Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:1713060rdf:typepubmed:Citationlld:pubmed
pubmed-article:1713060lifeskim:mentionsumls-concept:C0596972lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0007452lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0018338lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0031640lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C1704675lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C1167622lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0439851lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0014274lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0376451lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0231881lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C1521743lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0181904lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C1704646lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C1707310lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0728873lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C1552596lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C1879547lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C1947931lld:lifeskim
pubmed-article:1713060lifeskim:mentionsumls-concept:C0040664lld:lifeskim
pubmed-article:1713060pubmed:issue29lld:pubmed
pubmed-article:1713060pubmed:dateCreated1991-8-27lld:pubmed
pubmed-article:1713060pubmed:abstractTextResonance energy-transfer approaches have been used to directly monitor the interactions of the GTP gamma S-bound alpha subunit of transducin (alpha T GTP gamma S) with the retinal cyclic GMP phosphodiesterase (PDE). The PDE was labeled with 5-(iodoacetamido) fluorescein (IAF-PDE) and served as the fluorescence donor in these experiments while the alpha T GTP gamma S was labeled with eosin-5-isothiocyanate (EITC-alpha T GTP gamma S) and served as the energy acceptor. The EITC-alpha T GTP gamma S species was able to quench a significant percentage of the IAF-PDE fluorescence (typically greater than or equal to 30%) due to resonance energy transfer between the IAF and EITC moieties. The quenching by the EITC-alpha T GTP gamma S species was dose-dependent, saturable (Kd = 21 nM), and specific for the GTP gamma S-bound form of the alpha T subunit. Limited trypsin treatment of the IAF-PDE, which selectively removes a fluorescein-labeled gamma subunit (gamma PDE), completely eliminates the quenching of the IAF fluorescence by the EITC-alpha T GTP gamma S complex. Although the EITC-alpha T GTP gamma S complex competes with the unlabeled alpha T GTP gamma S for a binding site on the IAF-PDE, as well as for a site on the native PDE, it is not able to stimulate PDE activity. Thus, the modification of a single EITC-reactive residue on the alpha T GTP gamma S complex prevents this subunit from eliciting a key activation event within the retinal effector enzyme.lld:pubmed
pubmed-article:1713060pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:languageenglld:pubmed
pubmed-article:1713060pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:citationSubsetIMlld:pubmed
pubmed-article:1713060pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1713060pubmed:statusMEDLINElld:pubmed
pubmed-article:1713060pubmed:monthJullld:pubmed
pubmed-article:1713060pubmed:issn0006-2960lld:pubmed
pubmed-article:1713060pubmed:authorpubmed-author:EricksonJ WJWlld:pubmed
pubmed-article:1713060pubmed:authorpubmed-author:CerioneR ARAlld:pubmed
pubmed-article:1713060pubmed:issnTypePrintlld:pubmed
pubmed-article:1713060pubmed:day23lld:pubmed
pubmed-article:1713060pubmed:volume30lld:pubmed
pubmed-article:1713060pubmed:ownerNLMlld:pubmed
pubmed-article:1713060pubmed:authorsCompleteYlld:pubmed
pubmed-article:1713060pubmed:pagination7112-8lld:pubmed
pubmed-article:1713060pubmed:dateRevised2008-11-21lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:meshHeadingpubmed-meshheading:1713060-...lld:pubmed
pubmed-article:1713060pubmed:year1991lld:pubmed
pubmed-article:1713060pubmed:articleTitleResonance energy transfer as a direct monitor of GTP-binding protein-effector interactions: activated alpha-transducin binding to the cGMP phosphodiesterase in the bovine phototransduction cascade.lld:pubmed
pubmed-article:1713060pubmed:affiliationDepartment of Pharmacology, New York State College of Veterinary Medicine, Cornell University, Ithaca 14853-6401.lld:pubmed
pubmed-article:1713060pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1713060pubmed:publicationTypeIn Vitrolld:pubmed
pubmed-article:1713060pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:1713060pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:1713060pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:1713060lld:pubmed