potassium channel, two pore domain subfamily K, member 18 L homeolog ; Xenopus laevis






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1 14981085 The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin. J Biol Chem 2004 Apr 30 12
2 16354767 Zinc and mercuric ions distinguish TRESK from the other two-pore-domain K+ channels. Mol Pharmacol 2006 Mar 1
3 16569637 Targeting of calcineurin to an NFAT-like docking site is required for the calcium-dependent activation of the background K+ channel, TRESK. J Biol Chem 2006 May 26 3
4 17717222 Anesthetic properties of the ketone bodies beta-hydroxybutyric acid and acetone. Anesth Analg 2007 Sep 1
5 20006580 N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK. Biochem Biophys Res Commun 2010 Jan 8 2
6 20215114 TRESK background K(+) channel is inhibited by phosphorylation via two distinct pathways. J Biol Chem 2010 May 7 6
7 22145024 TRESK background K(+) channel is inhibited by PAR-1/MARK microtubule affinity-regulating kinases in Xenopus oocytes. PLoS One 2011 2
8 26224542 Activation of TRESK channels by the inflammatory mediator lysophosphatidic acid balances nociceptive signalling. Sci Rep 2015 Jul 30 1
9 30992311 TRESK (K2P18.1) Background Potassium Channel Is Activated by Novel-Type Protein Kinase C via Dephosphorylation. Mol Pharmacol 2019 Jun 3