{"doi":"10.1021/acschembio.5b00554","title":"Regulation of Proteasomal Degradation by Modulating Proteasomal Initiation Regions","abstract":null,"journal":"ACS Chemical Biology","year":2015,"id":639849,"datarank":0.6255781522377654,"base_score":2.639057329615259,"endowment":2.639057329615259,"self_citation_contribution":0.3958585994422889,"citation_network_contribution":0.22971955279547643,"self_endowment_contribution":0.3958585994422889,"citer_contribution":0.22971955279547643,"corpus_percentile":null,"corpus_rank":null,"citation_count":13,"citer_count":8,"citers_with_citation_signal":8,"citers_with_endowment":8,"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":253739,"name":"Andreas Matouschek","orcid":"0000-0001-6016-2341","position":1,"is_corresponding":false},{"id":1662743,"name":"Tomonao Inobe","orcid":null,"position":2,"is_corresponding":false},{"id":1662742,"name":"Kazunobu Takahashi","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Regulation of Proteasomal Degradation by Modulating Proteasomal Initiation Regions","abstract":"Methods for regulating the concentrations of specific cellular proteins are valuable tools for biomedical studies. Artificial regulation of protein degradation by the proteasome is receiving increasing attention. Efficient proteasomal protein degradation requires a degron with two components: a ubiquitin tag that is recognized by the proteasome and a disordered region at which the proteasome engages the substrate and initiates degradation. Here we show that degradation rates can be regulated by modulating the disordered initiation region by the binding of modifier molecules, in vitro and in vivo. These results suggest that artificial modulation of proteasome initiation is a versatile method for conditionally inhibiting the proteasomal degradation of specific proteins.","is_dataset_classified":null,"base_score":2.639057329615259,"endowment":2.639057329615259,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26278914","pmcid":"PMC4922138","openalex_id":"https://openalex.org/W2245441002","authors":[],"funders":[{"funder_name":"Welch Foundation","grant_id":"F-1817","title":null},{"funder_name":"National Institute of General Medical Sciences","grant_id":"U54GM105816","title":null},{"funder_name":"Cancer Prevention and Research Institute of Texas","grant_id":"RP140328","title":null},{"funder_name":"Japan Society for the Promotion of Science","grant_id":"15H01531","title":null},{"funder_name":"Japan Society for the Promotion of Science","grant_id":"23107733","title":null},{"funder_name":"Japan Society for the Promotion of Science","grant_id":"26870216","title":null},{"funder_name":"Japan Society for the Promotion of Science","grant_id":"50568855","title":null},{"funder_name":"NCI NIH HHS","grant_id":"R21 CA191664","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM063004","title":null},{"funder_name":"Naito Foundation","grant_id":"","title":null},{"funder_name":"Asahi Glass Foundation","grant_id":"","title":null},{"funder_name":"Suzuken Memorial Foundation","grant_id":"","title":null},{"funder_name":"Ministry of Education, Culture, Sports, Science, and Technology","grant_id":"","title":null}],"total_grants":13,"fwci":1.3783,"citation_percentile":0.81155359,"influential_citations":0,"citation_trend":[{"year":2015,"count":1},{"year":2016,"count":3},{"year":2017,"count":4},{"year":2018,"count":2},{"year":2020,"count":3}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4922138","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4922138","host_type":"repository"},{"url":"https://pubs.acs.org/doi/pdf/10.1021/acschembio.5b00554","host_type":"publisher"},{"url":"https://doi.org/10.1021/acschembio.5b00554","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/26278914","host_type":"repository"}],"fields_of_study":["Ubiquitin and proteasome pathways","Protein Degradation and Inhibitors","Peptidase Inhibition and Analysis","Electrophoresis, Polyacrylamide Gel","HEK293 Cells","Humans","Peptide Initiation Factors","Proteasome Endopeptidase Complex","Protein Folding","Proteolysis","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins"],"mesh_terms":["Electrophoresis, Polyacrylamide Gel","Humans","Peptide Initiation Factors","Saccharomyces cerevisiae","Protein Folding","Saccharomyces cerevisiae Proteins","Proteasome Endopeptidase Complex","HEK293 Cells","Proteolysis"],"keywords":["Degron","Proteasome","Ubiquitin","Cell biology","Protein degradation","Degradation (telecommunications)","Chemistry","In vitro","Biochemistry","Biophysics","Biology","Ubiquitin ligase","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-07T03:02:27.724328Z","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":[]}