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Hierarchical structure investigations of biogenic ferrihydrite samples / M. Balasoiu [et al.] // Rom. J. Phys. - 2010. - Vol. 55, Is. 7-8. - P. 782-789. - Cited References: 21. - The work was accomplished with the financial support of Grant 224/11.04.2008 of Romanian Governmental Plenipotentiary at JINR. . - ISSN 1221-146X

РУБ Physics, Multidisciplinary
Рубрики:
ELECTRON NANODIFFRACTION
   6-LINE FERRIHYDRITE
   SYNTHETIC 2-LINE
   FERROFLUIDS
Кл.слова (ненормированные):
ferrihydrite nanoparticles -- Klebsiella oxytoca bacteria -- optical microscopy -- SEM -- SAXS
Аннотация: Results of observation and preliminary analysis on morphology and structure of ferrihydrite particles produced in vivo by Klebsiella oxytoca bacteria are presented. In particular, optical microscopy, scanning electron microscopy and small angle X-ray scattering in accordance with one another point out the fractal structure of the biomineral particle surface. The effect of the bacteria age (the duration of growth) on the fractal dimension is established and characterized.

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Держатели документа:
[Balasoiu, M.] Horia Hulubei Natl Inst Phys & Nucl Engn, Bucharest, Romania
[Stolyar, S. V.
Iskhakov, R. S.
Ishchenko, L. A.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Raikher, Yu. L.] RAS, Ural Branch, Inst Continuum Media Mech, Perm 614013, Russia
[Balasoiu, M.
Kuklin, A. I.
Orelovich, O. L.
Kovalev, Yu. S.
Arzumanian, G. M.] Joint Inst Nucl Res, Dubna 141980, Russia
[Kurkin, T. S.] RAS, Inst Synthet Polymer Mat, Moscow 117393, Russia
[Stolyar, S. V.
Iskhakov, R. S.] RAS, Siberian Branch, Inst Phys, Krasnoyarsk 660036, Russia
ИФ СО РАН

Доп.точки доступа:
Balasoiu, M.; Stolyar, S. V.; Столяр, Сергей Викторович; Iskhakov, R. S.; Исхаков, Рауф Садыкович; Ishchenko, L. A.; Raikher, Y. L.; Kuklin, A. I.; Orelovich, O. L.; Kovalev, Y. S.; Kurkin, T. S.; Arzumanian, G. M.
}
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Molecular design of aptamer structure by computer simulations / I. Shchugoreva [et al.] // VI Euro-Asian Symposium "Trends in MAGnetism" (EASTMAG-2016) : abstracts / ed.: O. A. Maksimova, R. D. Ivantsov. - Krasnoyarsk : KIP RAS SB, 2016. - Ст. P12.2. - P. 558. - We acknowledge the grant by the Ministry of Education and Science (Agreement No.14.607.21.0104 (RFMEFI60714X0104)) for the financial support of this work . - ISBN 978-5-904603-06-9
Кл.слова (ненормированные):
DNA -- SELEX -- SAXS -- QM/MM -- aptamer -- G-quartets

Доп.точки доступа:
Shchugoreva, I.; Moryachkov, R.; Zabluda, V. N.; Заблуда, Владимир Николаевич; Sokolov, A. E.; Соколов, Алексей Эдуардович; Spiridonova, V. A.; Спиридонова В. А.; Gruzinov, A.; Zamay, A. S.; Замай, Анна Сергеевна; Veprincev, D.; Zamay, G. S.; Замай Г. С.; Tomilin, F. N.; Томилин, Феликс Николаевич; Ovchinnikov, S. G.; Овчинников, Сергей Геннадьевич; Euro-Asian Symposium "Trends in MAGnetism"(6 ; 2016 ; Aug. ; 15-19 ; Krasnoyarsk); "Trends in MAGnetism", Euro-Asian Symposium(6 ; 2016 ; Aug. ; 15-19 ; Krasnoyarsk); Институт физики им. Л.В. Киренского Сибирского отделения РАН

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Small angle X-ray scattering on RE31 aptamer / R. Moryachkov [et al.] // VI Euro-Asian Symposium "Trends in MAGnetism" (EASTMAG-2016) : abstracts / ed.: O. A. Maksimova, R. D. Ivantsov. - Krasnoyarsk : KIP RAS SB, 2016. - Ст. P12.3. - P. 559-560. - References: 3. - The work was supported by Ministry of education and science of Russia (Agreement No.14.607.21.0104 (RFMEFI60714X0104)) . - ISBN 978-5-904603-06-9
Кл.слова (ненормированные):
SAXS -- aptamer -- biomolecules structure -- ATSAS -- DAMMIN

Доп.точки доступа:
Moryachkov, R.; Spiridonova, V. A.; Спиридонова В. А.; Zabluda, V. N.; Заблуда, Владимир Николаевич; Peters, G.; Петерс Георгий; Sokolov, A. E.; Соколов, Алексей Эдуардович; Euro-Asian Symposium "Trends in MAGnetism"(6 ; 2016 ; Aug. ; 15-19 ; Krasnoyarsk); "Trends in MAGnetism", Euro-Asian Symposium(6 ; 2016 ; Aug. ; 15-19 ; Krasnoyarsk); Институт физики им. Л.В. Киренского Сибирского отделения РАН

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Characterization of biogenic ferrihydrite nanoparticles by means of SAXS, SRD and IBA methods / M. Balasoiu [et al.] // J. Phys.: Conf. Ser. - 2018. - Vol. 994: 3rd International School and Workshop on Complex and Magnetic Soft Matter Systems: Structure and Physico - Mechanical Properties, CMSMS 2017 (28 - 30 June 2017), Is. 1. - Ст. 012012, DOI 10.1088/1742-6596/994/1/012012. - Cited References: 20. - The work was accomplished in the frame of IFIN-HH User Beam schedule at the 3 MV Tandetron accelerator and partially was supported by the Joint Institute for Nuclear Research (JINR) Dubna Theme No. 04-4-1121-2015/2017, RO-JINR Projects Nos. 95/15.02.2016 and 96/15.02.2016, items 77, 82; Nos. 219/10.04.2017 and 220/10.04.2017 item 38; RFBR and Krasnoyarsk region Project No. 17-43-240527. Support by the Special Program for Siberian Federal University of the Ministry of Education and Science of the Russian Federation is acknowledged.
Кл.слова (ненормированные):
Bacteria -- Data handling -- Ion beams -- Mechanical properties -- Nanoparticles -- Synchrotron radiation
Аннотация: Investigations of biogenic ferrihydrite nanoparticles produced by bacteria Klebsiella oxytoca by applying small angle X-ray scattering, synchrotron radiation diffraction and ion beam analysis methods are reviewed. Different experimental data processing methods are used and analyzed.

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Держатели документа:
Joint Institute for Nuclear Research, Moscow Region, Dubna, Russian Federation
Horia Hulubei National Institute for Physics and Nuclear Engineering, Bucharest, Romania
Siberian Federal University, Krasnoyarsk, Russian Federation
Kirensky Institute of Physics, Siberian Branch of RAS, Krasnoyarsk, Russian Federation
Extreme Light Intrastructure Nuclear Physics (ELI-NP), Bucharest, Romania
Institute of Synthetic Polymer Materials RAS, Moscow, Russian Federation

Доп.точки доступа:
Balasoiu, M.; Kichanov, S.; Pantelica, A.; Pantelica, D.; Stolyar, S. V.; Столяр, Сергей Викторович; Iskhakov, R. S.; Исхаков, Рауф Садыкович; Aranghel, D.; Ionescu, P.; Badita, C. R.; Kurkin, S.; Orelovich, O.; Tiutiunikov, S.; International School and Workshop on Complex and Magnetic Soft Matter Systems: Structure and Physico - Mechanical Properties(3 ; 2017 ; 28 - 30 June ; Dubna, Russian Federation)
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Moryachkov, R. V.
Structure approaches to study of DNA aptamers in solution / R. V. Moryachkov, P. A. Nikolaeva, V. A. Spiridonova // Sib. Med. Rev. - 2021. - Vol. 2021, Is. 2. - P. 76-78 ; Сиб. мед. обозрение, DOI 10.20333/2500136-2021-2-76-78. - Cited References: 5. - The reported study was funded by RFBR, project number 19-32-90266 . - ISSN 1819-9496
Кл.слова (ненормированные):
biomolecules in solution -- tertiary structure -- small-angle X-ray scattering (SAXS) -- structure analysis
Аннотация: The high potential of aptamers – specific molecular agents based on short single-stranded nucleic acids – makes high demands on the molecules under development for the efficiency of interaction with target biomolecules. In this work, approaches are considered for studying the spatial structure of DNA aptamers in solution using various complementary methods, which make it possible to obtain a more complete picture of the formation of the structure and conformational changes, to track the interaction with the target protein, the tendency to oligomerization, and to characterize the spatial structure of both individual molecules and complexes.

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Держатели документа:
Federal Research Center “Krasnoyarsk Science Center SB RAS”, 50, Akademgorodok St., Krasnoyarsk, 660036, Russian Federation
Kirensky Institute of Physics, Bld. 38, 50, Akademgorodok St., Krasnoyarsk, 660036, Russian Federation
Lomonosov Moscow State University, 1, Leninskie Gory St., Moscow, 119992, Russian Federation
A. N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Bld. 40, 1, Leninskie Gory St., Moscow, 119992, Russian Federation

Доп.точки доступа:
Nikolaeva, P. A.; Spiridonova, V. A.; Морячков, Роман Владимирович

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Applying joint theoretical experimental research to aptamer modeling / I. A. Shchugoreva, P. V. Artyushenko, F. N. Tomilin [et al.] // Sib. Med. Rev. - 2021. - Vol. 2021, Is. 2. - P. 105-106 ; Сиб. мед. обозрение, DOI 10.20333/2500136-2021-2-105-106. - Cited References: 4 . - ISSN 1819-9496
Кл.слова (ненормированные):
LC-18 -- DNA aptamer -- lung adenocarcinoma -- SAXS -- DFTB3
Аннотация: The aim of the research. In this work we studied the structure of LC-18 DNA aptamer, which exhibits specific binding to lung adenocarcinoma cells. Obtain-ing the 3D structure of the aptamer is necessary for understanding the mechanism of binding of the aptamer to the target. Therefore, the aim of the research was modeling of the LC-18 aptamer spatial structure using combination of theoretical methods: DNA folding tools, quantum-chemical calculations and molecular dynamic simulations. Material and methods. The secondary structure of the LC-18 aptamer was predicted by using OligoAnalyzer and MFold online software under the conditions typical small-angle X-ray scattering (SAXS) experiment. The molecular modeling of the aptamer was carried out using the Avogadro program. For prediction of the structure two computational methods were used: quantum-mechanical method with third-order density-functional tight-binding (DFTB3) and molecular dynamics (MD) with force fields. Results. In this paper it was shown that molecular simulations can predict structures from the SAXS experiments. OligoAnalyzer and MFold web servers have been used to generate a set of several likely models. However, more accurate calculations have showed that these models do not predict the relative importance of isomers. Meanwhile, application of quantum-chemical and molecular dynamics calculations have showed reliable molecular structures which have a small deviations from the experimental SAXS curves. Conclusion. This study demonstrates the approach for modeling 3D structures of DNA-aptamers in solution using both experimental and theoretical meth-ods. It could be very helpful in designing more efficient aptamers based on results obtained from molecular simulations.

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Держатели документа:
Laboratory for Digital Controlled Drugs and Theranostics, Federal Research Center "Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Department of Chemistry, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Laboratory of Physics of Magnetic Phenomena, Kirensky Institute of Physics, Krasnoyarsk, 660012, Russian Federation
Nanoscience Center and Department of Chemistry, University of Jyvaskyla, Jyvaskyla, 40014, Finland
Department of Chemistry, Lomonosov Moscow State University, Moscow, 119234, Russian Federation

Доп.точки доступа:
Shchugoreva, I. A.; Artyushenko, P. V.; Tomilin, F. N.; Morozov, D. I.; Mironov, V. A.; Moryachkov, R. V.; Морячков, Роман Владимирович; Kichkailo, A. S.

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    The role of SAXS and molecular simulations in 3D structure elucidation of a DNA aptamer against lung cancer / D. Morozov, V. Mironov, R. V. Moryachkov [et al.] // Mol. Ther. Nucl. Acids. - 2021. - Vol. 25. - P. 316-327, DOI 10.1016/j.omtn.2021.07.015. - Cited References: 84. - The research was performed using equipment of the Shared Core Facilities of Molecular and Cell Technologies at Krasnoyarsk State Medical University. The synchrotron SAXS data were collected at beamline P12 operated by EMBL Hamburg at the PETRA III storage ring (DESY, Hamburg, Germany). A.S.K. is grateful to Aptamerlab LLC for the assistance in aptamer design and 3D structure analyses. We thank Ivan Lapin for his help with microscopic analyses. Microscopic analyses using Carl Zeiss LSM 800 were carried out at the Center for Bioassay, Nanotechnology and Nanomaterials Safety (“Biotest-Nano”) (Multiple-Access Center, Tomsk State University, Tomsk, Russia). D.M. also thanks the CSC-IT Center in Espoo, Finland, for providing computational resources. The study was supported by a grant from the Russian Science Foundation (project number 21-73-20240) for A.S.K. R.V.M aknowledges Russian Foundation for Basic Research (project number 19-32-90266) for funding. D.G.F. acknowledges financial support by JSPS KAKENHI, grant number 19H02682. D.S.M. acknowledges financial support by BMBF grant number 16QK10A (SAS-BSOFT). Y.A.’s work at Argonne National Laboratory was supported by the US Department of Energy, Office of Science, under contract DE-AC02-06CH11357. D.M. received funding as a part of BioExcel CoE (https://bioexcel.eu/), a project funded by the European Union contracts H2020-INFRAEDI-02-2018-823830 and H2020-EINFRA-2015-1-675728. V.M. thanks Russian Foundation for Basic Research (project number 19-03-00043) for funding . - ISSN 2162-2531
   Перевод заглавия: Роль малоуглового рентгеновского рассеяния и молекулярного моделирования в выснении трёхмерной структуры ДНК аптамера против рака лёгкого
Кл.слова (ненормированные):
aptamer -- oligonucleotide -- tertiary structure -- spatial structure -- lung adenocarcinoma -- small-angle X-ray scattering -- SAXS -- molecular dynamics -- fragment molecular orbital -- molecular simulations
Аннотация: Aptamers are short, single-stranded DNA or RNA oligonucleotide molecules that function as synthetic analogs of antibodies and bind to a target molecule with high specificity. Aptamer affinity entirely depends on its tertiary structure and charge distribution. Therefore, length and structure optimization are essential for increasing aptamer specificity and affinity. Here, we present a general optimization procedure for finding the most populated atomistic structures of DNA aptamers. Based on the existed aptamer LC-18 for lung adenocarcinoma, a new truncated LC-18 (LC-18t) aptamer LC-18t was developed. A three-dimensional (3D) shape of LC-18t was reported based on small-angle X-ray scattering (SAXS) experiments and molecular modeling by fragment molecular orbital or molecular dynamic methods. Molecular simulations revealed an ensemble of possible aptamer conformations in solution that were in close agreement with measured SAXS data. The aptamer LC-18t had stronger binding to cancerous cells in lung tumor tissues and shared the binding site with the original larger aptamer. The suggested approach reveals 3D shapes of aptamers and helps in designing better affinity probes.

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Держатели документа:
Nanoscience Center and Department of Chemistry, University of Jyvaskyla, P.O. Box 35, Jyvaskyla, 40014, Finland
Department of Chemistry, Lomonosov Moscow State University, Moscow, Russian Federation
Laboratory of Physics of Magnetic Phenomena, Kirensky Institute of Physics, 50/38 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Laboratory for Digital Controlled Drugs and Theranostics, Federal Research Center “Krasnoyarsk Science Center SB RAS,” 50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Krasnoyarsk State Medical University, 1 Partizana Zheleznyaka, Krasnoyarsk, 660022, Russian Federation
Department of Chemistry, Siberian Federal University, 79 Svobodny pr., Krasnoyarsk, 660041, Russian Federation
European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, Hamburg, 22603, Germany
Department of Chemistry and Biomolecular Sciences, University of Ottawa, 10 Marie-Curie, Ottawa, ON K1N 6N5, Canada
Research Center for Computational Design of Advanced Functional Materials, National Institute of Advanced Industrial Science and Technology, Tsukuba, 305-8568, Japan
Computational Science Division, Argonne National Laboratory, Lemont, IL, United States

Доп.точки доступа:
Morozov, D.; Mironov, V.; Moryachkov, R. V.; Морячков, Роман Владимирович; Shchugoreva, I. A.; Artyushenko, P. V.; Zamay, G. S.; Kolovskaya, O. S.; Zamay, T. N.; Krat, A. V.; Molodenskiy, D. S.; Zabluda, V. N.; Заблуда, Владимир Николаевич; Veprintsev, D. V.; Sokolov, A. Е.; Соколов, Алексей Эдуардович; Zukov, R. A.; Berezovski, M. V.; Tomilin, F. N.; Томилин, Феликс Николаевич; Fedorov, D. G.; Alexeev, Y.; Kichkailo, A. S.
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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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