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Article

Functional characterization of sticholysin I and W111C mutant reveals the sequence of the actinoporin's pore assembly.

PloS one - 1 Jan 2014

Antonini Valeria, Pérez-Barzaga Victor, Bampi Silvia, Pentón David, Martínez Diana, Dalla Serra Mauro, Tejuca Mayra

Abstract excerpt

The use of pore-forming toxins in the construction of immunotoxins against tumour cells is an alternative for cancer therapy. In this protein family one of the most potent toxins are the actinoporins, cytolysins from sea anemones. We work on the construction of tumour proteinase-activated immunotoxins using sticholysin I (StI), an actinoporin isolated from the sea anemone Stichodactyla helianthus. To accomplish...

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Identifiers

PMID: 25350457
DOI: 10.1371/journal.pone.0110824
PMCID: PMC4211696

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Functional characterization of sticholysin I and W111C mutant reveals the sequence of the actinoporin's pore assembly.PMID 25350457Read ↗

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