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• W1522940126 abstract "Research Article15 January 1994free access Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase. S.E. Francis S.E. Francis Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author I.Y. Gluzman I.Y. Gluzman Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author A. Oksman A. Oksman Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author A. Knickerbocker A. Knickerbocker Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author R. Mueller R. Mueller Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author M.L. Bryant M.L. Bryant Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author D.R. Sherman D.R. Sherman Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author D.G. Russell D.G. Russell Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author D.E. Goldberg D.E. Goldberg Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author S.E. Francis S.E. Francis Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author I.Y. Gluzman I.Y. Gluzman Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author A. Oksman A. Oksman Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author A. Knickerbocker A. Knickerbocker Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author R. Mueller R. Mueller Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author M.L. Bryant M.L. Bryant Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author D.R. Sherman D.R. Sherman Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author D.G. Russell D.G. Russell Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author D.E. Goldberg D.E. Goldberg Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. Search for more papers by this author Author Information S.E. Francis1, I.Y. Gluzman1, A. Oksman1, A. Knickerbocker1, R. Mueller1, M.L. Bryant1, D.R. Sherman1, D.G. Russell1 and D.E. Goldberg1 1Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO. The EMBO Journal (1994)13:306-317https://doi.org/10.1002/j.1460-2075.1994.tb06263.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Intraerythrocytic malaria parasites rapidly degrade virtually all of the host cell hemoglobin. We have cloned the gene for an aspartic hemoglobinase that initiates the hemoglobin degradation pathway in Plasmodium falciparum. It encodes a protein with 35% homology to human renin and cathepsin D, but has an unusually long pro-piece that includes a putative membrane spanning anchor. Immunolocalization studies place the enzyme in the digestive vacuole and throughout the hemoglobin ingestion pathway, suggesting an unusual protein targeting route. A peptidomimetic inhibitor selectively blocks the aspartic hemoglobinase, prevents hemoglobin degradation and kills the organism. We conclude that Plasmodium hemoglobin catabolism is a prime target for antimalarial chemotherapy and have identified a lead compound towards this goal. Previous ArticleNext Article Volume 13Issue 21 January 1994In this issue RelatedDetailsLoading ..." @default.
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• W1522940126 title "Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase." @default.
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