HDAC Inhibitors against SARS-CoV-2

Zhou, P.; Yang, X-L.; Wang, X-G.; Hu, B.; Zhang, L.; Zhang, W. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature, 2020, 579(7798), 270-273.

Hui, D.S.; I Azhar, E. ; Madani, T.A.; Ntoumi, F.; Kock, R.; Dar, O.; Ippolito, G.; Mchugh, T.D.; Memish, Z.A.; Drosten, C.; Zumla, A.; Petersen, E. The continuing 2019-nCoV epidemic threat of novel coronaviruses to global health - the latest 2019 novel coronavirus outbreak in Wuhan, China. Int. J. Infect. Dis., 2020, 91, 264-266.
[http://dx.doi.org/10.1016/j.ijid.2020.01.009] [PMID: 31953166]

Baig, A.M.; Khaleeq, A.; Ali, U.; Syeda, H. Evidence of the COVID-19 virus targeting the CNS: tissue distribution, host–virus interaction, and proposed neurotropic mechanisms. ACS Chem. Neurosci., 2020, 11(7), 995-998.
[http://dx.doi.org/10.1021/acschemneuro.0c00122] [PMID: 32167747]

Bogoch, I.I.; Watts, A.; Thomas-Bachli, A.; Huber, C.; Kraemer, M.U.; Khan, K. Pneumonia of unknown aetiology in Wuhan, China: potential for international spread via commercial air travel. J. Travel Med., 2020, 27(2)

Wu, F.; Zhao, S.; Yu, B.; Chen, Y-M.; Wang, W.; Song, Z-G.; Hu, Y.; Tao, Z.W.; Tian, J.H.; Pei, Y.Y.; Yuan, M.L.; Zhang, Y.L.; Dai, F.H.; Liu, Y.; Wang, Q.M.; Zheng, J.J.; Xu, L.; Holmes, E.C.; Zhang, Y.Z. A new coronavirus associated with human respiratory disease in China. Nature, 2020, 579(7798), 265-269.
[http://dx.doi.org/10.1038/s41586-020-2008-3] [PMID: 32015508]

Zhou, Y.; Hou, Y.; Shen, J.; Huang, Y.; Martin, W.; Cheng, F. Network-based drug repurposing for novel coronavirus 2019-nCoV/SARS-CoV-2. Cell Discov., 2020, 6(1), 14.
[http://dx.doi.org/10.1038/s41421-020-0153-3] [PMID: 32194980]

Fehr, A.R.; Perlman, S. Coronaviruses: an overview of their replication and pathogenesis. Coronaviruses, 2015, 1282, 1-23.
[http://dx.doi.org/10.1007/978-1-4939-2438-7_1] [PMID: 25720466]

Perlman, S.; Netland, J. Coronaviruses post-SARS: Update on replication and pathogenesis. Nat. Rev. Microbiol., 2009, 7(6), 439-450.
[http://dx.doi.org/10.1038/nrmicro2147] [PMID: 19430490]

Cong, Y.; Ren, X. Coronavirus entry and release in polarized epithelial cells: a review. Rev. Med. Virol., 2014, 24(5), 308-315.
[http://dx.doi.org/10.1002/rmv.1792] [PMID: 24737708]

Mesli, F.; Ghalem, M.; Daoud, I.; Ghalem, S. Potential inhibitors of angiotensin converting enzyme 2 receptor of COVID-19 by Corchorus olitorius Linn using docking, molecular dynamics, conceptual DFT investigation and pharmacophore mapping. J. Biomol. Struct. Dyn., 2021, 1-13.
[http://dx.doi.org/10.1080/07391102.2021.1896389] [PMID: 33706683]

Abbas, S.H.; Abd El-Hafeez, A.A.; Shoman, M.E.; Montano, M.M.; Hassan, H.A. New quinoline/chalcone hybrids as anti-cancer agents: design, synthesis, and evaluations of cytotoxicity and PI3K inhibitory activity. Bioorg. Chem., 2019, 82, 360-377.
[http://dx.doi.org/10.1016/j.bioorg.2018.10.064] [PMID: 30428415]

Enayatkhani, M.; Hasaniazad, M.; Faezi, S.; Gouklani, H.; Davoodian, P.; Ahmadi, N.; Einakian, M.A.; Karmostaji, A.; Ahmadi, K. Reverse vaccinology approach to design a novel multi-epitope vaccine candidate against COVID-19: An in silico study. J. Biomol. Struct. Dyn., 2021, 39(8), 2857-2872.
[http://dx.doi.org/10.1080/07391102.2020.1756411] [PMID: 32295479]

Wu, C.; Liu, Y.; Yang, Y.; Zhang, P.; Zhong, W.; Wang, Y.; Wang, Q.; Xu, Y.; Li, M.; Li, X.; Zheng, M.; Chen, L.; Li, H. Analysis of therapeutic targets for SARS-CoV-2 and discovery of potential drugs by computational methods. Acta Pharm. Sin. B, 2020, 10(5), 766-788.
[http://dx.doi.org/10.1016/j.apsb.2020.02.008] [PMID: 32292689]

Mishra, D.; Maurya, R.R.; Kumar, K.; Munjal, N.S.; Bahadur, V.; Sharma, S.; Singh, P.; Bahadur, I. Structurally modified compounds of hydroxychloroquine, remdesivir and tetrahydrocannabinol against main protease of SARS-CoV-2, a possible hope for COVID-19: docking and molecular dynamics simulation studies. J. Mol. Liq., 2021, 335, 116185.
[http://dx.doi.org/10.1016/j.molliq.2021.116185] [PMID: 33879934]

Wu, Z.; McGoogan, J.M. Characteristics of and important lessons from the coronavirus disease 2019 (COVID-19) outbreak in China: Summary of a report of 72 314 cases from the Chinese Center for Disease Control and Prevention. JAMA, 2020, 323(13), 1239-1242.
[http://dx.doi.org/10.1001/jama.2020.2648] [PMID: 32091533]

Mélo Silva Júnior, M.L.; Souza, L.M.A.; Dutra, R.E.M.C.; Valente, R.G.M.; Melo, T.S. Review on therapeutic targets for COVID-19: Insights from cytokine storm. Postgrad. Med. J., 2021, 97(1148), 391-398.
[http://dx.doi.org/10.1136/postgradmedj-2020-138791] [PMID: 33008960]

Anthony, S.J.; Johnson, C.K.; Greig, D.J.; Kramer, S.; Che, X.; Wells, H.; Hicks, A.L.; Joly, D.O.; Wolfe, N.D.; Daszak, P.; Karesh, W.; Lipkin, W.I.; Morse, S.S.; Mazet, J.A.K.; Goldstein, T. Global patterns in coronavirus diversity. Virus Evol., 2017, 3(1), vex012.
[http://dx.doi.org/10.1093/ve/vex012] [PMID: 28630747]

Zhu, N.; Zhang, D.; Wang, W.; Li, X.; Yang, B.; Song, J.; Zhao, X.; Huang, B.; Shi, W.; Lu, R.; Niu, P.; Zhan, F.; Ma, X.; Wang, D.; Xu, W.; Wu, G.; Gao, G.F.; Tan, W. A novel coronavirus from patients with pneumonia in China, 2019. N. Engl. J. Med., 2020, 382(8), 727-733.
[http://dx.doi.org/10.1056/NEJMoa2001017] [PMID: 31978945]

Su, S.; Wong, G.; Shi, W.; Liu, J.; Lai, A.C.K.; Zhou, J.; Liu, W.; Bi, Y.; Gao, G.F. Epidemiology, genetic recombination, and pathogenesis of coronaviruses. Trends Microbiol., 2016, 24(6), 490-502.
[http://dx.doi.org/10.1016/j.tim.2016.03.003] [PMID: 27012512]

Tang, B.; Bragazzi, N.L.; Li, Q.; Tang, S.; Xiao, Y.; Wu, J. An updated estimation of the risk of transmission of the novel coronavirus (2019-nCov). Infect. Dis. Model., 2020, 5, 248-255.
[http://dx.doi.org/10.1016/j.idm.2020.02.001] [PMID: 32099934]

Xue, X.; Yu, H.; Yang, H.; Xue, F.; Wu, Z.; Shen, W.; Li, J.; Zhou, Z.; Ding, Y.; Zhao, Q.; Zhang, X.C.; Liao, M.; Bartlam, M.; Rao, Z. Structures of two coronavirus main proteases: Implications for substrate binding and antiviral drug design. J. Virol., 2008, 82(5), 2515-2527.
[http://dx.doi.org/10.1128/JVI.02114-07] [PMID: 18094151]

Al-Karmalawy, A.A.; Alnajjar, R.; Dahab, M.; Metwaly, A.; Eissa, I. Molecular docking and dynamics simulations reveal the potential of anti-HCV drugs to inhibit COVID-19 main protease. Ulum-i Daruyi, 2021, 10.
[http://dx.doi.org/10.34172/PS.2021.3]

Zhang, S.; Gao, C.; Das, T.; Luo, S.; Tang, H.; Yao, X.; Cho, C.Y.; Lv, J.; Maravillas, K.; Jones, V.; Chen, X.; Huang, R. The spike-ACE2 binding assay: an in vitro platform for evaluating vaccination efficacy and for screening SARS-CoV-2 inhibitors and neutralizing antibodies. J. Immunol. Methods, 2022, 503, 113244.
[http://dx.doi.org/10.1016/j.jim.2022.113244] [PMID: 35218866]

Zhang, Y.; Tang, L.V. Overview of targets and potential drugs of SARS-CoV-2 according to the viral replication. J. Proteome Res., 2021, 20(1), 49-59.
[http://dx.doi.org/10.1021/acs.jproteome.0c00526] [PMID: 33347311]

Rizzuti, B.; Grande, F.; Conforti, F.; Jimenez-Alesanco, A.; Ceballos-Laita, L.; Ortega-Alarcon, D.; Vega, S.; Reyburn, H.T.; Abian, O.; Velazquez-Campoy, A. Rutin is a low micromolar inhibitor of SARS-CoV-2 main protease 3CLpro: Implications for drug design of quercetin analogs. Biomedicines, 2021, 9(4), 375.
[http://dx.doi.org/10.3390/biomedicines9040375] [PMID: 33918402]

Pomplun, S. Targeting the SARS-CoV-2-spike protein: From antibodies to miniproteins and peptides. RSC Medicinal Chemistry., 2020, 12(2), 197-202.
[http://dx.doi.org/10.1039/D0MD00385A] [PMID: 34041482]

Wang, L.; Hu, W.; Fan, C. Structural and biochemical characterization of SADS-CoV papain-like protease 2. Protein Sci., 2020, 29(5), 1228-1241.
[http://dx.doi.org/10.1002/pro.3857] [PMID: 32216114]

Yoshida, M.; Kudo, N.; Kosono, S.; Ito, A. Chemical and structural biology of protein lysine deacetylases. Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci., 2017, 93(5), 297-321.
[http://dx.doi.org/10.2183/pjab.93.019] [PMID: 28496053]

Omidkhah, N.; Hadizadeh, F.; Ghodsi, R. Dual HDAC/BRD4 inhibitors against cancer. Med. Chem. Res., 2021, 1-15.

Zwergel, C.; Stazi, G.; Valente, S.; Mai, A. Histone deacetylase inhibitors: updated studies in various epigenetic-related diseases. J Clin Epigenetics., 2016, 2(1), 7.

Zagni, C.; Floresta, G.; Monciino, G.; Rescifina, A. The search for potent, small‐molecule HDACIs in cancer treatment: a decade after vorinostat. Med. Res. Rev., 2017, 37(6), 1373-1428.
[http://dx.doi.org/10.1002/med.21437] [PMID: 28181261]

Falkenberg, K.J.; Johnstone, R.W. Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders. Nat. Rev. Drug Discov., 2014, 13(9), 673-691.
[http://dx.doi.org/10.1038/nrd4360] [PMID: 25131830]

Kelly, W.K.; O’Connor, O.A.; Krug, L.M.; Chiao, J.H.; Heaney, M.; Curley, T.; MacGregore-Cortelli, B.; Tong, W.; Secrist, J.P.; Schwartz, L.; Richardson, S.; Chu, E.; Olgac, S.; Marks, P.A.; Scher, H.; Richon, V.M. Phase I study of an oral histone deacetylase inhibitor, suberoylanilide hydroxamic acid, in patients with advanced cancer. J. Clin. Oncol., 2005, 23(17), 3923-3931.
[http://dx.doi.org/10.1200/JCO.2005.14.167] [PMID: 15897550]

Stazi, G.; Fioravanti, R.; Mai, A.; Mattevi, A.; Valente, S. Histone deacetylases as an epigenetic pillar for the development of hybrid inhibitors in cancer. Curr. Opin. Chem. Biol., 2019, 50, 89-100.
[http://dx.doi.org/10.1016/j.cbpa.2019.03.002] [PMID: 30986654]

Coiffier, B.; Pro, B.; Prince, H.M.; Foss, F.; Sokol, L.; Greenwood, M.; Caballero, D.; Borchmann, P.; Morschhauser, F.; Wilhelm, M.; Pinter-Brown, L.; Padmanabhan, S.; Shustov, A.; Nichols, J.; Carroll, S.; Balser, J.; Balser, B.; Horwitz, S. Results from a pivotal, open-label, phase II study of romidepsin in relapsed or refractory peripheral T-cell lymphoma after prior systemic therapy. J. Clin. Oncol., 2012, 30(6), 631-636.
[http://dx.doi.org/10.1200/JCO.2011.37.4223] [PMID: 22271479]

Ueda, H.; Manda, T.; Matsumoto, S.; Mukumoto, S.; Nishigaki, F.; Kawamura, I.; Shimomura, K. FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968. III. Antitumor activities on experimental tumors in mice. J. Antibiot. (Tokyo), 1994, 47(3), 315-323.
[http://dx.doi.org/10.7164/antibiotics.47.315] [PMID: 8175484]

Novotny-Diermayr, V; Hart, S; Goh, K; Cheong, A; Ong, L; Hentze, H The oral HDAC inhibitor pracinostat (SB939) is efficacious and synergistic with the JAK2 inhibitor pacritinib (SB1518) in preclinical models of AML Blood Cancer J.,, 2012, 2(5), e69-e.2012.

Qiao, Z.; Ren, S.; Li, W.; Wang, X.; He, M.; Guo, Y.; Sun, L.; He, Y.; Ge, Y.; Yu, Q. Chidamide, a novel histone deacetylase inhibitor, synergistically enhances gemcitabine cytotoxicity in pancreatic cancer cells. Biochem. Biophys. Res. Commun., 2013, 434(1), 95-101.
[http://dx.doi.org/10.1016/j.bbrc.2013.03.059] [PMID: 23541946]

Zhang, D.; Damoiseaux, R.; Babayan, L.; Rivera-Meza, E.K.; Yang, Y.; Bergsneider, M.; Wang, M.B.; Yong, W.H.; Kelly, K.; Heaney, A.P. Targeting corticotroph HDAC and PI3-kinase in cushing disease. J. Clin. Endocrinol. Metab., 2021, 106(1), e232-e246.
[http://dx.doi.org/10.1210/clinem/dgaa699] [PMID: 33000123]

He, F.; Ran, Y.; Li, X.; Wang, D.; Zhang, Q.; Lv, J.; Yu, C.; Qu, Y.; Zhang, X.; Xu, A.; Wei, C.; Chou, C.J.; Wu, J. Design, synthesis and biological evaluation of dual-function inhibitors targeting NMDAR and HDAC for Alzheimer’s disease. Bioorg. Chem., 2020, 103, 104109.
[http://dx.doi.org/10.1016/j.bioorg.2020.104109] [PMID: 32768741]

Buonvicino, D.; Ranieri, G.; Chiarugi, A. Treatment with non-specific HDAC inhibitors administered after disease onset does not delay evolution in a mouse model of progressive multiple sclerosis. Neuroscience, 2021, 465, 38-45.
[http://dx.doi.org/10.1016/j.neuroscience.2021.04.002] [PMID: 33862148]

Mukhi, M.; Jai, J. Evaluating the potency of three plant compounds as HDAC Inhibitors for the treatment of Huntington’s disease: An in silico study. Int. J. Herb. Med., 2020, 8(5), 10-13.

Luan, Y.; Li, J.; Bernatchez, J.A.; Li, R. Kinase and histone deacetylase hybrid inhibitors for cancer therapy. J. Med. Chem., 2019, 62(7), 3171-3183.
[http://dx.doi.org/10.1021/acs.jmedchem.8b00189] [PMID: 30418766]

Omidkhah, N.; Ghodsi, R. NO-HDAC dual inhibitors. Eur. J. Med. Chem., 2022, 227, 113934.
[http://dx.doi.org/10.1016/j.ejmech.2021.113934] [PMID: 34700268]

Teodori, L.; Sestili, P.; Madiai, V.; Coppari, S.; Fraternale, D.; Rocchi, M.B.L.; Ramakrishna, S.; Albertini, M.C. MicroRNAs bioinformatics analyses identifying HDAC pathway as a putative target for existing Anti-COVID-19 therapeutics. Front. Pharmacol., 2020, 11, 582003.
[http://dx.doi.org/10.3389/fphar.2020.582003] [PMID: 33363465]

Kumar, V.; Jung, Y-S.; Liang, P-H. Anti-SARS coronavirus agents: a patent review (2008 - present). Expert Opin. Ther. Pat., 2013, 23(10), 1337-1348.
[http://dx.doi.org/10.1517/13543776.2013.823159] [PMID: 23905913]

Piechotta, V.; Iannizzi, C.; Chai, K.L.; Valk, S.J.; Kimber, C.; Dorando, E. Convalescent plasma or hyperimmune immunoglobulin for people with COVID-19: a living systematic review. Cochrane Database Syst. Rev., 2021, 5(5), CD013600.
[http://dx.doi.org/10.1002/14651858.CD013600.pub4] [PMID: 34013969]

Wang, Z.; Chen, X.; Lu, Y.; Chen, F.; Zhang, W. Clinical characteristics and therapeutic procedure for four cases with 2019 novel coronavirus pneumonia receiving combined Chinese and Western medicine treatment. Biosci. Trends, 2020, 14(1), 64-68.
[http://dx.doi.org/10.5582/bst.2020.01030] [PMID: 32037389]

Fan, Y.; Siklenka, K.; Arora, S.K.; Ribeiro, P.; Kimmins, S.; Xia, J. miRNet - dissecting miRNA-target interactions and functional associations through network-based visual analysis. Nucleic Acids Res., 2016, 44(W1), W135-41.
[http://dx.doi.org/10.1093/nar/gkw288] [PMID: 27105848]

Baek, D.; Villén, J.; Shin, C.; Camargo, F.D.; Gygi, S.P.; Bartel, D.P. The impact of micrornas on protein output nature. Nature, 2008, 455(7209), 64-71.
[http://dx.doi.org/10.1038/nature07242] [PMID: 18668037]

Oliveira, A.C.; Bovolenta, L.A.; Alves, L.; Figueiredo, L.; Ribeiro, A.O.; Campos, V.F.; Lemke, N.; Pinhal, D. Understanding the modus operandi of MicroRNA regulatory clusters. Cells, 2019, 8(9), 1103.
[http://dx.doi.org/10.3390/cells8091103] [PMID: 31540501]

Patel, A.B.; Verma, A. Nasal ACE2 levels and COVID-19 in children. JAMA, 2020, 323(23), 2386-2387.
[http://dx.doi.org/10.1001/jama.2020.8946] [PMID: 32432681]

El Baba, R.; Herbein, G. Management of epigenomic networks entailed in coronavirus infections and COVID-19. Clin. Epigenetics, 2020, 12(1), 118.
[http://dx.doi.org/10.1186/s13148-020-00912-7] [PMID: 32758273]

Liew, W.C.; Sundaram, G.M.; Quah, S.; Lum, G.G.; Tan, J.S.; Ramalingam, R.; Common, J.E.A.; Tang, M.B.Y.; Lane, E.B.; Thng, S.T.G.; Sampath, P. Belinostat resolves skin barrier defects in atopic dermatitis by targeting the dysregulated miR-335:SOX6 axis. J. Allergy Clin. Immunol., 2020, 146(3), 606-620.e12.
[http://dx.doi.org/10.1016/j.jaci.2020.02.007] [PMID: 32088305]

Alhazzani, W.; Møller, M.H.; Arabi, Y.M.; Loeb, M.; Gong, M.N.; Fan, E.; Oczkowski, S.; Levy, M.M.; Derde, L.; Dzierba, A.; Du, B.; Aboodi, M.; Wunsch, H.; Cecconi, M.; Koh, Y.; Chertow, D.S.; Maitland, K.; Alshamsi, F.; Belley-Cote, E.; Greco, M.; Laundy, M.; Morgan, J.S.; Kesecioglu, J.; McGeer, A.; Mermel, L.; Mammen, M.J.; Alexander, P.E.; Arrington, A.; Centofanti, J.E.; Citerio, G.; Baw, B.; Memish, Z.A.; Hammond, N.; Hayden, F.G.; Evans, L.; Rhodes, A. Surviving sepsis campaign: guidelines on the management of critically ill adults with Coronavirus Disease 2019 (COVID-19). Intensive Care Med., 2020, 46(5), 854-887.
[http://dx.doi.org/10.1007/s00134-020-06022-5] [PMID: 32222812]

Liu, K.; Zou, R.; Cui, W.; Li, M.; Wang, X.; Dong, J.; Li, H.; Li, H.; Wang, P.; Shao, X.; Su, W.; Chan, H.C.S.; Li, H.; Yuan, S. Clinical HDAC inhibitors are effective drugs to prevent the entry of SARS-CoV2. ACS Pharmacol. Transl. Sci., 2020, 3(6), 1361-1370.
[http://dx.doi.org/10.1021/acsptsci.0c00163] [PMID: 34778724]

Yang, L.P. Romidepsin: In the treatment of T-cell lymphoma. Drugs, 2011, 71(11), 1469-1480.
[http://dx.doi.org/10.2165/11207170-000000000-00000] [PMID: 21812508]

Bennion, C.; Brown, R.C.; Cook, A.R.; Manners, C.N.; Payling, D.W.; Robinson, D.H. Design, synthesis, and physicochemical properties of a novel, conformationally restricted 2,3-dihydro-1,3,4-thiadiazole-containing angiotensin converting enzyme inhibitor which is preferentially eliminated by the biliary route in rats. J. Med. Chem., 1991, 34(1), 439-447.
[http://dx.doi.org/10.1021/jm00105a066] [PMID: 1992145]

Coric, P.; Turcaud, S.; Meudal, H.; Roques, B.P.; Fournie-Zaluski, M-C. Optimal recognition of neutral endopeptidase and angiotensin-converting enzyme active sites by mercaptoacyldipeptides as a means to design potent dual inhibitors. J. Med. Chem., 1996, 39(6), 1210-1219.
[http://dx.doi.org/10.1021/jm950590p] [PMID: 8632427]

Corradi, H.R.; Schwager, S.L.; Nchinda, A.T.; Sturrock, E.D.; Acharya, K.R. Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design. J. Mol. Biol., 2006, 357(3), 964-974.
[http://dx.doi.org/10.1016/j.jmb.2006.01.048] [PMID: 16476442]

Li, F. Structural analysis of major species barriers between humans and palm civets for severe acute respiratory syndrome coronavirus infections. J. Virol., 2008, 82(14), 6984-6991.
[http://dx.doi.org/10.1128/JVI.00442-08] [PMID: 18448527]

Towler, P.; Staker, B.; Prasad, S.G.; Menon, S.; Tang, J.; Parsons, T.; Ryan, D.; Fisher, M.; Williams, D.; Dales, N.A.; Patane, M.A.; Pantoliano, M.W. ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. J. Biol. Chem., 2004, 279(17), 17996-18007.
[http://dx.doi.org/10.1074/jbc.M311191200] [PMID: 14754895]

Lyman, E.; Higgs, C.; Kim, B.; Lupyan, D.; Shelley, J.C.; Farid, R.; Voth, G.A. A role for a specific cholesterol interaction in stabilizing the Apo configuration of the human A(2A) adenosine receptor. Structure, 2009, 17(12), 1660-1668.
[http://dx.doi.org/10.1016/j.str.2009.10.010] [PMID: 20004169]

Di Paola, L.; Hadi-Alijanvand, H.; Song, X.; Hu, G.; Giuliani, A. The discovery of a putative allosteric site in the SARS-CoV-2 spike protein using an integrated structural/dynamic approach. J. Proteome Res., 2020, 19(11), 4576-4586.
[http://dx.doi.org/10.1021/acs.jproteome.0c00273] [PMID: 32551648]

Mohamed, M.F.; Abuo-Rahma, G.E-D.A.; Hayallah, A.M.; Aziz, M.A.; Nafady, A.; Samir, E. Molecular docking study reveals the potential repurposing of histone deacetylase inhibitors against COVID-19. Int. J. Pharm. Sci. Res., 2020, •••, 4261-4270.

Ziegler, C.G.; Allon, S.J.; Nyquist, S.K.; Mbano, I.M.; Miao, V.N.; Tzouanas, C.N. SARS-CoV-2 receptor ACE2 is an interferon-stimulated gene in human airway epithelial cells and is detected in specific cell subsets across tissues. Cell, 2020, 181(5), 1016-1035.e19.
[http://dx.doi.org/10.1016/j.cell.2020.04.035] [PMID: 32413319]

Liu, M.; Wang, T.; Zhou, Y.; Zhao, Y.; Zhang, Y.; Li, J. Potential role of ACE2 in coronavirus disease 2019 (COVID-19) prevention and management. J. Transl. Int. Med., 2020, 8(1), 9-19.
[http://dx.doi.org/10.2478/jtim-2020-0003] [PMID: 32435607]

Li, C.; Xu, B.H. The viral, epidemiologic, clinical characteristics and potential therapy options for COVID-19: a review. Eur. Rev. Med. Pharmacol. Sci., 2020, 24(8), 4576-4584.
[PMID: 32373998]

Fang, L.; Karakiulakis, G.; Roth, M. Are patients with hypertension and diabetes mellitus at increased risk for COVID-19 infection? Lancet Respir. Med., 2020, 8(4), e21.
[http://dx.doi.org/10.1016/S2213-2600(20)30116-8] [PMID: 32171062]

Mostafa-Hedeab, G. ACE2 as drug target of COVID-19 virus treatment, simplified updated review. Rep. Biochem. Mol. Biol., 2020, 9(1), 97-105.
[http://dx.doi.org/10.29252/rbmb.9.1.97] [PMID: 32821757]

Gue, Y.X.; Gorog, D.A. Reduction in ACE2 may mediate the prothrombotic phenotype in COVID-19. Eur. Heart J., 2020, 41(33), 3198-3199.
[http://dx.doi.org/10.1093/eurheartj/ehaa534] [PMID: 32691041]

Hoffmann, M.; Kleine-Weber, H.; Schroeder, S.; Krüger, N.; Herrler, T.; Erichsen, S. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell, 2020, 181(2), 271-280.e8.
[http://dx.doi.org/10.1016/j.cell.2020.02.052] [PMID: 32142651]

Bao, L.; Deng, W.; Huang, B.; Gao, H.; Liu, J.; Ren, L.; Wei, Q.; Yu, P.; Xu, Y.; Qi, F.; Qu, Y.; Li, F.; Lv, Q.; Wang, W.; Xue, J.; Gong, S.; Liu, M.; Wang, G.; Wang, S.; Song, Z.; Zhao, L.; Liu, P.; Zhao, L.; Ye, F.; Wang, H.; Zhou, W.; Zhu, N.; Zhen, W.; Yu, H.; Zhang, X.; Guo, L.; Chen, L.; Wang, C.; Wang, Y.; Wang, X.; Xiao, Y.; Sun, Q.; Liu, H.; Zhu, F.; Ma, C.; Yan, L.; Yang, M.; Han, J.; Xu, W.; Tan, W.; Peng, X.; Jin, Q.; Wu, G.; Qin, C. The pathogenicity of SARS-CoV-2 in hACE2 transgenic mice. Nature, 2020, 583(7818), 830-833.
[http://dx.doi.org/10.1038/s41586-020-2312-y] [PMID: 32380511]

Xiao, F.; Tang, M.; Zheng, X.; Liu, Y.; Li, X.; Shan, H. Evidence for gastrointestinal infection of SARS-CoV-2. Gastroenterology, 2020, 158(6), 1831-1833.e3.
[http://dx.doi.org/10.1038/s41586-020-2312-y] [PMID: 32380511]

Gérard, C.; Maggipinto, G.; Minon, J.M. COVID-19 and ABO blood group: another viewpoint. Br. J. Haematol., 2020, 190(2), e93-e94.
[http://dx.doi.org/10.1111/bjh.16884] [PMID: 32453863]

Li, J.; Wang, X.; Chen, J.; Cai, Y.; Deng, A.; Yang, M. Association between ABO blood groups and risk of SARS-CoV-2 pneumonia. Br. J. Haematol., 2020, 190(1), 24-27.
[http://dx.doi.org/10.1111/bjh.16797] [PMID: 32379894]

Takahashi, Y.; Hayakawa, A.; Sano, R.; Fukuda, H.; Harada, M.; Kubo, R.; Okawa, T.; Kominato, Y. Histone deacetylase inhibitors suppress ACE2 and ABO simultaneously, suggesting a preventive potential against COVID-19. Sci. Rep., 2021, 11(1), 3379.
[http://dx.doi.org/10.1038/s41598-021-82970-2] [PMID: 33564039]

Ellinghaus, D.; Degenhardt, F.; Bujanda, L.; Buti, M.; Albillos, A.; Invernizzi, P.; Fernández, J.; Prati, D.; Baselli, G.; Asselta, R.; Grimsrud, M.M.; Milani, C.; Aziz, F.; Kässens, J.; May, S.; Wendorff, M.; Wienbrandt, L.; Uellendahl-Werth, F.; Zheng, T.; Yi, X.; de Pablo, R.; Chercoles, A.G.; Palom, A.; Garcia-Fernandez, A.E.; Rodriguez-Frias, F.; Zanella, A.; Bandera, A.; Protti, A.; Aghemo, A.; Lleo, A.; Biondi, A.; Caballero-Garralda, A.; Gori, A.; Tanck, A.; Carreras Nolla, A.; Latiano, A.; Fracanzani, A.L.; Peschuck, A.; Julià, A.; Pesenti, A.; Voza, A.; Jiménez, D.; Mateos, B.; Nafria Jimenez, B.; Quereda, C.; Paccapelo, C.; Gassner, C.; Angelini, C.; Cea, C.; Solier, A.; Pestaña, D.; Muñiz-Diaz, E.; Sandoval, E.; Paraboschi, E.M.; Navas, E.; García Sánchez, F.; Ceriotti, F.; Martinelli-Boneschi, F.; Peyvandi, F.; Blasi, F.; Téllez, L.; Blanco-Grau, A.; Hemmrich-Stanisak, G.; Grasselli, G.; Costantino, G.; Cardamone, G.; Foti, G.; Aneli, S.; Kurihara, H.; ElAbd, H.; My, I.; Galván-Femenia, I.; Martín, J.; Erdmann, J.; Ferrusquía-Acosta, J.; Garcia-Etxebarria, K.; Izquierdo-Sanchez, L.; Bettini, L.R.; Sumoy, L.; Terranova, L.; Moreira, L.; Santoro, L.; Scudeller, L.; Mesonero, F.; Roade, L.; Rühlemann, M.C.; Schaefer, M.; Carrabba, M.; Riveiro-Barciela, M.; Figuera Basso, M.E.; Valsecchi, M.G.; Hernandez-Tejero, M.; Acosta-Herrera, M.; D’Angiò, M.; Baldini, M.; Cazzaniga, M.; Schulzky, M.; Cecconi, M.; Wittig, M.; Ciccarelli, M.; Rodríguez-Gandía, M.; Bocciolone, M.; Miozzo, M.; Montano, N.; Braun, N.; Sacchi, N.; Martínez, N.; Özer, O.; Palmieri, O.; Faverio, P.; Preatoni, P.; Bonfanti, P.; Omodei, P.; Tentorio, P.; Castro, P.; Rodrigues, P.M.; Blandino Ortiz, A.; de Cid, R.; Ferrer, R.; Gualtierotti, R.; Nieto, R.; Goerg, S.; Badalamenti, S.; Marsal, S.; Matullo, G.; Pelusi, S.; Juzenas, S.; Aliberti, S.; Monzani, V.; Moreno, V.; Wesse, T.; Lenz, T.L.; Pumarola, T.; Rimoldi, V.; Bosari, S.; Albrecht, W.; Peter, W.; Romero-Gómez, M.; D’Amato, M.; Duga, S.; Banales, J.M.; Hov, J.R.; Folseraas, T.; Valenti, L.; Franke, A.; Karlsen, T.H. Group SC-G. Genomewide association study of severe Covid-19 with respiratory failure. N. Engl. J. Med., 2020, 383(16), 1522-1534.
[http://dx.doi.org/10.1056/NEJMoa2020283] [PMID: 32558485]

Takahashi, Y.; Kubo, R.; Sano, R.; Nakajima, T.; Takahashi, K.; Kobayashi, M.; Handa, H.; Tsukada, J.; Kominato, Y. Histone deacetylase inhibitors suppress ABO transcription in vitro, leading to reduced expression of the antigens. Transfusion, 2017, 57(3), 554-562.
[http://dx.doi.org/10.1111/trf.13958] [PMID: 28019030]

He, B.; Garmire, L. Prediction of repurposed drugs for treating lung injury in COVID-19. F1000 Res., 2020, 9, 609.
[http://dx.doi.org/10.12688/f1000research.23996.2] [PMID: 32934806]

Sinha, S.; Cheng, K.; Aldape, K.; Schiff, E.; Ruppin, E. Systematic cell line-based identification of drugs modifying ACE2 expression. Preprints, 2020, 2020030446.
[http://dx.doi.org/10.20944/preprints202003.0446.v1]

Pitt, B.; Sutton, N.R.; Wang, Z.; Goonewardena, S.N.; Holinstat, M. Potential repurposing of the HDAC inhibitor valproic acid for patients with COVID-19. Eur. J. Pharmacol., 2021, 898, 173988.
[http://dx.doi.org/10.1016/j.ejphar.2021.173988] [PMID: 33667455]

Singh, S.; Singh, K. Valproic acid in prevention and treatment of covid-19. Authorea Preprints, 2020.

Cui, Q; Huang, C; Ji, X; Zhang, W; Zhang, F; Wang, L. Possible inhibitors of ACE2, the receptor of 2019-nCoV. 2020.

Fortson, W.S.; Kayarthodi, S.; Fujimura, Y.; Xu, H.; Matthews, R.; Grizzle, W.E.; Rao, V.N.; Bhat, G.K.; Reddy, E.S. Histone deacetylase inhibitors, valproic acid and trichostatin-A induce apoptosis and affect acetylation status of p53 in ERG-positive prostate cancer cells. Int. J. Oncol., 2011, 39(1), 111-119.
[PMID: 21519790]

Jin, J-M.; Bai, P.; He, W.; Wu, F.; Liu, X-F.; Han, D-M.; Liu, S.; Yang, J.K. Gender differences in patients with COVID-19: focus on severity and mortality. Front. Public Health, 2020, 8, 152.
[http://dx.doi.org/10.3389/fpubh.2020.00152] [PMID: 32411652]

Lucas, J.M.; Heinlein, C.; Kim, T.; Hernandez, S.A.; Malik, M.S.; True, L.D.; Morrissey, C.; Corey, E.; Montgomery, B.; Mostaghel, E.; Clegg, N.; Coleman, I.; Brown, C.M.; Schneider, E.L.; Craik, C.; Simon, J.A.; Bedalov, A.; Nelson, P.S. The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis. Cancer Discov., 2014, 4(11), 1310-1325.
[http://dx.doi.org/10.1158/2159-8290.CD-13-1010] [PMID: 25122198]

Shirato, K.; Kawase, M.; Matsuyama, S. Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2. J. Virol., 2013, 87(23), 12552-12561.
[http://dx.doi.org/10.1128/JVI.01890-13] [PMID: 24027332]

Cetinkaya, M.; Cansev, M.; Cekmez, F.; Tayman, C.; Canpolat, F.E.; Kafa, I.M.; Yaylagul, E.O.; Kramer, B.W.; Sarici, S.U. Protective effects of valproic acid, a histone deacetylase inhibitor, against hyperoxic lung injury in a neonatal rat model. PLoS One, 2015, 10(5), e0126028.
[http://dx.doi.org/10.1371/journal.pone.0126028] [PMID: 25938838]

Bambakidis, T.; Dekker, S.E.; Halaweish, I.; Liu, B.; Nikolian, V.C.; Georgoff, P.E.; Piascik, P.; Li, Y.; Sillesen, M.; Alam, H.B. Valproic acid modulates platelet and coagulation function ex vivo. Blood Coagul. Fibrinolysis, 2017, 28(6), 479-484.
[http://dx.doi.org/10.1097/MBC.0000000000000626] [PMID: 28230635]

Larsson, P.; Alwis, I.; Niego, B.; Sashindranath, M.; Fogelstrand, P.; Wu, M.C.; Glise, L.; Magnusson, M.; Daglas, M.; Bergh, N.; Jackson, S.P.; Medcalf, R.L.; Jern, S. Valproic acid selectively increases vascular endothelial tissue-type plasminogen activator production and reduces thrombus formation in the mouse. J. Thromb. Haemost., 2016, 14(12), 2496-2508.
[http://dx.doi.org/10.1111/jth.13527] [PMID: 27706906]

Olesen, J.B.; Abildstrøm, S.Z.; Erdal, J.; Gislason, G.H.; Weeke, P.; Andersson, C.; Torp-Pedersen, C.; Hansen, P.R. Effects of epilepsy and selected antiepileptic drugs on risk of myocardial infarction, stroke, and death in patients with or without previous stroke: A nationwide cohort study. Pharmacoepidemiol. Drug Saf., 2011, 20(9), 964-971.
[http://dx.doi.org/10.1002/pds.2186] [PMID: 21766386]

Dregan, A.; Charlton, J.; Wolfe, C.D.; Gulliford, M.C.; Markus, H.S. Is sodium valproate, an HDAC inhibitor, associated with reduced risk of stroke and myocardial infarction? A nested case-control study. Pharmacoepidemiol. Drug Saf., 2014, 23(7), 759-767.
[http://dx.doi.org/10.1002/pds.3651] [PMID: 24890032]

Brookes, R.L.; Crichton, S.; Wolfe, C.D.A.; Yi, Q.; Li, L.; Hankey, G.J.; Rothwell, P.M.; Markus, H.S. Sodium valproate, a histone deacetylase inhibitor, is associated with reduced stroke risk after previous ischemic stroke or transient ischemic attack. Stroke, 2018, 49(1), 54-61.
[http://dx.doi.org/10.1161/STROKEAHA.117.016674] [PMID: 29247141]

Panigada, M.; Bottino, N.; Tagliabue, P.; Grasselli, G.; Novembrino, C.; Chantarangkul, V.; Pesenti, A.; Peyvandi, F.; Tripodi, A. Hypercoagulability of COVID-19 patients in intensive care unit: a report of thromboelastography findings and other parameters of hemostasis. J. Thromb. Haemost., 2020, 18(7), 1738-1742.
[http://dx.doi.org/10.1111/jth.14850] [PMID: 32302438]

Greene, R.; Lind, S.; Jantsch, H.; Wilson, R.; Lynch, K.; Jones, R.; Carvalho, A.; Reid, L.; Waltman, A.C.; Zapol, W. Pulmonary vascular obstruction in severe ARDS: angiographic alterations after i.v. fibrinolytic therapy. AJR Am. J. Roentgenol., 1987, 148(3), 501-508.
[http://dx.doi.org/10.2214/ajr.148.3.501] [PMID: 3492876]

Manne, B.K.; Denorme, F.; Middleton, E.A.; Portier, I.; Rowley, J.W.; Stubben, C.; Petrey, A.C.; Tolley, N.D.; Guo, L.; Cody, M.; Weyrich, A.S.; Yost, C.C.; Rondina, M.T.; Campbell, R.A. Platelet gene expression and function in patients with COVID-19. Blood, 2020, 136(11), 1317-1329.
[http://dx.doi.org/10.1182/blood.2020007214] [PMID: 32573711]

Ackermann, M.; Verleden, S.E.; Kuehnel, M.; Haverich, A.; Welte, T.; Laenger, F.; Vanstapel, A.; Werlein, C.; Stark, H.; Tzankov, A.; Li, W.W.; Li, V.W.; Mentzer, S.J.; Jonigk, D. Pulmonary vascular endothelialitis, thrombosis, and angiogenesis in COVID-19. N. Engl. J. Med., 2020, 383(2), 120-128.
[http://dx.doi.org/10.1056/NEJMoa2015432] [PMID: 32437596]

Iizuka, N.; Morita, A.; Kawano, C.; Mori, A.; Sakamoto, K.; Kuroyama, M.; Ishii, K.; Nakahara, T. Anti-angiogenic effects of valproic acid in a mouse model of oxygen-induced retinopathy. J. Pharmacol. Sci., 2018, 138(3), 203-208.
[http://dx.doi.org/10.1016/j.jphs.2018.10.004] [PMID: 30409713]

Zhao, Y.; You, W.; Zheng, J.; Chi, Y.; Tang, W.; Du, R. Valproic acid inhibits the angiogenic potential of cervical cancer cells via HIF-1α/VEGF signals. Clin. Transl. Oncol., 2016, 18(11), 1123-1130.
[http://dx.doi.org/10.1007/s12094-016-1494-0] [PMID: 26942921]

Guo, T.; Fan, Y.; Chen, M.; Wu, X.; Zhang, L.; He, T.; Wang, H.; Wan, J.; Wang, X.; Lu, Z. Cardiovascular implications of fatal outcomes of patients with coronavirus disease 2019 (COVID-19). JAMA Cardiol., 2020, 5(7), 811-818.
[http://dx.doi.org/10.1001/jamacardio.2020.1017] [PMID: 32219356]

Arentz, M.; Yim, E.; Klaff, L.; Lokhandwala, S.; Riedo, F.X.; Chong, M.; Lee, M. Characteristics and outcomes of 21 critically ill patients with COVID-19 in Washington State. JAMA, 2020, 323(16), 1612-1614.
[http://dx.doi.org/10.1001/jama.2020.4326] [PMID: 32191259]

Scholz, B.; Schulte, J.S.; Hamer, S.; Himmler, K.; Pluteanu, F.; Seidl, M.D.; Stein, J.; Wardelmann, E.; Hammer, E.; Völker, U.; Müller, F.U. HDAC (histone deacetylase) inhibitor valproic acid attenuates atrial remodeling and delays the onset of atrial fibrillation in mice. Circ. Arrhythm. Electrophysiol., 2019, 12(3), e007071.
[http://dx.doi.org/10.1161/CIRCEP.118.007071] [PMID: 30879335]

Tian, S.; Lei, I.; Gao, W.; Liu, L.; Guo, Y.; Creech, J.; Herron, T.J.; Xian, S.; Ma, P.X.; Eugene Chen, Y.; Li, Y.; Alam, H.B.; Wang, Z. HDAC inhibitor valproic acid protects heart function through Foxm1 pathway after acute myocardial infarction. EBioMedicine, 2019, 39, 83-94.
[http://dx.doi.org/10.1016/j.ebiom.2018.12.003] [PMID: 30552062]

Lee, H-A.; Lee, D-Y.; Cho, H-M.; Kim, S-Y.; Iwasaki, Y.; Kim, I.K. Histone deacetylase inhibition attenuates transcriptional activity of mineralocorticoid receptor through its acetylation and prevents development of hypertension. Circ. Res., 2013, 112(7), 1004-1012.
[http://dx.doi.org/10.1161/CIRCRESAHA.113.301071] [PMID: 23421989]

Kang, S-H.; Seok, Y.M.; Song, M.J.; Lee, H-A.; Kurz, T.; Kim, I. Histone deacetylase inhibition attenuates cardiac hypertrophy and fibrosis through acetylation of mineralocorticoid receptor in spontaneously hypertensive rats. Mol. Pharmacol., 2015, 87(5), 782-791.
[http://dx.doi.org/10.1124/mol.114.096974] [PMID: 25667225]

Kee, H.J.; Sohn, I.S.; Nam, K.I.; Park, J.E.; Qian, Y.R.; Yin, Z.; Ahn, Y.; Jeong, M.H.; Bang, Y.J.; Kim, N.; Kim, J.K.; Kim, K.K.; Epstein, J.A.; Kook, H. Inhibition of histone deacetylation blocks cardiac hypertrophy induced by angiotensin II infusion and aortic banding. Circulation, 2006, 113(1), 51-59.
[http://dx.doi.org/10.1161/CIRCULATIONAHA.105.559724] [PMID: 16380549]

Kook, H.; Lepore, J.J.; Gitler, A.D.; Lu, M.M.; Wing-Man Yung, W.; Mackay, J.; Zhou, R.; Ferrari, V.; Gruber, P.; Epstein, J.A. Cardiac hypertrophy and histone deacetylase-dependent transcriptional repression mediated by the atypical homeodomain protein Hop. J. Clin. Invest., 2003, 112(6), 863-871.
[http://dx.doi.org/10.1172/JCI19137] [PMID: 12975471]

Mannaerts, I.; Nuytten, N.R.; Rogiers, V.; Vanderkerken, K.; van Grunsven, L.A.; Geerts, A. Chronic administration of valproic acid inhibits activation of mouse hepatic stellate cells in vitro and in vivo. Hepatology, 2010, 51(2), 603-614.
[http://dx.doi.org/10.1002/hep.23334] [PMID: 19957378]

Khan, S.; Jena, G.; Tikoo, K. Sodium valproate ameliorates diabetes-induced fibrosis and renal damage by the inhibition of histone deacetylases in diabetic rat. Exp. Mol. Pathol., 2015, 98(2), 230-239.
[http://dx.doi.org/10.1016/j.yexmp.2015.01.003] [PMID: 25576297]

Van Beneden, K.; Geers, C.; Pauwels, M.; Mannaerts, I.; Verbeelen, D.; van Grunsven, L.A.; Van den Branden, C. Valproic acid attenuates proteinuria and kidney injury. J. Am. Soc. Nephrol., 2011, 22(10), 1863-1875.
[http://dx.doi.org/10.1681/ASN.2010111196] [PMID: 21868496]

Kabel, A.M.; Omar, M.S.; Elmaaboud, M.A.A. Amelioration of bleomycin-induced lung fibrosis in rats by valproic acid and butyrate: Role of nuclear factor kappa-B, proinflammatory cytokines and oxidative stress. Int. Immunopharmacol., 2016, 39, 335-342.
[http://dx.doi.org/10.1016/j.intimp.2016.08.008] [PMID: 27526269]

Korfei, M.; Skwarna, S.; Henneke, I.; MacKenzie, B.; Klymenko, O.; Saito, S.; Ruppert, C.; von der Beck, D.; Mahavadi, P.; Klepetko, W.; Bellusci, S.; Crestani, B.; Pullamsetti, S.S.; Fink, L.; Seeger, W.; Krämer, O.H.; Guenther, A. Aberrant expression and activity of histone deacetylases in sporadic idiopathic pulmonary fibrosis. Thorax, 2015, 70(11), 1022-1032.
[http://dx.doi.org/10.1136/thoraxjnl-2014-206411] [PMID: 26359372]

Wu, C.; Li, A.; Leng, Y.; Li, Y.; Kang, J. Histone deacetylase inhibition by sodium valproate regulates polarization of macrophage subsets. DNA Cell Biol., 2012, 31(4), 592-599.
[http://dx.doi.org/10.1089/dna.2011.1401] [PMID: 22054065]

Jin, H.; Guo, X. Valproic acid ameliorates coxsackievirus-B3-induced viral myocarditis by modulating Th17/Treg imbalance. Virol. J., 2016, 13(1), 168.
[http://dx.doi.org/10.1186/s12985-016-0626-z] [PMID: 27724948]

Vázquez-Calvo, A.; Saiz, J-C.; Sobrino, F.; Martín-Acebes, M.A. Inhibition of enveloped virus infection of cultured cells by valproic acid. J. Virol., 2011, 85(3), 1267-1274.
[http://dx.doi.org/10.1128/JVI.01717-10] [PMID: 21106740]

Delgado, F.G.; Cárdenas, P.; Castellanos, J.E. Valproic acid downregulates cytokine expression in human macrophages infected with dengue virus. Diseases, 2018, 6(3), 59.
[http://dx.doi.org/10.3390/diseases6030059] [PMID: 29986388]

Wang, J.; Feng, H.; Zhang, J.; Jiang, H. Lithium and valproate acid protect NSC34 cells from H2O2-induced oxidative stress and upregulate expressions of SIRT3 and CARM1. Neuroendocrinol. Lett., 2013, 34(7), 648-654.
[PMID: 24464007]

D’Marco, L.; Puchades, M.J.; Romero-Parra, M.; Gimenez-Civera, E.; Soler, M.J.; Ortiz, A.; Gorriz, J.L. Coronavirus disease 2019 in chronic kidney disease. Clin. Kidney J., 2020, 13(3), 297-306.
[http://dx.doi.org/10.1093/ckj/sfaa104] [PMID: 32699615]

Wen, L.; Tang, K.; Chik, K.K-H.; Chan, C.C-Y.; Tsang, J.O-L.; Liang, R.; Cao, J.; Huang, Y.; Luo, C.; Cai, J.P.; Ye, Z.W.; Yin, F.; Chu, H.; Jin, D.Y.; Yuen, K.Y.; Yuan, S.; Chan, J.F. In silico structure-based discovery of a SARS-CoV-2 main protease inhibitor. Int. J. Biol. Sci., 2021, 17(6), 1555-1564.
[http://dx.doi.org/10.7150/ijbs.59191] [PMID: 33907519]

Case, D.A.; Cheatham, T.E., III; Darden, T.; Gohlke, H.; Luo, R.; Merz, K.M., Jr; Onufriev, A.; Simmerling, C.; Wang, B.; Woods, R.J. The Amber biomolecular simulation programs. J. Comput. Chem., 2005, 26(16), 1668-1688.
[http://dx.doi.org/10.1002/jcc.20290] [PMID: 16200636]

Gordon, J.C.; Myers, J.B.; Folta, T.; Shoja, V.; Heath, L.S.; Onufriev, A.H. ++: A server for estimating pKas and adding missing hydrogens to macromolecules. Nucleic Acids Res., 2005, 33(Suppl. 2), W368-71.
[http://dx.doi.org/10.1093/nar/gki464] [PMID: 15980491]

Raschka, S.; Wolf, A.J.; Bemister-Buffington, J.; Kuhn, L.A. Protein-ligand interfaces are polarized: discovery of a strong trend for intermolecular hydrogen bonds to favor donors on the protein side with implications for predicting and designing ligand complexes. J. Comput. Aided Mol. Des., 2018, 32(4), 511-528.
[http://dx.doi.org/10.1007/s10822-018-0105-2] [PMID: 29435780]

Zavodszky, M.I.; Sanschagrin, P.C.; Korde, R.S.; Kuhn, L.A. Distilling the essential features of a protein surface for improving protein-ligand docking, scoring, and virtual screening. J. Comput. Aided Mol. Des., 2002, 16(12), 883-902.
[http://dx.doi.org/10.1023/A:1023866311551] [PMID: 12825621]

You, W.; Steegborn, C. Structural basis of sirtuin 6 inhibition by the hydroxamate trichostatin A: Implications for protein deacylase drug development. J. Med. Chem., 2018, 61(23), 10922-10928.
[http://dx.doi.org/10.1021/acs.jmedchem.8b01455] [PMID: 30395713]

Vanhaecke, T.; Papeleu, P.; Elaut, G.; Rogiers, V. Trichostatin A-like hydroxamate histone deacetylase inhibitors as therapeutic agents: toxicological point of view. Curr. Med. Chem., 2004, 11(12), 1629-1643.
[http://dx.doi.org/10.2174/0929867043365099] [PMID: 15180568]

Blanchard, J.E.; Elowe, N.H.; Huitema, C.; Fortin, P.D.; Cechetto, J.D.; Eltis, L.D.; Brown, E.D. High-throughput screening identifies inhibitors of the SARS coronavirus main proteinase. Chem. Biol., 2004, 11(10), 1445-1453.
[http://dx.doi.org/10.1016/j.chembiol.2004.08.011] [PMID: 15489171]

Vuong, W.; Khan, M.B.; Fischer, C.; Arutyunova, E.; Lamer, T.; Shields, J. Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication. Nat. Commun., 2020, 11(1), 1-8.
[PMID: 31911652]

Zhu, Z.; Chu, H.; Wen, L.; Yuan, S.; Chik, K.K-H.; Yuen, T.T-T.; Yip, C.C.; Wang, D.; Zhou, J.; Yin, F.; Jin, D.Y.; Kok, K.H.; Yuen, K.Y.; Chan, J.F. Targeting SUMO modification of the non-structural protein 5 of Zika virus as a host-targeting antiviral strategy. Int. J. Mol. Sci., 2019, 20(2), 392.
[http://dx.doi.org/10.3390/ijms20020392] [PMID: 30658479]

Riva, L.; Yuan, S.; Yin, X.; Martin-Sancho, L.; Matsunaga, N.; Pache, L.; Burgstaller-Muehlbacher, S.; De Jesus, P.D.; Teriete, P.; Hull, M.V.; Chang, M.W.; Chan, J.F.; Cao, J.; Poon, V.K.; Herbert, K.M.; Cheng, K.; Nguyen, T.H.; Rubanov, A.; Pu, Y.; Nguyen, C.; Choi, A.; Rathnasinghe, R.; Schotsaert, M.; Miorin, L.; Dejosez, M.; Zwaka, T.P.; Sit, K.Y.; Martinez-Sobrido, L.; Liu, W.C.; White, K.M.; Chapman, M.E.; Lendy, E.K.; Glynne, R.J.; Albrecht, R.; Ruppin, E.; Mesecar, A.D.; Johnson, J.R.; Benner, C.; Sun, R.; Schultz, P.G.; Su, A.I.; García-Sastre, A.; Chatterjee, A.K.; Yuen, K.Y.; Chanda, S.K. Discovery of SARS-CoV-2 antiviral drugs through large-scale compound repurposing. Nature, 2020, 586(7827), 113-119.
[http://dx.doi.org/10.1038/s41586-020-2577-1] [PMID: 32707573]

Yuan, S.; Chan, J.F.W.; Chik, K.K.H.; Chan, C.C.Y.; Tsang, J.O.L.; Liang, R.; Cao, J.; Tang, K.; Chen, L.L.; Wen, K.; Cai, J.P.; Ye, Z.W.; Lu, G.; Chu, H.; Jin, D.Y.; Yuen, K.Y. Discovery of the FDA-approved drugs bexarotene, cetilistat, diiodohydroxyquinoline, and abiraterone as potential COVID-19 treatments with a robust two-tier screening system. Pharmacol. Res., 2020, 159, 104960.
[http://dx.doi.org/10.1016/j.phrs.2020.104960] [PMID: 32473310]

Tsang, J.O-L.; Zhou, J.; Zhao, X.; Li, C.; Zou, Z.; Yin, F.; Yuan, S.; Yeung, M.L.; Chu, H.; Chan, J.F. Development of three-dimensional human intestinal organoids as a physiologically relevant model for characterizing the viral replication kinetics and antiviral susceptibility of enteroviruses. Biomedicines, 2021, 9(1), 88.
[http://dx.doi.org/10.3390/biomedicines9010088] [PMID: 33477611]

Yuan, S.; Chan, C.C-Y.; Chik, K.K-H.; Tsang, J.O-L.; Liang, R.; Cao, J.; Tang, K.; Cai, J.P.; Ye, Z.W.; Yin, F.; To, K.K.; Chu, H.; Jin, D.Y.; Hung, I.F.; Yuen, K.Y.; Chan, J.F. Broad-spectrum host-based antivirals targeting the interferon and lipogenesis pathways as potential treatment options for the pandemic coronavirus disease 2019 (COVID-19). Viruses, 2020, 12(6), 628.
[http://dx.doi.org/10.3390/v12060628] [PMID: 32532085]

Yuan, S.; Chu, H.; Zhao, H.; Zhang, K.; Singh, K.; Chow, B.K.; Kao, R.Y.; Zhou, J.; Zheng, B.J. Identification of a small-molecule inhibitor of influenza virus via disrupting the subunits interaction of the viral polymerase. Antiviral Res., 2016, 125, 34-42.
[http://dx.doi.org/10.1016/j.antiviral.2015.11.005] [PMID: 26593979]

Chan, J.F-W.; Chik, K.K-H.; Yuan, S.; Yip, C.C-Y.; Zhu, Z.; Tee, K-M.; Tsang, J.O.; Chan, C.C.; Poon, V.K.; Lu, G.; Zhang, A.J.; Lai, K.K.; Chan, K.H.; Kao, R.Y.; Yuen, K.Y. Novel antiviral activity and mechanism of bromocriptine as a Zika virus NS2B-NS3 protease inhibitor. Antiviral Res., 2017, 141, 29-37.
[http://dx.doi.org/10.1016/j.antiviral.2017.02.002] [PMID: 28185815]

Salvador, L.A.; Luesch, H. Discovery and mechanism of natural products as modulators of histone acetylation. Curr. Drug Targets, 2012, 13(8), 1029-1047.
[http://dx.doi.org/10.2174/138945012802008973] [PMID: 22594471]

Hamze, A. How do we improve histone deacetylase inhibitor drug discovery?; Taylor & Francis, 2020, pp. 527-529.

Subramanian, S.; Bates, S.E.; Wright, J.J.; Espinoza-Delgado, I.; Piekarz, R.L. Clinical toxicities of histone deacetylase inhibitors. Pharmaceuticals (Basel), 2010, 3(9), 2751-2767.
[http://dx.doi.org/10.3390/ph3092751] [PMID: 27713375]