| pubmed-article:15595821 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15595821 | lifeskim:mentions | umls-concept:C0682972 | lld:lifeskim |
| pubmed-article:15595821 | lifeskim:mentions | umls-concept:C0016884 | lld:lifeskim |
| pubmed-article:15595821 | pubmed:issue | 50 | lld:pubmed |
| pubmed-article:15595821 | pubmed:dateCreated | 2004-12-14 | lld:pubmed |
| pubmed-article:15595821 | pubmed:abstractText | G protein-coupled receptor (GPCR)-mediated signal transduction has been studied for more than a century. Despite the intense focus on this class of proteins, a molecular understanding of what constitutes the functional form of the receptor is still uncertain. GPCRs have traditionally been conceptualized as monomeric proteins, and this view has changed little over the years until relatively recently. Recent biochemical and biophysical studies have challenged this traditional concept, and point instead to a mechanistic view of signal transduction wherein the receptor functions as an oligomer. Cooperative interactions within such an oligomeric array may be critical for the propagation of an external signal across the cell membrane and to the G protein, and may therefore underlie the mechanistic basis of signaling. | lld:pubmed |
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