X-ray Structure of Plasmepsin II Complexed with a Potent Achiral Inhibitor
Open Access
- 1 June 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (25) , 23837-23843
- https://doi.org/10.1074/jbc.m501519200
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The Role of Plasmodium falciparum Food Vacuole PlasmepsinsJournal of Biological Chemistry, 2005
- Design and Synthesis of Potent Inhibitors of the Malaria Aspartyl Proteases Plasmepsin I and II. Use of Solid-Phase Synthesis to Explore Novel Statine MotifsJournal of Medicinal Chemistry, 2004
- Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparumProceedings of the National Academy of Sciences, 2004
- Potent Inhibitors of the Plasmodium falciparum Enzymes Plasmepsin I and II Devoid of Cathepsin D Inhibitory ActivityJournal of Medicinal Chemistry, 2003
- High-Affinity Inhibition of a Family of Plasmodium falciparum Proteases by a Designed Adaptive InhibitorBiochemistry, 2003
- Inhibitors of the Plasmodium Falciparum Parasite Aspartic Protease Plasmepsin II As Potential Antimalarial AgentsCurrent Medicinal Chemistry, 2003
- Four plasmepsins are active in thePlasmodium falciparumfood vacuole, including a protease with an active-site histidineProceedings of the National Academy of Sciences, 2002
- New Class of Small Nonpeptidyl Compounds Blocks Plasmodium falciparum Development In Vitro by Inhibiting PlasmepsinsAntimicrobial Agents and Chemotherapy, 2001
- Cellular Uptake of Chloroquine Is Dependent on Binding to Ferriprotoporphyrin IX and Is Independent of NHE Activity in Plasmodium falciparum The Journal of cell biology, 1999
- A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparumFEBS Letters, 1999