{"doi":"10.1002/1873-3468.13245","title":"The role of chaperones in iron–sulfur cluster biogenesis","abstract":"<jats:p>Iron–sulfur cluster biogenesis is a complex process mediated by numerous proteins among which two from bacteria chaperones, called HscB and HscA in bacteria. They are highly conserved up to eukaryotes and homologous to DnaJ and DnaK, respectively, but with specific differences. As compared with other chaperones, HscB and HscA have escaped attention and relatively little is known about their functions. After briefly introducing the various chaperone families, we reviewed here the current structural and functional knowledge HscA and HscB and on their role in cluster formation. We critically evaluated the literature and highlighted the weak aspects which will require more attention in the future. We sincerely hope that this study will inspire new interest on this important and interesting system.</jats:p>","journal":"FEBS Letters","year":2018,"id":681045,"datarank":0.49983067652628066,"base_score":3.332204510175204,"endowment":3.332204510175204,"self_citation_contribution":0.49983067652628066,"citation_network_contribution":0.0,"self_endowment_contribution":0.49983067652628066,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":27,"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":1178358,"name":"Annalisa Pastore","orcid":"0000-0002-3047-654X","position":1,"is_corresponding":false},{"id":1779367,"name":"Rita Puglisi","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"The role of chaperones in iron–sulfur cluster biogenesis","abstract":"<jats:p>Iron–sulfur cluster biogenesis is a complex process mediated by numerous proteins among which two from bacteria chaperones, called HscB and HscA in bacteria. They are highly conserved up to eukaryotes and homologous to DnaJ and DnaK, respectively, but with specific differences. As compared with other chaperones, HscB and HscA have escaped attention and relatively little is known about their functions. After briefly introducing the various chaperone families, we reviewed here the current structural and functional knowledge HscA and HscB and on their role in cluster formation. We critically evaluated the literature and highlighted the weak aspects which will require more attention in the future. We sincerely hope that this study will inspire new interest on this important and interesting system.</jats:p>","is_dataset_classified":null,"base_score":3.332204510175204,"endowment":3.332204510175204,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"30194723","pmcid":"PMC6506825","openalex_id":"https://openalex.org/W2889873632","authors":[],"funders":[{"funder_name":"Biotechnology and Biological Sciences Research Council","grant_id":"BB/S001832/1","title":null},{"funder_name":"Medical Research Council","grant_id":"MC_PC_13054","title":null},{"funder_name":"Medical Research Council","grant_id":"MC_U117584256","title":null},{"funder_name":"Medical Research Council","grant_id":"UKDRI-6002","title":null},{"funder_name":"Medical Research Council","grant_id":"","title":null},{"funder_name":"Medical Research Council","grant_id":"","title":null}],"total_grants":6,"fwci":0.8597,"citation_percentile":0.69406778,"influential_citations":1,"citation_trend":[{"year":2019,"count":1},{"year":2020,"count":4},{"year":2021,"count":10},{"year":2022,"count":2},{"year":2023,"count":2},{"year":2024,"count":3},{"year":2025,"count":4},{"year":2026,"count":1}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"https://febs.onlinelibrary.wiley.com/doi/pdfdirect/10.1002/1873-3468.13245","host_type":"journal"},{"url":"https://febs.onlinelibrary.wiley.com/doi/pdfdirect/10.1002/1873-3468.13245","host_type":"HYBRID"},{"url":"https://febs.onlinelibrary.wiley.com/doi/pdfdirect/10.1002/1873-3468.13245","host_type":"publisher"},{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2F1873-3468.13245","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.13245","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/full-xml/10.1002/1873-3468.13245","host_type":"publisher"},{"url":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.13245","host_type":"publisher"},{"url":"https://doi.org/10.1002/1873-3468.13245","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/30194723","host_type":"repository"},{"url":"https://kclpure.kcl.ac.uk/portal/en/publications/7cc85458-4a6c-439e-86f8-5b05f8300f9b","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6506825","host_type":"repository"},{"url":"http://hdl.handle.net/11384/77922","host_type":"repository"},{"url":"https://kclpure.kcl.ac.uk/ws/files/101507474/The_role_of_chaperones_in_PUGLISI_Firstonline8September2018_GREEN_AAM.pdf","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC6506825","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC6506825?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Metalloenzymes and iron-sulfur proteins","Enzyme Structure and Function","Genomics and Phylogenetic Studies","Chemistry","Medicine","Biology","Bacterial Proteins","Escherichia coli","Escherichia coli Proteins","HSP70 Heat-Shock Proteins","Heat-Shock Proteins","Iron-Sulfur Proteins","Models, Molecular","Molecular Chaperones","Multigene Family","Protein Domains"],"mesh_terms":["Protein Domains","Bacterial Proteins","Escherichia coli","Multigene Family","Heat-Shock Proteins","Iron-Sulfur Proteins","Models, Molecular","Molecular Chaperones","HSP70 Heat-Shock Proteins","Escherichia coli Proteins"],"keywords":["Biogenesis","Iron–sulfur cluster","Co-chaperone","Chaperone (clinical)","Biology","Bacteria","Cluster (spacecraft)","Computational biology","Genetics","Cell biology","Biochemistry","Heat shock protein","Hsp90","Medicine","Gene","Computer science","Enzyme","Protein folding","Neurodegeneration","Structural Biology","Chaperones","Iron-sulfur Cluster"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T16:49:20.378135Z","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":[]}