{"refrec":{"BRefID":121606,"RR":"<b>Bosmans, F.; Tytgat, J.</b> (2007). Sea anemone venom as a source of insecticidal peptides acting on voltage-gated Na<sup>+</sup> channels. <i>Toxicon 49(4)</i>: 550-560. <a href=\"http://dx.doi.org/10.1016/j.toxicon.2006.11.029\" target=\"_blank\">dx.doi.org/10.1016/j.toxicon.2006.11.029</a>","BEntID":115699,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Toxicon 49(4)</i>: 550-560. <a href=\"https://dx.doi.org/10.1016/j.toxicon.2006.11.029\" target=\"_blank\">https://dx.doi.org/10.1016/j.toxicon.2006.11.029</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Bosmans, F.; Tytgat, J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Bosmans, F.; Tytgat, J.","Englishabstract":"Sea anemones produce a myriad of toxic peptides and proteins of which a large group acts on voltage-gated Na<sup>+</sup> channels. However, in comparison to other organisms, their venoms and toxins are poorly studied. Most of the known voltage-gated Na<sup>+</sup> channel toxins isolated from sea anemone venoms act on neurotoxin receptor site 3 and inhibit the inactivation of these channels. Furthermore, it seems that most of these toxins have a distinct preference for crustaceans. Given the close evolutionary relationship between crustaceans and insects, it is not surprising that sea anemone toxins also profoundly affect insect voltage-gated Na<sup>+</sup> channels, which constitutes the scope of this review. For this reason, these peptides can be considered as insecticidal lead compounds in the development of insecticides. 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