ArticleToxicon: X2026
A novel, non-invasive cnidarian venom extraction device.
Article in Toxicon: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
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Who cites it
1 citing paper in PubMed.
- Cnidarian Venoms in the Omics Era: Toxin Discovery and Bioactive Potential.Marine drugs · 2026Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cnidaria represent one of the most ancient venomous lineages with thousands of extant species and their toxins have long been known to signify a source of therapeutic potential. Despite this recognition, cnidarian toxin research has progressed relatively slowly when compared to other taxa. One of the major factors for this slow development pertains to the difficulties involved with obtaining samples, particularly from benthic species which are sessile, where dissected tissues have historically been required. Additionally, the instability of marine venoms has further hindered progression of cnidarian venom research. The research presented aimed to address these issues through the design and development of a novel, non-invasive, venom extraction device that works on a range of cnidarian species. The device functioned underwater at depths ranging from 50 mm down to 5 m whilst scuba diving and was able to successfully obtain venom samples from all 12 species tested. These species were from three taxonomic groups Actiniaria (sea anemones), Scleractinia (corals) and Scyphozoan (Jellyfish) with four species from each. These venom samples revealed the expected phospholipase A2 activity but also the four Scleractinia venoms demonstrated phospholipase A2 inhibitory properties. This is the first description of phospholipase A2 inhibitory activity in cnidarian venoms and further work is required for full characterisation.
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