Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10788321rdf:typepubmed:Citationlld:pubmed
pubmed-article:10788321lifeskim:mentionsumls-concept:C0036126lld:lifeskim
pubmed-article:10788321lifeskim:mentionsumls-concept:C0039020lld:lifeskim
pubmed-article:10788321lifeskim:mentionsumls-concept:C0440043lld:lifeskim
pubmed-article:10788321lifeskim:mentionsumls-concept:C1705994lld:lifeskim
pubmed-article:10788321lifeskim:mentionsumls-concept:C1513492lld:lifeskim
pubmed-article:10788321pubmed:issue4lld:pubmed
pubmed-article:10788321pubmed:dateCreated2000-6-2lld:pubmed
pubmed-article:10788321pubmed:abstractTextThree Salmonella typhimurium flagellar motor proteins, FliG, FliM and FliN, are required for the switching of rotation sense. The proteins have been localized to the cytoplasmic module of the flagellar base. Structures, which were morphologically indistinguishable from the native transmembrane MS-ring and cytoplasmic C-ring basal body modules, formed in Escherichia coli upon plasmid-encoded synthesis of these proteins together with FliF. The structures localized to the cell membrane and contained all three motor proteins, as determined by immuno-electron microscopy. This result supports the deduction, based on earlier biochemical analysis, that the C-ring is composed entirely of these proteins and, therefore, functions as a dedicated motor component. In addition, it demonstrates that the morphologically correct assembly of the C-ring onto the MS-ring proceeds independently of other structural components of these modules.lld:pubmed
pubmed-article:10788321pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:languageenglld:pubmed
pubmed-article:10788321pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:citationSubsetIMlld:pubmed
pubmed-article:10788321pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10788321pubmed:statusMEDLINElld:pubmed
pubmed-article:10788321pubmed:monthMaylld:pubmed
pubmed-article:10788321pubmed:issn0022-2836lld:pubmed
pubmed-article:10788321pubmed:authorpubmed-author:KhanSSlld:pubmed
pubmed-article:10788321pubmed:authorpubmed-author:KanJJlld:pubmed
pubmed-article:10788321pubmed:authorpubmed-author:LuyMMlld:pubmed
pubmed-article:10788321pubmed:copyrightInfoCopyright 2000 Academic Press.lld:pubmed
pubmed-article:10788321pubmed:issnTypePrintlld:pubmed
pubmed-article:10788321pubmed:day12lld:pubmed
pubmed-article:10788321pubmed:volume298lld:pubmed
pubmed-article:10788321pubmed:ownerNLMlld:pubmed
pubmed-article:10788321pubmed:authorsCompleteYlld:pubmed
pubmed-article:10788321pubmed:pagination577-83lld:pubmed
pubmed-article:10788321pubmed:dateRevised2007-11-14lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:meshHeadingpubmed-meshheading:10788321...lld:pubmed
pubmed-article:10788321pubmed:year2000lld:pubmed
pubmed-article:10788321pubmed:articleTitleOverproduced Salmonella typhimurium flagellar motor switch complexes.lld:pubmed
pubmed-article:10788321pubmed:affiliationLaboratory of Cellular Bioenergetics, Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA.lld:pubmed
pubmed-article:10788321pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10788321pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10788321lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10788321lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10788321lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10788321lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10788321lld:pubmed