ArticleScience (New York, N.Y.)2015
ACTIN-DIRECTED TOXIN. ACD toxin-produced actin oligomers poison formin-controlled actin polymerization.
Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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.
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Who cites it
38 citing papers in PubMed, 54 citations in OpenAlex.
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- 3D printing cytoskeletal networks: ROS-induced filament severing leads to surge in actin polymerization.bioRxiv : the preprint server for biology · 2025Article
- Antagonistic Effects of Actin-Specific Toxins onBiomolecules · 2024Article
- Antagonistic effects of actin-specific toxins onbioRxiv : the preprint server for biology · 2024Article
- Stabilization of F-actin by Salmonella effector SipA resembles the structural effects of inorganic phosphate and phalloidin.Structure (London, England : 1993) · 2024Article
- Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024Article
- Stabilization of F-actin bybioRxiv : the preprint server for biology · 2023Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- Membrane-dependent actin polymerization mediated by the Legionella pneumophila effector protein MavH.PLoS pathogens · 2023Article
- Functional Mimicry of Eukaryotic Actin Assembly by Pathogen Effector Proteins.International journal of molecular sciences · 2022Review
- Article
- Allosteric regulation controls actin-bundling properties of human plastins.Nature structural & molecular biology · 2022Article
- Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode.Nature communications · 2022Article
- Identification of Type VI Secretion Systems Effector Proteins That Contribute to Interbacterial Competition inFrontiers in microbiology · 2022Article
- Beyond dueling: roles of the type VI secretion system in microbiome modulation, pathogenesis and stress resistance.Stress biology · 2021Review
- Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
The actin cross-linking domain (ACD) is an actin-specific toxin produced by several pathogens, including life-threatening spp. of Vibrio cholerae, Vibrio vulnificus, and Aeromonas hydrophila. Actin cross-linking by ACD is thought to lead to slow cytoskeleton failure owing to a gradual sequestration of actin in the form of nonfunctional oligomers. Here, we found that ACD converted cytoplasmic actin into highly toxic oligomers that potently "poisoned" the ability of major actin assembly proteins, formins, to sustain actin polymerization. Thus, ACD can target the most abundant cellular protein by using actin oligomers as secondary toxins to efficiently subvert cellular functions of actin while functioning at very low doses.
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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.