Лаборатория ДНК-белковых взаимодействий

Избранные публикации
Структурно-функциональный анализ биополимеров

Лаборатория ДНК-белковых взаимодействий

Избранные публикации

Избранные публикации

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  2. 2.Nekrasov, A. N., Alekseeva, L. G., Pogosyan, R. А., Dolgikh, D. A., Kirpichnikov, M. P., de Brevern, A. G., & Anashkina, A. A. (2019). A minimum set of stable blocks for rational design of polypeptide chains. Biochimie, 160:88-92.
  3. 3.Koval V.S., Arutyunyan A.F., Salyanov V.I., Klimova R.R., Kushch A.A., Rybalkina E.Y., Susova O.Y., Zhuze A.L. (2018) DNA sequence-specific ligands. XVII. Synthesis, spectral properties, virological and biochemical studies of fluorescent dimeric bisbenzimidazoles DBA(n). Bioorgan Med Chem, 26, 9, 2302 – 2309
  4. 4.Anashkina, A. A., Kravatsky, Y., Kuznetsov, E., Makarov, A. A., & Adzhubei, A. A. (2018). Meta-server for automatic analysis, scoring and ranking of docking models. Bioinformatics, 34(2), 297-299.
  5. 5.Moiseeva, E.D., Bazhulina, N.P., Gursky, Y.G., Grokhovsky, S.L., Surovaya, A.N., Gursky, G.V. (2017) Targeting Holliday junctions by origin DNA-binding protein of herpes simplex virus type 1 J Biomol Struct Dyn, 35, 4, 704 - 723
  6. 6.Esipova N.G., Tumanyan V.G. (2017) Omnipresence of the polyproline II helix in fibrous and globular proteins. Curr Opin Struct Biol, 42, 41-49.
  7. 7.Kulakovskiy I.V., Vorontsov I.E., Yevshin I.S., Soboleva A.V., Kasianov A.S., Ashoor H., Ba-Alawi W., Bajic V.B., Medvedeva Y.A., Kolpakov F.A., Makeev V.J. (2016) HOCOMOCO: expansion and enhancement of the collection of transcription factor binding sites models. Nucleic Acids Res, 44 (D1), D116-D125.
  8. 8.Il'icheva, I.A., Khodikov, M.V., Poptsova, M.S., Nechipurenko, D.Y., Nechipurenko, Y.D., Grokhovsky, S.L. (2016) Structural features of DNA that determine RNA polymerase II core promoter. BMC Genomics, 17, 1973
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