| pubmed-article:18648921 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18648921 | lifeskim:mentions | umls-concept:C0004651 | lld:lifeskim |
| pubmed-article:18648921 | lifeskim:mentions | umls-concept:C1917885 | lld:lifeskim |
| pubmed-article:18648921 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:18648921 | lifeskim:mentions | umls-concept:C0040085 | lld:lifeskim |
| pubmed-article:18648921 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:18648921 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:18648921 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:18648921 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18648921 | pubmed:dateCreated | 2008-8-15 | lld:pubmed |
| pubmed-article:18648921 | pubmed:abstractText | Thymidylate synthase (TS) is essential for de novo synthesis of dTMP and is a key enzyme involved in DNA synthesis and transcriptional regulation of organisms. Due to their biologic importance, TSs have been intensively studied. In this investigation, a thermostable TS was identified from a deep-sea thermophilic bacteriophage Geobacillus virus E2 (GVE2). It was demonstrated that GVE2-TS was highly homologous to known TSs and contained five characteristic conserved domains. The temporal analyses by Northern and Western blots revealed that the GVE2-TS was transcribed and expressed early after Geobacillus virus E2 infection, identifying it as a viral early gene. As shown by gel mobility shift assays, the recombinant GVE2-TS protein had the capacity to bind its own mRNA. Our study presented the first report on thymidylate synthase from deep-sea thermophilic bacteriophage. | lld:pubmed |
| pubmed-article:18648921 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18648921 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18648921 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18648921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18648921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18648921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18648921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18648921 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18648921 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:18648921 | pubmed:issn | 0920-8569 | lld:pubmed |
| pubmed-article:18648921 | pubmed:author | pubmed-author:ZhangXiaoboX | lld:pubmed |
| pubmed-article:18648921 | pubmed:author | pubmed-author:WangYiqianY | lld:pubmed |
| pubmed-article:18648921 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18648921 | pubmed:volume | 37 | lld:pubmed |
| pubmed-article:18648921 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18648921 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18648921 | pubmed:pagination | 218-24 | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:meshHeading | pubmed-meshheading:18648921... | lld:pubmed |
| pubmed-article:18648921 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18648921 | pubmed:articleTitle | Identification and characterization of a novel thymidylate synthase from deep-sea thermophilic bacteriophage Geobacillus virus E2. | lld:pubmed |
| pubmed-article:18648921 | pubmed:affiliation | School of Life Sciences, Xiamen University, Xiamen, 361005, People's Republic of China. | lld:pubmed |
| pubmed-article:18648921 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18648921 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5247241 | entrezgene:pubmed | pubmed-article:18648921 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18648921 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18648921 | lld:pubmed |
