ArticleNature communications2013
Spatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytes.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
49 citing papers in PubMed, 96 citations in OpenAlex.
- Article
- The inner membrane complex protein, IMC55, is dispensable for intra-erythrocytic development ofbioRxiv : the preprint server for biology · 2025Article
- Functional characterisation of components in two Plasmodium falciparum Cullin-RING-Ligase complexes.Scientific reports · 2025Article
- Targeting Bottlenecks in Malaria Transmission: Antibody-Epitope Descriptions Guide the Design of Next-Generation Biomedical Interventions.Immunological reviews · 2025Review
- Sequence elements within the PEXEL motif and its downstream region modulate PTEX-dependent protein export in Plasmodium falciparum.Traffic (Copenhagen, Denmark) · 2024Article
- Time-resolved proximity biotinylation implicates a porin protein in export of transmembrane malaria parasite effectors.Journal of cell science · 2023Article
- Three-dimensional structured illumination microscopy with enhanced axial resolution.Nature biotechnology · 2023Article
- PTEX helps efficiently traffic haemoglobinases to the food vacuole in Plasmodium falciparum.PLoS pathogens · 2023Article
- Toxoplasma ERK7 protects the apical complex from premature degradation.The Journal of cell biology · 2023Article
- Dissecting EXP2 sequence requirements for protein export in malaria parasites.Frontiers in cellular and infection microbiology · 2023Article
- The Plasmodium falciparum parasitophorous vacuole protein P113 interacts with the parasite protein export machinery and maintains normal vacuole architecture.Molecular microbiology · 2022Article
- Protein Sorting in Plasmodium Falciparum.Life (Basel, Switzerland) · 2021Review
- A single-cell atlas of Plasmodium falciparum transmission through the mosquito.Nature communications · 2021Article
- Transport mechanisms at the malaria parasite-host cell interface.PLoS pathogens · 2021Review
- AGIA Tag System for Ultrastructural Protein Localization Analysis in Blood-StageFrontiers in cellular and infection microbiology · 2021Article
- The Modular Circuitry of Apicomplexan Cell Division Plasticity.Frontiers in cellular and infection microbiology · 2021Review
- Plasmodium falciparum parasites exit the infected erythrocyte after haemolysis with saponin and streptolysin O.Parasitology research · 2020Article
- Plasmodium translocon component EXP2 facilitates hepatocyte invasion.Nature communications · 2020Article
- Contacting domains segregate a lipid transporter from a solute transporter in the malarial host-parasite interface.Nature communications · 2020Article
- Directing traffic: Chaperone-mediated protein transport in malaria parasites.Cellular microbiology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Export of proteins into the infected erythrocyte is critical for malaria parasite survival. The majority of effector proteins are thought to export via a proteinaceous translocon, resident in the parasitophorous vacuole membrane surrounding the parasite. Identification of the Plasmodium translocon of exported proteins and its biochemical association with exported proteins suggests it performs this role. Direct evidence for this, however, is lacking. Here using viable purified Plasmodium falciparum merozoites and three-dimensional structured illumination microscopy, we investigate remodelling events immediately following parasite invasion. We show that multiple complexes of the Plasmodium translocon of exported proteins localize together in foci that dynamically change in clustering behaviour. Furthermore, we provide conclusive evidence of spatial association between exported proteins and exported protein 2, a core component of the Plasmodium translocon of exported proteins, during native conditions and upon generation of translocation intermediates. These data provide the most direct cellular evidence to date that protein export occurs at regions of the parasitophorous vacuole membrane housing the Plasmodium translocon of exported proteins complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.