[1. C. Huang, Y. Wang, X. Li, L. Ren, J. Zhao, Y. Hu, L. Zhang, G. Fan, J. Xu and X. Gu, Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China, Lancet395 (2020) 497–506; https://doi.org/10.1016/S0140-673610.1016/S0140-6736(20)30183-5]Search in Google Scholar
[2. H. Lu, C. W. Stratton and Y. W. Tang, Outbreak of pneumonia of unknown etiology in Wuhan China: the mystery and the miracle, J. Med. Virol.92 (2020) 401–402; https://doi.org/10.1002/jmv.2567810.1002/jmv.25678716662831950516]Search in Google Scholar
[3. P. Colson, J. M. Rolain and D. Raoult, Chloroquine for the 2019 novel coronavirus SARS Cov2, Int. J. Antimicrob. Agents 55 (2020) Article ID 105923 (3 pages); https://doi.org/10.1016/j.ijantimicag.2020.10592310.1016/j.ijantimicag.2020.105923713486632070753]Search in Google Scholar
[4. M. Wang, R. Cao, L. Zhang, X. Yang, J. Liu, M. Xu, Z. Shi, Z. Hu, W. Zhong and G. Xiao, Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro, Cell Res.30 (2020) 269–271; https://doi.org/10.1038/s41422-020-0282-010.1038/s41422-020-0282-0705440832020029]Search in Google Scholar
[5. W. Ko, J. Rolain, N. Lee, P. Chen, C. Huang and P. Lee, Arguments in favour of remdesivir for treating SARS-CoV-2 infections, Int. J. Antimicrob. Agents (2020) Article ID 105933 (4 pages); https://doi.org/10.1016/j.ijantimicag.2020.10593310.1016/j.ijantimicag.2020.105933713536432147516]Search in Google Scholar
[6. N. Vankadari and J. A. Wilce, Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26, Emerg. Microbes Infect.9 (2020) 601–604; https://doi.org/10.1080/22221751.2020.173956510.1080/22221751.2020.1739565710371232178593]Search in Google Scholar
[7. W. Song, M. Gui, X. Wang and Y. Xiang, Cryo-EM structure of the SARS coronavirus spike glyco-protein in complex with its host cell receptor ACE2, PLoS Pathog.14 (2018) e1007236 (19 pages); https://doi.org/10.1371/journal.ppat.100723610.1371/journal.ppat.1007236610729030102747]Search in Google Scholar
[8. Y. Zhou, Y. Hou, J. Shen, Y. Huang, W. Martin and F. Cheng, Network-based drug repurposing for novel coronavirus 2019-nCoV/SARS-CoV-2, Cell Discov.6 (2020) 1–18; https://doi.org/10.1038/s41421-020-0153-310.1038/s41421-020-0153-3707333232194980]Search in Google Scholar
[9. A. A. Al-Qahtani, K. Lyroni, M. Aznaourova, M. Tseliou, M. R. Al-Anazi, M. N. Al-Ahdal, S. Alkahtani, G. Sourvinos and C. Tsatsanis, Middle east respiratory syndrome corona virus spike glycoprotein suppresses macrophage responses via DPP4-mediated induction of IRAK-M and PPARγ, Oncotarget8 (2017) 9053–9066; https://doi.org/10.18632/oncotarget.1475410.18632/oncotarget.14754535471428118607]Search in Google Scholar
[10. A. Makdissi, H. Ghanim, M. Vora, K. Green, S. Abuaysheh, A. Chaudhuri, S. Dhindsa and P. Dandona, Sitagliptin exerts an antinflammatory action, J. Clin. Endocrinol. Metab.97 (2012) 3333–3341; https://doi.org/10.1210/jc.2012-154410.1210/jc.2012-1544343158022745245]Search in Google Scholar
[11. J. R. Ussher and D. J. Drucker, Cardiovascular biology of the incretin system, Endocr. Rev.33 (2012) 187–215; https://doi.org/10.1210/er.2011-105210.1210/er.2011-1052352878522323472]Search in Google Scholar
[12. H. Yanai, Dipeptidyl peptidase-4 inhibitor sitagliptin significantly reduced hepatitis C virus replication in a diabetic patient with chronic hepatitis C virus infection, Hepatobiliary Pancreat. Dis. Int.13 (2014) 556; https://doi.org/10.1016/S1499-3872(14)60308-810.1016/S1499-3872(14)60308-8]Search in Google Scholar
[13. M. P. Dubé, E. S. Chan, J. E. Lake, B. Williams, J. Kinslow, A. Landay, R. W. Coombs, M. Floris-Moore, H. J. Ribaudo and K. E. Yarasheski, A randomized, double-blinded, placebo-controlled trial of sitagliptin for reducing inflammation and immune activation in treated and suppressed human immunodeficiency virus infection, Clin. Infect. Dis.69 (2019) 1165–1172; https://doi.org/10.1093/cid/ciy105110.1093/cid/ciy1051674381430535188]Search in Google Scholar
[14. M. Liao, Y. Liu, J. Yuan, Y. Wen, G. Xu, J. Zhao, L. Chen, J. Li, X. Wang, F. Wang, L. Liu, S. Zhang and Z. Zhang, The landscape of lung bronchoalveolar immune cells in COVID-19 revealed by single-cell RNA sequencing, medRxiv preprint, posted February 26, 2020 (23 pages); https://doi.org/10.1101/2020.02.23.2002669010.1101/2020.02.23.20026690]Search in Google Scholar
[15. P. Shannon, A. Markiel, O. Ozier, N. S. Baliga, J. T. Wang, D. Ramage, N. Amin, B. Schwikowski and T. Ideker, Cytoscape: a software environment for integrated models of biomolecular interaction networks, Genome Res.13 (2013) 2498–2504; https://doi.org/10.1101/gr.123930310.1101/gr.123930340376914597658]Search in Google Scholar
[16. D. Szklarczyk, A. L. Gable, D. Lyon, A. Junge, S. Wyder, J. Huerta-Cepas, M. Simonovic, N. T. Doncheva, J. H. Morris, P. Bork, L. J. Jensen and C. V. Mering, STRING v11: protein-protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets, Nucleic Acids Res.47 (2019) D607–D613; https://doi.org/10.1093/nar/gky113110.1093/nar/gky1131632398630476243]Search in Google Scholar
[17. A. Chatr-Aryamontri, A. Ceol, L. M. Palazzi, G. Nardelli, M. V. Schneider, L. Castagnoli and G. Cesareni, MINT: the Molecular INTeraction database, Nucleic Acids Res.35 (2007) D572–D574; https://doi.org/10.1093/nar/gkl95010.1093/nar/gkl950175154117135203]Search in Google Scholar
[18. S. Peri, J. D. Navarro, T. Z. Kristiansen, R. Amanchy, V. Surendranath, B. Muthusamy, T. Gandhi, K. Chandrika, N. Deshpande and S. Suresh, Human protein reference database as a discovery resource for proteomics, Nucleic Acids Res.32 (2004) D497–D501; https://doi.org/10.1093/nar/gkh07010.1093/nar/gkh07030880414681466]Search in Google Scholar
[19. R. Wang, X. Fang, Y. Lu and S. Wang, The PDBbind database: Collection of binding affinities for protein- ligand complexes with known three-dimensional structures, J. Med. Chem.47 (2004) 2977–2980; https://doi.org/10.1021/jm030580l10.1021/jm030580l15163179]Search in Google Scholar
[20. L. Salwinski, C. S. Miller, A. J. Smith, F. K. Pettit, J. U. Bowie and D. Eisenberg, The database of interacting proteins: 2004 update, Nucleic Acids Res.32 (2004) D449–D451; https://doi.org/10.1093/nar/gkh08610.1093/nar/gkh08630882014681454]Search in Google Scholar
[21. B. J. Breitkreutz, C. Stark, T. Reguly, L. Boucher, A. Breitkreutz, M. Livstone, R. Oughtred, D. H. Lackner, J. Bähler and V. Wood, The BioGRID interaction database: 2008 update, Nucleic Acids Res.36 (2008) D637–D640; https://doi.org/10.1093/nar/gkm100110.1093/nar/gkm1001223887318000002]Search in Google Scholar
[22. M. Kanehisa, M. Araki, S. Goto, M. Hattori, M. Hirakawa, M. Itoh, T. Katayama, S. Kawashima, S. Okuda and T. Tokimatsu, KEGG for linking genomes to life and the environment, Nucleic Acids Res.36 (2007) D480–D484; https://doi.org/10.1093/nar/gkm88210.1093/nar/gkm882]Search in Google Scholar
[23. D. Croft, A. F. Mundo, R. Haw, M. Milacic, J. Weiser, G. Wu, M. Caudy, P. Garapati, M. Gillespie and M. R. Kamdar, The Reactome pathway knowledgebase, Nucleic Acids Res.42 (2014) D472–D477; https://doi.org/10.1093/nar/gkt110210.1093/nar/gkt1102]Search in Google Scholar
[24. I. M. Keseler, J. Collado-Vides, S. Gama-Castro, J. Ingraham, S. Paley, I. T. Paulsen, M. Peralta-Gil and P. D. Karp, EcoCyc: a comprehensive database resource for Escherichia coli, Nucleic Acids Res.33 (2005) D334–D337; https://doi.org/10.1093/nar/gkq114310.1093/nar/gkq1143]Search in Google Scholar
[25. S. Krupa, K. Anthony, J. Buchoff, M. Day, T. Hannay and C. Schaefer, Pathway Interaction Database: A cell signaling resource, Nature446 (2007) 153–158; https://doi.org/10.1038/npre.2007.1311.110.1038/npre.2007.1311.1]Search in Google Scholar
[26. Gene Ontology Consortium, The Gene Ontology (GO) database and informatics resource, Nucleic Acids Res.32 (2004) D258–D261; https://doi.org/10.1093/nar/gkh03610.1093/nar/gkh036]Search in Google Scholar
[27. D. Kim, L. Wang, M. Beconi, G. J. Eiermann, M. H. Fisher, H. He, G. J. Hickey, J. E. Kowalchick, B. Leiting and K. Lyons, (2R)-4-oxo-4-[3-(trifluoromethyl)-5,6-dihydro[1,2,4]triazolo[4,3-a] pyrazin-7(8H)-yl]-1-(2,4,5-trifluorophenyl)butan-2-amine: a potent, orally active dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes, J. Med. Chem.48 (2005) 141–151; https://doi.org/10.1021/jm049315610.1021/jm0493156]Search in Google Scholar
[28. H. Berman, K. Henrick and H. Nakamura, Announcing the worldwide protein data bank, Nat. Struct. Mol. Biol.10 (2003) 980; https://doi.org/10.1038/nsb1203-98010.1038/nsb1203-980]Search in Google Scholar
[29. R. Lu, X. Zhao, J. Li, P. Niu, B. Yang, H. Wu, W. Wang, H. Song, B. Huang and N. Zhu, Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding, Lancet395 (2020) 565–574; https://doi.org/10.1016/S0140-6736(20)30251-810.1016/S0140-6736(20)30251-8]Search in Google Scholar
[30. M. Hoffmann, H. Kleine-Weber, N. Krüger, M. Mueller, C. Drosten and S. Pöhlmann, The novel coronavirus 2019 (2019-nCoV) uses the SARS-coronavirus receptor ACE2 and the cellular protease TMPRSS2 for entry into target cells, bioRxiv preprint, posted January 31, 2020 (23 pages); https://doi.org/10.1101/2020.01.31.92904210.1101/2020.01.31.929042]Search in Google Scholar
[31. X. Zou, K. Chen, J. Zou, P. Han, J. Hao and Z. Han, Single-cell RNA-seq data analysis on the receptor ACE2 expression reveals the potential risk of different human organs vulnerable to 2019-nCoV infection, Front. Med. (2020) (8 pages); https://doi.org/10.1007/s11684-020-0754-010.1007/s11684-020-0754-0708873832170560]Search in Google Scholar
[32. F. Qi, S. Qian, S. Zhang and Z. Zhang, Single cell RNA sequencing of 13 human tissues identify cell types and receptors of human coronaviruses, Biochem. Biophys. Res. Commun. (2020) (7 pages); https://doi.org/10.1016/j.bbrc.2020.03.04410.1016/j.bbrc.2020.03.044715611932199615]Search in Google Scholar
[33. M. Abouelkheir and T. H. El-Metwally, Dipeptidyl peptidase-4 inhibitors can inhibit angiotensin converting enzyme, Eur. J. Pharmacol.862 (2019) Article ID 172638; https://doi.org/10.1016/j.ejphar.2019.17263810.1016/j.ejphar.2019.17263831491403]Search in Google Scholar
[34. A. S. Rose, A. R. Bradley, Y. Valasatava, L. M. Duarte, A. Prlić and P. W. Rose, NGL viewer: web-based molecular graphics for large complexes, Bioinformatics34 (2018) 3755–3758; https://doi.org/10.1093/bioinformatics/bty41910.1093/bioinformatics/bty419619885829850778]Search in Google Scholar
[35. N. Yang and H.-M. Shen, Targeting the endocytic pathway and autophagy process as a novel therapeutic strategy in COVID-19, Int. J. Biol. Sci.16 (2020) 1724–1731; https://doi.org/10.7150/ijbs.4549810.7150/ijbs.45498709802732226290]Search in Google Scholar
[36. H. Wang, P. Yang, K. Liu, F. Guo, Y. Zhang, G. Zhang and C. Jiang, SARS coronavirus entry into host cells through a novel clathrin-and caveolae-independent endocytic pathway, Cell Res.18 (2008) 290–301; https://doi.org/10.1038/cr.2008.1510.1038/cr.2008.15709189118227861]Search in Google Scholar
[37. Y. Inoue, N. Tanaka, Y. Tanaka, S. Inoue, K. Morita, M. Zhuang, T. Hattori and K. Sugamura, Clathrin-dependent entry of severe acute respiratory syndrome coronavirus into target cells expressing ACE2 with the cytoplasmic tail deleted, J. Virol.81 (2007) 8722–8729; https://doi.org/10.1128/JVI.00253-0710.1128/JVI.00253-07195134817522231]Search in Google Scholar
[38. C. Callebaut, B. Krust, E. Jacotot and A. G. Hovanessian, T cell activation antigen, CD26, as a cofactor for entry of HIV in CD4+ cells, Science262 (1993) 2045–2050; https://doi.org/10.1126/science.790347910.1126/science.79034797903479]Search in Google Scholar