{"doi":"10.1073/pnas.95.6.2795","title":"Characterization of a human\n            <i>RPD3</i>\n            ortholog, HDAC3","abstract":"<jats:p>\n            Histone acetylation levels in cells result from a dynamic equilibrium between competing histone acetylases and deacetylases. Changes in histone acetylation levels occur during both transcriptional activation and silencing. Cloning of the cDNA for a human histone deacetylase (HDAC1) has shown that it represents a human ortholog of the yeast transcriptional regulator\n            <jats:italic>RPD3</jats:italic>\n            . We have screened the expressed sequence tag database (National Center for Biotechnology Information) with the yeast RPD3 sequence and identified a human ortholog of\n            <jats:italic>RPD3</jats:italic>\n            , HDAC3. This cDNA encodes a protein of 428 amino acids with 58% sequence identity with HDAC1p. By using a specific polyclonal antiserum recognizing the C-terminal domain of HDAC3p and Western blotting, we detected a single ∼49-kDa band in several tumor cell lines. HDAC3p is expressed predominantly in the nuclear compartment. Immunoprecipitation experiments with either an antiserum against HDAC3p or an anti-FLAG antiserum and a flagged HDAC3 cDNA showed that HDAc3p exhibits deacetylase activity both on free histones and on purified nucleosomes. This deacetylase activity is inhibited by trichostatin, trapoxin, and butyrate\n            <jats:italic>in vitro</jats:italic>\n            to the same degree as the deacetylase activity associated to HDAC1p. These observations identify another member of a growing family of human HDAC genes.\n          </jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1998,"id":13672,"datarank":14.082938596914635,"base_score":5.673323267171493,"endowment":5.673323267171493,"self_citation_contribution":0.850998490075724,"citation_network_contribution":13.23194010683891,"self_endowment_contribution":0.850998490075724,"citer_contribution":13.23194010683891,"corpus_percentile":null,"corpus_rank":null,"citation_count":290,"citer_count":200,"citers_with_citation_signal":200,"citers_with_endowment":200,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":111202,"name":"Wolfgang Fischle","orcid":null,"position":1,"is_corresponding":false},{"id":111203,"name":"Carine Van Lint","orcid":null,"position":2,"is_corresponding":false},{"id":111204,"name":"Yousef Al-Abed","orcid":null,"position":3,"is_corresponding":false},{"id":95315,"name":"Eric Verdin","orcid":"0000-0003-3703-3183","position":4,"is_corresponding":false},{"id":111201,"name":"Stephane Emiliani","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":5.673323267171493,"endowment":5.673323267171493,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"9501169","pmcid":"PMC19648","openalex_id":"https://openalex.org/W2113261653","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM51671","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM051671","title":null}],"total_grants":2,"fwci":10.7319,"citation_percentile":0.98923488,"influential_citations":22,"citation_trend":[{"year":2012,"count":6},{"year":2013,"count":10},{"year":2014,"count":7},{"year":2015,"count":6},{"year":2016,"count":12},{"year":2017,"count":5},{"year":2018,"count":4},{"year":2019,"count":6},{"year":2020,"count":7},{"year":2021,"count":7},{"year":2022,"count":9},{"year":2023,"count":1},{"year":2024,"count":6},{"year":2025,"count":2},{"year":2026,"count":1}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/19648","host_type":"repository"},{"url":"https://europepmc.org/articles/pmc19648?pdf=render","host_type":"GREEN"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/19648","host_type":"repository"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.95.6.2795","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.95.6.2795","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/9501169","host_type":"repository"}],"fields_of_study":["Histone Deacetylase Inhibitors Research","Epigenetics and DNA Methylation","Ubiquitin and proteasome pathways","Biology","Medicine","Amino Acid Sequence","Anti-Bacterial Agents","Base Sequence","Butyrates","Butyric Acid","DNA, Complementary","Gene Expression","Gene Library","Histone Deacetylase 1","Histone Deacetylase Inhibitors","Histone Deacetylases","Histones","Humans","Hydroxamic Acids","Molecular Sequence Data","Nuclear Proteins","Nucleosomes","Peptides","Sequence Homology, Amino Acid","Transcription Factors","Histone Deacetylase 3"],"mesh_terms":["Histone Deacetylase 3","Amino Acid Sequence","Anti-Bacterial Agents","Base Sequence","Butyrates","Histone Deacetylases","Histones","Humans","Hydroxamic Acids","Molecular Sequence Data","Nuclear Proteins","Nucleosomes","Peptides","Transcription Factors","Gene Library","Gene Expression","Sequence Homology, Amino Acid","DNA, Complementary","Butyric Acid","Histone Deacetylase 1","Histone Deacetylase Inhibitors"],"keywords":["Histone deacetylase 5","SAP30","Histone deacetylase","HDAC11","Histone deacetylase 2","Biology","HDAC10","HDAC4","Molecular biology","HDAC3","Acetylation","Histone","Complementary DNA","Trichostatin A","Biochemistry","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"gen"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-05-31T09:39:33.145329Z","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,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}