Results 21 to 30 of about 19,368 (234)
CO2-dependent opening of an inwardly rectifying K+ channel [PDF]
, 2011 CO2 chemosensing is a vital function for the maintenance of life that helps to control acid–base balance. Most studies have reported that CO2 is measured via its proxy, pH. Here we report an inwardly rectifying channel, in outside-out excised patches
Dale, Nicholas, Huckstepp, Robert T. R.
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Frontiers in Physiology, 2014 Alcohol (ethanol)-induced behaviors arise from direct interaction of alcohol with discrete protein cavities within brain proteins. Recent structural and biochemical studies have provided new insights into the mechanism of alcohol-dependent activation of ...
Karthik eBodhinathan, Paul A Slesinger
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Why do platelets express K+ channels?
Platelets, 2021 Potassium ions have widespread roles in cellular homeostasis and activation as a consequence of their large outward concentration gradient across the surface membrane and ability to rapidly move through K+-selective ion channels.
Joy R Wright, Martyn P. Mahaut-Smith
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Transmembrane Structure of an Inwardly Rectifying Potassium Channel [PDF]
Cell, 1999 Inwardly rectifying potassium channels (K(ir)), comprising four subunits each with two transmembrane domains, M1 and M2, regulate many important physiological processes. We employed a yeast genetic screen to identify functional channels from libraries of K(ir) 2.1 containing mutagenized M1 or M2 domains.
Minor, Daniel L +3 more
openaire +2 more sources
Nature Communications, 2019 Opening of G protein-gated inwardly rectifying potassium channels (GIRK) is coupled to the activation of a GPCR. Here the authors use NMR and cell-based BRET assays to gain insights into the mechanisms underlying family-specific activation and find that ...
Hanaho Kano +7 more
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Gain of function mutants: Ion channels and G protein-coupled receptors [PDF]
, 2000 Many ion channels and receptors display striking phenotypes for gain-of-function mutations but milder phenotypes for null mutations. Gain of molecular function can have several mechanistic bases: selectivity changes, gating changes including constitutive
Karschin, Andreas, Lester, Henry A.
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The role of inhibitory G proteins and regulators of G protein signaling in the in vivo control of heart rate and predisposition to cardiac arrhythmias [PDF]
, 2012 Inhibitory heterotrimeric G proteins and the control of heart rate. The activation of cell signaling pathways involving inhibitory heterotrimeric G proteins acts to slow the heart rate via modulation of ion channels.
Ang, R, Opel, A, Tinker, A
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Frontiers in Genetics, 2019 Inwardly rectifying K+ channel 4.1 (Kir4.1), encoded by KCNJ10, is a member of the inwardly rectifying potassium channel family. In the brain, Kir4.1 is predominant in astrocytic glia and accounts for the spatial buffering of K+ released by neurons ...
Hongfeng Zhang +14 more
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Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids [PDF]
, 2016 Inward rectifier potassium (Kir) channel activity is controlled by plasma membrane lipids. Phosphatidylinositol-4,5-bisphosphate (PIP(2)) binding to a primary site is required for opening of classic inward rectifier Kir2.1 and Kir2.2 channels, but ...
Anna Stary-Weinzinger +55 more
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Expression of an atrial G-protein-activated potassium channel in Xenopus oocytes [PDF]
, 1993 Injection of rat atrial RNA into Xenopus oocytes resulted in the expression of a guanine nucleotide binding (G) protein-activated K+ channel. Current through the channel could be activated by acetylcholine or, if RNA encoding a neuronal 5HT1A receptor ...
Dascal, Nathan +5 more
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