Molecular cloning and sequence analysis of the Plasmodium falciparum dihydrofolate reductase-thymidylate synthase gene.

@article{Bzik1987MolecularCA,
  title={Molecular cloning and sequence analysis of the Plasmodium falciparum dihydrofolate reductase-thymidylate synthase gene.},
  author={David J Bzik and W. B. Li and Toshihiro Horii and Joseph Inselburg},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1987},
  volume={84 23},
  pages={8360-4}
}
Genomic DNA clones that coded for the bifunctional dihydrofolate reductase (DHFR) and thymidylate synthase (TS) (DHFR-TS) activities from a pyrimethamine-sensitive strain of Plasmodium falciparum were isolated and sequenced. The deduced DHFR-TS protein contained 608 amino acids (71,682 Da). The coding region for DHFR-TS contained no intervening sequences and had a high A + T content (75%). The DHFR domain, in the amino-terminal portion of the protein, was joined by a 94-amino acid junction… CONTINUE READING

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