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The cytoplasmic “cage” domain of the bacterial MscS channel senses macromolecular crowding to promote channel inactivation and prevent excessive loss of small osmolytes.

Angiotensin signaling promotes interactions between AKAP150, PKC, and TRPV4 channels to form signaling domains that control Ca2+ influx into arterial myocytes.

Numerical modeling indicates that hierarchical clustering of ryanodine receptors in cells of the sinoatrial node is crucial to the calcium clock and thereby to regulation of heart rate.

Ca2+ movements during intercall intervals in superfast toadfish swimbladder muscle fibers depend on the accumulation of Ca2+ on parvalbumin and a consequent slow rate of Ca2+ pumping.

Residue E165, in transmembrane helix 3, participates in formation of the dilated pore of the 2-APB–activated Orai3 channel but not that of the more selective store-operated Orai3 pore.

Singlet oxygen acts through a histidine residue to delay HCN channel deactivation and enhance voltage-insensitive current.

Conserved acidic and aromatic residues in the four sodium channel voltage-sensor domains make domain-specific functional contributions.

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