Borshchevskiy, V. I, Vakhrameev, D. D and Yakunin, S. N. XANES Measurements for Studies of Adsorbed Protein Layers at Liquid Interfaces. In Materials, 13 (20): 4635, 2020. [doi..
  83. Kuklin, A., Zabelskii, D., Gordeliy, I., Teixeira, J., Br\^ulet, A., Chupin, V., Cherezov, V. and Gordeliy, V. On the Origin of the Anomalous Behavior of Lipid Membrane Properties in the Vicinity of the Chain-Melting Phase Transition. In Scientific Reports, 10 (1), 2020. [doi..
  84. Siposova, K., Petrenko, V. I, Ivankov, O. I, Musatov, A., Bulavin, L. A, Avdeev, M. V and Kyzyma, O. A. Fullerenes as an Effective Amyloid Fibrils Disaggregating Nanomaterial. In ACS Applied Materials & Interfaces, 12 (29), 2020. [doi..
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  86. Pakhomov, A. A, Frolova, A. Yu., Tabakmakher, V. M, Chugunov, A. O, Efremov, R. G and Martynov, V. I. Impact of external amino acids on fluorescent protein chromophore biosynthesis revealed by molecular dynamics and mutagenesis studies. In Journal of Photochemistry and Photobiology B: Biology, 206, 2020. [doi..
  87. Aleksenko, V. A, Anand, D., Remeeva, A., Nazarenko, V. V, Gordeliy, V., Jaeger, K., Krauss, U. and Gushchin, I. Phylogeny and Structure of Fatty Acid Photodecarboxylases and Glucose-Methanol-Choline Oxidoreductases. In Catalysts, 10 (9): 1072, 2020. [doi..

2019

  1. Novitskaia, O., Buslaev, P. and Gushchin, I. Assembly of Spinach Chloroplast ATP Synthase Rotor Ring Protein-Lipid Complex. In Frontiers in Molecular Biosciences, 6, 2019. [doi..
  2. Audet, M., White, K. L., Breton, B., Zarzycka, B., Han, G. W., Lu, Y., Gati, C., Batyuk, A., Popov, P., Velasquez, J., Manahan, D., Hu, H., Weierstall, U., Liu, W., Shui, W., Katritch, V., Cherezov, V., Hanson, M. A. and Stevens, R. C. Crystal structure of misoprostol bound to the labor inducer prostaglandin E2 receptor. In Nature Chemical Biology, 15 (1), 2019. [doi..
  3. Popov, P., Bizin, I., Gromiha, M., A, K. and Frishman, D. Prediction of disease-associated mutations in the transmembrane regions of proteins with known 3D structure. In PLOS ONE, 14 (7), 2019. [doi..
  4. Pospelov, N., Nechaev, S., Anokhin, K., Valba, O., Avetisov, V. and Gorsky, A. Spectral peculiarity and criticality of a human connectome. In Physics of Life Reviews, 31: 240-256, 2019. [doi..
  5. Haro-Moreno, J. M., Rodriguez-Valera, F. and López-Pérez, M. Prokaryotic Population Dynamics and Viral Predation in a Marine Succession Experiment Using Metagenomics. In Frontiers in Microbiology, 10, 2019. [doi..
  6. Orekhov, P.S., Kirillov, I.V., Fedorov, V.A., Kovalenko, I.B., Gudimchuk, N.B. and Zhmurov, A.A. Parametrization of the Elastic Network Model Using High-Throughput Parallel Molecular Dynamics Simulations. In Supercomputing Frontiers and Innovations, 6 (1), 2019. [doi..
  7. Popov, P., Kozlovskii, I. and Katritch, V. Computational design for thermostabilization of GPCRs. In Current Opinion in Structural Biology, 55, 2019. [doi..
  8. Feldman, T. B., Ivankov, O. I., Kuklin, A. I., Murugova, T. N., Yakovleva, M. A., Smitienko, O. A., Kolchugina, I. B., Round, A., Gordeliy, V. I., Belushkin, A. V. and Ostrovsky, M. A. Small-angle neutron and X-ray scattering analysis of the supramolecular organization of rhodopsin in photoreceptor membrane. In Biochimica et Biophysica Acta (BBA) - Biomembranes, 1861 (10), 2019. [doi..
  9. Shtykova, E. V., Petoukhov, M. V., Mozhaev, A. A., Deyev, I. E., Dadinova, L. A., Loshkarev, N. A., Goryashchenko, A. S., Bocharov, E. V., Jeffries, Cy M., Svergun, D. I., Batishchev, O. V. and Petrenko, A. G. The dimeric ectodomain of the alkali-sensing insulin receptor–related receptor (ectoIRR) has a droplike shape. In Journal of Biological Chemistry, 294 (47): 17790-17798, 2019. [doi..
  10. Mishin, A., Gusach, A., Luginina, A., Marin, E., Borshchevskiy, V. and Cherezov, V. An outlook on using serial femtosecond crystallography in drug discovery. In Expert Opinion on Drug Discovery, 14 (9), 2019. [doi..
  11. Bocharov, E. V., Nadezhdin, K. D., Urban, A. S., Volynsky, P. E., Pavlov, K. V., Efremov, R. G., Arseniev, A. S. and Bocharova, O. V. Familial L723P Mutation Can Shift the Distribution between the Alternative APP Transmembrane Domain Cleavage Cascades by Local Unfolding of the Ε-Cleavage Site Suggesting a Straightforward Mechanism of Alzheimer's Disease Pathogenesis. In ACS Chemical Biology, 14 (7): 1573-1582, 2019. [doi..
  12. Orekhov, P. S., Bozdaganyan, M. E., Voskoboynikova, N., Mulkidjanian, A. Y., Steinhoff, H. and Shaitan, K. V. Styrene/Maleic Acid Copolymers Form SMALPs by Pulling Lipid Patches out of the Lipid Bilayer. In Langmuir, 35 (10): 3748-3758, 2019. [doi..
  13. Popov, P., Grudinin, S., Kurdiuk, A., Buslaev, P. and Redon, S. Controlled‐advancement rigid‐body optimization of nanosystems. In Journal of Computational Chemistry, 40 (27): 2391-2399, 2019. [doi..
  14. Fedorov, V. A., Orekhov, P. S., Kholina, E. G., Zhmurov, A. A., Ataullakhanov, F. I., Kovalenko, I. B. and Gudimchuk, N. B. Mechanical properties of tubulin intra- and inter-dimer interfaces and their implications for microtubule dynamic instability. In PLOS Computational Biology, 15 (8): e1007327, 2019. [doi..
  15. Aliper, A. M., Bozdaganyan, M. E., Orekhov, P. S., Zhavoronkov, A. and Osipov, A. N. Replicative and radiation-induced aging: a comparison of gene expression profiles. In Aging, 11 (8): 2378-2387, 2019. [doi..
  16. Bratanov, D., Kovalev, K., Machtens, J., Astashkin, R., Chizhov, I., Soloviov, D., Volkov, D., Polovinkin, V., Zabelskii, D., Mager, T., Gushchin, I., Rokitskaya, T., Antonenko, Y., Alekseev, A., Shevchenko, V., Yutin, N., Rosselli, R., Baeken, C., Borshchevskiy, V., Bourenkov, G., Popov, A., Balandin, T., B\"uldt, G., Manstein, D. J., Rodriguez-Valera, F., Fahlke, C., Bamberg, E., Koonin, E. and Gordeliy, V. Unique structure and function of viral rhodopsins. In Nature Communications, 10 (1): 4939, 2019. [doi..
  17. Kovalev, K., Polovinkin, V., Gushchin, I., Alekseev, A., Shevchenko, V., Borshchevskiy, V., Astashkin, R., Balandin, T., Bratanov, D., Vaganova, S., Popov, A., Chupin, V., B\"uldt, G., Bamberg, E. and Gordeliy, V. Structure and mechanisms of sodium-pumping KR2 rhodopsin. In Science Advances, 5 (4), 2019. [doi..
  18. Cabello-Yeves, P. J. and Rodriguez-Valera, F. Marine-freshwater prokaryotic transitions require extensive changes in the predicted proteome. In Microbiome, 7 (1): 117, 2019. [doi..
  19. Luginina, A., Gusach, A., Marin, E., Mishin, A., Brouillette, R., Popov, P., Shiriaeva, A., Besserer-Offroy, \., Longpré, J., Lyapina, E., Ishchenko, A., Patel, N., Polovinkin, V., Safronova, N., Bogorodskiy, A., Edelweiss, E., Hu, H., Weierstall, U., Liu, W., Batyuk, A., Gordeliy, V., Han, G. W., Sarret, P., Katritch, V., Borshchevskiy, V. and Cherezov, V. Structure-based mechanism of cysteinyl leukotriene receptor inhibition by antiasthmatic drugs. In Science Advances, 5 (10), 2019. [doi..
  20. Coutinho, F. H., Rosselli, R. and Rodríguez-Valera, F. Trends of Microdiversity Reveal Depth-Dependent Evolutionary Strategies of Viruses in the Mediterranean. In mSystems, 4 (6), 2019. [doi..
  21. Popov, P.A., Sharaevskaya, A.Yu., Beginin, E.N., Sadovnikov, A.V., Stognij, A.I., Kalyabin, D.V. and Nikitov, S.A. Spin wave propagation in three-dimensional magnonic crystals and coupled structures. In Journal of Magnetism and Magnetic Materials, 476, 2019. [doi..
  22. Lensink, M. F., Brysbaert, G., Nadzirin, N., Velankar, S., Chaleil, R. A. G., Gerguri, T., Bates, P. A., Laine, E., Carbone, A., Grudinin, S., Kong, R., Liu, R., Xu, X., Shi, H., Chang, S., Eisenstein, M., Karczynska, A., Czaplewski, C., Lubecka, E., Lipska, A., Krupa, P., Mozolewska, M., Golon, \., Samsonov, S., Liwo, A., Crivelli, S., Pagès, G., Karasikov, M., Kadukova, M., Yan, Y., Huang, S., Rosell, M., Rodríguez‐Lumbreras, L. A., Romero‐Durana, M., Díaz‐Bueno, L., Fernandez‐Recio, J., Christoffer, C., Terashi, G., Shin, W., Aderinwale, T., R., Maddhuri V. S. S., Kihara, D., Kozakov, D., Vajda, S., Porter, K., Padhorny, D., Desta, I., Beglov, D., Ignatov, M., Kotelnikov, S., Moal, I. H., Ritchie, D. W., I., Chauvot de B., Maigret, B., Devignes, M., E., Ruiz E. M., Barradas‐Bautista, D., Cao, Z., Cavallo, L., Oliva, R., Cao, Y., Shen, Y., Baek, M., Park, T., Woo, H., Seok, C., Braitbard, M., Bitton, L., Scheidman‐Duhovny, D., Dapkūnas, J., Olechnovi\vc, K., Venclovas, \., Kundrotas, P. J., Belkin, S., Chakravarty, D., Badal, V. D., Vakser, I. A., Vreven, T., Vangaveti, S., Borrman, T., Weng, Z., Guest, J. D., Gowthaman, R., Pierce, B. G., Xu, X., Duan, R., Qiu, L., Hou, J., B., Ryan M., Ma, Z., Cheng, J., Zou, X., Koukos, P. I., Roel‐Touris, J., Ambrosetti, F., Geng, C., Schaarschmidt, J., Trellet, M. E., Melquiond, A. S. J., Xue, Li, Jiménez‐García, B., Noort, C. W., Honorato, R. V., Bonvin, A. M. J. J. and Wodak, S. J. Blind prediction of homo‐ and hetero‐protein complexes: The CASP13‐CAPRI experiment. In Proteins: Structure, Function, and Bioinformatics, 87 (12): 1200-1221, 2019. [doi..
  23. Nazarenko, V. V., Remeeva, A., Yudenko, A., Kovalev, K., Dubenko, A., Goncharov, I. M., Kuzmichev, P., Rogachev, A. V., Buslaev, P., Borshchevskiy, V., Mishin, A., Dhoke, G. V., Schwaneberg, U., Davari, M. D., Jaeger, K., Krauss, U., Gordeliy, V. and Gushchin, I. A thermostable flavin-based fluorescent protein from Chloroflexus aggregans : a framework for ultra-high resolution structural studies. In Photochemical & Photobiological Sciences, 18 (7): 1793-1805, 2019. [doi..
  24. Cirtoaje, C., Petrescu, E., Stan, C. and Rogachev, A. Electric Freedericksz transition in nematic liquid crystals with graphene quantum dot mixture. In Applied Surface Science, 487: 1301-1306, 2019. [doi..
  25. Anghel, L., Rogachev, A., Kuklin, A. and Erhan, R. V. $\beta$-Lactoglobulin associative interactions: a small-angle scattering study. In European Biophysics Journal, 48 (3), 2019. [doi..
  26. Polyansky, A. A., Bocharov, E. V., Velghe, A. I., Kuznetsov, A. S., Bocharova, O. V., Urban, A. S., Arseniev, A. S., Zagrovic, B., Demoulin, J. and Efremov, R. G. Atomistic mechanism of the constitutive activation of PDGFRA via its transmembrane domain. In Biochimica et Biophysica Acta (BBA) - General Subjects, 1863 (1): 82-95, 2019. [doi..
  27. Shibaev, A. V., Kuklin, A. I. and Philippova, O. E. Different responsiveness to hydrocarbons of linear and branched anionic/cationic-mixed wormlike surfactant micelles. In Colloid and Polymer Science, 297 (3), 2019. [doi..
  28. Li, X., Hua, T., Vemuri, K., Ho, J., Wu, Y., Wu, L., Popov, P., Benchama, O., Zvonok, N., Locke, K., Qu, Lu, Han, G. W., Iyer, M. R., Cinar, R., Coffey, N. J., Wang, J., Wu, M., Katritch, V., Zhao, S., Kunos, G., Bohn, L. M., Makriyannis, A., Stevens, R. C. and Liu, Z. Crystal Structure of the Human Cannabinoid Receptor CB2. In Cell, 176 (3), 2019. [doi..
  29. Gusach, A., Luginina, A., Marin, E., Brouillette, R. L., Besserer-Offroy, \., Longpré, J., Ishchenko, A., Popov, P., Patel, N., Fujimoto, T., Maruyama, T., Stauch, B., Ergasheva, M., Romanovskaia, D., Stepko, A., Kovalev, K., Shevtsov, M., Gordeliy, V., Han, G. W., Katritch, V., Borshchevskiy, V., Sarret, P., Mishin, A. and Cherezov, V. Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors. In Nature Communications, 10 (1), 2019. [doi..
  30. Ignatov, M., Liu, C., Alekseenko, A., Sun, Z., Padhorny, D., Kotelnikov, S., Kazennov, A., Grebenkin, I., Kholodov, Y., Kolosvari, I., Perez, A., Dill, K. and Kozakov, D. Monte Carlo on the manifold and MD refinement for binding pose prediction of protein–ligand complexes: 2017 D3R Grand Challenge. In Journal of Computer-Aided Molecular Design, 33 (1), 2019. [doi..
  31. Kuter, K. Z., Olech, \. and Dencher, N. A. Increased energetic demand supported by mitochondrial electron transfer chain and astrocyte assistance is essential to maintain the compensatory ability of the dopaminergic neurons in an animal model of early Parkinson's disease. In Mitochondrion, 47: 227-237, 2019. [doi..
  32. Dadayan, A. K., Borisov, Yu. A., Bocharov, E. V., Zolotarev, Yu. A., Nagaev, I. Yu. and Myasoedov, N. F. Solid-State Catalytic Isotope Exchange of Hydrogen for Deuterium in Cyclopropylglycine. In Doklady Physical Chemistry, 484 (1): 15-19, 2019. [doi..
  33. Vlasov, A. V., Kovalev, K. V., Marx, S.-H., Round, E. S., Gushchin, I. Yu., Polovinkin, V. A., Tsoy, N. M., Okhrimenko, I. S., Borshchevskiy, V. I., B\"uldt, G. D., Ryzhykau, Yu. L., Rogachev, A. V., Chupin, V. V., Kuklin, A. I., Dencher, N. A. and Gordeliy, V. I. Unusual features of the c-ring of F1FO ATP synthases. In Scientific Reports, 9 (1): 18547, 2019. [doi..
  34. Lesovoy, D. M., Dubinnyi, M. A., Nolde, S. B., Bocharov, E. V. and Arseniev, A. S. Accurate measurement of dipole/dipole transverse cross-correlated relaxation $$\varGamma _2$$ in methylenes and primary amines of uniformly $$^13\text C/^15\text N$$-labeled proteins. In Journal of Biomolecular NMR, 73 (5): 245-260, 2019. [doi..

2018

  1. Okhrimenko, I S, Popov, P A, Malyar, N L, Chupin, V V, Petrovskaya, L E, Dolgikh, D A, Novoseletsky, V N, Kudriavtsev, A V, Shaitan, K V, Gordeliy, V I and Kirpichnikov, M P. Functional studies and spatial structure of new retinal-binding proteins. In Journal of Bioenergetics and Biomembranes, 50 (6): 568, 2018.
  2. Goryanin, I I, Kudryavtseva, A A, Balabanov, V P, Biryukova, V S, Manukhov, I V and Zavilgelsky, G B. Antirestriction activities of KlcA (RP4) and ArdB (R64) proteins. In Fems Microbiology Letters, 365 (23): 6, 2018. [doi..
  3. Belikov, N E, Melnikova, I A, Demina, O V, Kryukova, E A, Petrovskaya, L E, Kuzmichev, P K, Chupin, V V, Lukin, A Y, Soloviov, D V, Chizhov, I, Shumsky, A N, Levin, P P, Varfolomeev, S D and Khodonov, A A. The effect of chromophoric groupmodifications on the spectral properties of proteorhodopsin from E. sibiricum (ESRh). In Journal of Bioenergetics and Biomembranes, 50 (6): 526, 2018.
  4. Salnikov, E, Drung, B, Fabre, G, Itkin, A, Otyepka, M, Dencher, N A, Schmidt, B, Hauss, T, Trouillas, P and Bechinger, B. Lipid bilayer position and orientation of novel carprofens, modulators of gamma-secretase in Alzheimer's disease. In Biochimica Et Biophysica Acta-Biomembranes, 1860 (11): 2224-2233, 2018. [doi..
  5. Ishchenko, A, Gati, C and Cherezov, V. Structural biology of G protein-coupled receptors: new opportunities from XFELs and cryoEM. In Current Opinion in Structural Biology, 51: 44-52, 2018. [doi..
  6. Gushchin, I and Gordeliy, V. Transmembrane Signal Transduction in Two-Component Systems: Piston, Scissoring, or Helical Rotation?. In Bioessays, 40 (2): 10, 2018. [doi..
  7. Maslov, I V, Ilyinsky, N S, Khorn, P A, Vistunov, V K, Safronova, N A, Kuzmichev, P K, Maksutov, A M, Bogorodskiy, A O, Gensch, T, Mishin, A V, Cherezov, V and Borshchevskiy, V I. Exploration of a conformational landscape for a membrane protein via single-molecule fluorescence microscopy. In Journal of Bioenergetics and Biomembranes, 50 (6): 513, 2018.
  8. Cherezov, V. A decade of GPCR structural biology. In Journal of Bioenergetics and Biomembranes, 50 (6): 508-509, 2018.
  9. Che, T, Majumdar, S, Zaidi, S A, Ondachi, P, McCorvy, J D, Wang, S, Mosier, P D, Uprety, R, Vardy, E, Krumm, B E, Han, G W, Lee, M Y, Pardon, E, Steyaert, J, Huang, X P, Strachan, R T, Tribo, A R, Pasternak, G W, Carroll, F I, Stevens, R C, Cherezov, V, Katritch, V, Wacker, D and Roth, B L. Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor. In Cell, 172 (1-2): 55-+, 2018. [doi..
  10. Cherezov, A, Sanchez, R and Joo, H G. A reduced-basis element method for pin-by-pin reactor core calculations in diffusion and SP3 approximations. In Annals of Nuclear Energy, 116: 195-209, 2018. [doi..
  11. Shumming, H and Cherezov, V. Structural basis of Human GPR55 for diabetes and obesity therapies. In Journal of Bioenergetics and Biomembranes, 50 (6): 584, 2018.
  12. Dzinic, T and Dencher, N A. Oxygen Concentration and Oxidative Stress Modulate the Influence of Alzheimer's Disease A beta(1-42) Peptide on Human Cells. In Oxidative Medicine and Cellular Longevity: 16, 2018. [doi..
  13. Kuklin, A I, Rogachev, A V, Soloviov, D V, Ivankov, O I, Murugova, T N, Chupin, V V, Rulev, M I, Skoi, V V, Kucerka, N, Vlasov, A V and Gordeliy, V I. SANS investigations of biological objects on a YuMO spectrometer: results and possibilities. In Journal of Bioenergetics and Biomembranes, 50 (6): 555, 2018.
  14. Balagurunathan, Y, Beers, A, Kalpathy-Cramer, J, McNitt-Gray, M, Hadjiiski, L, Zhao, B S, Zhu, J G, Yang, H, Yip, S S F, Aerts, H., Napel, S, Cherezov, D, Cha, K, Chan, H P, Flores, C, Garcia, A, Gillies, R and Goldgof, D. Semi-automated pulmonary nodule interval segmentation using the NLST data (vol 45, pg 1093, 2018). In Medical Physics, 45 (6): 2689-2690, 2018. [doi..
  15. Skoi, V V, Rulev, M I, Kazantsev, A S, Pavlova, A A, Chupin, V V, Soloviov, D V, Gordeliy, V I and Kuklin, A I. SAXS and densimetry studies of DMPC/POPE mixture: morphology or structure changes?. In Journal of Bioenergetics and Biomembranes, 50 (6): 584, 2018.
  16. Shevchenko, M A, Bogorodskiy, A O, Troyanova, N I, Servuli, E A, Bolkhovitina, E L, Buldt, G, Fahlke, C, Gordeliy, V I, Gensch, T, Borshchevskiy, V I and Sapozhnikov, A M. Aspergillus fumigatus Infection-Induced Neutrophil Recruitment and Location in the Conducting Airway of Immunocompetent, Neutropenic, and Immunosuppressed Mice. In Journal of Immunology Research: 12, 2018. [doi..
  17. Gusach, A, Luginina, A, Lyapina, E, Shevtsov, M, Safronova, N, Khorn, P, Borshchevskiy, V, Mishin, A and Cherezov, V. Optimization of G protein-coupled receptor expression for functional studies. In Journal of Bioenergetics and Biomembranes, 50 (6): 512, 2018.
  18. Belikov, N. E, Melnikova, I. A, Demina, O. V, Petrovskaya, L. E, Kryukova, E. A, Dolgikh, D. A, Kuzmichev, P. K, Chupin, V. V, Lukin, A. Yu., Shumsky, A. N, Chizhov, I., Levin, P. P, Kirpichnikov, M. P, Varfolomeev, S. D and Khodonov, A. A. The effect of the chromophoric group modification on the optical properties of retinal proteins. In Mendeleev Communications, 28 (4): 406-408, 2018. [doi..
  19. Mikhailov, A E, Kuzmichev, P K, Senko, D A, Andreev, S M and Chupin, V V. Design and synthesis of new amphiphilic polymers for specific interaction with streptavidin and solubilization of membrane proteins. In Journal of Bioenergetics and Biomembranes, 50 (6): 563, 2018.
  20. Kadukova, M, Chupin, V and Grudinin, S. Knowledge-based prediction of protein-ligand binding affinities. In Journal of Bioenergetics and Biomembranes, 50 (6): 546-547, 2018.
  21. Handel, T, Gustaysson, M, Zheng, Y, Stephens, B, Baker, G, Ngo, T, Holden, L, Stevens, R, Cherezov, V, Abagyan, R and Kufareva, I. Structure and Signaling Mechanisms of G Protein-Coupled and b-Arrestin-Biased Chemokine Receptors. In Faseb Journal, 32 (1): 2, 2018.
  22. Cherezov, D, Hawkhis, S H, Goldga, D B, Hall, L O, Liu, Y, Li, Q, Balagurtmathan, Y, Gillies, R J and Schabath, M B. Delta radiomic features improve prediction for lung cancer incidence: A nested case-control analysis of the National Lung Screening Trial. In Cancer Medicine, 7 (12): 6340-6356, 2018. [doi..
  23. Podolyak, E Y, Okhrimenko, I S, Maslov, I V, Bogorodskiy, A O, Burkatovskiy, D S, Borshchevskiy, V I and Dencher, N A. Time-dependent intracellular localization of externally applied Alzheimer's disease A beta(1-42) peptide. In Journal of Bioenergetics and Biomembranes, 50 (6): 571-572, 2018.
  24. Valkov, M S, Shevtsov, M B, Mishin, A V and Cherezov, V. LCP crystallization of A(2A) adenosine receptor bound to amilorides. In Journal of Bioenergetics and Biomembranes, 50 (6): 594, 2018.
  25. Zabelskii, D V, Vlasov, A V, Ryzhykau, Y L, Murugova, T N, Brennich, M, Soloviov, D V, Ivankov, O I, Borshchevskiy, V I, Mishin, A V, Rogachev, A V, Round, A, Dencher, N A, Buldt, G, Gordeliy, V I and Kuklin, A I. Ambiguities and completeness of SAS data analysis: investigations of apoferritin by SAXS/SANS EID and SEC-SAXS methods. [doi..
  26. Dencher, N A, Bogorodskiy, A O, Borshchevskiy, V I, Gordeliy, V I, Malyar, N L, Maslov, I V, Okhrimenko, I S, Podolyak, E Y, Dani, D, Decker, V, Dzinic, T, Frenzel, M, Kratochwil, M, Meckel, T, Schafer, E, Guevara, C R, Poetsch, A, Kuter, K, Hauss, T and Sugawa, M D. Challenge the "free radical theory of ageing" and the "A beta peptide extracellular plaque hypothesis of Alzheimer's disease". In Journal of Bioenergetics and Biomembranes, 50 (6): 491, 2018.
  27. Luginina, A A, Gusach, A Y, Mishin, A V, Marin, E V, Popov, P A, Lyapina, E A, Katritch, V Y, Borshchevskiy, V I and Cherezov, V. Effects of mono- and divalent cations on GPCR stability. In Journal of Bioenergetics and Biomembranes, 50 (6): 511-512, 2018.
  28. Maslov, I V, Burkatovskiy, D S, Zykov, I O, Bogorodskiy, A O, Altschmied, J, Gensch, T, Haendeler, J, Buldt, G and Borshchevskiy, V. Mitochondrial network dynamics examined with photoconvertible Dendra2-protein. In Journal of Bioenergetics and Biomembranes, 50 (6): 532, 2018.
  29. Alahmari, S S, Cherezov, D, Goldgof, D B, Hall, L O, Gillies, R J and Schabath, M B. Delta Radiomics Improves Pulmonary Nodule Malignancy Prediction in Lung Cancer Screening. In Ieee Access, 6: 77796-77806, 2018. [doi..
  30. Stauch, B and Cherezov, V. Serial Femtosecond Crystallography of G Protein-Coupled Receptors. [doi..
  31. Velikanova, A V, Kuzmichev, P K, Soloviov, D V, Petrovskaya, L E, Dolgikh, D A, Shaitan, K V, Kirpichnikov, M P and Chupin, V V. Bacteriorhodopsin from Exiguobacterium sibiricum/amphipathic polymers complexes: functional studies. In Journal of Bioenergetics and Biomembranes, 50 (6): 594-595, 2018.
  32. Broecker, J, Morizumi, T, Ou, W L, Klingel, V, Kuo, A L, Kissick, D J, Ishchenko, A, Lee, M Y, Xu, S L, Makarov, O, Cherezov, V, Ogata, C M and Ernst, O P. High-throughput in situ X-ray screening of and data collection from protein crystals at room temperature and under cryogenic conditions. In Nature Protocols, 13 (2): 260-291, 2018. [doi..
  33. Malyar, N L, Okhrimenko, I S, Petrovskaya, L E, Popov, P A, Soloviov, D V, Alekseev, A A, Kovalev, K V, Zabelskii, D V, Chizhov, I V, Borshchevskiy, V I, Rokitskaya, T I, Antonenko, Y N, Dolgikh, D A, Kirpichnikov, M P, Gordeliy, V I and Bueldt, G. Novel light-driven proton pump: functional and structural study. In Journal of Bioenergetics and Biomembranes, 50 (6): 562, 2018.
  34. Bogorodskiy, A O, Bolkhovitina, E L, Borshchevskiy, V I, Sapozhnikov, A M and Shevchenko, M A. Simultaneous imaging of structurally different objects: pathogens, phagocytic cells lymphatic and blood vessels in whole-mount airway samples using advanced fluorescent microscopy. In Journal of Bioenergetics and Biomembranes, 50 (6): 582, 2018.
  35. Kovalev, K, Polovinkin, V, Gushchin, I, Alekseev, A, Shevchenko, V, Borshchevskiy, V and Gordeliy, V. Structural and functional features of the light-driven sodium pump KR2. In Journal of Bioenergetics and Biomembranes, 50 (6): 512-513, 2018.
  36. Ferre, G, Saurel, O, Czaplicki, G, Demange, P, Marie, J, Fehrentz, J A, Baneres, J L, Stevens, R C, Cherezov, V and Milon, A. Structure and dynamics of receptor-bound neuropeptides. In Journal of Bioenergetics and Biomembranes, 50 (6): 489-490, 2018.
  37. Kurbatov, N M, Drobyshev, A L, Vlasov, A V, Okhrimenko, I S, Kuklin, A I, Dencher, N A and Gordeliy, V I. DDM solubilization-based protocol for isolation and purification of spinach chloroplast ATP synthase. In Journal of Bioenergetics and Biomembranes, 50 (6): 555, 2018.
  38. Bogorodskiy, A O, Gensch, T, Malyar, N L, Okhrimenko, I S, Buldt, G and Borshchevskiy, V I. Protein expression with intact N-terminal sequence. In Journal of Bioenergetics and Biomembranes, 50 (6): 530, 2018.
  39. Maslov, I, Bogorodskiy, A, Mishin, A, Okhrimenko, I, Gushchin, I, Kalenov, S, Dencher, N A, Fahlke, C, Buldt, G, Gordeliy, V, Gensch, T and Borshchevskiy, V. Efficient non-cytotoxic fluorescent staining of halophiles. In Scientific Reports, 8: 12, 2018. [doi..
  40. Popov, P, Peng, Y, Shen, L, Stevens, R C, Cherezov, V, Liu, Z J and Katritch, V. Computational design of thermostabilizing point mutations for G protein-coupled receptors. In Elife, 7: 22, 2018. [doi..
  41. Kouzmitchev, P K and Chupin, V V. Lipidic nanocarriers for drug delivery. In Journal of Bioenergetics and Biomembranes, 50 (6): 508, 2018.
  42. Rulev, M I, Pavlova, A A, Ivankov, O I, Soloviov, D V, Rogachev, A V, Skoi, V V, Chupin, V V, Gordeliy, V I and Kuklin, A I. SAS investigations of size changes in lipid vesicles near temperature point of phase transition. In Journal of Bioenergetics and Biomembranes, 50 (6): 569, 2018.
  43. Kuklin, A I, Vlasov, A V, Ryzhykau, Y L, Dencher, N A, Hauss, T, Tugan-Baranovskaya, A D, Teixeira, J, Yaguzhinskiy, L S, Buldt, G and Gordeliy, V I. Guanidine hydrochloride fixed bacteriorhodopsin in the intermediate state of its photocycle. In Journal of Bioenergetics and Biomembranes, 50 (6): 595, 2018.
  44. Stauch, B and Cherezov, V. Serial Femtosecond Crystallography of G Protein-Coupled Receptors. [doi..
  45. Cherezov, I, Cardoso, S S S and Kim, M C. Acceleration of convective dissolution by an instantaneous chemical reaction: A comparison of experimental and numerical results. In Chemical Engineering Science, 181: 298-310, 2018. [doi..
  46. Sushko, T A, Smolskaya, S, Vasilevskaya, A, Bukhdruker, S, Tsumoto, K, Kavaleuski, A, Marin, E, Usanov, S A, Borshchevskiy, V and Strushkevich, N V. Complex biochemical and biophysical study of CYP136 from M. tuberculosis. In Journal of Bioenergetics and Biomembranes, 50 (6): 587-588, 2018.
  47. Shevchenko, M, Bogorodskiy, A, Bolkhovitina, E, Borshchevskiy, V and Sapozhnikov, A. Airway intraepithelial dendritic cell network contributes for resistance to Aspergillus fumigatus infection. In European Journal of Immunology, 48: 105-106, 2018.
  48. Marin, E, Gusach, A, Luginina, A, Kovalev, K, Liu, W, Weierstall, U, Nam, K H, Cho, Y, Mishin, A, Borshchevskiy, V and Cherezov, V. Successful GPCR structure determination using PAL XFEL. In Journal of Bioenergetics and Biomembranes, 50 (6): 513, 2018.

2017

  1. Buslaev, P and Gushchin, I. Effects of Coarse Graining and Saturation of Hydrocarbon Chains on Structure and Dynamics of Simulated Lipid Molecules. In Scientific Reports, 7: 15, 2017. [doi..
  2. Vasilchenko, A S, Vasilchenko, A V, Pashkova, T M, Smirnova, M P, Kolodkin, N I, Manukhov, I V, Zavilgelsky, G B, Sizova, E A, Kartashova, O L, Simbirtsev, A S, Rogozhin, E A, Duskaev, G K and Sycheva, M V. Antimicrobial activity of the indolicidin-derived novel synthetic peptide In-58. In Journal of Peptide Science, 23 (12): 855-863, 2017. [doi..
  3. Zheng, Y, Han, G W, Abagyan, R, Wu, B L, Stevens, R C, Cherezov, V, Kufareva, I and Handel, T M. Structure of CC Chemokine Receptor 5 with a Potent Chemokine Antagonist RevealsMechanisms of Chemokine Recognition and Molecular Mimicry by HIV. In Immunity, 46 (6): 1005-+, 2017. [doi..
  4. Padayatti, P S, Leung, J H, Mahinthichaichan, P, Tajkhorshid, E, Ishchenko, A, Cherezov, V, Soltis, S M, Jackson, J B, Stout, C D, Gennis, R B and Zhang, Q H. Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. In Structure, 25 (7): 1111-+, 2017. [doi..
  5. Zhang, X J, Zhao, F, Wu, Y R, Yang, J, Han, G W, Zhao, S W, Ishchenko, A, Ye, L T, Lin, X, Ding, K, Dharmarajan, V, Griffin, P R, Gati, C, Nelson, G, Hunter, M S, Hanson, M A, Cherezov, V, Stevens, R C, Tan, W F, Tao, H C and Xu, F. Crystal structure of a multi-domain human smoothened receptor in complex with a super stabilizing ligand. In Nature Communications, 8: 10, 2017. [doi..
  6. Maslov, I, Bogorodskiy, A, Mishin, A, Okhrimenko, I and Borshchevskiy, V. Gentle staining of halophilic microorganisms for fluorescence microscopy. In Febs Journal, 284: 378, 2017.
  7. Marin, E, Kornilov, D, Zinovev, E, Talyzina, A, Shevtsov, M, Mishin, A, Lazarev, V, Gordeliy, V, Manuvera, V and Borshchevskiy, V. Crystallographic structure of destabilase from Hirudo medicinalis - a small bifunctional enzyme with isopeptidase and lysozyme activities. In Febs Journal, 284: 203-204, 2017.
  8. Wang, P., Chang, A. Y, Novosad, V., Chupin, V. V, Schaller, R. D and Rozhkova, E. A. Cell-Free Synthetic Biology Chassis for Nanocatalytic Photon-to-Hydrogen Conversion. In ACS Nano, 2017. [doi..
  9. Zhou, X E, He, Y Z, W, de W. P, Gao, X, Kang, Y Y, N, Van E., Yin, Y T, Pal, K, Goswami, D, White, T A, Barty, A, Latorraca, N R, Chapman, H N, Hubbell, W L, Dror, R O, Stevens, R C, Cherezov, V, Gurevich, V V, Griffin, P R, Ernst, O P, Melcher, K and Xu, H E. Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors. In Cell, 170 (3): 457-+, 2017. [doi..
  10. Martin-Garcia, J M, Conrad, C E, Nelson, G, Stander, N, Zatsepin, N A, Zook, J, Zhu, L, Geiger, J, Chun, E, Kissick, D, Hilgart, M C, Ogata, C, Ishchenko, A, Nagaratnam, N, Roy-Chowdhury, S, Coe, J, Subramanian, G, Schaffer, A, James, D, Ketwala, G, Venugopalan, N, Xu, S L, Corcoran, S, Ferguson, D, Weierstall, U, Spence, J C H, Cherezov, V, Fromme, P, Fischetti, R F and Liu, W. Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation. In Iucrj, 4: 439-454, 2017. [doi..
  11. Grudinin, S., Garkavenko, M. and Kazennov, A. Pepsi-SAXS: an adaptive method for rapid and accurate computation of small-angle X-ray scattering profiles. In Acta Crystallographica Section D, 73 (5): 449-464, 2017. [doi..
  12. Zimin, V G and Cherezov, A L. Application of Backward Differentiation Formulas to Neutron Kinetics Problems. In Physics of Atomic Nuclei, 80 (8): 1377-1386, 2017. [doi..
  13. Nikolaev, M, Round, E, Gushchin, I, Polovinkin, V, Balandin, T, Kuzmichev, P, Shewhenko, V, Borshchevskiy, V, Kuklin, A, Round, A, Bernhard, F, Willbold, D, Biildt, G and Gordeliy, V. Integral Membrane Proteins Can Be Crystallized Directly from Nanodiscs. In Crystal Growth & Design, 17 (3): 945-948, 2017. [doi..
  14. Shevchenko, V, Mager, T, Kovalev, K, Polovinkin, V, Alekseev, A, Juettner, J, Chizhov, I, Bamann, C, Vavourakis, C, Ghai, R, Gushchin, I, Borshchevskiy, V, Rogachev, A, Melnikov, I, Popov, A, Balandin, T, Rodriguez-Valera, F, Manstein, D J, Bueldt, G, Bamberg, E and Gordeliy, V. Inward H+ pump xenorhodopsin: Mechanism and alternative optogenetic approach. In Science Advances, 3 (9): 10, 2017. [doi..
  15. Cherezov, D, Hawkins, S, Goldgof, D, Hall, L, Balagurunathan, Y, Gillies, R and Schabath, M. Quantitative Imaging Features Predict Incidence Lung Cancer in Low-Dose Computed Tomography (LDCT) Screening. In Journal of Thoracic Oncology, 12 (1): S582-S582, 2017.
  16. Ishchenko, A, Wacker, D, Kapoor, M, Zhang, A, Han, G W, Basu, S, Patel, N, Messerschmidt, M, Weierstall, U, Liu, W, Katritch, V, Roth, B L, Stevens, R C and Cherezov, V. Structural insights into the extracellular recognition of the human serotonin 2B receptor by an antibody. In Proceedings of the National Academy of Sciences of the United States of America, 114 (31): 8223-8228, 2017. [doi..
  17. Lyapina, E, Safronova, N, Burdakova, A, Gusach, A, Luginina, A, Semelina, M, Astashkin, R, Shevtsov, M, Mishin, A and Cherezov, V. Crystallization trials of human endothelin receptor B. In Febs Journal, 284: 161, 2017.
  18. Shevchenko, V., Gushchin, I., Polovinkin, V., Kovalev, K., Balandin, T., Borshchevskiy, V. and Gordeliy, V. Sodium and Engineered Potassium Light-Driven Pumps. [doi..
  19. Volkov, O, Kovalev, K, Polovinkin, V, Borshchevskiy, V, Bamann, C, Astashkin, R, Marin, E, Popov, A, Balandin, T, Willbold, D, Buldt, G, Bamberg, E and Gordeliy, V. Structural insights into ion conduction by channelrhodopsin 2. In Science, 358 (6366): 8, 2017. [doi..
  20. Polovinkin, V, Gushchin, I, Sintsov, M, Round, E, Balandin, T, Chervakov, P, Shevchenko, V, Utrobin, P, Popov, A, Borshchevskiy, V, Mishin, A, Kuklin, A, Willbold, D, Chupin, V, Popot, J.-L. and Gordeliy, V. Erratum to: High-Resolution Structure of a Membrane Protein Transferred from Amphipol to a Lipidic Mesophase (The Journal of Membrane Biology, (2014), 247, 9-10, (997-1004), 10.1007/s00232-014-9700-x). In Journal of Membrane Biology, 250 (2), 2017. [doi..
  21. Ishchenko, A., Peng, L., Zinovev, E., Vlasov, A., Lee, S. C., Kuklin, A., Mishin, A., Borshchevskiy, V., Zhang, Q. and Cherezov, V. Chemically Stable Lipids for Membrane Protein Crystallization. In Crystal Growth & Design, 17 (6): 3502-3511, 2017. [doi..
  22. Akishina, A A, Vorontsova, J E, Cherezov, R O, Mertsalov, I B, Zatsepina, O G, Slezinger, M S, Panin, V M, Petruk, S, Enikolopov, G N, Mazo, A, Simonova, O B and Kuzin, B A. Xenobiotic-induced activation of human aryl hydrocarbon receptor target genes in Drosophila is mediated by the epigenetic chromatin modifiers. In Oncotarget, 8 (61): 102934-102947, 2017. [doi..
  23. Hauss, T, Barrett, M and Dencher, N. Modulation of lipid membrane structure and dynamics in the presence of amyloid-beta peptide. In Abstracts of Papers of the American Chemical Society, 253: 2, 2017.
  24. Barykina, N V, Subach, O M, Piatkevich, K D, Jung, E E, Malyshev, A Y, Smirnov, I V, Bogorodskiy, A O, Borshchevskiy, V I, Varizhuk, A M, Pozmogova, G E, Boyden, E S, Anokhin, K V, Enikolopov, G N and Subach, F V. Green fluorescent genetically encoded calcium indicator based on calmodulin/M13-peptide from fungi. In Plos One, 12 (8): 27, 2017. [doi..
  25. Chupin, V V and Boldyrev, I A. 3-4- (E)-4- (E)-Phenyldiazenyl phenyldiazenyl phenoxypropane-1,2-dio l. In Molbank (1): 4, 2017. [doi..
  26. Johansson, L C, Stauch, B, Ishchenko, A and Cherezov, V. A Bright Future for Serial Femtosecond Crystallography with XFELs. In Trends in Biochemical Sciences, 42 (9): 749-762, 2017. [doi..
  27. Kudryavtseva, A A, Osetrova, M S, Livinyuk, V Y, Manukhov, I V and Zavilgelsky, G B. The importance of C-terminal aspartic acid residue (D141) to the antirestriction activity of the ArdB (R64) protein. In Molecular Biology, 51 (5): 724-727, 2017. [doi..
  28. Manukhov, V V and Fedortsov, A B. Contactless nondestructive method for determination of the carrier diffusion length in semiconductors and dielectrics. [doi..
  29. Melnikov, I., Polovinkin, V., Kovalev, K., Gushchin, I., Shevtsov, M., Shevchenko, V., Mishin, A., Alekseev, A., Rodriguez-Valera, F., Borshchevskiy, V., Cherezov, V., Leonard, G. A, Gordeliy, V. and Popov, A. Fast iodide-SAD phasing for high-throughput membrane protein structure determination. In Science Advances, 3 (5): e1602952, 2017. [doi..
  30. Ishchenko, A, Round, E, Borshchevskiy, V, Grudinin, S, Gushchin, I, Klare, J P, Remeeva, A, Polovinkin, V, Utrobin, P, Balandin, T, Engelhard, M, B\"uldt, G and Gordeliy, V. New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex. In Scientific Reports, 7: 41811, 2017. [doi..
  31. Bratanov, D, Borshchevskiy, V and Gordeliy, V. Heterologous expression of bacteriorhodopsin from Halobium salinarum. In Febs Journal, 284: 159, 2017.
  32. Gushchin, I., Melnikov, I., Polovinkin, V., Ishchenko, A., Yuzhakova, A., Buslaev, P., Bourenkov, G., Grudinin, S., Round, E., Balandin, T., Borshchevskiy, V., Willbold, D., Leonard, G., B\"uldt, G., Popov, A. and Gordeliy, V. Mechanism of transmembrane signaling by sensor histidine kinases. In Science, 356 (6342): eaah6345, 2017. [doi..

2016

  1. Kulvelis, Yu V, Ivanchev, S S, Primachenko, O N, Lebedev, V T, Marinenko, E A, Ivanova, I N, Kuklin, A I, Ivankov, O I and Soloviov, D V. Structure and property optimization of perfluorinated short side chain membranes for hydrogen fuel cells using orientational stretching. In RSC Advances, 6 (110): 108864-108875, 2016. [doi..
  2. Vartanyan, N, Gusach, A, Luginina, A, Ergasheva, M, Astashkin, R, Shevtsov, M, Mishin, A and Borshchevskiy, V. GPR17 (GPCR) expression in Sf9 cells. Evaluation of protein stability and surface expression. In Febs Journal, 283: 290, 2016.
  3. Cherezov, I and Cardoso, S S S. Acceleration of convective dissolution by chemical reaction in a Hele-Shaw cell. In Physical Chemistry Chemical Physics, 18 (34): 23727-23736, 2016. [doi..
  4. Batyuk, A, Galli, L, Ishchenko, A, Han, G W, Gati, C, Popov, P A, Lee, M Y, Stauch, B, White, T A, Barty, A, Aquila, A, Hunter, M S, Liang, M N, Boutet, S, Pu, M C, Liu, Z J, Nelson, G, James, D, Li, C F, Zhao, Y, Spence, J C H, Liu, W, Fromme, P, Katritch, V, Weierstall, U, Stevens, R C and Cherezov, V. Native phasing of x-ray free-electron laser data for a G protein-coupled receptor. In Science Advances, 2 (9): 9, 2016. [doi..
  5. Ishchenko, A, Cherezov, V and Liu, W. Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography. In Jove-Journal of Visualized Experiments (115): 8, 2016. [doi..
  6. Lee, M Y, Patel, N, Katritch, V, Stevens, R C and Cherezov, V. Structural Studies of the Human Kappa Opioid Receptor Active State Conformations. In Biophysical Journal, 110 (3): 38A-39A, 2016. [doi..
  7. Astashkin, R, Vartanyan, N, Gusach, A, Luginina, A, Ergasheva, M, Shevtsov, M, Mishin, A, Borshchevskiy, V and Cherezov, V. Pre-crystallization assays of an engineered human endothelin receptor type B. In Febs Journal, 283: 292, 2016.
  8. Lichtmannegger, J, Leitzinger, C, Wimmer, R, Schmitt, S, Schulz, S, Kabiri, Y, Eberhagen, C, Rieder, T, Janik, D, Neff, F, Straub, B K, Schirmacher, P, DiSpirito, A A, Bandow, N, Baral, B S, Flatley, A, Kremmer, E, Denk, G, Reiter, F P, Hohenester, S, Eckardt-Schupp, F, Dencher, N A, Adamski, J, Sauer, V, Niemietz, C, Schmidt, H H J, Merle, U, Gotthardt, D N, Kroemer, G, Weiss, K H and Zischka, H. Methanobactin reverses acute liver failure in a rat model of Wilson disease. In Journal of Clinical Investigation, 126 (7): 2721-2735, 2016. [doi..
  9. Padhorny, D, Kazennov, A, Zerbe, B S, Porter, K A, Xia, B, Mottarella, S E, Kholodov, Y, Ritchie, D W, Vajda, S and Kozakov, D. Protein-protein docking by fast generalized Fourier transforms on 5D rotational manifolds. In Proceedings of the National Academy of Sciences of the United States of America, 113 (30): E4286-E4293, 2016. [doi..
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  11. Bogorodskiy, A, Polovinkin, V, Mishin, A, Ilyinsky, N, Gordeliy, V, Cherezov, V, Buldt, G, Gensch, T and Borshchevskiy, V. Fluorescent study of in meso crystallization of membrane proteins. In Febs Journal, 283: 181, 2016.
  12. Kadukova, M. and Grudinin, S. Knodle: A Support Vector Machines-Based Automatic Perception of Organic Molecules from 3D Coordinates. In Journal of Chemical Information and Modeling, 56 (8): 1410-1419, 2016. [doi..
  13. Zheng, Y, Qin, L, Zacarias, N V O, H, de V., Han, G W, Gustavsson, M, Dabros, M, Zhao, C X, Cherney, R J, Carter, P, Stamos, D, Abagyan, R, Cherezov, V, Stevens, R C, Ijzerman, A P, Heitman, L H, Tebben, A, Kufareva, I and Handel, T M. Structure of CC chemokine receptor 2 with orthosteric and allosteric antagonists. In Nature, 540 (7633): 458-+, 2016. [doi..
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  16. Kalpathy-Cramer, J, Mamomov, A, Zhao, B S, Lu, L, Cherezov, D, Napel, S, Echegaray, S, Rubin, D, McNitt-Gray, M, Lo, P, Sieren, J C, Uthoff, J, Dilger, S K N, Driscoll, B, Yeung, I, Hadjiiski, L, Cha, K, Balagurunathan, Y, Gillies, R and Goldgof, D. Radiomics of Lung Nodules: A Multi-Institutional Study of Robustness and Agreement of Quantitative Imaging Features. In Tomography, 2 (4): 430-437, 2016. [doi..
  17. White, T A, Barty, A, Liu, W, Ishchenko, A, Zhang, H T, Gati, C, Zatsepin, N A, Basu, S, Oberthur, D, Metz, M, Beyerlein, K R, Yoon, C H, Yefanov, O M, James, D, Wang, D J, Messerschmidt, M, Koglin, J E, Boutet, S, Weierstall, U and Cherezov, V. Serial femto-second crystallography datasets from G protein-coupled receptors. In Scientific Data, 3: 9, 2016. [doi..
  18. Kuter, K, Kratochwil, M, Berghauzen-Maciejewska, K, Glowacka, U, Sugawa, M D, Ossowska, K and Dencher, N A. Adaptation within mitochondrial oxidative phosphorylation supercomplexes and membrane viscosity during degeneration of dopaminergic neurons in an animal model of early Parkinson's disease. In Biochimica Et Biophysica Acta-Molecular Basis of Disease, 1862 (4): 741-753, 2016. [doi..
  19. Heifetz, A., Chudyk, E. I, Gleave, L., Aldeghi, M., Cherezov, V., Fedorov, D. G, Biggin, P. C and Bodkin, M. J. The Fragment Molecular Orbital Method Reveals New Insight into the Chemical Nature of GPCR–Ligand Interactions. In Journal of Chemical Information and Modeling, 56 (1): 159-172, 2016. [doi..
  20. Hawkins, S, Wang, H, Liu, Y, Garcia, A, Stringfield, O, Krewer, H, Li, Q, Cherezov, D, Gatenby, R A, Balagurunathan, Y, Goldgof, D, Schabath, M B, Hall, L and Gillies, R J. Predicting Malignant Nodules from Screening CT Scans. In Journal of Thoracic Oncology, 11 (12): 2120-2128, 2016. [doi..
  21. Konopleva, M N, Khrulnova, S A, Baranova, A, Ekimov, L V, Bazhenov, S V, Goryanin, I I and Manukhov, I V. A combination of luxR1 and luxR2 genes activates Pr-promoters of psychrophilic Aliivibrio logei lux-operon independently of chaperonin GroEL/ES and protease Lon at high concentrations of autoinducer. In Biochem Biophys Res Commun, 473 (4): 1158-1162, 2016. [doi..
  22. Karimova, D N, Manukhov, I V, Gnuchikh, E Y, Karimov, I F and Deryabin, D G. Reactive Oxygen and Nitrogen Species' Effect on lux-Biosensors Based on Escherichia coli and Salmonella typhimurium. In Applied Biochemistry and Microbiology, 52 (3): 269-276, 2016. [doi..
  23. Bury, C. S, McGeehan, J. E, Antson, A. A, Carmichael, I., Gerstel, M., Shevtsov, M. B and Garman, E. F. RNA protects a nucleoprotein complex against radiation damage. In Acta Crystallographica Section D, 72 (5): 648-657, 2016. [doi..
  24. Barrett, M A, Trapp, M, Lohstroh, W, Seydel, T, Ollivier, J, Ballauff, M, Dencher, N A and Hauss, T. Alzheimer's peptide amyloid-beta, fragment 22-40, perturbs lipid dynamics. In Soft Matter, 12 (5): 1444-1451, 2016. [doi..
  25. Zhernenkov, M, Bolmatov, D, Soloviov, D, Zhernenkov, K, Toperverg, B P, Cunsolo, A, Bosak, A and Cai, Y Q. Revealing the mechanism of passive transport in lipid bilayers via phonon-mediated nanometre-scale density fluctuations. In Nature Communications, 7: 11575, 2016. [doi..
  26. Zhou, X E, Gao, X, Barty, A, Kang, Y Y, He, Y Z, Liu, W, Ishchenko, A, White, T A, Yefanov, O, Han, G W, Xu, Q P, W, de W. P, Suino-Powell, K M, Boutet, S, Williams, G J, Wang, M T, Li, D F, Caffrey, M, Chapman, H N, Spence, J C H, Fromme, P, Weierstall, U, Stevens, R C, Cherezov, V, Melcher, K and Xu, H E. X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex. In Scientific Data, 3: 13, 2016. [doi..
  27. Kadochnikov, V V, Egorov, V V, Shvetsov, A V, Kuklin, A I, Isaev-Ivanov, V V and Lebedev, D V. Modeling of conformational transitions of fibrillogenic peptide, homologous to beta-domain of human alpha-lactalbumin. In Crystallography Reports, 61 (1): 98-105, 2016. [doi..
  28. Karimov, I F, Deryabin, D G, Karimova, D N, Subbotina, T Y and Manukhov, I V. Evaluation of Oxidative Metabolism in Leukocytes during Phagocytosis of Escherichia coli Carrying Genetic Constructs soxS::lux or katG::lux. In Bull Exp Biol Med, 161 (2): 276-280, 2016. [doi..
  29. Cherezov, A L. Analysis of the Correlation Function of the Neutron Field in a Critical Reactor Taking Account of the Neutron Intensity Regulation System. In Atomic Energy, 120 (2): 100-104, 2016. [doi..
  30. Khrulnova, S. A, Baranova, A., Bazhenov, S. V, Goryanin, I. I, Konopleva, M. N, Maryshev, I. V, Salykhova, A. I, Vasilyeva, A. V, Manukhov, I. V and Zavilgelsky, G. B. Lux-operon of the marine psychrophilic bacterium Aliivibrio logei: a comparative analysis of the LuxR1/LuxR2 regulatory activity in Escherichia coli cells. In Microbiology, 162 (4): 717-724, 2016. [doi..
  31. Byvshev, I. M, Vangeli, I. M, Murugova, T. N, Ivankov, O. O, Kuklin, A. I, Popov, V. I, Teplova, V. V and Yaguzhinsky, L. S. On the existence of two states of OXPHOS system supercomplex in heart mitochondria. In Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1857: e35-e36, 2016. [doi..
  32. Schmidt, A E, Shvetsov, A V, Kuklin, A I, Lebedev, D V, Surzhik, M A, Sergeev, V R and Isaev-Ivanov, V V. Small-angle scattering study of Aspergillus awamori glycoprotein glucoamylase. In Crystallography Reports, 61 (1): 149-152, 2016. [doi..
  33. Lensink, M F, Velankar, S, Kryshtafovych, A, Huang, S Y, Schneidman-Duhovny, D, Sali, A, Segura, J, Fernandez-Fuentes, N, Viswanath, S, Elber, R, Grudinin, S, Popov, P, Neveu, E, Lee, H, Baek, M, Park, S, Heo, L, G, Rie L., Seok, C, Qin, S, Zhou, H X, Ritchie, D W, Maigret, B, Devignes, M D, Ghoorah, A, Torchala, M, Chaleil, R A, Bates, P A, Ben-Zeev, E, Eisenstein, M, Negi, S S, Weng, Z, Vreven, T, Pierce, B G, Borrman, T M, Yu, J, Ochsenbein, F, Guerois, R, Vangone, A, Rodrigues, J P, G, van Z., Nellen, M, Xue, L, Karaca, E, Melquiond, A S, Visscher, K, Kastritis, P L, Bonvin, A M, Xu, X, Qiu, L, Yan, C, Li, J, Ma, Z, Cheng, J, Zou, X, Shen, Y, Peterson, L X, Kim, H R, Roy, A, Han, X, Esquivel-Rodriguez, J, Kihara, D, Yu, X, Bruce, N J, Fuller, J C, Wade, R C, Anishchenko, I, Kundrotas, P J, Vakser, I A, Imai, K, Yamada, K, Oda, T, Nakamura, T, Tomii, K, Pallara, C, Romero-Durana, M, Jimenez-Garcia, B, Moal, I H, Fernandez-Recio, J, Joung, J Y, Kim, J Y, Joo, K, Lee, J, Kozakov, D, Vajda, S, Mottarella, S, Hall, D R, Beglov, D, Mamonov, A, Xia, B, Bohnuud, T, A, Del C. C, Ichiishi, E, Marze, N, Kuroda, D, S, Roy B. S, Gray, J J, Chermak, E, Cavallo, L, Oliva, R and , . Prediction of homoprotein and heteroprotein complexes by protein docking and template-based modeling: A CASP-CAPRI experiment. In Proteins, 84 Suppl 1: 323-348, 2016. [doi..
  34. Deryabina, D G, Efremova, L V, Karimov, I F, Manukhov, I V, Gnuchikh, E Y and Miroshnikov, S A. Comparative Sensitivity of the Luminescent Photobacterium phosphoreum, Escherichia coli, and Bacillus subtilis Strains to Toxic Effects of Carbon-Based Nanomaterials and Metal Nanoparticles. In Mikrobiologiia, 85 (2): 177-186, 2016.
  35. Gushchin, I., Shevchenko, V., Polovinkin, V., Borshchevskiy, V., Buslaev, P., Bamberg, E. and Gordeliy, V. Structure of the light-driven sodium pump KR2 and its implications for optogenetics. In The FEBS journal, 283 (7): 1232-1238, 2016. [doi..
  36. Buslaev, P., Gordeliy, V., Grudinin, S. and Gushchin, I. Principal Component Analysis of Lipid Molecule Conformational Changes in Molecular Dynamics Simulations. In Journal of Chemical Theory and Computation, 12 (3): 1019-1028, 2016. [doi..
  37. Mishin, A V, Luginina, A P, Potapenko, A P, Borshchevskiy, V I, Katritch, V, Edelweiss, E, Okhrimenko, I S, Gordeliy, V I and Cherezov, V G. Expression and purification of an engineered human endothelin receptor B in a monomeric form. In Doklady Biochemistry and Biophysics, 467 (1): 157-161, 2016. [doi..
  38. Arzumanyan, G. M, Doroshkevich, N. V, Mamatkulov, K. Z, Shashkov, S. N, Zinovev, E. V, Vlasov, A. V, Round, E. S and Gordeliy, V. I. Highly Sensitive Coherent Anti-Stokes Raman Scattering Imaging of Protein Crystals. In Journal of the American Chemical Society, 138 (41): 13457-13460, 2016. [doi..
  39. Dzinic, T, Hartwig, S, Lehr, S and Dencher, N A. Oxygen and differentiation status modulate the effect of X-ray irradiation on physiology and mitochondrial proteome of human neuroblastoma cells. In Archives of Physiology and Biochemistry, 122 (5): 257-265, 2016. [doi..
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  41. Egorov, V V, Shaldzhyan, A A, Gorshkov, A N, Zabrodskaya, Ya A, Lebedev, D V, Kuklin, A I, Ksenofontova, O I, Shvetsov, A V, Vasin, A V, Tsybalova, L M and Isaev-Ivanov, V V. On the structural features of influenza A nucleoprotein particles from small-angle X-ray scattering data. In Journal of Surface Investigation. X-ray, Synchrotron and Neutron Techniques, 10 (2): 322-325, 2016. [doi..

2015

  1. Popov, P and Grudinin, S. Knowledge of Native Protein-Protein Interfaces Is Sufficient To Construct Predictive Models for the Selection of Binding Candidates. In J Chem Inf Model, 55 (10): 2242-2255, 2015. [doi..
  2. Wolff, M., Unuchek, D., Zhang, Bo, Gordeliy, V., Willbold, D. and Nagel-Steger, L. Amyloid $\beta$ Oligomeric Species Present in the Lag Phase of Amyloid Formation. In PloS ONE, 10 (5): e0127865, 2015. [doi..
  3. Petrovskaya, L E, Balashov, S P, Lukashev, E P, Imasheva, E S, Gushchin, I Yu, Dioumaev, A K, Rubin, A B, Dolgikh, D A, Gordeliy, V I, Lanyi, J K and , . ESR—A retinal protein with unusual properties from Exiguobacterium sibiricum. In Biochemistry (Moscow), 80: 688-700, 2015. [doi..
  4. Gushchin, I., Shevchenko, V., Polovinkin, V., Kovalev, K., Alekseev, A., Round, E., Borshchevskiy, V., Balandin, T., Popov, A., Gensch, T., Fahlke, C., Bamann, C., Willbold, D., B\"uldt, G., Bamberg, E. and Gordeliy, V. Crystal structure of a light-driven sodium pump. In Nature Structural & Molecular Biology, 22 (5): 390-395, 2015. [doi..
  5. Nguyen, H Q, Chupin, V V, Prokhorov, D I, Chikunov, I E, Kovtun, V Y, Tarumov, R A, Grebenyuk, A N and Shvets, V I. Creation and study of triterpenoid nanoparticles and radioprotective substance genistein. In Dokl Biochem Biophys, 464: 338-340, 2015. [doi..
  6. Borshchevskiy, V., Round, E., Bertsova, Y., Polovinkin, V., Gushchin, I., Ishchenko, A., Kovalev, K., Mishin, A., Kachalova, G., Popov, A., Bogachev, A. and Gordeliy, V. Structural and functional investigation of flavin binding center of the NqrC subunit of sodium-translocating NADH:quinone oxidoreductase from Vibrio harveyi. In PloS ONE, 10 (3): e0118548, 2015. [doi..
  7. Zavilgelsky, G B, Melkina, O E, Kotova, V Y, Konopleva, M N, Manukhov, I V and Pustovoit, K S. Photoreactivating Activity of Bioluminescence: Repair of UV-damaged DNA of Escherichia coli Occurs with Assistance of lux-Genes of Marine Bacteria. In Biofizika, 60 (5): 898-905, 2015.
  8. Ryzhykau, Y L, Nikolaev, M Y, Soloviov, D V, Ivankov, O I, Kovalev, Y S, Murugova, T N, Zinovev, E V, Vlasov, A V, Rogachev, A V, Borshchevskiy, V I, Gordeliy, V I and Kuklin, A I. Small-angle scattering studies of phospholipids phase transition in membrane mimicking systems. In Febs Journal, 282: 235, 2015.
  9. Nguen, H Q, Zhdanova, K A, Uvarova, V S, Bragina, N A, Mironov, A F, Chupin, V V and Shvets, V I. Development and characterization of nanoparticles prepared from the mixture of triterpenoids and amphiphilic meso-arylporphirins. In Russian Journal of Bioorganic Chemistry, 41 (2): 161-169, 2015. [doi..
  10. Anufrieva, N V, Morozova, E A, Kulikova, V V, Bazhulina, N P, Manukhov, I V, Degtev, D I, Gnuchikh, E Y, Rodionov, A N, Zavilgelsky, G B and Demidkina, T V. Sulfoxides, Analogues of L-Methionine and L-Cysteine As Pro-Drugs against Gram-Positive and Gram-Negative Bacteria. In Acta Naturae, 7 (4): 128-135, 2015.
  11. Dzhumashev, D B, Byvshev, I M, Eremeev, S A and Yaguzhinsky, L S. Specificity of interactions of the surface-active protonophore 2,4,6-trichloro-3-pentadecylphenol with artificial and mitochondrial membranes. In Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology, 9 (2): 100-106, 2015. [doi..
  12. Zander, U., Bourenkov, G., Popov, A. N, D., de S., Svensson, O., McCarthy, A. A, Round, E., Gordeliy, V., Mueller-Dieckmann, C. and Leonard, G. A. MeshAndCollect: an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines. In Acta Crystallographica Section D: Biological Crystallography, 71 (Pt 11): 2328-2343, 2015. [doi..
  13. Pattni, B S, Chupin, V V and Torchilin, V P. New Developments in Liposomal Drug Delivery. In Chemical Reviews, 115 (19): 10938-10966, 2015. [doi..
  14. Vlasov, A V, Ivankov, O I, Borshchevskiy, V I, Ishchenko, A, Peng, L, Lee, S, Zhang, Q, Kuklin, A I and Cherezov, V. High-throughput SAXS analysis of lipidic mesophases for structural studies of membrane proteins. In Febs Journal, 282: 234, 2015.
  15. Bulavin, L A, Soloviov, D V, Gordeliy, V I, Svechnikova, O S, Krasnikova, A O, Kasian, N A, Vashchenko, O V and Lisetski, L N. Lyotropic model membrane structures of hydrated DPPC: DSC and small-angle X-ray scattering studies of phase transitions in the presence of membranotropic agents. In Phase Transitions, 88 (6): 582-592, 2015. [doi..
  16. Melkina, O E, Kotova, V Y, Konopleva, M N, Manukhov, I V, Pustovoit, K S and Zavilgelsky, G B. Photoreactivation of UV-irradiated Escherichia coli K12 AB1886 uvrA6 with assistance of luminescence of Photobacterium leiognathi Luciferase. In Mol Biol (Mosk), 49 (6): 1035-1040, 2015. [doi..
  17. Фельдман, Т Б, Иваньков, А И, Муругова, Т Н, Куклин, А И, Шелякин, П В, Яковлева, М А, Горделий, В И, Белушкин, А В and Островский, М А. Исследование супрамолекулярной организации зрительного пигмента родопсина в фоторецепторной мембране методом малоуглового рассеяния нейтронов с вариацией контраста. In Доклады Академии наук, 465 (5): 627-630, 2015. [doi..
  18. Nguyen, H Q, Zhdanova, K A, Uvarova, V S, Bragina, N A, Mironov, A F, Chupin, V V and Svets, V I. Creation and Study of Triterpenoid Nanoparticles and Amphiphilic meso-Arylporphyrins. In Bioorg Khim, 41 (2): 185-194, 2015.
  19. Bratanov, D., Balandin, T., Round, E., Shevchenko, V., Gushchin, I., Polovinkin, V., Borshchevskiy, V. and Gordeliy, V. An Approach to Heterologous Expression of Membrane Proteins. The Case of Bacteriorhodopsin. In PloS ONE, 10 (6): e0128390, 2015. [doi..
  20. Bogorodskiy, A, Frolov, F, Mishin, A, Round, E, Polovinkin, V, Cherezov, V, Gordeliy, V, Buldt, G, Gensch, T and Borshchevskiy, V. Nucleation and Growth of Membrane Protein Crystals In Meso-A Fluorescence Microscopy Study. In Crystal Growth & Design, 15 (12): 5656-5660, 2015. [doi..
  21. Kuter, K, Olech, L and Dencher, N A. Prolonged astrocytes dysfunction and dopaminergic neurons degeneration cause small changes in mitochondrial complex I and IV activity and supercomplexes assembly in substantia nigra. In Glia, 63: E141-E142, 2015.

2014

  1. Polovinkin, V, Gushchin, I, Sintsov, M, Round, E, Balandin, T, Chervakov, P, Schevchenko, V, Utrobin, P, Popov, A, Borshchevskiy, V, Mishin, A, Kuklin, A, Willbold, D, Chupin, V, Popot, J.-L. and Gordeliy, V. High-Resolution Structure of a Membrane Protein Transferred from Amphipol to a Lipidic Mesophase. In The Journal of Membrane Biology, 247 (9-10): 997-1004, 2014. [doi..
  2. Kotova, V., Ryzhenkova, K V, Manukhov, I V and Zavil'gel'skii, G B. Inducible specific lux-biosensors for the detection of antibiotics: construction and main parameters. In Prikl Biokhim Mikrobiol, 50 (1): 112-117, 2014.
  3. Murugova, T N and Balgavy, P. Molecular volumes of DOPC and DOPS in mixed bilayers of multilamellar vesicles. In Phys Chem Chem Phys, 16 (34): 18211-18216, 2014. [doi..
  4. Cherny, A Yu., Anitas, E M, Osipov, V A and Kuklin, A I. Small-angle scattering from multiphase fractals. In Journal of Applied Crystallography, 47 (1): 198-206, 2014. [doi..
  5. Polovinkin, V, Balandin, T, Volkov, O, Round, E, Borshchevskiy, V, Utrobin, P, D, von S., Royant, A, Willbold, D, Arzumanyan, G, Chupin, V, Popot, J L and Gordeliy, V. Nanoparticle surface-enhanced Raman scattering of bacteriorhodopsin stabilized by amphipol a8-35. In The Journal of membrane biology, 247 (9-10): 971-980, 2014. [doi..
  6. Potapenko, A, Mishin, A, Borshchevskiy, V, Cherezov, V and Gordeliy, V. Gene-engineering and expression of the human endothelin A receptor' modifications. In Febs Journal, 281: 197-198, 2014.
  7. Beli\vcka, M., Ku\vcerka, N., Uhríková, D., Islamov, A. Kh, Kuklin, A. I, Devínsky, F. and Balgavý, P. Effects of N,N-dimethyl-N-alkylamine-N-oxides on DOPC bilayers in unilamellar vesicles: small-angle neutron scattering study. In European Biophysics Journal, 43 (4): 179-189, 2014. [doi..
  8. Popov, P and Grudinin, S. Rapid determination of RMSDs corresponding to macromolecular rigid body motions. In J Comput Chem, 35 (12): 950-956, 2014. [doi..
  9. Byvshev, I., Murugova, T N, Ivankov, O O, Vangeli, I M, Kuklin, A I and Yaguzhinskiy, L S. Respiration chain and ATP-synthesis system function as tightly-bounded supercomplex. In Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1837, Supp: e25-e26, 2014. [doi..
  10. Shibaev, A V, Tamm, M V, Molchanov, V S, Rogachev, A V, Kuklin, A I, Dormidontova, E E and Philippova, O E. How a viscoelastic solution of wormlike micelles transforms into a microemulsion upon absorption of hydrocarbon: new insight. In Langmuir, 30 (13): 3705-3714, 2014. [doi..
  11. Luginina, A, Alexey, M, Gusach, A, Cherezov, V and Borshchevskiy, V. Expression, purification and functional analyses of human CysLT1 and GPR17 proteins. In Febs Journal, 281: 196-197, 2014.
  12. Melkina, O E, Goryanin, I I, Manukhov, I V, Baranova, A V, Kolb, V A, Svetlov, M S and Zavilgelsky, G B. Trigger factor assists the refolding of heterodimeric but not monomeric luciferases. In Biochemistry (Mosc), 79 (1): 62-68, 2014. [doi..
  13. Mishin, A, Luginina, A, Potapenko, A, Gusach, A, Borshchevskiy, V, Cherezov, V and Gordeliy, V. Expression and purification of the human endothelin receptor B for structural studies. In Febs Journal, 281: 196, 2014.
  14. Shevchenko, V, Gushchin, I, Polovinkin, V, Round, E, Borshchevskiy, V, Utrobin, P, Popov, A, Balandin, T, Buldt, G and Gordeliy, V. Crystal Structure of Escherichia coli-Expressed Haloarcula marismortui Bacteriorhodopsin I in the Trimeric Form. In Plos One, 9 (12): 20, 2014. [doi..
  15. Khabibullina, N, Borshchevskiy, V, Gushchin, I, Gordeliy, V and Buldt, G. Expression of the human HCN channels - promising targets for nervous system and heart diseases treatment. In Febs Journal, 281: 196, 2014.
  16. Popov, P, Ritchie, D W and Grudinin, S. DockTrina: docking triangular protein trimers. In Proteins, 82 (1): 34-44, 2014. [doi..
  17. Vlasov, A, Murugova, T, Grudinin, S, Ivankov, O, Soloviov, D, Rogachev, A, Round, A, Ryzhykau, Y, Mishin, A, Balandin, T, Borshchevskiy, V, Gordeliy, V and Kuklin, A. Protein structure and structural ordering versus concentration dependence. In Febs Journal, 281: 593-594, 2014.
  18. Nogly, P., Gushchin, I., Remeeva, A., Esteves, A. M, Borges, N., Ma, P., Ishchenko, A., Grudinin, S., Round, E., Moraes, I., Borshchevskiy, V., Santos, H., Gordeliy, V. and Archer, M. X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism. In Nature Communications, 5: 1-10, 2014. [doi..
  19. Gibhardt, H., R., Haramagatti C., K., Islamov A., I., Ivankov O., I., Kuklin A. and Eckold, G. Universal Behaviour of the Structure and Dynamics of Micelles Formed from Cationic Surfactants. In Zeitschrift f\"ur Physikalische Chemie, 228 (6-7): 769, 2014. [doi..
  20. Borshchevskiy, V., Round, E., Erofeev, I., Weik, M., Ishchenko, A., Gushchin, I., Mishin, A., Willbold, D., B\"uldt, G. and Gordeliy, V. Low-dose X-ray radiation induces structural alterations in proteins. In Acta Crystallographica. Section D, Biological Crystallography, 70 (10): 2675-2685, 2014. [doi..

2013

  1. Ishchenko, A, Round, E, Borshchevskiy, V, Grudinin, S, Gushchin, I, Klare, J P, Balandin, T, Remeeva, A, Engelhard, M, B\"uldt, G and Gordeliy, V. Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer. In Journal of Photochemistry and Photobiology B: Biology, 123: 55-58, 2013. [doi..
  2. Kuzmichev, P, Chupin, V, Dubinnyi, M, Petrovskaya, L and Arseniev, A. Novel affinity medium for purification of the human beta-adrenergic receptors. In Febs Journal, 280: 138, 2013.
  3. Gushchin, I, Gordeliy, V and Grudinin, S. Two Distinct States of the HAMP Domain from Sensory Rhodopsin Transducer Observed in Unbiased Molecular Dynamics Simulations. In Plos One, 8 (7), 2013. [doi..
  4. Moretti, R, Fleishman, S J, Agius, R, Torchala, M, Bates, P A, Kastritis, P L, Rodrigues, J P, Trellet, M, Bonvin, A M, Cui, M, Rooman, M, Gillis, D, Dehouck, Y, Moal, I, Romero-Durana, M, Perez-Cano, L, Pallara, C, Jimenez, B, Fernandez-Recio, J, Flores, S, Pacella, M, K, Praneeth K., Gray, J J, Popov, P, Grudinin, S, Esquivel-Rodriguez, J, Kihara, D, Zhao, N, Korkin, D, Zhu, X, Demerdash, O N, Mitchell, J C, Kanamori, E, Tsuchiya, Y, Nakamura, H, Lee, H, Park, H, Seok, C, Sarmiento, J, Liang, S, Teraguchi, S, Standley, D M, Shimoyama, H, Terashi, G, Takeda-Shitaka, M, Iwadate, M, Umeyama, H, Beglov, D, Hall, D R, Kozakov, D, Vajda, S, Pierce, B G, Hwang, H, Vreven, T, Weng, Z, Huang, Y, Li, H, Yang, X, Ji, X, Liu, S, Xiao, Y, Zacharias, M, Qin, S, Zhou, H X, Huang, S Y, Zou, X, Velankar, S, Janin, J, Wodak, S J and Baker, D. Community-wide evaluation of methods for predicting the effect of mutations on protein-protein interactions. In Proteins, 81 (11): 1980-1987, 2013. [doi..
  5. Gushchin, I, Chervakov, P, Kuzmichev, P, Popov, A N, Round, E, Borshchevskiy, V, Ishchenko, A, Petrovskaya, L, Chupin, V, Dolgikh, D A, Arseniev, A S, Kirpichnikov, M and Gordeliy, V. Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria (vol 110, pg 12631, 2013). In Proceedings of the National Academy of Sciences of the United States of America, 110 (36): 14813, 2013. [doi..
  6. Borshchevskiy, V. and Buldt, G. Structural biology: Active arrestin proteins crystallized. In Nature, 497 (7447): 45-46, 2013. [doi..

2012

  1. Ivanova, E A, Maslov, M A, Morozova, N G, Serebrennikova, G A and Chupin, V V. Synthesis of bivalent neogalactolipids via modified Staudinger reaction. In Rsc Advances, 2 (11): 4600-4602, 2012. [doi..
  2. Tarahovsky, Y S, Yagolnik, E A, Muzafarov, E N, Abdrasilov, B S and Kim, Y A. Calcium-dependent aggregation and fusion of phosphatidylcholine liposomes induced by complexes of flavonoids with divalent iron. In Biochim Biophys Acta, 1818 (3): 695-702, 2012. [doi..
  3. Gushchin, I., Gordeliy, V. and Grudinin, S. A novel dimerization interface of cyclic nucleotide binding domain, which is disrupted in presence of cAMP: implications for CNG channels gating. In Journal of Molecular Modeling, 18: 4053-4060, 2012. [doi..
  4. Semenova, A A, Chugunov, A O, Dubovskii, P V, Chupin, V V, Volynsky, P E and Boldyrev, I A. The role of chain rigidity in lipid self-association: Comparative study of dihexanoyl- and disorbyl-phosphatidylcholines. In Chemistry and Physics of Lipids, 165 (4): 382-386, 2012. [doi..
  5. Gushchin, I. Yu, Gordeliy, V. I and Grudinin, S. HAMP Domain Region of Sensory Rhodopsin Transducers. In From Computational Biophysics to Systems Biology (CBSB11)–Celebrating Harold Scheraga's 90th Birthday, 8: 53, 2012.
  6. Kubicek, J., Schlesinger, R., Baeken, C., B\"uldt, G., Sch\"afer, F. and Labahn, J. Controlled In Meso Phase Crystallization – A Method for the Structural Investigation of Membrane Proteins. In PloS ONE, 7 (4): e35458, 2012. [doi..
  7. Erik, G., Andreas, M S., Sam, F., Stefanie, F., Jan, G., Bastian, P., Torbj\"orn, R., Stefan, S., Georg, B. and Stefan, E. Soft x-ray tomoholography. In New Journal of Physics, 14 (1): 13022, 2012.
  8. Granzin, J, Cousin, A, Weirauch, M, Schlesinger, R, Buldt, G and Batra-Safferling, R. Crystal structure of p44, a constitutively active splice variant of visual arrestin. In J Mol Biol, 416 (5): 611-618, 2012. [doi..
  9. Shmendel, E V, Timakova, A A, Maslov, M A, Morozova, N G and Chupin, V V. Synthesis of mannose-containing neoglycolipids as a component of targeted delivery system for transfer of nucleic acids into antigen-presenting cells. In Russian Chemical Bulletin, 61 (7): 1497-1501, 2012. [doi..
  10. Borshchevskiy, V. and Gordeliy, V. Crystallization of Membrane Proteins: Merohedral Twinning of Crystals. [doi..

2011

  1. Kirchberg, K., Kim, T., M\"oller, M., Skegro, D., G., Dasara R., Granzin, J., B\"uldt, G., Schlesinger, R. and Alexiev, U. Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process. In Proceedings of the National Academy of Sciences, 108 (46): 18690-18695, 2011. [doi..
  2. Murugova, T N, Solodovnikova, I M, Yurkov, V I, Gordeliy, V I, Kuklin, A I, Ivankov, O I, Kovalev, Yu S, Popov, V I, Teplova, V V and Yaguzhinsky, L S. Potentials of Small-angle Neutron Scattering for Studies of the Structure of “Live” Mitochondria. In Neutron News, 22 (3): 11-14, 2011. [doi..
  3. Borshchevskiy, V. I, Round, E. S, Popov, A. N, Bldt, G. and Gordeliy, V. I. X-ray-Radiation-Induced Changes in Bacteriorhodopsin Structure. In Journal of molecular biology, 409 (5): 813-825, 2011. [doi..
  4. Katranidis, A, Grange, W, Schlesinger, R, Choli-Papadopoulou, T, Bruggemann, D, Hegner, M and Buldt, G. Force measurements of the disruption of the nascent polypeptide chain from the ribosome by optical tweezers. In FEBS Lett, 585 (12): 1859-1863, 2011. [doi..
  5. Gushchin, I., Gordeliy, V. I and Grudinin, S. Role of the HAMP Domain Region of Sensory Rhodopsin Transducers in Signal Transduction. In Biochemistry, 50 (4): 574-580, 2011. [doi..
  6. Gushchin, I, Reshetnyak, A, Borshchevskiy, V, Ishchenko, A, Round, E, Grudinin, S, Engelhard, M, Buldt, G and Gordeliy, V. Active State of Sensory Rhodopsin II: Structural Determinants for Signal Transfer and Proton Pumping. In Journal of Molecular Biology, 412 (4): 591-600, 2011. [doi..
  7. Fitter, J., Katranidis, A., Rosenkranz, T., Atta, D., Schlesinger, R. and Buldt, G. Single molecule fluorescence spectroscopy: a tool for protein studies approaching cellular environmental conditions. In Soft Matter, 7 (4): 1254-1259, 2011. [doi..
  8. Solov'ev, D V, Kuklin, A I, Utrobin, P K, Ozerin, A N, Kurkin, T S, Ivan'kov, O I, Bulavin, L A and Gordelii, V I. X-ray scattering and volumetric P-V-T studies of the dimyristoylphosphatidylcholine-water system. In Journal of Surface Investigation. X-ray, Synchrotron and Neutron Techniques, 5 (1): 7-10, 2011. [doi..

2010

  1. Borshchevskiy, V., Efremov, R., Moiseeva, E., Bldt, G. and Gordeliy, V. Overcoming merohedral twinning in crystals of bacteriorhodopsin grown in lipidic mesophase. In Acta crystallographica. Section D, Biological crystallography, 66 (Pt 1): 26-32, 2010. [doi..
  2. Borshchevskiy, V., Moiseeva, E., Kuklin, A., Bldt, G., Hato, M. and Gordeliy, V. Isoprenoid-chained lipid $\beta$-XylOC16+4—A novel molecule for in meso membrane protein crystallization. In Journal of Crystal Growth, 312 (22): 3326-3330, 2010. [doi..

2009

  1. Moiseeva, E S, Reshetnyak, A B, Borshchevskiy, V I, Baeken, C, Buldt, G and Gordeliy, V I. Comparative analysis of the quality of membrane protein bacteriorhodopsin crystals during crystallization in octylglucoside and octylthioglucoside. In Journal of Surface Investigation. X-ray, Synchrotron and Neutron Techniques, 3 (1): 29-32, 2009. [doi..
  2. Моисеева, Е, Решетняк, А, Борщевский, В, Баекен, К, Бюлдт, Г and Горделий, В. Сравнительный анализ качества кристаллов мембранного белка бактериородопсина при кристаллизации в октилглюкозиде и октилглюкозиде. In Поверхность. Рентгеновские, синхротронные и нейтронные исследования., 1: 34-37, 2009.

2008

  1. Решетняк, А, Борщевский, В, Кларе, Й, Моисеева, Е, Энгельгардт, М, Бюлдт, Г and Горделий, В. Сравнительный анализ структур мембранного белка сенсорного родопсина II в комплексе с трансдюсером и без него. In Поверхность. Рентгеновские, синхротронные и нейтронные исследования., 12: 78-84, 2008.
  2. Reshetnyak, A B, Borshchevskiy, V I, Klare, J, Moiseeva, E S, Engelhardt, M, Buldt, G and Gordeliy, V I. Comparative analysis of sensory rhodopsin II structures in complex with a transducer and without it. In Journal of Surface Investigation. X-ray, Synchrotron and Neutron Techniques, 2 (6): 894-899, 2008. [doi..

2005

  1. Yevdokimov, Yu. M, Salyanov, V I, Kondrashina, O V, Lagutina, M A, Gasanov, A A, Nikiforov, V N, Borshchevskii, V I, Dembo, K A and Reshetov, I V. Liquid Crystal Dispersions of DNA Complexes with Gadolinium As a Possible Basis for Neutron-Trapping Therapy. In Doklady Biochemistry and Biophysics, 402 (1-6): 240-242, 2005. [doi..
  2. Yevdokimov, Y. M, Salyanov, V. I, Kondrashina, O. V, Borshevsky, V. I, Semenov, S. V, Gasanov, A. A, Reshetov, I. V, Kuznetsov, V. D, Nikiforov, V. N, Akulinichev, S. V, Mordovskoi, M. V, Potashev, S. I and Skorkin, V. M. Particles of liquid-crystalline dispersions formed by (nucleic acid-rare earth element) complexes as a potential platform for neutron capture therapy. In International journal of biological macromolecules, 37 (4): 165-173, 2005. [doi..

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