Results 101 to 110 of about 5,030 (211)

Allosteric modulation of the mouse kir6.2 channel by intracellular H+ and ATP

open access: yesThe Journal of Physiology, 2002
The ATP‐sensitive K+ (KATP) channels are regulated by intracellular H+ in addition to ATP, ADP, and phospholipids. Here we show evidence for the interaction of H+ with ATP in regulating a cloned KATP channel, i.e. Kir6.2 expressed with and without the SUR1 subunit.
Jianping, Wu   +6 more
openaire   +3 more sources

Direct photoaffinity labeling of Kir6.2 by [gamma-(32)P]ATP-[gamma]4-azidoanilide.

open access: yes, 2000
ATP-sensitive potassium (K(ATP)) channels are under complex regulation by intracellular ATP and ADP. The potentiatory effect of MgADP is conferred by the sulfonylurea receptor subunit of the channel, SUR, whereas the inhibitory effect of ATP appears to ...
Proks, P   +6 more
core   +1 more source

Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels

open access: yesProtein & Cell, 2018
ATP-sensitive potassium channels (KATP) are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of β-cells, pancreatic KATP channels control insulin release and regulate metabolism at the whole body level.
Jing-Xiang Wu   +5 more
doaj   +1 more source

Utrwalona cukrzyca noworodków - obserwacja trzyletnia [PDF]

open access: yesPediatric Endocrinology, Diabetes and Metabolism, 2010
Badanie dotyczy 3-letniego okresu obserwacji dzieci z utrwaloną cukrzycą noworodkową, spowodowaną mutacją aktywującą w genie KCJN11, kodującym wrażliwą na ATP podjednostkę Kir6.2 kanału potasowego (3 dzieci) oraz mutacją w genie ABCC8 kodującym ...
Anna Noczyńska   +4 more
doaj  

Anti-diabetic drug binding site in a mammalian KATP channel revealed by Cryo-EM

open access: yeseLife, 2017
Sulfonylureas are anti-diabetic medications that act by inhibiting pancreatic KATP channels composed of SUR1 and Kir6.2. The mechanism by which these drugs interact with and inhibit the channel has been extensively investigated, yet it remains unclear ...
Gregory M Martin   +4 more
doaj   +1 more source

Kir6.2-dependent high-affinity repaglinide binding to beta-cell K(ATP) channels.

open access: yes, 2005
1. The beta-cell K(ATP) channel is composed of two types of subunit - the inward rectifier K(+) channel (Kir6.2) which forms the channel pore, and the sulphonylurea receptor (SUR1), which serves as a regulatory subunit.
Ashcroft, FM   +5 more
core   +1 more source

Functional characterization of a novel KCNJ11 in frame mutation-deletion associated with infancy-onset diabetes and a mild form of intermediate DEND: a battle between K(ATP) gain of channel activity and loss of channel expression.

open access: yesPLoS ONE, 2013
ATP-sensitive potassium (K(ATP)) channels are widely distributed in various tissues and cell types where they couple cell metabolism to cell excitability.
Yu-Wen Lin   +7 more
doaj   +1 more source

Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.

open access: yes, 1999
The amino-terminal and carboxyl-terminal domains of inwardly rectifying potassium (Kir) channel subunits are both intracellular. There is increasing evidence that both of these domains are required for the regulation of Kir channels by agents such as G ...
Ashcroft, FM   +3 more
core   +1 more source

Expression of ATP-sensitive potassium channels in human pregnant myometrium

open access: yesReproductive Biology and Endocrinology, 2011
Background Potassium channels play critical roles in the regulation of cell membrane potential, which is central to the excitability of myometrium. The ATP-sensitive potassium (KATP) channel is one of the most abundant potassium channels in myometrium ...
Hui Ning   +7 more
doaj   +1 more source

Interaction of the cytosolic domains of the Kir6.2 subunit of the K(ATP) channel is modulated by sulfonylureas.

open access: yes, 2002
The NH(2)- and COOH-termini of the ATP-sensitive potassium (K(ATP)) channel pore-forming subunit, Kir6.2, both lie intracellularly and interact with one another.
Ashcroft, FM   +3 more
core   +1 more source

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