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Cover Image
Cover Image
Cover picture: The voltage-sensor domains (VSDs) of domain I of mutated R222Q (top) and R225W (bottom) Nav1.5 channels are shown in their resting (left, green), activated (middle, red), and immobilized (right, orange) states. The gating pore permeation pathway is open during the activated and the immobilized states, resulting in an outward K+ leak and an inward Na+ leak (see research article by Moreau et al., 93–106).
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Editorial
To better serve our community: Introducing new Associate Editors and an expanded Editorial Advisory Board for 2015
We are pleased to welcome several new JGP Associate Editors and Editorial Advisory Board members.
Generally Physiological
Article
Gating pore currents are defects in common with two Nav1.5 mutations in patients with mixed arrhythmias and dilated cardiomyopathy
Nav1.5 channels bearing voltage-sensor domain mutations associated with atypical cardiac arrhythmias and dilated cardiomyopathy generate gating pore currents.
Mapping the membrane topography of the TH6–TH7 segment of the diphtheria toxin T-domain channel
Cysteine substitution accessibility analysis suggests that the TH6–TH7 segment forms a constriction in the diphtheria toxin T-domain channel.
Methods and Approaches
New method for determining total calcium content in tissue applied to skeletal muscle with and without calsequestrin
The concentration of total calcium in a skeletal muscle appears to be correlated with the muscle’s likely force requirements given by the ratio of body weight to muscle weight.
Communication
A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif
The isolated Nav channel domain IV paddle motif remains susceptible to toxins that inhibit fast inactivation.
