Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:19539506rdf:typepubmed:Citationlld:pubmed
pubmed-article:19539506lifeskim:mentionsumls-concept:C0030705lld:lifeskim
pubmed-article:19539506lifeskim:mentionsumls-concept:C0026764lld:lifeskim
pubmed-article:19539506lifeskim:mentionsumls-concept:C0123256lld:lifeskim
pubmed-article:19539506lifeskim:mentionsumls-concept:C0486805lld:lifeskim
pubmed-article:19539506lifeskim:mentionsumls-concept:C2263455lld:lifeskim
pubmed-article:19539506pubmed:issue6lld:pubmed
pubmed-article:19539506pubmed:dateCreated2009-11-26lld:pubmed
pubmed-article:19539506pubmed:abstractTextCleavage of IGFBPs by proteases results in IGFBP fragments that have altered IGF-binding affinity, and IGF-independent roles. We have previously purified a specific IGFBP-1 protease activity from the urine of an individual with multiple myeloma and dermatitis. The aim of this study was to determine whether IGFBP-1 protease activity and/or IGFBP-1 fragments were present in the circulation of this patient.lld:pubmed
pubmed-article:19539506pubmed:languageenglld:pubmed
pubmed-article:19539506pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:citationSubsetIMlld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19539506pubmed:statusMEDLINElld:pubmed
pubmed-article:19539506pubmed:monthDeclld:pubmed
pubmed-article:19539506pubmed:issn1532-2238lld:pubmed
pubmed-article:19539506pubmed:authorpubmed-author:JörnvallHansHlld:pubmed
pubmed-article:19539506pubmed:authorpubmed-author:EhrenborgEwaElld:pubmed
pubmed-article:19539506pubmed:authorpubmed-author:WangJingJlld:pubmed
pubmed-article:19539506pubmed:authorpubmed-author:LundellKersti...lld:pubmed
pubmed-article:19539506pubmed:authorpubmed-author:HallKerstinKlld:pubmed
pubmed-article:19539506pubmed:authorpubmed-author:StåhlbergMari...lld:pubmed
pubmed-article:19539506pubmed:authorpubmed-author:LewittMoiraMlld:pubmed
pubmed-article:19539506pubmed:authorpubmed-author:BrandtKatrinKlld:pubmed
pubmed-article:19539506pubmed:authorpubmed-author:HornHenrik...lld:pubmed
pubmed-article:19539506pubmed:issnTypeElectroniclld:pubmed
pubmed-article:19539506pubmed:volume19lld:pubmed
pubmed-article:19539506pubmed:ownerNLMlld:pubmed
pubmed-article:19539506pubmed:authorsCompleteYlld:pubmed
pubmed-article:19539506pubmed:pagination507-12lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:meshHeadingpubmed-meshheading:19539506...lld:pubmed
pubmed-article:19539506pubmed:year2009lld:pubmed
pubmed-article:19539506pubmed:articleTitleIGFBP-1 protease activity and IGFBP-1 fragments in a patient with multiple myeloma.lld:pubmed
pubmed-article:19539506pubmed:affiliationDepartment of Molecular Medicine and Surgery, Karolinska Institutet, L1:01 Karolinska University Hospital Solna, SE-171 76 Stockholm, Sweden.lld:pubmed
pubmed-article:19539506pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19539506pubmed:publicationTypeCase Reportslld:pubmed
pubmed-article:19539506pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:3484entrezgene:pubmedpubmed-article:19539506lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:19539506lld:entrezgene