Results 21 to 30 of about 19,097 (250)

Structural insights into GIRK2 channel modulation by cholesterol and PIP2

open access: yesCell Reports, 2021
Summary: G-protein-gated inwardly rectifying potassium (GIRK) channels are important for determining neuronal excitability. In addition to G proteins, GIRK channels are potentiated by membrane cholesterol, which is elevated in the brains of people with ...
Yamuna Kalyani Mathiharan   +5 more
doaj   +1 more source

A new familial form of a late-onset, persistent hyperinsulinemic hypoglycemia of infancy caused by a novel mutation in KCNJ11. [PDF]

open access: yes, 2017
The ATP-sensitive potassium channel (KATP) functions as a metabo-electric transducer in regulating insulin secretion from pancreatic β-cells. The pancreatic KATP channel is composed of a pore-forming inwardly-rectifying potassium channel, Kir6.2, and a ...
Ferrara, Christine   +5 more
core   +1 more source

Alcohol modulation of G-protein-gated inwardly rectifying potassium channels: from binding to therapeutics

open access: yesFrontiers 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
doaj   +1 more source

Why do platelets express K+ channels?

open access: yesPlatelets, 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
doaj   +1 more source

Structural mechanism underlying G protein family-specific regulation of G protein-gated inwardly rectifying potassium channel

open access: yesNature 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
doaj   +1 more source

Reciprocal modulation of IK1-INa extends excitability in cardiac ventricular cells

open access: yesFrontiers in Physiology, 2016
The inwardly rectifying potassium current (IK1) and the fast inward sodium current (INa) are reciprocally modulated in mammalian ventricular myocytes.
Anthony Varghese
doaj   +1 more source

Gain of function mutants: Ion channels and G protein-coupled receptors [PDF]

open access: yes, 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.
core   +1 more source

Novel KCNJ10 Compound Heterozygous Mutations Causing EAST/SeSAME-Like Syndrome Compromise Potassium Channel Function

open access: yesFrontiers 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
doaj   +1 more source

The Possible Role of TASK Channels in Rank-Ordered Recruitment of Motoneurons in the Dorsolateral Part of the Trigeminal Motor Nucleus. [PDF]

open access: yes, 2016
Because a rank-ordered recruitment of motor units occurs during isometric contraction of jaw-closing muscles, jaw-closing motoneurons (MNs) may be recruited in a manner dependent on their soma sizes or input resistances (IRs). In the dorsolateral part of
Emura, Norihito   +18 more
core   +2 more sources

Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids [PDF]

open access: yes, 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
core   +2 more sources

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