Артемьев Игорь Владимирович


Научный сотрудник (Лаборатория рентгеноструктурных исследований биополимеров)

Тел.: +7 (495) 335-16-77

Эл. почта: artem1@ibch.ru

Избранные публикации

  1. Pletneva NV, Pletnev SV, Efremov RG, Goryacheva EA, Artemyev IV, Arkhipova SF, Pletnev VZ (2017). Crystal structure of the pH-dependent green fluorescent protein WasCFP with the tryptophan based chromophore at extremely low value pH 2.0. CRYSTALLOGR REP+  (0), in press
  2. Pletnev VZ, Pletneva NV, Efremov RG, Goryacheva EA, Artemyev IV, Arkhipova SF, Sarkisyan KS, Mishin AS, Lukyanov KA, Pletnev SV (2016). Three-dimensional structure of a pH-dependent fluorescent protein WasCFP with a tryptophan based deprotonated chromophore. Russ. J. Bioorganic Chem. 42 (6), 612–618
  3. Плетнёв ВЗ, Плетнева НВ, Ефремов РГ, Горячева ЕА, Артемьев ИВ, Архипова СФ, Саркисян КС, Мишин АС, Лукьянов КА, Плетнев СВ (2016). Пространственная структура рН-зависимого зеленого флуоресцентного белка WASCFP с депротонированным хромофором на основе триптофана. 42 (6), 675–682
  4. Pletnev VZ, Pletneva NV, Efremov RG, Goryacheva EA, Artemyev IV, Arkhipova SF, Sarkisyan KS, Mishin AS, Lukyanov KA, Pletnev SV (2016). Three-dimensional structure of pH-dependent fluorescent protein WasCFP with the tryptophan based deprotonated chromophore. 42 (6), 612–618
  5. Pletneva NV, Pletnev SV, Bogdanov AM, Goriacheva EA, Artemev IV, Suslova EA, Arkhipova SF, Pletnev VZ (2014). Three dimensional structure of the dimeric gene-engineered variant of green fluorescent protein EGFP-K162Q in P6(1) crystal space group. Russ. J. Bioorganic Chem. 40 (4), 414–420
  6. Pletneva NV, Pletnev SV, Bogdanov AM, Goryacheva EA, Artemyev IV, Suslova EA, Arkhipova SF, Pletnev VZ (2014). Spatial structure of dimeric a genetically engineered variant of green fluorescent protein EGFP-K162Q in the P61crystal space group. Russ. J. Bioorganic Chem. 40 (4), 383–389
  7. Arkhipova SF, ArtemYev IV, Goryacheva EA, Pletnev VZ (2008). Conformational analysis of cyclic dipeptides: I. [InlineMediaObject not available: See fulltext.], [InlineMediaObject not available: See fulltext.], [InlineMediaObject not available: See fulltext.], and [InlineMediaObject not available: See fulltext.]. Russ. J. Bioorganic Chem. 34 (5), 544–549
  8. Afonin PV, Fokin AV, Shingarova LN, Korobko VG, Tsygannik IN, Artemev IV, Pletnev SV, Pangborn W, Duax WL, Pletnev VZ (2002). Three-dimensional structure of the Arg32His mutant of the human tumor necrosis factor determined at 2.5 Å resolution from X-ray data for a twin crystal. CRYSTALLOGR REP+ 47 (4), 629–634
  9. Kostetsky PV, Artemev IV (2000). A conformational analysis of biologically active RGD-containing cyclopentapeptides. Bioorg Khim 26 (4), 297–298
  10. Kostetsky PV, Artemev IV (2000). A conformational analysis of biologically active RGD-containing cyclopentapeptides. Russ. J. Bioorganic Chem. 26 (4), 262–270
  11. Kostetsky PV, Artemev IV (1998). Substitution by Glu for restricting the conformational freedom of Lys-Xaa fragments in bioactive peptides by side chain lactamization. Mol Biol 32 (3), 410–416
  12. Kostetsky PV, Arkhipova SF, Artemev IV, Rodionov IL, Rodionova LN, Ivanov VT (1997). Conformational States of Cyclic Dipeptides with a Lactam Bond between ω-Functions of Lysine and Aspartic or Glutamic Acid Residues. Bioorg Khim 23 (7), 538
  13. Kostetsky PV, Arkhipova SF, Artemev IV, Rodionov IL, Rodionova LN, Ivanov VT (1997). Conformational states of cyclic dipeptides with a lactam bond between ω-functions of lysine and aspartic or glutamic acid residues. Russ. J. Bioorganic Chem. 23 (7), 491–497
  14. Kostetsky PV, Artemev IV (1997). Substitution of an Amino Acid Residue by Lys for Conformational Constraint of Xaa-Asp Fragment in Biologically Active Peptides by Side Chain Lactamization. Bioorg Khim 23 (3), 173
  15. Kostetsky PV, Artemev IV (1997). Substitution of an amino acid residue by Lys for conformational constraint of Xaa-Asp fragment in biologically active peptides by side chain lactamization. Russ. J. Bioorganic Chem. 23 (3), 150–155