| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8395909 | Toxicon | 2014 | 10 Pages |
Abstract
Since AaTX1 is not highly abundant in Aa venom, it was synthesized as well as AmmTX3. Synthetic peptides, native AaTX1 and rAmmTX3 peptides showed qualitatively the same pharmacological activity. Overall, these data identify a new biologically active toxin that belongs to a family of peptides active on Kv4.3 channel.
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Authors
Saoussen Mlayah-Bellalouna, Martial Dufour, Kamel Mabrouk, Hafedh Mejdoub, Edmond Carlier, Houcemeddine Othman, Maya Belghazi, Marion Tarbe, Jean Marc Goaillard, Didier Gigmes, Michael Seagar, Mohamed El Ayeb, Dominique Debanne, Najet Srairi-Abid,