pubmed-article:19734539 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19734539 | lifeskim:mentions | umls-concept:C0005859 | lld:lifeskim |
pubmed-article:19734539 | lifeskim:mentions | umls-concept:C0920283 | lld:lifeskim |
pubmed-article:19734539 | lifeskim:mentions | umls-concept:C0558295 | lld:lifeskim |
pubmed-article:19734539 | lifeskim:mentions | umls-concept:C1538704 | lld:lifeskim |
pubmed-article:19734539 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
pubmed-article:19734539 | lifeskim:mentions | umls-concept:C0332297 | lld:lifeskim |
pubmed-article:19734539 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
pubmed-article:19734539 | lifeskim:mentions | umls-concept:C1548789 | lld:lifeskim |
pubmed-article:19734539 | lifeskim:mentions | umls-concept:C0081381 | lld:lifeskim |
pubmed-article:19734539 | pubmed:issue | 45 | lld:pubmed |
pubmed-article:19734539 | pubmed:dateCreated | 2009-11-2 | lld:pubmed |
pubmed-article:19734539 | pubmed:abstractText | 8-Oxo-2'-deoxyguanosine (8-oxodG) is one of the most important oxidative DNA lesions, and G-rich telomeric DNA is especially susceptible to oxidative DNA damage. RecQ helicases WRN and BLM and telomere-binding protein POT1 are thought to play roles in telomere maintenance. This study examines the ability of WRN, BLM, and RecQ5 to unwind and POT1 to bind telomeric D-loops containing 8-oxodG. The results demonstrate that WRN and BLM preferentially unwind telomeric D-loops containing 8-oxodG and that POT1 binds with higher affinity to telomeric D-loops with 8-oxodG but shows no preference for telomeric single-stranded DNA with 8-oxodG. We speculate that telomeric D-loops with 8-oxodG may have a greater tendency to form G-quadruplex DNA structures than telomeric DNA lacking 8-oxodG. | lld:pubmed |
pubmed-article:19734539 | pubmed:language | eng | lld:pubmed |
pubmed-article:19734539 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19734539 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19734539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19734539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19734539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19734539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19734539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19734539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19734539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19734539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19734539 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19734539 | pubmed:month | Nov | lld:pubmed |
pubmed-article:19734539 | pubmed:issn | 1083-351X | lld:pubmed |
pubmed-article:19734539 | pubmed:author | pubmed-author:BohrVilhelm... | lld:pubmed |
pubmed-article:19734539 | pubmed:author | pubmed-author:AuldsJasonJ | lld:pubmed |
pubmed-article:19734539 | pubmed:author | pubmed-author:GALLYJ AJA | lld:pubmed |
pubmed-article:19734539 | pubmed:author | pubmed-author:RossiMarie... | lld:pubmed |
pubmed-article:19734539 | pubmed:author | pubmed-author:CroteauDebora... | lld:pubmed |
pubmed-article:19734539 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19734539 | pubmed:day | 6 | lld:pubmed |
pubmed-article:19734539 | pubmed:volume | 284 | lld:pubmed |
pubmed-article:19734539 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19734539 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19734539 | pubmed:pagination | 31074-84 | lld:pubmed |
pubmed-article:19734539 | pubmed:dateRevised | 2010-11-9 | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:meshHeading | pubmed-meshheading:19734539... | lld:pubmed |
pubmed-article:19734539 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19734539 | pubmed:articleTitle | Telomeric D-loops containing 8-oxo-2'-deoxyguanosine are preferred substrates for Werner and Bloom syndrome helicases and are bound by POT1. | lld:pubmed |
pubmed-article:19734539 | pubmed:affiliation | Laboratory of Molecular Gerontology, NIA, National Institutes of Health, Baltimore, Maryland 21224, USA. | lld:pubmed |
pubmed-article:19734539 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19734539 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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