• Publications
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TASK-3, a New Member of the Tandem Pore K+ Channel Family*
  • Yangmi Kim, H. Bang, Donghee Kim
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 31 March 2000
TLDR
Reverse transcriptase-polymerase chain reaction analysis showed that TASK-3 mRNA is expressed in many rat tissues including brain, kidney, liver, lung, colon, stomach, spleen, testis, and skeletal muscle, and at very low levels in the heart and small intestine. Expand
TREK-2, a New Member of the Mechanosensitive Tandem-pore K+ Channel Family*
  • H. Bang, Yangmi Kim, Donghee Kim
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 9 June 2000
TLDR
Results show that TREK-2 is a new member of the tandem-pore K+ channel family and belongs to the class of mechanosensitive and fatty acid-stimulated K+ channels. Expand
Synergistic interaction and the role of C-terminus in the activation of TRAAK K+ channels by pressure, free fatty acids and alkali
TLDR
Rat TRAAK is an alkali-sensing K+ channel that shows synergistic activation with pressure, and that the mechanism of activation of rTRAAK and TREK by free fatty acids are different. Expand
Localization of TREK-2 K+ channel domains that regulate channel kinetics and sensitivity to pressure, fatty acids and pHi
TLDR
The C-terminus endows TREK-2 with unique channel kinetics and the ability to be gated by free fatty acids and low pHi, and with increased mechanosensitivity. Expand
Zinc Activates TREK-2 Potassium Channel Activity
TLDR
Stimulation by Zn2+ may be used as a criterion of TREK-2, distinguishing it from other two-pore K+ channels. Expand
TBAK-1 and TASK-1, two-pore K(+) channel subunits: kinetic properties and expression in rat heart.
TLDR
Results indicate that TBAK- 1/TASK-1 represents a functional native K(+) channel in the rat heart and a 14-pS K(+) channel with kinetic properties similar to those of TBAk-1/T ask1 was identified in rat atrial and ventricular cells. Expand
TBAK-1 and TASK-1, two-pore K+ channel subunits: kinetic properties and expression in rat heart.
TLDR
Results indicate that TBAK-1/TASk-1 represents a functional native K+ channel in the rat heart and a 14-pS K+channel with kinetic properties similar to those of TBAK/TasK- 1 was identified in rat atrial and ventricular cells. Expand
Modulation of rat atrial G protein‐coupled K+ channel function by phospholipids
  • D. Kim, H. Bang
  • Chemistry, Medicine
  • The Journal of physiology
  • 1 May 1999
TLDR
It is concluded that exogenously applied PIP2 and other phospholipids block agonist‐mediated KACh channel activation, and a shift in the gating mode of the channel from a short‐lived to a longer‐lived open state was the result of a modulatory effect qualitatively similar to that produced by intracellular ATP. Expand
The Inhibition of TREK 2 Channel by an Oxidizing Agent , 5 , 5 '-dithio-bis ( 2-nitrobenzoic acid ) , via Interaction with the C-terminus Distal to the 353 rd Amino Acid
211 ABBREVIATIONS: TREK, TWIK-related K channel; TRAAK, TWIK-related arachidonic acid activated K channel; TASK, TWIKrelated acid sensitive K channel; 5,5'-dithio-bis (2-nitrobenzoic acid), DTNB;Expand
The Inhibition of TREK2 Channel by an Oxidizing Agent, 5,5'-dithio-bis (2-nitrobenzoic acid), via Interaction with the C-terminus Distal to the 353rd Amino Acid.
TLDR
Results indicate that TREK 2 is inhibited by oxidation, and that the target site for oxidation is located between the amino acid residues 353 and 383 in the C-terminus of the TREK2 protein. Expand
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