Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:8550294rdf:typepubmed:Citationlld:pubmed
pubmed-article:8550294lifeskim:mentionsumls-concept:C0935640lld:lifeskim
pubmed-article:8550294lifeskim:mentionsumls-concept:C0025252lld:lifeskim
pubmed-article:8550294lifeskim:mentionsumls-concept:C0017262lld:lifeskim
pubmed-article:8550294lifeskim:mentionsumls-concept:C2911684lld:lifeskim
pubmed-article:8550294lifeskim:mentionsumls-concept:C0320843lld:lifeskim
pubmed-article:8550294lifeskim:mentionsumls-concept:C0185117lld:lifeskim
pubmed-article:8550294pubmed:issue8lld:pubmed
pubmed-article:8550294pubmed:dateCreated1996-2-21lld:pubmed
pubmed-article:8550294pubmed:abstractTextPrevious studies detected a single amino acid substitution (Ala196 to Gly196) between cDNA clones encoding a 32 kDa antigen (p32) of Theileria sergenti (Chitose stock) obtained from a persistently infected calf. In this study, 2 different recombinant baculoviruses (pAc/p32-Ala196 and pAc/p32-Gly196) were constructed for the expression of p32. Molecular masses of the polypeptides produced in Spodoptera frugiperda cells infected with the recombinant baculoviruses were the same as that of authentic p32. pAc/p32-Ala196 produced additional polypeptides, with molecular masses higher than 32 kDa, which resulted from differential N-glycosylation as revealed by endo N-glycosidase treatment. The results indicate that a single amino acid substitution may lead to a conformational change in p32 which affected post-translational modification of recombinant products.lld:pubmed
pubmed-article:8550294pubmed:languageenglld:pubmed
pubmed-article:8550294pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8550294pubmed:citationSubsetIMlld:pubmed
pubmed-article:8550294pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8550294pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8550294pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8550294pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8550294pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8550294pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8550294pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8550294pubmed:statusMEDLINElld:pubmed
pubmed-article:8550294pubmed:monthAuglld:pubmed
pubmed-article:8550294pubmed:issn0020-7519lld:pubmed
pubmed-article:8550294pubmed:authorpubmed-author:HattoriMMlld:pubmed
pubmed-article:8550294pubmed:authorpubmed-author:SakoYYlld:pubmed
pubmed-article:8550294pubmed:authorpubmed-author:OnumaMMlld:pubmed
pubmed-article:8550294pubmed:authorpubmed-author:FujisakiKKlld:pubmed
pubmed-article:8550294pubmed:authorpubmed-author:SugimotoCClld:pubmed
pubmed-article:8550294pubmed:authorpubmed-author:MatsubaTTlld:pubmed
pubmed-article:8550294pubmed:issnTypePrintlld:pubmed
pubmed-article:8550294pubmed:volume25lld:pubmed
pubmed-article:8550294pubmed:ownerNLMlld:pubmed
pubmed-article:8550294pubmed:authorsCompleteYlld:pubmed
pubmed-article:8550294pubmed:pagination939-43lld:pubmed
pubmed-article:8550294pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:meshHeadingpubmed-meshheading:8550294-...lld:pubmed
pubmed-article:8550294pubmed:year1995lld:pubmed
pubmed-article:8550294pubmed:articleTitleExpression of a 32 kilodalton Theileria sergenti piroplasm surface protein by recombinant baculoviruses.lld:pubmed
pubmed-article:8550294pubmed:affiliationDepartment of Disease Control, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.lld:pubmed
pubmed-article:8550294pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8550294pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8550294lld:pubmed