{"doi":"10.1007/s00726-019-02710-9","title":"Crucial aminoacids in the FO sector of the F1FO-ATP synthase address H+ across the inner mitochondrial membrane: molecular implications in mitochondrial dysfunctions","abstract":null,"journal":"Amino Acids","year":2019,"id":595508,"datarank":0.26876392038420827,"base_score":1.791759469228055,"endowment":1.791759469228055,"self_citation_contribution":0.26876392038420827,"citation_network_contribution":0.0,"self_endowment_contribution":0.26876392038420827,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":5,"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":1524987,"name":"Alessandra Pagliarani","orcid":"0000-0002-0604-4587","position":1,"is_corresponding":false},{"id":1524988,"name":"Vittoria Ventrella","orcid":null,"position":2,"is_corresponding":false},{"id":1524989,"name":"Cristina Algieri","orcid":null,"position":3,"is_corresponding":false},{"id":1524990,"name":"Salvatore Nesci","orcid":"0000-0001-8569-7158","position":4,"is_corresponding":false},{"id":1524986,"name":"Fabiana Trombetti","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Crucial aminoacids in the FO sector of the F1FO-ATP synthase address H+ across the inner mitochondrial membrane: molecular implications in mitochondrial dysfunctions","abstract":"The eukaryotic F<sub>1</sub>F<sub>O</sub>-ATP synthase/hydrolase activity is coupled to H<sup>+</sup> translocation through the inner mitochondrial membrane. According to a recent model, two asymmetric H<sup>+</sup> half-channels in the a subunit translate a transmembrane vertical H<sup>+</sup> flux into the rotor rotation required for ATP synthesis/hydrolysis. Along the H<sup>+</sup> pathway, conserved aminoacid residues, mainly glutamate, address H<sup>+</sup> both in the downhill and uphill transmembrane movements to synthesize or hydrolyze ATP, respectively. Point mutations responsible for these aminoacid changes affect H<sup>+</sup> transfer through the membrane and, as a cascade, result in mitochondrial dysfunctions and related pathologies. The involvement of specific aminoacid residues in driving H<sup>+</sup> along their transmembrane pathway within a subunit, sustained by the literature and calculated data, leads to depict a model consistent with some mitochondrial disorders.","is_dataset_classified":null,"base_score":1.791759469228055,"endowment":1.791759469228055,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"30798467","pmcid":null,"openalex_id":"https://openalex.org/W2917307989","authors":[],"funders":[{"funder_name":"Università di Bologna","grant_id":"","title":null}],"total_grants":1,"fwci":0.3793,"citation_percentile":0.56481496,"influential_citations":0,"citation_trend":[{"year":2019,"count":2},{"year":2020,"count":3}],"oa_status":"green","license":"other-oa","oa_locations":[{"url":"http://hdl.handle.net/11585/684713","host_type":"repository"},{"url":"http://hdl.handle.net/11585/684713","host_type":"repository"},{"url":"http://link.springer.com/article/10.1007/s00726-019-02710-9/fulltext.html","host_type":"publisher"},{"url":"http://link.springer.com/content/pdf/10.1007/s00726-019-02710-9.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1007/s00726-019-02710-9","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/30798467","host_type":"repository"}],"fields_of_study":["ATP Synthase and ATPases Research","Mitochondrial Function and Pathology","Metabolism and Genetic Disorders","Amino Acids","Animals","Humans","Hydrogen","Hydrolysis","Mitochondria","Mitochondrial Membranes","Mitochondrial Proton-Translocating ATPases","Protein Conformation"],"mesh_terms":["Amino Acids","Animals","Humans","Hydrogen","Hydrolysis","Mitochondria","Protein Conformation","Mitochondrial Proton-Translocating ATPases","Mitochondrial Membranes"],"keywords":["ATP synthase","Inner mitochondrial membrane","ATP synthase gamma subunit","Transmembrane domain","Transmembrane protein","Protein subunit","Inner membrane","Mitochondrial carrier","ATP hydrolysis","ATP–ADP translocase","F-ATPase","Mitochondrion","Cell biology","Biochemistry","Biology","Chemistry","Biophysics","ATPase","Enzyme","Membrane","Bacterial outer membrane","Receptor","Gene","Mitochondrial Dysfunctions","F1fo-atp Synthase","Crucial Aminoacids","H+ Pathway","A Subunit"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-27T17:32:33.468710Z","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":[]}