Results 81 to 90 of about 39,562,488 (191)

Electrophysiological characterization of the human two-pore channel 2

, 2015
The Two-pore channel (TPC1-3) family represents a recently identified class of endolysosomal ion channels. TPCs were originally proposed to be promising candidate channels for NAADP-induced Ca2+ release. However, subsequent studies have emerged to propose an alternative view where TPCs may be Na+-selective channels regulated by the lysosome-specific ...
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Structures of the human two-pore domain potassium channels TREK-1 and TREK-2 [PDF]

Acta Crystallographica Section A Foundations and Advances, 2014
TREK-1/2 are members of the mechano-gated subfamily of two-pore (K2P) domain potassium channels leaking K+ out of the cell and contributing to the resting membrane potential. In contrast to the classical tetrameric potassium channels, K2P channels are dimeric with an atypical architecture and the structural mechanisms underlying their channel gating ...
Ashley Pike, Yin Dong, Alexandra Mackenzie, Conor McClenaghan, Shubhashish Mukhopadhyay, Nicola Burgess-Brown, Stephen Tucker, Elisabeth Carpenter   +7 more
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Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense [PDF]

, 1993
Schürholz T, Dloczik L, Neumann E. Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense. Biophysical Journal.
Schürholz, Theo, Neumann, Eberhard, Dloczik, Larissa   +2 more
core   +1 more source

Assembly and lipid-gating of LRRC8A:D volume-regulated anion channels

Nature Communications
Volume-regulated anion channels (VRACs) are ubiquitously expressed vertebrate ion channels that open in response to hypotonic swelling. VRACs assemble as heteromers of LRRC8A and LRRC8B-E subunits, with different subunit combinations resulting in ...
Antony Lurie, Christina A. Stephens, David M. Kern, Katharine M. Henn, Naomi R. Latorraca, Stephen G. Brohawn   +5 more
doaj   +1 more source

The Role of TASK-3 Two-Pore Domain Potassium Channels in the Entrainment of Mammalian Circadian Rhythms [PDF]

, 2014
In mammals light is the principal timing cue for alignment of physiology to the external environment. Illumination from the unrelenting 24-hour day-night cycle enters the biological system and is communicated to the master pacemaker, the suprachiasmatic
Atkinson, Lynsey A
core  

Molecular pharmacology of an insect GABA receptor [PDF]

, 2010
Cys-loop receptors are ligand-gated ion channels that are involved in fast synaptic neurotransmission in the central and peripheral nervous system. The Cys-loop receptor RDL (‘resistant to dieldrin’) is a GABA-gated chloride channel from Drosophila ...

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An alternating GluN1-2-1-2 subunit arrangement in mature NMDA receptors. [PDF]

PLoS ONE, 2012
NMDA receptors (NMDARs) form glutamate-gated ion channels that play a critical role in CNS physiology and pathology. Together with AMPA and kainate receptors, NMDARs are known to operate as tetrameric complexes with four membrane-embedded subunits ...
Morgane Riou, David Stroebel, J Michael Edwardson, Pierre Paoletti   +3 more
doaj   +1 more source

The Hydrophobic Effect Contributes to the Closed State of a Simplified Ion Channel through a Conserved Hydrophobic Patch at the Pore-Helix Crossing.

Frontiers in Pharmacology, 2015
Ion selectivity-filter structures are strikingly similar throughout the large family of K+ channels and other p-loop-like receptors (i.e., glutamate receptors). At the same time, the triggers for opening these channels, or gating, are diverse.
Michael eYonkunas, Maria eKurnikova
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Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits [PDF]

, 2003
The subunits that compose eukaryotic glutamate ion channel receptors have three transmembrane domains (TMs) and terminate with intracellular tails that are important for controlling channel expression and localization.
Schorge, S., David Colquhoun, Colquhoun, D., Stephanie Schorge   +3 more
core   +1 more source

Ion occupancy of the selectivity filter controls opening of a cytoplasmic gate in the K2P channel TALK-2

Nature Communications
Two-pore domain K+ (K2P) channel activity was previously thought to be controlled primarily via a selectivity filter (SF) gate. However, recent crystal structures of TASK-1 and TASK-2 revealed a lower gate at the cytoplasmic pore entrance.
Lea C. Neelsen, Elena B. Riel, Susanne Rinné, Freya-Rebecca Schmid, Björn C. Jürs, Mauricio Bedoya, Jan P. Langer, Bisher Eymsh, Aytug K. Kiper, Sönke Cordeiro, Niels Decher, Thomas Baukrowitz, Marcus Schewe   +12 more
doaj   +1 more source