Ping Wang
University of Manchester
20 Papers
190 Citations
Ping Wang is an academic researcher from University of Manchester. The author has contributed to research in topics: Plasmodium falciparum & Dihydropteroate. The author has an hindex of 18, co-authored 20 publications.
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Papers
Sequence Variation of the Hydroxymethyldihydropterin Pyrophosphokinase: Dihydropteroate Synthase Gene in Lines of the Human Malaria Parasite, Plasmodium falciparum, with Differing Resistance to Sulfadoxine
TL;DR: To investigate a possible genetic basis for clinical resistance to sulfa drugs, the complete H2Pte synthase domains from eleven isolates of P. falciparum with diverse geographical origins and levels of sulfadoxine resistance were sequenced.
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Sulfadoxine resistance in the human malaria parasite Plasmodium falciparum is determined by mutations in dihydropteroate synthetase and an additional factor associated with folate utilization.
TL;DR: A profound influence of exogenous folate on IC50 values, which, under physiological conditions, may have a major role in determining resistance levels, has major implications for the acquisition of Fansidar resistance by malaria parasites.
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A modified in vitro sulfadoxine susceptibility assay for Plasmodium falciparum suitable for investigating Fansidar resistance
TL;DR: Conditions which better control the levels of the drug antagonists folate and p-aminobenzoate are defined, yielding reproducible differences between lines of P. falciparum with differing alleles of the dihydropteroatic synthetase gene, which encodes the target enzyme of SDX.
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Transcriptional analysis of genes encoding enzymes of the folate pathway in the human malaria parasite Plasmodium falciparum.
TL;DR: Although conventionally regarded as performing housekeeping functions, these genes show disparate levels of and changes in expression through the cell cycle, but respond quite uniformly to folate pathway‐specific stress factors, with no evidence of feedback at the transcriptional level.
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An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites.
Sabine Dittrich,Sarah L. Mitchell,Andrew M. Blagborough,Qi Wang,Ping Wang,Paul F. G. Sims,John E. Hyde +6 more
TL;DR: It is demonstrated that P.’falciparum cell extracts lack detectable DHNA activity, but that the parasite possesses an unusual orthologue of 6‐pyruvoyltetrahydropterin synthase (PTPS), which can provide a bypass for the missingDHNA activity and thus a means of completing the biosynthetic pathway from GTP to dihydrofolate.
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