| pubmed-article:12181449 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12181449 | lifeskim:mentions | umls-concept:C0019381 | lld:lifeskim |
| pubmed-article:12181449 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:12181449 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:12181449 | lifeskim:mentions | umls-concept:C0017066 | lld:lifeskim |
| pubmed-article:12181449 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:12181449 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:12181449 | pubmed:dateCreated | 2002-8-15 | lld:pubmed |
| pubmed-article:12181449 | pubmed:abstractText | The human herpesvirus 6 (HHV-6) U69 gene product (pU69) is the presumed functional homolog of the human cytomegalovirus (HCMV) UL97-encoded kinase (pUL97), which converts ganciclovir to its monophosphate metabolite in HCMV-infected cells. It has been reported that insertion of U69 into baculovirus confers sensitivity to ganciclovir in insect cells (J Virol 73:3284-3291, 1999). Our metabolic studies in HHV-6-infected human T-lymphoblast cells indicated that the efficiency of ganciclovir phosphorylation induced by HHV-6 was relatively poor. Recombinant vaccinia viruses (rVVs), expressing high levels of pU69 from two HHV-6 strains (representing the A and B variant), were constructed and used to compare the ganciclovir-phosphorylating capacity of pU69 and pUL97 in human cells. Metabolic studies with [8-(3)H]ganciclovir showed that ganciclovir was phosphorylated in human cells infected with pU69-expressing rVVs, although the levels of phosphorylated ganciclovir metabolites were approximately 10-fold lower than those observed with pUL97. We also demonstrated that pU69, like pUL97, is expressed as a nuclear protein. Our results indicate that the limited phosphorylation of ganciclovir by pU69 may contribute to its modest antiviral activity against HHV-6 in certain cell systems. | lld:pubmed |
| pubmed-article:12181449 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12181449 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12181449 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12181449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12181449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12181449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12181449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12181449 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12181449 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12181449 | pubmed:issn | 0026-895X | lld:pubmed |
| pubmed-article:12181449 | pubmed:author | pubmed-author:IncasJ SJS | lld:pubmed |
| pubmed-article:12181449 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:12181449 | pubmed:author | pubmed-author:ManichanhChay... | lld:pubmed |
| pubmed-article:12181449 | pubmed:author | pubmed-author:MichelDetlefD | lld:pubmed |
| pubmed-article:12181449 | pubmed:author | pubmed-author:MertensThomas... | lld:pubmed |
| pubmed-article:12181449 | pubmed:author | pubmed-author:NaesensLieveL | lld:pubmed |
| pubmed-article:12181449 | pubmed:author | pubmed-author:De BolleLeenL | lld:pubmed |
| pubmed-article:12181449 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12181449 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:12181449 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12181449 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12181449 | pubmed:pagination | 714-21 | lld:pubmed |
| pubmed-article:12181449 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:12181449 | pubmed:meshHeading | pubmed-meshheading:12181449... | lld:pubmed |
| pubmed-article:12181449 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12181449 | pubmed:articleTitle | Role of the human herpesvirus 6 u69-encoded kinase in the phosphorylation of ganciclovir. | lld:pubmed |
| pubmed-article:12181449 | pubmed:affiliation | Rega Institute for Medical Research, Katholieke Universiteit Leuven, Leuven, Belgium. | lld:pubmed |
| pubmed-article:12181449 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12181449 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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