ArticlePLoS pathogens2014
Structural differences explain diverse functions of Plasmodium actins.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
41 citing papers in PubMed, 77 citations in OpenAlex.
- Highly divergent apicomplexan cytoskeletons provide additional models for actin biology.The FEBS journal · 2025Review
- Plasmodium actin-like proteins are essential for DNA segregation during male gametogenesis and malaria transmission.PLoS pathogens · 2025Article
- The divergent intron-containing actin in sponge morphogenetic processes.NAR genomics and bioinformatics · 2025Article
- Fungal-derived methyldeoxaphomins targetProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Computational approach for decoding malaria drug targets from single-cell transcriptomics and finding potential drug molecule.Scientific reports · 2024Article
- Toxoplasma gondii actin filaments are tuned for rapid disassembly and turnover.Nature communications · 2024Article
- Article
- Plasmodium falciparum formins are essential for invasion and sexual stage development.Communications biology · 2023Article
- Structure and function of Plasmodium actin II in the parasite mosquito stages.PLoS pathogens · 2023Article
- Divergent Plasmodium actin residues are essential for filament localization, mosquito salivary gland invasion and malaria transmission.PLoS pathogens · 2022Article
- Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite.Nature communications · 2022Article
- High-resolution structures of malaria parasite actomyosin and actin filaments.PLoS pathogens · 2022Article
- Structure and function of an atypical homodimeric actin capping protein from the malaria parasite.Cellular and molecular life sciences : CMLS · 2022Article
- The malaria parasite chaperonin containing TCP-1 (CCT) complex: Data integration with other CCT proteomes.Frontiers in molecular biosciences · 2022Article
- The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.Nature communications · 2021Article
- Unusual dynamics of the divergent malaria parasiteProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism.Nature communications · 2019Article
- Formin-2 drives polymerisation of actin filaments enabling segregation of apicoplasts and cytokinesis ineLife · 2019Article
- Atomic view into Plasmodium actin polymerization, ATP hydrolysis, and fragmentation.PLoS biology · 2019Article
- Inter-subunit interactions drive divergent dynamics in mammalian and Plasmodium actin filaments.PLoS biology · 2018Article
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 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than α-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.
Indexed as
Identifiers
What OpenQuestion holds
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.