{"doi":"10.1055/s-0036-1596420","title":"Polyphenols and proteostasis: The role of heat shock response and the ubiquitin-proteasome system","abstract":null,"journal":"Planta Medica","year":2016,"id":685739,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"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":1791582,"name":"Z Glen","orcid":null,"position":1,"is_corresponding":false},{"id":1791581,"name":"IV Ogungbe","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Polyphenols and proteostasis: The role of heat shock response and the ubiquitin-proteasome system","abstract":"Reduced proteostasis is believed to be one of the major consequences of aging and oxidative stress. Exogenous compounds that promote proteostasis by regulating the heat shock response and the ubiquitin-proteasome system – key components of the proteostasis framework – are being investigated as potential therapeutics that slow down, or even prevent, loss of healthy proteostasis. A number of plant-derived polyphenols are assessed as potential promoters of proteostasis by monitoring their effect on proteasome activity, on expression levels of ubiquitin-proteasome (UPS) subunits, and on the heat shock response (HSR). A preliminary proteomics study was carried out to identify and quantify levels of UPS subunits, levels of HSR proteins, and other stress response proteins during exposure to a plant polyphenol. A number of small HSR proteins were upregulated in the presence of the polyphenol. There was no change in the levels of UPS subunits, however organismal proteasome activity was altered in a concentration dependent manner. The preliminary proteome study also identified additional stress-responsive pathways associated with exposure to plant polyphenols. Acknowledgements: National Institutes of Health.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26207759","pmcid":null,"openalex_id":"https://openalex.org/W2565851697","authors":[],"funders":[],"total_grants":0,"fwci":0.0,"citation_percentile":0.11692138,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":null,"oa_locations":[{"url":"http://www.thieme-connect.de/products/ejournals/html/10.1055/s-0036-1596420","host_type":"publisher"},{"url":"https://doi.org/10.1055/s-0036-1596420","host_type":"journal"}],"fields_of_study":["Endoplasmic Reticulum Stress and Disease","Ubiquitin and proteasome pathways","Autophagy in Disease and Therapy"],"mesh_terms":[],"keywords":["Proteostasis","Proteasome","Heat shock protein","Heat shock","Proteome","Biology","Cell biology","Ubiquitin","Oxidative stress","Proteomics","Biochemistry"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-18T17:30:56.728944Z","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":[]}