{"doi":"10.1126/science.aad2450","title":"Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer","abstract":"<jats:title>A more complete look at the HIV-1 envelope</jats:title>\n                  <jats:p>\n                    HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee\n                    <jats:italic>et al.</jats:italic>\n                    used cryo–electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts.\n                  </jats:p>\n                  <jats:p>\n                    <jats:italic>Science</jats:italic>\n                    , this issue p.\n                    <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" issue=\"6277\" page=\"1043\" related-article-type=\"in-this-issue\" vol=\"351\" xlink:href=\"10.1126/science.aad2450\">1043</jats:related-article>\n                  </jats:p>","journal":"Science","year":2016,"id":638303,"datarank":0.9190303776171279,"base_score":6.126869184114185,"endowment":6.126869184114185,"self_citation_contribution":0.9190303776171279,"citation_network_contribution":0.0,"self_endowment_contribution":0.9190303776171279,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":457,"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":230741,"name":"Gabriel Ozorowski","orcid":"0000-0002-9695-8138","position":1,"is_corresponding":false},{"id":106561,"name":"Andrew B. Ward","orcid":null,"position":2,"is_corresponding":false},{"id":318058,"name":"Jeong Hyun Lee","orcid":"0000-0001-7371-845X","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer","abstract":"<jats:title>A more complete look at the HIV-1 envelope</jats:title>\n                  <jats:p>\n                    HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee\n                    <jats:italic>et al.</jats:italic>\n                    used cryo–electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts.\n                  </jats:p>\n                  <jats:p>\n                    <jats:italic>Science</jats:italic>\n                    , this issue p.\n                    <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" issue=\"6277\" page=\"1043\" related-article-type=\"in-this-issue\" vol=\"351\" xlink:href=\"10.1126/science.aad2450\">1043</jats:related-article>\n                  </jats:p>","is_dataset_classified":null,"base_score":6.126869184114185,"endowment":6.126869184114185,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26941313","pmcid":"PMC5001164","openalex_id":"https://openalex.org/W2332658587","authors":[],"funders":[{"funder_name":"NIH","grant_id":"UM1 AI100663","title":null},{"funder_name":"Collaboration for AIDS Vaccine Discovery","grant_id":"OPP1084519","title":null},{"funder_name":"Collaboration for AIDS Vaccine Discovery","grant_id":"OPP1115782","title":null},{"funder_name":"U.S. Agency for International Development (USAID)","grant_id":"","title":null},{"funder_name":"Bill and Melinda Gates Foundation","grant_id":"","title":null},{"funder_name":"California HIV/AIDS Research Program Dissertation Award","grant_id":"","title":null},{"funder_name":"Ministry of Foreign Affairs of the Netherlands","grant_id":"","title":null}],"total_grants":7,"fwci":40.5569,"citation_percentile":0.99936174,"influential_citations":0,"citation_trend":[{"year":2016,"count":39},{"year":2017,"count":63},{"year":2018,"count":77},{"year":2019,"count":59},{"year":2020,"count":58},{"year":2021,"count":37},{"year":2022,"count":37},{"year":2023,"count":26},{"year":2024,"count":27},{"year":2025,"count":24},{"year":2026,"count":10}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://science.sciencemag.org/content/sci/351/6277/1043.full.pdf","host_type":"journal"},{"url":"https://science.sciencemag.org/content/sci/351/6277/1043.full.pdf","host_type":"publisher"},{"url":"https://www.science.org/doi/pdf/10.1126/science.aad2450","host_type":"publisher"},{"url":"https://doi.org/10.1126/science.aad2450","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/26941313","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/5001164","host_type":"repository"}],"fields_of_study":["HIV Research and Treatment","Cytomegalovirus and herpesvirus research","Bacteriophages and microbial interactions"],"mesh_terms":["Amino Acid Sequence","Antibodies, Monoclonal","Glycosylation","Humans","Molecular Sequence Data","HIV-1","HIV Envelope Protein gp120","HIV Envelope Protein gp41","Protein Structure, Tertiary","Crystallography, X-Ray","Virus Internalization","Protein Multimerization","Antibodies, Neutralizing","Hydrophobic and Hydrophilic Interactions"],"keywords":["Trimer","Glycoprotein","Human immunodeficiency virus (HIV)","Viral envelope","Envelope (radar)","Cryo-electron microscopy","Chemistry","Gp41","Cytoplasm","Protein structure","Viral protein","Antibody","Virology","Biophysics","Viral entry","Biology","Biochemistry","Viral replication","Virus","Epitope","Computer science","Genetics"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Good health and well-being"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"emdb"},{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-06T20:27:34.315551Z","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":[]}