Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:18989099rdf:typepubmed:Citationlld:pubmed
pubmed-article:18989099lifeskim:mentionsumls-concept:C0004391lld:lifeskim
pubmed-article:18989099lifeskim:mentionsumls-concept:C0243043lld:lifeskim
pubmed-article:18989099lifeskim:mentionsumls-concept:C0302583lld:lifeskim
pubmed-article:18989099lifeskim:mentionsumls-concept:C0376315lld:lifeskim
pubmed-article:18989099lifeskim:mentionsumls-concept:C1527256lld:lifeskim
pubmed-article:18989099pubmed:issue1lld:pubmed
pubmed-article:18989099pubmed:dateCreated2008-12-29lld:pubmed
pubmed-article:18989099pubmed:abstractTextLysosomes contain most of the cell's supply of labile iron, which makes them sensitive to oxidative stress. To keep lysosomal labile iron at a minimum, a cellular strategy might be to autophagocytose iron binding proteins that temporarily would chelate iron in a non-redox-active form. Previously we have shown that autophagy of metallothioneins, as well as of non-Fe-saturated ferritin, meets this goal. Here we add another stress-regulated protein to the list, namely HSP70.lld:pubmed
pubmed-article:18989099pubmed:languageenglld:pubmed
pubmed-article:18989099pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18989099pubmed:citationSubsetIMlld:pubmed
pubmed-article:18989099pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18989099pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18989099pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18989099pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18989099pubmed:statusMEDLINElld:pubmed
pubmed-article:18989099pubmed:monthJanlld:pubmed
pubmed-article:18989099pubmed:issn1554-8635lld:pubmed
pubmed-article:18989099pubmed:authorpubmed-author:BrunkUlf TUTlld:pubmed
pubmed-article:18989099pubmed:authorpubmed-author:KurzTinoTlld:pubmed
pubmed-article:18989099pubmed:issnTypeElectroniclld:pubmed
pubmed-article:18989099pubmed:volume5lld:pubmed
pubmed-article:18989099pubmed:ownerNLMlld:pubmed
pubmed-article:18989099pubmed:authorsCompleteYlld:pubmed
pubmed-article:18989099pubmed:pagination93-5lld:pubmed
pubmed-article:18989099pubmed:dateRevised2011-6-30lld:pubmed
pubmed-article:18989099pubmed:meshHeadingpubmed-meshheading:18989099...lld:pubmed
pubmed-article:18989099pubmed:meshHeadingpubmed-meshheading:18989099...lld:pubmed
pubmed-article:18989099pubmed:meshHeadingpubmed-meshheading:18989099...lld:pubmed
pubmed-article:18989099pubmed:meshHeadingpubmed-meshheading:18989099...lld:pubmed
pubmed-article:18989099pubmed:meshHeadingpubmed-meshheading:18989099...lld:pubmed
pubmed-article:18989099pubmed:meshHeadingpubmed-meshheading:18989099...lld:pubmed
pubmed-article:18989099pubmed:meshHeadingpubmed-meshheading:18989099...lld:pubmed
pubmed-article:18989099pubmed:meshHeadingpubmed-meshheading:18989099...lld:pubmed
pubmed-article:18989099pubmed:year2009lld:pubmed
pubmed-article:18989099pubmed:articleTitleAutophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form.lld:pubmed
pubmed-article:18989099pubmed:affiliationDivision of Pharmacology, Faculty of Health Sciences, Linköping University, Linköping, Sweden.lld:pubmed
pubmed-article:18989099pubmed:publicationTypeJournal Articlelld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18989099lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18989099lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18989099lld:pubmed