| pubmed-article:1656338 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1656338 | lifeskim:mentions | umls-concept:C0043342 | lld:lifeskim |
| pubmed-article:1656338 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:1656338 | lifeskim:mentions | umls-concept:C1517880 | lld:lifeskim |
| pubmed-article:1656338 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:1656338 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:1656338 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1656338 | pubmed:dateCreated | 1991-11-5 | lld:pubmed |
| pubmed-article:1656338 | pubmed:abstractText | In the Xenopus central nervous system the binding sites for [3H]kainate and [3H]alpha-amino-3-hydroxy-5-methylisoxazolepropionate [( 3H]AMPA) are highly localised and the distributions of both ligands are largely coincident. The telencephalon was the most strongly labelled area with a relatively uniform distribution of binding sites. In addition, the infundibulum and the cerebellum were also heavily labelled. Areas containing a lower density of binding sites included the septum, the thalamus and the optic lobes. [3H]Kainate binding was potently inhibited by 1 microM AMPA in the presence of 0.1 M KSCN and [3H]AMPA binding was blocked by 1 microM kainate. These data are consistent with the hypothesis that kainate and AMPA bind to the same site on a single protein entity and that this unitary AMPA/KA binding protein may constitute the predominant type of excitatory amino acid receptor in the Xenopus brain. | lld:pubmed |
| pubmed-article:1656338 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1656338 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1656338 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1656338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1656338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1656338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1656338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1656338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1656338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1656338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1656338 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1656338 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1656338 | pubmed:issn | 0304-3940 | lld:pubmed |
| pubmed-article:1656338 | pubmed:author | pubmed-author:BarnardE AEA | lld:pubmed |
| pubmed-article:1656338 | pubmed:author | pubmed-author:BonoLL | lld:pubmed |
| pubmed-article:1656338 | pubmed:author | pubmed-author:HenleyJ MJM | lld:pubmed |
| pubmed-article:1656338 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1656338 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1656338 | pubmed:volume | 129 | lld:pubmed |
| pubmed-article:1656338 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1656338 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1656338 | pubmed:pagination | 35-8 | lld:pubmed |
| pubmed-article:1656338 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:meshHeading | pubmed-meshheading:1656338-... | lld:pubmed |
| pubmed-article:1656338 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1656338 | pubmed:articleTitle | Autoradiographic localisations of glutamatergic ligand binding sites in Xenopus brain. | lld:pubmed |
| pubmed-article:1656338 | pubmed:affiliation | Department of Pharmacology, Medical School, University of Birmingham, U.K. | lld:pubmed |
| pubmed-article:1656338 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1656338 | lld:pubmed |
