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  • Plasmodium falciparum neutral aminopeptidases: new targets for anti-malarials

    Author(s)
    Skinner-Adams, Tina S
    Stack, Colin M
    Trenholme, Katharine R
    Brown, Chris L
    Grembecka, Jolanta
    Lowther, Jonathan
    Mucha, Artur
    Drag, Marcin
    Kafarski, Pawel
    McGowan, Sheena
    Whisstock, James C
    Gardiner, Donald L
    Dalton, John P
    Griffith University Author(s)
    Skinner-Adams, Tina
    Year published
    2010
    Metadata
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    Abstract
    The neutral aminopeptidases M1 alanyl aminopeptidase (PfM1AAP) and M17 leucine aminopeptidase (PfM17LAP) of the humanmalaria parasite Plasmodiumfalciparumare targets for the development of novel anti-malarial drugs. Although the functions of these enzymes remain unknown, they are believed to act in the terminal stages of haemoglobin degradation, generating amino acids essential for parasite growth and development. Inhibitors of both enzymes are lethal to P. falciparum in culture and kill the murine malaria P. chabaudi in vivo. Recent biochemical, structural and functional studies provide the substrate specificity ...
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    The neutral aminopeptidases M1 alanyl aminopeptidase (PfM1AAP) and M17 leucine aminopeptidase (PfM17LAP) of the humanmalaria parasite Plasmodiumfalciparumare targets for the development of novel anti-malarial drugs. Although the functions of these enzymes remain unknown, they are believed to act in the terminal stages of haemoglobin degradation, generating amino acids essential for parasite growth and development. Inhibitors of both enzymes are lethal to P. falciparum in culture and kill the murine malaria P. chabaudi in vivo. Recent biochemical, structural and functional studies provide the substrate specificity and mechanistic binding data needed to guide the development of more potent antimalarial drugs. Together with biological studies, these data form the rationale for choosing PfM1AAP and PfM17LAP as targets for anti-malarial development.
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    Journal Title
    Trends in Biochemical Sciences
    Volume
    35
    Issue
    1
    DOI
    https://doi.org/10.1016/j.tibs.2009.08.004
    Subject
    Chemical sciences
    Medicinal and biomolecular chemistry not elsewhere classified
    Biological sciences
    Biomedical and clinical sciences
    Publication URI
    http://hdl.handle.net/10072/36802
    Collection
    • Journal articles

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