Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:3680176rdf:typepubmed:Citationlld:pubmed
pubmed-article:3680176lifeskim:mentionsumls-concept:C0317968lld:lifeskim
pubmed-article:3680176lifeskim:mentionsumls-concept:C0025252lld:lifeskim
pubmed-article:3680176lifeskim:mentionsumls-concept:C1167331lld:lifeskim
pubmed-article:3680176lifeskim:mentionsumls-concept:C0009968lld:lifeskim
pubmed-article:3680176lifeskim:mentionsumls-concept:C0030016lld:lifeskim
pubmed-article:3680176lifeskim:mentionsumls-concept:C1881217lld:lifeskim
pubmed-article:3680176pubmed:issue12lld:pubmed
pubmed-article:3680176pubmed:dateCreated1988-1-14lld:pubmed
pubmed-article:3680176pubmed:abstractTextAmong a set of frameshift mutagen (ICR-191; Polysciences, Inc.)-induced mutations that confer inability to grow anaerobically with N2O as the sole electron acceptor, one class was found that produced an inactive N2O reductase which lacked copper. All of these mutant strains failed to produce a 61,000-Mr protein located in the outer membrane. This protein, termed NosA, seems not to be responsible for bringing copper into the cell because the mutant strains and their parent were similarly sensitive to the copper content of the growth medium and no intermediate copper concentration in the medium permitted the mutant strains (nosA) to grow anaerobically with N2O as the sole electron acceptor. We conclude that NosA is necessary to insert copper into N2O reductase or to maintain it there.lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:languageenglld:pubmed
pubmed-article:3680176pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:citationSubsetIMlld:pubmed
pubmed-article:3680176pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3680176pubmed:statusMEDLINElld:pubmed
pubmed-article:3680176pubmed:monthDeclld:pubmed
pubmed-article:3680176pubmed:issn0021-9193lld:pubmed
pubmed-article:3680176pubmed:authorpubmed-author:ClarkM AMAlld:pubmed
pubmed-article:3680176pubmed:authorpubmed-author:IngrahamJ LJLlld:pubmed
pubmed-article:3680176pubmed:authorpubmed-author:TangY JYJlld:pubmed
pubmed-article:3680176pubmed:authorpubmed-author:MokheleKKlld:pubmed
pubmed-article:3680176pubmed:issnTypePrintlld:pubmed
pubmed-article:3680176pubmed:volume169lld:pubmed
pubmed-article:3680176pubmed:ownerNLMlld:pubmed
pubmed-article:3680176pubmed:authorsCompleteYlld:pubmed
pubmed-article:3680176pubmed:pagination5721-6lld:pubmed
pubmed-article:3680176pubmed:dateRevised2009-11-18lld:pubmed
pubmed-article:3680176pubmed:meshHeadingpubmed-meshheading:3680176-...lld:pubmed
pubmed-article:3680176pubmed:meshHeadingpubmed-meshheading:3680176-...lld:pubmed
pubmed-article:3680176pubmed:meshHeadingpubmed-meshheading:3680176-...lld:pubmed
pubmed-article:3680176pubmed:meshHeadingpubmed-meshheading:3680176-...lld:pubmed
pubmed-article:3680176pubmed:meshHeadingpubmed-meshheading:3680176-...lld:pubmed
pubmed-article:3680176pubmed:meshHeadingpubmed-meshheading:3680176-...lld:pubmed
pubmed-article:3680176pubmed:meshHeadingpubmed-meshheading:3680176-...lld:pubmed
pubmed-article:3680176pubmed:year1987lld:pubmed
pubmed-article:3680176pubmed:articleTitleA Pseudomonas stutzeri outer membrane protein inserts copper into N2O reductase.lld:pubmed
pubmed-article:3680176pubmed:affiliationDepartment of Bacteriology, University of California, Davis 95616.lld:pubmed
pubmed-article:3680176pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:3680176pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:3680176lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:3680176lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:3680176lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:3680176lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:3680176lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:3680176lld:pubmed