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Genetic Manipulation of Leishmania Parasites Facilitates the Exploration of the Polyamine Biosynthetic Pathway as a Potential Therapeutic Target. Adv Genet Reseach. 2013;10:29-54. Accessed March 25, 2021. http:\/\/commons.pacificu.edu\/phrmfac."},{"key":"10.1016\/j.bmc.2021.116365_b0305","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20121743","article-title":"The glyoxalase pathway: The first hundred years... and beyond","volume":"453","author":"Sousa Silva","year":"2013","journal-title":"Biochem J"},{"key":"10.1016\/j.bmc.2021.116365_b0310","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.molbiopara.2009.12.004","article-title":"Phospholipid and sphingolipid metabolism in Leishmania","volume":"170","author":"Zhang","year":"2010","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.bmc.2021.116365_b0315","unstructured":"Abu-Mejdad N. Evaluation of therapeutic effects of vicine against leishmania donovani. in vitro. J Am Sci. 2013;9(5):115-20. 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