Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:2966734rdf:typepubmed:Citationlld:pubmed
pubmed-article:2966734lifeskim:mentionsumls-concept:C0032148lld:lifeskim
pubmed-article:2966734lifeskim:mentionsumls-concept:C0014792lld:lifeskim
pubmed-article:2966734lifeskim:mentionsumls-concept:C0010853lld:lifeskim
pubmed-article:2966734lifeskim:mentionsumls-concept:C0021699lld:lifeskim
pubmed-article:2966734lifeskim:mentionsumls-concept:C0475264lld:lifeskim
pubmed-article:2966734pubmed:issue2lld:pubmed
pubmed-article:2966734pubmed:dateCreated1988-6-14lld:pubmed
pubmed-article:2966734pubmed:abstractTextThe distributions of ankyrin, spectrin, band 3, and glycophorin A were examined in Plasmodium falciparum-infected erythrocytes by immunoelectron microscopy to determine whether movement of parasite proteins and membrane vesicles between the parasitophorous vacuole membrane and erythrocyte surface membrane involves internalization of host membrane skeleton proteins. Monospecific rabbit antisera to spectrin, band 3 and ankyrin and a mouse monoclonal antibody to glycophorin A reacted with these erythrocyte proteins in infected and uninfected human erythrocytes by immunoblotting. Cross-reacting malarial proteins were not detected. The rabbit sera also failed to immunoprecipitate [3H]isoleucine labeled malarial proteins from Triton X-100 and sodium dodecyl sulfate (SDS) extracts of infected erythrocytes. These three antibodies as well as the monoclonal antibody to glycophorin A bound to the membrane skeleton of infected and uninfected erythrocytes. The parasitophorous vacuole membrane was devoid of bound antibody, a result indicating that this membrane contains little, if any, of these host membrane proteins. With ring-, trophozoite- and schizont-infected erythrocytes, spectrin, band 3 and glycophorin A were absent from intracellular membranes including Maurer's clefts and other vesicles in the erythrocyte cytoplasm. In contrast, Maurer's clefts were specifically labeled by anti-ankyrin antibody. There was a slight, corresponding decrease in labeling of the membrane skeleton of infected erythrocytes. A second, morphologically distinct population of circular, vesicle-like membranes in the erythrocyte cytoplasm was not labeled with anti-ankyrin antibody. We conclude that membrane movement between the host erythrocyte surface membrane and parasitophorous vacuole membrane involves preferential sorting of ankyrin into a subpopulation of cytoplasmic membranes.lld:pubmed
pubmed-article:2966734pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:languageenglld:pubmed
pubmed-article:2966734pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:citationSubsetIMlld:pubmed
pubmed-article:2966734pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2966734pubmed:statusMEDLINElld:pubmed
pubmed-article:2966734pubmed:monthFeblld:pubmed
pubmed-article:2966734pubmed:issn0171-9335lld:pubmed
pubmed-article:2966734pubmed:authorpubmed-author:DavidsonE AEAlld:pubmed
pubmed-article:2966734pubmed:authorpubmed-author:HowardR JRJlld:pubmed
pubmed-article:2966734pubmed:authorpubmed-author:BennettVVlld:pubmed
pubmed-article:2966734pubmed:authorpubmed-author:AikawaMMlld:pubmed
pubmed-article:2966734pubmed:authorpubmed-author:FujinoTTlld:pubmed
pubmed-article:2966734pubmed:authorpubmed-author:PerryGGlld:pubmed
pubmed-article:2966734pubmed:authorpubmed-author:AtkinsonC TCTlld:pubmed
pubmed-article:2966734pubmed:issnTypePrintlld:pubmed
pubmed-article:2966734pubmed:volume45lld:pubmed
pubmed-article:2966734pubmed:ownerNLMlld:pubmed
pubmed-article:2966734pubmed:authorsCompleteYlld:pubmed
pubmed-article:2966734pubmed:pagination192-9lld:pubmed
pubmed-article:2966734pubmed:dateRevised2007-11-14lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:meshHeadingpubmed-meshheading:2966734-...lld:pubmed
pubmed-article:2966734pubmed:year1988lld:pubmed
pubmed-article:2966734pubmed:articleTitleUltrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes.lld:pubmed
pubmed-article:2966734pubmed:affiliationInstitute of Pathology, Case Western Reserve University, Cleveland, OH 44106.lld:pubmed
pubmed-article:2966734pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2966734pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:2966734pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:2966734pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:2966734lld:pubmed