Linked Life Data

3049938

Source:http://linkedlifedata.com/resource/pubmed/id/3049938

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:3049938rdf:typepubmed:Citationlld:pubmed
pubmed-article:3049938lifeskim:mentionsumls-concept:C1145669lld:lifeskim
pubmed-article:3049938lifeskim:mentionsumls-concept:C0086418lld:lifeskim
pubmed-article:3049938lifeskim:mentionsumls-concept:C1314972lld:lifeskim
pubmed-article:3049938lifeskim:mentionsumls-concept:C0014792lld:lifeskim
pubmed-article:3049938lifeskim:mentionsumls-concept:C0237497lld:lifeskim
pubmed-article:3049938lifeskim:mentionsumls-concept:C0185023lld:lifeskim
pubmed-article:3049938lifeskim:mentionsumls-concept:C1947904lld:lifeskim
pubmed-article:3049938lifeskim:mentionsumls-concept:C1999228lld:lifeskim
pubmed-article:3049938lifeskim:mentionsumls-concept:C2825781lld:lifeskim
pubmed-article:3049938pubmed:dateCreated1988-11-8lld:pubmed
pubmed-article:3049938pubmed:abstractTextBinding experiments with radioactively labelled influenza C virions were carried out to investigate the interaction of the virus with human erythrocytes. The erythrocytes from any of 35 different individuals were found to contain influenza C virus-binding sites though their number was variable among the individuals and was much less than that on mouse, rat and chicken erythrocytes. Attachment of influenza C virus to human erythrocytes was inhibited completely by prior treatment of the virus with anti-HE monoclonal antibody having a strong haemagglutination inhibition activity. Pretreatment of erythrocytes with neuraminidase or the neuraminate-O-acetylesterase of influenza C virus resulted in a marked reduction in the level of virus binding. Thus it appears that human erythrocytes have a low level of O-acetylated sialic acid-containing glycoconjugates that can interact specifically with the HE glycoprotein of influenza C virus. Proteolytic digestion of erythrocytes with ficin, bromelain or V-8 protease inhibited virus binding almost completely, suggesting that the erythrocyte receptor for influenza C virus is a glycoprotein. In contrast to these enzymes, trypsin treatment of erythrocytes reduced virus binding by only about 50%, and alpha-chymotrypsin treatment did not inhibit at all. It was also found that treatment of erythrocytes with monoclonal antibody to the M or N blood group antigen greatly inhibited virus binding to the cells. These results, taken together, suggest that most influenza C virus receptors on human erythrocytes, if not all, reside on glycophorin A which is known to possess the M or N blood group activity.lld:pubmed
pubmed-article:3049938pubmed:languageenglld:pubmed
pubmed-article:3049938pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3049938pubmed:citationSubsetIMlld:pubmed
pubmed-article:3049938pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3049938pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3049938pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3049938pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3049938pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3049938pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3049938pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3049938pubmed:statusMEDLINElld:pubmed
pubmed-article:3049938pubmed:monthOctlld:pubmed
pubmed-article:3049938pubmed:issn0022-1317lld:pubmed
pubmed-article:3049938pubmed:authorpubmed-author:KitameFFlld:pubmed
pubmed-article:3049938pubmed:authorpubmed-author:NakamuraKKlld:pubmed
pubmed-article:3049938pubmed:authorpubmed-author:SugawaraKKlld:pubmed
pubmed-article:3049938pubmed:authorpubmed-author:NishimuraHHlld:pubmed
pubmed-article:3049938pubmed:issnTypePrintlld:pubmed
pubmed-article:3049938pubmed:volume69 ( Pt 10)lld:pubmed
pubmed-article:3049938pubmed:ownerNLMlld:pubmed
pubmed-article:3049938pubmed:authorsCompleteYlld:pubmed
pubmed-article:3049938pubmed:pagination2545-53lld:pubmed
pubmed-article:3049938pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:meshHeadingpubmed-meshheading:3049938-...lld:pubmed
pubmed-article:3049938pubmed:year1988lld:pubmed
pubmed-article:3049938pubmed:articleTitleAttachment of influenza C virus to human erythrocytes.lld:pubmed
pubmed-article:3049938pubmed:affiliationDepartment of Bacteriology, Yamagata University School of Medicine, Japan.lld:pubmed
pubmed-article:3049938pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:3049938pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:3049938lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:3049938lld:pubmed