ArticlePLoS pathogens2010
A small-molecule inhibitor of T. gondii motility induces the posttranslational modification of myosin light chain-1 and inhibits myosin motor activity.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 44 citations in OpenAlex.
- Identification of UCB-9721 as a potent inhibitor of MyoA, the essential class XIV myosin motor of apicomplexan parasites.bioRxiv : the preprint server for biology · 2026Article
- Emergent actin flows explain distinct modes of gliding motility.Nature physics · 2024Article
- TgMORN2, a MORN Family Protein Involved in the Regulation of Endoplasmic Reticulum Stress inInternational journal of molecular sciences · 2023Article
- MyosinA is a druggable target in the widespread protozoan parasite Toxoplasma gondii.PLoS biology · 2023Article
- A comprehensive ultrastructural analysis of the Toxoplasma gondii cytoskeleton.Parasitology research · 2022Article
- The BCC7 Protein Contributes to theInternational journal of molecular sciences · 2022Article
- Dual-Stage Picolinic Acid-Derived Inhibitors ofACS medicinal chemistry letters · 2020Article
- Targeting malaria parasite invasion of red blood cells as an antimalarial strategy.FEMS microbiology reviews · 2019Review
- Gliding motility powers invasion and egress in Apicomplexa.Nature reviews. Microbiology · 2017Review
- Direct measurement of cortical force generation and polarization in a living parasite.Molecular biology of the cell · 2017Article
- Article
- Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?Acta crystallographica. Section F, Structural biology communications · 2015Review
- A Toxoplasma gondii class XIV myosin, expressed in Sf9 cells with a parasite co-chaperone, requires two light chains for fast motility.The Journal of biological chemistry · 2014Article
- Calcium-dependent phosphorylation alters class XIVa myosin function in the protozoan parasite Toxoplasma gondii.Molecular biology of the cell · 2014Article
- The calcium-dependent protein kinase 3 of toxoplasma influences basal calcium levels and functions beyond egress as revealed by quantitative phosphoproteome analysis.PLoS pathogens · 2014Article
- Cloning and molecular characterization of a myosin light chain gene from Puccinia striiformis f. sp. tritici.World journal of microbiology & biotechnology · 2014Article
- Article
- The toxoplasma Acto-MyoA motor complex is important but not essential for gliding motility and host cell invasion.PloS one · 2014Article
- Myosin light chains: Teaching old dogs new tricks.Bioarchitecture · 2014Review
- Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Toxoplasma gondii is an obligate intracellular parasite that enters cells by a process of active penetration. Host cell penetration and parasite motility are driven by a myosin motor complex consisting of four known proteins: TgMyoA, an unconventional Class XIV myosin; TgMLC1, a myosin light chain; and two membrane-associated proteins, TgGAP45 and TgGAP50. Little is known about how the activity of the myosin motor complex is regulated. Here, we show that treatment of parasites with a recently identified small-molecule inhibitor of invasion and motility results in a rapid and irreversible change in the electrophoretic mobility of TgMLC1. While the precise nature of the TgMLC1 modification has not yet been established, it was mapped to the peptide Val46-Arg59. To determine if the TgMLC1 modification is responsible for the motility defect observed in parasites after compound treatment, the activity of myosin motor complexes from control and compound-treated parasites was compared in an in vitro motility assay. TgMyoA motor complexes containing the modified TgMLC1 showed significantly decreased motor activity compared to control complexes. This change in motor activity likely accounts for the motility defects seen in the parasites after compound treatment and provides the first evidence, in any species, that the mechanical activity of Class XIV myosins can be modulated by posttranslational modifications to their associated light chains.
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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.