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Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K+ ion channelK2P channel gating mechanisms revealed by structures of TREK-2 and a complex with ProzacGating of a pH-sensitive K(2P) potassium channel by an electrostatic effect of basic sensor residues on the selectivity filterSeparate gating mechanisms mediate the regulation of K2P potassium channel TASK-2 by intra- and extracellular pHGolgi anti-apoptotic proteins are highly conserved ion channels that affect apoptosis and cell migration.Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.Human trypanolytic factor APOL1 forms pH-gated cation-selective channels in planar lipid bilayers: relevance to trypanosome lysis.Multiple modalities converge on a common gate to control K2P channel function.External Ba2+ block of the two-pore domain potassium channel TREK-1 defines conformational transition in its selectivity filter.Acid-sensitive TWIK and TASK two-pore domain potassium channels change ion selectivity and become permeable to sodium in extracellular acidificationGating of two pore domain potassium channels.Molecular physiology of pH-sensitive background K(2P) channels.K(+) channels: function-structural overview.Hydrophobic gating in ion channelsTwo-pore domain potassium channels: potential therapeutic targets for the treatment of pain.The pore structure and gating mechanism of K2P channels.How ion channels sense mechanical force: insights from mechanosensitive K2P channels TRAAK, TREK1, and TREK2.Enhancement of TWIK-related acid-sensitive potassium channel 3 (TASK3) two-pore domain potassium channel activity by tumor necrosis factor α.Influence of lipids on the hydrophobic barrier within the pore of the TWIK-1 K2P channel.TASK-2: a K2P K(+) channel with complex regulation and diverse physiological functions.State-independent intracellular access of quaternary ammonium blockers to the pore of TREK-1An extracellular ion pathway plays a central role in the cooperative gating of a K(2P) K+ channel by extracellular pH.The Insensitivity of TASK-3 K₂P Channels to External Tetraethylammonium (TEA) Partially Depends on the Cap Structure
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 29 April 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Gating the pore of potassium leak channels.
@en
Gating the pore of potassium leak channels.
@nl
type
label
Gating the pore of potassium leak channels.
@en
Gating the pore of potassium leak channels.
@nl
prefLabel
Gating the pore of potassium leak channels.
@en
Gating the pore of potassium leak channels.
@nl
P2093
P2860
P1476
Gating the pore of potassium leak channels.
@en
P2093
Noam Zilberberg
Yuval Ben-Abu
P2860
P2888
P356
10.1007/S00249-009-0457-6
P577
2009-04-29T00:00:00Z