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pubmed-article:11060316 | lifeskim:mentions | umls-concept:C0949654 | lld:lifeskim |
pubmed-article:11060316 | lifeskim:mentions | umls-concept:C1416593 | lld:lifeskim |
pubmed-article:11060316 | lifeskim:mentions | umls-concept:C1416594 | lld:lifeskim |
pubmed-article:11060316 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:11060316 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:11060316 | lifeskim:mentions | umls-concept:C1711207 | lld:lifeskim |
pubmed-article:11060316 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:11060316 | pubmed:dateCreated | 2001-5-25 | lld:pubmed |
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pubmed-article:11060316 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11060316 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11060316 | pubmed:abstractText | Two cDNAs encoding novel K(+) channels, THIK-1 and THIK-2 (tandem pore domain halothane inhibited K(+) channel), were isolated from rat brain. The proteins of 405 and 430 amino acids were 58% identical to each other. Homology analysis showed that the novel channels form a separate subfamily among tandem pore domain K(+) channels. The genes of the human orthologs were identified as human genomic data base entries. They possess one intron each and were assigned to chromosomal region 14q24.1-14q24.3 (human (h) THIK-1) and 2p22-2p21 (hTHIK-2). In rat (r), THIK-1 (rTHIK-1) is expressed ubiquitously; rTHIK-2 expression was found in several tissues including brain and kidney. In situ hybridization of brain slices showed that rTHIK-2 is strongly expressed in most brain regions, whereas rTHIK-1 expression is more restricted. Heterologous expression of rTHIK-1 in Xenopus oocytes revealed a K(+) channel displaying weak inward rectification in symmetrical K(+) solution. The current was enhanced by arachidonic acid and inhibited by halothane. rTHIK-2 did not functionally express. Confocal microscopy of oocytes injected with green fluorescent protein-tagged rTHIK-1 or rTHIK-2 showed that both channel subunits are targeted to the outer membrane. However, coinjection of rTHIK-2 did not affect the currents induced by rTHIK-1, indicating that the two channel subunits do not form heteromers. | lld:pubmed |
pubmed-article:11060316 | pubmed:language | eng | lld:pubmed |
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pubmed-article:11060316 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:11060316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11060316 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11060316 | pubmed:month | Mar | lld:pubmed |
pubmed-article:11060316 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:11060316 | pubmed:author | pubmed-author:GrzeschikK... | lld:pubmed |
pubmed-article:11060316 | pubmed:author | pubmed-author:DautJJ | lld:pubmed |
pubmed-article:11060316 | pubmed:author | pubmed-author:DerstCC | lld:pubmed |
pubmed-article:11060316 | pubmed:author | pubmed-author:RajanSS | lld:pubmed |
pubmed-article:11060316 | pubmed:author | pubmed-author:KarschinAA | lld:pubmed |
pubmed-article:11060316 | pubmed:author | pubmed-author:Preisig-Mülle... | lld:pubmed |
pubmed-article:11060316 | pubmed:author | pubmed-author:WischmeyerEE | lld:pubmed |
pubmed-article:11060316 | pubmed:author | pubmed-author:KarschinCC | lld:pubmed |
pubmed-article:11060316 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11060316 | pubmed:day | 9 | lld:pubmed |
pubmed-article:11060316 | pubmed:volume | 276 | lld:pubmed |
pubmed-article:11060316 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11060316 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11060316 | pubmed:pagination | 7302-11 | lld:pubmed |
pubmed-article:11060316 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:11060316 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11060316 | pubmed:articleTitle | THIK-1 and THIK-2, a novel subfamily of tandem pore domain K+ channels. | lld:pubmed |
pubmed-article:11060316 | pubmed:affiliation | Institut für Normale und Pathologische Physiologie, Göttingen, Germany. | lld:pubmed |
pubmed-article:11060316 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11060316 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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