{"doi":"10.1038/41358","title":"Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells","abstract":null,"journal":"Nature","year":1997,"id":672941,"datarank":0.9774289614064448,"base_score":6.516193076042964,"endowment":6.516193076042964,"self_citation_contribution":0.9774289614064448,"citation_network_contribution":0.0,"self_endowment_contribution":0.9774289614064448,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":675,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"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":14858,"name":"Matthias Wilm","orcid":"0000-0002-5461-6834","position":1,"is_corresponding":false},{"id":1758241,"name":"Xiantuo Wu","orcid":null,"position":2,"is_corresponding":false},{"id":1758242,"name":"Peter Kulesza","orcid":null,"position":3,"is_corresponding":false},{"id":699693,"name":"Thomas E. Wilson","orcid":"0000-0002-8345-4985","position":4,"is_corresponding":false},{"id":2937,"name":"Matthias Mann","orcid":"0000-0003-1292-4799","position":5,"is_corresponding":false},{"id":175797,"name":"Michael R. Lieber","orcid":null,"position":6,"is_corresponding":false},{"id":1758240,"name":"Ulf Grawunder","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells","abstract":"Mutation of the XRCC4 gene in mammalian cells prevents the formation of the signal and coding joints in the V(D)J recombination reaction, which is necessary for production of a functional immunoglobulin gene, and renders the cells highly sensitive to ionizing radiation. However, XRCC4 shares no sequence homology with other proteins, nor does it have a biochemical activity to indicate what its function might be. Here we show that DNA ligase IV co-immunoprecipitates with XRCC4 and that these two proteins specifically interact with one another in a yeast two-hybrid system. Ligation of DNA double-strand breaks in a cell-free system by DNA ligase IV is increased fivefold by purified XRCC4 and seven- to eightfold when XRCC4 is co-expressed with DNA ligase IV. We conclude that the biological consequences of mutating XRCC4 are primarily due to the loss of its stimulatory effect on DNA ligase IV: the function of the XRCC4-DNA ligase IV complex may be to carry out the final steps of V(D)J recombination and joining of DNA ends.","is_dataset_classified":null,"base_score":6.516193076042964,"endowment":6.516193076042964,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"9242410","pmcid":null,"openalex_id":"https://openalex.org/W1532833901","authors":[],"funders":[],"total_grants":0,"fwci":14.3059,"citation_percentile":0.99412665,"influential_citations":0,"citation_trend":[{"year":2012,"count":23},{"year":2013,"count":24},{"year":2014,"count":28},{"year":2015,"count":24},{"year":2016,"count":20},{"year":2017,"count":20},{"year":2018,"count":12},{"year":2019,"count":18},{"year":2020,"count":14},{"year":2021,"count":16},{"year":2022,"count":17},{"year":2023,"count":12},{"year":2024,"count":12},{"year":2025,"count":9},{"year":2026,"count":4}],"oa_status":"bronze","license":"https://www.springernature.com/gp/researchers/text-and-data-mining","oa_locations":[{"url":"https://www.nature.com/articles/41358.pdf","host_type":"journal"},{"url":"https://www.nature.com/articles/41358.pdf","host_type":"publisher"},{"url":"https://www.nature.com/articles/41358","host_type":"publisher"},{"url":"http://www.nature.com/doifinder/10.1038/41358","host_type":"publisher"},{"url":"https://doi.org/10.1038/41358","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/9242410","host_type":"repository"}],"fields_of_study":["DNA Repair Mechanisms","CRISPR and Genetic Engineering","PARP inhibition in cancer therapy"],"mesh_terms":["DNA Ligase ATP","Animals","Cloning, Molecular","DNA","DNA-Binding Proteins","Enzyme Activation","Cricetinae","Humans","Mammals","Mutation","DNA Ligases","Recombinant Fusion Proteins","Recombination, Genetic","Transfection","CHO Cells"],"keywords":["DNA repair protein XRCC4","DNA ligase","DNA repair","Ubiquitin ligase","Biology","Non-homologous end joining","DNA","Molecular biology","V(D)J recombination","DDB1","Cell biology","Gene","Genetics","Nucleotide excision repair","Recombination","Ubiquitin"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T11:49:13.836624Z","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":[]}