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Peculiarities of the time evolution of magnetoresistance of granular HTSC in a constant applied magnetic field / D. A. Balaev [et al.] // Solid State Commun. - 2008. - Vol. 147, Is. 7-8. - P. 284-287, DOI 10.1016/j.ssc.2008.05.044. - Cited References: 17. - This work was Supported by program "Quantum macrophysics" No. 3.4 of RAS and integration project No. 3.4 of SB RAS and in part by KSF, grant 18G011. D.A.B. and A.A.D. acknowledge the Russian Science Support Foundation. . - ISSN 0038-1098

РУБ Physics, Condensed Matter
Рубрики:
CRITICAL-STATE
   SUPERCONDUCTORS
   COMPOSITES
   HYSTERESIS
   RESISTANCE
Кл.слова (ненормированные):
superconductors -- flux pinning and creep -- tunneling -- Superconductors -- Flux pinning and creep -- Tunneling -- Agricultural products -- Carbon fiber reinforced plastics -- Copper oxides -- Electric conductivity -- Electric resistance -- Evolutionary algorithms -- Ferromagnetism -- Galvanomagnetic effects -- Grain (agricultural product) -- Health -- Hysteresis -- Magnetic devices -- Magnetic field effects -- Magnetic field measurement -- Magnetic fields -- Magnetic materials -- Magnetoelectronics -- Magnetoresistance -- Semiconductor metal boundaries -- Superconducting magnets -- Superconductivity -- Yttrium barium copper oxides -- p ,p ,t measurements -- Applied (CO) -- Applied magnetic fields -- Constant magnetic field (CMF) -- Elsevier (CO) -- Evolution (CO) -- External fields -- Field induced -- Flux creep -- Hysteretic behavior -- Josephson couplings -- Low magnetic fields -- Magnetic (CE) -- Poly crystalline -- Superconducting grains -- Time evolutions -- time relaxation -- Magnetism
Аннотация: The time evolution of the magnetoresistance of bulk YBCO + CuO composites at T = 4.2 K in constant applied magnetic fields was studied to clarify the mechanism of hysteretic behavior of magnetoresistance R(H) of granular HTSC. The composites represent "model" granular HTSC with weakened Josephson coupling between superconducting (YBCO) crystallites. It was found for the first time that on the ascending branch of R(H) dependence, the resistance at H = const decreased with time while on the descending branch, the resistance increased with time in ail applied constant magnetic field. In the range of low magnetic fields (below the minimum point of the descending branch of the R(H) dependence), the resistance at H const decreased again. Similar measurements performed oil pure polycrystalline YBCO at T = 77.4 K have shown that the behavior of evolution of resistance with time is similar to that observed for the composite. This proves the peculiarity of time evolution of maignetoresistance to be a common feature of granular HTSCs. The behavior revealed is well described by the model Of granular HTSC, where the intergrain media is in an effective magnetic field which is the superposition of the external field and the field induced by superconducting grains. The time evolution of resistance reflects the time relaxation of magnetization of HTSC grains due to the intragrain flux Creep Processes. (C) 2008 Elsevier Ltd. All rights reserved.

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Держатели документа:
[Balaev, D. A.
Dubrovskiy, A. A.
Shaykhutdinov, K. A.
Popkov, S. I.
Petrov, M. I.] LV Kirenskii Inst Phys, Krasnoyarsk 660036, Russia
ИФ СО РАН
Kirensky Institute of Physics, 660036 Krasnoyarsk, Russian Federation

Доп.точки доступа:
Balaev, D. A.; Балаев, Дмитрий Александрович; Dubrovskiy, A. A.; Дубровский, Андрей Александрович; Shaykhutdinov, K. A.; Шайхутдинов, Кирилл Александрович; Popkov, S. I.; Попков, Сергей Иванович; Petrov, M. I.; Петров, Михаил Иванович
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Structure- and interaction-based design of anti-SARS-CoV-2 Aptamers / V. Mironov, I. A. Shchugoreva, P. V. Artyushenko [et al.] // Chem. - Eur. J. - 2022. - Vol. 28, Is. 12. - Ст. e202104481, DOI 10.1002/chem.202104481. - Cited References: 85. - The authors are grateful to JCSS Joint Super Computer Center of the Russian Academy of Sciences – Branch of Federal State Institution “Scientific Research Institute for System Analysis of the Russian Academy of Sciences” for providing supercomputers for computer simulations. The authors thank the RSC Group (www.rscgroup.ru) and personally Mr. Oleg Gorbachev for the constant support and establishment of “The Good Hope Net Project” (www.thegoodhope.net) multifunctional non-profit anti-CoVID research project. The authors also thank the Helicon Company (www.helicon.ru) and personally Olesya Kucenko, Alexander Kolobov, Leonid Klimov for instrumental support and help with conducting fluorescence polarization assays, which were performed on a demo instrument Clariostar Plus microplate reader (BMG LABTECH, Germany). We thank Dr. Yong-Zhen Zhang for providing the genome sequence of 2019-nCoV and Dr. Xinquan Wang for providing the crystal structure of the binding domain of the SARS-2 Spike protein. The authors are grateful to Aptamerlab LCC financial support (www.aptamerlab.com). Y.A.’s work at Argonne National Laboratory was supported by the U.S. Department of Energy, Office of Science, under contract DE-AC02-06CH11357. The work of D.M. and G.G. has been done as part of the BioExcel CoE (www.bioexcel.eu), a project funded by the European Union contracts H2020-INFRAEDI-02-2018-823830 and H2020-EINFRA-2015-1-675728. D.M. and G.G. also thank the CSC-IT center in Espoo, Finland, as well as PRACE for awarding access to resource Curie-Rome based in France at GENCI. V.M. thanks Russian Foundation for Basic Research (project number 19-03-00043). A.B.’s and N.K.’s work was supported by the Ministry of Science and Higher Education of Russian Federation (state assignment of the Research Center of Biotechnology RAS). V. deF. G.C., N.B and G.O. are grateful to FISR2020 _00177 Shield, Italian Ministry of Education and Research, for funding. GC is grateful to the European Union's Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement: cONCReTE 872391; PRISAR2 872860. Use of the 13 A BioSAXS beamtime at the Taiwan Photon Source is acknowledged. The work of M.V.B was funded by the Canadian Institutes of Health Research grant OV1-170353. SAXS measurements and PIEDA analyses were funded by the Russian Science Foundation (project No 21-73-20240 for A.S.K.) . - ISSN 0947-6539. - ISSN 1521-3765

РУБ Chemistry, Multidisciplinary
Рубрики:
BIOLOGICAL MACROMOLECULES
   SOLUTION SCATTERING
   BINDING
   SPIKE
Кл.слова (ненормированные):
aptamers -- fragment molecular orbitals method -- molecular dynamics -- SARS-CoV-2 -- SAXS
Аннотация: Aptamer selection against novel infections is a complicated and time-consuming approach. Synergy can be achieved by using computational methods together with experimental procedures. This study aims to develop a reliable methodology for a rational aptamer in silico et vitro design. The new approach combines multiple steps: (1) Molecular design, based on screening in a DNA aptamer library and directed mutagenesis to fit the protein tertiary structure; (2) 3D molecular modeling of the target; (3) Molecular docking of an aptamer with the protein; (4) Molecular dynamics (MD) simulations of the complexes; (5) Quantum-mechanical (QM) evaluation of the interactions between aptamer and target with further analysis; (6) Experimental verification at each cycle for structure and binding affinity by using small-angle X-ray scattering, cytometry, and fluorescence polarization. By using a new iterative design procedure, structure- and interaction-based drug design (SIBDD), a highly specific aptamer to the receptor-binding domain of the SARS-CoV-2 spike protein, was developed and validated. The SIBDD approach enhances speed of the high-affinity aptamers development from scratch, using a target protein structure. The method could be used to improve existing aptamers for stronger binding. This approach brings to an advanced level the development of novel affinity probes, functional nucleic acids. It offers a blueprint for the straightforward design of targeting molecules for new pathogen agents and emerging variants.

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Держатели документа:
Lomonosov Moscow State Univ, Dept Chem, Moscow 119991, Russia.
Kyungpook Natl Univ, Dept Chem, Daegu 702701, South Korea.
Fed Res Ctr KSC SB RAS, Lab Digital Controlled Drugs & Theranost, Krasnoyarsk 660036, Russia.
Natl Tsing Hua Univ, Dept Chem Engn, Hsinchu 30013, Taiwan.
Siberian Fed Univ, Sch Nonferrous Met & Mat Sci, Krasnoyarsk 660041, Russia.
IRCCS Neuromed Ist Neurol Mediterraneo Pozzilli, Via Atinense 18, I-86077 Pozzilli, Italy.
Krasnoyarsk State Med Univ, Lab Biomol & Med Technol, Krasnoyarsk 660022, Russia.
Univ Jyvaskyla, Nanosci Ctr, Jyvaskyla 40014, Finland.
Univ Jyvaskyla, Dept Chem, Jyvaskyla 40014, Finland.
Univ Naples Federico II, Dept Pharm, I-80138 Naples, Italy.
Univ Naples Federico II, Dept Mol Med & Med Biotechnol, I-80131 Naples, Italy.
Kirensky Inst Phys, Lab Phys Magnet Phenomena, Krasnoyarsk 660012, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.
Xiamen Univ, Coll Chem & Chem Engn, Dept Chem Biol, Xiamen 361005, Peoples R China.
State Res Ctr Virol & Biotechnol Vector, Koltsov 630559, Russia.
NRC Kurchatov Inst, Moscow 117259, Russia.
Russian Acad Sci, Siberian Branch, Inst Chem Biol & Fundamental Med, Novosibirsk 630090, Russia.
Russian Acad Sci, Res Ctr Biotechnol, AN Bach Inst Biochem, Lab Immunobiochem, Moscow 119071, Russia.
Tomsk State Univ, Lab Adv Mat & Technol, Tomsk 634050, Russia.
Altai State Univ, Barnaul 656049, Russia.
Fed Res Ctr KSC SB RAS, Dept Mol Elect, Krasnoyarsk 660036, Russia.
Krasnoyarsk State Med Univ, Dept Infect Dis & Epidemiol, Krasnoyarsk 660022, Russia.
Natl Pingtung Univ, Dept Appl Chem, Pingtung 900391, Taiwan.
Natl Synchrotron Radiat Res Ctr, Hsinchu Sci Pk, Hsinchu 30076, Taiwan.
Res Natl Council CNR, Inst Genet & Biomed Res IRGB, I-09042 Milan, Italy.
Shanghai Jiao Tong Univ, Sch Med, Renji Hosp, Inst Mol Med, Shanghai 200127, Peoples R China.
Natl Inst Adv Ind Sci & Technol, Res Ctr Computat Design Adv Funct Mat, Tsukuba, Ibaraki 3058560, Japan.
Hunan Univ, Coll Chem & Chem Engn, Changsha 410082, Hunan, Peoples R China.
Argonne Natl Lab, Computat Sci Div, Lemont, IL 60439 USA.
Dept Chem & Biomol Sci, Ottawa, ON K1N 6N5, Canada.

Доп.точки доступа:
Mironov, Vladimir; Shchugoreva, I. A.; Artyushenko, P. V.; Артюшенко, Полина Владимировна; Morozov, D. I.; Морозов, Дмитрий И.; Borbone, N.; Oliviero, G.; Zamay, T. N.; Замай, Т. Н.; Moryachkov, R. V.; Морячков, Роман Владимирович; Kolovskaya, .; Коловская О. С.; Lukyanenko, K. A.; Лукьяненко Кирилл А.; Song, Y. L.; Merkuleva, I. A.; Zabluda, V. N.; Заблуда, Владимир Николаевич; Peters, G.; Koroleva, L. S.; Veprintsev, D. V.; Glazyrin, Y. E.; Volosnikova, E. A.; Belenkaya, S. V.; Esina, T. I.; Isaeva, A. A.; Nesmeyanova, .; Shanshin, D. V.; Berlina, A. N.; Komova, N. S.; Svetlichnyi, V. A.; Silnikov, V. N.; Shcherbakov, D. N.; Zamay, G. S.; Замай, Галина Сергеевна; Zamay, S. S.; Замай, С. С.; Smolyarova, T. E.; Смолярова, Татьяна Евгеньевна; Tikhonova, E. P.; Chen, U. S.; Jeng, G.; Condorelli, V.; Franciscis, G.; Groenhof, C. Y.; Yang, A. A.; Moskovsky, D. G.; Fedorov, F. N.; Tomilin, F. N.; Томилин, Феликс Николаевич; Tan, Y.; Alexeev, M. V.; Berezovski, A. S.; Kichkailo, A.S.; Aptamerlab LCC; U.S. Department of Energy, Office of ScienceUnited States Department of Energy (DOE) [DE-AC02-06CH11357]; European UnionEuropean Commission [H2020-INFRAEDI-02-2018-823830, H2020-EINFRA-2015-1-675728, 872391, PRISAR2 872860]; CSC-IT center in Espoo, Finland; PRACE; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [19-03-00043]; Ministry of Science and Higher Education of Russian Federation (state assignment of the Research Center of Biotechnology RAS); Italian Ministry of Education and ResearchMinistry of Education, Universities and Research (MIUR) [FISR2020 _00177]; Canadian Institutes of Health ResearchCanadian Institutes of Health Research (CIHR) [OV1-170353]; Russian Science FoundationRussian Science Foundation (RSF) [21-73-20240]
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