{"refrec":{"BRefID":285471,"RR":"<b>Martínez-Morales, E.; Kopljar, I.; Rainier, J.D.; Tytgat, J.; Snyders, D.J.; Labro, A.J.</b> (2016). Gambierol and n-alkanols inhibit <i>Shaker</i> Kv channel via distinct binding sites outside the K+ pore. <i>Toxicon 120</i>: 57-60. <a href=\"https://dx.doi.org/10.1016/j.toxicon.2016.07.017\" target=\"_blank\">https://dx.doi.org/10.1016/j.toxicon.2016.07.017</a>","BEntID":277496,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Toxicon 120</i>: 57-60. <a href=\"https://dx.doi.org/10.1016/j.toxicon.2016.07.017\" target=\"_blank\">https://dx.doi.org/10.1016/j.toxicon.2016.07.017</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Martínez-Morales, E.; Kopljar, I.; Rainier, J.D.; Tytgat, J.; Snyders, D.J.; Labro, A.J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Martínez-Morales, E. <i>et al.</i>","Englishabstract":"The marine polycyclic-ether toxin gambierol and 1-butanol (n-alkanol) inhibit <i>Shaker</i>-type K<sub>v</sub> channels by interfering with the gating machinery. Competition experiments indicated that both compounds do not share an overlapping binding site but gambierol is able to affect 1-butanol affinity for <i>Shaker</i> through an allosteric effect. Furthermore, the <i>Shaker</i>-P475A mutant, which inverses 1-butanol effect, is inhibited by gambierol with nM affinity. 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