{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nHuman NTHL1 is a key DNA glycosylase–apurinic/apyrimidinic (AP) lyase that initiates the base excision repair (BER) pathway by recognizing and removing oxidized pyrimidines such as thymine glycol. Multiple studies demonstrate that loss‐of‐function or biallelic germline mutations in NTHL1 predispose individuals to a distinct polyposis syndrome associated with colorectal cancer and a broad spectrum of extracolonic malignancies—including endometrial and breast cancers—often marked by a characteristic mutational signature enriched in cytosine‐to‐thymine transitions. These findings, uncovered in familial adenomatous polyposis, multi‐tumor pedigrees, and population studies, firmly establish NTHL1 as a critical tumor suppressor in maintaining genomic integrity."}, {"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": "\nAt the biochemical level, NTHL1 acts as a bifunctional enzyme that excises oxidatively damaged bases and cleaves the resulting AP sites. Detailed kinetic and substrate‐specificity studies have shown that its activity is influenced by lesion stereochemistry, the base pair context, and the packaging of DNA into nucleosomes—with evidence that NTHL1 can process lesions both in naked DNA and in more complex chromatin structures. Moreover, its enzymatic function is modulated by a unique N‑terminal domain that controls dimerization and catalytic turnover, and by its direct interactions with regulatory partners (such as APE1, YB‑1, PCNA, p53, and XPG), which further fine‐tune its repair capacity. Complementary structural studies have revealed distinct open and closed conformations linked to an interdomain linker, while advanced biophysical assays and innovative fluorescence‐based detection strategies have provided real‐time insights into NTHL1’s dynamics on damaged DNA."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its core repair functions, NTHL1 is subject to multifaceted regulatory mechanisms that modulate its stability, localization, and activity under stress conditions. Aberrant expression and mislocalization of NTHL1 have been associated with cancer pathogenesis, while post‑translational modifications—including SUMOylation and ubiquitin-mediated degradation by ligases such as TRIM26—further control its protein levels in response to oxidative damage. Functional studies evaluating NTHL1 variants have reinforced the clinical relevance of its mutational spectrum and highlighted its interplay with replication machinery and repair complexes in chromatin. These cellular and clinical investigations underscore the importance of NTHL1 not only in preserving genomic integrity but also as a potential marker for genetic predisposition to multiple cancer types."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Robbert D A Weren, Marjolijn J L Ligtenberg, C Marleen Kets, et al. 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