| pubmed-article:17825467 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17825467 | lifeskim:mentions | umls-concept:C0085187 | lld:lifeskim |
| pubmed-article:17825467 | lifeskim:mentions | umls-concept:C0230739 | lld:lifeskim |
| pubmed-article:17825467 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:17825467 | lifeskim:mentions | umls-concept:C0963182 | lld:lifeskim |
| pubmed-article:17825467 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17825467 | pubmed:dateCreated | 2007-12-11 | lld:pubmed |
| pubmed-article:17825467 | pubmed:abstractText | Telomeres have special needs; they require distinct mechanisms for their protection, replication, and separation at mitosis. A dedicated six-subunit protein complex termed shelterin attends to these needs. But shelterin cannot do it alone and often relies on recruits from other cellular locales. One such recruit is tankyrase 1, a poly(ADP-ribose) polymerase that is brought to telomeres by the shelterin DNA binding subunit TRF1, where it functions in telomere length regulation and sister chromatid separation. An understanding of how tankyrase 1 functions at telomeres has been confounded by its complexity; it localizes to multiple subcellular sites, it has many diverse binding partners, and it has a closely related homolog (tankyrase 2) with which it may functionally overlap. This review summarizes our current knowledge of tankyrases focusing on their localization, binding partners, and function. | lld:pubmed |
| pubmed-article:17825467 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17825467 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17825467 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17825467 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17825467 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17825467 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17825467 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17825467 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17825467 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:17825467 | pubmed:issn | 0300-9084 | lld:pubmed |
| pubmed-article:17825467 | pubmed:author | pubmed-author:SmithSusanS | lld:pubmed |
| pubmed-article:17825467 | pubmed:author | pubmed-author:HsiaoSusan... | lld:pubmed |
| pubmed-article:17825467 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17825467 | pubmed:volume | 90 | lld:pubmed |
| pubmed-article:17825467 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17825467 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17825467 | pubmed:pagination | 83-92 | lld:pubmed |
| pubmed-article:17825467 | pubmed:meshHeading | pubmed-meshheading:17825467... | lld:pubmed |
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| pubmed-article:17825467 | pubmed:meshHeading | pubmed-meshheading:17825467... | lld:pubmed |
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| pubmed-article:17825467 | pubmed:meshHeading | pubmed-meshheading:17825467... | lld:pubmed |
| pubmed-article:17825467 | pubmed:meshHeading | pubmed-meshheading:17825467... | lld:pubmed |
| pubmed-article:17825467 | pubmed:meshHeading | pubmed-meshheading:17825467... | lld:pubmed |
| pubmed-article:17825467 | pubmed:meshHeading | pubmed-meshheading:17825467... | lld:pubmed |
| pubmed-article:17825467 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:17825467 | pubmed:articleTitle | Tankyrase function at telomeres, spindle poles, and beyond. | lld:pubmed |
| pubmed-article:17825467 | pubmed:affiliation | Skirball Institute of Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, 2nd Floor, New York, NY 10016, United States. | lld:pubmed |
| pubmed-article:17825467 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17825467 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:17825467 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17825467 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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