{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nHuman 8‐oxoguanine DNA glycosylase (OGG1) is a pivotal enzyme in the base excision repair pathway that safeguards genomic integrity by recognizing and excising 7,8‐dihydro-8‐oxoguanine (8-oxoG), one of the most abundant and mutagenic DNA lesions produced by reactive oxygen species. OGG1 employs a nearly barrierless, one-dimensional sliding mechanism along the DNA to rapidly locate rare lesions and uses a sophisticated catalytic strategy—including product-assisted catalysis and substrate discrimination mechanisms—to excise 8-oxoG efficiently. In addition, OGG1 function is coordinated by physical interactions with other repair proteins such as XRCC1 and APE1, thereby facilitating the hand‐off of repair intermediates and accelerating the overall repair process."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOGG1 activity is intricately regulated by post-translational modifications and cellular redox status. For example, acetylation by p300 markedly enhances its 8-oxoG excision efficiency, while deacetylation mediated by Sirtuin 3 (Sirt3) helps prevent proteolytic degradation and maintains optimal mitochondrial DNA repair. Conversely, oxidation of critical cysteine residues can reversibly inactivate OGG1, a process that is modulated by thiol-reactive compounds and metal ions such as cadmium. These regulatory mechanisms ensure that OGG1 function is tightly linked to the oxidative state of the cell and help determine its repair capacity under stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in DNA repair, OGG1 also contributes to cellular signaling and gene regulation. When bound to its 8-oxoG substrate in promoter regions, OGG1 can facilitate the binding of transcription factors such as NF-κB, thereby coupling oxidative DNA damage with the activation of pro-inflammatory and stress-responsive genes. Moreover, various epidemiologic studies have linked common OGG1 polymorphisms—most notably the Ser326Cys variant—with altered repair capacity and an increased risk for multiple cancer types (including lung, colorectal, esophageal, and head and neck cancers), highlighting its clinical importance as a modulator of both genomic stability and the cellular stress response. These genetic associations, along with evidence of functional interaction with other repair and metabolic proteins, underscore OGG1’s broader impact on disease susceptibility and inflammatory signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Rayjean J Hung, Janet Hall, Paul Brennan, et al. 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