{"doi":"10.1038/nature00970","title":"Trans-histone regulatory pathway in chromatin","abstract":null,"journal":"Nature","year":2002,"id":667573,"datarank":0.9392237526481564,"base_score":6.261491684321042,"endowment":6.261491684321042,"self_citation_contribution":0.9392237526481564,"citation_network_contribution":0.0,"self_endowment_contribution":0.9392237526481564,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":523,"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":820451,"name":"Tiaojiang Xiao","orcid":"0000-0002-2794-3944","position":1,"is_corresponding":false},{"id":538613,"name":"Zu-Wen Sun","orcid":null,"position":2,"is_corresponding":false},{"id":1743288,"name":"Jennifer A. Caldwell","orcid":null,"position":3,"is_corresponding":false},{"id":267554,"name":"Jeffrey Shabanowitz","orcid":"0000-0001-5750-3539","position":4,"is_corresponding":false},{"id":267543,"name":"Donald F. Hunt","orcid":"0000-0003-2815-6368","position":5,"is_corresponding":false},{"id":71450,"name":"C. David Allis","orcid":"0000-0001-7589-713X","position":6,"is_corresponding":false},{"id":71449,"name":"Brian D. Strahl","orcid":"0000-0002-4947-6259","position":7,"is_corresponding":false},{"id":191375,"name":"Scott D. Briggs","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Trans-histone regulatory pathway in chromatin","abstract":"The fundamental unit of eukaryotic chromatin, the nucleosome, consists of genomic DNA wrapped around the conserved histone proteins H3, H2B, H2A and H4, all of which are variously modified at their amino- and carboxy-terminal tails to influence the dynamics of chromatin structure and function -- for example, conjugation of histone H2B with ubiquitin controls the outcome of methylation at a specific lysine residue (Lys 4) on histone H3, which regulates gene silencing in the yeast Saccharomyces cerevisiae. Here we show that ubiquitination of H2B is also necessary for the methylation of Lys 79 in H3, the only modification known to occur away from the histone tails, but that not all methylated lysines in H3 are regulated by this 'trans-histone' pathway because the methylation of Lys 36 in H3 is unaffected. Given that gene silencing is regulated by the methylation of Lys 4 and Lys 79 in histone H3, we suggest that H2B ubiquitination acts as a master switch that controls the site-selective histone methylation patterns responsible for this silencing.","is_dataset_classified":null,"base_score":6.261491684321042,"endowment":6.261491684321042,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"12152067","pmcid":null,"openalex_id":"https://openalex.org/W2036479240","authors":[],"funders":[],"total_grants":0,"fwci":12.045,"citation_percentile":0.99255147,"influential_citations":0,"citation_trend":[{"year":2012,"count":31},{"year":2013,"count":23},{"year":2014,"count":26},{"year":2015,"count":19},{"year":2016,"count":13},{"year":2017,"count":10},{"year":2018,"count":11},{"year":2019,"count":18},{"year":2020,"count":19},{"year":2021,"count":23},{"year":2022,"count":13},{"year":2023,"count":13},{"year":2024,"count":20},{"year":2025,"count":14},{"year":2026,"count":8}],"oa_status":"bronze","license":"https://www.springernature.com/gp/researchers/text-and-data-mining","oa_locations":[{"url":"https://www.nature.com/articles/nature00970.pdf","host_type":"journal"},{"url":"https://www.nature.com/articles/nature00970.pdf","host_type":"publisher"},{"url":"https://www.nature.com/articles/nature00970","host_type":"publisher"},{"url":"https://doi.org/10.1038/nature00970","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/12152067","host_type":"repository"}],"fields_of_study":["Genomics and Chromatin Dynamics","Plant Molecular Biology Research","Cancer-related gene regulation","Chromatin","Gene Expression Regulation, Fungal","Gene Silencing","Histone-Lysine N-Methyltransferase","Histones","Ligases","Methylation","Models, Biological","Nuclear Proteins","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins","Ubiquitin","Ubiquitin-Conjugating Enzymes"],"mesh_terms":["Chromatin","Histones","Ligases","Methylation","Models, Biological","Nuclear Proteins","Histone-Lysine N-Methyltransferase","Saccharomyces cerevisiae","Gene Expression Regulation, Fungal","Gene Silencing","Ubiquitin","Saccharomyces cerevisiae Proteins","Ubiquitin-Conjugating Enzymes"],"keywords":["Histone methylation","Histone methyltransferase","Histone H2A","Histone H3","Histone code","Histone octamer","EZH2","Histone H1","Nucleosome","Histone H2B","Chromatin","Epigenomics","Biology","Histone","Cell biology","Genetics","DNA methylation","Gene","Gene expression"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-13T18:19:09.103016Z","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":[]}