{"doi":"10.1073/pnas.89.14.6570","title":"Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P.","abstract":"<jats:p>We have previously shown that phosphorylation of vesicular stomatitis virus (VSV) phosphoprotein P by cellular protein kinase activity is an essential prerequisite for its transcriptional function. We have now purified this protein kinase by monitoring its ability to phosphorylate bacterially expressed, unphosphorylated P protein. Biochemical studies showed that the kinase is indistinguishable from casein kinase II, a ubiquitous cyclic AMP-independent protein kinase present in a wide variety of eukaryotic cells and tissues. Functional VSV transcription could be reconstituted with viral L protein, N-RNA template, and P protein phosphorylated by either purified cellular protein kinase or purified casein kinase II. The unusual role of casein kinase II in the transcription process of a nonsegmented negative-strand RNA virus would have important implications in host-virus interactions and antiviral therapy.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1992,"id":641250,"datarank":0.7401710899696038,"base_score":4.9344739331306915,"endowment":4.9344739331306915,"self_citation_contribution":0.7401710899696038,"citation_network_contribution":0.0,"self_endowment_contribution":0.7401710899696038,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":138,"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":1667101,"name":"A K Banerjee","orcid":null,"position":1,"is_corresponding":false},{"id":1667100,"name":"S Barik","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P.","abstract":"<jats:p>We have previously shown that phosphorylation of vesicular stomatitis virus (VSV) phosphoprotein P by cellular protein kinase activity is an essential prerequisite for its transcriptional function. We have now purified this protein kinase by monitoring its ability to phosphorylate bacterially expressed, unphosphorylated P protein. Biochemical studies showed that the kinase is indistinguishable from casein kinase II, a ubiquitous cyclic AMP-independent protein kinase present in a wide variety of eukaryotic cells and tissues. Functional VSV transcription could be reconstituted with viral L protein, N-RNA template, and P protein phosphorylated by either purified cellular protein kinase or purified casein kinase II. The unusual role of casein kinase II in the transcription process of a nonsegmented negative-strand RNA virus would have important implications in host-virus interactions and antiviral therapy.</jats:p>","is_dataset_classified":null,"base_score":4.9344739331306915,"endowment":4.9344739331306915,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"1321444","pmcid":null,"openalex_id":"https://openalex.org/W2004363185","authors":[],"funders":[],"total_grants":0,"fwci":6.0782,"citation_percentile":0.96650965,"influential_citations":11,"citation_trend":[{"year":2012,"count":2},{"year":2013,"count":3},{"year":2014,"count":2},{"year":2015,"count":1},{"year":2016,"count":4},{"year":2019,"count":4},{"year":2020,"count":1},{"year":2021,"count":3},{"year":2022,"count":2},{"year":2023,"count":1},{"year":2024,"count":1},{"year":2025,"count":2},{"year":2026,"count":1}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://europepmc.org/articles/pmc49543?pdf=render","host_type":"GREEN"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.89.14.6570","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.89.14.6570","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/1321444","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/49543","host_type":"repository"}],"fields_of_study":["Virus-based gene therapy research","Virology and Viral Diseases","Cellular transport and secretion","Biology","Medicine"],"mesh_terms":["Capsid","Phosphoproteins","Phosphorylation","RNA-Dependent RNA Polymerase","Substrate Specificity","Transcription, Genetic","Vesicular stomatitis Indiana virus","Viral Core Proteins","Gene Expression Regulation, Viral","Protein Serine-Threonine Kinases","Viral Nonstructural Proteins","Casein Kinase II"],"keywords":["Casein kinase 2","Protein kinase R","Phosphoprotein","Vesicular stomatitis virus","Casein kinase 1","Biology","Cyclin-dependent kinase 9","MAP2K7","Cyclin-dependent kinase 2","Mitogen-activated protein kinase kinase","Protein kinase A","Casein kinase 2, alpha 1","Kinase","Biochemistry","c-Raf","Molecular biology","Rhabdoviridae","Phosphorylation","Virus","Virology"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-07T16:53:27.746750Z","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":[]}