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Публикации

  1. Shevchenko, M. A., Bogorodskiy, A. O., Troyanova, N. I., Servuli, E. A., Bolkhovitina, E. L., Büldt, G., Fahlke, C., Gordeliy, V. I., Gensch, T., Borshchevskiy, V. I. & Sapozhnikov, A. M. Aspergillus fumigatus Infection-Induced Neutrophil Recruitment and Location in the Conducting Airway of Immunocompetent, Neutropenic, and Immunosuppressed Mice. J. Immunol. Res. 2018, 1–12 (2018).

  2. Maslov, I., Bogorodskiy, A., Mishin, A., Okhrimenko, I., Gushchin, I., Kalenov, S., Dencher, N. A., Fahlke, C., Büldt, G., Gordeliy, V., Gensch, T. & Borshchevskiy, V. Efficient non-cytotoxic fluorescent staining of halophiles. Sci. Rep. 8, 2549 (2018).

  3. Ishchenko, A., Peng, L., Zinovev, E., Vlasov, A., Lee, S. C., Kuklin, A., Mishin, A., Borshchevskiy, V., Zhang, Q. & Cherezov, V. Chemically Stable Lipids for Membrane Protein Crystallization. Cryst. Growth Des. 17, 3502–3511 (2017).

  4. 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., Büldt, G., Popov, A. & Gordeliy, V. Mechanism of transmembrane signaling by sensor histidine kinases. Science 356, eaah6345 (2017).

  5. Ishchenko, A., Round, E., Borshchevskiy, V., Grudinin, S., Gushchin, I., Klare, J. P., Remeeva, A., Polovinkin, V., Utrobin, P., Balandin, T., Engelhard, M., Büldt, G. & Gordeliy, V. New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex. Sci. Rep. 7, 41811 (2017).

  6. 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. & Popov, A. Fast iodide-SAD phasing for high-throughput membrane protein structure determination. Sci. Adv. 3, e1602952 (2017).

  7. Volkov, O., Kovalev, K., Polovinkin, V., Borshchevskiy, V., Bamann, C., Astashkin, R., Marin, E., Popov, A., Balandin, T., Willbold, D., Büldt, G., Bamberg, E. & Gordeliy, V. Structural insights into ion conduction by channelrhodopsin 2. Science (80). 358, eaan8862 (2017).

  8. Nikolaev, M., Round, E., Gushchin, I., Polovinkin, V., Balandin, T., Kuzmichev, P., Shevchenko, V., Borshchevskiy, V., Kuklin, A., Round, A., Bernhard, F., Willbold, D., Büldt, G. & Gordeliy, V. Integral Membrane Proteins Can Be Crystallized Directly from Nanodiscs. Cryst. Growth Des. 17, 945–948 (2017).

  9. 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. & Subach, F. V. Green fluorescent genetically encoded calcium indicator based on calmodulin/M13-peptide from fungi. PLoS One 12, e0183757 (2017).

  10. Shevchenko, V., Gushchin, I., Polovinkin, V., Kovalev, K., Balandin, T., Borshchevskiy, V. & Gordeliy, V. in Optogenetics 79 (Cambridge University Press, 2017).

  11. 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. & Gordeliy, V. Inward H + pump xenorhodopsin: Mechanism and alternative optogenetic approach. Sci. Adv. 3, e1603187 (2017).

  12. Mishin, A. V., Luginina, A. P., Potapenko, A. P., Borshchevskiy, V. I., Katritch, V., Edelweiss, E., Okhrimenko, I. S., Gordeliy, V. I. & Cherezov, V. G. Expression and purification of an engineered human endothelin receptor B in a monomeric form. Dokl. Biochem. Biophys. 467, 157–161 (2016).

  13. Gushchin, I., Shevchenko, V., Polovinkin, V., Borshchevskiy, V., Buslaev, P., Bamberg, E. & Gordeliy, V. Structure of the light-driven sodium pump KR2 and its implications for optogenetics. FEBS J. 283, 1232–8 (2016).

  14. Arzumanyan, G. M., Doroshkevich, N. V., Mamatkulov, K. Z., Shashkov, S. N., Zinovev, E. V., Vlasov, A. V., Round, E. S. & Gordeliy, V. I. Highly Sensitive Coherent Anti-Stokes Raman Scattering Imaging of Protein Crystals. J. Am. Chem. Soc. 138, 13457–13460 (2016).

  15. 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., Büldt, G., Bamberg, E. & Gordeliy, V. Crystal structure of a light-driven sodium pump. Nat. Struct. Mol. Biol. 22, 390–5 (2015).

  16. Bratanov, D., Balandin, T., Round, E., Shevchenko, V., Gushchin, I., Polovinkin, V., Borshchevskiy, V. & Gordeliy, V. An Approach to Heterologous Expression of Membrane Proteins. The Case of Bacteriorhodopsin. PLoS One 10, e0128390 (2015).

  17. Borshchevskiy, V., Round, E., Bertsova, Y., Polovinkin, V., Gushchin, I., Ishchenko, A., Kovalev, K., Mishin, A., Kachalova, G., Popov, A., Bogachev, A. & Gordeliy, V. Structural and functional investigation of flavin binding center of the NqrC subunit of sodium-translocating NADH:quinone oxidoreductase from Vibrio harveyi. PLoS One 10, e0118548 (2015).

  18. Bogorodskiy, A., Frolov, F., Mishin, A., Round, E., Polovinkin, V., Cherezov, V., Gordeliy, V., Büldt, G., Gensch, T. & Borshchevskiy, V. Nucleation and Growth of Membrane Protein Crystals In Meso — A Fluorescence Microscopy Study. Cryst. Growth Des. 15, 5656–5660 (2015).

  19. Borshchevskiy, V., Round, E., Erofeev, I., Weik, M., Ishchenko, A., Gushchin, I., Mishin, A., Willbold, D., Büldt, G. & Gordeliy, V. Low-dose X-ray radiation induces structural alterations in proteins. Acta Crystallogr. D. Biol. Crystallogr. 70, 2675–85 (2014).

  20. Shevchenko, V., Gushchin, I., Polovinkin, V., Round, E., Borshchevskiy, V., Utrobin, P., Popov, A., Balandin, T., Büldt, G. & Gordeliy, V. Crystal Structure of Escherichia coli-Expressed Haloarcula marismortui Bacteriorhodopsin I in the Trimeric Form. PLoS One 9, e112873 (2014).

  21. 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. & Archer, M. X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism. Nat. Commun. 5, 4169 (2014).

  22. 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. & Gordeliy, V. High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase. J. Membr. Biol. 247, 997–1004 (2014).

  23. Polovinkin, V., Balandin, T., Volkov, O., Round, E., Borshchevskiy, V., Utrobin, P., von Stetten, D., Royant, A., Willbold, D., Arzumanyan, G., Chupin, V., Popot, J.-L. & Gordeliy, V. Nanoparticle surface-enhanced Raman scattering of bacteriorhodopsin stabilized by amphipol a8-35. J. Membr. Biol. 247, 971–80 (2014).

  24. Borshchevskiy V., & Büldt G. (2013). Structural biology: Active arrestin proteins crystallized. Nature, 497, 45–46. doi:10.1038/nature12096 

  25. Borshchevskiy, V., Round, E., Erofeev, I., Weik, M., Ishchenko, A., Gushchin, I., Mishin, A., Willbold, D., Büldt, G. & Gordeliy, V. Low-dose X-ray radiation induces structural alterations in proteins. Acta Crystallogr. D. Biol. Crystallogr. 70, 2675–85 (2014).

  26. Gushchin I., Chervakov P., Kuzmichev P., Popov A. N., Round E., Borshchevskiy V., … Gordeliy, V. (2013). Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria. Proceedings of the National Academy of Sciences of the United States of America, 110(31), 12631–6. doi:10.1073/pnas.1221629110

  27. Gushchin IY, Gordeliy VI and Grudinin S. (2013). Two Distinct States of the HAMP Domain from Sensory Rhodopsin Transducer Observed in Unbiased Molecular Dynamics Simulations, PLOS ONE 8(7):e66917 

  28. Guehrs E., Stadler A.M., Flewett S., Frömmel S., Geilhufe J., Pfau B., … Georg Büldt , Eisebitt S. (2012). Soft x-ray tomoholography. New Journal of Physics, 14(1), 013022. doi:10.1088/1367-2630/14/1/013022

  29. Granzin J., Cousin A., Weirauch M., Schlesinger R., Büldt G., & Batra-Safferling R. (2012). Crystal structure of p44, a constitutively active splice variant of visual arrestin. Journal of molecular biology, 416(5), 611–8. doi:10.1016/j.jmb.2012.01.028

  30. Gushchin I.Y., Gordeliy V.I. and Grudinin S. (2012). A novel dimerization interface of cyclic nucleotide binding domain, which is disrupted in presence of cAMP: implications for CNG channels gating. J Mol Model. 18:4053-4060.

  31. Tarahovsky Y.S., Yagolnik E.A., Muzafarov E.N., Abdrasilov B.S. & Kim Y.A. (2012). Calcium-dependent aggregation and fusion of phosphatidylcholine liposomes induced by complexes of flavonoids with divalent iron. Biochimica et biophysica acta, 1818(3), 695–702. doi:10.1016/j.bbamem.2011.12.001

  32. Kristina Kirchberg, Tai-Yang Kim, Martina Möller, DarkoSkegro, Gayathri Dasara Raju, Joachim Granzin, Georg Büldt, Ramona Schlesinger and Ulrike Alexieva (2011). Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process. Proceedings of the National Academy of Sciences of the United States of America 108(46), 18690-18695 doi:10.1073/pnas.1015461108

  33. Borshchevskiy V.I., Round E.S., Popov A.N., Büldt G. & Gordeliy V.I. (2011). X-ray-Radiation-Induced Changes in Bacteriorhodopsin Structure. Journal of molecular biology, 409(5), 813–25. doi:10.1016/j.jmb.2011.04.038

  34. Gushchin I., Reshetnyak A., Borshchevskiy V., Ishchenko A., Round E., Grudinin S., … Gordeliy V. (2011). Active State of Sensory Rhodopsin II: Structural determinants for signal transfer and proton pumping. Journal of Molecular Biology, 412(4), 591–600. doi:10.1016/j.jmb.2011.07.022

  35. Gushchin I.Y., Gordeliy V.I. and Grudinin S. (2011). Role of the HAMP domain region of sensory rhodopsin transducers in signal transduction. Biochemistry, 50 (4): 574-580

  36. Borshchevskiy V., Efremov R., Moiseeva E., Büldt G. & Gordeliy V. (2010). Overcoming merohedral twinning in crystals of bacteriorhodopsin grown in lipidic mesophase. Acta crystallographica. Section D, Biological crystallography, 66(Pt 1), 26–32. doi:10.1107/S0907444909042838
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