{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMethylpurine‐DNA glycosylase (MPG), also known as alkyladenine DNA glycosylase (AAG) or alkylpurine‐DNA‐N‐glycosylase, is a key enzyme in the base excision repair pathway that recognizes and removes a broad spectrum of damaged purine bases. In vitro and in vivo studies have demonstrated that MPG/AAG excises a variety of lesions—including alkylated bases (such as 3‐methyladenine and 7‐methylguanine), deaminated purines (e.g. hypoxanthine), and exocyclic adducts like 1,N⁶‐ethenoadenine—as well as oxidatively generated lesions. These activities are critical for preventing mutations that can lead to genomic instability and cancer. MPG/AAG employs a nucleotide flipping mechanism that extrudes the damaged base from the DNA helix so that it can be hydrolyzed; key active‐site residues (for example, Tyr162) have been shown to be essential for intercalating into the DNA and stabilizing the flipped conformation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its catalytic role, MPG exhibits dynamic mechanisms for locating and processing lesions in chromatin. Single‐molecule and ensemble studies have revealed that MPG can slide and hop along DNA—mechanisms that allow rapid scanning of vast genomic regions for rare damaged sites. Structural and kinetic investigations highlight the importance of conformational changes during nucleotide flipping and product release, as well as direct interactions with other proteins. MPG has been shown to interact with transcriptional regulators such as methylated DNA binding protein 1 and the estrogen receptor, and it associates with factors involved in chromatin organization, ensuring that lesion repair is coordinated with transcription and replication. Moreover, evidence indicates that MPG’s activity can be modulated by posttranslational modifications and intrinsic product inhibition, emphasizing its role not only in lesion excision but also in signaling to the broader DNA damage response network."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAlterations in MPG expression and coding sequence have significant biological and clinical consequences. Variants and polymorphisms in the MPG gene have been associated with cancer susceptibility—including lung, colorectal, and glioma—as well as with inflammatory conditions such as rheumatoid arthritis. Differential MPG expression can influence cellular sensitivity to alkylating chemotherapeutic agents (by affecting the rate of lesion removal and subsequent repair intermediate processing), contribute to replicative stress at DNA replication forks, and even lead to unintended frameshift mutagenesis when binding to incorrectly structured DNA intermediates. Furthermore, MPG’s interactions with tumor suppressors (for instance, p53) and with epigenetic regulators (such as UHRF proteins) underscore a multifaceted role in coordinating DNA repair with transcriptional regulation, with implications for both genomic stability and therapeutic response."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "M Saparbaev, J Laval "}, {"type": "b", "children": [{"type": "t", "text": "Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (1994)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.91.13.5873"}], "href": "https://doi.org/10.1073/pnas.91.13.5873"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "8016081"}], "href": "https://pubmed.ncbi.nlm.nih.gov/8016081"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Murat Saparbaev, Sophie Langouët, Cyril V Privezentzev, et al. "}, {"type": "b", "children": [{"type": "t", "text": "1,N(2)-ethenoguanine, a mutagenic DNA adduct, is a primary substrate of Escherichia coli mismatch-specific uracil-DNA glycosylase and human alkylpurine-DNA-N-glycosylase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111100200"}], "href": "https://doi.org/10.1074/jbc.M111100200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12016206"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12016206"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Aarthy C Vallur, Joyce A Feller, Clint W Abner, et al. 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