| pubmed-article:19777057 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19777057 | lifeskim:mentions | umls-concept:C0087071 | lld:lifeskim |
| pubmed-article:19777057 | lifeskim:mentions | umls-concept:C0754515 | lld:lifeskim |
| pubmed-article:19777057 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:19777057 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:19777057 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:19777057 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:19777057 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:19777057 | pubmed:dateCreated | 2009-9-24 | lld:pubmed |
| pubmed-article:19777057 | pubmed:abstractText | Telomerase is a reverse transcriptase that maintains the telomeres of linear chromosomes and preserves genomic integrity. The core components are a catalytic protein subunit, the telomerase reverse transcriptase (TERT), and an RNA subunit, the telomerase RNA (TR). Telomerase is unique in its ability to catalyze processive DNA synthesis, which is facilitated by telomere-specific DNA-binding domains in TERT called anchor sites. A conserved glutamine residue in the TERT N-terminus is important for anchor site interactions in lower eukaryotes. The significance of this residue in higher eukaryotes, however, has not been investigated. | lld:pubmed |
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| pubmed-article:19777057 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19777057 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19777057 | pubmed:issn | 1932-6203 | lld:pubmed |
| pubmed-article:19777057 | pubmed:author | pubmed-author:BeattieTara... | lld:pubmed |
| pubmed-article:19777057 | pubmed:author | pubmed-author:WyattHaley... | lld:pubmed |
| pubmed-article:19777057 | pubmed:author | pubmed-author:LobbDeirdre... | lld:pubmed |
| pubmed-article:19777057 | pubmed:author | pubmed-author:TsangAllison... | lld:pubmed |
| pubmed-article:19777057 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19777057 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:19777057 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19777057 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19777057 | pubmed:pagination | e7176 | lld:pubmed |
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| pubmed-article:19777057 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19777057 | pubmed:articleTitle | Human telomerase reverse transcriptase (hTERT) Q169 is essential for telomerase function in vitro and in vivo. | lld:pubmed |
| pubmed-article:19777057 | pubmed:affiliation | Southern Alberta Cancer Research Institute and Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta, Canada. | lld:pubmed |
| pubmed-article:19777057 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19777057 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:19777057 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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