{"doi":"10.1128/mcb.18.9.5229","title":"14-3-3 Proteins Are Required for Maintenance of Raf-1 Phosphorylation and Kinase Activity","abstract":null,"journal":"Molecular and Cellular Biology","year":1998,"id":609751,"datarank":0.813080249890843,"base_score":5.420534999272286,"endowment":5.420534999272286,"self_citation_contribution":0.813080249890843,"citation_network_contribution":0.0,"self_endowment_contribution":0.813080249890843,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":225,"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":1567367,"name":"Lily W. K. Yu","orcid":null,"position":1,"is_corresponding":false},{"id":1567368,"name":"Alice L. Hsu","orcid":null,"position":2,"is_corresponding":false},{"id":1567369,"name":"Neng-Yao Shih","orcid":null,"position":3,"is_corresponding":false},{"id":837172,"name":"Paul R. Graves","orcid":"0000-0002-4958-7450","position":4,"is_corresponding":false},{"id":1567370,"name":"J. William Tanner","orcid":null,"position":5,"is_corresponding":false},{"id":457488,"name":"Paul M. Allen","orcid":"0000-0003-3796-6047","position":6,"is_corresponding":false},{"id":62841,"name":"Helen Piwnica-Worms","orcid":null,"position":7,"is_corresponding":false},{"id":1567371,"name":"Andrey S. Shaw","orcid":null,"position":8,"is_corresponding":false},{"id":1567366,"name":"John A. Thorson","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"14-3-3 Proteins Are Required for Maintenance of Raf-1 Phosphorylation and Kinase Activity","abstract":"By binding to serine-phosphorylated proteins, 14-3-3 proteins function as effectors of serine phosphorylation. The exact mechanism of their action is, however, still largely unknown. Here we demonstrate a requirement for 14-3-3 for Raf-1 kinase activity and phosphorylation. Expression of dominant negative forms of 14-3-3 resulted in the loss of a critical Raf-1 phosphorylation, while overexpression of 14-3-3 resulted in enhanced phosphorylation of this site. 14-3-3 levels, therefore, regulate the stoichiometry of Raf-1 phosphorylation and its potential activity in the cell. Phosphorylation of Raf-1, however, was insufficient by itself for kinase activity. Removal of 14-3-3 from phosphorylated Raf abrogated kinase activity, whereas addition of 14-3-3 restored it. This supports a paradigm in which the effects of phosphorylation on serine as well as tyrosine residues are mediated by inducible protein-protein interactions.","is_dataset_classified":null,"base_score":5.420534999272286,"endowment":5.420534999272286,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"9710607","pmcid":"PMC109108","openalex_id":"https://openalex.org/W2155515046","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM047017","title":null},{"funder_name":"NIAID NIH HHS","grant_id":"AI54094","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM18428","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM47017","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"F32 GM018428","title":null}],"total_grants":5,"fwci":8.3775,"citation_percentile":0.98390209,"influential_citations":0,"citation_trend":[{"year":2012,"count":6},{"year":2013,"count":8},{"year":2014,"count":4},{"year":2015,"count":3},{"year":2016,"count":4},{"year":2017,"count":3},{"year":2018,"count":6},{"year":2019,"count":2},{"year":2020,"count":3},{"year":2021,"count":2},{"year":2022,"count":1},{"year":2023,"count":4},{"year":2024,"count":8},{"year":2025,"count":6},{"year":2026,"count":1}],"oa_status":"green","license":"https://journals.asm.org/non-commercial-tdm-license","oa_locations":[{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC109108/pdf/mb005229.pdf","host_type":"repository"},{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC109108/pdf/mb005229.pdf","host_type":"repository"},{"url":"https://journals.asm.org/doi/pdf/10.1128/MCB.18.9.5229","host_type":"publisher"},{"url":"https://www.tandfonline.com/doi/pdf/10.1128/MCB.18.9.5229","host_type":"publisher"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/109108","host_type":"repository"},{"url":"https://doi.org/10.1128/mcb.18.9.5229","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/9710607","host_type":"repository"},{"url":"http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.314.9744","host_type":""}],"fields_of_study":["14-3-3 protein interactions","Ubiquitin and proteasome pathways","Protein Tyrosine Phosphatases","14-3-3 Proteins","Amino Acid Sequence","Animals","Binding Sites","Cell Line","Chloramphenicol O-Acetyltransferase","Cloning, Molecular","Glutathione Transferase","Humans","Mice","Models, Molecular","Mutagenesis, Site-Directed","Phosphorylation","Phosphoserine","Phosphotyrosine","Polymerase Chain Reaction","Protein Biosynthesis","Protein Structure, Secondary","Proteins","Proto-Oncogene Proteins c-raf","Recombinant Fusion Proteins","Spectrum Analysis","Transfection","Tyrosine 3-Monooxygenase"],"mesh_terms":["Amino Acid Sequence","Animals","Binding Sites","Cell Line","Cloning, Molecular","Glutathione Transferase","Humans","Models, Molecular","Phosphorylation","Phosphoserine","Proteins","Recombinant Fusion Proteins","Spectrum Analysis","Transfection","Protein Biosynthesis","Tyrosine 3-Monooxygenase","Chloramphenicol O-Acetyltransferase","Polymerase Chain Reaction","Mutagenesis, Site-Directed","Protein Structure, Secondary","Phosphotyrosine","Proto-Oncogene Proteins c-raf","14-3-3 Proteins","Mice"],"keywords":["Phosphorylation","Phosphorylation cascade","Biology","Protein phosphorylation","Serine","Cell biology","Kinase","Protein kinase A","Biochemistry","Protein-Serine-Threonine Kinases"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-31T14:43:29.526250Z","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":[]}