{"doi":"10.1002/elps.201100565","title":"Proteome analysis of tunicamycin‐induced <scp>ER</scp> stress","abstract":"<jats:p>Endoplasmic reticulum (<jats:styled-content style=\"fixed-case\">ER</jats:styled-content>) stress occurs upon increased levels of unfolded proteins and results in activation of cellular responses such as the unfolded protein response (<jats:styled-content style=\"fixed-case\">UPR</jats:styled-content>) and <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>‐associated protein degradation (<jats:styled-content style=\"fixed-case\">ERAD</jats:styled-content>). To examine <jats:styled-content style=\"fixed-case\">ER</jats:styled-content> stress, we performed a quantitative proteome analysis of human neuroblastoma cells using stable isotope labeling with amino acids in cell culture (<jats:styled-content style=\"fixed-case\">SILAC</jats:styled-content>) in combination with <jats:styled-content style=\"fixed-case\">SDS</jats:styled-content>‐<jats:styled-content style=\"fixed-case\">PAGE</jats:styled-content> and <jats:styled-content style=\"fixed-case\">LC</jats:styled-content>‐<jats:styled-content style=\"fixed-case\">MS</jats:styled-content>/<jats:styled-content style=\"fixed-case\">MS</jats:styled-content>. Proteins associated with the <jats:styled-content style=\"fixed-case\">ER</jats:styled-content> were overrepresented in the dataset of altered proteins. In particular, <jats:styled-content style=\"fixed-case\">ER</jats:styled-content> chaperones responsible for protein folding were significantly upregulated in response to <jats:styled-content style=\"fixed-case\">ER</jats:styled-content> stress. The important <jats:styled-content style=\"fixed-case\">ER</jats:styled-content> stress regulator 78 k<jats:styled-content style=\"fixed-case\">D</jats:styled-content>a glucose‐regulated protein (<jats:styled-content style=\"fixed-case\">GRP</jats:styled-content>‐78 or <jats:styled-content style=\"fixed-case\">B</jats:styled-content>i<jats:styled-content style=\"fixed-case\">P</jats:styled-content>) was highly upregulated together with several proteins that have been found to form a multiprotein complex with <jats:styled-content style=\"fixed-case\">B</jats:styled-content>i<jats:styled-content style=\"fixed-case\">P</jats:styled-content> including cyclophilin <jats:styled-content style=\"fixed-case\">B</jats:styled-content>, <jats:styled-content style=\"fixed-case\">D</jats:styled-content>na<jats:styled-content style=\"fixed-case\">J</jats:styled-content> homolog subfamily <jats:styled-content style=\"fixed-case\">B</jats:styled-content> member 11, endoplasmin, hypoxia upregulated protein 1, protein disulfide isomerase and protein disulfide isomerase <jats:styled-content style=\"fixed-case\">A</jats:styled-content>4 upon tunicamycin‐induced <jats:styled-content style=\"fixed-case\">ER</jats:styled-content> stress. Furthermore, seven aminoacyl‐t<jats:styled-content style=\"fixed-case\">RNA</jats:styled-content> synthetases and five proteins belonging to the <jats:styled-content style=\"fixed-case\">S</jats:styled-content>ec61 complex were increased in response to tunicamycin‐induced <jats:styled-content style=\"fixed-case\">ER</jats:styled-content> stress.</jats:p>","journal":"ELECTROPHORESIS","year":2012,"id":22883,"datarank":3.827441921135637,"base_score":4.394449154672439,"endowment":4.394449154672439,"self_citation_contribution":0.6591673732008659,"citation_network_contribution":3.168274547934771,"self_endowment_contribution":0.6591673732008659,"citer_contribution":3.168274547934771,"corpus_percentile":null,"corpus_rank":null,"citation_count":80,"citer_count":80,"citers_with_citation_signal":68,"citers_with_endowment":68,"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":137006,"name":"Bernd Thiede","orcid":"0000-0002-2804-9522","position":1,"is_corresponding":false},{"id":142440,"name":"Vibeke Hervik Bull","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":4.394449154672439,"endowment":4.394449154672439,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"22740470","pmcid":null,"openalex_id":"https://openalex.org/W1507019195","authors":[],"funders":[],"total_grants":0,"fwci":3.0928,"citation_percentile":0.91343746,"influential_citations":3,"citation_trend":[{"year":2013,"count":7},{"year":2014,"count":5},{"year":2015,"count":10},{"year":2016,"count":6},{"year":2017,"count":5},{"year":2018,"count":4},{"year":2019,"count":4},{"year":2020,"count":4},{"year":2021,"count":7},{"year":2022,"count":10},{"year":2023,"count":4},{"year":2024,"count":8},{"year":2025,"count":4},{"year":2026,"count":2}],"oa_status":"closed","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Felps.201100565","host_type":"publisher"},{"url":"https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/pdf/10.1002/elps.201100565","host_type":"publisher"},{"url":"https://doi.org/10.1002/elps.201100565","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/22740470","host_type":"repository"}],"fields_of_study":["Endoplasmic Reticulum Stress and Disease","Signaling Pathways in Disease","Toxin Mechanisms and Immunotoxins","Biology","Medicine","Apoptosis","Cell Line, Tumor","Electrophoresis, Polyacrylamide Gel","Endoplasmic Reticulum","Endoplasmic Reticulum Stress","Humans","Isotope Labeling","Neuroblastoma","Protein Interaction Maps","Proteins","Proteome","Tandem Mass Spectrometry","Tunicamycin"],"mesh_terms":["Electrophoresis, Polyacrylamide Gel","Endoplasmic Reticulum","Humans","Isotope Labeling","Neuroblastoma","Proteins","Tunicamycin","Apoptosis","Proteome","Cell Line, Tumor","Tandem Mass Spectrometry","Endoplasmic Reticulum Stress","Protein Interaction Maps"],"keywords":["Tunicamycin","Unfolded protein response","Stable isotope labeling by amino acids in cell culture","Endoplasmic reticulum","Protein disulfide-isomerase","Proteome","Protein folding","Downregulation and upregulation","Endoplasmic-reticulum-associated protein degradation","Cell biology","Chemistry","Protein biosynthesis","Biochemistry","Biology","Proteomics"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-07T16:50:20.304379Z","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":[]}