{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRAD52 is an evolutionarily conserved protein that plays a central role in homologous recombination. Structural and biochemical studies have revealed that its N‐terminal domain self‐assembles into ring‐shaped oligomers (in human, an undecameric ring), which form the core of its single‑strand annealing and strand exchange activities. Detailed crystallographic and mutagenesis analyses have mapped key residues critical for binding both single‑ and double‑stranded DNA, while single‑molecule experiments have illuminated its dynamic interactions with ssDNA, thereby supporting its function in aligning homologous sequences and catalyzing D‑loop formation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the realm of DNA repair, RAD52 serves as an essential backup mediator in homologous recombination, particularly when the canonical BRCA1/BRCA2–RAD51 pathway is compromised. Loss of RAD52 function in BRCA‑deficient cells leads to a substantial decrease in both spontaneous and induced homologous recombination, resulting in chromosomal instability and synthetic lethality. Moreover, targeted disruption of critical residues in its DNA binding domain further validates its indispensable role in alternative repair pathways and underscores its potential as a therapeutic target in cancers with defective BRCA/PALB2 function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical role in homologous recombination, RAD52 is pivotal in managing replication stress and maintaining telomere integrity. It facilitates mitotic DNA synthesis at common fragile sites by coordinating the timely recruitment of nucleases and polymerases, thereby promoting replication restart. In the context of alternative lengthening of telomeres (ALT), RAD52 supports telomere clustering and break‑induced replication, and it also catalyzes an “inverse strand exchange” with RNA templates—a function that broadens its capacity to repair complex lesions. Interactions with chromatin remodelers and factors like p53 further underscore its role in orchestrating the exchange of replication protein A (RPA) with RAD51 at stalled forks, while partners such as PTEN modulate its post‑translational modifications in response to genotoxic stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMechanistically, RAD52 mediates the annealing of complementary single‑stranded DNA regions and is crucial for key steps in double‑strand break repair such as second‑end capture. Its interaction with other repair factors—including the XPF/ERCC1 endonuclease complex, replication protein A, and glycosylases like OGG1—fine‐tunes its strand pairing and exchange functions. Such cooperativity ensures that recombination intermediates are processed correctly and contributes to the balance between diverse homologous recombination outcomes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinically, the regulation of RAD52 has emerged as a double‑edged sword. Modulation of its expression and activity can significantly influence gene targeting efficiency and cellular responses to DNA damage. For example, while its overexpression may suppress precise homologous recombination events and gene targeting, RAD52 depletion in tumors harboring BRCA mutations enhances sensitivity to DNA‑damaging agents—a vulnerability that can be exploited therapeutically. In addition, polymorphisms affecting RAD52 expression or its interaction with regulatory microRNAs have been linked to altered risks and prognoses in breast, thyroid, and colorectal cancers, and transient co‑expression strategies have been shown to improve CRISPR/Cas9‑mediated genome editing outcomes. Collectively, these observations highlight the promise of RAD52 as both a biomarker and a target in precision medicine."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Wataru Kagawa, Hitoshi Kurumizaka, Ryuichiro Ishitani, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s1097-2765(02)00587-7"}], "href": "https://doi.org/10.1016/s1097-2765(02"}, {"type": "t", "text": "00587-7) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12191481"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12191481"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Martin R Singleton, Lois M Wentzell, Yilun Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure of the single-strand annealing domain of human RAD52 protein."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.212449899"}], "href": "https://doi.org/10.1073/pnas.212449899"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12370410"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12370410"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Baoyuan Bi, Nataliya Rybalchenko, Efim I Golub, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human and yeast Rad52 proteins promote DNA strand exchange."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0403205101"}], "href": "https://doi.org/10.1073/pnas.0403205101"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15205482"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15205482"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Janice A Lloyd, Dharia A McGrew, Kendall L Knight "}, {"type": "b", "children": [{"type": "t", "text": "Identification of residues important for DNA binding in the full-length human Rad52 protein."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2004.10.065"}], "href": "https://doi.org/10.1016/j.jmb.2004.10.065"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15571718"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15571718"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Eli Rothenberg, Jill M Grimme, Maria Spies, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human Rad52-mediated homology search and annealing occurs by continuous interactions between overlapping nucleoprotein complexes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0810317106"}], "href": "https://doi.org/10.1073/pnas.0810317106"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19074292"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19074292"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Masayoshi Honda, Yusuke Okuno, Jungmin Yoo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tyrosine phosphorylation enhances RAD52-mediated annealing by modulating its DNA binding."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/emboj.2011.238"}], "href": "https://doi.org/10.1038/emboj.2011.238"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21804533"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21804533"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Chu Jian Ma, Youngho Kwon, Patrick Sung, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human RAD52 interactions with replication protein A and the RAD51 presynaptic complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M117.794545"}], "href": "https://doi.org/10.1074/jbc.M117.794545"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28551686"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28551686"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Zhihui Feng, Shaun P Scott, Wendy Bussen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rad52 inactivation is synthetically lethal with BRCA2 deficiency."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1010959107"}], "href": "https://doi.org/10.1073/pnas.1010959107"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21148102"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21148102"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "B H Lok, A C Carley, B Tchang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RAD52 inactivation is synthetically lethal with deficiencies in BRCA1 and PALB2 in addition to BRCA2 through RAD51-mediated homologous recombination."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2012.391"}], "href": "https://doi.org/10.1038/onc.2012.391"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22964643"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22964643"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Kimberly Cramer-Morales, Margaret Nieborowska-Skorska, Kara Scheibner, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Personalized synthetic lethality induced by targeting RAD52 in leukemias identified by gene mutation and expression profile."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2013-05-501072"}], "href": "https://doi.org/10.1182/blood-2013-05-501072"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23836560"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23836560"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Sunetra Roy, Karl-Heinz Tomaszowski, Jessica W Luzwick, et al. "}, {"type": "b", "children": [{"type": "t", "text": "p53 orchestrates DNA replication restart homeostasis by suppressing mutagenic RAD52 and POLθ pathways."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Elife (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7554/eLife.31723"}], "href": "https://doi.org/10.7554/eLife.31723"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29334356"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29334356"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Andrew A Kelso, Felicia Wednesday Lopezcolorado, Ragini Bhargava, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Distinct roles of RAD52 and POLQ in chromosomal break repair and replication stress response."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Genet (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pgen.1008319"}], "href": "https://doi.org/10.1371/journal.pgen.1008319"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31381562"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31381562"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Tohru Matsuki, Albéna Pramatarova, Brian W Howell "}, {"type": "b", "children": [{"type": "t", "text": "Reduction of Crk and CrkL expression blocks reelin-induced dendritogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.027334"}], "href": "https://doi.org/10.1242/jcs.027334"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18477607"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18477607"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Byeong Hyeok Choi, Yan Chen, Wei Dai "}, {"type": "b", "children": [{"type": "t", "text": "Chromatin PTEN is involved in DNA damage response partly through regulating Rad52 sumoylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Cycle (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4161/cc.26465"}], "href": "https://doi.org/10.4161/cc.26465"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24047694"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24047694"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Wenjing Qi, Ruoxi Wang, Hongyu Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "BRG1 promotes the repair of DNA double-strand breaks by facilitating the replacement of RPA with RAD51."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.159103"}], "href": "https://doi.org/10.1242/jcs.159103"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25395584"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25395584"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Rahul Bhowmick, Sheroy Minocherhomji, Ian D Hickson "}, {"type": "b", "children": [{"type": "t", "text": "RAD52 Facilitates Mitotic DNA Synthesis Following Replication Stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2016.10.037"}], "href": "https://doi.org/10.1016/j.molcel.2016.10.037"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27984745"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27984745"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Hong Zan, Connie Tat, Zhifang Qiu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rad52 competes with Ku70/Ku86 for binding to S-region DSB ends to modulate antibody class-switch DNA recombination."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms14244"}], "href": "https://doi.org/10.1038/ncomms14244"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28176781"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28176781"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Olga M Mazina, Havva Keskin, Kritika Hanamshet, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rad52 Inverse Strand Exchange Drives RNA-Templated DNA Double-Strand Break Repair."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2017.05.019"}], "href": "https://doi.org/10.1016/j.molcel.2017.05.019"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28602639"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28602639"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Jaewon Min, Woodring E Wright, Jerry W Shay "}, {"type": "b", "children": [{"type": "t", "text": "Clustered telomeres in phase-separated nuclear condensates engage mitotic DNA synthesis through BLM and RAD52."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genes Dev (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1101/gad.324905.119"}], "href": "https://doi.org/10.1101/gad.324905.119"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31171703"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31171703"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Teresa A Motycka, Tadayoshi Bessho, Sean M Post, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Physical and functional interaction between the XPF/ERCC1 endonuclease and hRad52."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M313779200"}], "href": "https://doi.org/10.1074/jbc.M313779200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14734547"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14734547"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Michael J McIlwraith, Stephen C West "}, {"type": "b", "children": [{"type": "t", "text": "DNA repair synthesis facilitates RAD52-mediated second-end capture during DSB repair."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2007.11.037"}], "href": "https://doi.org/10.1016/j.molcel.2007.11.037"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18313388"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18313388"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Nadja C de Souza-Pinto, Scott Maynard, Kazunari Hashiguchi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The recombination protein RAD52 cooperates with the excision repair protein OGG1 for the repair of oxidative lesions in mammalian cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.00265-09"}], "href": "https://doi.org/10.1128/MCB.00265-09"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19506022"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19506022"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Xiaoyi Deng, Aishwarya Prakash, Kajari Dhar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human replication protein A-Rad52-single-stranded DNA complex: stoichiometry and evidence for strand transfer regulation by phosphorylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi900564k"}], "href": "https://doi.org/10.1021/bi900564k"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19530647"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19530647"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Jill M Grimme, Masayoshi Honda, Rebecca Wright, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human Rad52 binds and wraps single-stranded DNA and mediates annealing via two hRad52-ssDNA complexes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkp1249"}], "href": "https://doi.org/10.1093/nar/gkp1249"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20081207"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20081207"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "P M Kim, C Allen, B M Wagener, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Overexpression of human RAD51 and RAD52 reduces double-strand break-induced homologous recombination in mammalian cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2001)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/29.21.4352"}], "href": "https://doi.org/10.1093/nar/29.21.4352"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11691922"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11691922"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Rafael J Yáñez, Andrew C G Porter "}, {"type": "b", "children": [{"type": "t", "text": "Differential effects of Rad52p overexpression on gene targeting and extrachromosomal homologous recombination in a human cell line."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/30.3.740"}], "href": "https://doi.org/10.1093/nar/30.3.740"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11809887"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11809887"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "A K Siraj, M Al-Rasheed, M Ibrahim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RAD52 polymorphisms contribute to the development of papillary thyroid cancer susceptibility in Middle Eastern population."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Endocrinol Invest (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/BF03346438"}], "href": "https://doi.org/10.1007/BF03346438"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19092295"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19092295"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Yue Jiang, Zhenzhen Qin, Zhibin Hu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genetic variation in a hsa-let-7 binding site in RAD52 is associated with breast cancer susceptibility."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Carcinogenesis (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/carcin/bgs373"}], "href": "https://doi.org/10.1093/carcin/bgs373"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23188672"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23188672"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Alessio Naccarati, Fabio Rosa, Veronika Vymetalkova, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Double-strand break repair and colorectal cancer: gene variants within 3' UTRs and microRNAs binding as modulators of cancer risk and clinical outcome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.6804"}], "href": "https://doi.org/10.18632/oncotarget.6804"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26735576"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26735576"}]}, {"type": "r", "ref": 30, "children": [{"type": "t", "text": "Bruna S Paulsen, Pankaj K Mandal, Richard L Frock, et al. 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