D05.2 Statement on the completion of the publication list

Deeping collaboration on novel biomolecular electronics based on “smart” nanomaterials WIDESPREAD-05- Grant agreement ID: 951887 Call reference: 2020-Twinning Start date: 1st October 2020 Duration: 36 months

Deliverable identification Leading beneficiary: IMBG Related WP: WP5 Planned delivery date: M02 Related period: - Actual delivery date: M02 Dissemination level: PU Delivery status: Submitted

Contributors: Beneficiaries Name(s) Institute of Molecular Biology and Genetics of Sergei Dzyadevych – Yanina Mishchuk NASU Zentrum Fur Soziale Innovation Gmbh Gorazd Weiss

Reviews Version Reviewer Date V0.1 IMBG 22/11/2020

V0.2 ZSI 23/11/2020

IMBG publications in scientific journals reffered in Scopus, Web of Science Core Collection in 2017‐2020

2017………………………………………………………………………………………………………………………2 2018……………………………………………………………………………………………………………………..15 2019……………………………………………………………………………………………………………………..26 2020……………………………………………………………………………………………………………………..38

2017

1. Molecular modeling and molecular Journal of Molecular Graphics A.V. Rayevsky, M. Sharifi, dynamics simulation study of and Modelling ‐ 2017, V. 76. P. M.A. Tukalo archaeal leucyl‐tRNA synthetase in 289‐295. complex with different mischarged http://dx.doi.org/doi:10.1016/j.j tRNA in editing conformation mgm.2017.06.022

2. d(A)3d(T)3 and d(G)3d(C)3 B‐DNA Journal of Molecular Modeling 23 L Gorb, TA Zubatiuk, R mini‐helixes: the DFT/M06‐2x and (10), 289 (2017) Zubatyuk, D Hovorun, J DFT/B97‐D3 comparison of DOI: 10.1007/s00894‐017‐3449‐y Leszczynski geometrical and energetic characteristics 3. Enthalpy‐entropy compensation: Eur Biophys J. 2017 May; Dragan AI, Read CM, Crane‐ the role of solvation 46(4):301‐308. doi: Robinson C. 10.1007/s00249‐016‐1182‐6. https://www.researchgate.net/p ublication/309590885_Enthalpy‐ entropy_compensation_the_role _of_solvation

4. Izatizon, as an izatin‐ International Journal of Bolsunova Ol’ha I., Zaika thiosemicarbazone derivative, has Pharmaceutical Science Invention Leonid A., Potopalsky Anatoliy antiviral, anti‐tumor actions and no ‐2017 ‐V.6. ‐Is.5. – P.7‐9, Impact I., Voznyuk Anna V. side effects factor 1,695, Індія. http://www.ijpsi.org/Papers/Vol6 (5)/B06050709.pdf

5. A QM/QTAIM detailed look at the Journal of Biomolecular Structure Brovarets’ O.O., Voiteshenko, Watson‐Crick↔wobble tautomeric & Dynamics. – 2017. – DOI: I.S, Pérez‐Sánchez H.E., & transformations of the 2‐ 10.1080/07391102.2017.1331864 Hovorun D.M. aminopurine∙pyrimidine mispairs 6. A new mechanism of post‐transfer Journal of Biomolecular Structure Boyarshin K.S., Priss A.E., editing by aminoacyl‐tRNA and Dynamics. – 2017. – V. 35, N Rayevskiy A.V., Ilchenko M.M., synthetases: Catalysis of hydrolytic 3. – P. 669‐682. Dubey I.Ya., Kriklivyi I.A., reaction by bacterial‐type prolyl‐ https://doi.org/10.1080/0739110 Yaremchuk A.D., Tukalo M.A. tRNA synthetase 2.2016.1155171

7. Computational Modeling and Journal Biomol Struct Dyn. 2017 , Kravchuk VO, Savytskyi Molecular Dynamics Simulations of Vol.35, N13, 2772‐2788 . Impact OV, Odynets KO, Mykuliak Mammalian Cytoplasmic Tyrosyl‐ factor 3,123. VV, Kornelyuk AI. tRNA Synthetase and Its Complexes PMID: 27615678 with Substrates. DOI: 10.1080/07391102.2016.12 35512

8. A QM/QTAIM research under the New Journal of Chemistry 41 (15), OO Brovarets’, magnifying glass of the DPT 7232‐7243 (2017) IS Voiteshenko, H Pérez‐ tautomerisation of the wobble DOI:10.1039/c7nj00717e Sánchez, DM Hovorun mispairs involving 2‐aminopurine

9. Physico‐chemical profiles of the Physical Chemistry & Chemical OO Brovarets’, IS Voiteshenko, wobble↔ Watson‐Crick G*∙ 2AP Physics: 20 (1), 623‐636 (2017) DM Hovorun (w)↔ G∙ 2AP (WC) and A∙ 2AP DOI: 10.1039/c7cp05139e (w)↔ A*∙ 2AP (WC) tautomerisations: a QM/QTAIM comprehensive survey. 10 H.H. Repich, V.V. Orysyk, L.G. Synthesis, spectral characterization J. of Inorganic Biochemistry. 168, Palchykovska, S.I. Orysyk, Yu.L. of novel Pd(II), Pt(II) ‐ 98–106 (2017). Zborovskii, O.V. Vasylchenko, coordination compounds based on DOI:10.1016/j.jinorgbio.2016.12. O.V. Storozhuk, A.A. Biluk, V.V. N‐allylthioureas. Cytotoxic 004 Nikulina, L.V. Garmanchuk, V.I. properties and DNA binding ability Pekhnyo, M.V. Vovk 11 Complexes of Oligoribonucleotides Pharmaceuticals. – 2017. – V. 10, Melnichuk N. Semernikova L. with D‐Mannitol Inhibit №3. – P. 71. Tkachuk Z. Hemagglutinin–Glycan Interaction DOI: 10.3390/ph10030071 and Suppress Influenza A Virus H1N1 (A/FM/1/47) Infectivity In Vitro. 12 Structural hypervariability of the Pharmaceuticals (Basel). – 2017. K. Niefind, two human protein kinase CK2 – Vol. 10, № 1. – pii: E9. N. Bischoff, catalytic subunit paralogs revealed https://doi.org/10.3390/ph10010 A.G. Golub, by complex structures with a 009 V.G. Bdzhola, flavonoland a thieno[2,3‐ A.O. Balanda, d]pyrimidine‐based inhibitor A.O. Prykhod’ko, S.M. Yarmoluk 13 Structure and Function of Disease Markers. 2017.vol. 2017, K. Ferenc,T. Pilżys, T. Skrzypek, Enterocyte in Intrauterine Growth Article ID 5238134, 9 pages, 2017. D. Garbicz, M. Marcinkowski, Retarded Pig Neonates. doi:10.1155/2017/5238134" M. Dylewska,P. Gładysz, O. Skorobogatov, Z. Gajewski, E. Grzesiuk, R. Zabielski. 14 Quantification of S‐ International Journal of Mass R. Rodriguez O. Vakulenko S. adenosylmethionine and S‐ Spectrometry 2017, 421: 279‐284. Ralchenko A. Kostiuk adenosylhomocysteine in human doi.org/10.1016/j.ijms.2017.08.0 L. Porublyova I. Konovets placenta and placental explants 02 I. Voronina under homocysteine treatment. M. Obolenskaya, 15 Biofilm formation and cellulose Res Microbiol./ 2017 McLaughlinK., expression by Bordetellaavium Jun;168(5):419‐430. FolorunsoA.O., 197N, the causative agent of DeeniY.Y., bordetellosis in birds and an FosterD., opportunistic respiratory pathogen https://doi.org/10.1016/j.resmic. GorbatiukO., in humans 2017.01.002 HapcaS.M., ImmoorC., KozaA., MohammedI.U., MoshynetsO., RogalskyS., ZawadzkiK., SpiersA.J. 16 DNA loop domain organization in Biochemical and biophysical Afanasieva, K., Chopei, M., nucleoids from cells of different research communications. ‐ 2017. Lozovik, A., Semenova, A., types. – 483(1). – pp.142‐146. Lukash, L., https://doi.org/10.1016/j.bbrc.20 Sivolob, A. 16.12.177 17 Mammalian verprolin CR16 acts as BiochemBiophys Res Kropyvko S. a modulator of ITSN scaffold Commun,V.484, p. 813‐819, 2017 Gryaznova T. proteins association with actin DOI: 10.1016/j.bbrc.2017.01.177 Morderer D. RynditchA.V. 18 Intra‐and interregional The FASEB Journal. – 2017. – Kononenko, O., Galatenko, V., coregulation of opioid genes: 31(5). – pp.1953‐1963. Anderson, M., broken symmetry in spinal circuits. https://doi.org/10.1096/fj.20160 Bazov, I., 1039R Watanabe, H., Zhou, X.W., Iatsyshyna, A., Mityakina, I., Yakovleva, T., Sarkisyan, D., Ponomarev, I. 19 Experimental biology and The canonical way to make a heart: medicine, 2017, 242 issue: 18, Piven O., β‐catenin and plakoglobin in heart page(s): 1735‐1745. Winata C. development and remodeling. https://doi.org/10.1177%2F1535 370217732737 20 Comparative molecular cytogenetic PloS one. – 2017. – Vol.12, N4. – Amosova A.V., Bolsheva N.L., characterization of seven e0175760. Zoshchuk S.A., Twardovska Deschampsia (Poaceae) species https://doi.org/10.1371/journal.p M.O., Yurkevich O.Y., Andreev

one.0175760 I.O., Samatadze T.E., Badaeva E.D., Kunakh V.A., Muravenko O.V. 21 The current state of steppe Biologia. – 2017. – Vol.72, N 1. – Parnikoza I. Yu., Andreev I. O., perennial plants populations: A P.24‐35. Bublyk O. M., Spiridonova K. case study on Iris pumila https://doi.org/10.1515/biolog‐ V., Gołębiewska J., Kubiak M., 2017‐0002 Kuczyńska A., Mystkowska K.,

Olędrzyńska N., Urasińska B., Ślęzak‐Parnikoza A., Górniak M., Wojciechowski K., Didukh Y. P., Kunakh V. A. 22 Peatland ecosystem processes in Scientific Reports. – 2017. – Vol.7. Loisel J., Yu Z., Beilman D. W., the Maritime Antarctic during – 12344. Kaiser K., Parnikoza I. warm climates https://doi.org/10.1038/s41598‐ 017‐12479‐0

23 bayozturkii sp. nov. on Polar Record.‐ 2017:1‐5. Halıcı M. G., Güllü M., the Acarosporamacrocyclos https://doi.org/10.1017/S003224 Parnikoza I . from Antarctica with a key to the 7417000043 known species of the (, Adelococcaceae) 24 Tardigrades from Larus Polar Biology – 2017: 1‐19. Kaczmarek Ł., Parnikoza, I., dominicanus Lichtenstein, 1823 https://doi.org/10.1007/s00300‐ Gawlak M., Esefeld J., Peter nests on the Argentine Islands 017‐2190‐4 H.‐U., Kozeretska I., (maritime Antarctic) Roszkowska M.

25 Analysis of EX5del4232ins268 and Genes and Diseases Volodymyr Pampukha, EX5del955 PAH gene mutations in 2017, V.4(Is.2), P.108‐110. Maryna Nechyporenko, Ukrainian patients with doi:10.1016/j.gendis.2016.11.004 Ludmila Livshyts phenylketonuria

[1,10]Phenanthroline based Methods and Applications in Kovalska V., Kuperman M., cyanine dyes as fluorescent probes Fluorescence. – 2017. – V. 5, N 4. Varzatskii O., Kryvorotenko D., for ribonucleic acids in live cells – 045002. Kinski E., Schikora M., Janko https://doi.org/10.1088/2050‐ C., Alexiou C., Yarmoluk S., 6120/aa8510 Mokhir A. 26 The manifestation of optical Methods and applications in Yu G Terent'yeva, V M centers in UV–Vis absorption fluorescence. – Dec2016 Methods Yashchuk, L A Zaika, O M and luminescence spectra of Appl. Fluoresc. 4 044010 Snitserova, M Yu Losytsky

white blood human cells https://doi.org/10.1088/2050- 6120/4/4/044010 27 Comparison of the ability of Biological Chemistry. 2017 Jan Novosylna O, Doyle A, mammalian eEF1A1 and its 1;398(1):113‐124. Vlasenko D, Murphy M, oncogenic variant eEF1A2 to doi: 10.1515/hsz‐2016‐0172. Negrutskii B, El'skaya A. 28 interact with actin and calmodulin Protein CoAlation: A Redox‐ Biochem J. 2017 Jul 11; 474(14): TsuchiyaY, Peak‐Chew SY, Regulated Protein Modification by 2489‐2508. Newell Cl, Miller‐Aidoo Sh, Coenzyme A in Mammalian Cells https://doi.org/10.1042/BCJ2017 Mangal S, Zhyvoloup A, Bakovi 0129 J, Malanchuk O, Pereira GC, WOS:000406485400015 Kotiadis V, Szabadkai G, Duchen MR, Campbell M., Cuenca SR, Vidal‐Puig A, James AM, MurphyMP Filonenko V, 29 Skehel M, Gout I. Panel of SEREX‐defined antigens Biomarkers. 2017 Mar;22(2):149‐ Kostianets O, Shyyan M, for breast cancer autoantibodies 156. Antoniuk SV, Filonenko V, profile detection. https://doi.org/10.1080/1354750 Kiyamova R. X.2016.1252952 30 WOS:000393904000008 LRRK2 functions as a scaffolding Biochim. Biophys. Acta. – 2017. – J.H. Yoon,J.S. Mo,M.Y. Kim,E.J. kinase of ASK1‐mediated neuronal Vol. 1864. – № 12. – Р. 2356‐ Ann,J.S. Ahn, cell death 2368. E.H. Jo, H.J. Lee,Y.C. Lee,W. https://doi.org/10.1016/j.bbamcr Seol,S.M. Yarmoluk,T. .2017.09.001 Gasser,P.J. Kahle,G.H. Liu,J.C.I. 31 Belmonte, H.S. Park 32 Opioid precursor protein isoform Biochim Biophys Acta Gen Subj. O.Kononenko, is targeted to the cell nuclei in the 2017 Feb; 1861(2):246‐255 I.Bazov, H. Watanabe, human brain doi: G. Gerashchenko et al 10.1016/j.bbagen.2016.11.002

Spectral‐fluorescent study of the Spectrochimica Acta Part A: A.S. Tatikolov, interaction of the polymethine dye Molecular and Biomolecular T.M. Akimkin, probe Cyan 2 with chondroitin‐4‐ Spectroscopy. – 2017. – Vol. 177. I.G. Panova, sulfate – P. 93‐96. S.M. Yarmoluk https://doi.org/10.1016/j.saa.201 33 7.01.033 The Discovery of the Effect of Chemistry Select. – 2017. – Kuperman, M., closo‐Borate on Amyloid Fibril 2(34). – P. 10965‐10970. Chernii, S., Formation https://doi.org/10.1002/slct.2017 Varzatskii, O., (...), 01936 Yarmoluk, S., 34 Kovalska, V. Effective binding of Journal of Molecular Structure. – M.V. Kuperman, M.Yu. perhalogenated closo‐borates to 2017. – Vol. 1141. – P. 75‐80. Losytskyy, A.Yu. Bykov, serum albumins revealed by https://doi.org/10.1016/j.molstru S.M. Yarmoluk, spectroscopic and ITC studies c.2017.03.059 K.Yu. Zhizhin, N.T. Kuznetsov, O.A. Varzatskii, E. Gumienna‐Kontecka, 35 V.B. Kovalska. The impact of binding of Journal of Molecular Recognition. V. Kovalska, macrocyclic metal complexes on – 2017. –30(8):e2622. S. Chernii, amyloid fibrillization of insulin and https://doi.org/10.1002/jmr.2622 V. Cherepanov, lysozyme M. Losytskyy, V. Chernii, O. Varzatskii, A. Naumovets, 36 S. Yarmoluk. Dextran‐Polyacrilamide as Matrices International Journal of Polymer G. Teleegeev for Creation of Anticancer Science Volume 2017, Article ID N. Kutsevol, Nanocomposite. 4929857, 9 pages V. Chumachenko, https://www.hindawi.com/journa A Naumenko, ls/ijps/2017/4929857/ P. Telegeeva, S. Filipchenko, and Yu. Harahuts 37 The controversial role of Cancer research ‐2017.‐V.8.‐№ 5. Tyutyunnykova Anna, phospholipase C epsilon (PLC ) in ‐p.716‐729. Gennady Telegeev, cancer development and https://www.ncbi.nlm.nih.gov/p Anna Dubrovska 38 progression. mc/articles/PMC5381159/ Transient and stable vector Mutation Research ‐ Reviews in Stepanenko A.A., Heng. H.H. transfection: Pitfalls, off‐target Mutation Research effects, artifacts – 2017. – Vol. 773. – P. 91‐103. DOI: 10.1016/j.mrrev.2017.05.00 2 39 Placenta‐derived multipotent cells Exp Ther Med. – 2017. – Vol. 14, H. Svitina, V. Kyryk, have no effect on the size and N. 3. – P. 2135‐47. I. Skrypkina, M. Kuchma, number of DMH‐induced colon doi: 10.3892/etm.2017.4792 T. Bukreieva, 40 tumors in rats https://doi.org/10.3892/etm.201 P. Areshkov, Y. Shablii, 7.4792 Y. Denis, P. Klymenko, L. Garmanchuk, L. Ostapchenko, G. Lobintseva, and V. Shablii Molecular mechanisms of Bdp1 in Nat Commun. 2017 25;8(1):130 Gouge J. Guthertz TFIIIB assemblyand RNA DOI: 10.1038/s41467‐017‐00126‐ N.Kramm K.Dergai polymerase III 1 O.Abascal‐Palacios G. transcriptioninitiation Satia K. Cousin P. Hernandez N. Grohmann 41 D.Vannini A. Functionalassaysfortheassessment Dis Model Mech., 2017, 5. pii: Völker JM Dergai of thepathogenicity of variantsin dmm.029132. MAbriata LA Mingard Y GOSR2, an ER‐to‐Golgi SNARE DOI: 10.1242/dmm.029132 Ysselstein D Krainc D involvedinprogressivemyoclonuse Dal Peraro M pilepsies von Mollard GF Fasshauer D Koliwer J 42 Schwake M. Prostate cancer cells specifically Cell Adhesion & Migration 2017, A. Suhovskih, reorganize epithelial cells‐ Jan 2; 11(1) p. 39‐53 V. Kashuba, fibroblast communication through DOI: 10.1080/19336918.2016.118 G. Klein, proteoglycan and junction 2292 E. Grigorieva 43 pathways RhoA knockout fibroblasts lose Proc Natl Acad Sci U S A. 2017 T. Alkasalias, tumor‐inhibitory capacity in vitro Feb 7. pii: 201621161. doi: A. Alexeyenko , K.Hennig , and promote tumor growth in 10.1073/pnas.1621161114 V. Kashuba vivo. 1‐9 44 DOI: 10.1073/pnas.1621161114 Ancient permafrost staphylococci Microbial Ecology in Health and E. Kashuba, carry antibiotic resistance genes Disease 2017. Vol. 28. Issue 1. A. Dmitriev, p.1‐9 S. Kamal, DOI: 10.1080/16512235.2017.134 O. Melefors, 5574 G.Griva, I. Ernberg, 45 V. Kashuba Quercetin prevents type 1 diabetes Pharmacological Reports, 2017 O.Maksymchuk., A.Shysh, liver damage through inhibition of Dec; 69(6):1386‐1392. I.Rosohatska, M.Chashchyn CYP2E1 doi: 10.1016/j.pharep.2017.05.020. E pub 2017 Jun 24. 46 The First Space‐Related Study of a Orig Life Evol Biosph. ‐ 2017. – Podolich O., Zaets I., Kombucha Multimicrobial 47(2):169‐185 Kukharenko O., Orlovska I., Cellulose‐Forming Community: doi: 10.1007/s11084‐016‐9483‐4. Reva O., Khirunenko L., Preparatory Laboratory Sosnin M., Haidak A., Experiments. Shpylova S., Rohutskyy I., Kharina A., Skoryk М., Kremenskoy M., Klymchuk D., 47 Demets R., de Vera J.‐P. Kombucha Multimicrobial Astrobiology. ‐ 2017. – 17(5):459‐ Podolich O., Zaets I., Community under Simulated 469. Kukharenko O., Orlovska I., Spaceflight and Martian doi:10.1089/ast.2016.1480. Reva O., Khirunenko L., Sosnin Conditions. M., Haidak A., Shpylova S., 48 Rabbow E., Skoryk M., Kremenskoy M., Demets R., Kozyrovska N., de Vera J.‐P. Conductometric enzyme biosensor Sensors and Actuators B 239 Soldatkin O.O for patulin determination (2017) P. 1010‐1015. Stepurska K. DOI: 10.1016/j.snb.2016.08.121 Arkhypova V. Soldatkin A.P. El’skaya A. Lagarde F. 49 Dzyadevich S. Surface Plasmon Resonance Nanoscale Res. Lett. (2017) 12: Bakhmachuk A. Gorbatiuk O. Investigations of Bioselective 112. Rachkov A. Element Based on the doi:10.1186/s11671‐017‐1903‐5 Dons’koi B. Recombinant Protein A for Khristosenko R. Immunoglobulin Detection. Ushenin I. Peshkova V. 50 Soldatkin A. Improvement of amperometric Nanoscale Research Letters – Soldatkina O.V. transducer selectivity using 2017 – Vol. 12, art. №.594. Kucherenko I.S. Pyeshkova V. nanosized phenylenediamine films DOI: 10.1186/s11671‐017‐2353‐9 Alekseev S.A. Soldatkin O.O. 51 Dzyadevych S. A novel amperometric glutamate Nanoscale Research Letters Soldatkina O.V., biosensor based on glutamate (2017) 12:260 Soldatkin O.O., oxidase adsorbed on silicalite DOI 10.1186/s 11671‐017‐2026‐8 B. Ozansoy Kasap, Kucherenko D., Kucherenko I., B. Akata Rurc Dzyadevich S. 52 Biosensors based on nano‐ Nanoscale Research Letters B. Ozansoy Kasap, gold/zeolite‐modified ion selective (2017) 12:162 Marchenko S. field‐effect transistors for DOI 10.1186/s 11671‐017‐1943‐x Soldatlin O.O creatinine detection Dzyadevich S. 53 B. Akata Rurc Amperometric L‐arginine biosensor Microchim. Acta.‐2017.‐ 184(8).‐ Zhybak M. based on novel recombinant .P. 2679‐2686 Fayura L. arginine deiminase DOI 10.1007/s00604‐017‐2290‐4 Boretsky Yu. Gonchar M. Sibirny A. Dempsey E. Turner A. Korpan Ya. 54 L‐lactate selective impedimetric Electrochimica Acta 231 (2017) Deni Chan bienzymatic biosensor based on 209‐215. M. Barshan lactate dehydrogenase and DOI: 10.1016/j.electacta.2017.02. Ya. Korpan pyruvate oxidase 050 C. Brett 55 Fluorescent sensor systems based Talanta, 2017, vol. 175. P. 101‐ T.A.Sergeyeva, D.V.Yarinka, on nanostructured polymeric 107 E.V.Piletska, R.P.Linnik, membranes for selective DOI: 10.1016/j.talanta.2017.07.0 O.A.Zaporozhets, O.O.Brovko, recognition of aflatoxin B1 30 S.A.Piletsky, A.V.El’skaya 56 Development of a new biosensor In Nanophysics, Nanomaterials, Marchenko S. by adsorption of creatinine Interface studies, and Piliponskiy I. deiminase on monolayers of micro‐ Applications / Ed. by O. Fesenko, Mamchur O. and nanoscale zeolites L.Yatsenko. Soldatkin O.O. ‐ Springer Proceedings in Physics Kucherenko I.S., 195 – Springer International Berna Ozansoy Kasap, Publishing AG 2017. ‐ Chapter 42. Burcu Akata Kurc, – P. 573‐584. Dzyadevich S. DOI 10.1007/978‐3‐319‐56422‐7 Soldatkin A.P. 57 Gold nanoparticle/polymer/ In Nanophysics, Nanomaterials, Kucherenko I.S., enzyme nanocomposite for the Interface studies, and Carole Farre, development of adenosine Applications / Ed. by O. Fesenko, Gaetan Raimondi, triphosphate biosensor L.Yatsenko. Carole Chaix, ‐ Springer Proceedings in Physics N.Jaffrezic‐Renault, 195 – Springer International Soldatkin O.O. Publishing AG 2017. – Chapter 39. Soldatkin A.P. – P. 533‐545 Florence Lagarde DOI: 10.1007/978‐3‐319‐56422‐ 58 7_39 Adaptive radiation of P. fluorescens FEMS Microbiol Lett. – 2017. – Koza A., Kusmierska A., SBW25 in experimental 364 (12). McLauglin Kimberley, microcosms provides an Moshynets O., Spiers A.J. understanding of the evolutionary https://pubmed.ncbi.nlm.nih.gov ecology and molecular biology of /28535292/ A‐L interface biofilm‐formation 59 Cuprizone‐Induced Disorders J Aging Geriatr Med, 2017,1:2, Labunets IF, P.1‐8 of Central Nervous System Melnyk NO , Neurons, Behavioral https://www.scitechnol.com/pee Reactions,Brain Activity of r‐review/cuprizoneinduced‐ Rodnichenko AE, Macrophages and Antioxidant disorders‐of‐central‐nervous‐ Rymar SE, Enzymes in the Mice of Different system‐neurons‐behavioral‐ Ages: Role of Leukemia Inhibitory reactions‐brain‐activity‐of‐ Utko NA Factor in their Improvement macrophages‐and‐antioxidant‐ en‐Dw0O.php?article_id=6063

60 A quantum chemical based toxicity SAR and QSAR in Environmental Gooch, A., Sizochenko, N., study of estimated reduction Research 28(2), pp. 133‐137, Sviatenko, L., Gorb, L., potential and hydrophobicity in 2017 Leszczynski, J. series of nitroaromatic compounds https://www.tandfonline.com/do i/abs/10.1080/1062936X.2017.12 86687 61 In silico kinetics of alkaline Environmental science. Processes Sviatenko, L.K., Gorb, L., hydrolysis of 1,3,5‐trinitro‐1,3,5‐ & impacts, 19(3), pp. 388‐392, Leszczynska, D., Okovytyy, S.I., triazinane (RDX): M06‐2X 2017 Shukla, M.K., Leszczynski, J. investigation DOI: 10.1039/c6em00565a 62 Gene therapy effects on structural Innovation in Aging, 2017, Vol. V. Bezrukov , T. Kvitnitskaya‐ changes in various organs of young V.1. ‐ No. S1.‐ P.897 Ryzhova , and old mice with diabetes https://www.ncbi.nlm.nih.gov/p S. Mikhalskiy , mc/articles/PMC6184551/ S. Lugovskoy , P. Klymenko , 63 O. Toporova Adv Tissue Eng Regen Med, Future Perspectives in Heart Volume 2 Issue 5 – 2017 Pathology Diagnosis and Therapy. Piven O. DOI: 10.15406/atroa.2017.02.000 How We Can Use the Micro RNA? 64 43 Placenta‐derived multipotent cells Placenta. – 2017. ‐ Vol. 57. – P. V. Shablii, P. Areshkov, T. express syncytin‐1 and posses 254. DOI: Bukreieva, I. Skrypkina, V. ability to fuse with trophoblast http://dx.doi.org/10.1016/j.place Nikulina, V. Dotsenko, V. nta.2017.07.109 Kyryk, G. Lobintseva 65 66 Endothelial monocyte-activating Fiziol. Zh. 2017; 63(6): 3‐8. N.A. Dorofeyeva, G.G. polypeptide-II improves DOI: https://doi.org/10.15407/fz6 Vorobyov, I.Y. Cherepaha, diastolic heart function and 3.06.003 A.I. Kornelyuk, V.F. Sagach vascular relaxation in streptozotocin-induced experimental diabetes 67 The influence of native MSC, Ukrainian Neurosurgical Journal Tsymbaliuk VI., interleukin‐10 and MSC transfected with interleukin‐10 gene on 2018;No 1:66‐72 Velichko OM., behavioral reactions of rats with Pichkur LD., EAE DOI: https://doi.org/10.25305/un Akinola ST., j.117776 Verbovska SA., Shuvalova NS.,

Toporova OK.,

Deriabina OG.

68 Embryonic cardiospecific knockout Bulletin of the Taras Shevchenko Balatskyi V. V., Macewicz L. L., of α‐E‐catenin gene leads to National University of Kyiv. alteration of energy metabolism in Problems of regulation of Piven O. O. adult heart physiological functions – 2017. – V. 22. – № 2. – С. 65‐68.

http://biovestnik.com/index.php/ problems/article/view/306

69 Bulletin of the Zaporizhzhya National University. Biological α‐E‐catenin regulates sciences – 2017. – Т. 20. – № 2. – Balatskyi V. V., Macewicz L. L., С. 42‐48. hypertrophic signalings Piven O. O. in heart http://journalsofznu.zp.ua/index. php/biology/article/view/95

70 Cardiac deletion of α‐E‐catenin Фактори експериментальної Balatskyi V. V., Macewicz L. leads to reduced expression of the еволюції організмів.‐ 2017. – V. L., main component of desmosomes – 21. – P. 293‐296. γ‐catenin Piven O. O. http://utgis.org.ua/journals/index .php/Faktory/article/view/854

71 Large‐scale expansion and ExpOncol., 2017 Sep;39(3):171‐ Vasyliev R.G.Rodnichenko A.E. characterization of human adult 180 Gubar O.S.Zlatska neuralcrest‐derived multipotent A.V.Gordiienko I.M.Novikova stem cells from hair follicle for https://pubmed.ncbi.nlm.nih.gov/ S.N.Zubov D.O. regenerative medicine applications 28967641/

72 Endometrial stromal cells: ExpOncol. 2017 Sep;39(3):197‐202 Zlatska A.V.Rodnichenko A.E. isolation, expansion, morphological Gubar O.S.Zubov and functional properties https://pubmed.ncbi.nlm.nih.gov/ D.O.Novikova S.N.Vasyliev 28967640/ R.G.

73 Tissue‐engineered bone for ExpOncol. 2017 Sep;39(3):191‐196 Vasyliev R.G.Oksymets treatment of combat related limb V.M.Rodnichenko A.E.Zlatska injuries https://pubmed.ncbi.nlm.nih.gov/ A.V.Gubar O.S.Gordiienko 28967639/ I.M.Zubov D.O.

74 Postnatal extra‐embryonic tissues ExpOncol. 2017 Sep;39(3):186‐ Gubar O.S. Rodnichenko A.E. as a source of multiple cell types 190. Vasyliev R.G.Zlatska A.V. for regenerative medicine Zubov D.O. applications https://pubmed.ncbi.nlm.nih.gov/ 28967638/

75 Expression of Cancer- ExpOncol. 2017 — Т. 39, № 2. — E.E. Rosenberg, Associated Genes in Prostate С. 131‐137 Tumor G.V. Gerashchenko, https://exp- oncology.com.ua/wp/wp- N.V. Hryshchenko, content/uploads/2017/07/2298.pdf ?upload= L.V. Mevs,

K.A. Nekrasov,

Y.V. Vitruk,

O.P. Gryzodub,

E.A. Stakhovsky,

V.I. Kashuba

76 Dependence of DNA persistence Вiopolymers and Cell. 33, № 2, MI Zarudnaya, length on ionic conditions 81‐91 (2017) AL Potyahaylo, DOI: 10.7124/bc.000946 DM Hovorun

77 Amazing MSC – phenomenology, Biopolym. Cell. 2017; 33(1):64‐76. KordiumV. A., problems, solutions and opportunities DOI:10.7124/bc.000942 Irodov D. M.

78 Generation of HEK-293 stable cell Biopolym. Cell. 2017;33(5):356- Zaiets IV, Sivchenko AS, lines with disrupted expression of 366. Khoruzhenko AI, Filonenko ribosomal protein S6 kinase (S6K1) http://dx.doi.org/10.7124/bc.0009 VV. isoforms using the CRISPR/Cas9 5F genome editing system 79 Creation of gene expression Biopolymers and Cell 2017 33(6), Lykhenko, O., Frolova, A.O., database on preeclampsia‐affected с. 442‐452 Obolenskaya, M.Y. human placenta http://biopolymers.org.ua/conte nt/33/6/442/

80 Protein isoforms. Origin, structure Biopolym. Cell. 2017;33(3):161‐ Novosylna O.V. and functions. 171.

http://dx.doi.org/10.7124/bc.000 94E

81 Objective clustering inductive S. A. Babichev, A. Gozhyj, A. technology of gene expression Biopolymers and Cell. 2017. Vol. I. Kornelyuk, V. I. Lytvynenko profiles based on sota clustering 33. N 5. P 379–392 . doi: algorithm http://dx.doi.org/10.7124/bc.000 961

82 Protein partners of the eEF1Bβ Biopolym. Cell. 2017;33(4):243‐ Kapustian, L.M., Dadlez, M., subunit of the translation 255. Negrutskii, B.S. elongation complex eEF1B in the nuclear fraction of human lung http://dx.doi.org/10.7124/bc.000 carcinoma cells 95D

83 Hit identification of CK2 inhibitors Biopolym. Cell. – 2017. – Vol. 33, M.V. Protopopov, by methods of virtual screening № 4. – P. 291‐301. S.A. Starosyla, http://dx.doi.org/10.7124/bc.000 95B O.V. Borovykov, V.N. Sapelkin,

Y.V. Bilokin,

V.G. Bdzhola,

S.M. Yarmoluk

84 Synthesis and biological evaluation Biopolym. Cell. – 2017. – Vol. 33, A.N. Zinchenko, of novel amino‐substituted № 5. – P. 367‐378. derivatives of pyrido[2,3‐ L.V. Muzychka, http://dx.doi.org/10.7124/bc.000 d]pyrimidine as inhibitors of O.B. Smolii, protein kinase CK2 960 V.G. Bdzhola,

M.V. Protopopov,

S.M. Yarmoluk

85 Identification of rye chromosomes Biopolym. Cell. 2017; 33(2):116‐ Alkhimova O. G., by flow cytogenetics. 123. Zimina O. V. http://dspace.nbuv.gov.ua/handl e/123456789/152915 86 Expression of epithelial‐ Biopolymers and Cell. – 2017. G.V. mesenchymal transition – related – V. 33, № 5. – P.335-355. Gerashchenko,O.S.Mankovska genes in prostate tumours ,A.A.Dmitriev, L.V. Mevs, http://dx.doi.org/10.7124/bc. 00095E E.E. Rosenberg,

M.V. Pikul,

M.V. Marynychenko, O.P. Gryzodub, E.O. Stakhovsky,

V.I. Kashuba

87 Detection of prostate specific ETS Biopolymers and Cell. – 2017. L.V. Mevs, fusion transcripts in cancer – V. 33, № 4. – P.256-267. samples. G.V. Gerashchenko, E.E. Rosenberg,

http://dx.doi.org/10.7124/ M. V. Pikul, bc.000958 M. V. Marynychenko,O.P. Gryzodub,

S.O. Vozianov, E.A. Stakhovsky,

V.I. Kashuba

88 Cardiospecific knockout of αE- Biopolym. Cell – 2017. – Vol. 33. – Balatskyi V. V., Ruban T. P., catenin leads to violation of the № 6. Р. 434-441. Macewicz L. L., neonatal cardiomyocytes http://dx.doi.org/10.7124/bc.000 maturation via β-catenin and 96A Piven O. O. Yap signalling 89 Highly selective amperometric Biopolym. Cell. 2017; 33(2):124‐ Zinchenko O. A., Shkotova L. biosensor for uric acid 134. V., Kulynych T. U., Zinkina O. determination in real samples O., Soldatkin A. P. DOI: 10.7124/bc.00094A

90 Surface plasmon resonance Biopolymers and Cell (2017) 33, N Matsishin M. Kucherov A. investigation of DNA hybridization 4. C. 268–279 on a sensor surface using gold Ushenin Iu. DOI: nanoparticles modified by specific Lyapin A. oligonucleotides http://dx.doi.org/10.7124/bc.000 959 Lopatynskyi A.

Chegel V.

Rachkov A.

91 The origin of dystrophin gene Cytology and Genetics, 2017. ‐ v Kravchenko S.A., deletions among Duchenne and 51, Issue 3. – P.46‐53. DOI: Nechyporenko M.V., Livshits Becker muscular dystrophy 10.3103/S0095452717030057 L.A. patients from Ukraine.

92 Comprehensive characterisation of Cytology and Genetics –2017. – Navrotska D.O., Andreev I.O., cultivated in vitro Deschampsia Vol. 51, № 6 – P. 12–21. Parnikoza I.Yu., Spiridonova antarсtica E. Desv. plants with K.V., Poronnik O.O., Miryuta different chromosome numbers https://doi.org/10.3103/S009545 N.Yu., Myryuta G.Yu., 271706010X Zahrychuk O.M., Drobyk N.M., Kunakh V.A.

93 Search of protein kinase CK2 Ukr. Biochem. J. – 2017. – 89(5). – M.V. Protopopov, inhibitors based on purine‐2,6‐ P. 32‐39. Diones derivatives O.V. Ostrynska, https://doi.org/10.15407/ubj89.0 5.032 D.H. Ivanchenko, S.A. Starosyla,

V.G. Bdzhola,

M.I. Romanenko,

S.M. Yarmoluk

94 Molecular docking study of Bulletin of the Ukrainian Society Shchodryi V.B. Lozhko D., oligonucleotides with D-mannitol of Geneticists and Breeders Vol Tkachuk Z.

15 No 1 (2017)

DOI: https://doi.org/10.7124/visn yk.utgis.15.1.714

2018

1. Spread of Antarctic vegetation by Polar. Biol. – 2018. – V. 41, No 6. Parnikoza I., Rozhok A., the kelp gull: comparison of two – P. 1143‐1155. Convey P., Veselski M., Esefeld maritime Antarctic regions https://doi.org/10.1007/s00300‐ J., Ochyra R., Mustafa O., 018‐2274‐9 Braun C., Peter H. U., Smykla J., Kunakh V., Kozeretska I.

2. Assessment of the molecular Polish Polar Research. –2018. – Navrotska D., Andreev I., cytogenetic, morphometric and Vol.38, No.4. Betekhtin A., Rojek M., biochemical parameters of https://doi.org/10.24425/118759 Parnikoza I., Myryuta G., Deschampsia antarctica from its Poronnik O., Miryuta N., southern range limit in maritime Szymanowska‐Pułka J., Antarctic Grakhov V., Ivannikov R., Hasterok R., Kunakh V. 3. New proton conducting membrane Polymer . – 2018. – 142: 183– Rogalsky S., Bardeau J.‐F., based on bacterial 195. Makhno S., Babkina N., cellulose/polyaniline doi:10.1016/j.polymer.2018.03.0 Tarasyuk O., Cherniavska T., nanocomposite film impregnated 32 Orlovska I., Kozyrovska N., with guanidinium‐based ionic liquid Brovko O.

4. Bacterial cellulose‐lignin composite Int J Biol Macromol. – 2018. – Zmejkoski D., Spasojević D., hydrogel as a promising agent in 18(Pt A):494‐503. Orlovska I., Kozyrovska N., chronic wound healing doi:10.1016/j.ijbiomac.2018.06.0 Soković M., Glamočlija J., 67. Dmitrović S., Matović B., Tasić N., Maksimović V., Sosnin M., Radotić K. 5. Transplantation of placenta‐derived Oncology Letters, 2018,15, P. Svitina H., multipotent cells in rats with 5034‐5042 I. Skrypkina, dimethylhydrazine‐induced colon DOI: 10.3892/ol.2018.7996 Areshkov P., cancer decreases survival rate Kyryk V., Bukreieva T., Klymenko P., Garmanchuk L., Lobintseva G., Shablii V. 6. The Dual Role of the 2′‐OH Group of J Mol Biol (2018) 430, 2670–2676 M. Yu. Rybak O. P. Kovalenko A76 tRNA Tyr in the Prevention of D‐ doi: 10.1016/j.jmb.2018.06.036. M.A. Tukalo tyrosine Mistranslation Epub 2018 Jun 25

7. A molecular dynamics simulation Journal of Molecular Graphics A.Rayevsky, study of amino acid selectivity of and Modelling (2018) 84 P, 74‐81 M. Sharifi, LeuRS editing domain from Thermus DOI:10.1016/j.jmgm.2018.06.015 M. Tukalo thermophilus , 8. Theoretical coupling and stability of Letters in Drug Design & Demianenko E. Rayevsky A. boronic acid adducts with Discovery 07/2018; 15., Soriano‐Ursua M.‐ A Trujillo‐ catecholamines DOI:10.2174/1570180815666180 Ferrara J.‐ G: 710101604 9. 2'‐5'‐Linked Triadenylates Act as Journal of Proteomics & Skorobogatov OY, Kukharenko Protein Kinase Activity Modulators Bioinformatics DOI: AP, Kozlov O.V 10.4172/jpb.1000457 Dubey IY Tkachuk ZY 10. The Potential Protective Effect of Pharmaceuticals 2018, 11, P. Marchyshak T.V. Yakovenko Oligoribonucleotides‐d‐Mannitol 77(1‐14); T.G. Complexes against Thioacetamide‐ doi:10.3390/ph11030077 Shmarakov I Induced Hepatotoxicity in Mice Tkachuk Z.Yu.

11. Complexes of Oligoribonucleotides Pharmaceuticals. 2018. – V. 11, Melnichuk N.S. Kashuba V.I. with D‐Mannitol № 73. – Р.1‐16 Rybalko S.L. Tkachuk Z. Yu Modulate the Innate Immune doi:10.3390/ph11030073 Response to Influenza A Virus H1N1 (A/FM/1/47) In Vivo

12. Pre‐Clinical and Clinical Efficiency of Pharmaceutics. 2018. – V. 10, № Melnichuk N. Zarubaev V. Complexes of Oligoribonucleotides 59. P. 1‐11/ Iosyk I. Andreychyn M. with D‐Mannitol against Respiratory doi:10.3390/pharmaceutics10020 Semernikova L. Tkachuk Z. Viruses. 059.

13. mRNA‐Independent Way to Regulate B. Negrutskii , D. Vlasenko, Translation Elongation Rate in IUBMB Life. 2018 Mar;70(3):192‐ M.Mirande, P. Futernyk, A. Eukaryotic Cells 196. El'skaya doi: 10.1002/iub.1724.

14. Mitochondrial Nicotinic Front Pharmacol. 2018; 9:626. K. Uspenska, Acetylcholine Receptors Support doi: 10.3389/fphar.2018.00626. O, Lykhmus, . Liver Cells Viability After Partial eCollection 2018. M, Obolenskaya, Hepatectomy. S/ Pons, U. Maskos, S.Komisarenko, M. Skok 15. Distributed Bayesian networks PeerJ 6:e5692 Frolova A, Wilczyński B. reconstruction on the whole genome https://doi.org/10.7717/peerj.56

scale 92

16. Designing the Database for IEEE International Young O.Lykhenko Microarray Experiments Metadata Scientists Forum on Applied A,Frolova Physics and Engineering, YSF M. Obolenska

2017‐January, с. 127‐131 DOI: 10.1109/YSF.2017.8126658" 17. Planar Electrodes Modified by IEEE Xplore 2018 Oksana Tananaiko ; Anna Nanodiamonds and Biocomposite doi:10.1109/ELNANO.2018.84774 Trofimchuk ; Yana Silica‐Choline Oxidase Film For 33 Nechiporuk ; Viktor Choline Determination Garbuz ; Valery Muratov ; Oleksandr Vasil'ev.. O.Biloivan 18. Metal‐enhanced fluorescence of the Journal of Luminescence. – 2018. Losytskyy M.Yu., Akbay N., trimethine cyanine dyes complexed – V. 204. – P. 209‐215. Chernii S.V., Kryvorotenko with amyloid fibrils https://doi.org/10.1016/j.jlumin. D.V., Yarmoluk S.M., Kovalska 2018.08.001 V.B. 19. Differential effects of left and right Brain Res. 2018 Sep 15;1695:78‐ Kononenko O, Mityakina I, neuropathy on opioid gene 83 Galatenko V, Watanabe H, expression in lumbar spinal cord. https://doi.org/10.1016/j.brainre Bazov I, Gerashchenko A, s.2018.05.043 Sarkisyan D, Iatsyshyna A, Yakovleva T, Tonevitsky A, Marklund N, Ossipov MH, Bakalkin G. 20. The MRPS18‐2 protein levels Sci Rep. 2018 Feb 2;8(1):2268. M.Mushtaq, correlate with prostate tumor p.1‐14 L. Jensen, progression and it induces CXCR4‐ doi: 10.1038/s41598‐018‐20765‐ S.Davidsson, dependent migration of cancer 8. OV. Grygoruk, cells. O. Andrén, V. Kashuba , E. Kashuba.

21. Non‐dissociative structural Sci Rep 8, 10371 (2018) OO Brovarets, transitions of the Watson‐Crick and DOI:10.1038/s41598‐018‐28636‐ KS Tsiupa, reverse Watson‐Crick А∙Т DNA base y DM Hovorun pairs into the Hoogsteen and reverse Hoogsteen forms. 22. Endothelial Monocyte‐Activating International Journal of Nataliya A. Dorofeyeva, Polypeptide‐II Improves Diastolic Physiology and Pathophysiology, Georgiy G. Vorobyov, I. Y. Heart Function and Vascular vol.9, N 3, pp. 221‐228. Cherepaxa, Alexander I. Relaxation in Type‐I Diabetes DOI: 10.1615/IntJPhysPathophys. Kornelyuk, Vadim F. Sagach Mellitus, v9.i3.40 23. Cyclodextrins Application in Urease‐ Sensor Letters, Volume Marchenko S.V. Soldatkin Based Biosensor for Urea 16, Number 4, April 2018, O.O., Kolomiets Determination pp. 298‐303. L.A., Kornelyuk O.I. Soldatkin DOI: 10.1166/sl.2018.3955 A.P.

24. Effects of Some Growth Factors and Biochem Genet. 2018 Mar 27. Kotsarenko K, Lylo V, Ruban T, Cytokines on the Expression of the doi: 10.1007/s10528‐018‐9854‐9. Macewicz L, Lukash L. Repair Enzyme MGMT and Protein https://pubmed.ncbi.nlm.nih.gov

MARP in Human Cells In Vitro. /29589213/ https://doi.org/10.1007/s10528‐ 018‐9854‐9 25. Identification of 1,3‐thiazole‐5‐ Curr. Enzyme Inhib. – 2018. – Vol. M.V. Protopopov, carboxylic acid derivatives as 14, № 2. – Р. 152‐159. G.P. Volynets, inhibitors of protein kinase CK2 https://doi.org/10.2174/1573408 S.A. Starosyla, 013666170929163056 V.S. Vdovin,

S.S. Lukashov, Y.V. Bilokin, V.G. Bdzhola, S.M. Yarmoluk 26. Characterization of the interaction Anal. Lett. – 2018. – Vol. 51, № 1‐ M. Losytskyy, between phthalocyanine and 2. – P. 221‐228. N. Akbay, amyloid fibrils by surface‐enhanced https://doi.org/10.1080/0003271 S. Chernii, Raman scattering (SERS) 9.2017.1321655 E. Avci,

V. Chernii, S. Yarmoluk, M. Culha, V. Kovalska 27. Induced chirality of cage metal Dalton Trans. – 2018. – Vol. 47, V.B. Kovalska, complexes switched by their № 4. – Р. 1036‐1052. S.V. Vakarov, supramolecular and covalent https://doi.org/10.1039/C7DT037 M.V. Kuperman, binding 31G M.Y. Losytskyy, E. Gumienna‐Kontecka, Y.Z. Voloshin, O.A. Varzatskii 28. Design of functionalized β‐ New J. Chem. – 2018. – Vol. 42. – V. Kovalska, ketoenole derivatives as efficient P. 13308‐13318. S. Chernii, fluorescent dyes for detection of https://doi.org/10.1039/C8NJ010 M. Losytskyy, amyloid fibrils 20J I. Tretyakova, Y. Dovbii, A. Gorski, V. Chernii, R. Czerwieniec, S. Yarmoluk 29. The use of the docking studies with PHARMACIA. – 2018. – Vol. 65, I. Drapak, the purpose of searching potential № 2. – P. 40‐46. L. Perekhoda, cardioprotectors http://www.scopus.com/inward/ O. Vynogradova, record.url?eid=2‐s2.0‐ M. Protopopov,

85054500575%26partnerID=MN8 M. Suleiman, TOARS I. Sych, N. Kobzar, O. Kiz 30. Dihydrobenzo[4,5]imidazo[1,2‐ Mol. Divers. – 2018. – Vol. 22, № M.V. Protopopov, a]pyrimidine‐4‐ones as a new class 4. – P. 991‐998. O.V. Ostrynska, of CK2 inhibitors DOI: 10.1007/s11030‐018‐9836‐1 S.A. Starosyla, M.A. Vodolazhenko, S.M. Sirko, N.Y. Gorobets, V. Bdzhola, S.M. Desenko, S.M. Yarmoluk 31. Activity of Zn and Mg J. Mol. Recognit. – 2018. – Vol. V. Kovalska, phthalocyanines and porphyrazines 31, № 1: e2660. S. Chernii, in amyloid aggregation of insulin https://doi.org/10.1002/jmr.2660 M. Losytskyy, J. Ostapko,

I. Tretyakova, A. Gorski, V. Chernii, S. Yarmoluk 32. Protein CoAlation and antioxidant Biochem J. 2018 Jun Tsuchiya Y, Zhyvoloup A, function of Coenzyme A in 6;475(11):1909‐1937 Baković J, Thomas N, Yu BYK, prokaryotic cells https://doi.org/10.1042/BCJ2018 Das S, Orengo C, Newell C, 0043 Ward J, Saladino G, Comitani

WOS:000436048700003 F, Gervasio FL, Malanchuk OM, Khoruzhenko AI, Filonenko V, Peak‐Chew SY, Skehel M, Gout I 33. Nucleocytoplasmic distribution of F1000Research 2018, 7:1332. Kosach V., Shkarina K., S6K1 depends on the density and https://doi.org/10.12688/f1000r Kravchenko A., Tereshchenko motility of MCF‐7 cells in vitro esearch.15447.2 Y., Kovalchuk E., Skoroda L., Krotevych M., Khoruzhenko A. 34. Ubiquitin‐ligase AIP4 FEBS Lett, V.592, 13, 2259‐2267, Dergai O. controlsdifferentialubiquitinationan 2018 Dergai M. dstability of isoforms of thescaffold DOI: 10.1002/1873‐3468.13118 RynditchA.V. protein ITSN1 35. WIP/ITSN1 Gene, 674, 49‐56, 2018 GryaznovaT. complexisinvolvedincellularvesicletr DOI: 10.1016/j.gene.2018.06.078 Gubar O. affickingandformation of filopodia‐ Burdyniuk M. Kropyvko S. likeprotrusions Rynditch A 36. Mechanism of selectiverecruitment Genes Development,32(9‐10), DergaiO of RNA polymerases II and III 711‐722, 2018 CousinP, tosnRNAgenepromoters DOI: 10.1101/gad.314245.118 GougeJ, SatiaK, PrazV, KuhlmanT, LhôteP, VanniniA, HernandezN 37. Relation between stress granules Current Neurology and Dobra I. and cytoplasmic protein aggregates Neuroscience reports, 18, 107, Pankivskyi S. linked to neurodegenerative 2018 Samsonova A.

diseases DOI: 10.1007/s11910‐018‐0914‐7 Pastre D. Hamon L.

38. The A center dot T (rWC)/A center RSC Advances 8 (24), 13433‐ OO Brovarets, KS Tsiupa, DM dot T (H)/A center dot T (rH) A 13445 (2018) Hovorun. center dot T*(rw (WC))/A center dot DOI:10.1039/C8RA01446A

T*(w (H))/A center dot T*(rw (H)) mutagenic tautomerization via sequential 39. Novel pathway for mutagenic PLoS One 13, 6, e0199044 (2018) OO Brovarets’, KS Tsiupa, DM tautomerization of classical А∙Т DNA DOI: Hovorun. base pairs via sequential proton https:/10.1371/journal.pone.019

transfer through quasi‐orthogonal 9044 transition states: A QM/QTAIM investigation 40. Surprising conformers of the Frontiers in chemistry 6, article 8 OO Brovarets, biologically important A∙ T DNA base (2018) KS Tsiupa, pairs: QM/QTAIM proofs DOI:10.3389/fchem.2018.00008 DM Hovorun

41. Unexpected routes of the mutagenic Front. Chem.,2018, 6:532; doi: Brovarets’ O.O., Tsiupa K.S., tautomerization of the T nucleobase 10.3389/fchem.2018.00532 Dinets A., Hovorun D.M. in the classical A•T DNA base pairs: A QM/QTAIM comprehensive view

42. A QM/QTAIM detailed look at the Journal of Biomolecular Structure OO Brovarets’, IS Voiteshenko, Watson–Crick↔ wobble tautomeric and Dynamics 36 (7), 1649‐1665 H Pérez‐Sánchez, DM transformations of the 2‐ (2018) Hovorun. aminopurine∙ pyrimidine mispairs. DOI: Journal of Biomolecular Structure https://doi.org/10.1080/0739110 and Dynamics 36 (7), 1649‐1665 2.2017.1331864 (2018) 43. Structural transitions in poly(A), J. Biomol. Struct. Dyn. – 2018. – Zarudnaya M. I. , Kolomiets I. poly(C), poly(U) and poly(G) and Jul 27:1‐114. doi: M., Potyahaylo A. L., Hovorun their possible biological roles 10.1080/07391102.2018.1503972 D. M.

44. Diffusion of energetic compounds Journal of Biomolecular Structure Golius, through biological membrane: and Dynamics, 1‐9 L Gorb, Application of classical MD and 22018, 2018: . doi: O Isayev, COSMOmic approximations 10.1080/07391102.2018.1424037 J Leszczynski

45. Multimicrobial Kombucha Culture Astrobiology 2018 Nov 28. Podolich O., Kukharenko O., Tolerates Mars‐like Conditions DOI: 10.1089/ast.2017.1746 Haidak A., Zaets I., Zaika L., Simulated on Low‐Earth Orbit. StorozhukO., Palchikovska L., Orlovska I., Reva O., Borisova T., KhirunenkoL., Sosnin M., Rabbow E., Kravchenko V., Skoryk M., Kremenskoy M., Demets R., Olsson‐Francis K., Kozyrovska N., de Vera J‐P. 46. Renaissance of the Tautomeric Mitochondrial DNA ‐ New Insights Brovarets' O.O., Hypothesis of the Spontaneous Point / Ed. by Herve Seligmann. – Hovorun D.M. Mutations in DNA: New Ideas and London, United Kingdom: Computational Approaches IntechOpen, 2018. DOI: 10.5772/intechopen.77366 47. Cardiospecific deletion of αE‐catenin Pflügers Archiv‐European Journal Balatskyi V.V., Macewicz L.L., leads to heart failure and lethality in of Physiology. 2018 Jun 20:1‐5. Gan A.M., mice. https://doi.org/10.1007/s00424‐ Goncharov S.V., Pawelec P., 018‐2174‐4 Portnichenko G.V., Lapikova‐

Bryginska T.Y., Navrulin V.O., Dosenko V.E., Olichwier A., Dobrzyn P. Piven O.O. 48. Identification of protein kinase Monatshefte für Chemie ‐ Volynets Galyna, fibroblast growth factor receptor 1 Chemical Monthly (Monatsh Lukashov Sergiy, (FGFR1) inhibitors among the Chem), Oct 2019, Vol 150, Borysenko Iryna, derivatives of 5‐(5,6‐ Issue 10, pp 1801–1808. Gryshchenko Andrii, Starosyla dimethoxybenzimidazol‐1‐yl)‐3‐ Submitted manuscript, published Sergiy, hydroxythiophene‐2‐carboxylic acid on‐line 28 September 2019, Bdzhola Volodymyr, Ruban https://doi.org/10.1007/s00706‐ Tetiana, 019‐02493‐5 Iatsyshyna Anna, Lukash Lyubov, BilokinYaroslav, Yarmoluk Sergiy 49. Conductometric sensor with Chemical Papers.‐ 2018.‐ P. 1‐11 Soldatkina O.V. Cherenok S. calixarene‐based chemosensitive https://doi.org/10.1007/s11696‐ Kalchenko O. element for the arginine detection 018‐0515‐6 Prynova O.

Sylenko O. Kalchenko V. Dzyadevych S. 50. Conductometric biosensor for Bioelectrochemistry 124 (2018) Soldatkina O.V. Soldatkin O.O. arginine determination in 40‐46 Velychko T. pharmaceutics DOI: 10.1016/j.bioelechem.2018. Prilipko V. 07.002 Kuibida M. Dzyadevych S. 51. An amperometric glutamate Analytica Chimica Acta 1022 Borisova T. biosensor for monitoring glutamate (2018) 113‐123. Kucherenko D. Soldatkin O. release from brain nerve terminals DOI: 10.1016/j.aca.2018.03.015 Kucherenko I. and n blood plasma Pastukhov A. Nazarova A.

Galkin M. Borysov A. Krisanova N. Soldatkin A. El’skaya A. 52. Potentiometric enzyme biosensor for Sensors and Actuators B: Stepurska K. aflatoxin B1 detection – Kinetic Chemical, 259 (2018), P. 580‐586 Dzyadevych S. simulation DOI: 10.1016/j.snb.2017.12.092 Gridin S.

53. Electronic, thermodynamics and Physica B: Condensed Matter VI Ivashchenko, mechanical properties of LaB6 from 531, 216‐222, 2018 PEA Turchi, first‐principles https://www.sciencedirect.com/s L. Gorb,

cience/article/pii/S092145261731 VI Shevchenko, 0372 NR Medukh, J Leszczynski 54. Unexpected Int. J. Quantum. Chem., 2018, V. Brovarets’ O.O., A•T(WC)↔A•T(rWC)/A•T(rH) and 118, P. e25674 Tsiupa K.S., A•T(H)↔A•T(rH)/A•T(rWC) https://onlinelibrary.wiley.com/doi/ Hovorun D.M.

conformational transitions between abs/10.1002/qua.25692 the classical A•T DNA base pairs: A QM/QTAIM comprehensive study 55. Regulatory potential of mobile J. Genet. Genomic. Sci.‐ 2018.‐ N genetic elements in the human 3.‐ P. 008‐015 Pidpala O., Lukash L.

MGMT gene DOI:10.24966/GGS‐2485/100008

56. Ophioglossaceae (Psilotopsida) in Biodiv. Res. Conserv. – 2017 – Parnikoza I., Chernyshenko Ukraine Vol. 48. – P. 25‐47. Doi: M., Celka Z.

10.1515/biorc‐2017‐0009

57. Influence of oligoribonucleotides‐D‐ Reports of the National Academy Marchyshak T.V., Yakovenko mannitol complexes on the of Sciences of Ukraine, N 7, 2018 T.G., Tkachuk Z.Yu. expression of genes under acute http://dopovidi‐

thioacetaamide‐induced nanu.org.ua/en/archive/2018/7/ hepatotoxicity 14

58. Інгібування гемаглютенін‐ Допов. Нац. акад. наук Укр. Мельнічук Н.С. Ткачук З.Ю. гліканової взаємодії комплексами 2018. – № 1. – С. 92‐99. олігорибонуклеотидів з D‐ doi:https://doi.org/10.15407/dop манітолом ovidi2018.01.092

59. Dopov. Nac. akad. naukUkr., 6, Gerashchenko GV, 113‐119, 2018 Rynditch,AV, Kashuba VI Molecular profiling of

prostatetumors https://doi.org/10.15407/dopovi di2018.06.113 60. Impaired up‐Expression of pro‐ Mikrobiol. Z. 2018; – V 80, № 4. . Melnichuk N.S. Rybalko S.L. Oxidation Genes by – P. 88‐95. doi: Tkachuk Z.Yu Oligoribonucleotides at Influenza А https://doi.org/10.15407/microbi Virus Infection in vivo olj80.04.088

61. Bacteriophages of Lactococcus Mikrobiol. Z. 2018; Naumenko O.V., Skripkina I.Y., lactis ssp. and Streptococcus 80(6):123‐135. Voychuk S.I., Korol N.A., thermоphilus Isolated in Dairy doi: Tovkach F.I., Kigel N.F. Processing Plants of Ukraine https://doi.org/10.15407/microbi

olj80.06.123

62. The influence of native MSC, Ukrainian Neurosurgical Journal Tsymbaliuk VI., interleukin‐10 and MSC transfected with interleukin‐10 gene on 2018;No 1:66‐72 Velichko OM., behavioral reactions of rats with EAE Pichkur LD.,

DOI: https://doi.org/10.25305/un Akinola ST., j.117776 Verbovska SA., Shuvalova NS.,

Toporova OK.,

Deriabina OG.

63. Application of glutamate‐sensitive Biotechnologia Acta.‐ 2018.‐ 11 Kucherenko D. Kucherenko I. biosensor for analysis of food stuff (4).‐ P. 57‐67. Soldatkin O.О.

http://nbuv.gov.ua/UJRN/biot_20 18_11_4_6 Soldatkin О.P.

64. Effects of MTHFR gene on Journal for Veterinary Medicine, Fedota O. M., Skrypkina I. Y., reproductive health and Biotechnology and Biosafety, Mitioglo L. V., Tyzhnenko T. V., productive traits of dairy cows 2018, Volume 4, Issue 1, P. 24‐27 Ruban S. Yu.

http://jvmbbs.kharkov.ua/archive

/2018/volume4/issue1/article5.p hp

65. Computational approaches for Biopolymers and Cell. 2018. Vol. A. V. Rayevsky, M. A. parameterization of aminoacyl‐tRNA 34. N 3. P 239–247 doi: Tukalo synthetase substrates http://dx.doi.org/10.7124/bc.000 97E 66. Expression and purification of full‐ Biopolymers and Cell 2018, 8. Rybak M., Priss A., Gudzera length Alanyl‐tRNA‐synthetase from 34(6):435‐44. DOI: O., Kovalchuk A., Kryklyvyi I., Thermus thermophilus HB27. http://doi.org/10.7124/bc.00098 Tukalo M. E

67. Interaction of cationic porphyrin‐ Biopolymers and Cell. – 2018. – Didan Yu.V., Ilchenko M.M., imidazophenazine conjugates with V. 34, N 5. – P. 387-399. Negrutska V.V., Dubey L.V., http://dx.doi.org/10.7124/bc.000 DNA quadruplex: FID assay and Ryazanova O.A., Dubey I.Ya. 98B quantum‐chemical modeling

68. N‐alkylaryl styrylcyanine dyes as Biopolymers and Cell. – 2018. – Kuperman M.V., Snihirova fluorescent probes for nucleic acids V. 34, N 5. – P. 374-386. Y.V., Kryvorotenko D.V., http://dx.doi.org/10.7124/bc.000 detection Losytskyy M.Yu., Kovalska 987 V.B., Yarmoluk S.M.

69. Mass‐spectrometric and Biopolym. Cell. 2018;34(4):292‐ Kapustian L. M., Lysetsky I. L., bioinformatic analysis of eEF1Bγ 302. Bondarchuk T. V., Novosylna interactome in the cytoplasmic O. V., Negrutskii B. S. fraction of A549 cells http://dx.doi.org/10.7124/bc.000 982

70. Control of the amount and Biopolym. Cell. 2018;34(6):411‐ Negrutskii B. S., Novosylna O. functionality of the eEF1A1 and 425. V., Porubleva L. V., Vislovukh eEF1A2 isoforms in mammalian cells A. A. http://dx.doi.org/10.7124/bc.000 98C

71. Optimization of in vitro model for Biopolym. Cell. 2018;34(6):476- Kravchenko A. O., Kosach V. analysis of tumor cell migration 486. R., Shkarina K. A., Zaiets I. dynamics http://dx.doi.org/10.7124/bc.0009 V., Tykhonkova I. O., 92 Khoruzhenko A. I.

72. Study of SNRPN genetic and Вiopolymers and Cell. — 2018. — S.Yu. Chernushyn, N.V. epigenetic mutations in Prader‐Willi Т. 34, № 5. — С. 361‐366. Hryshchenko and Angelman patients DOI: http://dx.doi.org/10.7124/bc.000 98A

73. Expression patterns of genes, Biopolymers and Cell. – 2018. G.V. Gerashchenko, regulating lipid metabolism in – V. 34, № 6. – P.445-460. prostate tumors O.A. Kononenko, http://dx.doi.org/10.7124/bc. 000990 Yu. Bondarenko,

E.O. Stakhovsky,

V.I. Kashuba 74. Regenerative medicine advanced Biopolymers and Cell. – 2018. – Orlovska I.V., Yakovenko I.O., therapy for the non‐healing 34 ( 3): P 171–195 Haidak A.H., Zmejkoski D.Z., Kozyrovska N.O. cutaneous wound http://dx.doi.org/10.7124/bc.000 979

75. Anti‐HIV activity of ellagitannins Вiopolymers and Cell 2018. Vol. T. Yu. Trokhymchuk, A. S. from alder tree fruits 34. N 3. P 218–228 doi: Shalamay, M. P. Zavelevich, L. G. Palchykovska,O. V. DOI: Vasylchenko, S. L.Rybalko, D. http://dx.doi.org/10.7124/bc. B. Starosyla, S. T. Diadiun.. 0097C

76. Establishment and analysis of tissue Biopolym. Cell. 2018. V.34(6). P. Drobyk N. M., Mel’nyk V. M., and fast‐growing normal root 461‐476. Hrytsak L. R., Kravets N. B., cultures of four Gentiana L. species, Konvalyuk I. I., Twardovska M. rare highland medicinal plants http://dx.doi.org/10.7124/bc.000 O., Kunakh V. A. 991

77. Development of pyruvate oxidase‐ Biopolymers and cell. 2018. Vol. Knyzhnykova D. based biosensor for pyruvate 34. N 1. P. 14‐31. determination Topolnikova Ya. DOI: 10.7124/bc.00096C Kucherenko I. Soldatkin O.O.

78. Amperometric glucose biosensor Biopolymers and Cell.‐ 2018.‐ L.V.Shkotova, with IrNPs/Ludox - modified matrix 34(5).‐ Р. 367‐373. I.M.Voloshina, DOI: 10.7124/bc.000984 V.V.Kovalchuk,

M.T.Zhybak,

S.V.Dzyadevych

79. DNA loop organization in Biopolymers and Cell 2018 34(6), Afanasieva, K.S., Semenova, glioblastoma T98G cells at their pp. 426‐434 A.Y., Lukash, L.L., Sivolob, A.V. different functional states http://dx.doi.org/10.7124/bc.000

98D

80. Examining c‐di‐GMP andpossible QS Ukr. Biochem. J. – 2018. – 90 (3). Moshynets O.V., regulationinPseudomonasfluorescen – 17‐31. s SBW25: Foster D.,

linksbetweenintraandinter‐ Karakhim S.A., McLaughlin K.,

cellularregulationbenefitscommunity https://doi.org/10.15407/ubj90.0 cooperativeactivitiessuchasbiofilmfo 3.017 Rogalsky S.P., rmation Rymar S.Y., Volynets G.P.,

Spiers A.J.

81. The p60-S6K1 isoform of ribosomal Ukr. Biochem. J. 2018; 90(4): 25- Zaiets I.V., Sivchenko A.S., protein S6 kinase 1 is a product of 35. Khoruzhenko A.I., Savinsk alternative mRNA translation http://dx.doi.org/10.15407/ubj90.0 L.O., Filonenko V.V. 4.025

82. Expression pattern of genes Exp Oncol 2018. 40, 4, p.315- G.V. Gerashchenko, associated with tumor 322 microenvironment in prostate O.V Grygoruk, http://www.exp‐ cancer oncology.com.ua/article/12184 O.A. Kononenko,

O.P. Gryzodub,

E.A. Stakhovsky,

V.I. Kashuba

83. Vitaman E actavates expression of Exp Oncol.‐2018.‐V40.‐ L. Shvachko, C/EBR alpha transcription factor and №4.р.328‐331. G‐CSF receptor in leukemic K562 M. Zavelevich, cells. https://exp‐ oncology.com.ua/article/11958/v D. Gluzman,

itamin‐e‐activates‐expression‐of‐ I. Kravchuk, s‐ebp‐alpha‐transcription‐factor‐ and‐g‐csf‐receptor‐in‐leukemic‐ G. Teleegeev k562cells

84. Expression of steroid and peptide Exp Oncol 2018. 40, 2, P. 101 – G.V. Gerashchenko, hormone receptors, metabolic 108 L.V. Mevs, enzymes and EMT‐ related genes in https://exp‐ prostate tumors in relation to the oncology.com.ua/article/11260/e L.I.Chashchina, presence of the TMPRSS2/ERG xpression‐of‐steroid‐and‐peptide‐ fusion M. V. Pikul, hormone‐receptors‐metabolic‐ enzymes‐and‐emt‐related‐genes‐ O.P. Gryzodub, in‐prostate‐tumors‐in‐relation‐to‐ E.A. Stakhovsky, the‐presence‐of‐the‐tmprss2‐erg‐ fusion V.I. Kashuba

85. Tsitologiya i Genetika, 2018, Vol. S. Chernushyn, A novel mutation in the MECP2 gene 52, №. 4, pp. 68–75. identified in cohort of Rett syndrome R. Gulkovskyi,

patients from Ukraine. DOI:10.3103/S009545271804002 3 L. Livshits 86. Molecular organization of 5S Cytology and Genetics. – 2018. – Ishchenko O.O., Panchuk І.І., ribosomal DNА of Deschapmpsia Vol. 52, No. 6. – P. 416–421 Andreev І.O., Kunakh V.A., antarctica Volkov R.A. https://doi.org/10.3103/S009545 2719010146.

2019

1. Substrate‐assisted mechanism of Biochem J. 2019 Feb 28; 476 (4), Ilchenko M., catalytic hydrolysis of 719‐732. DOI: Rybak M. Yu., Rayevsky A., misaminoacylated tRNA required for 10.1042/BCJ20180910. Kovalenko O., protein synthesis fidelity. Dubey I., Tukalo M.

2. Stereospecificity control in Nucleic Acids Res. 2019. V. 47, Rybak M. Yu., Rayevsky A., aminoacyl‐tRNA‐synthetases revised: Nо. 18, Р. 9777‐9788. Gudzera O., Tukalo M. new evidence of D‐amino acids https://doi.org/10.1093/nar/gkz7 activation and editing. 56 3. Benzaldehyde thiosemicarbazone J Antibiot (Tokyo) 2019, v, 72 Volynets GP Tukalo MA derivatives against replicating and No, 4, p, :218‐224. Bdzhola VG Derkach NM nonreplicating Mycobacterium https://doi.org/10.1038/s41429‐ Gumeniuk MI Tarnavskiy SS tuberculosis 019‐0140‐9 Starosyla SA Yarmoluk SM.

4. Dual‐targeted hit identification using Journal of Computer‐Aided G.P. Volynets ∙ S. A. pharmacophore screening Molecular Design 2019, V, 33, p. Starosyla ∙ M. Yu. Rybak ∙ 955‐964. V. G. Bdzhola ∙ O. P. https://doi.org/10.1007/s10822‐ Kovalenko ∙ 019‐00245‐5 V.l S. Vdovin ∙ S. M. Yarmoluk ∙ M.l A. Tukalo 5. Dual‐targeted inhibitors of MedChemComm 2019, 10 (12), Kovalenko O. Volynets G., mycobacterial aminoacyl‐tRNA 2161‐2169. DOI: Rybak M., Starosyla S., synthetases among N‐benzylidene‐ https://doi.org/10.1039/C9MD00 Gudzera O., Lukashov S., N'‐thiazol‐2‐yl‐hydrazines. 347A Bdzhola V., Yarmoluk S., Boshoff H. and Tukalo M. 6. Topological Index of Conjugated Journal Polycyclic Aromatic N. Obernikhina, M. Kachaeva, Heterocyclic Compounds as Their Compounds 19 Jan 2019 V. Shchodryi, Y. Prostota, O. Donor/Acceptor Parameter. https://doi.org/10.1080/1040663 Kachkovsky, V. Brovarets Polycyclic Aromatic Compounds. 8.2018.1538056 Z. Tkachuk

7. Fluorescent Probe for Investigation o IEEE 39th International Conf on V Shchodryi, V Obernikhina, f Influence of Ribonucleosides With Nanotechnology and Electronics N ; Shaydyk, Y ; ; Slominskiy, D‐Mannitol (ELNANO) Y ; Tkachuk, Z Р.: 385‐389, 2019 DOI: 10.1109/ELNANO.2019.8783 955 8. Placental CX3CL1 is Deregulated by Int. J. Mol. Sci. 2019, 20, 641; Frolova A, і ін Всього 10 Angiotensin II and Contributes to a doi:10.3390/ijms20030641. Pro‐Inflammatory Trophoblast‐ Monocyte Interaction

9. Genome Sequence of Flavor‐ Microbiol Resour Announc, 8(9), Alina Frolova, І ін. Всього 19 Producing Yeast Saprochaete e00094‐19. DOI: suaveolens NRRL Y‐17571 10.1128/MRA.00094‐19

10. Genome sequence of the yeast Microbiology Resource Alina Frolova, І ін. Всього 18 saprochaete ingens CBS 517.90 Announcements 8(50),e01366 DOI: 10.1128/MRA.01366‐19

11. The Pediatric Cell Atlas: Defining the Dev Cell. 2019 April 08; 49(1): 10– Alina Frolova, І ін. Всього 71. Growth Phase of Human 29. Development at Single‐Cell doi:10.1016/j.devcel.2019.03.001 Resolution . 12. Regulatory antibodies against GPCR Frontiers in bioscience (Landmark A Frolova, і ін Всього 12 in women ten years after early‐onset edition), 24, 1462‐1476. preeclampsia. https://pubmed.ncbi.nlm.nih.gov /31136991/ 13. ComparativeAnalysis of Stem Cells Int., 19;2019:9640790. Vasyliev R.G. BiologicalProperties of Large‐ eCollection, 2019 Gubar O.S. GordiienkoI. M. ScaleExpandedAdultNeuralCrest‐ DOI: 10.1155/2019/9640790 Litvinova L.S. Rodnichenko DerivedStemCellsIsolatedfromHuma A.E. Shupletsova V.V. Zlatska nHairFollicleandSkinDermis A.V. Yurova K.A. Todosenko N.M. Khadzhynova V.E. ShulhaM.V. 14. Bondarchuk TV, Lozhko DM, The protein‐binding N‐terminal Int J Biol Macromol. 2019 Apr Shalak VF, Fatalska A, domain of human translation 1;126:899‐907. doi: Szczepanowski RH, Dadlez M, elongation factor 1Bβ possesses a 10.1016/j.ijbiomac.2018.12.220. Negrutskii BS, El'skaya AV. dynamic α‐helical structural organization. 15. Adsorption of nitrogen‐containing RSC Advances. – 2019. – V. 9, N Tsendra O., Boese D., Isayev compounds on hydroxylated α‐ 62. – P. 36066‐36074. O., Gorb L., Michalkova‐Scott quartz surfaces https://doi.org/10.1039/C9RA071 A., Hill F.C., Ilchenko M.M., 30J Lobanov V., Leszczynska D., Leszczynski J.

16. Multimicrobial Kombucha Culture Astrobiology. – 2019. – 19(2): Podolich O., Kukharenko O., Tolerates Mars‐like Conditions 183‐196. Haidak A., Zaets I., Zaika L., Simulated on Low‐Earth Orbit. doi: 10.1089/ast.2017.1746 Storozhuk O., Palchikovska L., Orlovska I., Reva O., Borisova T., Khirunenko L., Sosnin M., Rabbow E., Kravchenko V., Skoryk M., Kremenskoy M., Demets R., Olsson‐Francis K., Kozyrovska N., de Vera J‐P. 17. Limits of life and the habitability of Astrobiology. – 2019. – 19(2): de Vera J.‐P., Alawi M., Mars: The ESA space experiment 145‐157. doi: Backhaus T., Baqué M., Billi D., BIOMEX on the ISS. 10.1089/ast.2018.1897. Böttger U., Berger T., Bohmeier M., Cockell C., Demets R., de la Torre Noetzel R., Edwards H., Elsaesser A., Fagliarone C., Fiedler A., Foing B., Foucher F., Fritz J., Hanke F., Herzog T., Horneck G., Hübers H.‐W., Huwe B., Joshi J., Kozyrovska N., et al 18. 16S rRNA Gene Amplicon Based Frontiers in Microbiology, 2019, Madangchanok Metagenomic Signatures of 10:2103 Imchen, Ranjith Rhizobiome Community in Rice Field https://doi.org/10.3389/fmicb.20 Kumavath, Aline B. M. During Various Growth Stages 19.02103 Vaz, Aristóteles Góes‐ Neto, Debmalya Barh, Preetam Ghosh, Natalia Kozyrovska, Olga Podolich and Vasco Azevedo 19. Efficiency of Izatizon against IOSR Journal of Pharmacy and Zaika L.. Bolsunova O., Rybalko Experimental Hsv‐1 Infection Biological Sciences (IOSR‐JPBS). – S.. Starosilya D., Porva Y.. Vol. 14. ‐Issue 5. ‐Ser.III (Sep‐Oct Gomolyaka I, Potopalsky A., 2019). –PP. 89‐94 Zavelevich M. www.iosrjournals.org. DOI: 10.9790/3008‐1405038994

20. Stabilization of AIMP1/p43 and EMAP Pharmacological Reports, L. A. Kolomiets, II recombinant proteins in the (Accepted25 September 2019 ) N.V.Vorobyova, D. M. Lozhko, complexes with dextran‐70 volume 72, pages238–245 V.N. Zayets and A. I. polysaccharide, https://doi.org/10.1007/s43440‐ Kornelyuk 019‐00016‐x 21. Identification of protein kinase Monatshefte für Chemie – G. Volynets, fibroblast growth factor receptor 1 Chemical Monthly. – 2019. – S. Lukashov, (FGFR1) inhibitors among the Vol. 150, № 10. – P. 1801‐1808. I. Borysenko, derivatives of 5‐(5,6‐ http://dx.doi.org/10.1007/s0070 A. Gryshchenko, dimethoxybenzimidazol‐1‐yl)‐3‐ 6‐019‐02493‐5 S. Starosyla, hydroxythiophene‐2‐carboxylic acid V. Bdzhola, T. Ruban, A. Iatsyshyna, L. Lukash, Y. Bilokin, S. Yarmoluk 22. Induced CD of iron(ii) Metallomics. – 2019. – Vol. 11. – P. V.B. Kovalska, clathrochelates: sensing of the 338‐348. M.V. Kuperman, structural and conformational https://doi.org/10.1039/C8MT00 M.Yu. Losytskyy, alterations of serum albumins 278A S.V. Vakarov, S. Potocki, S.M. Yarmoluk, Y.Z. Voloshin, O.A. Varzatskii, E. Gumienna‐Kontecka 23. Dicarboxyl‐terminated iron(ii) RSC Advances. – 2019. – Vol. 9, V. Kovalska, clathrochelates as ICD‐reporters for Issue 42 – P. 24218‐24230. S. Vakarov, globular proteins https://doi.org/10.1039/C9RA041 M. Losytskyy, 02H M. Kuperman, N. Chornenka, Y. Toporivska, E. Gumienna‐Kontecka Y. Voloshin, O. Varzatskii, A. Mokhir 24. The use of the docking studies with Research J. Pharm. and Tech. – I. Drapak, the purpose of searching potential 2019. – Vol. 12, № 10. – P. 4889‐ M. Suleiman, antihypertensive drugs 4894. M. Protopopov, http://dx.doi.org/10.5958/0974‐ H Yeromina, 360X.2019.00846.1 I. Sych, Z. Ieromina, I. Sych, L. Perekhoda 25. Coenzyme A and protein CoAlation Biochem Biophys Res Commun. Aloum L, Brimson CA, levels are regulated in response to 2019. 2;511(2):294‐299. Zhyvoloup A, Baines R, Baković oxidative stress and during https://doi.org/10.1016/j.bbrc.20 J, Filonenko V, Thompson CRL, morphogenesis in Dictyosteliumdis 19.02.031 Gout I. coideum. WOS:000461404700014 26. A key metabolic integrator, Mol Cell Biochem. 2019;461(1‐ Baković J, Yu BYK, Silva D, coenzyme A, modulates the activity 2):91‐102. Chew SP, Kim S, Ahn SH, of peroxiredoxin 5 via covalent https://doi.org/10.1007/s11010‐ Palmer L, Aloum L, Stanzani G, modification. 019‐03593‐w Malanchuk O, Duchen MR, WOS:000490391400010 Singer M, Filonenko V, Lee TH, Skehel M, Gout I. 27. High Proliferative Placenta‐Derived BioMed Research International, Shablii V., Kuchma M., Svitina H., Multipotent Cells Express Research Article (13 pages), Skrypkina I., Areshkov P., Kyryk Cytokeratin 7 at Low Level Article ID 2098749, Volume 2019 V., Bukreieva T., Nikulina V., (2019) Shablii Iu., Lobyntseva G. https://doi.org/10.1155/2019/20 98749

28. Selection and analysis of International Journal of Dairy Naumenko O., bacteriophage‐insensitive mutants Technology, 2019, 9р. Skrypkina I., (BIMs) of Streptococcus DOI: 10.1111/1471‐0307.12607 Zhukova Ya., Vakulenko M., thermophilus isolated in Ukraine Kigel N. 29. Mesenchymal Stem Cells or Neuroscience2019;413(10):31‐44 Lykhmus, O., Interleukin‐6 Improve Episodic https://doi.org/10.1016/j.neurosc Kalashnyk, O., Memory of Mice Lacking α7 Nicotinic ience.2019.06.004 Koval, L., Acetylcholine Receptors Voytenko, L., Uspenska, K., Komisarenko, S., Deryabina, O., Shuvalova, N., Kordium, V., Ustymenko, A., Kyryk, V., Skok, M. 30. Intravenously injected mesenchymal Frontiers in Pharmacology Lykhmus, O., stem cells penetrate the brain and 2019;10(Issue MAR), Koval, L., treat inflammation‐induced brain Номерстатьи 355 Voytenko, L., damage and memory impairment in https://doi.org/10.3389/fphar.20 Uspenska, K., Komisarenko, S., mice(Article)(Открытыйдоступ) 19.00355 Deryabina, O., Shuvalova, N., Kordium, V., Ustymenko, A., Kyryk, V., Skok, M. 31. Setting our sights on infectious ACS Infect. Dis. 2020, 6, 1, 3–13 RyckerM.D., HornD., diseases Publication Date: December 6, AldridgeB., AmewuR.K., 2019 BarryC.E., III, BucknerF.S., https://doi.org/10.1021/acsinfec CookS., FergusonM.A.J., dis.9b00371 GobeauN., HerrmannJ., HerrlingP., HopeW., KeiserJ., LafuenteM.J., LeesonP.D., LeroyD., ManjunathaU.H., McCarthyJ., MizrahiV., MoshynetsO., NilesJ., OveringtonJ.P., PottageJ., RaoS.P.S., ReadK.D., RibeiroI., SilverL.L., SouthernJ., SpangenbergT., SundarS., TaylorC., VoorhisW.V., WhiteN.J., WyllieS., WyattP.G., GilbertI.H. 32. Priming winter wheat seeds with the PLoS ONE – 2019, 14 (2): Moshynets O., bacterial quorum sensing signal N‐ e0209460 Babenko L., hexanoyl‐L‐homoserine lactone (C6‐ https://doi.org/10.1371/journal.p Rogalsky S., HSL) shows potential to improve one.0209460 Iungin O., plant growth and seed yield Foster J., Kosakivska I., Potters G., Spiers A. 33. Antibiofilm activity of polyamide 11 Int J Mol Sci. 2019 Jan; 20(2): 348. Moshynets O., modified with thermally stable https://doi.org/10.3390/ijms2002 Bardeau J.F., polymeric biocide 0348 Tarasyuk O., polyhexamethylene guanidine 2‐ Makhno S., naphtalenesulfonate Cherniavska T., Dzhuzha O., Potters G., Rogalsky S.

34. Dietary lipids and environmental Pharmacological Reports O. Maksymchuk, xenobiotics as risk factors for 71 (2019) P.826‐832 V. Kashuba prostate cancer: The role of DOI: 10.1016/j.pharep.2019.04.0 cytochrome P450 11

35. Vitamin D3 deficiency in puberty rats Food and Chemical Toxicology, N.Krisanova, causes presynaptic malfunctioning 2019, V.123, p. 142‐150 N.Pozdnyakova, through alterations in exocytotic DOI: 10.1016/j.fct.2018.10.054 A.Pastukhov, release and uptake of M.Dudarenko, glutamate/GABA and expression of O.Maksymchuk, EAAC‐1/GAT‐3 transporters P.Parkhomets, R.Sivko, T. Borisova 36. 6‐gene promoter methylation OncolLett K. Nekrasov , assayis potentially applicable for 2019 Dec;18(6):6917‐6925. M.Vikarchuk , prostate cancer clinical staging base doi: 10.3892/ol.2019.11015 E. Rudenko , I.Ivanitskiy , donurine collection following V.Grygorenko , prostatic massage R.Danylets, A.Kondratov , L.Stoliar , B.Sharopov, V. Kashuba 37. Atomistic mechanisms of the double Journal of Biomolecular Structure OO Brovarets, DM Hovorun proton transfer in the H‐bonded and Dynamics 37, 7, 1880‐ nucleobase pairs: QM/QTAIM 1907 (2019) computational lessons DOI: 10.1080/07391102.2018.1467795 38. Conformational transitions of the Journal of Biomolecular Structure OO Brovarets, DM Hovorun. quercetin molecule via the rotations and Dynamics 38(10):2865‐2883 of its rings: A comprehensive (2019) theoretical study. DOI: 10.1080/07391102.2019.164 5734

39. Key microstructural mechanisms of Journal of Biomolecular Structure OO Brovarets’, DM Hovorun. the 2‐aminopurine mutagenicity: and Dynamics 37 (10), 2716‐2732 Results of extensive quantum‐ (2019) chemical research. DOI:10.1080/07391102.2018.149 5577 40. Conformational diversity of the Journal of Biomolecular Structure OO Brovarets’, quercetin molecule: A quantum‐ and Dynamics 38, – Pages 2817‐ DM Hovorun chemical view. 2836 (2019) DOI: 10.1080/07391102.2019.1656671 41. A new era of the prototropic Journal of Biomolecular Structure OO. Brovarets,’ DM Hovorun tautomerism of the quercetin and Dynamics DOI: molecule: A QM/QTAIM DOI: 10.1080/07391102.2019.169 computational advances 1660

42. Role of Singlet Oxygen in the Journal Phys. Chem. A 123, 35, LK. Sviatenko, L Gorb, D Degradation of Selected Insensitive 7597–7608 (2019) Leszczynska, SI. Okovytyy, MK. Munitions Compounds: A DOI: 10.1021/acs.jpca.9b01772 Shukla, Jerzy Leszczynski. Comprehensive, Quantum Chemical Investigation. . 43. C60 FULLERENES SELECTIVELY Nanomedicine: Nanotechnology, Mariia Melnyk; Irina V INHIBIT BKCa BUT NOT Kv CHANNELS Biology and Medicine 19, 1‐11б Ivanova; Dariia Dryn; Yuriy I IN PULMONARY ARTERY SMOOTH (2019) Prylutskyy; Vasyl V Hurmach; MUSCLE CELLS DOI: 10.1016/j.nano.2019.03.018 Maxim Platonov; Lina T Al Kury; Uwe Ritter; Anatoly I Soloviev; Alexander V Zholos

44. A density functional theory Journal of Molecular LK Sviatenko, L Gorb, J investigation of degradation of Modeling. 25, Leszczynski, D Leszczynska, SI. Nitroguanidine in the photoactivated Article number: 372 (2019) Okovytyy, MK. Shukla. triplet state DOI:10.1007/s00894‐019‐4252‐8

45. Novel tautomerisation mechanisms Front. Chem., 7, 2019, Brovarets’, O.O., Oliynyk, T.O. of the biologically important DOI: 10.3389/fchem.2019.00597 & Hovorun, D.M conformers of the reverse Löwdin, Hoogsteen and reverse Hoogsteen G*∙C* DNA base pairs via proton transfer: A quantum‐mechanical survey 46. Intron length polymorphism of β‐ Polar Science, 2019, V.19, P. 151‐ Rabokon A.M., Pirko М, tubulin genes in Deschampsia 154. Demkovych A. Ye, Andreev antarctica E.Desv. across the https://doi.org/10.1002/cbin.108 I.O., Parnikoza I. Yu., western coast of the Antarctic 86 Kozeretska I.A., Yu Z., Kunakh Peninsula V.A., BlumeY.B. 47. Isoprene hotspots at the Western Polar science, 2019, V.20, Pt.1, P. Nadzir M.S.M, Cain M., Coast of Antarctic Peninsula during 63‐74. Robinson A.D., Bolas C., Harris MASEC′16 https://doi.org/10.1016/j.polar.2 N.R.P., Parnikoza I. et al. 018.12.006 48. Antarctic terrestrial biome – most Encyclopedia of the World's Parnikoza I. Yu. Kozeretska I. poor, extreme and sensitive on the Biomes. Reference module in planet earth systems and environmental sciences. Elsevier, 2019. https://doi.org/10.1016/B978‐0‐ 12‐409548‐9.12005‐6 49. A highly selective amperometric Bioelectrochemistry.‐ 2019.‐ 128.‐ D.Yu.Kucherenko, biosensor array for the simultaneous P100‐108. I.S.Kucherenko, determination of glutamate, glucose, DOI: 10.1016/j.bioelechem.2019. O.O.Soldatkin, choline, acetylcholine, lactate and 03.010 Ya.V.Topolnikova, pyruvate S.V.Dzyadevych, A.P.Soldatkin 50. Amperometric biosensor modified SN Applied Science.‐ 2019.‐ L.Shkotova, with platinum and palladium 1:306.‐ DOI:10.1007/s42452‐019‐ A.Bohush, nanoparticles for detection of lactate 0315‐9 I.Voloshina, concentrations in wine O.Smutok, S.Dzyadevych 51. Novel multiplexed biosensor system Electroanalysis.‐ 2019.‐ 31(8).‐ I.S.Kucherenko, for the determination of lactate and P.1625‐1631. O.O.Soldatkin, pyruvate in blood serum DOI: 10.1002/elan.201900229 Ya.V.Topolnikova, S.V.Dzyadevych, A.P.Soldatkin 52. Advances in nanomaterial Nanoscale Advances.‐ 2019.‐ P. 1‐ I.S.Kucherenko, application in enzyme based 18 O.O.Soldatkin, electrochemical biosensors: a review DOI: 10.1039/c9na00491b D.Yu.Kucherenko, O.V.Soldatkina S.V.Dzyadevych 53. Development of a smartphone‐ Talanta, 201, 2019, P. 204‐210. Sergeyeva T., based biomimetic sensor for DOI: 10.1016/j.talanta.2019.04.0 Yarynka D., aflatoxin B1 detection using 16 Piletska E., molecularly imprinted polymer Lynnik R., membranes Zaporozhets O., Brovko O., Piletsky S., El'skaya A. 54. Development of electrochemical Applied Nanoscience (2019) O.V. Soldatkina biosensors with various types of 9:737–747 I. S. Kucherenko zeolites DOI: 10.1007/s13204‐018‐0725‐9 O.O. Soldatkin V.M. Pyeshkova O.Y. Dudchenko B. Akata Kurç S.V. Dzyadevych 55. 3‐Methylsulfidopropoxy Phosphorus, Sulfur, and Silicon S.O. Cherenok calixarene methylenebisphosphonic and the Related Element, 2019, O.O. Soldatkin acid for aminoacids chemosensor Volume 194, Issue 4‐6, Pages S.V. Marchenko 382‐383. O.V. Soldatkina DOI: 10.1080/10426507.2018.15 O.I. Kalchenko 50491 O.S. Prineva O.M. Silenko S.V. Dzyadevych V.I. Kalchenko. 56. Advances in the biosensors for Trends in Analytical Chemistry, ‐ Kucherenko I., lactate and pyruvate detection for 2019, ‐Vol 110, ‐P. 160‐172. Topolnikova Y., medical applications: A review DOI: 10.1016/j.trac.2018.11.004 Soldatkin O. 57. Study of tetraphenylporphyrins as J. Mol. Recognit. – 2019:e2811. S. Chernii, M. Losytskyy, modifiers of insulin amyloid https://doi.org/10.1002/jmr.2811 A. Kelm, A. Gorski, aggregation I. Tretyakova, S. Yarmoluk, V. Chernii, V. Kovalska 58. Wireless smart multisensor networks Information theories and Romanov V., Galelyuka I., for winemaking process control applications, Volume 26, Number Voronenko O., Kovyrova O., 2.– 2019. – P. 165–177 Dzyadevych S., Shkotova L. http://www.foibg.com/ijita/vol26 /ijita26‐02‐p05.pdf 59. Covalent Aurora A regulation by the Redox Biol. 2019. 5;28:101318 Tsuchiya Y, Byrne DP, Burgess metabolic integrator coenzyme A https://doi.org/10.1016/j.redox.2 SG, Bormann J, Baković J, 019.101318 Huang Y, Zhyvoloup A, Yu BYK, Peak‐Chew S, Tran T, Bellany F, Tabor AB, Chan AE, Guruprasad L, Garifulin O, Filonenko V, Vonderach M, Ferries S, Eyers CE, Carroll J, Skehel M, Bayliss R, Eyers PA, Gout I.

60. The use of the docking studies with Research Journal of Pharmacy I. Drapak, M. Suleiman, the purpose of searching potential and Technology. – 2019. – Vol. M. Protopopov, H Yeromina, I. antihypertensive drugs 12, № 10. – P. 4889-4894. Sych, Z. Ieromina, I. Sych, L. DOI: 10.5958/0974- Perekhoda

360X.2019.00846.1 61. PERINATOLOGY AND PEDIATRIC, L.A. Livshits, Polymorphism of the ADRB2 gene as 2019, Vol.78, No.2, pp.38‐45 a factor of hereditary susceptibility P.F. Tatarsky, to the development of asthma and Doi:10.15574/PP.2019.78.38 O.V.Gorodna, response to salbutamol therapy. A.V.Mayakovskaya,

G.P.Volynets

62. Dopov. Nac. akad. naukUkr., 1, Gerashchenko G.V. Rynditch 100‐106, 2019 A.V.KashubaV.I. Development of gene expression panels to determine prostate cancer https://doi.org/10.15407/dopovi di2019.01.100

63. The gene expression pattern as a Допов.Нац.акад. наук Укр. G.V. Gerashchenko, L.I. tool for assessment of components Chashchina, A.V. Rynditch, 2019. №4. С. 86-93 of microenvironment and response V.I. Kashuba to anti‐cancer therapy of prostate https://doi.org/10.15407/dopovid tumors i2019.04.086

64. Identification of parameters and Scientific Journal of Ternopil National V.Martsenyuk, A.Sverstiuk, investigation of stability of the Technical University.‐ 2019.‐ 96 (4).‐ P. S.Dzyadevych 101–111. mathematical model of biosensor for measuring α‐chaconine https://doi.org/10.33108/visnyk_ tntu2019.04

65. Site‐Directed Mutagenesis of Cytology and Genetics, 2019, Vol. V. N. Zayets, A. Yu. Tryptophan Residues in the 53, No. 3, pp. 219–226., 2019 Tsuvarev, L. A. Kolomiiets Structure of the Catalytic Module of and A. I. Kornelyuk Tyrosyl‐tRNA Synthetase from Bos https://doi.org/10.3103/S009545 taurus 271903006X

66. Investigation of rs11536889 + 3725G Cytology and Genetics, 2019, Vol. Kucherenko A.M., Моrоz L.V., / C polymorphism of the TLR4 gene 53, No. 4, pp. 300–306. in patients with autoimmune and Bеvz Т.I., chronic viral hepatitis C. DOI:10.3103/S009545271904007 8 Bulavenko V.I.,

Antypkin Y.G., Berezenko V.S.,

Dyba M.B., Pampukha V.M., Gorodna O.V.,

Livshits L.А.

67. Expression pattern of immune‐ and Biopolymers and Cell. – 2019. G.V. Gerashchenko, cancer‐ associated genes in peripheral blood of mice bearing Vol.35 N 4.P. 313‐320 I.M.Vagina, melanoma cells Yu.V. Vagin,

http://dx.doi.org/10.7124/bc.000 Z.Yu. Tkachuk, A0D V.I. Kashuba

68. Expression of cancer – associated Biopolymers and Cell. – 2019. – V. G.V. Gerashchenko, genes in prostate tumors at mRNA 35, № 1. – P.39‐53. and protein levels O.V Grygoruk,

E.E. Rosenberg, http://dx.doi.org/10.7124/bc.000 995 Yu. Bondarenko, E.V. Kashuba,

V.I. Kashuba

69. Study of SNRPN genetic and Biopolym. Cell. 2018; 34(5):361‐ Chernushyn S.Yu., epigenetic mutations in Prader‐Willi 366. Hryshchenko N.V. and Angelman patients. http://dx.doi.org/10.7124/bc.000 98A

70. Set of STR‐markers for 6p21.31 Biopolym. Cell. 2019; 35(5):333‐ Hryshchenko N. V., chromosomal region linkage analysis 339. Kirichenkova O. P., Gordiyk V. and CNV study V., Kravchenko S. A., Kashuba doi:10.7124/bc.000A10 V. I.

71. Spectroscopic study of binding of Biopolymers and Cell. – 2019. – V. Ryazanova O.A., Zozulya V.N., cationic Pheophorbide‐a to 35, N 2. – P. 129‐142. Voloshin I.M., Glamazda A.Yu., antiparallel quadruplex Tel22 Dubey I.Ya., http://dx.doi.org/10.7124/bc.000 99E Dubey L.V., Karachevtsev V.A.

72. Analysis of eEF1Bγ interactome in Biopolym. Cell. 2019;35(4):268‐ Kapustian L. M., Lysetsky I. L., the nuclear fraction of A549 human 287. Bondarchuk T. V., Novosylna lung adenocarcinoma cells O. V., Negrutskii B. S. http://dx.doi.org/10.7124/bc.000 A0A

73. Identification of 4‐ Вiopolym. Cell. – 2019. – Vol. 35, I.M. Kotey, methoxythieno[2,3‐d]pyrimidines as № 2. – P. 152‐162. FGFR1 inhibitors M.V. Protopopov, http://dx.doi.org/10.7124/bc.000 9A0 S.A. Starosyla, A.O. Balanda, L.V. Pletnova,

A.O. Prykhod'ko,

V.G. Bdzhola,

S.M. Yarmoluk

74. Biopolymers and Cell. – 2019. – Pernatii, A.Y., 35(6), pp. 448‐466. Identification and Volynets, G.P., characterization of potential http://dx.doi.org/10.7124/bc.000 membrane‐bound molecular A18 Protopopov, M.V., (...), drug targets of methicillin‐ Bdzhola, V.G., resistant Staphylococcus aureus using in silico approaches Yarmoluk, S.M.

75. Вiopolym. Cell. – 2019. – Vol. 35, S.S. Tarnavskiy, № 2. – P. 143‐151. Hit identification of FGFR1 M.V. Protopopov, O.V. inhibitors using receptor‐based http://dx.doi.org/10.7124/bc.000 Borovykov, virtual screening 99F A.O. Pryhodko,

V.G. Bdzhola,

S.M. Yarmoluk

76. Generation and characterization of the Biopolymers and Cell. 2019. HoliarV, GotsulyakNYa, MCF‐7 cell line with aknockout of a p85‐ 35(4):303–312 KhoruzhenkoAI, ZaietsIV. S6K1 isoform of the S6 kinase 1 http://dx.doi.org/10.7124/bc.000A ribosomal protein. 0B

77. Fibroblasts modulate the tumor cell Biopolym. Cell. 2019;35(6):417- Hotsuliak N. Ya., Kosach V. motility and their mTOR/S6K1 426. V., Tykhonkova I. O., phosphorylation status in vitro http://dx.doi.org/10.7124/bc.000A Palchevskii S. S., 15 Khoruzhenko A. I. 78. Identification of a novel S6K1 splice Biopolymers and Cell, 2019; Zaiets, I. V., Holiar, V. V., variant coding for the p60‐S6K1 isoform. 35(2): 99-106. Filonenko V. V. http://dx.doi.org/10.7124/bc.0009 9B 79. Phylogenetic analysis of two Biopolym. Cell. 2019; 35(1):64‐77. Mishchenko L. T., Dunich A. A., Ukrainian isolates of Wheat streak Skrypkina I. Ya., Kozub N. O. mosaic virus http://dx.doi.org/10.7124/bc .000997

80. Scaffold proteins ITSN1 and ITSN2 Biopolym. Cell., 35(2):81‐90, 2019 Pankivskyi S. V.Senchenko N. interact with nuclear RNA‐binding V. proteins http://dx.doi.org/10.7124/bc.000 999 Busko P. B.

Rynditch A. V. 81. Expression of ITSN2 and TKS5 Biopolym. Cell, 35, 21‐29, 2019 KropyvkoS.V., indifferentsubtypes of breastcancertumors http://dx.doi.org/10.7124/bc.000 TsybaL.O., 98F NovokhatskaO.V.,

Nemesh Y.M.,

Syvak L.A., TarasenkoT.Ye., Grabovoy A.N., Rynditch A.V

82. p60-S6K1 represents a novel kinase Ukr Biochem J, 2019; 91(4):17- ZaietsI. V., Holiar V. V., active isoform with the mode of 25 Sivchenko A. S.,Smialkovska regulation distinct from p70/p85- https://doi.org/10.15407/ubj91.04. V. V., Filonenko V. V. S6K1 isoforms. 017 83. Analysis of Aurora Kinases Genes Ukr.Biochem.J., 2019,Vol. 91, O. Mankovska, Expression Points on their distinct N 6, p.15-26 roles in Prostate Cancer G.Gerashchenko, doi: https://doi.org/10.15407/u Development bj91.06.015 E. Rozenberg,

E. Stakhovsky,

O. Kononenko,

Yu. Bondarenko,

V. Kashuba

84. Influence of interleukin-10 on factors INTERNATIONAL Labunets I. F., Rodnichenko A. of immune and antioxidant protection NEUROLOGICAL JOURNAL.- E., of the brain, thymic function and 2019.- Вип. 5.107. – С. 26-32. behaviour in the cuprizone mouse Utko N. A., model of demyelination doi.org/10.22141/2224- 0713.5.107.2019.176703 Pokholenko Ya.O.

85. The effects of interleukin-10 and Cell and Organ Transplantology.- Labunets I. F., Rodnichenko A. fibroblasts growth factor-2 in mice 2019.- V.7(1)- C. 25-31 E., Utko N. A., Panteleimonova with toxic cuprizone model of T. M., Pokholenko Ya. O., demyelination DOI: 10.22494/cot.v7i1.93 Litoshenko Z. L., Butenko G.

M.

86. ISOLATION AND CHARACTERIZATION Bulletin of Taras Shevchenko V. M. Zayets, A. Tsuvarev, L. A. OF THE MUTANT N‐TERMINAL National University of Kyiv ‐ Kolomiiets, P. Е. Zub, A. I. CATALYTICAL MODULE OF B. taurus Problems of Physiological Kornelyuk TYROSYL‐tRNA SYNTHETASE WITH Functions Regulation THE REPLACEMENT OF Trp 40 AND Trp 283 BY ALANINE. Vol 26, No 1 (2019)

http://www.biovestnik.com/inde x.php/problems/article/view/414 2020

1. Alterations in expression of s6k1 Biopolymers and Cell, Kosach, V.R., Hotsuliak, isoforms in mcf7 cells have a 2020, 36(2), р. 110-121 N.Y., Zaiets, strong impact on the locomotor I.V., ...Khoruzhenko, activity as well as on s6k1 and akt http://dx.doi.org/10.7124/bc.000 A.I., Filonenko, V.V. signaling A25

2. Novel isoniazid derivative as Future Microbiology, Volynets, G.P., Tukalo, promising antituberculosis agent 2020, 15(10), р. 869-879 M.A., Bdzhola, V.G., ...Tarnavskiy, doi: 10.2217/fmb-2019-0085 S.S., Yarmoluk, S.M.

3. Flavone inspired discovery of Bioorganic Chemistry, 2020, Protopopov, M.V., benzylidenebenzofuran-3(2H)-ones 102, 104062 Vdovin, V.S., (aurones) as potent inhibitors of Starosyla, S.A., ... Bdzhola, V.G., human protein kinase CK2 https://doi.org/10.1016/j.bioorg.2 020.104062 Yarmoluk, S.M.

4. Far-red pentamethine cyanine dyes Royal Society Open Science, Aristova, D., as fluorescent probes for the 2020, 7(7), 200453 Volynets, G., detection of serum albumins: Chernii, S., ... Yarmoluk, S., Probes for detection of serum https://doi.org/10.1098/rsos.200 Kovalska, V. albumins 453

5. Fluorescent β-ketoenole AmyGreen Methods and Applications in Moshynets, O., dye for visualization of amyloid Fluorescence, 2020, 8(3), Chernii, S., components of bacterial biofilms 035006 Chernii, V., ... Yarmoluk, S., doi: 10.1088/2050-6120/ab90e0 Kovalska, V.

6. Variation of photostability of DNA- Biopolymers and Cell, 2020, Snihirova, Y.V., sensitive styrylcyanine dyes caused 36(2), р. 146-160 Losytskyy, M.Y., by N-alkyl functionalization Kryvorotenko, D.V., ... http://dx.doi.org/10.7124/bc.000 Mokhir, A., A28 Kovalska, V.B.

7. Study of tetraphenylporphyrins as Journal of Molecular Chernii, S., modifiers of insulin amyloid Recognition, 2020, 33(1), e2811 Losytskyy, M., aggregation Kelm, A., ... https://doi.org/10.1002/jmr.2811 Chernii, V., Kovalska, V.

8. Altered expression of cytochrome Pharmacological Reports, 2020, Maksymchuk, O.V., P450 enzymes involved in 72(5), р. 1161-1172 Kashuba, V.I. metabolism of androgens and vitamin D in the prostate as a risk https://doi.org/10.1007/s434 factor for prostate cancer 40-020-00133-y 9. Cell stemness is maintained upon Proceedings of the National Mushtaq, M., Kovalevska, L., concurrent expression of rb and the Academy of Sciences of the Darekar, S., ...Arsenian- mitochondrial ribosomal protein United States of America, 2020, Henriksson, M., Kashuba, E. s18-2 117(27), р. 15673-15683 https://doi.org/10.1073/pnas.19225 35117

10. Functional Hypermethylation of Molecular Biology, 2020, 54(2), Dmitriev, A.A., Beniaminov, ALDH1L1, PLCL2, and PPP2R3A р. 178-184 A.D., Melnikova, N.V., in Colon Cancer ...Kudryavtseva, A.V., https://doi.org/10.1134/S002 Kashuba, V.I. 6893320010057

11. Electrochemical biosensors based on Analytica Chimica Acta, 2020, Kucherenko, I.S., Soldatkin, multienzyme systems: Main groups, 1111, р. 114‐131 O.O., Dzyadevych, S.V., advantages and limitations – A https://doi.org/10.1016/j.aca.202 Soldatkin, A.P. review 0.03.034

12. Study on efficiency of oriented Biopolymers and Cell, 2020, Bakhmachuk, A.O., Gorbatiuk, immobilization of antibodies on the 36(4), р. 271‐278 O.B., Rachkov, A.E., Soldatkin, spr sensor surface using http://dx.doi.org/10.7124/bc.000 A.P. staphylococcal protein a or its A32 recombinant analogue 13. Clinoptilolite‐based Conductometric Electroanalysis, 2020, 32(9), р. Saiapina, O., Sensors for Detection of Ammonium 1993‐2001 Vronska, Y., in Aqueous Solutions https://doi.org/10.1002/elan.202 Dzyadevych, S., 060026 Jaffrezic‐Renault, N. 14. Potentiometric sensing of histamine Journal of Food Science and Hidouri, S., using immobilized enzymes on Technology, 2020 Errachid, A.H., layered double hydroxides https://doi.org/10.1007/s13197‐ Baussels, J., 020‐04795‐7 Korpan Ya.I., ... Ruiz‐Sanchez, O., Baccar, Z.M. 15. Non‐translational Connections of Frontiers in Molecular Negrutskii, B. eEF1B in the Cytoplasm and Nucleus Biosciences, 2020, 7, 56 of Cancer Cells doi: 10.3389/fmolb.2020.00056

16. Methylation of human elongation Biopolymers and Cell, 2020, Porubleva, L.V., Kolesnik, D.L., factor eef1a2 is not essential for 36(4), р. 254‐263 El’skaya, A.V., Negrutskii, B.S. eef1a2‐eef1b interaction http://dx.doi.org/10.7124/bc.000 A31 17. Personalized responsiveness of Biopolymers and Cell, 2020, Kovalchuk, M.V., human PBMCs to the action of IL‐7 36(4), р. 304‐312 Ruban, T.A., http://dx.doi.org/10.7124/bc.000 Usenko, M.O., A33 Kordium, V.A.

18. The atypical Rho GTPase RhoU Journal of cell science, 2020, Gubar, O., Croisé, P., interacts with intersectin‐2 to 133(16) Kropyvko, S., ...Gasman, S., regulate endosomal recycling doi:10.1016/j.devcel.2013.06.01 Ory, S. pathways 9

19. ITSN1 regulates SAM68 solubility Cellular and Molecular Life Pankivskyi, S., Pastré, D., through SH3 domain interactions Sciences, 2020 Steiner, E., ...Rynditch, A., with SAM68 proline‐rich motifs doi: 10.1007/s00018-020-03610- Hamon, L. y 20. Analysis of Aurora Kinases Genes Ukr.Biochem.J., 2019,Vol. 91, O. Mankovska, Expression Points on their distinct G.Gerashchenko, E. N 6, p.15-26 roles in Prostate Cancer Rozenberg, E. Stakhovsky, O. Development https://doi.org/10.15407/ubj91.0 6.015 Kononenko, Yu. Bondarenko, V. Kashuba

21. Pattern of expression of immuneand Ukr.Biochem.J., 2020,Vol. 92, G. V. Gerashchenko, I. M. stroma‐associated genes in blood of Vagina, Yu. V. Vagin , V. I. N 1, p.p.5-11 mice with experimental B16 Kashuba melanoma doi: https://doi.org/10.15407/ubj92.0 1.005 22. Cholesterol‐metabolizing P450s as Exp. Oncol., 2019, Vol. 21, N3, O.Maksymchuk, I.Rosohatska , potential molecular targets for P.268 O.Mankovska , S.Semko , E. prostate cancer therapy DOI: Stakhovsky , V.Kashuba. 10.2174/1573408016666200218 122044

23. Stabilization of AIMP1/p43 and Pharmacological Reports, 2020, Kolomiiets, L.A., Vorobyova, EMAP II recombinant proteins in the 72(1), р. 238‐245 N.V., Lozhko, D.M., Zayets, complexes with polysaccharide V.M., Kornelyuk, A.I. dextran‐70 https://doi.org/10.1007/s43440- 019-00016-x. 24. Predicting the Protein Tertiary Proceedings ‐ 15th International Fefelova, I., Fefelov, A., Structure by Hybrid Clonal Selection Conference on Advanced Trends Voronenko, M., ...Ryzhkov, E., Algorithms on 3D Square Lattice in Radioelectronics, Lytvynenko, V. Telecommunications and Computer Engineering, TCSET 2020, 2020, р. 965‐968, 9088634 doi: 10.1016/j.ijbiomac.2018.12.220

25. The use of inductive methods to Conference Paper Lurie, I., Lytvynenko, V., identify subtypes of glioblastomas in CEUR Workshop Proceedings, Olszewski, S., ...Zhunissova, gene clustering 2020, 2631, р. 406‐418 U., Boskin, I. http://ceur‐ws.org/Vol‐ 2631/paper31.pdf

26. Aberrant expression of placental‐like Experimental Oncology, 2020, Shvachko, L.P., Zavelevich, alkaline phosphatase in chronic 42(1), р. 31‐34 M.P., Gluzman, D.F., Telegeev, myeloid leukemia cells in vitro and DOI: 10.32471/exp-oncology.2312- G.D. its modulation by vitamin e 8852.vol-42-no-1.14285

27. Inhibition of USP1, a new partner of Experimental Oncology, 2020, Antonenko, S.V., Telegeev, Bcr‐Abl, results in decrease of Bcr‐ 42(2), р. 109‐114 G.D. Abl level in K562 cells DOI: 10.32471/exp-oncology.2312- 8852.vol-42-no-2.14533

28. Interaction of Bcl‐Abl Oncoprotein Cytology and Genetics, 2020, Antonenko, S.V., Kravchuk, with the Glg1 Protein in K562 Cells: 54(1), р. 48‐54 I.V., Telegeev, G.D. its Role in the Pathogenesis of https://doi.org/10.3103/S0095 Chronic Myeloid Leukemia 452720010028

29. The fkbp4 gene, encoding a International Journal of Ilaslan, E., Markosyan, R., regulator of the androgen receptor Molecular Sciences, 2020, 21(21), Sproll, P., ...Jaruzelska, J., signaling pathway, is a novel р. 1‐12, 8403 Kusz‐zamelczyk, K. candidate gene for androgen https://doi.org/10.3390/ijms212 insensitivity syndrome 18403

30. Genetic Modifiers of the Spinal Cytology and Genetics, 2020, Hryshchenko, N.V., Muscular Atrophy Phenotype 54(2), р. 130‐136 Yurchenko, A.A., Karaman, https://doi.org/10.5435/JAAOS- H.S., Livshits, L.A. 20-06-393

31. Role of IL6 ‐174 G/C, IL10 1082G/A Oftalmologicheskii Zhurnal, 2020, Livshits, L.A., Drozhzhyna, G.I., and IL10 ‐592C/A in the (2), р. 3‐11 Kucherenko, A.M., ...Gorodna, pathogenesis of keratoconus and http://doi.org/10.31288/oftalmolz O.V., Sereda, K.V. development of recurrent erosion in h20202311 Ukrainian patients with lattice corneal dystrophy

32. Effect of Microenvironment on the The journal of physical chemistry. Gorb, L., Pekh, A., Nyporko, Geometrical Structure of d(A)5 d(T)5 B, 2020, 124(42), р. 9343‐9353 A., ...Hovorun, D.M., and d(G)5 d(C)5 DNA Mini‐Helixes https://doi.org/10.1021/acs.jpcb.0c06 Leszczynski, J. and the Dickerson Dodecamer: A 154

Density Functional Theory Study

33. A density functional theory study of Journal of Molecular Modeling, Gorb, L., Ilchenko, M., simplest nanocomposites formed by 2020, 26(7), 183 Leszczynski, J. graphene oxide and polyvinyl doi: 10.1007/s00894-020- alcohol: geometry, interaction 04447-9 energy and vibrational spectrum

34. A new era of the prototropic Journal of Biomolecular Structure Brovarets’, O.O., Hovorun, tautomerism of the quercetin and Dynamics, 2020, 38(16), р. D.M. molecule: A QM/QTAIM 4774‐4800 Epub 2019 Dec 16 computational advances doi: 10.1080/07391102.2019.16916 60.

35. Energy of the CH⋯O H‐bonds and Journal of Molecular Liquids, Brovarets', O.O., Hovorun, others specific contacts in the 2020, 313, 113456 D.M. quercetin molecule: QM/QTAIM DOI: approximation formulas 10.1016/j.molliq.2020.113456

36. A never‐ending conformational story Applied Sciences (Switzerland), Brovarets', O.O., Hovorun, of the quercetin molecule: 2020, 10(3), 1147 D.M. Quantum‐mechanical investigation https://doi.org/10.3390/app1003 of the O3'H and O4'H hydroxyl 1147 groups rotations

37. A hidden side of the conformational Symmetry, 2020, 12(2), 230 Brovarets', O.O., Hovorun, mobility of the quercetin molecule https://doi.org/10.3390/sym120 D.M. caused by the rotations of the O3H, 20230 O5H and O7H hydroxyl groups: In Silico scrupulous study

38. Conformational diversity of the Journal of Biomolecular Structure Brovarets’, O.O., Hovorun, quercetin molecule: A quantum‐ and Dynamics, 2020, 38(10), р. D.M. chemical view 2817‐2836 https://doi.org/10.1080/0739110 2.2019.1656671

39. Tautomeric hypothesis: To be or not Ukrainian Biochemical Journal, Brovarets, O.O., Hovorun, to be? quantum‐mechanical verdict 2020, 92(4), р. 124‐126 D.M., https://doi.org/10.15407/ubj92.0 4.124

40. Synthesis, spectral properties and Tetrahedron Letters, 2020, Kuziv, I., Dubey, L., Dubey, I. evaluation of carboxy‐functionalized 61(35), 152227 3‐thiazolylcoumarins as blue‐ https://doi.org/10.1016/j.tetlet.2 emitting fluorescent labeling 020.152227 reagents

41. Pheophorbide–phenazinium Journal of Molecular Structure, Ryazanova, O.A., Zozulya, conjugate as a fluorescent light‐up 2020, 1214, 128218 V.N., Voloshin, I.M., ...Dubey, probe for G‐quadruplex structure DOI:10.1016/j.molstruc.2020.12 I.Y., Karachevtsev, V.A. 8218

42. Sensor based on molecularly Sensors (Switzerland), 2020, Sergeyeva, T., Yarynka, D., imprinted polymer membranes and 20(15), р. 1‐20, 4304 Dubey, L., ...Piletsky, S., smartphone for detection of https://doi.org/10.3390/s20154 El’skaya, A. Fusarium contamination in cereals 304

43. Direct labeling of nucleosides with Biopolymers and Cell, 2020, Kuziv, I.A.B., Dubey, I.Y.A. 3‐thiazolylcoumarin fluorescent 36(1), р. 36‐47 dyes DOI: 10.7124/bc.000A1F

44. Setting our sights on infectious ACS Infect. Dis. 2020, 6, 1, 3–13 RyckerM.D., HornD., diseases Publication Date: December 6, AldridgeB., AmewuR.K., 2019 BarryC.E., III, BucknerF.S., https://doi.org/10.1021/acsinfec CookS., FergusonM.A.J., dis.9b00371 GobeauN., HerrmannJ., HerrlingP., HopeW., KeiserJ., LafuenteM.J., LeesonP.D., LeroyD., ManjunathaU.H., McCarthyJ., MizrahiV., MoshynetsO., NilesJ., OveringtonJ.P., PottageJ., RaoS.P.S., ReadK.D., RibeiroI., SilverL.L., SouthernJ., SpangenbergT., SundarS., TaylorC., VoorhisW.V., WhiteN.J., WyllieS., WyattP.G., GilbertI.H. 45. Synthesis and Reactivity of Russian Journal of Inorganic Chernii, V., Tretyakova, I., Zirconium and Hafnium Chemistry, 2020, 65(10), р. 1489‐ Selin, R., Fedosova, N., Dihydroxophthalocyaninates 1493 Kovalska, V. https://doi.org/10.1134/S0036 023620100046

46. Sensing of a Protein’s Structure Russian Journal of Inorganic Kovalska, V., Vakarov, S., Using the Induced Circular Chemistry, 2020, 65(10), р. 1513‐ Chornenka, N., Gumienna‐ Dichroism Spectra by the 1521 Kontecka, E., Voloshin, Y. Monocarboxyphenylsulfide Iron(II) https://doi.org/10.1134/S0036 Clathrochelates as Optical Reporters 023620100137

47. Cyclodextrin encapsulated pH Molecules, 2020, 25(19), 4397 Sardaru, M.‐C., Carp, O., Ursu, sensitive dyes as fluorescent cellular doi.org/10.3390/molecules2519 E.‐L., ...Danac, R., Rotaru, A. probes: Self‐aggregation and in vitro 4397 assessments

48. Population genetic structure of iris Acta Biologica Cracoviensia Bublyk, O., pumila L. In Ukraine: Effects of Series Botanica, 2020, 62(1), р. Andreev, I., habitat fragmentation 51‐ doi: 10.1007/s00018-020- Parnikoza, I., 03610-y 61 Kunakh, V.