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Turkish Journal of Parasitology. 2020; 44: 12-6.","journal-title":"Turkish Journal of Parasitology"},{"key":"ref23","doi-asserted-by":"publisher","first-page":"444","DOI":"10.5578\/mb.69702","article-title":"T\u00fcrkiye'de Kutan\u00f6z Ley\u015fmanyazis Etkeni Leishmania tropica'da Antimon Diren\u00e7 Mekanizmas\u0131n\u0131n Belirlenmesi","volume":"54","author":"\u00d6zbilgin","year":"2020","unstructured":"24. \u00d6zbilgin A, Zeyrek FY, G\u00fcray MZ, \u00c7ulha G, Akyar I, Harman M, ve ark. T\u00fcrkiye'de Kutan\u00f6z Ley\u015fmanyazis Etkeni Leishmania tropica'da Antimon Diren\u00e7 Mekanizmas\u0131n\u0131n Belirlenmesi. 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Amino Acids. 2019; 51: 1633-48.","journal-title":"Amino Acids"},{"key":"ref30","doi-asserted-by":"publisher","first-page":"8205","DOI":"10.1016\/j.bmc.2008.07.032","article-title":"Synthesis and antimicrobial activity of dermaseptin S1 analogues","volume":"16","author":"Savoia","year":"2008","unstructured":"31. Savoia D, Guerrini R, Marzola E, Salvadori S. Synthesis and antimicrobial activity of dermaseptin S1 analogues. Bioorg Med Chem. 2008; 16: 8205-9.","journal-title":"Bioorg Med Chem"},{"key":"ref31","doi-asserted-by":"publisher","first-page":"6040","DOI":"10.4049\/jimmunol.1301921","article-title":"Protective Role of the Neuropeptide Urocortin II against Experimental Sepsis and Leishmaniasis by Direct Killing of Pathogens","volume":"191","author":"Campos-Salinas","year":"2013","unstructured":"32. Campos-Salinas J, Caro M, Cavazzuti A, Forte-Lago I, Beverley SM, O'Valle F, et al. Protective Role of the Neuropeptide Urocortin II against Experimental Sepsis and Leishmaniasis by Direct Killing of Pathogens. The Journal of Immunology. 2013; 191: 6040-51.","journal-title":"The Journal of Immunology"},{"key":"ref32","doi-asserted-by":"publisher","first-page":"446","DOI":"10.3390\/ph15040446","article-title":"1,2,4-Trioxolane and 1,2,4,5-Tetraoxane Endoperoxides against Old-World Leishmania Parasites: In Vitro Activity and Mode of Action","volume":"15","author":"Mendes","year":"2022","unstructured":"33. Mendes A, Armada A, Cabral LIL, Amado PSM, Campino L, Cristiano MLS, et al. 1,2,4-Trioxolane and 1,2,4,5-Tetraoxane Endoperoxides against Old-World Leishmania Parasites: In Vitro Activity and Mode of Action. Pharmaceuticals. 2022; 15: 446.","journal-title":"Pharmaceuticals"},{"key":"ref33","doi-asserted-by":"publisher","unstructured":"34. Crauwels P, Bank E, Walber B, Wenzel UA, Agerberth B, Chanyalew M, et al. 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