ArticleScientific reports2011
Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery.
Article in Scientific reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 41 citations in OpenAlex.
- Trx4, a novel thioredoxin protein, is important for Toxoplasma gondii fitness.Parasites & vectors · 2024Article
- Transport mechanisms at the malaria parasite-host cell interface.PLoS pathogens · 2021Review
- Redox interactome in malaria parasite Plasmodium falciparum.Parasitology research · 2021Review
- Development of a target identification approach using native mass spectrometry.Scientific reports · 2021Article
- Genomic and transcriptomic evidence for descent from Plasmodium and loss of blood schizogony in Hepatocystis parasites from naturally infected red colobus monkeys.PLoS pathogens · 2020Article
- The parasitophorous vacuole of the blood-stage malaria parasite.Nature reviews. Microbiology · 2020Review
- Crossing the Vacuolar Rubicon: Structural Insights into Effector Protein Trafficking in Apicomplexan Parasites.Microorganisms · 2020Review
- Functional Characterization of Two Thioredoxin Proteins ofFrontiers in veterinary science · 2020Article
- Characterization of TrxC, an Atypical Thioredoxin Exclusively Present in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2018Article
- Molecular characterization of Babesia microti thioredoxin (BmTrx2) and its expression patterns induced by antiprotozoal drugs.Parasites & vectors · 2018Article
- Binding of phenothiazines into allosteric hydrophobic pocket of human thioredoxin 1.European biophysics journal : EBJ · 2016Article
- Structural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug design.Protein science : a publication of the Protein Society · 2015Article
- Crystal structure and solution characterization of the thioredoxin-2 from Plasmodium falciparum, a constituent of an essential parasitic protein export complex.Biochemical and biophysical research communications · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Thioredoxins are vital components of Plasmodium proteome and act as both reducing agents and protein disulfide reductases. The malaria parasite P. falciparum thioredoxin-2 (PfTrx-2) is part of the multi-protein complex embedded within the parasite parasitophorous vacuolar membrane (PVM) which purportedly directs protein secretion. We have characterized structural and enzymatic features of PfTrx-2, and we show that PfTrx-2 adopts a canonical thioredoxin fold but with significant structural differences in its N-terminus. Our confocal localization data suggest distinct PVM residency of PfTrx-2. Based on the crystal structure of PfTrx-2, we screened and tested small molecule drug-like libraries for compounds which target unique structural features of PfTrx-2. Disruption of PfTrx-2 interactions using specific inhibitors may result in a dysfunctional parasite translocon that is rendered unable to secrete pathogenic proteins into hosts. This approach therefore offers a new focus for anti-malarial drug development.
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