Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:14565460rdf:typepubmed:Citationlld:pubmed
pubmed-article:14565460lifeskim:mentionsumls-concept:C0086418lld:lifeskim
pubmed-article:14565460lifeskim:mentionsumls-concept:C0010723lld:lifeskim
pubmed-article:14565460lifeskim:mentionsumls-concept:C1704675lld:lifeskim
pubmed-article:14565460pubmed:issue5-8lld:pubmed
pubmed-article:14565460pubmed:dateCreated2003-10-20lld:pubmed
pubmed-article:14565460pubmed:abstractTextIn order to design new efficient cytidine based drugs, an intersubunit interactions study related to the active site has been performed on the wild-type cytidine deaminase (CDA) and on the mutant enzyme F137W/W113F. F137 is the homologous to the Bacillus subtilis CDA F125 involved in the subunit interactions. In presence of the dissociating agent SDS, wild-type human CDA dissociate into enzymatically inactive monomers without intermediate forms via a non-cooperative transition. Extensive dialysis or dilution of the inactivated monomers restores completely the activity. The presence of the strong human CDA competitive inhibitor 5-fluorozebularine disfavour dissociation of the tetramer into subunits in the wild-type CDA but not in mutant enzyme F137W/W113F.lld:pubmed
pubmed-article:14565460pubmed:languageenglld:pubmed
pubmed-article:14565460pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14565460pubmed:citationSubsetIMlld:pubmed
pubmed-article:14565460pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14565460pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14565460pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14565460pubmed:statusMEDLINElld:pubmed
pubmed-article:14565460pubmed:issn1525-7770lld:pubmed
pubmed-article:14565460pubmed:authorpubmed-author:VitiIIlld:pubmed
pubmed-article:14565460pubmed:authorpubmed-author:MarianiPPlld:pubmed
pubmed-article:14565460pubmed:authorpubmed-author:CristalliGGlld:pubmed
pubmed-article:14565460pubmed:authorpubmed-author:CostanziSSlld:pubmed
pubmed-article:14565460pubmed:authorpubmed-author:VincenzettiSSlld:pubmed
pubmed-article:14565460pubmed:authorpubmed-author:QuadriniBBlld:pubmed
pubmed-article:14565460pubmed:authorpubmed-author:CammertoniNNlld:pubmed
pubmed-article:14565460pubmed:issnTypePrintlld:pubmed
pubmed-article:14565460pubmed:volume22lld:pubmed
pubmed-article:14565460pubmed:ownerNLMlld:pubmed
pubmed-article:14565460pubmed:authorsCompleteYlld:pubmed
pubmed-article:14565460pubmed:pagination1535-8lld:pubmed
pubmed-article:14565460pubmed:dateRevised2004-11-17lld:pubmed
pubmed-article:14565460pubmed:meshHeadingpubmed-meshheading:14565460...lld:pubmed
pubmed-article:14565460pubmed:meshHeadingpubmed-meshheading:14565460...lld:pubmed
pubmed-article:14565460pubmed:meshHeadingpubmed-meshheading:14565460...lld:pubmed
pubmed-article:14565460pubmed:meshHeadingpubmed-meshheading:14565460...lld:pubmed
pubmed-article:14565460pubmed:meshHeadingpubmed-meshheading:14565460...lld:pubmed
pubmed-article:14565460pubmed:meshHeadingpubmed-meshheading:14565460...lld:pubmed
pubmed-article:14565460pubmed:meshHeadingpubmed-meshheading:14565460...lld:pubmed
pubmed-article:14565460pubmed:meshHeadingpubmed-meshheading:14565460...lld:pubmed
pubmed-article:14565460pubmed:meshHeadingpubmed-meshheading:14565460...lld:pubmed
pubmed-article:14565460pubmed:articleTitleIntersubunit interactions in human cytidine deaminase.lld:pubmed
pubmed-article:14565460pubmed:affiliationDipartimento di Scienze Veterinarie, University of Camerino, Matelica (MC), Italy.lld:pubmed
pubmed-article:14565460pubmed:publicationTypeJournal Articlelld:pubmed
entrez-gene:978entrezgene:pubmedpubmed-article:14565460lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:14565460lld:entrezgene