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dc.contributor.authorSiwanon Jirawatnotaien_US
dc.contributor.authorYiduo Huen_US
dc.contributor.authorWojciech Michowskien_US
dc.contributor.authorJoshua E. Eliasen_US
dc.contributor.authorLisa Becksen_US
dc.contributor.authorFrederic Bienvenuen_US
dc.contributor.authorAgnieszka Zagozdzonen_US
dc.contributor.authorTapasree Goswamien_US
dc.contributor.authorYaoyu E. Wangen_US
dc.contributor.authorAlan B. Clarken_US
dc.contributor.authorThomas A. Kunkelen_US
dc.contributor.authorTanja Van Harnen_US
dc.contributor.authorBing Xiaen_US
dc.contributor.authorMick Correllen_US
dc.contributor.authorJohn Quackenbushen_US
dc.contributor.authorDavid M. Livingstonen_US
dc.contributor.authorSteven P. Gygien_US
dc.contributor.authorPiotr Sicinskien_US
dc.contributor.otherHarvard Medical Schoolen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherMassachusetts College of Pharmacy and Health Sciencesen_US
dc.contributor.otherDana-Farber Cancer Instituteen_US
dc.contributor.otherNational Institutes of Health, Bethesdaen_US
dc.contributor.otherRutgers Robert Wood Johnson Medical School at New Brunswicken_US
dc.contributor.otherHarvard School of Public Healthen_US
dc.contributor.otherStanford University School of Medicineen_US
dc.contributor.otherUniversite de Montpellieren_US
dc.date.accessioned2018-05-03T08:46:53Z-
dc.date.available2018-05-03T08:46:53Z-
dc.date.issued2011-06-08en_US
dc.identifier.citationNature. Vol.474, No.7350 (2011), 230-234en_US
dc.identifier.issn14764687en_US
dc.identifier.issn00280836en_US
dc.identifier.other2-s2.0-79958254560en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79958254560&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/12918-
dc.description.abstractCyclin D1 is a component of the core cell cycle machinery 1 . Abnormally high levels of cyclin D1 are detected in many human cancer types 2 . To elucidate the molecular functions of cyclin D1 in human cancers, we performed a proteomic screen for cyclin D1 protein partners in several types of human tumours. Analyses of cyclin D1 interactors revealed a network of DNA repair proteins, including RAD51, a recombinase that drives the homologous recombination process. We found that cyclin D1 directly binds RAD51, and that cyclin D1-RAD51 interaction is induced by radiation. Like RAD51, cyclin D1 is recruited to DNA damage sites in a BRCA2-dependent fashion. Reduction of cyclin D1 levels in human cancer cells impaired recruitment of RAD51 to damaged DNA, impeded the homologous recombination-mediated DNA repair, and increased sensitivity of cells to radiation in vitro and in vivo. This effect was seen in cancer cells lacking the retinoblastoma protein, which do not require D-cyclins for proliferation. These findings reveal an unexpected function of a core cell cycle protein in DNA repair and suggest that targeting cyclin D1 may be beneficial also in retinoblastoma-negative cancers which are currently thought to be unaffected by cyclin D1 inhibition. © 2011 Macmillan Publishers Limited. All rights reserved.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79958254560&origin=inwarden_US
dc.subjectMultidisciplinaryen_US
dc.titleA function for cyclin D1 in DNA repair uncovered by protein interactome analyses in human cancersen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1038/nature10155en_US
Appears in Collections:Scopus 2011-2015

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