{"doi":"10.1073/pnas.91.5.1642","title":"Efficient removal of uracil from G.U mispairs by themismatch-specific thymine DNA glycosylase from HeLa cells.","abstract":"<jats:p>The uracil DNA glycosylases (EC 3.2.2.3)\ncharacterized to date remove uracil from DNA irrespective of whether it is base\npaired with adenine or mispaired with guanine in double-stranded substrates or\nwhether it is found in single-stranded DNA. We report here the characterization\nof uracil glycosylase activity that can remove the base solely from a mispair\nwith guanine. It does not recognize uracil either in A.U pairs or in\nsingle-stranded substrates. The enzyme, a 55-kDa polypeptide, was previously\ncharacterized as a mismatch-specific thymine DNA glycosylase and was thought to\nbe responsible solely for the correction (to G.C) of G.T mispairs that arise as\na result of spontaneous hydrolytic deamination of 5-methylcytosine to thymine.\nGiven the broader substrate specificity of the enzyme (in addition to uracil and\nthymine, the protein can also remove 5-bromouracil from mispairs with guanine),\nwe propose that its biological role in vivo may also include the correction of a\nsubset of G.U mispairs inefficiently removed by the more abundant ubiquitous\nuracil glycosylases, such as those arising from cytosine deamination in G+C-rich\nregions of the genome.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1994,"id":46887,"datarank":7.4410121181861575,"base_score":5.062595033026967,"endowment":5.062595033026967,"self_citation_contribution":0.7593892549540452,"citation_network_contribution":6.681622863232112,"self_endowment_contribution":0.7593892549540452,"citer_contribution":6.681622863232112,"corpus_percentile":null,"corpus_rank":null,"citation_count":157,"citer_count":142,"citers_with_citation_signal":122,"citers_with_endowment":122,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":216815,"name":"J Jiricny","orcid":null,"position":1,"is_corresponding":false},{"id":216814,"name":"P Neddermann","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Efficient removal of uracil from G.U mispairs by themismatch-specific thymine DNA glycosylase from HeLa cells.","abstract":"<jats:p>The uracil DNA glycosylases (EC 3.2.2.3)\ncharacterized to date remove uracil from DNA irrespective of whether it is base\npaired with adenine or mispaired with guanine in double-stranded substrates or\nwhether it is found in single-stranded DNA. We report here the characterization\nof uracil glycosylase activity that can remove the base solely from a mispair\nwith guanine. It does not recognize uracil either in A.U pairs or in\nsingle-stranded substrates. The enzyme, a 55-kDa polypeptide, was previously\ncharacterized as a mismatch-specific thymine DNA glycosylase and was thought to\nbe responsible solely for the correction (to G.C) of G.T mispairs that arise as\na result of spontaneous hydrolytic deamination of 5-methylcytosine to thymine.\nGiven the broader substrate specificity of the enzyme (in addition to uracil and\nthymine, the protein can also remove 5-bromouracil from mispairs with guanine),\nwe propose that its biological role in vivo may also include the correction of a\nsubset of G.U mispairs inefficiently removed by the more abundant ubiquitous\nuracil glycosylases, such as those arising from cytosine deamination in G+C-rich\nregions of the genome.</jats:p>","is_dataset_classified":null,"base_score":5.062595033026967,"endowment":5.062595033026967,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"8127859","pmcid":"PMC43219","openalex_id":"https://openalex.org/W2056986228","authors":[],"funders":[],"total_grants":0,"fwci":2.0477,"citation_percentile":0.87316512,"influential_citations":1,"citation_trend":[{"year":2012,"count":5},{"year":2013,"count":6},{"year":2014,"count":4},{"year":2015,"count":5},{"year":2016,"count":3},{"year":2017,"count":4},{"year":2018,"count":2},{"year":2019,"count":3},{"year":2020,"count":2},{"year":2021,"count":2},{"year":2022,"count":3},{"year":2023,"count":3},{"year":2024,"count":8},{"year":2025,"count":7},{"year":2026,"count":5}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/43219","host_type":"repository"},{"url":"https://doi.org/10.1073/pnas.91.5.1642","host_type":"BRONZE"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/43219","host_type":"repository"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.91.5.1642","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/8127859","host_type":"repository"}],"fields_of_study":["DNA Repair Mechanisms","Genomics and Chromatin Dynamics","RNA and protein synthesis mechanisms","Biology","Medicine","Chemistry"],"mesh_terms":["Base Composition","Base Sequence","DNA","DNA Repair","Endodeoxyribonucleases","HeLa Cells","Humans","Molecular Sequence Data","Substrate Specificity","Thymine","Uracil","Deoxyribonuclease (Pyrimidine Dimer)","Hela Cells"],"keywords":["Deamination","Uracil","DNA glycosylase","Guanine","Thymine","Cytosine","DNA","Biochemistry","Uracil-DNA glycosylase","Chemistry","Pyrimidine","Biology","DNA repair","Molecular biology","Enzyme","Nucleotide","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-14T22:07:29.268286Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}