{"doi":"10.1126/science.aad9421","title":"Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome","abstract":"<jats:title>The yin and yang of proteasomal regulation</jats:title>\n          <jats:p>\n            The ubiquitin-proteasome pathway regulates myriad proteins through their selective proteolysis. The small protein ubiquitin is attached, typically in many copies, to the target protein, which is then recognized and broken down by the proteasome. Shi\n            <jats:italic>et al.</jats:italic>\n            found a repeat structure in the proteasome for recognizing ubiquitin as well as ubiquitin-like (UBL) proteins. Tandem binding sites allow the proteasome to dock multiple proteins. One of the bound UBL proteins is an enzyme that cleaves ubiquitin-protein conjugates, which antagonizes degradation. Thus, the repetition of related binding sites with distinct specificity achieves a balance of positive and negative regulation of the proteasome.\n          </jats:p>\n          <jats:p>\n            <jats:italic>Science</jats:italic>\n            , this issue p.\n            <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" related-article-type=\"in-this-issue\" xlink:href=\"10.1126/science.aad9421\">10.1126/science.aad9421</jats:related-article>\n          </jats:p>","journal":"Science","year":2016,"id":24321,"datarank":8.25997881396984,"base_score":5.777652323222656,"endowment":5.777652323222656,"self_citation_contribution":0.8666478484833986,"citation_network_contribution":7.393330965486441,"self_endowment_contribution":0.8666478484833986,"citer_contribution":7.393330965486441,"corpus_percentile":null,"corpus_rank":null,"citation_count":322,"citer_count":200,"citers_with_citation_signal":200,"citers_with_endowment":200,"datacite_reuse_total":4,"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":52790,"name":"Xiang Chen","orcid":"0000-0001-8187-636X","position":1,"is_corresponding":false},{"id":146317,"name":"Suzanne Elsasser","orcid":null,"position":2,"is_corresponding":false},{"id":146318,"name":"Bradley B. Stocks","orcid":null,"position":3,"is_corresponding":false},{"id":146319,"name":"Geng Tian","orcid":null,"position":4,"is_corresponding":false},{"id":146320,"name":"Byung-Hoon Lee","orcid":null,"position":5,"is_corresponding":false},{"id":141910,"name":"Yanhong Shi","orcid":null,"position":6,"is_corresponding":false},{"id":146321,"name":"Naixia Zhang","orcid":null,"position":7,"is_corresponding":false},{"id":146322,"name":"Stefanie A. H. de Poot","orcid":null,"position":8,"is_corresponding":false},{"id":146323,"name":"Fabian Tuebing","orcid":null,"position":9,"is_corresponding":false},{"id":146324,"name":"Shuangwu Sun","orcid":null,"position":10,"is_corresponding":false},{"id":146325,"name":"Jacob Vannoy","orcid":null,"position":11,"is_corresponding":false},{"id":146326,"name":"Sergey G. Tarasov","orcid":null,"position":12,"is_corresponding":false},{"id":141411,"name":"John R. Engen","orcid":null,"position":13,"is_corresponding":false},{"id":146327,"name":"Daniel Finley","orcid":null,"position":14,"is_corresponding":false},{"id":146328,"name":"Kylie J. Walters","orcid":null,"position":15,"is_corresponding":false},{"id":77853,"name":"Yuan Shi","orcid":"0000-0002-4571-4424","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":5.777652323222656,"endowment":5.777652323222656,"datacite_reuse_total":4,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26912900","pmcid":"PMC4980823","openalex_id":"https://openalex.org/W2277539891","authors":[],"funders":[{"funder_name":"National Institutes of Health","grant_id":"R37-GM043601","title":null},{"funder_name":"National Institutes of Health","grant_id":"CA136472","title":null},{"funder_name":"National Institutes of Health","grant_id":"R01-GM101135","title":null},{"funder_name":"Intramural NIH HHS","grant_id":"ZIA BC011490","title":null},{"funder_name":"Intramural NIH HHS","grant_id":"Z99 CA999999","title":null},{"funder_name":"NCI NIH HHS","grant_id":"R01 CA136472","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM043601","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R37 GM043601","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM101135","title":null},{"funder_name":"Intramural Research Program of the NIH","grant_id":"","title":null},{"funder_name":"National Cancer Institute","grant_id":"","title":null},{"funder_name":"Center for Cancer Research","grant_id":"","title":null}],"total_grants":12,"fwci":18.104,"citation_percentile":0.99461,"influential_citations":33,"citation_trend":[{"year":2016,"count":21},{"year":2017,"count":22},{"year":2018,"count":27},{"year":2019,"count":33},{"year":2020,"count":44},{"year":2021,"count":33},{"year":2022,"count":37},{"year":2023,"count":29},{"year":2024,"count":31},{"year":2025,"count":37},{"year":2026,"count":8}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://science.sciencemag.org/content/sci/351/6275/aad9421.full.pdf","host_type":"GREEN"},{"url":"https://www.science.org/doi/pdf/10.1126/science.aad9421","host_type":"publisher"},{"url":"https://doi.org/10.1126/science.aad9421","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/26912900","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4980823","host_type":"repository"}],"fields_of_study":["Ubiquitin and proteasome pathways","Peptidase Inhibition and Analysis","RNA modifications and cancer","Biology","Medicine","DNA-Binding Proteins","Endopeptidases","Metabolic Networks and Pathways","Models, Molecular","Mutation","Proteasome Endopeptidase Complex","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins","Ubiquitin-Specific Proteases","Ubiquitination"],"mesh_terms":["DNA-Binding Proteins","Models, Molecular","Mutation","Endopeptidases","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins","Proteasome Endopeptidase Complex","Metabolic Networks and Pathways","Ubiquitination","Ubiquitin-Specific Proteases"],"keywords":["Proteasome","Cell biology","Receptor","Substrate (aquarium)","Chemistry","Biophysics","Biochemistry","Biology","Ecology"],"sdg_mappings":[],"linked_datasets":[{"doi":"10.6084/m9.figshare.26579132.v1","title":"Additional file 1 of PSMD2 contributes to the progression of esophageal squamous cell carcinoma by repressing autophagy","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.26579132","title":"Additional file 1 of PSMD2 contributes to the progression of esophageal squamous cell carcinoma by repressing autophagy","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.26579135.v1","title":"Additional file 2 of PSMD2 contributes to the progression of esophageal squamous cell carcinoma by repressing autophagy","publisher":"figshare","resource_type":"Dataset"},{"doi":"10.6084/m9.figshare.26579135","title":"Additional file 2 of PSMD2 contributes to the progression of esophageal squamous cell carcinoma by repressing autophagy","publisher":"figshare","resource_type":"Dataset"}],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-07T22:08:08.920281Z","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":[]}