IndraLab

Statements



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"Early experiments with CTX inhibition of the BK channel revealed that CTX binds to the extracellular surface of the channel with a 1:1 channel : toxin stoichiometry, that both the open and closed states of the channel are competent for toxin binding, and that electrostatic interactions play an important role in enhancing the toxin 's affinity."

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"Our result of the CTX block of hSlo was clearly bimolecular, as has been shown with native maxi-K channels (Miller et al., 1985)."

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"As expected from the idea that hypoxia inhibits BK channels leading to depolarization, one study did report that the BK channel blocker CTX depolarized glomus cells (Wyatt and Peers, 1995)."

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"XREF_BIBR The ability of CTX and IbTX to block Slo1 and MC13 channels were compared in outside-out patches (XREF_FIG)."

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"Furthermore, vessel experiments demonstrated that another BK channel blocker CTX could enhance ACh stimulated vasoconstrictions in the umbilical veins."

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"Although scorpion toxins such as iberiotoxin and charybdotoxin (CTX) can also inhibit Slo1 channels at nM concentrations, Slo1 channels containing particular auxiliary beta subunits exhibit resistance to block by such toxins."

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"When Na+ is the only internal monovalent cation, voltage no longer affects CTX block of the BK channel (MacKinnon and Miller, 1988)."

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"Tetraethylammonium is usually believed to induce a " rapid open-channel block " that reduces the apparent current flow through BK channels, while CTX reduces the probability of BK channel opening."

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"Whereas nM concentrations of CTX effectively blocked Slo1 current (XREF_FIG), concentrations of CTX up to 100 nM were without effect on MC13 current (XREF_FIG)."