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Generally Physiological


Chromaffin cells from mice lacking the BK β2 subunit show decreased action potential firing during current injection but an increase in spontaneous burst firing.

The pathway through which preferentially GqPCRs inhibit CaV2.2 channels depends on which β subunits are present.

The pathogenic G551D mutation of CFTR converts one of the two ATP-binding sites from excitatory to inhibitory.

The head and tail regions of 5-nitro-2-(3-phenylpropylamino)benzoate increase CFTR open probability through distinct mechanisms.

Residues forming interfaces between the three ENaC subunits participate in conformational changes required for transition between open and closed states.

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