{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNEIL1 is a versatile DNA glycosylase that initiates base excision repair of oxidatively damaged bases throughout the genome. It recognizes and excises a broad range of substrates—including oxidized pyrimidines and purines such as 5‐hydroxyuracil, thymine glycol, and the hydantoin lesions guanidinohydantoin (Gh) and spiroiminodihydantoin (Sp)—often with a preference that is context dependent. Structural studies have revealed that NEIL1, although homologous to bacterial Nei, harbors a “zincless” DNA‐binding motif and a flexible C‐terminal domain that, while not essential for catalysis per se, is critical for modulating substrate specificity and stabilization of the enzyme conformation. Its excision rates can vary dramatically depending on the DNA context (duplex, bubble, fork, or single‐stranded), emphasizing a unique role in recognizing lesions not only in canonical duplex DNA but also in replication‐ or transcription‐associated DNA structures."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its catalytic function, NEIL1 is intimately coupled to DNA replication and repair coordination through numerous protein–protein interactions. It is induced by oxidative stress and activated primarily in S phase, interacting directly with key replication and repair factors such as proliferating cell nuclear antigen (PCNA), replication protein A (RPA), flap endonuclease 1 (FEN-1), and the Werner syndrome helicase (WRN) to facilitate prereplicative repair. Post-transcriptional modifications including adenosine-to-inosine RNA editing further modulate its substrate specificity, while its flexible C-terminal region mediates high-affinity binding with these partner proteins and is essential for its proper chromatin recruitment in replication complexes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its fundamental enzymatic role, dysregulation or mutation of NEIL1 has been linked to genomic instability and disease. Altered expression levels, genetic polymorphisms, and post-translational modifications such as polyubiquitylation have been associated with various human disorders, including certain cancers and even neuropsychiatric conditions. Moreover, NEIL1 participates in complex repair networks by interacting with additional factors such as the 9-1-1 complex and PARP-1, and it collaborates with TDG during oxidative DNA demethylation. Collectively, these studies highlight how NEIL1 not only repairs oxidative lesions but also interfaces with replication and checkpoint machinery to preserve genomic integrity under stress conditions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Viswanath Bandaru, Sirisha Sunkara, Susan S Wallace, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Repair (Amst) (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s1568-7864(02)00036-8"}], "href": "https://doi.org/10.1016/s1568-7864(02"}, {"type": "t", "text": "00036-8) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12509226"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12509226"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Hong Dou, Sankar Mitra, Tapas K Hazra "}, {"type": "b", "children": [{"type": "t", "text": "Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M308658200"}], "href": "https://doi.org/10.1074/jbc.M308658200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14522990"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14522990"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Sylvie Doublié, Viswanath Bandaru, Jeffrey P Bond, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity."}]}, {"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.0402051101"}], "href": "https://doi.org/10.1073/pnas.0402051101"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15232006"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15232006"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Kazuya Shinmura, Hong Tao, Masanori Goto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inactivating mutations of the human base excision repair gene NEIL1 in gastric cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Carcinogenesis (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/carcin/bgh267"}], "href": "https://doi.org/10.1093/carcin/bgh267"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15319300"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15319300"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Sanath K Mokkapati, Lee Wiederhold, Tapas K Hazra, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Stimulation of DNA glycosylase activity of OGG1 by NEIL1: functional collaboration between two human DNA glycosylases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi049097i"}], "href": "https://doi.org/10.1021/bi049097i"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15350146"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15350146"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Qiu-Mei Zhang, Shin-Ichiro Yonekura, Masashi Takao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Repair (Amst) (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.dnarep.2004.08.002"}], "href": "https://doi.org/10.1016/j.dnarep.2004.08.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15533839"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15533839"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Maria T Ocampo-Hafalla, Alvin Altamirano, Ashis K Basu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Repair of thymine glycol by hNth1 and hNeil1 is modulated by base pairing and cis-trans epimerization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Repair (Amst) (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.dnarep.2005.12.004"}], "href": "https://doi.org/10.1016/j.dnarep.2005.12.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16446124"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16446124"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Lei Jia, Vladimir Shafirovich, Nicholas E Geacintov, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Lesion specificity in the base excision repair enzyme hNeil1: modeling and dynamics studies."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi062269m"}], "href": "https://doi.org/10.1021/bi062269m"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17432829"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17432829"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Nirmala Krishnamurthy, Xiaobei Zhao, Cynthia J Burrows, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Superior removal of hydantoin lesions relative to other oxidized bases by the human DNA glycosylase hNEIL1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi800160s"}], "href": "https://doi.org/10.1021/bi800160s"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18543945"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18543945"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Xiaobei Zhao, Nirmala Krishnamurthy, Cynthia J Burrows, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi901852q"}], "href": "https://doi.org/10.1021/bi901852q"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20099873"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20099873"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Aditi Das, Tapas K Hazra, Istvan Boldogh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Induction of the human oxidized base-specific DNA glycosylase NEIL1 by reactive oxygen species."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M505526200"}], "href": "https://doi.org/10.1074/jbc.M505526200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16118226"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16118226"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Aditi Das, Istvan Boldogh, Jae Wan Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The human Werner syndrome protein stimulates repair of oxidative DNA base damage by the DNA glycosylase NEIL1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M703343200"}], "href": "https://doi.org/10.1074/jbc.M703343200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17611195"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17611195"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Hong Dou, Corey A Theriot, Aditi Das, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M709186200"}], "href": "https://doi.org/10.1074/jbc.M709186200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18032376"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18032376"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Corey A Theriot, Muralidhar L Hegde, Tapas K Hazra, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Repair (Amst) (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.dnarep.2010.02.014"}], "href": "https://doi.org/10.1016/j.dnarep.2010.02.014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20338831"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20338831"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Jongchan Yeo, Rena A Goodman, Nicole T Schirle, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RNA editing changes the lesion specificity for the DNA repair enzyme NEIL1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1009231107"}], "href": "https://doi.org/10.1073/pnas.1009231107"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21068368"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21068368"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Lorena Taricani, Frances Shanahan, Rob H Pierce, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phenotypic enhancement of thymidylate synthetase pathway inhibitors following ablation of Neil1 DNA glycosylase/lyase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Cycle (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4161/cc.9.24.14155"}], "href": "https://doi.org/10.4161/cc.9.24.14155"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21131780"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21131780"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "J Chaisaingmongkol, O Popanda, R Warta, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Epigenetic screen of human DNA repair genes identifies aberrant promoter methylation of NEIL1 in head and neck squamous cell carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2011.660"}], "href": "https://doi.org/10.1038/onc.2011.660"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22286769"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22286769"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Muralidhar L Hegde, Susan E Tsutakawa, Pavana M Hegde, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactions."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2013.03.030"}], "href": "https://doi.org/10.1016/j.jmb.2013.03.030"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23542007"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23542007"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Muralidhar L Hegde, Pavana M Hegde, Larry J Bellot, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Prereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1304231110"}], "href": "https://doi.org/10.1073/pnas.1304231110"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23898192"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23898192"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Pavana M Hegde, Arijit Dutta, Shiladitya Sengupta, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The C-terminal Domain (CTD) of Human DNA Glycosylase NEIL1 Is Required for Forming BERosome Repair Complex with DNA Replication Proteins at the Replicating Genome: DOMINANT NEGATIVE FUNCTION OF THE CTD."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M115.642918"}], "href": "https://doi.org/10.1074/jbc.M115.642918"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26134572"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26134572"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Peter Broderick, Tina Bagratuni, Jairam Vijayakrishnan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Evaluation of NTHL1, NEIL1, NEIL2, MPG, TDG, UNG and SMUG1 genes in familial colorectal cancer predisposition."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Cancer (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1471-2407-6-243"}], "href": "https://doi.org/10.1186/1471-2407-6-243"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17029639"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17029639"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Xin Guan, Haibo Bai, Guoli Shi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates NEIL1 glycosylase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkm075"}], "href": "https://doi.org/10.1093/nar/gkm075"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17395641"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17395641"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Xiadong Zhai, Hui Zhao, Zhensheng Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Functional variants of the NEIL1 and NEIL2 genes and risk and progression of squamous cell carcinoma of the oral cavity and oropharynx."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Cancer Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/1078-0432.CCR-07-5282"}], "href": "https://doi.org/10.1158/1078-0432.CCR-07-5282"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18594018"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18594018"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Monika Forsbring, Erik S Vik, Bjørn Dalhus, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Catalytically impaired hMYH and NEIL1 mutant proteins identified in patients with primary sclerosing cholangitis and cholangiocarcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Carcinogenesis (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/carcin/bgp118"}], "href": "https://doi.org/10.1093/carcin/bgp118"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19443904"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19443904"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Lars Schomacher, Dandan Han, Michael U Musheev, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Neil DNA glycosylases promote substrate turnover by Tdg during DNA demethylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Struct Mol Biol (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nsmb.3151"}], "href": "https://doi.org/10.1038/nsmb.3151"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26751644"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26751644"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Kazuya Shinmura, Hisami Kato, Yuichi Kawanishi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Abnormal Expressions of DNA Glycosylase Genes NEIL1, NEIL2, and NEIL3 Are Associated with Somatic Mutation Loads in Human Cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oxid Med Cell Longev (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1155/2016/1546392"}], "href": "https://doi.org/10.1155/2016/1546392"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27042257"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27042257"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Matthew J Edmonds, Rachel J Carter, Catherine M Nickson, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ubiquitylation-dependent regulation of NEIL1 by Mule and TRIM26 is required for the cellular DNA damage response."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkw959"}], "href": "https://doi.org/10.1093/nar/gkw959"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27924031"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27924031"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Karine Ø Bj Rås, Mirta M L Sousa, Animesh Sharma, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Monitoring of the spatial and temporal dynamics of BER/SSBR pathway proteins, including MYH, UNG2, MPG, NTH1 and NEIL1-3, during DNA replication."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkx476"}], "href": "https://doi.org/10.1093/nar/gkx476"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28575236"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28575236"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Anton Slyvka, Karolina Mierzejewska, Matthias Bochtler "}, {"type": "b", "children": [{"type": "t", "text": "Nei-like 1 (NEIL1) excises 5-carboxylcytosine directly and stimulates TDG-mediated 5-formyl and 5-carboxylcytosine excision."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-017-07458-4"}], "href": "https://doi.org/10.1038/s41598-017-07458-4"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28827588"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28827588"}]}, {"type": "r", "ref": 30, "children": [{"type": "t", "text": "Piotr Czarny, Dominik Kwiatkowski, Piotr Galecki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Association between single nucleotide polymorphisms of MUTYH, hOGG1 and NEIL1 genes, and depression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Affect Disord (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jad.2015.05.044"}], "href": "https://doi.org/10.1016/j.jad.2015.05.044"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26074017"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26074017"}]}, {"type": "r", "ref": 31, "children": [{"type": "t", "text": "Mustafa S Albelazi, Peter R Martin, Soran Mohammed, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Biochemical Role of the Human NEIL1 and NEIL3 DNA Glycosylases on Model DNA Replication Forks."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genes (Basel) (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/genes10040315"}], "href": "https://doi.org/10.3390/genes10040315"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31018584"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31018584"}]}]}]}