| pubmed-article:10734231 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10734231 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10734231 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:10734231 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:10734231 | lifeskim:mentions | umls-concept:C0597358 | lld:lifeskim |
| pubmed-article:10734231 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:10734231 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10734231 | pubmed:dateCreated | 2000-4-24 | lld:pubmed |
| pubmed-article:10734231 | pubmed:abstractText | To delineate the role of the cytoplasmic tail in the distinct binding and coupling properties of human dopamine D1-like receptors, chimeric receptors were generated in which the entire tail region of wild-type human D1A (or D1) and D1B (or D5) receptors was exchanged. The hD1A-D1BT, but not hD1B-D1AT, receptor expression was dramatically reduced compared with wild-type receptor expression. Swapping the cytoplasmic tail resulted in a full switch of dopamine binding affinity and constitutive activity, while dopamine potency decreased and agonist-mediated maximal activation of adenylyl cyclase increased for both chimeras. Hence, the cytoplasmic tail plays a crucial role in D1-like receptor expression, agonist binding affinity and constitutive activation but regulates in a distinct fashion the formation of D1A and D1B receptor active states upon dopamine binding. | lld:pubmed |
| pubmed-article:10734231 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10734231 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10734231 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10734231 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10734231 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10734231 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10734231 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10734231 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10734231 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:10734231 | pubmed:author | pubmed-author:JacksonAA | lld:pubmed |
| pubmed-article:10734231 | pubmed:author | pubmed-author:TiberiMM | lld:pubmed |
| pubmed-article:10734231 | pubmed:author | pubmed-author:IwasiowR MRM | lld:pubmed |
| pubmed-article:10734231 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10734231 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:10734231 | pubmed:volume | 470 | lld:pubmed |
| pubmed-article:10734231 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10734231 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10734231 | pubmed:pagination | 183-8 | lld:pubmed |
| pubmed-article:10734231 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10734231 | pubmed:meshHeading | pubmed-meshheading:10734231... | lld:pubmed |
| pubmed-article:10734231 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10734231 | pubmed:articleTitle | Distinct function of the cytoplasmic tail in human D1-like receptor ligand binding and coupling. | lld:pubmed |
| pubmed-article:10734231 | pubmed:affiliation | Neurosciences, Loeb Health Research Institute, Ottawa Hospital (Civic Campus) and Department of Cellular and Molecular Medicine, University of Ottawa, Ontario, Canada. | lld:pubmed |
| pubmed-article:10734231 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10734231 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10734231 | lld:pubmed |
