| pubmed-article:20090852 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20090852 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:20090852 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:20090852 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:20090852 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:20090852 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:20090852 | pubmed:dateCreated | 2010-1-21 | lld:pubmed |
| pubmed-article:20090852 | pubmed:abstractText | Specific delivery to synapses of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptors with long-tailed subunits is believed to be a key event in many forms of activity-dependent changes in synaptic strength. GluA1, the best characterized long-tailed AMPA receptor subunit, contains a C-terminal class I PDZ binding motif, which mediates its interaction with scaffold and trafficking proteins, including synapse-associated protein 97 (SAP97). In GluA4, another long-tailed subunit implicated in synaptic plasticity, the PDZ motif is blocked by a single proline residue. This feature is highly conserved in vertebrates, whereas the closest invertebrate homologs of GluA4 have a canonical class I PDZ binding motif. In this work, we have examined the role of GluA4 in PDZ interactions. | lld:pubmed |
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| pubmed-article:20090852 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20090852 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20090852 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20090852 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20090852 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20090852 | pubmed:issn | 1932-6203 | lld:pubmed |
| pubmed-article:20090852 | pubmed:author | pubmed-author:KorpiEsa RER | lld:pubmed |
| pubmed-article:20090852 | pubmed:author | pubmed-author:KalkkinenNiss... | lld:pubmed |
| pubmed-article:20090852 | pubmed:author | pubmed-author:CaiChunlinC | lld:pubmed |
| pubmed-article:20090852 | pubmed:author | pubmed-author:ColemanSarah... | lld:pubmed |
| pubmed-article:20090852 | pubmed:author | pubmed-author:KeinänenKariK | lld:pubmed |
| pubmed-article:20090852 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20090852 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:20090852 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20090852 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20090852 | pubmed:pagination | e8715 | lld:pubmed |
| pubmed-article:20090852 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:meshHeading | pubmed-meshheading:20090852... | lld:pubmed |
| pubmed-article:20090852 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20090852 | pubmed:articleTitle | Analysis of the potential role of GluA4 carboxyl-terminus in PDZ interactions. | lld:pubmed |
| pubmed-article:20090852 | pubmed:affiliation | Department of Biosciences, Division of Biochemistry, Viikki Biocenter, University of Helsinki, Helsinki, Finland. | lld:pubmed |
| pubmed-article:20090852 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20090852 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
