Structure of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae bound to an allophenylnorstatine-based inhibitor.

@article{Clemente2006StructureOT,
  title={Structure of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae bound to an allophenylnorstatine-based inhibitor.},
  author={Jose C. Clemente and Lakshmanan Govindasamy and Amrita Madabushi and Suzanne Zo{\"e} Fisher and Rebecca E Moose and C. A. Yowell and Koushi Hidaka and Tooru Kimura and Yoshio Hayashi and Yoshiaki Kiso and Mavis Agbandje-McKenna and J. B. Dame and Ben Dunn and Robert McKenna},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2006},
  volume={62 Pt 3},
  pages={246-52}
}
The malarial parasite continues to be one of the leading causes of death in many developing countries. With the development of resistance to the currently available treatments, the discovery of new therapeutics is imperative. Currently, the plasmepsin enzymes found in the food vacuole of the parasite are a chief target for drug development. Allophenylnorstatine-based compounds originally designed to inhibit HIV-1 protease have shown efficacy against all four plasmepsin enzymes found in the food… CONTINUE READING

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