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The pore-forming activity of PFT actinoporins, such as Equinatoxin II (EqtII) and Frageceatoxin C (FraC), isolated from the sea anemones Actinia equina and Actinia fragacea , respectively, is boosted by the presence of Sphingomyelin (SM) in the target membrane, which acts as a receptor for these toxins, enhancing their binding through interaction with multiple binding sites [71,72,73,74,75]

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