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Legube, ATM-dependent formation of a novel chromatin compartment regulates the Response to DNA Double Strand Breaks and the biogenesis of translocations, (2021) 2021.11.07.467654. https:\/\/doi.org\/10.1101\/2021.11.07.467654.","DOI":"10.1101\/2021.11.07.467654"},{"key":"10.1016\/j.dnarep.2023.103524_bib77","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1016\/j.cell.2015.09.057","article-title":"53BP1 and the LINC complex promote microtubule-dependent DSB mobility and DNA repair","volume":"163","author":"Lottersberger","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.dnarep.2023.103524_bib78","doi-asserted-by":"crossref","unstructured":"J. Huang, C. Wu, J.A. Kloeber, H. Gao, M. Gao, Q. Zhu, Y. Chang, F. Zhao, G. Guo, K. Luo, H. Dai, S. Liu, Q. Huang, W. Kim, Q. Zhou, S. Zhu, Z. Wu, X. Tu, P. Yin, M. Deng, L. Wang, J. Yuan, Z. Lou, SLFN5-mediated chromatin dynamics sculpt higher-order DNA repair topology, Mol Cell. (2023) S1097\u20132765(23)00083\u20137. https:\/\/doi.org\/10.1016\/j.molcel.2023.02.004.","DOI":"10.1016\/j.molcel.2023.02.004"},{"key":"10.1016\/j.dnarep.2023.103524_bib79","doi-asserted-by":"crossref","first-page":"2596","DOI":"10.1016\/j.molcel.2021.04.010","article-title":"AHNAK controls 53BP1-mediated p53 response by restraining 53BP1 oligomerization and phase separation","volume":"81","author":"Ghodke","year":"2021","journal-title":"Mol. Cell"},{"key":"10.1016\/j.dnarep.2023.103524_bib80","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1038\/s41467-022-28019-y","article-title":"53BP1 regulates heterochromatin through liquid phase separation","volume":"13","author":"Zhang","year":"2022","journal-title":"Nat. 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Cell Sci."},{"key":"10.1016\/j.dnarep.2023.103524_bib121","doi-asserted-by":"crossref","first-page":"15760","DOI":"10.1038\/ncomms15760","article-title":"Identification of the elementary structural units of the DNA damage response","volume":"8","author":"Natale","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.dnarep.2023.103524_bib122","doi-asserted-by":"crossref","DOI":"10.3389\/fgene.2021.784167","article-title":"Exploring the structures and functions of macromolecular SLX4-nuclease complexes in genome stability","volume":"12","author":"Payliss","year":"2021","journal-title":"Front Genet"},{"key":"10.1016\/j.dnarep.2023.103524_bib123","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1080\/10409238.2018.1488803","article-title":"SLX4: multitasking to maintain genome stability","volume":"53","author":"Guervilly","year":"2018","journal-title":"Crit. Rev. Biochem Mol. Biol."},{"key":"10.1016\/j.dnarep.2023.103524_bib124","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1038\/ng.750","article-title":"Mutations of the SLX4 gene in Fanconi anemia","volume":"43","author":"Kim","year":"2011","journal-title":"Nat. Genet."},{"key":"10.1016\/j.dnarep.2023.103524_bib125","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1038\/ng.751","article-title":"SLX4, a coordinator of structure-specific endonucleases, is mutated in a new Fanconi anemia subtype","volume":"43","author":"Stoepker","year":"2011","journal-title":"Nat. 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Struct. Mol. Biol."},{"key":"10.1016\/j.dnarep.2023.103524_bib137","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.molcel.2014.11.014","article-title":"The SLX4 complex is a SUMO E3 ligase that impacts on replication stress outcome and genome stability","volume":"57","author":"Guervilly","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.dnarep.2023.103524_bib138","doi-asserted-by":"crossref","first-page":"4871","DOI":"10.1093\/nar\/gkw354","article-title":"Dimerization of SLX4 contributes to functioning of the SLX4-nuclease complex","volume":"44","author":"Yin","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.dnarep.2023.103524_bib139","doi-asserted-by":"crossref","unstructured":"E. Alghoul, M. Paloni, A. Takedachi, S. Urbach, A. Barducci, P.-H. Gaillard, J. Basbous, A. 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