Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10516269rdf:typepubmed:Citationlld:pubmed
pubmed-article:10516269lifeskim:mentionsumls-concept:C0022009lld:lifeskim
pubmed-article:10516269lifeskim:mentionsumls-concept:C0949771lld:lifeskim
pubmed-article:10516269lifeskim:mentionsumls-concept:C0243046lld:lifeskim
pubmed-article:10516269lifeskim:mentionsumls-concept:C0205245lld:lifeskim
pubmed-article:10516269lifeskim:mentionsumls-concept:C0552635lld:lifeskim
pubmed-article:10516269lifeskim:mentionsumls-concept:C1880371lld:lifeskim
pubmed-article:10516269pubmed:issue4 Pt 2lld:pubmed
pubmed-article:10516269pubmed:dateCreated1999-11-17lld:pubmed
pubmed-article:10516269pubmed:abstractTextRecent studies of glutamate transporters in the central nervous system indicate that in addition to their fundamental role in mediating neurotransmitter uptake, these proteins may contribute to the modulation of a variety of cellular processes. Activation of the excitatory amino acid (EAA) carriers generates an electrogenic current attibutable to ion-coupled cotransport. In addition to this transport-associated current, a substrate-gated thermodynamically uncoupled anion flux has been identified that has been proposed to dampen neuronal excitability. Arachidonic acid has been reported to modulate a variety of membrane proteins involved in cellular signaling. Here we discuss recent findings that indicate arachidonic acid stimulates a previously uncharacterized proton-selective conductance in the Purkinje cell-specific subtype, EAAT4. The unique channel-like porperties of the EAATs, their unexpected localization, and physiological evidence propose a modulatory role for the EAATs in neuronal signaling and suggest a broader role for glutamate transporters than simply the clearance of synaptically released glutamate. Thus, the identification of this arachidonate-stimulated proton conductance extends the complexity of mechanisms through which glutamate transporters modulate neuronal excitability.lld:pubmed
pubmed-article:10516269pubmed:languageenglld:pubmed
pubmed-article:10516269pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:citationSubsetIMlld:pubmed
pubmed-article:10516269pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10516269pubmed:statusMEDLINElld:pubmed
pubmed-article:10516269pubmed:monthOctlld:pubmed
pubmed-article:10516269pubmed:issn0002-9513lld:pubmed
pubmed-article:10516269pubmed:authorpubmed-author:AmaraS GSGlld:pubmed
pubmed-article:10516269pubmed:authorpubmed-author:FairmanW AWAlld:pubmed
pubmed-article:10516269pubmed:issnTypePrintlld:pubmed
pubmed-article:10516269pubmed:volume277lld:pubmed
pubmed-article:10516269pubmed:ownerNLMlld:pubmed
pubmed-article:10516269pubmed:authorsCompleteYlld:pubmed
pubmed-article:10516269pubmed:paginationF481-6lld:pubmed
pubmed-article:10516269pubmed:dateRevised2005-11-17lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:meshHeadingpubmed-meshheading:10516269...lld:pubmed
pubmed-article:10516269pubmed:year1999lld:pubmed
pubmed-article:10516269pubmed:articleTitleFunctional diversity of excitatory amino acid transporters: ion channel and transport modes.lld:pubmed
pubmed-article:10516269pubmed:affiliationHoward Hughes Medical Institute, Vollum Institute for Advanced Biomedical Research, Portland, Oregon 97201, USA.lld:pubmed
pubmed-article:10516269pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10516269pubmed:publicationTypeReviewlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10516269lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10516269lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10516269lld:pubmed