ArticleNature communications2025
Structures of Native Doublet Microtubules from Trichomonas vaginalis Reveal Parasite-Specific Proteins.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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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.
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Who cites it
6 citing papers in PubMed.
- Microtubule Inner Protein CFAP77 Contributes to Sperm Motility and Male Fertility in Mice.Andrology · 2026Article
- The cytoskeleton of pathogenic protists.Bioscience reports · 2026Review
- Structure first - exploration and discovery with cryo-electron microscopy.Journal of cell science · 2026Review
- Microtubule inner proteins in apicomplexan parasites.Biochemical Society transactions · 2026Review
- Alpha-tubulin tails regulate axoneme differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Evolutionary adaptations of doublet microtubules in trypanosomatid parasites.Science (New York, N.Y.) · 2025Article
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Authors and funding
7 authors.
Funding
Abstract
Doublet microtubules (DMTs) are flagellar components required for the protist Trichomonas vaginalis (Tv) to swim through the human genitourinary tract to cause trichomoniasis, the most common non-viral sexually transmitted disease. Lack of structures of Tv's DMT (Tv-DMT) has prevented structure-guided drug design to manage Tv infection. Here, we determine the 16 nm, 32 nm, 48 nm and 96 nm-repeat structures of native Tv-DMT at resolution ranging from 3.4 to 4.4 Å by cryogenic electron microscopy (cryoEM) and built an atomic model for the entire Tv-DMT. These structures show that Tv-DMT is composed of 30 different proteins, including the α- and β-tubulin, 19 microtubule inner proteins (MIPs) and 9 microtubule outer proteins. While the A-tubule of Tv-DMT is simplistic compared to DMTs of other organisms, the B-tubule of Tv-DMT features parasite-specific proteins, such as TvFAP40 and TvFAP35. Notably, TvFAP40 and TvFAP35 form filaments near the inner and outer junctions, respectively, and interface with stabilizing MIPs. This atomic model of the Tv-DMT highlights diversity of eukaryotic motility machineries and provides a structural framework to inform rational design of therapeutics against trichomoniasis.
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