{"doi":"10.1016/j.jbc.2026.111440","title":"HECT-type ubiquitin ligases: Emerging principles in the era of full-length structures","abstract":null,"journal":"Journal of Biological Chemistry","year":2026,"id":611021,"datarank":0.10397207708399181,"base_score":0.6931471805599453,"endowment":0.6931471805599453,"self_citation_contribution":0.10397207708399181,"citation_network_contribution":0.0,"self_endowment_contribution":0.10397207708399181,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":1,"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":347653,"name":"Blanca Baños‐Jaime","orcid":"0000-0002-3358-7720","position":1,"is_corresponding":false},{"id":439626,"name":"Sonja Lorenz","orcid":"0000-0002-9639-2381","position":2,"is_corresponding":false},{"id":1571231,"name":"Thornton J. Fokkens","orcid":"0009-0005-4689-4024","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"HECT-type ubiquitin ligases: Emerging principles in the era of full-length structures","abstract":"Ubiquitin coordinates a complex network of cellular pathways through covalent modification of substrates. Specificity in substrate recognition and modification choice is largely conferred by ubiquitin ligases (E3s), a highly diversified enzyme family comprising 672 members in human cells. Among these, 28 belong to the homologous to E6AP C-terminus (HECT) family, whose distinctive structural features and functional specializations have remained incompletely understood. While the catalytic principles of the defining C-terminal HECT domain are well established, the manner in which this domain is embedded and regulated within full-length enzyme contexts long remained elusive. Over the past 5 years, a series of cryogenic electron microscopy studies have yielded unprecedented insight into the overall architectures, regulation modes, as well as linkage and substrate specificities of full-length HECT-type ligases. Here, we synthesize these advances to provide an up-to-date structural framework for HECT E3 mechanisms and highlight key questions for future investigation, including implications for small-molecule discovery.","is_dataset_classified":null,"base_score":0.6931471805599453,"endowment":0.6931471805599453,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"41966274","pmcid":"PMC13196369","openalex_id":"https://openalex.org/W7152520561","authors":[],"funders":[{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"unidentified","title":"unidentified"},{"funder_name":"German Research Foundation","grant_id":"","title":null},{"funder_name":"Max Planck Society","grant_id":"","title":null}],"total_grants":3,"fwci":4.1252,"citation_percentile":0.93334739,"influential_citations":0,"citation_trend":[{"year":2026,"count":1}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.1016/j.jbc.2026.111440","host_type":"journal"},{"url":"https://doi.org/10.1016/j.jbc.2026.111440","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925826003108?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925826003108?httpAccept=text/plain","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/41966274","host_type":"repository"},{"url":"https://resolver.sub.uni-goettingen.de/purl?gro-2/165273","host_type":"repository"},{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC13196369/","host_type":"repository"},{"url":"https://hdl.handle.net/21.11116/0000-0012-F4A3-0","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC13196369","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC13196369?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Ubiquitin and proteasome pathways","Microtubule and mitosis dynamics","Protein Degradation and Inhibitors","0301 basic medicine","03 medical and health sciences","Ubiquitin-Protein Ligases","Humans","Substrate Specificity"],"mesh_terms":["Humans","Substrate Specificity","Ubiquitin-Protein Ligases"],"keywords":["Ubiquitin","Ubiquitin-Protein Ligases","Mechanism (biology)","Protein structure","Protein–protein interaction","Ubiquitin ligase","Ubiquitination","Enzyme Mechanism","Cryo Electron Microscopy","Posttranslational Modification","Substrate Recognition","E3"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Zero hunger"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-01T14:32:33.236751Z","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":[]}