{"doi":"10.1006/viro.2000.0688","title":"Differential Roles of Two Conserved Glycine Residues in the Fusion Peptide of Semliki Forest Virus","abstract":null,"journal":"Virology","year":2001,"id":607380,"datarank":0.3958585994422889,"base_score":2.639057329615259,"endowment":2.639057329615259,"self_citation_contribution":0.3958585994422889,"citation_network_contribution":0.0,"self_endowment_contribution":0.3958585994422889,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":13,"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":328677,"name":"Margaret Kielian","orcid":"0000-0002-7395-4791","position":1,"is_corresponding":false},{"id":1559579,"name":"Swati Ghosh Shome","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Differential Roles of Two Conserved Glycine Residues in the Fusion Peptide of Semliki Forest Virus","abstract":"Semliki Forest Virus (SFV) is an enveloped alphavirus that infects cells by a low-pH-dependent membrane fusion reaction. SFV fusion is catalyzed by the spike protein E1 subunit, which contains a putative fusion peptide between residues 79 and 97. Prior mutagenesis studies demonstrated that an E1 G91D mutation blocks both virus-membrane fusion and the formation of a highly stable E1 trimer believed to be a critical fusion intermediate. We have here demonstrated that the G91D mutant was also inactive in hemifusion, suggesting that the E1 homotrimer is important in the initial stages of lipid mixing. Revertant analysis of a G91 deletion mutant indicated that G91 was crucial for the viability of SFV. In contrast, a G83D mutation produced infectious virus with both efficient fusion and homotrimer formation. Thus, the G83 position, although highly conserved among alphaviruses, was functional if replaced with a charged amino acid.","is_dataset_classified":null,"base_score":2.639057329615259,"endowment":2.639057329615259,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"11145898","pmcid":null,"openalex_id":"https://openalex.org/W2000593698","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM52929","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"T32 GM-07491","title":null},{"funder_name":"NCPDCID CDC HHS","grant_id":"NCI P30-CA-13330","title":null},{"funder_name":"National Institutes of Health","grant_id":"5T32GM007491-28","title":"Training in Cellular and Molecular Biology and Genetics"},{"funder_name":"National Institutes of Health","grant_id":"3P30CA013330-39S3","title":"Core Support for Cancer Center"},{"funder_name":"National Institutes of Health","grant_id":"5R01GM052929-12","title":"Molecular Analysis of Alphavirus Membrane Fusion Protein"}],"total_grants":6,"fwci":1.8551,"citation_percentile":0.85439249,"influential_citations":0,"citation_trend":[{"year":2016,"count":1},{"year":2022,"count":1}],"oa_status":"closed","license":"Elsevier Non-Commercial","oa_locations":[{"url":"https://doi.org/10.1006/viro.2000.0688","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/11145898","host_type":"repository"},{"url":"http://dx.doi.org/10.1006/viro.2000.0688","host_type":""},{"url":"https://dx.doi.org/10.1006/viro.2000.0688","host_type":""}],"fields_of_study":["Mosquito-borne diseases and control","Viral Infections and Vectors","Insect symbiosis and bacterial influences","0301 basic medicine","0303 health sciences","03 medical and health sciences","Amino Acid Sequence","Animals","Cell Line","Cricetinae","Glycine","Liposomes","Membrane Fusion","Molecular Sequence Data","Mutation","Peptides","Phenotype","Semliki forest virus","Transcription, Genetic","Viral Fusion Proteins","Virus Assembly"],"mesh_terms":["Amino Acid Sequence","Animals","Cell Line","Glycine","Cricetinae","Liposomes","Membrane Fusion","Molecular Sequence Data","Mutation","Peptides","Phenotype","Semliki forest virus","Transcription, Genetic","Viral Fusion Proteins","Virus Assembly"],"keywords":["Semliki Forest virus","Alphavirus","Biology","Lipid bilayer fusion","Sindbis virus","Togaviridae","Mutant","Virus","Amino acid","Mutagenesis","Virology","Biochemistry","RNA","Gene","Transcription, Genetic","Virus Assembly","Molecular Sequence Data","Glycine","Membrane Fusion","Cell Line","Phenotype","Cricetinae","Liposomes","Mutation","Animals","Amino Acid Sequence","Peptides","Viral Fusion Proteins"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. Good health"},{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-30T06:17:28.563596Z","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":[]}