{"doi":"10.1002/cbic.201800797","title":"Optimal Substrate‐Trapping Mutants to Discover Substrates of HDAC1","abstract":"<jats:title>Abstract</jats:title><jats:p>Histone deacetylase 1 (HDAC1) regulates transcription by deacetylating histones. In addition to histones, several non‐histone proteins are HDAC1 substrates, which suggests a role for HDAC1 beyond epigenetics. Unfortunately, the identification of non‐histone substrates has been largely serendipitous, which makes full characterization of HDAC1 functions difficult. To overcome this challenge, inactive “trapping” mutants were recently developed to identify HDAC1 substrates. To optimize substrate trapping, the relative trapping abilities of 17 inactive HDAC1 mutants was assessed. HDAC1 H141A, F150A, and C151A showed strong binding to substrates LSD1 and p53. Interestingly, each mutant preferentially trapped a different substrate. By combining several inactive mutants, the trapping strategy will facilitate the discovery of new HDAC1 substrates and shed light on the variety of HDAC1‐related functions in cell biology.</jats:p>","journal":"ChemBioChem","year":2019,"id":31488,"datarank":0.2753727939694021,"base_score":1.6094379124341003,"endowment":1.6094379124341003,"self_citation_contribution":0.24141568686511508,"citation_network_contribution":0.03395710710428703,"self_endowment_contribution":0.24141568686511508,"citer_contribution":0.03395710710428703,"corpus_percentile":null,"corpus_rank":null,"citation_count":4,"citer_count":2,"citers_with_citation_signal":1,"citers_with_endowment":1,"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":168688,"name":"Mary Kay H. Pflum","orcid":"0000-0002-1396-3194","position":1,"is_corresponding":false},{"id":168687,"name":"Inosha D. Gomes","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":1.6094379124341003,"endowment":1.6094379124341003,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"30701667","pmcid":"PMC6858619","openalex_id":"https://openalex.org/W2914139318","authors":[],"funders":[{"funder_name":"National Institute of General Medical Sciences","grant_id":"GM121061","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R35 GM131821","title":null},{"funder_name":"NIH HHS","grant_id":"S10 OD025170","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM121061","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM067657","title":null}],"total_grants":5,"fwci":0.2563,"citation_percentile":0.55178414,"influential_citations":0,"citation_trend":[{"year":2021,"count":2},{"year":2022,"count":1},{"year":2025,"count":1}],"oa_status":"green","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6858619","host_type":"repository"},{"url":"https://europepmc.org/articles/pmc6858619?pdf=render","host_type":"GREEN"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6858619","host_type":"repository"},{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcbic.201800797","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.201800797","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/full-xml/10.1002/cbic.201800797","host_type":"publisher"},{"url":"https://chemistry-europe.onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.201800797","host_type":"publisher"},{"url":"https://doi.org/10.1002/cbic.201800797","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/30701667","host_type":"repository"}],"fields_of_study":["Histone Deacetylase Inhibitors Research","Protein Degradation and Inhibitors","Click Chemistry and Applications","Medicine","Biology","Chemistry","Epigenesis, Genetic","HEK293 Cells","Histone Deacetylase 1","Histone Demethylases","Histones","Humans","Mutation","Protein Binding","Substrate Specificity","Tumor Suppressor Protein p53"],"mesh_terms":["Histones","Humans","Mutation","Protein Binding","Substrate Specificity","Tumor Suppressor Protein p53","Epigenesis, Genetic","Histone Deacetylase 1","Histone Demethylases","HEK293 Cells"],"keywords":["HDAC1","Histone","Mutant","Histone deacetylase","Epigenetics","Trapping","Cell biology","HDAC11","Histone deacetylase 5","Biology","Chemistry","Computational biology","Biochemistry","Gene","Proteins","Mutagenesis","Proteomics","Histones","Substrate Trapping Mutants"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-09T07:19:01.014121Z","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":[]}