[1. Y. Li, J. Geng, Y. Liu, S. Yu and G. Zhao, Thiadiazole – a promising structure in medicinal chemistry, ChemMedChem8 (2013) 27–41; https://doi.org/10.1002/cmdc.20120035510.1002/cmdc.20120035523208773]Search in Google Scholar
[2. T. L. Lemke, Antiparasitic Agents, in Foye’s Principles of Medicinal Chemistry (Eds. T. L. Lemke, D. A. Williams, V. F. Roche and S. W. Zito), 7th ed., Lippincott Williams and Wilkins, Baltimore 2013, pp.1126.]Search in Google Scholar
[3. World Health Organization, Neglected Tropical Diseases. Prevention, Control, Elimination and Eradication, Sixty-six world health assembly A66/20, Provisional agenda item 16.2, 15 March 2013; https://www.who.int/neglected_diseases/A66_20_Eng.pdf; last access date: March 27, 2019]Search in Google Scholar
[4. P. J. Hotez, The Neglected Tropical Diseases and the Neglected Infections of Poverty: Overview of Their Common Features, Global Disease Burden and Distribution, New Control Tools, and Prospects for Disease Elimination, in Institute of Medicine (US) Forum on Microbial Threats. The Causes and Impacts of Neglected Tropical and Zoonotic Diseases: Opportunities for Integrated Intervention Strategies, National Academies Press, Washington (DC) 2011, A7; last access date March 27, 2019]Search in Google Scholar
[5. D. Molyneux, Neglected tropical diseases, Community Eye Health J. 26 (2013) 21–24.]Search in Google Scholar
[6. T. Furst, P. Salari, L. M. Llamas, P. Steinmann, C. Fitzpatrick and F. Tediosi, Global health policy and neglected tropical diseases: then, now and in the years to come, PLoS Negl. Trop. Dis. 11 (2017) e0005759; https://doi.org/10.1371/journal.pntd.000575910.1371/journal.pntd.0005759559892828910281]Search in Google Scholar
[7. F. Pourrajab, S. K. Forouzannia and S. A. Tabatabaee, Novel immunomodulatory function of 1,3,4-thiadiazole derivatives with leishmanicidal activity, J. Antimicrob. Chemother.67 (2012) 1968–1978; https://doi.org/10.1093/jac/dks14410.1093/jac/dks14422581907]Search in Google Scholar
[8. J. A. Joule, Natural Products Containing Nitrogen Heterocycles – Some Highlights 1990-2015, in Advances in Heterocyclic Chemistry: Heterocyclic Chemistry in the 21st Century – A Tribute to Alan Katritzky (Eds. E. F. V. Scriven and C. A. Ramsden), 1st ed., Academic Press, Cambridge (MA) 2016, Vol. 119, pp. 81–106.10.1016/bs.aihch.2015.10.005]Search in Google Scholar
[9. S. B. A. M. W. Van den Broek, S. A. Meeuwissen, F. L. van Delft and F. P. J. T. Rutjes, Natural Products Containing Medium-Sized Nitrogen Heterocycles Synthesized by Ring-Closing Alkene Metathesis, in Metathesis in Natural Product Synthesis: Strategies, Substrates and Catalysts (Eds. J. Cossy, S. Arseniyadis and C. Meyer), Wiley-VCH, Weinheim 2010, pp. 45–85.10.1002/9783527629626.ch2]Search in Google Scholar
[10. F. Diaba, J. A.Montiel, G. Serban and J. Bonjoch, Synthesis of normorphans through an efficient intramolecular carbamoylation of ketones, Org. Lett.17 (2015) 3860–3863; https://doi.org/10.1021/acs.orglett.5b0183210.1021/acs.orglett.5b0183226197207]Search in Google Scholar
[11. G. Serban, H. Abe and Y. Takeuchi, Synthetic studies of substituted pyridine aldehydes as intermediates for the synthesis of toddaquinoline, its derivatives and other natural products, Heterocycles83 (2011) 1989–2000; https://doi.org/10.3987/COM-11-1223910.3987/COM-11-12239]Search in Google Scholar
[12. G. Serban, H. Abe, Y. Takeuchi and T. Harayama, A new approach to the benzopyridoxepine core by metal mediated intramolecular biaryl ether formation, Heterocycles75 (2008) 2949–2958; https://doi.org/10.3987/COM-08-1144310.3987/COM-08-11443]Search in Google Scholar
[13. G. Serban, Y. Shigeta, H. Nishioka, H. Abe, Y. Takeuchi and T. Harayama, Studies toward the synthesis of toddaquinoline by intramolecular cyclization, Heterocycles71 (2007) 1623–1630; https://doi.org/10.3987/COM-07-1106210.3987/COM-07-11062]Search in Google Scholar
[14. D. Sole, F. Diaba and J. Bonjoch, Nitrogen heterocycles by palladium-catalyzed cyclization of amino-tethered vinyl halides and ketone enolates, J. Org. Chem.68 (2003) 5746–5749; https://doi.org/10.1021/jo034299q10.1021/jo034299q12839475]Search in Google Scholar
[15. B. Bradshaw, C. Parra and J. Bonjoch, Organocatalyzed asymmetric synthesis of morphans, Org. Lett.15 (2013) 2458–2461; https://doi.org/10.1021/ol400926p10.1021/ol400926p23627688]Search in Google Scholar
[16. P. K. Shukla, A. Verma and P. Mishra, Significance of Nitrogen Heterocyclic Nuclei in the Search of Pharmacological Active Compounds, in New Perspective in Agricultural and Human Health (Eds. R. P. Shukla, R. S. Mishra, A. D. Tripathi, A. K. Yadav, M. Tiwari and R. R. Mishra), Bharti Publication, New Delhi 2017, pp. 100–126.]Search in Google Scholar
[17. P. Martins, J. Jesus, S. Santos, L. R. Raposo, C. Roma-Rodrigues, P. V. Baptista and A. R. Fernandes, Heterocyclic anticancer compounds: recent advances and the paradigm shift towards the use of nanomedicine’s tool box, Molecules20 (2015) 16852–16891; https://doi.org/10.3390/molecules20091685210.3390/molecules200916852633190026389876]Search in Google Scholar
[18. The Top 200 Drugs of 2019; https://clincalc.com/DrugStats/Top200Drugs.aspx; last access date March 29, 2019]Search in Google Scholar
[19. A. V. Fuentes, M. D. Pineda and K. C. N. Venkata, Comprehension of top 200 prescribed drugs in the US as a resource for pharmacy teaching, training and practice, Pharmacy6 (2018) 43–52; https://doi.org/10.3390/pharmacy602004310.3390/pharmacy6020043602500929757930]Search in Google Scholar
[20. Antiparasitic Drugs (Antiprotozoal Drugs, Nitazoxanide and Ivermectin); https://www.tm.mahidol.ac.th/pediatrics/?q=Antiparasitic-drugs; last access date July 12, 2019]Search in Google Scholar
[21. J. Keiser, K. Ingram and J. Utzinger, Antiparasitic drugs for paediatrics: systemic review, formulations, pharmacokinetcs, safety, efficacy and implications for control, Parasitology138 (2011) 1620–1632; https://doi.org/10.1017/S003118201100002310.1017/S003118201100002321349223]Search in Google Scholar
[22. F. Castelli, L. R. Tomasoni and A. Matteelli, Advances in treatment of malaria, Mediterr. J. Hematol. Infect. Dis.4 (2012) e2012064;https://doi.org/10.4084/MJHID.2012.06410.4084/mjhid.2012.064]Search in Google Scholar
[23. S. Rajapakse, P. Weeratunga, C. Rodrigo, N. L. de Silva and S. D. Fernando, Prophylaxis of human toxoplasmosis: a systematic review, Pathog. Glob. Health111 (2017) 333–342; https://doi.org/10.1080/20477724.2017.137052810.1080/20477724.2017.1370528569488628948861]Search in Google Scholar
[24. M. Yoosefian, Z. J. Chermahini, H. Raissi, A. Mola and M. Sadeghi, A theoretical study on the structure of 2-amino-1,3,4-thiadiazole and its 5-substituted derivatives in the gas phase, water, THF and DMSO solutions, J. Mol. Liq.203 (2015) 137–142; https://doi.org/10.1016/j.molliq.2015.01.00210.1016/j.molliq.2015.01.002]Search in Google Scholar
[25. K. M. Dawood and T. A. Farghaly, Thiadiazole inhibitors: a patent review, Expert Opin. Ther. Pat.27 (2017) 477–505; https://doi.org/10.1080/13543776.2017.127257510.1080/13543776.2017.127257527976971]Search in Google Scholar
[26. S. Haider, M. S. Alam and H. Hamid, 1,3,4-Thiadiazoles: a potent multi targeted pharmacological scaffold, Eur. J. Med. Chem.92 (2015) 156–177; https://doi.org/10.1016/j.ejmech.2014.12.03510.1016/j.ejmech.2014.12.03525553540]Search in Google Scholar
[27. G. Serban, O. Stanasel, E. Serban and S. Bota, 2-Amino-1,3,4-thiadiazole as a potential scaffold for promising antimicrobial agents, Drug Des. Devel. Ther.12 (2018) 1545–1566; https://doi.org/10.2147/DDDT.S15595810.2147/DDDT.S155958598778729910602]Search in Google Scholar
[28. M. G. Yang, T. G. M. Dhar, Z. Xiao, H. Y. Xiao, J. J. W. Duan, B. Jiang, M. A. Galella, M. Cunningham, J. Wang, S. Habte, D. Shuster, K. W. McIntyre, J. Carman, D. A. Holloway, J. E. Somerville, S. G. Nadler, L. Salter-Cid, J. C. Barrish and D. S. Weinstein, Improving the pharmacokinetic and CYP inhibition profiles of azaxanthene-based glucocorticoid receptor modulators – Identification of (S)-5-(2-(9-fluoro-2-(4-(2-hydroxypropan-2-yl)phenyl)-5H-chromeno[2,3-b]pyridin-5-yl)-2-methylpropan amido)-N-(tetrahydro-2H-pyran-4-yl)-1,3,4-thiadiazole-2-carboxamide (BMS-341), J. Med. Chem.58 (2015) 4278–4290; https://doi.org/10.1021/acs.jmedchem.5b0025710.1021/acs.jmedchem.5b00257]Search in Google Scholar
[29. Y. J. Wu, Five-membered ring systems: with N and S atom, in Progress in Heterocyclic Chemistry (Eds. G. W. Gribble and J. A. Joule), Elsevier, Amsterdam 2017, Vol. 29, pp. 315–335.10.1016/B978-0-08-102310-5.00009-6]Search in Google Scholar
[30. R. Sink, I. Sosic, M. Zivec, R. Fernandez-Menendez, S. Turk, S. Pajk, D. Alvarez-Gomez, E. M. Lopez-Roman, C. Gonzales-Cortez, J. Rullas-Triconado, I. Angulo-Barturen, D. Barros, L. Ballell-Pages, R. J. Young, L. Encinas and S. Gobec, Design, synthesis and evaluation of new thiadiazole based direct inhibitors of enoyl acyl carrier protein reductase (InhA) for the treatment of tuberculosis, J. Med. Chem.58 (2015) 613–624;https://doi.org/10.1021/jm501029r10.1021/jm501029r]Search in Google Scholar
[31. F. Hipler, M. Winter and R. A. Fischer, N-H…S hydrogen bonding in 2-mercapto-5-methyl-1,3,4-thiadiazole. Synthesis and crystal structures of mercapto functionalized 1,3,4-thiadiazoles, J. Mol. Struct.658 (2003) 179–191; https://doi.org/10.1016/S0022-2860(03)00386-710.1016/S0022-2860(03)00386-7]Search in Google Scholar
[32. Y. Hu, C. Y. Li, X. M. Wang, Y. H. Yang and H. L. Zhu, 1,3,4-Thiadiazole: synthesis, reactions and applications in medicinal, agricultural, and materials chemistry, Chem. Rev.114 (2014) 5572–5610; https://doi.org/10.1021/cr400131u10.1021/cr400131u24716666]Search in Google Scholar
[33. A. T. Balaban, D. C. Oniciu and A. R. Katritzky, Aromaticity as a cornerstone of heterocyclic chemistry, Chem. Rev.104 (2004) 2777–2812;https://doi.org/10.1021/cr030679010.1021/cr030679015137807]Search in Google Scholar
[34. G. Kornis, Five-membered Rings with More than Two Heteroatoms and Fused Carbocyclic Derivatives, in Comprehensive Heterocyclic Chemistry II (Eds. A. R. Katritzky, C. W. Rees and E. F. V. Scriven), Elsevier, Oxford 1996, Volume 4, pp. 379–408.]Search in Google Scholar
[35. A. Senff-Ribeiro, A. Echevarria, E. F. Silva, C. R. C. Franco, S. S. Veiga and M. B. M. Oliveira, Cytotoxic effect of a new 1,3,4-thiadiazolium mesoionic compound (MI-D) on cell lines of human mellanoma, Br. J. Cancer91 (2004) 297–304; https://doi.org/10.1038/sj.bjc.660194610.1038/sj.bjc.6601946240979915199390]Search in Google Scholar
[36. M. M. Ciotti, S. R. Humphreys, J. M. Venditti, N. O. Kaplan and A. Goldin, The antileukemic action of two thiadiazole derivatives, Cancer Res.20 (1960) 1195–1201.]Search in Google Scholar
[37. M. Juszczak, J. Matysiak, W. Brzana, A. Niewiadomy and W. Rzeski, Evaluation of antiproliferative activity of 2-(monohalogenophenylamino)-5-(2, 4-dihydroxyphenyl)-1,3,4-thiadiazoles, Arzneim. Forsch. Drug Res.58 (2008) 353–357; https://doi.org/10.1055/s-0031-129651910.1055/s-0031-129651918751502]Search in Google Scholar
[38. J. Matysiak, Evaluation of antiproliferative effect in vitro of some 2-amino-5-(2, 4-dihydroxyphenyl)-1,3,4-thiadiazole derivatives, Chem. Pharm. Bull.54 (2006) 988–991; https://doi.org/10.1248/cpb.54.98810.1248/cpb.54.98816819217]Search in Google Scholar
[39. J. Matysiak and A. Opolski, Synthesis and antiproliferative activity of N-substituted 2-amino-5-(2,4-dihydroxyphenyl)-1,3,4-thiadiazoles, Bioorg. Med. Chem.14 (2006) 4483–4489; https://doi.org/10.1016/j.bmc.2006.02.02710.1016/j.bmc.2006.02.02716517170]Search in Google Scholar
[40. W. Rzeski, J. Matysiak and M. Kandefer-Szerszen, Anticancer, neuroprotective activities and computational studies of 2-amino-1,3,4-thiadiazole based compound, Bioorg. Med.Chem.15 (2007) 3201–3207; https://doi.org/10.1016/j.bmc.2007.02.04110.1016/j.bmc.2007.02.041]Search in Google Scholar
[41. R. Asbury, J. A. Blessing and D. Moore, A phase II trial of aminothiadiazole in patients with mixed mesodermal tumors of the uterine corpus: a gynecologic oncology group study, Am. J. Clin. Oncol.19 (1996) 400–402.]Search in Google Scholar
[42. P. L. Elson, L. K. Kvols, S. E. Vogl, D. J. Glover, R. G. Hahn and D. L. Trump, Phase II trials of 5-day vinblastine infusion (NSC 49842), L-alanosine (NSC153353), acivicin (NSC 163501), and aminothiadiazole (NSC 4728) in patients with recurrent or metastatic renal cell carcinoma, Invest. New Drugs6 (1988) 97–103.10.1007/BF00195367]Search in Google Scholar
[43. P. F. Engstrom, L. M. Ryan, G. Falkson and D. G. Haller, Phase II study of aminothiadiazole in advanced squamous cell carcinoma of the esophagus, Am. J. Clin. Oncol.14 (1991) 33–35.10.1097/00000421-199102000-00007]Search in Google Scholar
[44. G. Y. Locker, L. Kilton, J. D. Khandekar, T. E. Lad, R. H. Knop, K. Albain, R. Blough, S. French and A. B. Benson, High-dose aminothiadiazole in advanced colorectal cancer. An Illinois Cancer Center phase II trial, Invest. New Drugs12 (1994) 299–301.10.1007/BF00873044]Search in Google Scholar
[45. I. H. Krakoff, Purine metabolism in the chick embryo: influence of 2-substituted thiadiazoles, Biochem. Pharmacol. 13 (1964) 449–459; https://doi.org/10.1016/0006-2952(64)90165-010.1016/0006-2952(64)90165-0]Search in Google Scholar
[46. H. F. Oettgen, J. A. Reppert, V. Coley and J. H. Burchenal, Effects of nicotinamide and related compounds on the antileukemic activity of 2-amino-1,3,4-thiadiazole, Cancer Res. 20 (1960) 1597–1601.]Search in Google Scholar
[47. D. M. Shapiro, M. E. Shils, R. A. Fugmann andI. M. Friedland, Quantitative biochemical differences between tumor and host as a basis for cancer chemotherapy IV. Niacin and 2-ethylamino-1,3,4-thiadiazole, Cancer Res. 17 (1957) 29–33.]Search in Google Scholar
[48. G. Serban, Future prospects in the treatment of parasitic diseases: 2-amino-1,3,4-thiadiazoles in leishmaniasis, Molecules24 (2019) 1557–1578; https://doi.org/10.3390/molecules2408155710.3390/molecules24081557651467331010226]Search in Google Scholar
[49. G. Serban, 5-Arylamino-1,3,4-thiadiazol-2-yl acetic acid esters as intermediates for the synthesis of new bisheterocyclic compounds, Farmacia63 (2015) 146–149.]Search in Google Scholar
[50. T. Horvath, G. Serban and S. Cuc, Synthesis of new 2-phenylamino-5-[(α-acylamino)-p-X-stiryl]-1,3,4-thiadiazole compounds, Farmacia62 (2014) 422–427.]Search in Google Scholar
[51. G. Serban, A. Suciu, M. Coman and E. Curea, Synthesis and physical-chemical study of some 3-(5-arylamino-1,3,4-thiadiazol-2-yl)coumarins, Farmacia50 (2002) 50–54.]Search in Google Scholar
[52. G. Serban, M. Coman and E. Curea, Synthesis of some heterocyclic nitrocoumarins by Knoevenagel condensation, Farmacia53 (2005) 78–84.]Search in Google Scholar
[53. G. Serban, D. Matinca, O. Bradea, L. Gherman, M. Coman and E. Curea, The study of the biological activity of some heterocyclic coumarins, Farmacia53 (2005) 91–99.]Search in Google Scholar
[54. G. Serban, M. Coman, E. Curea and L. Proinov, Synthesis and description of some heterocyclic coumarins, Farmacia49 (2001) 45–52.]Search in Google Scholar
[55. World Health Organization, Integrating Neglected Tropical Diseases Into Global Health and Development: Fourth WHO Report on Neglected Tropical Diseases, WHO, Geneva, 19 April 2017, licence: CC BY-NC-SA 3.0 IGO; https://apps.who.int/iris/bitstream/handle/10665/255011/9789241565448-eng.pdf;jsessionid=9AA10810B00430B8A67751281F4AEFDD?sequence=1; last access date March 27, 2019]Search in Google Scholar
[56. World Health Organization, WHO Dept. of Control of Neglected Tropical Diseases, Working to Overcome the Global Impact of Neglected Tropical Diseases: First WHO Report on Neglected Tropical Diseases, WHO Press, Geneva 2010; https://apps.who.int/iris/bitstream/handle/10665/44440/9789241564090_eng.pdf;jsessionid=FADC468AEF33A190CEC5CAB713DAAB9F?sequence=1; last access date September 25, 2017]Search in Google Scholar
[57. J. A. Chandler and P. M. James, Discovery of trypanosomatid parasites in globally distributed Drosophila species, PLoS ONE8 (2013) e61937; https://doi.org/10.1371/journal.pone.006193710.1371/journal.pone.0061937363921523658617]Search in Google Scholar
[58. P. Linciano, A. Dawson, I. Poohner, D. M. Costa, M. S. Sa, A. Cordeiro-da-Silva, R. Luciani, S. Gul, G. Witt, B. Ellinger, M. Kuzikov, P. Gribbon, J. Reinshagen, M. Wolf, B. Behrens, V. Hannaert, P. A. M. Michels, E. Nerini, C. Pozzi, F. di Pisa, G. Landi, N. Santarem, S. Ferrari, P. Saxena, S. Lazzari, G. Cannazza, L. H. Freitas-Junior, C. B. Moraes, B. S. Pascoalino, L. M. Alcantara, C. P. Bertolacini, V. Fontana, U. Wittig, W. Muller, R. C. Wade, W. N. Hunter, S. Mangani, L. Costantino and M. P. Costi, Exploiting the 2-amino-1,3,4-thiadiazole scaffold to inhibit Trypanosoma brucei pteridine reductase in support of early-stage drug discovery, ACS Omega2 (2017) 5666−5683; https://doi.org/10.1021/acsomega.7b0047310.1021/acsomega.7b00473562394928983525]Search in Google Scholar
[59. K. T. Andrews, G. Fisher and T. S. Skinner-Adams, Drug repurposing and human parasitic protozoan diseases, Int. J. Parasitol. Drugs Drug Resist.4 (2014) 95–111; https://doi.org/10.1016/j.ijpddr.2014.02.00210.1016/j.ijpddr.2014.02.002409505325057459]Search in Google Scholar
[60. World Health Organization, Neglected Tropical Diseases; http://www.who.int/neglected_diseases/diseases/en/; last access date July 21, 2018]Search in Google Scholar
[61. S. Patterson and S. Wyllie, Nitro drugs for the treatment of trypanosomatid diseases: past, present, and future prospects, Trend Parasitol.30 (2014) 289–298; https://doi.org/10.1016/j.pt.2014.04.00310.1016/j.pt.2014.04.003404520624776300]Search in Google Scholar
[62. World Health Organization, Chagas Disease in the Americas: A Review of the Current Public Health Situation and a Vision for the Future. Report: Conclusions and Recommendations, Washington, D.C., 3-4 May 2018; https://www.paho.org/hq/index.php?option=com_content&view=article&id=14399:enfermedad-chagas-en-americas-revision-de-situacion-vision-futuro&Itemid=72315&lang=en; last access date July 17, 2018]Search in Google Scholar
[63. C. J. Schofield and J. P. Kabayo, Trypanosomiasis vector control in Africa and Latin America, Parasit. Vectors1 (2008) Article ID 24 (7 pages); https://doi.org/10.1186/1756-3305-1-2410.1186/1756-3305-1-24]Search in Google Scholar
[64. A. K. Jain, S. Sharma, A. Vaidya, V. Ravichandran and R. K. Agrawal, 1,3,4-Thiadiazole and its derivatives: a review on recent progress in biological activities, Chem. Biol. Drug Des.81 (2013) 557–576; https://doi.org/10.1111/cbdd.1212510.1111/cbdd.12125]Search in Google Scholar
[65. S. Tomlinson, F. Vandekerckhove, U. Frevert and V. Nussenzweig, The induction of Trypanosoma cruzi trypomastigote transformation by low pH, Parasitology110 (1995) 547–554; https://doi.org/10.1017/S003118200006526410.1017/S0031182000065264]Search in Google Scholar
[66. A. S. Nagle, S. Khare, A. B. Kumar, F. Supek, A. Buchynskyy, C. J. N. Mathison, N. K. Chennamaneni, N. Pendem, F. S. Buckner, M. H. Gelb and V. Molteni, Recent developments in drug discovery for leishmaniasis and human African trypanosomiasis, Chem. Rev.114 (2014) 11305–11347; https://doi.org/10.1021/cr500365f10.1021/cr500365f]Search in Google Scholar
[67. Centers for Disease Control and Prevention, Parasites, African trypanosomiasis; https://www.cdc.gov/parasites/sleepingsickness/biology.html; last access date May 9, 2019]Search in Google Scholar
[68. Parasites in humans, Trypanosoma brucei – sleeping sickness; http://www.parasitesinhumans.org/trypanosoma-brucei-sleeping-sickness.html; last access date May 9, 2019]Search in Google Scholar
[69. World Health Organization, Human African Trypanosomiasis, Symptoms, Diagnosis and Treatment; http://www.who.int/trypanosomiasis_african/disease/diagnosis/en/; last access date November 1st, 2018]Search in Google Scholar
[70. World Health Organization, Trypanosomiasis; http://www.who.int/ith/diseases/trypanosomiasis/en/; last access date November 1, 2018]Search in Google Scholar
[71. World Health Organization, Chagas Disease (American Trypanosomiasis), 1 February 2018; http://www.who.int/news-room/fact-sheets/detail/chagas-disease-(american-trypanosomiasis); last access date July 24, 2018]Search in Google Scholar
[72. World Health Organization, Chagas Disease: Control and Elimination, Sixty-third World Health Assembly, 22 April 2010; http://apps.who.int/gb/ebwha/pdf_files/WHA63/A63_17-en.pdf; last access date November 1, 2018]Search in Google Scholar
[73. S. Pund and A. Joshi, Nanoarchitectures for Neglected Tropical Diseases: Challenges and State of the Art, in Nano- and Microscale Drug Delivery Systems: Design and Fabrication (Ed. A. M. Grumezescu), 1st ed., Elsevier, Amsterdam 2017, pp. 449.10.1016/B978-0-323-52727-9.00023-6]Search in Google Scholar
[74. J. D. Maya, S. Bollo, L. J. Nunez-Vergara, J. A. Squella, Y. Repetto, A. Morello, J. Perie and G. Chauviere, Trypanosoma cruzi: effect and mode of action of nitroimidazole and nitrofuran derivatives, Biochem. Pharmacol.65 (2003) 999–1006; https://doi.org/10.1016/S0006-2952(02)01663-510.1016/S0006-2952(02)01663-5]Search in Google Scholar
[75. A. Silva de Carvalho, K. Salomao, S. Lisboa de Castro, T. R. Conde, H. P. da Silva Zamith, E. R. Caffarena, B. S. Hall, S. R. Wilkinson and N. Boechat, Megazol and its bioisostere 4H-1,2,4-triazole: comparing the trypanocidal, cytotoxic and genotoxic activities and their in vitro and in silico interactions with the Trypanosoma brucei nitroreductase enzyme, Mem. Inst. Oswaldo Cruz109 (2014) 315–323; https://doi.org/10.1590/0074-027614049710.1590/0074-0276140497]Search in Google Scholar
[76. B. Bouteille, A. Marie-Daragon, G. Chauviere, C. de Albuquerque, B. Enanga, M. L. Darde, J. M. Vallat, J. Perie and M. Dumas, Effect of megazol on Trypanosoma brucei brucei acute and subacute infections in Swiss mice, Acta Tropica60 (1995) 73–80; https://doi.org/10.1016/0001-706X(95)00109-R10.1016/0001-706X(95)00109-R]Search in Google Scholar
[77. G. Chauviere, B. Bouteille, B. Enanga, C. de Albuquerque, S. L. Croft, M. Dumas and J. Perie, Synthesis and biological activity of nitro heterocycles analogous to megazol, a trypanocidal lead, J. Med. Chem.46 (2003) 427–440; https://doi.org/10.1021/jm021030a10.1021/jm021030a12540242]Search in Google Scholar
[78. S. R. Wilkinson and J. M. Kelly, Trypanocidal drugs: mechanisms, resistance and new targets, Expert Rev. Mol. Med.11 (2009) e31; https://doi.org/10.1017/S146239940900125210.1017/S146239940900125219863838]Search in Google Scholar
[79. B. Enanga, M. R. Ariyanayagam, M. L. Stewart and M. P. Barrett, Activity of megazol, a trypanocidal nitroimidazole, is associated with DNA damage, Antimicrob. Agents Chemother.47 (2003) 3368–3370; https://doi.org/10.1128/AAC.47.10.3368-3370.200310.1128/AAC.47.10.3368-3370.200320114514506061]Search in Google Scholar
[80. H. B. Leites, F. S. Damasceno, A. M. Silber, R. Z. Mendonca and C. N. Albuquerque, Synthesis and evaluation of trypanosomicidal activity of new derivatives of megazol, Pharm. Biol. Eval.5 (2018) 40–51.10.26510/2394-0859.pbe.2018.05]Search in Google Scholar
[81. T. J. Vickers and S. M. Beverley, Folate metabolic pathways in Leishmania, Essays Biochem.51 (2011) 63–80; https://doi.org/10.1042/bse051006310.1042/bse0510063327821422023442]Search in Google Scholar
[82. N. Sienkiewicz, H. B. Ong and A. H. Fairlamb, Trypanosoma brucei pteridine reductase 1 is essential for survival in vitro and for virulence in mice, Mol. Microbiol.77 (2010) 658–671; https://doi.org/10.1111/j.1365-2958.2010.07236.x10.1111/j.1365-2958.2010.07236.x291622220545846]Search in Google Scholar
[83. H. B. Ong, N. Sienkiewicz, S. Wyllie and A. H. Fairlamb, Dissecting the metabolic roles of pteridine reductase 1 in Trypanosoma bruceiand Leishmania major, J. Biol. Chem.286 (2011) 10429–10438; https://doi.org/10.1074/jbc.M110.20959310.1074/jbc.M110.209593306049621239486]Search in Google Scholar
[84. S. Ferrari, F. Morandi, D. Motiejunas, E. Nerini, S. Henrich, R. Luciani, A. Venturelli, S. Lazzari, S. Calo, S. Gupta, V. Hannaert, P. A. M. Michels, R. C. Wade and M. P. Costi, Virtual screening identification of nonfolate compounds, including a CNS drug, as antiparasitic agents inhibiting pteridine reductase, J. Med. Chem.54 (2011) 211–221; https://doi.org/10.1021/jm101057210.1021/jm101057221126022]Search in Google Scholar
[85. A. Dawson, F. Gibellini, N. Sienkiewicz, L. B. Tulloch, P. K. Fyfe, K. McLuskey, A. H. Fairlamb and W. N. Hunter, Structure and reactivity of Trypanosoma brucei pteridine reductase: inhibition by the archetypal antifolate methotrexate, Mol. Microbiol.61 (2006) 1457–1468; https://doi.org/10.1111/j.1365-2958.2006.05332.x10.1111/j.1365-2958.2006.05332.x161873316968221]Search in Google Scholar
[86. D. Spinks, H. B. Ong, C. P. Mpamhanga, E. J. Shanks, D. A. Robinson, I. T. Collie, K. D. Read, J. A. Frearson, P. G. Wyatt, R. Brenk, A. H. Fairlamb and I. H. Gilbert, Design, synthesis and biological evaluation of novel inhibitors of Trypanosoma brucei pteridine reductase 1, Chem. Med. Chem.6 (2011) 302–308; https://doi.org/10.1002/cmdc.20100045010.1002/cmdc.201000450304771021275054]Search in Google Scholar
[87. B. Nare, J. Luba, L. W. Hardy and S. Beverley, New approaches to Leishmania chemotherapy: pteridine reductase 1 (PTR1) as a target and modulator of antifolate sensitivity, Parasitology114 (1997) S101–S110.10.1017/S0031182097001133]Search in Google Scholar
[88. A. Cavazzuti, G. Paglietti, W. N. Hunter, F. Gamarro, S. Piras, M. Loriga, S. Allecca, P. Corona, K. McLuskey, L. Tulloch, F. Gibellini, S. Ferrari and M. P. Costi, Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development, Proc. Natl. Acad. Sci. USA105 (2008) 1448–1453; https://doi.org/10.1073/pnas.070438410510.1073/pnas.0704384105223416418245389]Search in Google Scholar
[89. R. F. Rodrigues, D. Castro-Pinto, A. Echevarria, C. M. dos Reis, C. N. Del Cistia, C. M. R. Sant’Anna, F. Teixeira, H. Castro, M. Canto-Cavalheiro, L. L. Leon and A. Tomas, Investigation of trypanothione reductase inhibitory activity by 1,3,4-thiadiazolium-2-aminide derivatives and molecular docking studies, Bioorg. Med. Chem.20 (2012) 1760–1766; https://doi.org/10.1016/j.bmc.2012.01.00910.1016/j.bmc.2012.01.00922304847]Search in Google Scholar
[90. G. Colotti, P. Baiocco, A. Fiorillo, A. Boffi, E. Poser, F. Di Chiaro and A. Ilari, Structural insights into the enzymes of the trypanothione pathway: Targets for antileishmaniasis drugs, Future Med. Chem. 5 (2013) 1861–1875; https://doi.org/10.4155/fmc.13.14610.4155/fmc.13.14624144416]Search in Google Scholar
[91. M. O. F. Khan, Trypanothione reductase: A viable chemotherapeutic target for antitrypanosomal and antileishmanial drug design, Drug Target Insights2 (2007) 129–146; https://doi.org/10.1177/11773928070020000710.1177/117739280700200007]Search in Google Scholar
[92. D. Benítez, A. Medeiros, L. Fiestas, E. A. Panozzo-Zenere, F. Maiwald, K. C. Prousis, M. Roussaki, T. Calogeropoulou, A. Detsi, T. Jaeger, J. Šarlauskas, L. P. Mašič, C. Kunick, G. R. Labadie, L. Flohé and M. A. Comini, Identification of novel chemical scaffolds inhibiting trypanothione synthetase from pathogenic trypanosomatids, PLoS Negl. Trop. Dis.10 (2016) e0004617 (25 pages); https://doi.org/10.1371/journal.pntd.000461710.1371/journal.pntd.0004617482923327070550]Search in Google Scholar
[93. A. Ilari, A. Fiorillo, I. Genovese and G. Colotti, An update on structural insights into the enzymes of the polyamine-trypanothione pathway: targets for new drugs against leishmaniasis, Future Med. Chem.9 (2017) 61–77; https://doi.org/10.4155/fmc-2016-018010.4155/fmc-2016-018027957878]Search in Google Scholar
[94. V. Olin-Sandoval, Z. Gonzalez-Chavez, M. Berzunza-Cruz, I. Martinez, R. Jasso-Chavez, I. Becker, B. Espinoza, R. Moreno-Sanchez and E. Saavedra, Drug target validation of the trypanothione pathway enzymes through metabolic modeling, FEBS J.279 (2012) 1811–1833; https://doi.org/10.1111/j.1742-4658.2012.08557.x10.1111/j.1742-4658.2012.08557.x22394478]Search in Google Scholar
[95. R. F. Rodrigues, E. F. da Silva, A. Echevarria, R. Fajardo-Bonin, V. F. Amaral, L. L. Leon and M. Canto-Cavalheiro, A comparative study of mesoionic compounds in Leishmania sp. and toxicity evaluation, Eur. J. Med. Chem. 42 (2007) 1039–1043; https://doi.org/10.1016/j.ejmech.2006.12.02610.1016/j.ejmech.2006.12.02617367894]Search in Google Scholar
[96. R. F. Rodrigues, K. S. Charret, E. F. da Silva, A. Echevarria, V. F. Amaral, L. L. Leon and M. Canto-Cavalheiro, Antileishmanial activity of 1,3,4-thiadiazolium-2-aminide in mice infected with Leishmania amazonensis, Antimicrob. Agents Chemother. 53 (2009) 839–842; https://doi.org/10.1128/AAC.00062-0810.1128/AAC.00062-08263063319015338]Search in Google Scholar
[97. D. Spinks, L. S. Torrie, S. Thompson, J. R. Harrison, J. A. Frearson, K. D. Read, A. H. Fairlamb, P. G. Wyatt and I. H. Gilbert, Design, synthesis and biological evaluation of Trypanosoma brucei trypanothione synthetase inhibitors, Chem. Med. Chem.7 (2012) 95–106; https://doi.org/10.1002/cmdc.20110042010.1002/cmdc.201100420332066322162199]Search in Google Scholar
[98. A. F. Sousa, A. G. Gomes-Alves, D. Benitez, M. A. Comini, L. Flohe, T. Jaeger, J. Passos, F. Stuhlmann, A. M. Tomas and H. Castro, Genetic and chemical analyses reveal that trypanothione synthetase but not glutathionylspermidine synthetase is essential for Leishmania infantu, Free Radic. Biol. Med.73 (2014) 229–238; https://doi.org/10.1016/j.freeradbiomed.2014.05.00710.1016/j.freeradbiomed.2014.05.00724853758]Search in Google Scholar
[99. P. K. Fyfe, S. L. Oza, A. H. Fairlamb and W. N. Hunter, Leishmania trypanothione synthetaseamidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities, J. Biol. Chem.283 (2008) 17672–17680; https://doi.org/10.1074/jbc.M80185020010.1074/jbc.M801850200242736718420578]Search in Google Scholar
[100. W. da Silva Ferreira, L. Freire-de-Lima, V. Barbosa Saraiva, F. Alisson-Silva, L. Mendonca-Previato, J. O. Previato, A. Echevarria and M. E. Freire de Lima, Novel 1,3,4-thiadiazolium-2-phenylamine chlorides derived from natural piperine as trypanocidal agents: chemical and biological studies, Bioorg. Med. Chem.16 (2008) 2984–2991; https://doi.org/10.1016/j.bmc.2007.12.04910.1016/j.bmc.2007.12.04918226906]Search in Google Scholar
[101. A. Tahghighi and F. Babalouei, Thiadiazoles: the appropriate pharmacological scaffolds with leishmanicidal and antimalarial activities: a review, Iran. J. Basic Med. Sci.20 (2017) 613–622; https://doi.org/10.22038/IJBMS.2017.8828]Search in Google Scholar
[102. World Health Organization, World Malaria Report 2018, World Health Organization, Geneva 2018, Licence: CC BY-NC-SA 3.0 IGO, ISBN 978-92-4-156565-3; https://apps.who.int/iris/bitstream/handle/10665/275867/9789241565653-eng.pdf; last access date November 29, 2018]Search in Google Scholar
[103. World Health Organization, Malaria Vaccine: WHO Position Paper – January 2016, Weekly Epidemiological Record91 (2016) 33–52; https://www.who.int/wer; last access date June 8, 2019]Search in Google Scholar
[104. World Health Organization, Malaria, 19 November 2018; http://www.who.int/en/news-room/fact-sheets/detail/malaria; last access date November 29, 2018]Search in Google Scholar
[105. World Health Organization, First Malaria Vaccine in Africa: A Potential New Tool for Child Health and Improved Malaria Control, WHO/CDS/GMP/2018.05; https://www.who.int/malaria/publications/atoz/first-malaria-vaccine/en/; last access date June 8, 2019]Search in Google Scholar
[106. World Health Organization, Short Overview of the Malaria Vaccine Implementation Programme, April 2019; https://www.who.int/malaria/media/malaria-vaccine-overview/en/; last access date June 8, 2019]Search in Google Scholar
[107. L. Foquet, C. Hermsen, G. J. van Gemert, E. Van Braeckel, K. Weening, R. Sauerwein, P. Meuleman and G. Leroux-Roels, Vaccine-induced monoclonal antibodies targeting circumsporozoite protein prevent Plasmodium falciparum infection, J. Clin. Invest.124 (2014) 140–144; https://doi.org/10.1172/JCI7034910.1172/JCI70349387123824292709]Search in Google Scholar
[108. World Health Organization, Malaria Vaccine Implementation Programme (MVIP); https://www.who.int/immunization/diseases/malaria/malaria_vaccine_implementation_programme/about/en/; last access date June 8, 2019]Search in Google Scholar
[109. World Health Organization, Malaria Vaccine Pilot Launched in Malawi. Country First of Three in Africa to Roll Out Landmark Vaccine, Geneva 23 April 2019; https://www.who.int/news-room/detail/23-04-2019-malaria-vaccine-pilot-launched-in-malawi; last access dateJune 8, 2019]Search in Google Scholar
[110. E. A. Ashley and A. P. Phyo, Drugs in development for malaria, Drugs78 (2018) 861–879; https://doi.org/10.1007/s40265-018-0911-910.1007/s40265-018-0911-9601350529802605]Search in Google Scholar
[111. P. B. Bloland and H. A. Williams, Malaria Control During Mass Population Movements and Natural Disasters, National Academies Press, Washington (DC) 2002, pp. 145–150.]Search in Google Scholar
[112. V. M. Avery, S. Bashyam, J. N. Burrows, S. Duffy, G. Papadatos, S. Puthukkuti, Y. Sambandan, S. Singh, T. Spangenberg, D. Waterson and P. Willis, Screening and hit evaluation of a chemical library against blood-stage Plasmodium falciparum, Malar. J.13 (2014) Article ID 190 (12 pages); https://doi.org/10.1186/1475-2875-13-19010.1186/1475-2875-13-190409491924886460]Search in Google Scholar
[113. E. G. Severance, J. Xiao, L. Jones-Brando, S. Sabunciyan, Y. Li, M. Pletnikov, E. Prandovszky and R. Yolken, Toxoplasma gondii – a gastrointestinal pathogen associated with human brain diseases, Int. Rev. Neurobiol.131 (2016) 143–163; https://doi.org/10.1016/bs.irn.2016.08.00810.1016/bs.irn.2016.08.008550873827793216]Search in Google Scholar
[114. P. R. Torgerson and P. Mastroiacovo, The global burden of congenital toxoplasmosis: a systematic review, Bull. World Health Organ.91 (2013) 501–508.10.2471/BLT.12.111732369979223825877]Search in Google Scholar
[115. M. Pan, C. Lyu, J. Zhao and B. Shen, Sixty years (1957-2017) of research on toxoplasmosis in China – an overview, Front. Microbiol.8 (2017) 1–16; https://doi.org/10.3389/fmicb.2017.0182510.3389/fmicb.2017.01825562219328993763]Search in Google Scholar
[116. World Health Organization, Toxoplasmosis: Greater Awareness Needed; http://www.euro.who.int/en/health-topics/disease-prevention/food-safety/news/news/2016/11/toxoplasmosis-greater-awareness-needed; last access date November 23, 2018]Search in Google Scholar
[117. K. Dzitko, A. Paneth, T. Plech, J. Pawelczyk, P. Staczek, J. Stefanska and P. Paneth, 1,4-Disubstituted thiosemicarbazide derivatives are potent inhibitors of Toxoplasma gondii proliferation, Molecules19 (2014) 9926–9943; https://doi.org/10.3390/molecules1907992610.3390/molecules19079926629055625010466]Search in Google Scholar
[118. J. M. Furtado, J. R. Smith, R. Belfort, D. Gattey and K. L. Winthrop, Toxoplasmosis: a global threat, J. Global Infect. Dis.3 (2011) 281–284; https://doi.org/10.4103/0974-777X.8353610.4103/0974-777X.83536316281721887062]Search in Google Scholar
[119. R. P. Tenorio, C. S. Carvalho, C. S. Pessanha, J. G. de Lima, A. R. de Faria, A. J. Alves, E. J. T. de Melo and A. J. S. Goes, Synthesis of thiosemicarbazone and 4-thiazolidinone derivatives and their in vitro anti-Toxoplasma gondii activity, Bioorg. Med. Chem. Lett.15 (2005) 2575–2578; https://doi.org/10.1016/j.bmcl.2005.03.04810.1016/j.bmcl.2005.03.04815863319]Search in Google Scholar
[120. T. M. de Aquino, A. P. Liesen, R. E. A. da Silva, V. T. Lima, C. S. Carvalho, A. R. de Faria, J. M. de Araujo, J. G. de Lima, A. J. Alves, E. J. T. de Melo and A. J. S. Goes, Synthesis, anti-Toxoplasma gondii and antimicrobial activities of benzaldehyde 4-phenyl-3-thiosemicarbazones and 2-[(phenylmethylene)hydrazono]-4-oxo-3-phenyl-5-thiazolidineacetic acids, Bioorg. Med. Chem.16 (2008) 446–456; https://doi.org/10.1016/j.bmc.2007.09.02510.1016/j.bmc.2007.09.02517905587]Search in Google Scholar
[121. A. P. Liesen, T. M. de Aquino, C. S. Carvalho, V. T. Lima, J. M. de Araujo, J. G. de Lima, A. R. de Faria, E. J. T. de Melo, A. J. Alves, E. W. Alves, A. Q. Alves and A. J. S. Goes, Synthesis and evaluation of anti-Toxoplasma gondii and antimicrobial activities of thiosemicarbazides, 4-thiazolidinones and 1,3,4-thiadiazoles, Eur. J. Med. Chem.45 (2010) 3685–3691; https://doi.org/10.1016/j.ejmech.2010.05.01710.1016/j.ejmech.2010.05.01720541294]Search in Google Scholar
[122. L. Monzote and A. Siddiq, Drug development to protozoan diseases, Open Med. Chem. J.5 (2011) 1–3; https://doi.org/10.2174/187410450110501000110.2174/1874104501105010001310387821629506]Search in Google Scholar