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Inactivation of sodium channels terminates the sodium current responsible for initiation of action potentials in excitable cells. A hydrophobic sequence (isoleucine-phenylalanine-methionine, IFM), located in the inactivation gate segment connecting homologous domains III and IV of the sodium channel alpha subunit, is required for fast inactivation. A(More)
Two human subjects fixated a small light oscillating sinusoidally. After the light disappeared, sinusoidal post-pursuit eye motion (PPEM) continued to follow the unexpected trajectory of targets oscillating at 0.8 and 1.0 Hz. Saccades corrected differences between eye and expected target position during PPEM in complete darkness. Predictive tracking, the(More)
We analyzed the kinetics of interaction between the peptide KIFMK, containing the isoleucine, phen-ylalanine, and methionine (IFM) motif from the inactivation gate, and the brain type IIA sodium channels with a mutation that disrupts inactivation (F1489Q). The on-rate constant was concentration dependent, consistent with a bimolecular reaction with open(More)
Inactivation of sodium channels is thought to be mediated by an inactivation gate formed by the intracellular loop connecting domains III and IV. A hydrophobic motif containing the amino acid sequence isoleucine, phenylalanine, and methionine (IFM) is required for the inactivation process. Peptides containing the IFM motif, when applied to the cytoplasmic(More)
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