Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:1989597rdf:typepubmed:Citationlld:pubmed
pubmed-article:1989597lifeskim:mentionsumls-concept:C0014792lld:lifeskim
pubmed-article:1989597lifeskim:mentionsumls-concept:C0019046lld:lifeskim
pubmed-article:1989597lifeskim:mentionsumls-concept:C0016327lld:lifeskim
pubmed-article:1989597lifeskim:mentionsumls-concept:C0038838lld:lifeskim
pubmed-article:1989597lifeskim:mentionsumls-concept:C1704675lld:lifeskim
pubmed-article:1989597lifeskim:mentionsumls-concept:C0024485lld:lifeskim
pubmed-article:1989597lifeskim:mentionsumls-concept:C2603343lld:lifeskim
pubmed-article:1989597pubmed:issue1lld:pubmed
pubmed-article:1989597pubmed:dateCreated1991-2-22lld:pubmed
pubmed-article:1989597pubmed:abstractTextF- added to an erythrocyte suspension shows two separated resonances arisen from intra and extracellular compartments. Cu, Zn superoxide dismutase dominates the longitudinal relaxation rate of the intracellular F- resonance, while diamagnetic interactions with hemoglobin contribute mainly to the transversal relaxation rate.lld:pubmed
pubmed-article:1989597pubmed:languageenglld:pubmed
pubmed-article:1989597pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1989597pubmed:citationSubsetIMlld:pubmed
pubmed-article:1989597pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1989597pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1989597pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1989597pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1989597pubmed:statusMEDLINElld:pubmed
pubmed-article:1989597pubmed:monthJanlld:pubmed
pubmed-article:1989597pubmed:issn0006-291Xlld:pubmed
pubmed-article:1989597pubmed:authorpubmed-author:RigoAAlld:pubmed
pubmed-article:1989597pubmed:authorpubmed-author:ViglinoPPlld:pubmed
pubmed-article:1989597pubmed:authorpubmed-author:VianelloFFlld:pubmed
pubmed-article:1989597pubmed:authorpubmed-author:ScarpaMMlld:pubmed
pubmed-article:1989597pubmed:issnTypePrintlld:pubmed
pubmed-article:1989597pubmed:day15lld:pubmed
pubmed-article:1989597pubmed:volume174lld:pubmed
pubmed-article:1989597pubmed:ownerNLMlld:pubmed
pubmed-article:1989597pubmed:authorsCompleteYlld:pubmed
pubmed-article:1989597pubmed:pagination163-8lld:pubmed
pubmed-article:1989597pubmed:dateRevised2000-12-18lld:pubmed
pubmed-article:1989597pubmed:meshHeadingpubmed-meshheading:1989597-...lld:pubmed
pubmed-article:1989597pubmed:meshHeadingpubmed-meshheading:1989597-...lld:pubmed
pubmed-article:1989597pubmed:meshHeadingpubmed-meshheading:1989597-...lld:pubmed
pubmed-article:1989597pubmed:meshHeadingpubmed-meshheading:1989597-...lld:pubmed
pubmed-article:1989597pubmed:meshHeadingpubmed-meshheading:1989597-...lld:pubmed
pubmed-article:1989597pubmed:meshHeadingpubmed-meshheading:1989597-...lld:pubmed
pubmed-article:1989597pubmed:year1991lld:pubmed
pubmed-article:1989597pubmed:articleTitle19F NMR study of the interactions of fluoride with superoxide dismutase and hemoglobin in erythrocytes.lld:pubmed
pubmed-article:1989597pubmed:affiliationDepartment of Biological Chemistry, University of Padova, Italy.lld:pubmed
pubmed-article:1989597pubmed:publicationTypeJournal Articlelld:pubmed