ReviewToxins2013
Staphylococcus aureus α-toxin: nearly a century of intrigue.
Review in Toxins, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 342 papers, 1 of them a synthesis that pooled it.
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
342 citing papers in PubMed, 1 synthesis or guideline pooled it, 593 citations in OpenAlex.
- Host-Bacterium Interaction Mechanisms inInternational journal of molecular sciences · 2023Pooled it
- Article
- Evaluating the potential of Cajanus cajan (L.) Millsp. Root to improve atopic dermatitis with different anti-inflammatory models and active compounds.Journal of food and drug analysis · 2026Article
- Acidic and alkaline conditions enhance Staphylococcus aureus α-toxin pore formation and cytotoxicity.PLoS pathogens · 2026Article
- High-Throughput Characterization of Human Fibroblast Responses to a Panel ofOpen forum infectious diseases · 2026Article
- Multidrug-resistant livestock-associated ST9-MRSA causing severe human infection without animal exposure: the food chain as a potential transmission route in China.Archives of microbiology · 2026Article
- Article
- Article
- Virulence Determinants, Antimicrobial Resistance, and Biofilm Formation ofFoods (Basel, Switzerland) · 2026Article
- Genotypic and phenotypic features of MRSA with an incomplete hemolysis phenotype in a tertiary teaching hospital in China.BMC microbiology · 2026Article
- Reduced efficacy of an anti-toxin vaccine from senescence-driven attenuation of toxin virulence.JCI insight · 2026Article
- Multivalent nanobodies for potent and broad neutralization of Staphylococcus aureus toxins.Nature communications · 2026Article
- Genetic determinants of Staphylococcus aureus adhesion shape virulence trade-offs in bacteremia.Nature communications · 2026Article
- Adeno-associated virus delivery of anti-alpha toxin monoclonal antibodies confers protection against Staphylococcus aureus infections.PLoS pathogens · 2026Article
- An Imidazo[2,1-b][1,3,4]thiadiazole Derivative Inhibits the Virulence Factor α-Hemolysin by Blocking the Pullout of Its Stem Domain.ChemMedChem · 2026Article
- Beyond Antibiotics: Therapeutic Strategies Utilizing Probiotics and Bacteriophages Against Drug-ResistantMicroorganisms · 2026Review
- Article
- Microbiome dysbiosis and therapeutic restoration in atopic dermatitis.Frontiers in cellular and infection microbiology · 2026Review
- Solithromycin mitigatesFrontiers in cellular and infection microbiology · 2026Article
- Influence of substitution patterns on the antimicrobial properties of pyrrole sulfonamide scaffolds.Frontiers in chemistry · 2026Article
282 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Staphylococcus aureus secretes a number of host-injurious toxins, among the most prominent of which is the small β-barrel pore-forming toxin α-hemolysin. Initially named based on its properties as a red blood cell lytic toxin, early studies suggested a far greater complexity of α-hemolysin action as nucleated cells also exhibited distinct responses to intoxication. The hemolysin, most aptly referred to as α-toxin based on its broad range of cellular specificity, has long been recognized as an important cause of injury in the context of both skin necrosis and lethal infection. The recent identification of ADAM10 as a cellular receptor for α-toxin has provided keen insight on the biology of toxin action during disease pathogenesis, demonstrating the molecular mechanisms by which the toxin causes tissue barrier disruption at host interfaces lined by epithelial or endothelial cells. This review highlights both the historical studies that laid the groundwork for nearly a century of research on α-toxin and key findings on the structural and functional biology of the toxin, in addition to discussing emerging observations that have significantly expanded our understanding of this toxin in S. aureus disease. The identification of ADAM10 as a proteinaceous receptor for the toxin not only provides a greater appreciation of truths uncovered by many historic studies, but now affords the opportunity to more extensively probe and understand the role of α-toxin in modulation of the complex interaction of S. aureus with its human host.
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.