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Timestamp: 2019-04-23 15:56:49+00:00

Document:
1. Efremov R.G., Nabiev I.R. Retinal Schiff's base microenvironment in the bacteriorhodopsin. - Biologicheskie membrany (Russian), (1985), v. 2, N 5, p. 460-469. English translation: Biological membranes (Arch. Soviet Sci.), (1986), v. 2, p. 858-875. 2. Abdulaev N.G., Nabiev I.R., Efremov R.G., Chumanov G.D. Retinal Schiff's base position relative to the surfaces of photoreceptor disk. - FEBS Lett., (1987), v. 213, p. 113-118. 3. Nabiev I.R., Efremov R.G., Chumanov G.D. Surface-enhanced Raman scattering and its application to study of biological molecules. Uspekhi fizicheskikh nauk (Russian), (1988), v. 154, N 3, p. 459-496. English translation: Sov. Phys. Usp. (1988), v. 31, p. 241 4. Ovchinnikov Yu.A., Arystarkhova E.A., Arzamazova N.M., Dzhandzhugazyan K.N., Efremov R.G., Nabiev I.R., Modyanov N.N. Differentiated analysis of the secondary structure of hydrophilic and hydrophobic regions in a- and b-subunits of Na,K-ATPase by Raman spectroscopy. - FEBS Lett. (1988), v. 227, N 2, p. 235-239. 5. Nabiev I.R., Dzhandzhugazyan K.N., Efremov R.G., Modyanov N.N. Binding of monovalent cations induces large changes in the secondary structure of Na,K-ATPase as probed by Raman spectroscopy. - FEBS Lett., (1988), v. 236, N 1, p. 235-239. 6. Efremov R.G., Feofanov A.V., Dzhandzhugazyan K.N., Modyanov N.N., Nabiev I.R. Study of ATP binding in the active site of Nа,K-ATPase as probed by ultraviolet resonance Raman spectroscopy. FEBS Lett., (1990), v. 260, N 2, p. 257-260. 7. Efremov R.G., Feofanov A.V., Nabiev I.R. Effect of hydrophobic environment on the resonance Raman spectra of tryptophan residues in proteins. J. Raman Spectrosc. (1992). v. 23, N 1, p. 69-73. 8. Efremov R.G., Gulyaev D.I., Vergoten G., Modyanov N.N. Application of 3D molecular hydrophobicity potential to the analysis of spatial organization of membrane domains in proteins. I. Hydrophobic properties of transmembrane segments of Na,K-ATPase. J. Protein Chemistry. (1992). v. 11, N 6, p. 665-675. 9. Efremov R.G., Gulyaev D.I., Modyanov N.N. Application of 3D molecular hydrophobicity potential to the analysis of spatial organization of membrane domains in proteins. II. Optimization of hydrophobic contacts in transmembrane hairpin structures of Na,K-ATPase. J. Protein Chemistry. (1992). v. 11, N 6, p. 699-708. 10. Efremov R.G., Gulyaev D.I., Modyanov N.N. Application of 3D molecular hydrophobicity potential to the analysis of spatial organization of membrane domains in proteins. III. Modeling of intramembrane moiety of Na,K-ATPase. J. Protein Chemistry. (1993). v. 12, N 2, p. 143-152. 11. Efremov R.G., Alix A.J.P. Environmental characteristics of residues in proteins. J. Biomol. Struct. & Dynamics. (1993), v. 11, N 6, p. 483-507. 12. Efremov R.G., Vergoten G. The hydrophobic nature of membrane-spanning -helices as revealed by Monte Carlo simulations and molecular hydrophobicity potential analysis. J. Physical Chemistry. (1995). v. 99, N 26, p. 10658-10666. 13. Golovanov A.P., Efremov R.G., Jaravine V.A., Vergoten G., Arseniev A.S. Amino acid residue: is it structural or functional? FEBS Lett. (1995), v. 375, p. 162-166. 14. Efremov R.G., Vergoten G. Hydrophobic organization of membrane helix bundle in bacteriorhodopsin. J. Protein Chemistry. (1996). v. 15, N 1, p. 63-76. 15. Efremov R.G., Vergoten G. Recognition of transmembrane -helical segments with environmental profiles. Protein Engineering. (1996). v. 9, N 3, p. 253-263. 16. Nolde D.E., Arseniev A.S., Vergoten G., Efremov R.G. Atomic solvation parameters for protein in a membrane environment. Application to transmembrane -helices. J. Biomol. Struct. & Dynamics. (1997). v. 15, N 1, p. 1-18. 17. Efremov R.G., Nolde D.E., Vergoten G., Arseniev A.S. Peptides in membranes: assessment of the effects of environment via simulations with implicit solvation model. Theor. Chem. Acc. (1999). v. 101, N 1-3, p. 170-174. 18. Efremov R.G., Vergoten G., Arseniev A.S. A new "hydrophobic template" method detects segments forming transmembrane alpha-helical bundles in ion channels. Theor. Chem. Acc. (1999). v. 101, N 1-3, p. 73-76. 19. Efremov, R.G., Nolde, D.E., Vergoten G., Arseniev, A.S. A solvent model for simulations of peptides in bilayers. I. Membrane-promoting -helix formation. Biophys. J. (1999). v. 76, N 5, p. 2448-2459. 20. Efremov, R.G., Nolde, D.E., Vergoten G., Arseniev, A.S. A solvent model for simulations of peptides in bilayers. II. Membrane-spanning alpha-helices. Biophys. J. (1999). v. 76, N 5, p. 2460-2471. 21. Efremov R.G., Truong M.-J., Darcissac E.C.A., Zeng J., Grau O., Vergoten G., Debard C., Capron A., Bahr G.M. Human chemokine receptors CCR5, CCR3, and CCR2B share common polarity motif in the first extracellular loop with other human GPCRs: implications for HIV-1 coreceptor function. Eur. J. Biochem. (1999). 263, 746-756. 22. Efremov R.G., Nolde D.E., Volynsky P.E., Chernyavsky A.A., Dubovsky P.V., Arseniev A.S. Factors important for fusogenic activity of peptides: molecular modeling study of analogs of fusion peptide of influenza virus hemagglutinin. FEBS Lett. (1999). 462, 205-210. 23. Нольде Д.Е., Волынский П.Е., Арсеньев А.С., Ефремов Р.Г. Моделирование пептидов и белков в мембранном окружении. I. Модель сольватации, имитирующая липидный бислой. // Биоорганическая химия. (2000). 26, 131-142. 24. Волынский П.Е., Нольде Д.Е., Арсеньев А.С., Ефремов Р.Г. Моделирование пептидов и белков в мембранном окружении. II. Структурные и энергетические аспекты гликофорина А в бислое. // Биоорганическая химия. (2000). 26, 163-172. 25. Efremov R.G., Nolde D.E., Volynsky P.E., Arseniev A.S. Modeling of peptides in implicit membrane-mimetic media. Molecular Simulation (2000). 24, 275-291. 26. Efremov R.G., Volynsky P.E., Nolde D.E., Arseniev A.S. Implicit two-phase solvation model as a tool to assess conformation and energetics of proteins in membrane-mimic media. Theor. Chem. Acc. (2001). 106, 48-54 27. Efremov R.G., Volynsky P.E., Dauchez M.A.M., Nolde D.E., Arseniev A.S., Alix A.J.P. Assessment of conformation and energetics of the N-terminal part of elafin via computer simulations. Theor. Chem. Acc. (2001). 106, 55-61. 28. Efremov R.G., Volynsky P.E., Nolde D.E., Dubovskii P.V., Arseniev A.S. Interaction of cardiotoxins with membranes: a molecular modeling study. Biophys. J. (2002). v. 83 (1), 144-153. 29. Efremov R.G., Volynsky P.E., Nolde D.E., van Dalen A., de Kruijff B., Arseniev A.S. Monte Carlo simulations of voltage-driven translocation of a signal sequence. FEBS Lett. (2002). 526, 97-100. 30. Lutsenko S., Efremov R.G., Tsivkovskii R., Walker J.M. Human copper-transporting ATPase ATP7B (the Wilson's disease protein): Biochemical properties and regulation. J. Bioenerg. Biomemb. (2002). 34, 351-362. 31. Tsivkovskii R., Efremov R.G., Lutsenko S. The Role of Invariant His1069 in Folding and Function of the Wilson's disease Protein, the Human Copper-transporting ATPase ATP7B. J. Biol. Chem. (2003). 278, 13302-13308. 32. Efremov R.G., Nolde D.E., Konshina A.G., Syrtcev N.P., Arseniev A.S. Peptides and proteins in membranes: what can we learn via computer simulations? Curr. Med. Chem. (2004). 11, 763. 33. Kosinsky Yu.A., Volynsky P.E., Lagant P., Vergoten G., Suzuki E., Arseniev A.S., Efremov R.G. (2004) Development of the Force Field Parameters for Phosphoimidazole and Phosphohistidine. J. Comput. Chem. (2004). 25, 1313-1321. 34. Efremov, R. G., Kosinsky Yu.A., Nolde D.E., Tsivkovskii, R., Arseniev A.S., Lutsenko, S. Molecular Modeling of the Nucleotide-Binding Domain of the Wilson' Disease Protein: Location of the ATP-binding Site, Domain Dynamics, and Potential Effects of the Major Disease Mutations. Biochemical J. (2004). 382, accepted.

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