T
Tony Triglia
Researcher at Walter and Eliza Hall Institute of Medical Research
Publications - 81
Citations - 7357
Tony Triglia is an academic researcher from Walter and Eliza Hall Institute of Medical Research. The author has contributed to research in topics: Plasmodium falciparum & Antigen. The author has an hindex of 38, co-authored 76 publications receiving 6954 citations. Previous affiliations of Tony Triglia include University of Melbourne & Royal Melbourne Hospital.
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A procedure for in vitro amplification of DNA segments that lie outside the boundaries of known sequences
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Mutations in dihydropteroate synthase are responsible for sulfone and sulfonamide resistance in Plasmodium falciparum
TL;DR: In this paper, the authors show that the amino acid differences in the enzyme dihydropteroate synthase (DHPS) enzyme of sulfadoxine-resistant isolates of P. falciparum are central to resistance to sulfones and sulfonamides.
Mutations in dihydropteroate synthase are responsible for sulfone and sulfonamide resistance in Plasmodium falciparum (malariaysulfadoxineydrug resistance)
TL;DR: Results show that the amino acid differences in the DHPS enzyme of sulfadoxine-resistant isolates of P. falciparum are central to the mechanism of resistance to sulfones and sulfonamides.
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Apical membrane antigen 1 plays a central role in erythrocyte invasion by Plasmodium species
Tony Triglia,Julie Healer,Sonia R. Caruana,Anthony N. Hodder,Anthony N. Hodder,Robin F. Anders,Robin F. Anders,Brendan S. Crabb,Alan F. Cowman +8 more
TL;DR: It is shown that PcAMA1 expression in P. falciparum provides trans‐species complementation to at least 35% of the function of endogenous PfAMA1 in human red cells, which indicates an important role for AMA1 in the invasion of red blood cells (RBCs) across divergent Plasmodium species.
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Primary structure and expression of the dihydropteroate synthetase gene of Plasmodium falciparum
Tony Triglia,Alan F. Cowman +1 more
TL;DR: The cloning and sequencing of the gene encoding the P. falciparum DHPS enzyme is described and it is shown that it is a bifunctional enzyme that includes dihydro-6-hydroxymethylpterin pyrophosphokinase at the N terminus of DHPS.