Jean-Charles Hoda

TL;DR: Small differences in their binding pockets may allow development of isoform-selective modulators for LTCCs and that, because of their very low expression, Cav.1.1 and Cav1.4 are unlikely to serve as drug targets to treat CNS diseases.

TL;DR: A novel mechanism of channel modulation enabling cells to tightly control CaV1.3 activity at threshold voltages as required for modulation of neuronal firing behavior and sinoatrial node pacemaking is revealed.

TL;DR: It is shown that removal of the last 55 or 122 C-terminal amino acid residues of the human α1 subunit restores calmodulin-dependent CDI and shifts voltage of half-maximal activation to more negative potentials, which underlines its importance for normal retinal function in humans.

TL;DR: The biophysical and pharmacological properties of human retinal Cav1.4α1 + α2δ1 + β channel complexes can form LTCCs with intermediate DHP antagonist sensitivity lacking Ca2+-dependent inactivation, and their biophysical properties should enable them to contribute to sustained ICa,L at negative potentials.

TL;DR: In this article, the Ca2+ channel current in OHCs was found to be 1.8 times larger with 10 mM Ba2+ as charge carrier (IBa) than with equimolar Ca2+, while ICa was inactivated by 50.7 %.