{"doi":"10.1038/nsmb793","title":"Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit β-strand alignment","abstract":null,"journal":"Nature Structural & Molecular Biology","year":2004,"id":619581,"datarank":0.7772675325438129,"base_score":5.181783550292085,"endowment":5.181783550292085,"self_citation_contribution":0.7772675325438129,"citation_network_contribution":0.0,"self_endowment_contribution":0.7772675325438129,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":177,"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":1599006,"name":"Rodney K Tweten","orcid":null,"position":1,"is_corresponding":false},{"id":1599007,"name":"Arthur E Johnson","orcid":null,"position":2,"is_corresponding":false},{"id":329335,"name":"Rajesh Ramachandran","orcid":"0000-0002-4645-2841","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit β-strand alignment","abstract":"Cholesterol-dependent cytolysins are bacterial protein toxins that bind to cholesterol-containing membranes, form oligomeric complexes and insert into the bilayer to create large aqueous pores. Membrane-dependent structural rearrangements required to initiate the oligomerization of perfringolysin O monomers have been identified, as have the monomer-monomer interaction surfaces, using site-specific mutagenesis, disulfide trapping and multiple fluorescence techniques. Upon binding to the membrane, a structural element in perfringolysin O moves to expose the edge of a previously hidden beta-strand that forms the monomer-monomer interface and is required for oligomer assembly. The beta-strands that form the interface each contain a single aromatic residue, and these aromatics appear to stack, thereby aligning the transmembrane beta-hairpins of adjacent monomers in the proper register for insertion. Collectively, these data reveal a novel membrane binding-dependent mechanism for regulating cytolysin monomer-monomer association and pore formation.","is_dataset_classified":null,"base_score":5.181783550292085,"endowment":5.181783550292085,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"15235590","pmcid":null,"openalex_id":"https://openalex.org/W2045227909","authors":[],"funders":[{"funder_name":"NIAID NIH HHS","grant_id":"AI37657","title":null},{"funder_name":"NIAID NIH HHS","grant_id":"R01 AI037657","title":null}],"total_grants":2,"fwci":5.4335,"citation_percentile":0.96286534,"influential_citations":0,"citation_trend":[{"year":2012,"count":11},{"year":2013,"count":6},{"year":2014,"count":15},{"year":2015,"count":14},{"year":2016,"count":9},{"year":2017,"count":7},{"year":2018,"count":7},{"year":2019,"count":11},{"year":2020,"count":8},{"year":2021,"count":7},{"year":2022,"count":12},{"year":2023,"count":1},{"year":2024,"count":3},{"year":2025,"count":2},{"year":2026,"count":1}],"oa_status":"closed","license":"http://www.springer.com/tdm","oa_locations":[{"url":"http://www.nature.com/articles/nsmb793.pdf","host_type":"publisher"},{"url":"http://www.nature.com/articles/nsmb793","host_type":"publisher"},{"url":"https://doi.org/10.1038/nsmb793","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/15235590","host_type":"repository"}],"fields_of_study":["Antimicrobial Resistance in Staphylococcus","Streptococcal Infections and Treatments","Lipid Membrane Structure and Behavior","Bacterial Toxins","Cell Membrane","Cholesterol","Cross-Linking Reagents","Cytotoxins","DNA","Disulfides","Electrophoresis, Polyacrylamide Gel","Escherichia coli","Glycine","Hemolysin Proteins","Lipid Bilayers","Liposomes","Models, Molecular","Mutation","Peptides","Protein Binding","Protein Conformation","Protein Structure, Secondary","Protein Structure, Tertiary","Signal Transduction","Spectrometry, Fluorescence","Temperature","Time Factors","Tyrosine","Water"],"mesh_terms":["Bacterial Toxins","Cell Membrane","Cholesterol","Cross-Linking Reagents","Cytotoxins","Disulfides","DNA","Electrophoresis, Polyacrylamide Gel","Escherichia coli","Glycine","Hemolysin Proteins","Lipid Bilayers","Liposomes","Models, Molecular","Mutation","Peptides","Protein Binding","Protein Conformation","Spectrometry, Fluorescence","Temperature","Time Factors","Tyrosine","Water","Signal Transduction","Protein Structure, Secondary","Protein Structure, Tertiary"],"keywords":["Cytolysin","Monomer","Oligomer","Biophysics","Chemistry","Membrane","Transmembrane protein","Lipid bilayer","Protein structure","Biochemistry","Biology","Polymer chemistry"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Clean water and sanitation"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-03T07:39:52.603815Z","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":[]}