Louise Le Pensee

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The mitochondrial respiratory chain of the malaria parasite Plasmodium falciparum differs from that of its human host in that it lacks a canonical protonmotive NADH:ubiquinone oxidoreductase (Complex I), containing instead a single sub-unit, non-protonmotive Ndh2, similar to that found in plant mitochondria, fungi and some bacteria [1,2]. As such, the P.(More)
NADH:quinone oxidoreductase (PfNDH2) represents a metabolic choke point in the respiratory chain of Plasmo-dium falciparum mitochondria and is the focus of a drug discovery programme. A miniaturised assay for recombi-nant PfNDH2 with robust assay performance measures was generated for the high throughput screening (HTS) of a focused library of 17,000(More)
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