Molecular Analysis of BRCA1 in Human Breast Cancer Cells Under Oxidative Stress

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dc.contributor.authorGilmore, Brian L.en
dc.contributor.authorLiang, Yanpingen
dc.contributor.authorWinton, Carly E.en
dc.contributor.authorPatel, Kayaen
dc.contributor.authorKarageorge, Vasileaen
dc.contributor.authorVarano, A. Cameronen
dc.contributor.authorDearnaley, William J.en
dc.contributor.authorSheng, Zhien
dc.contributor.authorKelly, Deborah F.en
dc.contributor.departmentBiological Sciencesen
dc.contributor.departmentFralin Biomedical Research Instituteen
dc.contributor.departmentFralin Life Sciences Instituteen
dc.contributor.departmentBiomedical Engineering and Sciencesen
dc.date.accessioned2018-02-08T17:56:28Zen
dc.date.available2018-02-08T17:56:28Zen
dc.date.issued2017-03-06en
dc.description.abstractThe precise manner in which physical changes to the breast cancer susceptibility protein (BRCA1) affect its role in DNA repair events remain unclear. Indeed, cancer cells harboring mutations in BRCA1 suffer from genomic instability and increased DNA lesions. Here, we used a combination of molecular imaging and biochemical tools to study the properties of the BRCA1 in human cancer cells. Our results reveal new information for the manner in which full-length BRCA1 engages its binding partner, the BRCA1-associated Ring Domain protein (BARD1) under oxidative stress conditions. We also show how physical differences between wild type and mutated BRCA15382insC impact the cell’s response to oxidative damage. Overall, we demonstrate how clinically relevant changes to BRCA1 affect its structure-function relationship in hereditary breast cancer.en
dc.description.versionPublished versionen
dc.format.extent1 - 9 (9) page(s)en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1038/srep43435en
dc.identifier.issn2045-2322en
dc.identifier.orcidSheng, Z [0000-0002-0029-8666]en
dc.identifier.urihttp://hdl.handle.net/10919/82044en
dc.identifier.volume7en
dc.language.isoenen
dc.publisherNature Publishing Groupen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000395395000001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectovarian-canceren
dc.subjectdna-damageen
dc.subjectpolyubiquitin chainsen
dc.subjectubiquitin-ligaseen
dc.subjectmutationsen
dc.subjectexpressionen
dc.subjectpathwayen
dc.subjectcomplexen
dc.subjectbindingen
dc.subjectrepairen
dc.titleMolecular Analysis of BRCA1 in Human Breast Cancer Cells Under Oxidative Stressen
dc.title.serialScientific Reportsen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherArticle - Refereeden
dc.type.otherJournalen
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/University Research Institutesen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciencesen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciences/Fralin Affiliated Facultyen
pubs.organisational-group/Virginia Tech/University Research Institutes/Virginia Tech Carilion Research Instituteen

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