| pubmed-article:19245831 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19245831 | lifeskim:mentions | umls-concept:C0008633 | lld:lifeskim |
| pubmed-article:19245831 | lifeskim:mentions | umls-concept:C0085187 | lld:lifeskim |
| pubmed-article:19245831 | lifeskim:mentions | umls-concept:C0920283 | lld:lifeskim |
| pubmed-article:19245831 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:19245831 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:19245831 | pubmed:dateCreated | 2009-5-11 | lld:pubmed |
| pubmed-article:19245831 | pubmed:abstractText | Telomeres play critical roles in protecting genome stability, and their dysfunction contributes to cancer and age-related degenerative diseases. The precise architecture of telomeres, including their single-stranded 3' overhangs, bound proteins, and ability to form unusual secondary structures such as t-loops, is central to their function and thus requires careful processing by diverse factors. Furthermore, telomeres provide unique challenges to the DNA replication and recombination machinery, and are particularly suited for extension by the telomerase reverse transcriptase. Helicases use the energy from NTP hydrolysis to track along DNA and disrupt base pairing. Here we review current findings concerning how helicases modulate several aspects of telomere form and function. | lld:pubmed |
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