Linked Life Data

15184378

Source:http://linkedlifedata.com/resource/pubmed/id/15184378

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:15184378rdf:typepubmed:Citationlld:pubmed
pubmed-article:15184378lifeskim:mentionsumls-concept:C0000768lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C0018787lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C2339371lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C0257694lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C1416596lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C1514562lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C1883221lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C0205263lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C0439799lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C1883204lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C1879547lld:lifeskim
pubmed-article:15184378lifeskim:mentionsumls-concept:C1880389lld:lifeskim
pubmed-article:15184378pubmed:issue32lld:pubmed
pubmed-article:15184378pubmed:dateCreated2004-8-2lld:pubmed
pubmed-article:15184378pubmed:abstractTextActivation of the platelet-activating factor (PAF) receptor leads to a decrease in outward current in murine ventricular myocytes by inhibiting the TASK-1 channel. TASK-1 carries a background or "leak" current and is a member of the two-pore domain potassium channel family. Its inhibition is sufficient to delay repolarization, causing prolongation of the action potential duration, and in some cases, early after depolarizations. We set out to determine the cellular mechanisms that control regulation of TASK-1 by PAF. Inhibition of TASK-1 via activation of the PAF receptor is protein kinase C (PKC)-dependent. Using isoform-specific PKC inhibitor or activator peptides in patch clamp experiments, we now demonstrate that activation of PKCepsilon is both necessary and sufficient to regulate murine TASK-1 current in a heterologous expression system and to induce repolarization abnormalities in isolated myocytes. Furthermore, site-directed mutagenesis studies have identified threonine 381, in the C-terminal tail of murine TASK-1, as a critical residue in this regulation.lld:pubmed
pubmed-article:15184378pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:languageenglld:pubmed
pubmed-article:15184378pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:citationSubsetIMlld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15184378pubmed:statusMEDLINElld:pubmed
pubmed-article:15184378pubmed:monthAuglld:pubmed
pubmed-article:15184378pubmed:issn0021-9258lld:pubmed
pubmed-article:15184378pubmed:authorpubmed-author:RobinsonRicha...lld:pubmed
pubmed-article:15184378pubmed:authorpubmed-author:BarbutiAndrea...lld:pubmed
pubmed-article:15184378pubmed:authorpubmed-author:FeinmarkSteve...lld:pubmed
pubmed-article:15184378pubmed:authorpubmed-author:SymesAviva...lld:pubmed
pubmed-article:15184378pubmed:authorpubmed-author:BesanaAlessan...lld:pubmed
pubmed-article:15184378pubmed:authorpubmed-author:TateyamaMiyuk...lld:pubmed
pubmed-article:15184378pubmed:issnTypePrintlld:pubmed
pubmed-article:15184378pubmed:day6lld:pubmed
pubmed-article:15184378pubmed:volume279lld:pubmed
pubmed-article:15184378pubmed:ownerNLMlld:pubmed
pubmed-article:15184378pubmed:authorsCompleteYlld:pubmed
pubmed-article:15184378pubmed:pagination33154-60lld:pubmed
pubmed-article:15184378pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:meshHeadingpubmed-meshheading:15184378...lld:pubmed
pubmed-article:15184378pubmed:year2004lld:pubmed
pubmed-article:15184378pubmed:articleTitleActivation of protein kinase C epsilon inhibits the two-pore domain K+ channel, TASK-1, inducing repolarization abnormalities in cardiac ventricular myocytes.lld:pubmed
pubmed-article:15184378pubmed:affiliationCenter for Molecular Therapeutics, Department of Pharmacology, Columbia University, New York, New York 10032, USA.lld:pubmed
pubmed-article:15184378pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15184378pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:15184378pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:16527entrezgene:pubmedpubmed-article:15184378lld:entrezgene
entrez-gene:18754entrezgene:pubmedpubmed-article:15184378lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:15184378lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:15184378lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15184378lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15184378lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15184378lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15184378lld:pubmed