Worachart SirawarapornMahidol University2018-07-042018-07-041998-12-01Drug Resistance Updates. Vol.1, No.6 (1998), 397-406136876462-s2.0-0000715174https://repository.li.mahidol.ac.th/handle/123456789/18273The dihydrofolate reductase (DHFR, EC 1.5.1.3) domain of Plasmodium falciparum bifunctional dihydrofolate reductase-thymidylate synthase (DHFR-TS) is an attractive target of two important antifolate antimalarials: pyrimethamine (Pyr) and cycloguanil (Cyc). Over recent years, knowledge of malarial DHFR and mechanism(s) of antifolate resistance have increased substantially. These observations have provided an important framework for better understanding the molecular basis of antifolate resistance in malaria. This article provides a brief review and update on molecular aspects relevant to antifolate resistance in malaria. © 1998 Harcourt Brace & Co. Ltd All rights reserved.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyMedicinePharmacology, Toxicology and PharmaceuticsReviewSCOPUS10.1016/S1368-7646(98)80015-0