Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:1314596rdf:typepubmed:Citationlld:pubmed
pubmed-article:1314596lifeskim:mentionsumls-concept:C0059570lld:lifeskim
pubmed-article:1314596lifeskim:mentionsumls-concept:C0037083lld:lifeskim
pubmed-article:1314596lifeskim:mentionsumls-concept:C0041249lld:lifeskim
pubmed-article:1314596lifeskim:mentionsumls-concept:C1514562lld:lifeskim
pubmed-article:1314596lifeskim:mentionsumls-concept:C1709915lld:lifeskim
pubmed-article:1314596lifeskim:mentionsumls-concept:C0205224lld:lifeskim
pubmed-article:1314596lifeskim:mentionsumls-concept:C1517050lld:lifeskim
pubmed-article:1314596pubmed:issue1lld:pubmed
pubmed-article:1314596pubmed:dateCreated1992-5-20lld:pubmed
pubmed-article:1314596pubmed:abstractTextThe Trp-Ser-X-Trp-Ser motif commonly exists just outside the transmembrane domains of all cytokine receptors so far isolated. The role of this conserved motif in erythropoietin receptor was examined by assessing a series of mutant receptors on erythropoietin-induced signal transduction. Replacement of one of the two conserved Trp residues in the motif to Gly was found to completely abolish the binding of erythropoietin to the receptor and also to lose the ability to transduce the factor-dependent growth signal. While the mutants with one Ser residue converted to Gly or Ala retained full biological activities, the replacement of both conserved Ser residues diminished the functions of the receptor. Furthermore, the receptors lacking a part or all of the Trp-Ser-X-Trp-Ser motif did not respond to erythropoietin. The Trp-Ser-X-Trp-Ser motif, especially Trp residue, located in extracellular domains of the erythropoietin receptor thus appears to play a critical role in receptor-mediated signal transduction.lld:pubmed
pubmed-article:1314596pubmed:languageenglld:pubmed
pubmed-article:1314596pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1314596pubmed:citationSubsetIMlld:pubmed
pubmed-article:1314596pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1314596pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1314596pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1314596pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1314596pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1314596pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1314596pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:1314596pubmed:statusMEDLINElld:pubmed
pubmed-article:1314596pubmed:monthAprlld:pubmed
pubmed-article:1314596pubmed:issn0006-291Xlld:pubmed
pubmed-article:1314596pubmed:authorpubmed-author:AmanumaHHlld:pubmed
pubmed-article:1314596pubmed:authorpubmed-author:ChibaTTlld:pubmed
pubmed-article:1314596pubmed:authorpubmed-author:TodokoroKKlld:pubmed
pubmed-article:1314596pubmed:issnTypePrintlld:pubmed
pubmed-article:1314596pubmed:day15lld:pubmed
pubmed-article:1314596pubmed:volume184lld:pubmed
pubmed-article:1314596pubmed:ownerNLMlld:pubmed
pubmed-article:1314596pubmed:authorsCompleteYlld:pubmed
pubmed-article:1314596pubmed:pagination485-90lld:pubmed
pubmed-article:1314596pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:meshHeadingpubmed-meshheading:1314596-...lld:pubmed
pubmed-article:1314596pubmed:year1992lld:pubmed
pubmed-article:1314596pubmed:articleTitleTryptophan residue of Trp-Ser-X-Trp-Ser motif in extracellular domains of erythropoietin receptor is essential for signal transduction.lld:pubmed
pubmed-article:1314596pubmed:affiliationTsukuba Life Science Center, Institute of Physical and Chemical Research (RIKEN), Ibaraki, Japan.lld:pubmed
pubmed-article:1314596pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1314596pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:1314596lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:1314596lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:1314596lld:pubmed