Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The structure of Plasmodium falciparum hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase reveals the basis of sulfa resistance.

The FEBS journal - 1 Aug 2020

Chitnumsub Penchit, Jaruwat Aritsara, Talawanich Yuwadee, Noytanom Krittikar, Liwnaree Benjamas, Poen Sinothai, Yuthavong Yongyuth

Abstract excerpt

The clinical efficacy of sulfa drugs as antimalarials has declined owing to the evolution of resistance in Plasmodium falciparum (Pf) malaria parasites. In order to understand the basis of this resistance and to design more effective antimalarials, we have solved 13 structures of the bifunctional enzyme 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK)-dihydropteroate synthase (DHPS) from wild-type (WT)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antimalarials
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Dihydropteroate Synthase

Share to Drug Resistance

Share to Malaria, Falciparum

Share to Plasmodium falciparum

Share to Sequence Homology

Source

Identifiers

PMID: 31883412
DOI: 10.1111/febs.15196

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The structure of Plasmodium falciparum hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase reveals the basis of sulfa resistance.PMID 31883412Read ↗

Structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium vivax sheds light on drug resistance.Semantic proximity Read ↗

Mutations in dihydropteroate synthase are responsible for sulfone and sulfonamide resistance in Plasmodium falciparum.Semantic proximity Read ↗

Global Analysis of Plasmodium falciparum Dihydropteroate Synthase Variants Associated with Sulfadoxine Resistance Reveals Variant Distribution and Mechanisms of Resistance: A Computational-Based Study.Semantic proximity Read ↗

Sequence variation of the hydroxymethyldihydropterin pyrophosphokinase: dihydropteroate synthase gene in lines of the human malaria parasite, Plasmodium falciparum, with differing resistance to sulfadoxine.Semantic proximity Read ↗

The Structural and Functional Basis for Recurring Sulfa Drug Resistance Mutations in Staphylococcus aureus Dihydropteroate SynthaseSemantic proximity Read ↗

Resistance to antifolates in Plasmodium falciparum, the causative agent of tropical malaria.Semantic proximity Read ↗

Novel K540N mutation in Plasmodium falciparum dihydropteroate synthetase confers a lower level of sulfa drug resistance than does a K540E mutation.Semantic proximity Read ↗

Structure, evolution, and inhibitor interaction of S‐adenosyl‐ L ‐homocysteine hydrolase from Plasmodium falciparumSemantic proximity Read ↗

Discovery of some phenylhydrazones as potential antimalarials: An integrated computational approach on PfATP6 and PfDHFR mutant proteinsSemantic proximity Read ↗

Structure and function of the dihydropteroate synthase from Staphylococcus aureus.Semantic proximity Read ↗

Dihydropteroate synthase mutations in Pneumocystis jiroveci can affect sulfamethoxazole resistance in a Saccharomyces cerevisiae model.Semantic proximity Read ↗

Molecular mechanism of plasmid-borne resistance to sulfonamidesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.