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Generally Physiological


Voltage dependence of permeation enhances Ca2+ influx through CaV2.2 channels relative to that of other ions at depolarized voltages.

C-type inactivation in K+ channels is enhanced by external Ca2+ or La3+, consistent with a mechanism which involves dilation of the outer pore.

Analyses of toxin binding to a homology model of Nav1.4 indicate similar folding of the outer pore region in eukaryotic and prokaryotic sodium channels.

The selectivity of acid-sensing ion channels to cations depends on interactions with binding sites both within the pore and in the outer vestibule.

Fluc channels protect bacteria from accumulating F in acidic environments.


Cardiac ryanodine receptors (RyR2) from humans, rats, and sheep show differential sensitivity to calcium and magnesium, with regulation of human RyR2 resembling that of sheep more than that of rat.

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