| pubmed-article:19348678 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19348678 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
| pubmed-article:19348678 | lifeskim:mentions | umls-concept:C0061605 | lld:lifeskim |
| pubmed-article:19348678 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:19348678 | lifeskim:mentions | umls-concept:C1538051 | lld:lifeskim |
| pubmed-article:19348678 | pubmed:dateCreated | 2009-4-16 | lld:pubmed |
| pubmed-article:19348678 | pubmed:abstractText | N-methyl-D-aspartate receptors (NMDARs) are the most complex of ionotropic glutamate receptors (iGluRs). Subunits of this subfamily assemble into heteromers, which - depending on the subunit combination - may display very different pharmacological and electrophysiological properties. The least studied members of the NMDAR family, the NR3 subunits, have been reported to assemble with NR1 to form excitatory glycine receptors in heterologous expression systems. The heterogeneity of NMDARs in vivo is in part conferred to the receptors by splicing of the NR1 subunit, especially with regard to proton sensitivity. | lld:pubmed |
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| pubmed-article:19348678 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19348678 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19348678 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19348678 | pubmed:issn | 1471-2202 | lld:pubmed |
| pubmed-article:19348678 | pubmed:author | pubmed-author:HollmannMicha... | lld:pubmed |
| pubmed-article:19348678 | pubmed:author | pubmed-author:CavaraNora... | lld:pubmed |
| pubmed-article:19348678 | pubmed:author | pubmed-author:OrthAngelaA | lld:pubmed |
| pubmed-article:19348678 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19348678 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:19348678 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19348678 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19348678 | pubmed:pagination | 32 | lld:pubmed |
| pubmed-article:19348678 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:19348678 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19348678 | pubmed:articleTitle | Effects of NR1 splicing on NR1/NR3B-type excitatory glycine receptors. | lld:pubmed |
| pubmed-article:19348678 | pubmed:affiliation | Department of Biochemistry I - Receptor Biochemistry, Ruhr University Bochum, Universitätsstr, 150, D-44780 Bochum, Germany. Nora.Cavara@rub.de | lld:pubmed |
| pubmed-article:19348678 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19348678 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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