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  • Title: Redox state dependency of HERGS631C channel pharmacology: relation to C-type inactivation.
    Author: Ulens C, Tytgat J.
    Journal: FEBS Lett; 2000 May 26; 474(1):111-5. PubMed ID: 10828461.
    Abstract:
    The S631C mutation in human ether-à-go-go-related gene (HERG) channels has previously been reported to disrupt C-type inactivation and ion-selectivity when Cys-631 is in the oxidized state. In this study, we report the relation between pharmacology and C-type inactivation for HERGS631C channels. We demonstrate that HERGS631C in its reduced state is fully blocked by 1 microM astemizole, terfenadine and dofetilide, similar to wild-type HERG channels. In contrast, oxidized HERGS631C is insensitive for these blockers. Our results suggest that an interaction with HERG channels in the inactivated state might be a common mechanism to a variety of drugs known to block HERG channels with high affinity.
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