Stephen J. Tucker

TL;DR: It is shown that the primary site at which ATP acts to mediate K-ATP channel inhibition is located on Kir6.2, and that SUR1 is required for sensitivity to sulphonylureas and diazoxide and for activation by Mg-ADP.

TL;DR: It is reported here that phosphatidylinositol-4, 5-bisphosphate (PIP2) and phosphorus-4-phosphates(PIP) controlled ATP inhibition of cloned KATP channels (Kir6.2 and SUR1) and represents a mechanism for control of excitability through phospholipids.

TL;DR: The results indicate that the WA lysine of NBD1 (but not NBD2) is essential for activation of K‐ATP currents by diazoxide, and Mutant currents were slightly more sensitive to ATP than wild‐type currents.

TL;DR: A frameshift mutation, F139WfsX24, is reported, which segregates perfectly with typical migraine with aura in a large pedigree and demonstrates that it causes a complete loss of TRESK function and that the mutant subunit suppresses wild-type channel function through a dominant-negative effect, thus explaining the dominant penetrance of this allele.

TL;DR: In this article, a frameshift mutation, F139WfsX24, was found to cause complete loss of TRESK function and that the mutant subunit suppresses wild-type channel function through a dominant negative effect, thus explaining the dominant penetrance of this allele.