pubmed-article:21477594 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21477594 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:21477594 | lifeskim:mentions | umls-concept:C0682972 | lld:lifeskim |
pubmed-article:21477594 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:21477594 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
pubmed-article:21477594 | lifeskim:mentions | umls-concept:C0303920 | lld:lifeskim |
pubmed-article:21477594 | lifeskim:mentions | umls-concept:C0682770 | lld:lifeskim |
pubmed-article:21477594 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:21477594 | pubmed:dateCreated | 2011-5-30 | lld:pubmed |
pubmed-article:21477594 | pubmed:abstractText | We describe a rapid method to probe for mutations in cell surface ligand-binding proteins that affect the environment of bound ligand. The method uses fluorescence-activated cell sorting to screen randomly mutated receptors for substitutions that alter the fluorescence emission spectrum of environmentally sensitive fluorescent ligands. When applied to the yeast ?-factor receptor Ste2p, a G protein-coupled receptor, the procedure identified 22 substitutions that red shift the emission of a fluorescent agonist, including substitutions at residues previously implicated in ligand binding and at additional sites. A separate set of substitutions, identified in a screen for mutations that alter the emission of a fluorescent ?-factor antagonist, occurs at sites that are unlikely to contact the ligand directly. Instead, these mutations alter receptor conformation to increase ligand-binding affinity and provide signaling in response to antagonists of normal receptors. These results suggest that receptor--agonist interactions involve at least two sites, of which only one is specific for the activated conformation of the receptor. | lld:pubmed |
pubmed-article:21477594 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:language | eng | lld:pubmed |
pubmed-article:21477594 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:21477594 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21477594 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21477594 | pubmed:month | Jun | lld:pubmed |
pubmed-article:21477594 | pubmed:issn | 1089-8638 | lld:pubmed |
pubmed-article:21477594 | pubmed:author | pubmed-author:DingFa-XiangF... | lld:pubmed |
pubmed-article:21477594 | pubmed:author | pubmed-author:NaiderFredF | lld:pubmed |
pubmed-article:21477594 | pubmed:author | pubmed-author:DumontMark... | lld:pubmed |
pubmed-article:21477594 | pubmed:author | pubmed-author:ConnellySara... | lld:pubmed |
pubmed-article:21477594 | pubmed:author | pubmed-author:MathewElizabe... | lld:pubmed |
pubmed-article:21477594 | pubmed:author | pubmed-author:SargsyanHasmi... | lld:pubmed |
pubmed-article:21477594 | pubmed:author | pubmed-author:BajajAnshikaA | lld:pubmed |
pubmed-article:21477594 | pubmed:author | pubmed-author:HajduczokAlex... | lld:pubmed |
pubmed-article:21477594 | pubmed:copyrightInfo | Copyright © 2011. Published by Elsevier Ltd. | lld:pubmed |
pubmed-article:21477594 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21477594 | pubmed:day | 17 | lld:pubmed |
pubmed-article:21477594 | pubmed:volume | 409 | lld:pubmed |
pubmed-article:21477594 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21477594 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21477594 | pubmed:pagination | 513-28 | lld:pubmed |
pubmed-article:21477594 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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pubmed-article:21477594 | pubmed:meshHeading | pubmed-meshheading:21477594... | lld:pubmed |
pubmed-article:21477594 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:21477594 | pubmed:articleTitle | Differential interactions of fluorescent agonists and antagonists with the yeast G protein coupled receptor Ste2p. | lld:pubmed |
pubmed-article:21477594 | pubmed:affiliation | Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA. | lld:pubmed |
pubmed-article:21477594 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:21477594 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:850518 | entrezgene:pubmed | pubmed-article:21477594 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21477594 | lld:entrezgene |