{"doi":"10.1126/science.1227270","title":"Organization of the Influenza Virus Replication Machinery","abstract":"<jats:title>Influenza Revealed</jats:title>\n                  <jats:p>\n                    Influenza virus, a single-stranded RNA virus, is responsible for substantial morbidity and mortality worldwide. The influenza ribonucleoprotein (RNP) complex, which carries out viral replication and transcription, is central to the virus life-cycle and to viral host adaptation (see the Perspective by\n                    <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" issue=\"6114\" page=\"1545\" related-article-type=\"in-this-issue\" vol=\"338\" xlink:href=\"10.1126/science.1231588\">\n                      <jats:bold>Tao and Zheng</jats:bold>\n                    </jats:related-article>\n                    ). Structural characterization of the viral RNP has been challenging, but\n                    <jats:bold>\n                      Moeller\n                      <jats:italic>et al.</jats:italic>\n                    </jats:bold>\n                    (p.\n                    <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" page=\"1631\" related-article-type=\"in-this-issue\" vol=\"338\" xlink:href=\"10.1126/science.1227270\">1631</jats:related-article>\n                    , published online 22 November) and\n                    <jats:bold>\n                      Arranz\n                      <jats:italic>et al.</jats:italic>\n                    </jats:bold>\n                    (p.\n                    <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" page=\"1634\" related-article-type=\"in-this-issue\" vol=\"338\" xlink:href=\"10.1126/science.1228172\">1634</jats:related-article>\n                    , published online 22 November) now report the structure and assembly of this complex, using cryo-electron microscopy and negative-stain electron microscopy. The structures reveal how the viral polymerase, RNA genome, and nucleoprotein interact in the RNP providing insight into mechanisms for influenza genome replication and transcription.\n                  </jats:p>","journal":"Science","year":2012,"id":591813,"datarank":10.856030091196347,"base_score":5.568344503761097,"endowment":5.568344503761097,"self_citation_contribution":0.8352516755641646,"citation_network_contribution":10.020778415632183,"self_endowment_contribution":0.8352516755641646,"citer_contribution":10.020778415632183,"corpus_percentile":null,"corpus_rank":null,"citation_count":261,"citer_count":200,"citers_with_citation_signal":200,"citers_with_endowment":200,"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":558658,"name":"Robert N. Kirchdoerfer","orcid":"0000-0002-5974-2709","position":1,"is_corresponding":false},{"id":556157,"name":"Clinton S. Potter","orcid":"0000-0002-3287-121X","position":2,"is_corresponding":false},{"id":253673,"name":"Bridget Carragher","orcid":"0000-0002-0624-5020","position":3,"is_corresponding":false},{"id":105430,"name":"Ian A. Wilson","orcid":"0000-0002-6469-2419","position":4,"is_corresponding":false},{"id":1069539,"name":"Arne Moeller","orcid":"0000-0003-1101-5366","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Organization of the Influenza Virus Replication Machinery","abstract":"<jats:title>Influenza Revealed</jats:title>\n                  <jats:p>\n                    Influenza virus, a single-stranded RNA virus, is responsible for substantial morbidity and mortality worldwide. The influenza ribonucleoprotein (RNP) complex, which carries out viral replication and transcription, is central to the virus life-cycle and to viral host adaptation (see the Perspective by\n                    <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" issue=\"6114\" page=\"1545\" related-article-type=\"in-this-issue\" vol=\"338\" xlink:href=\"10.1126/science.1231588\">\n                      <jats:bold>Tao and Zheng</jats:bold>\n                    </jats:related-article>\n                    ). Structural characterization of the viral RNP has been challenging, but\n                    <jats:bold>\n                      Moeller\n                      <jats:italic>et al.</jats:italic>\n                    </jats:bold>\n                    (p.\n                    <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" page=\"1631\" related-article-type=\"in-this-issue\" vol=\"338\" xlink:href=\"10.1126/science.1227270\">1631</jats:related-article>\n                    , published online 22 November) and\n                    <jats:bold>\n                      Arranz\n                      <jats:italic>et al.</jats:italic>\n                    </jats:bold>\n                    (p.\n                    <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" page=\"1634\" related-article-type=\"in-this-issue\" vol=\"338\" xlink:href=\"10.1126/science.1228172\">1634</jats:related-article>\n                    , published online 22 November) now report the structure and assembly of this complex, using cryo-electron microscopy and negative-stain electron microscopy. The structures reveal how the viral polymerase, RNA genome, and nucleoprotein interact in the RNP providing insight into mechanisms for influenza genome replication and transcription.\n                  </jats:p>","is_dataset_classified":null,"base_score":5.568344503761097,"endowment":5.568344503761097,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23180774","pmcid":"PMC3578580","openalex_id":"https://openalex.org/W1996360948","authors":[],"funders":[{"funder_name":"NCRR NIH HHS","grant_id":"2P41RR017573-11","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"P50 GM073197","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM095573","title":null},{"funder_name":"NIAID NIH HHS","grant_id":"AI058113","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM095573","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"P41 GM103310","title":null},{"funder_name":"NIAID NIH HHS","grant_id":"P01 AI058113","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"9 P41 GM103310-11","title":null},{"funder_name":"NCRR NIH HHS","grant_id":"P41 RR017573","title":null}],"total_grants":9,"fwci":13.9734,"citation_percentile":0.99379948,"influential_citations":0,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":27},{"year":2014,"count":22},{"year":2015,"count":22},{"year":2016,"count":22},{"year":2017,"count":19},{"year":2018,"count":15},{"year":2019,"count":20},{"year":2020,"count":17},{"year":2021,"count":15},{"year":2022,"count":26},{"year":2023,"count":12},{"year":2024,"count":16},{"year":2025,"count":18},{"year":2026,"count":8}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://www.science.org/doi/pdf/10.1126/science.1227270","host_type":"publisher"},{"url":"https://doi.org/10.1126/science.1227270","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/23180774","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3578580","host_type":"repository"}],"fields_of_study":["Influenza Virus Research Studies","RNA and protein synthesis mechanisms","Respiratory viral infections research","Cryoelectron Microscopy","Crystallography, X-Ray","Genome, Viral","Image Processing, Computer-Assisted","Influenza A Virus, H1N1 Subtype","Microscopy, Electron","Models, Molecular","Nucleic Acid Conformation","Nucleocapsid Proteins","Protein Conformation","Protein Subunits","RNA, Viral","RNA-Binding Proteins","RNA-Dependent RNA Polymerase","Ribonucleoproteins","Transcription, Genetic","Viral Core Proteins","Viral Proteins","Virus Replication"],"mesh_terms":["Image Processing, Computer-Assisted","Microscopy, Electron","Models, Molecular","Nucleic Acid Conformation","Protein Conformation","Ribonucleoproteins","RNA-Dependent RNA Polymerase","RNA, Viral","Transcription, Genetic","Viral Core Proteins","Viral Proteins","Virus Replication","RNA-Binding Proteins","Genome, Viral","Crystallography, X-Ray","Nucleocapsid Proteins","Cryoelectron Microscopy","Protein Subunits","Influenza A Virus, H1N1 Subtype"],"keywords":["Nucleoprotein","Ribonucleoprotein","Virology","Viral replication","Biology","Virus","Polymerase","Influenza A virus","Transcription (linguistics)","Genome","RNA","Viral matrix protein","RNA polymerase","Cell biology","Genetics","Gene"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Good health and well-being"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-26T10:49:44.355226Z","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":[]}