Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:1587638rdf:typepubmed:Citationlld:pubmed
pubmed-article:1587638lifeskim:mentionsumls-concept:C0086418lld:lifeskim
pubmed-article:1587638lifeskim:mentionsumls-concept:C0524637lld:lifeskim
pubmed-article:1587638lifeskim:mentionsumls-concept:C0004358lld:lifeskim
pubmed-article:1587638lifeskim:mentionsumls-concept:C0020852lld:lifeskim
pubmed-article:1587638lifeskim:mentionsumls-concept:C1708096lld:lifeskim
pubmed-article:1587638lifeskim:mentionsumls-concept:C0445604lld:lifeskim
pubmed-article:1587638lifeskim:mentionsumls-concept:C0439855lld:lifeskim
pubmed-article:1587638lifeskim:mentionsumls-concept:C1704711lld:lifeskim
pubmed-article:1587638lifeskim:mentionsumls-concept:C0439098lld:lifeskim
pubmed-article:1587638pubmed:issue3lld:pubmed
pubmed-article:1587638pubmed:dateCreated1992-6-23lld:pubmed
pubmed-article:1587638pubmed:abstractTextCirculating IgG autoanti-IgE is detectable in a large proportion of individuals with allergic asthma where it is suggested to be potentially involved in the removal of IgE-allergen complexes. Since such a putative role will largely be determined by the subclass profile of complexed (i.e. IgE-bound) IgG anti-IgE, a study was undertaken to determine the subclass distribution of complexed IgG anti-IgE antibody in the sera of asthmatic patients. The study exploits the heat-labile property of IgE by heating (30 min at 56 degrees C) serum to liberate bound anti-IgE, pre- and post-heated sera are then assayed for IgG subclass anti-recombinant human Fc epsilon (rFc epsilon) activities by ELISA and any heat-induced increase in antibody activity is taken as a measure of complexed anti-IgE. This has revealed a disproportionately high amount of IgG4 in complexed (but not free) IgG anti-IgE. The propensity of IgG4 to form complexes with IgE has important biological consequences, particularly with regard to the activation of C1q and Fc gamma R by other subclasses.lld:pubmed
pubmed-article:1587638pubmed:languageenglld:pubmed
pubmed-article:1587638pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1587638pubmed:citationSubsetIMlld:pubmed
pubmed-article:1587638pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1587638pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1587638pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1587638pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1587638pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1587638pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1587638pubmed:statusMEDLINElld:pubmed
pubmed-article:1587638pubmed:issn1018-2438lld:pubmed
pubmed-article:1587638pubmed:authorpubmed-author:ShakibFFlld:pubmed
pubmed-article:1587638pubmed:authorpubmed-author:MillsC SCSlld:pubmed
pubmed-article:1587638pubmed:authorpubmed-author:Powell-Richar...lld:pubmed
pubmed-article:1587638pubmed:issnTypePrintlld:pubmed
pubmed-article:1587638pubmed:volume97lld:pubmed
pubmed-article:1587638pubmed:ownerNLMlld:pubmed
pubmed-article:1587638pubmed:authorsCompleteYlld:pubmed
pubmed-article:1587638pubmed:pagination243-8lld:pubmed
pubmed-article:1587638pubmed:dateRevised2008-11-21lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:meshHeadingpubmed-meshheading:1587638-...lld:pubmed
pubmed-article:1587638pubmed:year1992lld:pubmed
pubmed-article:1587638pubmed:articleTitleThe recognition of a recombinant human Fc epsilon fragment by the subclasses of IgG autoanti-IgE: disproportional subclasses distribution of complexed autoantibody.lld:pubmed
pubmed-article:1587638pubmed:affiliationDepartment of Immunology, University Hospital, Queen's Medical Centre, Nottingham, UK.lld:pubmed
pubmed-article:1587638pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1587638pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:1587638lld:pubmed