Source:http://linkedlifedata.com/resource/pubmed/id/17375039
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2007-3-21
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pubmed:abstractText |
Two-pore-domain K(+) (K(2P)) channel subunits are made up of four transmembrane segments and two pore-forming domains that are arranged in tandem and function as either homo- or heterodimeric channels. This structural motif is associated with unusual gating properties, including background channel activity and sensitivity to membrane stretch. Moreover, K(2P) channels are modulated by a variety of cellular lipids and pharmacological agents, including polyunsaturated fatty acids and volatile general anaesthetics. Recent in vivo studies have demonstrated that TREK1, the most thoroughly studied K(2P) channel, has a key role in the cellular mechanisms of neuroprotection, anaesthesia, pain and depression.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anesthetics,
http://linkedlifedata.com/resource/pubmed/chemical/Neuroprotective Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Tandem Pore...,
http://linkedlifedata.com/resource/pubmed/chemical/potassium channel protein TREK-1
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1471-003X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
251-61
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pubmed:meshHeading | |
pubmed:year |
2007
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pubmed:articleTitle |
The neuronal background K2P channels: focus on TREK1.
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pubmed:affiliation |
Institut de Pharmacologie Moléculaire et Cellulaire, CNRS UMR 6097, Université de Nice-Sophia Antipolis, 660 route des Lucioles, 06560 Valbonne, France. honore@ipmc.cnrs.fr
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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