Gene organization of a Plasmodium falciparum serine hydroxymethyltransferase and its functional expression in Escherichia coli.

@article{Alfadhli2000GeneOO,
  title={Gene organization of a Plasmodium falciparum serine hydroxymethyltransferase and its functional expression in Escherichia coli.},
  author={Suad Alfadhli and Pradipsinh K Rathod},
  journal={Molecular and biochemical parasitology},
  year={2000},
  volume={110 2},
  pages={283-91}
}
The global emergence of drug-resistant malarial parasites necessitates identification and characterization of novel drug targets. Three reactions are involved in methylenetetrahydrofolate recycling: Thymidylate synthase (TS), dihydrofolate reductase (DHFR), and serine hydroxymethyltransferase (SHMT). Malarial bifunctional DHFR-TS is a well-studied, important target of established drugs such as pyrimethamine and cycloguanil. In sharp contrast, malarial SHMT remains largely uncharacterized. In… CONTINUE READING

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