| pubmed-article:17596542 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17596542 | lifeskim:mentions | umls-concept:C0012860 | lld:lifeskim |
| pubmed-article:17596542 | lifeskim:mentions | umls-concept:C0165675 | lld:lifeskim |
| pubmed-article:17596542 | lifeskim:mentions | umls-concept:C0920283 | lld:lifeskim |
| pubmed-article:17596542 | lifeskim:mentions | umls-concept:C1412729 | lld:lifeskim |
| pubmed-article:17596542 | lifeskim:mentions | umls-concept:C1426958 | lld:lifeskim |
| pubmed-article:17596542 | lifeskim:mentions | umls-concept:C0205234 | lld:lifeskim |
| pubmed-article:17596542 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:17596542 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:17596542 | lifeskim:mentions | umls-concept:C0037183 | lld:lifeskim |
| pubmed-article:17596542 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:17596542 | pubmed:dateCreated | 2007-9-20 | lld:pubmed |
| pubmed-article:17596542 | pubmed:abstractText | The BRCA1 associated C-terminal helicase (BACH1, designated FANCJ) is implicated in the chromosomal instability genetic disorder Fanconi anemia (FA) and hereditary breast cancer. A critical role of FANCJ helicase may be to restart replication as a component of downstream events that occur during the repair of DNA cross-links or double-strand breaks. We investigated the potential interaction of FANCJ with replication protein A (RPA), a single-stranded DNA-binding protein implicated in both DNA replication and repair. FANCJ and RPA were shown to coimmunoprecipitate most likely through a direct interaction of FANCJ and the RPA70 subunit. Moreover, dependent on the presence of BRCA1, FANCJ colocalizes with RPA in nuclear foci after DNA damage. Our data are consistent with a model in which FANCJ associates with RPA in a DNA damage-inducible manner and through the protein interaction RPA stimulates FANCJ helicase to better unwind duplex DNA substrates. These findings identify RPA as the first regulatory partner of FANCJ. The FANCJ-RPA interaction is likely to be important for the role of the helicase to more efficiently unwind DNA repair intermediates to maintain genomic stability. | lld:pubmed |
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| pubmed-article:17596542 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17596542 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17596542 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:17596542 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17596542 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17596542 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:17596542 | pubmed:author | pubmed-author:BroshRobert... | lld:pubmed |
| pubmed-article:17596542 | pubmed:author | pubmed-author:CantorSharon... | lld:pubmed |
| pubmed-article:17596542 | pubmed:author | pubmed-author:SommersJoshua... | lld:pubmed |
| pubmed-article:17596542 | pubmed:author | pubmed-author:KennyMark KMK | lld:pubmed |
| pubmed-article:17596542 | pubmed:author | pubmed-author:SharmaSudhaS | lld:pubmed |
| pubmed-article:17596542 | pubmed:author | pubmed-author:GuptaRiguR | lld:pubmed |
| pubmed-article:17596542 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17596542 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17596542 | pubmed:volume | 110 | lld:pubmed |
| pubmed-article:17596542 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17596542 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17596542 | pubmed:pagination | 2390-8 | lld:pubmed |
| pubmed-article:17596542 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:meshHeading | pubmed-meshheading:17596542... | lld:pubmed |
| pubmed-article:17596542 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17596542 | pubmed:articleTitle | FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein. | lld:pubmed |
| pubmed-article:17596542 | pubmed:affiliation | Laboratory of Molecular Gerontology, National Institute on Aging (NIA), National Institutes of Health (NIH), Baltimore, MD 21224, USA. | lld:pubmed |
| pubmed-article:17596542 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17596542 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
