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Querido, J.B., Mancera-Martínez, E., Vicens, Q., Bochler, A., Chicher, J., Simonetti, A. and Hashem, Y. (2017) The Cryo-EM Structure of a Novel 40S Kinetoplastid-Specific Ribosomal Protein. Structure, 25, 1785-1794.
https://doi.org/10.1016/j.str.2017.09.014

has been cited by the following article:

• TITLE: Molecular Docking Studies on Streptomycin Antileishmanial Activity

  AUTHORS: Todd A. Young, Matthew George Jr., Ayele Gugssa, William M. Southerland, Yayin Fang, Clarence M. Lee

  KEYWORDS: Leishmaniasis, Streptomycin, Amphotericin B, Molecular Docking, Aminoglycosides, Antileishmanial

  JOURNAL NAME: Open Journal of Physical Chemistry, Vol.14 No.2, May 11, 2024

  ABSTRACT: Resistance to pentavalent antimonial drugs and the lack of vaccines make it urgent to find novel therapeutic options to treat Leishmaniasis, a tropical disease caused by the Leishmania protozoan parasite. The study reported here is to investigate if Streptomycin, an aminoglycoside, and Amphotericin B, the second-line treatment drug, exhibit antileishmanial activity through a similar mechanism. By using MOE (Molecular Operating Environment), we performed molecular docking studies on these drugs binding to a range of targets including ribosome targets in Leishmania and H. sapiens. Our study shows that the two drugs do not bind to the same pockets in Leishmania targets but to the same pockets in the human ribosome, with some differences in interactions. Moreover, our 2D maps indicated that Amphotericin B binds to the A-site in the human cytoplasmic ribosome, whereas streptomycin does not.