| pubmed-article:12417307 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12417307 | lifeskim:mentions | umls-concept:C0243192 | lld:lifeskim |
| pubmed-article:12417307 | lifeskim:mentions | umls-concept:C1415288 | lld:lifeskim |
| pubmed-article:12417307 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:12417307 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:12417307 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:12417307 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
| pubmed-article:12417307 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12417307 | pubmed:dateCreated | 2002-11-5 | lld:pubmed |
| pubmed-article:12417307 | pubmed:abstractText | X-ray structures of the GluR2 ligand-binding core in complex with (S)-Des-Me-AMPA and in the presence and absence of zinc ions have been determined. (S)-Des-Me-AMPA, which is devoid of a substituent in the 5-position of the isoxazolol ring, only has limited interactions with the partly hydrophobic pocket of the ligand-binding site, and adopts an AMPA-like binding mode. The structures, in comparison with other agonist complex structures, disclose the relative importance of the isoxazolol ring and of the substituent in the 5-position for the mode of binding. A relationship appears to exist between the extent of interaction of the ligand with the hydrophobic pocket and the affinity of the ligand. | lld:pubmed |
| pubmed-article:12417307 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12417307 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12417307 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12417307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12417307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12417307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12417307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12417307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12417307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12417307 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12417307 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:12417307 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:12417307 | pubmed:author | pubmed-author:EgebjergJJ | lld:pubmed |
| pubmed-article:12417307 | pubmed:author | pubmed-author:LiljeforsTT | lld:pubmed |
| pubmed-article:12417307 | pubmed:author | pubmed-author:KasperCC | lld:pubmed |
| pubmed-article:12417307 | pubmed:author | pubmed-author:KastrupJ SJS | lld:pubmed |
| pubmed-article:12417307 | pubmed:author | pubmed-author:GouauxEE | lld:pubmed |
| pubmed-article:12417307 | pubmed:author | pubmed-author:MadyG EGE | lld:pubmed |
| pubmed-article:12417307 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12417307 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:12417307 | pubmed:volume | 531 | lld:pubmed |
| pubmed-article:12417307 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12417307 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12417307 | pubmed:pagination | 173-8 | lld:pubmed |
| pubmed-article:12417307 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:12417307 | pubmed:meshHeading | pubmed-meshheading:12417307... | lld:pubmed |
| pubmed-article:12417307 | pubmed:meshHeading | pubmed-meshheading:12417307... | lld:pubmed |
| pubmed-article:12417307 | pubmed:meshHeading | pubmed-meshheading:12417307... | lld:pubmed |
| pubmed-article:12417307 | pubmed:meshHeading | pubmed-meshheading:12417307... | lld:pubmed |
| pubmed-article:12417307 | pubmed:meshHeading | pubmed-meshheading:12417307... | lld:pubmed |
| pubmed-article:12417307 | pubmed:meshHeading | pubmed-meshheading:12417307... | lld:pubmed |
| pubmed-article:12417307 | pubmed:meshHeading | pubmed-meshheading:12417307... | lld:pubmed |
| pubmed-article:12417307 | pubmed:meshHeading | pubmed-meshheading:12417307... | lld:pubmed |
| pubmed-article:12417307 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12417307 | pubmed:articleTitle | GluR2 ligand-binding core complexes: importance of the isoxazolol moiety and 5-substituent for the binding mode of AMPA-type agonists. | lld:pubmed |
| pubmed-article:12417307 | pubmed:affiliation | Department of Medicinal Chemistry, Royal Danish School of Pharmacy, Universitetsparken 2, Copenhagen, Denmark. | lld:pubmed |
| pubmed-article:12417307 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12417307 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12417307 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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