Talley, E M <br/><br/>
TASK-1, a two-pore domain K+ channel, is modulated by multiple neurotransmitters in motoneurons.  [electronic resource] 

 -  Neuron  Feb 2000 
 - 399-410 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0896-6273 
<br/><br/><label>Standard No.: </label>10.1016/s0896-6273(00)80903-4  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acids--pharmacology<br/>Animals<br/>Animals, Newborn<br/>Cell Line<br/>Electric Conductivity<br/>Gene Expression--physiology<br/>Glutamic Acid--metabolism<br/>Humans<br/>Hydrogen-Ion Concentration<br/>Hypoglossal Nerve--cytology<br/>Kidney--cytology<br/>Membrane Potentials--drug effects<br/>Motor Neurons--chemistry<br/>Nerve Tissue Proteins<br/>Neurotransmitter Agents--metabolism<br/>Norepinephrine--metabolism<br/>Patch-Clamp Techniques<br/>Potassium--metabolism<br/>Potassium Channels--chemistry<br/>Potassium Channels, Tandem Pore Domain<br/>Protein Structure, Tertiary<br/>RNA, Messenger--analysis<br/>Rats<br/>Rats, Sprague-Dawley<br/>Serotonin--metabolism<br/>Substance P--metabolism<br/>Thyrotropin-Releasing Hormone--metabolism<br/>Transfection