Linked Life Data

14617140

Source:http://linkedlifedata.com/resource/pubmed/id/14617140

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:14617140rdf:typepubmed:Citationlld:pubmed
pubmed-article:14617140lifeskim:mentionsumls-concept:C0026934lld:lifeskim
pubmed-article:14617140lifeskim:mentionsumls-concept:C0085501lld:lifeskim
pubmed-article:14617140lifeskim:mentionsumls-concept:C0040078lld:lifeskim
pubmed-article:14617140lifeskim:mentionsumls-concept:C1521991lld:lifeskim
pubmed-article:14617140lifeskim:mentionsumls-concept:C0018270lld:lifeskim
pubmed-article:14617140lifeskim:mentionsumls-concept:C0243077lld:lifeskim
pubmed-article:14617140lifeskim:mentionsumls-concept:C1880022lld:lifeskim
pubmed-article:14617140lifeskim:mentionsumls-concept:C1579410lld:lifeskim
pubmed-article:14617140pubmed:issue3lld:pubmed
pubmed-article:14617140pubmed:dateCreated2003-11-17lld:pubmed
pubmed-article:14617140pubmed:abstractTextUreaplasma urealyticum (U. urealyticum), belonging to the class Mollicutes, is a human pathogen colonizing the urogenital tract and causes among other things respiratory diseases in premature infants. We have studied the salvage of pyrimidine deoxynucleosides in U. urealyticum and cloned a key salvage enzyme, thymidine kinase (TK) from U. urealyticum. Recombinant Uu-TK was expressed in E. coli, purified and characterized with regards to substrate specificity and feedback inhibition. Uu-TK efficiently phosphorylated thymidine (dThd) and deoxyuridine (dUrd) as well as a number of pyrimidine nucleoside analogues. All natural ribonucleoside/deoxyribonucleoside triphosphates, except dTTP, served as phosphate donors, while dTTP was a feedback inhibitor. The level of Uu-TK activity in U. urealyticum extracts increased upon addition of dUrd to the growth medium. Fluoropyrimidine nucleosides inhibited U. urealyticum and M. pneumoniae growth and this inhibitory effect could be reversed by addition of dThd, dUrd or deoxytetrahydrouridine to the growth medium. Thus, the mechanism of inhibition was most likely the depletion of dTTP, either via a blocked thymidine kinase reaction and/or thymidylate synthesis step and these metabolic reactions should be suitable targets for antimycoplasma chemotherapy.lld:pubmed
pubmed-article:14617140pubmed:languageenglld:pubmed
pubmed-article:14617140pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:citationSubsetIMlld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14617140pubmed:statusMEDLINElld:pubmed
pubmed-article:14617140pubmed:monthNovlld:pubmed
pubmed-article:14617140pubmed:issn0950-382Xlld:pubmed
pubmed-article:14617140pubmed:authorpubmed-author:BölskeGöranGlld:pubmed
pubmed-article:14617140pubmed:authorpubmed-author:ErikssonStaff...lld:pubmed
pubmed-article:14617140pubmed:authorpubmed-author:WangLiyaLlld:pubmed
pubmed-article:14617140pubmed:authorpubmed-author:CarnrotCecili...lld:pubmed
pubmed-article:14617140pubmed:authorpubmed-author:WehelieRahmaRlld:pubmed
pubmed-article:14617140pubmed:issnTypePrintlld:pubmed
pubmed-article:14617140pubmed:volume50lld:pubmed
pubmed-article:14617140pubmed:ownerNLMlld:pubmed
pubmed-article:14617140pubmed:authorsCompleteYlld:pubmed
pubmed-article:14617140pubmed:pagination771-80lld:pubmed
pubmed-article:14617140pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:meshHeadingpubmed-meshheading:14617140...lld:pubmed
pubmed-article:14617140pubmed:year2003lld:pubmed
pubmed-article:14617140pubmed:articleTitleMolecular characterization of thymidine kinase from Ureaplasma urealyticum: nucleoside analogues as potent inhibitors of mycoplasma growth.lld:pubmed
pubmed-article:14617140pubmed:affiliationDepartment of Molecular Biosciences, The Swedish University of Agricultural Sciences, The Biomedical Centre, PO Box 575, SE-751 23 Uppsala, Sweden.lld:pubmed
pubmed-article:14617140pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:14617140pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14617140lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14617140lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14617140lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14617140lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14617140lld:pubmed