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Potassium Channels, Voltage-Gated
Coupling of voltage sensing to channel opening reflects intrasubunit interactions in kv channels.
A polyether biotoxin binding site on the lipid-exposed face of the pore domain of Kv channels revealed by the marine toxin gambierol.
Conserved negative charges in the N-terminal tetramerization domain mediate efficient assembly of Kv2.1 and Kv2.1/Kv6.4 channels.
KCNQ1 channels voltage dependence through a voltage-dependent binding of the S4-S5 linker to the pore domain.
Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by non-interacting residues.
Phosphatidylinositol-4,5-bisphosphate (PIP(2)) stabilizes the open pore conformation of the Kv11.1 (hERG) channel.
The ladder-shaped polyether toxin gambierol anchors the gating machinery of Kv3.1 channels in the resting state.
Modulation of Closed-State Inactivation in Kv2.1/Kv6.4 Heterotetramers as Mechanism for 4-AP Induced Potentiation.
Alkanols inhibit voltage-gated K(+) channels via a distinct gating modifying mechanism that prevents gate opening.
Determining the correct stoichiometry of Kv2.1/Kv6.4 heterotetramers, functional in multiple stoichiometrical configurations.
The Selectivity Filter Is Involved in the U-Type Inactivation Process of Kv2.1 and Kv3.1 Channels.
Immunosuppressive effects of new thiophene-based KV1.3 inhibitors.
Voltage Gated Potassium Channels