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http://purl.uniprot.org/citations/11060316http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11060316http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11060316http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m008985200"xsd:string
http://purl.uniprot.org/citations/11060316http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m008985200"xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Derst C."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Derst C."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Grzeschik K.-H."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Grzeschik K.-H."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Rajan S."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Rajan S."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Preisig-Mueller R."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Preisig-Mueller R."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Karschin A."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Karschin A."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Wischmeyer E."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Wischmeyer E."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Daut J."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Daut J."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Karschin C."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/author"Karschin C."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11060316http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string