Diverse antimalarials from whole-cell phenotypic screens disrupt malaria parasite ion and volume homeostasis
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-018-26819-1.pdf
Reference25 articles.
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2. Krishna, S. et al. Expression and functional characterization of a Plasmodium falciparum Ca2+-ATPase (PfATP4) belonging to a subclass unique to apicomplexan organisms. J Biol Chem 276, 10782–10787, https://doi.org/10.1074/jbc.M010554200 (2001).
3. Spillman, N. J., Allen, R. J. & Kirk, K. Na+ extrusion imposes an acid load on the intraerythrocytic malaria parasite. Mol Biochem Parasitol 189, 1–4, https://doi.org/10.1016/j.molbiopara.2013.04.004 (2013).
4. Spillman, N. J. et al. Na+ regulation in the malaria parasite Plasmodium falciparum involves the cation ATPase PfATP4 and is a target of the spiroindolone antimalarials. Cell Host Microbe 13, 227–237, https://doi.org/10.1016/j.chom.2012.12.006 (2013).
5. Jimenez-Diaz, M. B. et al. (+)-SJ733, a clinical candidate for malaria that acts through ATP4 to induce rapid host-mediated clearance of Plasmodium. Proc Natl Acad Sci USA 111, E5455–5462, https://doi.org/10.1073/pnas.1414221111 (2014).
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