A specific two-pore domain potassium channel blocker defines the structure of the TASK-1 open pore.
about
The genetics of pulmonary arterial hypertensionPancreatic β-cell-specific ablation of TASK-1 channels augments glucose-stimulated calcium entry and insulin secretion, improving glucose tolerance.Potent and selective inhibitors of the TASK-1 potassium channel through chemical optimization of a bis-amide scaffold.Heritable forms of pulmonary arterial hypertension.Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.TASK-1 Potassium Channels Limit Pancreatic α-Cell Calcium Influx and Glucagon Secretion.An N-terminal deletion variant of HCN1 in the epileptic WAG/Rij strain modulates HCN current densities.Breathing Stimulant Compounds Inhibit TASK-3 Potassium Channel Function Likely by Binding at a Common Site in the Channel Pore.TASK-1 channels may modulate action potential duration of human atrial cardiomyocytesA novel channelopathy in pulmonary arterial hypertension.TASK-1 (KCNK3) and TASK-3 (KCNK9) tandem pore potassium channel antagonists stimulate breathing in isoflurane-anesthetized rats.Reorientation of the first signal-anchor sequence during potassium channel biogenesis at the Sec61 complex.A Role for K2P Channels in the Operation of Somatosensory NociceptorsCardiac potassium channel subtypes: new roles in repolarization and arrhythmia.The role of acid-sensitive two-pore domain potassium channels in cardiac electrophysiology: focus on arrhythmias.Much more than a leak: structure and function of K₂p-channels.The pore structure and gating mechanism of K2P channels.Low pHo boosts burst firing and catecholamine release by blocking TASK-1 and BK channels while preserving Cav1 channels in mouse chromaffin cells.Functional characterization of zebrafish K2P18.1 (TRESK) two-pore-domain K+ channels.Heterodimerization of two pore domain K+ channel TASK1 and TALK2 in living heterologous expression systems.Parallel Evolution and Lineage-Specific Expansion of RNA Editing in Ctenophores.Kv1.5 blockers preferentially inhibit TASK-1 channels: TASK-1 as a target against atrial fibrillation and obstructive sleep apnea?Acetylcholine-dependent upregulation of TASK-1 channels in thalamic interneurons by a smooth muscle-like signalling pathway.Discovery of a pharmacologically active antagonist of the two-pore-domain potassium channel K2P9.1 (TASK-3).Novel electrophysiological properties of dronedarone: inhibition of human cardiac two-pore-domain potassium (K2P) channels.The inhibition of the potassium channel TASK-1 in rat cardiac muscle by endothelin-1 is mediated by phospholipase C.
P2860
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P2860
A specific two-pore domain potassium channel blocker defines the structure of the TASK-1 open pore.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh
2011年學術文章
@zh-hant
name
A specific two-pore domain pot ...... cture of the TASK-1 open pore.
@en
A specific two-pore domain pot ...... cture of the TASK-1 open pore.
@nl
type
label
A specific two-pore domain pot ...... cture of the TASK-1 open pore.
@en
A specific two-pore domain pot ...... cture of the TASK-1 open pore.
@nl
prefLabel
A specific two-pore domain pot ...... cture of the TASK-1 open pore.
@en
A specific two-pore domain pot ...... cture of the TASK-1 open pore.
@nl
P2093
P2860
P356
P1476
A specific two-pore domain pot ...... cture of the TASK-1 open pore.
@en
P2093
Anne K Streit
Franca Kempf
Jürgen Daut
Magdalena Walecki
Mark S P Sansom
Michael F Netter
Murali K Bollepalli
Niels Decher
Phillip J Stansfeld
Regina Preisig-Müller
P2860
P304
13977-13984
P356
10.1074/JBC.M111.227884
P407
P577
2011-03-01T00:00:00Z