ArticleNature microbiology2022
Conoid extrusion regulates glideosome assembly to control motility and invasion in Apicomplexa.
Article in Nature microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 45 citations in OpenAlex.
- Clustering of host N-glycans by the microneme MIC1/4/6 complex licenses Toxoplasma rhoptry discharge.The EMBO journal · 2026Article
- Dual apical methyltransferases orchestrate motility initiation in apicomplexan parasites.Nature communications · 2026Article
- The human parasite, Toxoplasma gondii, is paralyzed without two components of the apical polar ring.PLoS pathogens · 2026Article
- The cytoskeleton of pathogenic protists.Bioscience reports · 2026Review
- Two anchoring proteins control daughter apical complex assembly inbioRxiv : the preprint server for biology · 2026Article
- Atomic models of the Toxoplasma cell invasion machinery.Nature structural & molecular biology · 2026Article
- Evolutionarily convergent mechanism of formin regulation coordinates actin polymerization in apicomplexan parasites.Science advances · 2025Article
- An apical ring protein essential for conoid complex assembly and daughter cell formation in Toxoplasma gondii.Nature communications · 2025Article
- RNG2 tethers the conoid to the apical polar ring in Toxoplasma gondii to enable parasite motility and invasion.PLoS biology · 2025Article
- Motility-dependent processes inmSphere · 2025Article
- Submicrometre spatiotemporal characterization of the Toxoplasma adhesion strategy for gliding motility.Nature microbiology · 2024Article
- Architecture of theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Motility-dependent processes inbioRxiv : the preprint server for biology · 2024Article
- Article
- γ-tubulin complex controls the nucleation of tubulin-based structures in Apicomplexa.Molecular biology of the cell · 2024Article
- A geometrical theory of gliding motility based on cell shape and surface flow.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Toxoplasma gondii actin filaments are tuned for rapid disassembly and turnover.Nature communications · 2024Article
- Sustained rhoptry docking and discharge requires Toxoplasma gondii intraconoidal microtubule-associated proteins.Nature communications · 2024Article
- Emergent actin flows explain distinct modes of gliding motility.Nature physics · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of Apicomplexa are defined by apical cytoskeletal structures and secretory organelles, tailored for motility, invasion and egress. Gliding is powered by actomyosin-dependent rearward translocation of apically secreted transmembrane adhesins. In the human parasite Toxoplasma gondii, the conoid, composed of tubulin fibres and preconoidal rings (PCRs), is a dynamic organelle of undefined function. Here, using ultrastructure expansion microscopy, we established that PCRs serve as a hub for glideosome components including Formin1. We also identified components of the PCRs conserved in Apicomplexa, Pcr4 and Pcr5, that contain B-box zinc-finger domains, assemble in heterodimer and are essential for the formation of the structure. The fitness conferring Pcr6 tethers the PCRs to the cone of tubulin fibres. F-actin produced by Formin1 is used by Myosin H to generate the force for conoid extrusion which directs the flux of F-actin to the pellicular space, serving as gatekeeper to control parasite motility.
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.