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    Cover picture: External potassium (K+) enhances K channel blockade by the permeating blocker barium (Ba2+) by trapping Ba2+ in the selectivity filter (the lock-in effect). Shown here is a structural view of Ba2+ binding in NaK2K K+ channel filter in the presence of K+. A Ba2+ ion (yellow sphere) resides at site 3 in conjunction with a K+ (green sphere) at site 1 (top), representing the locked-in configuration (see research article by Lam et al., 181–192).

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ISSN 0022-1295
EISSN 1540-7748
In this Issue

Generally Physiological

Research Articles

Two subclades of the CLCF-type F/H+ antiporters show differences in F/Cl selectivity.

Defective coupling between gating charge displacement and channel activation may contribute to reduced muscle excitability in hypokalemic periodic paralysis.

Comparison of the kinetics and voltage dependence of gating pore current conducted by S4 gating charge mutants supports the sliding-helix model of voltage sensor function and elucidates the pathogenic mechanisms underlying periodic paralysis syndromes.

Disease-associated mutation of charged amino acids in extracellular loop 1 of CFTR may reduce chloride flow by damaging the outer pore architecture.

The ion-binding profile in NaK2K is distinct from that in KcsA, even though the selectivity filter has been conserved.

Structural analyses identify a molecular basis for Ba2+ blockade of K+ channels.



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