Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:12615322rdf:typepubmed:Citationlld:pubmed
pubmed-article:12615322lifeskim:mentionsumls-concept:C0032148lld:lifeskim
pubmed-article:12615322lifeskim:mentionsumls-concept:C0033684lld:lifeskim
pubmed-article:12615322lifeskim:mentionsumls-concept:C0032150lld:lifeskim
pubmed-article:12615322lifeskim:mentionsumls-concept:C0017262lld:lifeskim
pubmed-article:12615322lifeskim:mentionsumls-concept:C1145667lld:lifeskim
pubmed-article:12615322lifeskim:mentionsumls-concept:C2911684lld:lifeskim
pubmed-article:12615322lifeskim:mentionsumls-concept:C0185117lld:lifeskim
pubmed-article:12615322pubmed:issue2lld:pubmed
pubmed-article:12615322pubmed:dateCreated2003-3-4lld:pubmed
pubmed-article:12615322pubmed:databankReferencehttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:abstractTextPlasmodium falciparum iron regulatory-like protein (PfIRPa, accession AJ012289) has homology to a family of iron-responsive element (IRE)-binding proteins (IRPs) found in different species. We have previously demonstrated that erythrocyte P. falciparum PfIRPa binds a mammalian consensus IRE and that the binding activity is regulated by iron status. In the work we now report, we have cloned a C-terminus histidine-tagged PfIRPa and overexpressed it in a bacterial expression system in soluble form capable of binding IREs. To overexpress PfIRPa, we used the T7 promoter-driven vector, pET28a(+), in conjunction with the Rosetta(DE3)pLysS strain of E. coli, which carries extra copies of tRNA genes usually found in organisms such as P. falciparum whose genome is (A+T)-rich. The histidine-tagged recombinant protein (rPfIRPa) in soluble form was partially purified using His-bind resin. We searched the plasmodial database, plasmoDB, to identify sequences capable of forming IRE loops using a specially developed algorithm, and found three plasmodial sequences matching the search criteria. In gel retardation assays, rPfIRPa bound three 32P-labeled putative plasmodial IREs with affinity exceeding the affinity for the mammalian consensus IRE. The binding was concentration-dependent and was not inhibited by heparin, an inhibitor of non-specific binding. Immunodepletion of rPfIRPa resulted in substantial inhibition of the signal intensity in the gel retardation assays and in Western blot-determinations of rPfIRPa protein levels. Endogenous PfIRPa retained all three putative 32P-IREs at the same position on the gel as the recombinant PfIRPa.lld:pubmed
pubmed-article:12615322pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:languageenglld:pubmed
pubmed-article:12615322pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:citationSubsetIMlld:pubmed
pubmed-article:12615322pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12615322pubmed:statusMEDLINElld:pubmed
pubmed-article:12615322pubmed:monthFeblld:pubmed
pubmed-article:12615322pubmed:issn0166-6851lld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:GordeukVictor...lld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:YikilmazEmine...lld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:WoottonJohn...lld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:RouaultTracey...lld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:AltschulSteph...lld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:LoyevskyMarkMlld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:MompointFarah...lld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:MaddenThomasTlld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:Kurantsin-Mil...lld:pubmed
pubmed-article:12615322pubmed:authorpubmed-author:KassimOlakunl...lld:pubmed
pubmed-article:12615322pubmed:copyrightInfoCopyright 2002 Elsevier Science B.V.lld:pubmed
pubmed-article:12615322pubmed:issnTypePrintlld:pubmed
pubmed-article:12615322pubmed:volume126lld:pubmed
pubmed-article:12615322pubmed:ownerNLMlld:pubmed
pubmed-article:12615322pubmed:authorsCompleteYlld:pubmed
pubmed-article:12615322pubmed:pagination231-8lld:pubmed
pubmed-article:12615322pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:meshHeadingpubmed-meshheading:12615322...lld:pubmed
pubmed-article:12615322pubmed:year2003lld:pubmed
pubmed-article:12615322pubmed:articleTitleExpression of a recombinant IRP-like Plasmodium falciparum protein that specifically binds putative plasmodial IREs.lld:pubmed
pubmed-article:12615322pubmed:affiliationCenter for Sickle Cell Disease, Howard University, 2121 Georgia Avenue, NW, Washington, DC 20059, USA. mloyevsky@howard.edulld:pubmed
pubmed-article:12615322pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12615322pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12615322lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12615322lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12615322lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12615322lld:pubmed