Tao and Corry investigate how the binding of sodium channel inhibitors to the Na_v1.5 pore using simulations reveal promiscuous, polyspecific binding at the fenestrations and central cavity. These findings shed light on diverse ways drugs inhibit the channel, offering insights for improving therapeutic development for conditions like chronic pain, epilepsy, and cardiac arrhythmias.

Apel et al. demonstrate that the calcium-binding protein S100A1 binds the N2A region of titin and that binding is regulated through calcium concentration and pH. Their work suggests that this interaction is a physiological sensor to regulate titin function in the muscle.

Picollo and Pusch present ALLIN (Annotation of sequence aLignment and structuraL ProteIn visualizatioN), a web interface to generate an interactive HTML page for the simultaneous visualization of annotated protein sequences alignment and 3-D structures or homology models of the related proteins.

Defective Ca²⁺ signaling in muscle cells is thought to play a role in Duchenne muscular dystrophy. Schreiber et al. report that voltage-activated SR Ca²⁺ release is moderately depressed in muscle fibers isolated from a rat model that reproduces the human disease well.

Gupta et al. show that Pannexin 1 (PANX1) channels can function as both hexamers and heptamers, but that heptameric PANX1 shows higher conductance, longer mean open times, and supports greater ATP release and dye uptake. Structurally distinct mechanisms underlie C-tail cleavage and receptor-mediated PANX1 activation.

In this study, McIlvried, Del Rosario, and colleagues show that mechanisms of adaptive plasticity are engaged in mouse and human sensory neurons after sustained depolarization. This phenomenon is reversible and involves alterations of voltage-gated sodium channel currents.

In this study, Beaudoin et al. investigate the structural effects of N-linked glycosylation on Na_V channels using molecular modeling and dynamics simulations. They show that isoform-specific glycosylation on Na_V1.5 and Na_V1.8 alters the binding sites of regulatory β-subunits, potentially contributing to β-subunit homo-oligomerization and Na_V channel supramolecular clustering.