References
- Zakaryan H, Revilla Y. African swine fever virus: current state and future perspectives in vaccine and antiviral research. Vet Microbiol. 2016;185:15–19.
- Costard S, Wieland B, de Glanville W, et al. African swine fever: How can global spread be prevented? Philos Trans R Soc Lond B Biol Sci. 2009;364:2683–2696.
- Van Der Ryst E. Maraviroc – A CCR5 antagonist for the treatment of HIV-1 infection. Front Immunol. 2015;6(277).
- Stanciu C, Trifan A, Muzica C, et al. Efficacy and safety of alisporivir for the treatment of hepatitis C infection. Expert Opin Pharmacother. 2019;20(4):379–384.
- Alonso C, Miskin J, Hernaez B, et al. African swine fever virus protein p54 interacts with the microtubular motor complex through direct binding to light-chain dynein. J Virol. 2001;75(20):9819–9827.
- de Matos AP, Carvalho ZG. African swine fever virus interaction with microtubules. Biol Cell. 1993;78(3):229–234.
- Carvalho ZG, De Matos AP, Rodrigues-Pousada C. Association of African swine fever virus with the cytoskeleton. Virus Res. 1988;11(2):175–192.
- Jouvenet N, Monaghan P, Way M, et al. Transport of African swine fever virus from assembly sites to the plasma membrane is dependent on microtubules and conventional kinesin. J Virol. 2004;78(15):7990–8001.
- Hakobyan A, Arabyan E, Kotsinyan A, et al. Inhibition of African swine fever virus infection by genkwanin. Antiviral Res. 2019;167:78–82.
- Carrascosa AL, Bustos MJ, de Leon P. Methods for growing and titrating African swine fever virus: field and laboratory samples. Curr Protoc Cell Biol. 2011;26(26):14.
- Abagyan R, Totrov M, Kuznetsov D. ICM—a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. J Comput Chem. 1994;15(5):488–506.
- Kufareva I, Ilatovskiy AV, Abagyan R. Pocketome: an encyclopedia of small-molecule binding sites in 4D. Nucleic Acids Res. 2012;40(D1):D535–D540.
- Halgren TA. Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. J Comput Chem. 1996;17(5–6):490–519.
- Jakalian A, Bush BL, Jack DB, et al. Fast, efficient generation of high-quality atomic charges. AM1-BCC model: I. Method. J Comput Chem. 2000;21(2):132–146.
- Maier JA, Martinez C, Kasavajhala K, et al. ff14SB: improving the accuracy of protein side chain and backbone parameters from ff99SB. J Chem Theory Comput. 2015;11(8):3696–3713.
- Lee TS, Cerutti DS, Mermelstein D, et al. GPU-accelerated molecular dynamics and free energy methods in Amber18: performance enhancements and new features. J Chem Inf Model. 2018;58(10):2043–2050.
- Jorgensen WL, Chandrasekhar J, Madura JD, et al. Comparison of simple potential functions for simulating liquid water. J Chem Phys. 1983;79(2):926–935.
- Oliver DS, Cunha LB, Reynolds AC. Markov chain Monte Carlo methods for conditioning a permeability field to pressure data. Math Geology. 1997;29(1):61–91.
- Wu X, Brooks BR. Self-guided Langevin dynamics simulation method. Chem Physc Lett. 2003;381(3–4):512–518.
- Ryckaert JP, Ciccotti G, Berendsen HJ. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys. 1977;23(3):327–341.
- Miller III BR, McGee Jr TD, Swails JM, et al. MMPBSA. py: an efficient program for end-state free energy calculations. J Chem Theory Comput. 2012;8(9):3314–3321.
- Rosowsky A, Papathansopoulos N. Pyrimido[4,5-c]isoquinolines. 2. Synthesis and biological evaluation of some 6-alkyl-, 6-aralkyl-, and 6-aryl-l,3-diamino-7,8,9,10-tetrahydropyrimido[4,5-c]isoquinolines as potential folate antagonists. J Med Chem. 1974;17(12):1272–1276.
- Kamal El-Dean AM, Abdel Hafez AA. Synthesis of some new fused thieno- and furopyridines. Phosphorus Sulfur Silicon. 1989;46:1–6.
- Sirakanyan SN, Geronikaki A, Spinelli D, et al. Synthesis and structure of condensed triazolo- and tetrazolopyrimidines. Tetrahedron. 2013;69:10637–10643.
- Sirakanyan SN, Spinelli D, Geronikaki A, et al. On the reaction of 2-[(4-cyano-5,6,7,8-tetrahydroisoquinolin-3-yl)oxy]acetamides with bases: 1-amino-6,7,8,9-tetrahydrofuro[2,3-c]isoquinoline-2-carboxamides and 3-amino-4-cyano-5,6,7,8-tetrahydroisoquinolines via a smiles-type rearrangement. Tetrahedron. 2015;71: 3263–3272.
- Sirakanyan SN, Spinelli D, Geronikaki A, et al. New methods for the synthesis of 3-amino-6,7-dihydro-5H-cyclopenta[c]pyridine-4-carbonitriles and cyclopenta[d]pyrazolo[3,4-b]pyridines via a smiles-type rearrangement. J Heterocycl Chem. 2017;54:1199–1209.
- Freitas F, Frouco G, Martins C, et al. African swine fever virus encodes for an E2-ubiquitin conjugating enzyme that is mono- and di-ubiquitinated and required for viral replication cycle. Sci Rep. 2018;8:3471.
- Steinmetz MO, Prota AE. Microtubule-targeting agents: strategies to hijack the cytoskeleton. Trends Cell Biol. 2018;28(10):776–792.
- McLoughlin EC, O’Boyle NM. Colchicine-binding site inhibitors from chemistry to clinic: a review. Pharmaceuticals (Basel). 2020;13(1):8.
- Daina A, Michielin O, Zoete V. SwissADME: a free web tool to evaluate pharmacokinetics, drug-likeness and medicinal chemistry friendliness of small molecules. Sci Rep. 2017;7:42717.
- Dong M, Liu F, Zhou H, et al. Mechanisms of tubulin binding ligands to target cancer cells: updates on their therapeutic potential and clinical trials. Molecules. 2016;21(10):1375.
- Prota AE, Bargsten K, Zurwerra D, et al. Molecular mechanism of action of microtubule-stabilizing anticancer agents. Science. 2013;339(6119):587–590.
- Naghavi MH, Walsh D. Microtubule regulation and function during virus infection. J Virol. 2017;91(16):e00538–17.
- Vonderheit A, Helenius A. Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes. PLoS Biol. 2005;3(e233).
- Xiao PJ, Samulski RJ. Cytoplasmic trafficking, endosomal escape, and perinuclear accumulation of adeno-associated virus type 2 particles are facilitated by microtubule network. J Virol. 2012;86:10462–10473.
- Schepis A, Schramm B, de Haan CA, et al. Vaccinia virus-induced microtubule-dependent cellular rearrangements. Traffic. 2006;7:308–323.
- Kim S, Kim HY, Lee S, et al. Hepatitis B virus x protein induces perinuclear mitochondrial clustering in microtubule- and dynein-dependent manners. J Virol. 2007;81:1714–1726.
- Sol-Foulon N, Sourisseau M, Porrot F, et al. ZAP-70 kinase regulates HIV cell-to-cell spread and virological synapse formation. EMBO J. 2007;26:516–526.
- Rudnicka D, Feldmann J, Porrot F, et al. Simultaneous cell-to-cell transmission of human immunodeficiency virus to multiple targets through polysynapses. J Virol. 2009;83:6234–6246.
- Richter M, Boldescu V, Graf D, et al. Synthesis, biological evaluation, and molecular docking of combretastatin and colchicine derivatives and their hCE1-activated prodrugs as antiviral agents. Chem Med Chem. 2019;14(4):469–483.
- Worachartcheewan A, Songtawee N, Siriwong S, et al. Rational design of colchicine derivatives as anti-HIV agents via QSAR and molecular docking. Med Chem. 2019;15(4):328–340.
- Hurtado C, Bustos M, Sabina P, et al. Antiviral activity of lauryl gallate against animal viruses. Antivir Ther. 2008;13(7):909–917.
- Hakobyan A, Arabyan E, Avetisyan A, et al. Apigenin inhibits African swine fever virus infection in vitro. Arch Virol. 2016;161:3445–3453.
- Freitas F, Frouco G, Martins C, et al. In vitro inhibition of African swine fever virus-topoisomerase II disrupts viral replication. Antiviral Res. 2016;134:34–41.
- Frouco G, Freitas FB, Coelho J, et al. DNA-binding properties of African swine fever virus pA104R, a histone-like protein involved in viral replication and transcription. J Virol. 2017;91:e02498–16.
- Hakobyan A, Arabyan E, Kotsinyan A, et al. Inhibition of African swine fever virus infection by genkwanin. Antiviral Res. 2019;167:78–82.
- de León P, Bustos M, Torres E, et al. Inhibition of porcine viruses by different cell-targeted antiviral drugs. Front Microbiol. 2019;10:1853.
- Head B, Patel H, Insel P. Interaction of membrane/lipid rafts with the cytoskeleton: impact on signaling and function: membrane/lipid rafts, mediators of cytoskeletal arrangement and cell signaling. Biochim Biophys Acta. 2014;1838(2):532–545.
- Naghavi M, Walsh D. Microtubule Regulation and Function during virus infection. J Virol. 2017;91(16):e00538–17.
- Rohena CC, Mooberry SL. Recent progress with microtubule stabilizers: new compounds, binding modes and cellular activities. Nat Prod Rep. 2014;31(3):335–355.
- Pasquier E, Kavallaris M. Microtubules: a dynamic target in cancer therapy. IUBMB Life. 2008;60(3):165–170.
- Tangutur AD, Kumar D, Krishna KV, et al. Microtubule targeting agents as cancer chemotherapeutics: an overview of molecular hybrids as stabilizing and destabilizing agents. Curr Top Med Chem. 2017;17(22):2523–2537.
- Fennell B, Naughton J, Barlow J, et al. Microtubules as antiparasitic drug targets. Expert Opin Drug Discov. 2008;3(5):501–518.
- Chatterji BP, Jindal B, Srivastava S, et al. Microtubules as antifungal and antiparasitic drug targets. Expert Opin Ther Pat. 2011;21(2):167–186.