| Institute | Top | Institute | Publication | Universiteit Antwerpen; Faculteit Farmaceutische, Biomedische en Diergeneeskundige Wetenschappen; Laboratory for Molecular Biophysics, Physiology and Pharmacology, moreInstitutional address:
Campus Drie Eiken, building T
room T5.35
Universiteitsplein 1
2610 Wilrijk
Belgium
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| Publications (6) | Top | Institute | Publication | | A1 Publications (6) [show] | - Kopljar, I.; Grottesi, A.; de Block, T.; Rainier, J.D.; Tytgat, J.; Labro, A.J.; Snyders, D.J. (2016). Voltage-sensor conformation shapes the intra-membrane drug binding site that determines gambierol affinity in Kv channels. Neuropharmacology 107: 160-167. https://dx.doi.org/10.1016/j.neuropharm.2016.03.010, more
- Martínez-Morales, E.; Kopljar, I.; Rainier, J.D.; Tytgat, J.; Snyders, D.J.; Labro, A.J. (2016). Gambierol and n-alkanols inhibit Shaker Kv channel via distinct binding sites outside the K+ pore. Toxicon 120: 57-60. https://dx.doi.org/10.1016/j.toxicon.2016.07.017, more
- Kopljar, I.; Labro, A.J.; de Block, T.; Rainier, J.; Tytgat, J.; Snyders, D.J. (2013). The ladder-shaped polyether toxin gambierol anchors the gating machinery of Kv3.1 channels in the resting state. J. Gen. Physiol. 141(3): 359-369. https://dx.doi.org/10.1085/jgp.201210890, more
- Stas, J.; Kopljar, I.; Labro, A.; Peigneur, S.; Zaharenko, A.J.; Tytgat, J.; Snyders, D.J. (2013). A gating modulator peptide toxin for Shaker-type Kv1 channels derived from the sea anemone Bunodosoma cangicum. Biophys. J. 104(2): 125A-125A, more
- Kopljar, I.; Labro, A.J.; Rainier, J.D.; Tytgat, J.; Snyders, D.J. (2012). Voltage sensor trapping in voltage-gated K-channels by the marine neurotoxin Gambierol. Toxicon 60(2): 150-151. dx.doi.org/10.1016/j.toxicon.2012.04.111, more
 Kopljar, I.; Labro, A.J.; Cuypers, E.; Johnson, H.W.B.; Rainier, J.D.; Tytgat, J.; Snyders, D.J. (2009). A polyether biotoxin binding site on the lipid-exposed face of the pore domain of Kv channels revealed by the marine toxin gambierol. Proc. Natl. Acad. Sci. U.S.A. 106(24): 9896-9901. http://dx.doi.org/10.1073/pnas.0812471106, more
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