Trimethylamine N-oxide (TMAO) acutely alters ionic currents but does not increase cardiac cell death. [PDF]
Front PhysiolEsposito S +4 more
europepmc +1 more source
Differentiation of patient-specific induced pluripotent stem cells derived from type 1 diabetes peripheral blood mononuclear cells into pancreatic β-like cells. [PDF]
World J Stem CellsWang K +6 more
europepmc +1 more source
Dynamic duo: Kir6 and SUR in KATP channel structure and function. [PDF]
Channels (Austin)Patton BL +4 more
europepmc +1 more source
multiSMD - A Python Toolset for Multidirectional Steered Molecular Dynamics. [PDF]
J Chem Inf ModelWalczewska-Szewc K +3 more
europepmc +1 more source
Lipid probes to study ion channels. [PDF]
Curr Opin Chem BiolJahn H, Shyng SL, Schultz C.
europepmc +1 more source
Mapping the architecture of the ATP-binding site of Kir6.2
, 2016 Dabrowski, M, Ashcroft, F
openaire +1 more source
The N-terminus of Kir6.2 is involved in coupling to SUR1
, 2016 Reimann, F +3 more
openaire +1 more source
Effects of mitiglinide (S 21403) on Kir6.2/SUR1, Kir6.2/SUR2A and Kir6.2/SUR2B types of ATP-sensitive potassium channel [PDF]
British Journal of Pharmacology, 2001 We have investigated the mechanism of action of the novel anti‐diabetic agent mitiglinide (S 21403) on Kir6.2/SUR1, Kir6.2/SUR2A and Kir6.2/SUR2B types of ATP‐sensitive potassium (KATP) channel. These possess a common pore‐forming subunit, Kir6.2, and different regulatory sulphonylurea receptor (SUR) subunits.
Frank Reimann +2 more
exaly +4 more sources
Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2–SUR1 interactions [PDF]
EMBO Journal, 2005 ATP-sensitive K(+) (K(ATP)) channels, comprised of pore-forming Kir6.2 and regulatory SUR1 subunits, play a critical role in regulating insulin secretion. Binding of ATP to Kir6.2 inhibits, whereas interaction of MgATP with SUR1 activates, K(ATP) channels.
Paolo Tammaro +2 more
exaly +6 more sources