ArticleBioorganic & medicinal chemistry letters2012
Crystal structure of phosphoethanolamine methyltransferase from Plasmodium falciparum in complex with amodiaquine.
Article in Bioorganic & medicinal chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Antimalarial Properties of Isoquinoline Derivative fromBioMed research international · 2020Article
- Phosphoethanolamine-N-methyltransferase is a potential biomarker for the diagnosis of P. knowlesi and P. falciparum malaria.PloS one · 2018Article
- Conformational changes in the di-domain structure ofThe Journal of biological chemistry · 2017Article
- In vitro anthelmintic efficacy of inhibitors of phosphoethanolamine Methyltransferases in Haemonchus contortus.International journal for parasitology. Drugs and drug resistance · 2016Article
- Structure, function and inhibition of the phosphoethanolamine methyltransferases of the human malaria parasites Plasmodium vivax and Plasmodium knowlesi.Scientific reports · 2015Article
- An alternative mechanism for the methylation of phosphoethanolamine catalyzed by Plasmodium falciparum phosphoethanolamine methyltransferase.The Journal of biological chemistry · 2014Article
- Amodiaquine, an antimalarial drug, inhibits dengue virus type 2 replication and infectivity.Antiviral research · 2014Article
- Nematode phospholipid metabolism: an example of closing the genome-structure-function circle.Trends in parasitology · 2014Review
- Evolution of structure and mechanistic divergence in di-domain methyltransferases from nematode phosphocholine biosynthesis.Structure (London, England : 1993) · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Phosphoethanolamine N-methyltransferase (PMT) is essential for phospholipid biogenesis in the malarial parasite Plasmodium falciparum. PfPMT catalyzes the triple methylation of phosphoethanolamine to produce phosphocholine, which is then used for phosphatidylcholine synthesis. Here we describe the 2.0Å resolution X-ray crystal structure of PfPMT in complex with amodiaquine. To better characterize inhibition of PfPMT by amodiaquine, we determined the IC(50) values of a series of aminoquinolines using a direct radiochemical assay. Both structural and functional analyses provide a possible approach for the development of new small molecule inhibitors of PfPMT.
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