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TRESK-like potassium channels in leukemic T cells
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TRESK two-pore-domain K+ channels constitute a significant component of background potassium currents in murine dorsal root ganglion neurones
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Species-specific differences in response to anesthetics and other modulators by the K2P channel TRESK
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The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin
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Functional expression of TRESK-2, a new member of the tandem-pore K+ channel family
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Potent activation of the human tandem pore domain K channel TRESK with clinical concentrations of volatile anesthetics
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Structural delineation of the calcineurin-NFAT interaction and its parallels to PP1 targeting interactions
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Formation of functional heterodimers between the TASK-1 and TASK-3 two-pore domain potassium channel subunits
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