Публикации
| 1. | Tyuryaeva, I. I., Lyublinskaya, O. G., Podkorytov, I. S. & Skrynnikov, N. R.: Origin of anti-tumor activity of the cysteine-containing GO peptides and further optimization of their cytotoxic properties. Scientific Reports 7, 40217 (2017). |
DOI |
| 2. | Solomatina, A. I., Chelushkin, P. S., Krupenya, D. V., Podkorytov, I. S., Artamonova, T. O., Sizov, V. V., Melnikov, A. S., Gurzhiy, V. V., Koshel, E. I., Shcheslavskiy, V. I., Tunik, S. P.: Coordination to Imidazole Ring Switches on Phosphorescence of Platinum Cyclometalated Complexes: The Route to Selective Labeling of Peptides and Proteins via Histidine Residues. Bioconjugate Chem. (2016). |
DOI |
| 3. | Rogacheva, O. N., Izmailov, S. A., Kurauskas, V., Shilova, A., Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., Hessel, A., Woodhouse, J., Mikhailovskii, O., Willbold, D., Colletier, J., Skrynnikov, N. R., Schanda, P.: Dynamics in Protein Crystals: Insights from MD Simulations Complement New Solid-State NMR and X-Ray Data. FEBS Journal 283, 237 (2016). |
DOI |
| 4. | Yuwen, T., Xue, Y., Skrynnikov, N. R.: Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets: 2. The Model of Encounter Complex Involving the Double Mutant of the c-Crk N-SH3 Domain and Peptide Sos. Biochemistry 55 (12), 1784–1800 (2016). |
DOI |
| 5. | Rabdano, S. O., Podkorytov, I. S., Izmailov, S. A., Pivovarova, Y. V., Yakimov, A. P., Yuwen, T., Groves, A., Skrynnikov, N. R.: Loss of Protein Stability due to Formation of Intermolecular Disulfide Bonds under the Effect of Oxidative Stress: Case Study of the RRM2 Domain from Neuropathological Protein TDP-43. Biophysical Journal 110 (3), 210a (2016). |
DOI |
| 6. | Izmailov, S. A., Podkorytov, I. S., Skrynnikov, N. R.: MD Modeling of Oxidative Folding in Peptides and Proteins. Biophysical Journal 110 (3), 644a–645a (2016). |
DOI |
| 7. | Ledovskaya, M. S., Molchanov, A. P., Kostikov, R. R., Panikorovsky, T. L., Gurzhiy, V. V., Ryazantsev, M. N., Boitsov, V. M., Stepakov, A. V.: Anthracene-Fused isoxazolopyrrolo[2,1-A]isoquinolines via an Endocyclic N-Acyliminium Ion Cyclization: A Joint Experimental and Theoretical Study. Tetrahedron 72 (32), 4827–4834 (2016). |
DOI |
| 8. | Struts, A. V., Barmasov, A. V., Brown, M. F.: Spectral Methods for Study of the G-Protein-Coupled Receptor Rhodopsin. II. Magnetic Resonance Methods. Opt. Spectrosc. 120 (2), 286–293 (2016). |
DOI |
| 9. | Xu, X., Struts, A. V., Kumar Giri, A., Molugu, T. R., Guruge, C., Faylough, S., Nascimento, C. L., Nesnas, N., Hruby, V. J., Brown, M. F.: Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation. Biophysical Journal 110 (3), 73a (2016). |
DOI |
| 10. | Struts, A. V., Xu, X., Molugu, T. R., Pitman, M. C., Faylough, S., Guruge, C., Nascimento, C., Nesnas, N., Brown, M. F.: Retinal Chromophore Structure in Meta-II Rhodopsin Revealed by Solid-State 2H NMR and Molecular Modeling. Biophysical Journal 110 (3), 229a–230a (2016). |
DOI |
| 11. | Perera, S. M. D. C., Shrestha, U., Bhowmik, D., Chawla, U., Struts, A. V., Chu, X., Brown, M. F.: Neutron Scattering Reveals Protein Fluctuations in GPCR Activation. Biophysical Journal 110 (3), 228a–229a (2016). |
DOI |
| 12. | Chawla, U., Perera, S. M. D. C., Struts, A. V., Pitman, M. C., Brown, M. F.: Hydration Mediated G-Protein-Coupled Receptor Activation. Biophysical Journal 110 (3), 83a (2016). |
DOI |
| 13. | Smekalova, T. N., Yatsishina, E. B., Garipov, A. S., Pasumanskii, A. E., Ketsko, R. S., Chudin, A. V.: Natural Science Methods in Field Archaeology, with the Case Study of Crimea. Crystallogr. Rep. 61 (4), 533–542 (2016). |
DOI |
| 14. | Shmyreva, A. A., Safdari, M., Furó, I., Dvinskikh, S. V.: NMR Longitudinal Relaxation Enhancement in Metal Halides by Heteronuclear Polarization Exchange during Magic-Angle Spinning. The Journal of Chemical Physics 144 (22), 224201 (2016). |
DOI |
| 15. | Kharkov, B. B., Chizhik, V. I., Dvinskikh, S. V.: Broadband Cross-Polarization-Based Heteronuclear Dipolar Recoupling for Structural and Dynamic NMR Studies of Rigid and Soft Solids. The Journal of Chemical Physics 144 (3), 34201 (2016). |
DOI |
| 16. | Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., Mikhailovskii, O., Willbold, D., Colletier, J.-P., Skrynnikov, N. R., Schanda, P.: Observing the Overall Rocking Motion of a Protein in a Crystal. Nature Communications 6, 8361 (2015). |
DOI |
| 17. | Abrahamsson, C., Nordstierna, L., Nordin, M., Dvinskikh, S. V. & Nydén, M.: Magnetic orientation of nontronite clay in aqueous dispersions and its effect on water diffusion. Journal of Colloid and Interface Science 437, 205–210 (2015). |
DOI |
| 18. | Gerts, E. D., Komolkin, A. V., Burmistrov, V. A., Alexandriysky, V. V. & Dvinskikh, S. V.: Comparative study of local structure of two cyanobiphenyl liquid crystals by molecular dynamics method. The Journal of Chemical Physics 141, 074503 (2014). |
DOI |
| 19. | Kharkov, B. B., Corkery, R. W. & Dvinskikh, S. V.: Phase Transitions and Chain Dynamics of Surfactants Intercalated into the Galleries of Naturally Occurring Clay Mineral Magadiite. Langmuir 30, 7859–7866 (2014). |
DOI |
| 20. | Xue, Y. & Skrynnikov, N. R.: Ensemble MD simulations restrained via crystallographic data: Accurate structure leads to accurate dynamics: Ensemble MD Simulations. Protein Science 23, 488–507 (2014). |
DOI |
| 21. | Yuwen, T. & Skrynnikov, N. R.: CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions. Journal of Biomolecular NMR 58, 175–192 (2014). |
DOI |
| 22. | Xu, X., Struts, A. V. & Brown, M. F.: Generalized Model-Free Analysis of Nuclear Spin Relaxation Experiments. eMagRes, 2014, Vol 3: 275–286. |
DOI |
| 23. | Brown, M. F. & Struts, A. V.: Retinal in Rhodopsin Activation Viewed by Solid-State 2H NMR Spectroscopy. In New Developments in NMR, F. Separovic, and A. Naito, eds. (Cambridge: Royal Society of Chemistry), 320–352 (2014). |
DOI |
| 24. | Kharkov, B. B., Chizhik, V. I. & Dvinskikh, S. V.: Probing Molecular Mobility in Nanostructured Composites by Heteronuclear Dipolar NMR Spectroscopy. The Journal of Physical Chemistry C 118, 28308–28313 (2014). |
DOI |
| 25. | Xue, Y., Yuwen, T., Zhu, F. & Skrynnikov, N. R.: Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets. 1. NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the Peptide Sos. Biochemistry 53, 6473–6495 (2014). |
DOIPDF |