{"doi":"10.1016/j.febslet.2010.11.011","title":"Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilisin nattokinase","abstract":"<jats:p>Here, we show that during in vivo folding of the precursor, the propeptide of subtilisin nattokinase functions as an intramolecular chaperone (IMC) that organises the in vivo folding of the subtilisin domain. Two residues belonging to β‐strands formed by conserved regions of the IMC are crucial for the folding of the subtilisin domain through direct interactions. An identical protease can fold into different conformations in vivo due to the action of a mutated IMC, resulting in different kinetic parameters. Some interfacial changes involving conserved regions, even those induced by the subtilisin domain, blocked subtilisin folding and altered its conformation. Insight into the interaction between the subtilisin and IMC domains is provided by a three‐dimensional structural model.</jats:p>","journal":"FEBS Letters","year":2010,"id":22390,"datarank":1.044827398071978,"base_score":3.044522437723423,"endowment":3.044522437723423,"self_citation_contribution":0.4566783656585135,"citation_network_contribution":0.5881490324134645,"self_endowment_contribution":0.4566783656585135,"citer_contribution":0.5881490324134645,"corpus_percentile":null,"corpus_rank":null,"citation_count":20,"citer_count":18,"citers_with_citation_signal":13,"citers_with_endowment":13,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":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":32551,"name":"Hui Liu","orcid":"0000-0003-0444-5579","position":1,"is_corresponding":false},{"id":116977,"name":"Wei Bao","orcid":null,"position":2,"is_corresponding":false},{"id":140912,"name":"Meizhi Weng","orcid":null,"position":3,"is_corresponding":false},{"id":109275,"name":"Wei Chen","orcid":"0000-0001-7196-8703","position":4,"is_corresponding":false},{"id":140913,"name":"Yongjun Cai","orcid":null,"position":5,"is_corresponding":false},{"id":140914,"name":"Zhongliang Zheng","orcid":null,"position":6,"is_corresponding":false},{"id":140915,"name":"Guolin Zou","orcid":null,"position":7,"is_corresponding":false},{"id":74137,"name":"Yan Jia","orcid":"0000-0003-1048-9842","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":3.044522437723423,"endowment":3.044522437723423,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"21074529","pmcid":null,"openalex_id":"https://openalex.org/W2026727532","authors":[],"funders":[],"total_grants":0,"fwci":0.4758,"citation_percentile":0.70300446,"influential_citations":0,"citation_trend":[{"year":2012,"count":3},{"year":2014,"count":1},{"year":2015,"count":1},{"year":2016,"count":1},{"year":2017,"count":1},{"year":2020,"count":2},{"year":2021,"count":2},{"year":2022,"count":1},{"year":2023,"count":4},{"year":2024,"count":2},{"year":2025,"count":1}],"oa_status":"bronze","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1016/j.febslet.2010.11.011","host_type":"journal"},{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1016/j.febslet.2010.11.011","host_type":"BRONZE"},{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1016/j.febslet.2010.11.011","host_type":"publisher"},{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2Fj.febslet.2010.11.011","host_type":"publisher"},{"url":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2010.11.011","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.febslet.2010.11.011","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/21074529","host_type":"repository"}],"fields_of_study":["Protease and Inhibitor Mechanisms","Advanced Proteomics Techniques and Applications","Enzyme Production and Characterization","Chemistry","Medicine","Biology","Amino Acid Sequence","Bacillus subtilis","Conserved Sequence","Kinetics","Molecular Chaperones","Molecular Dynamics Simulation","Molecular Sequence Data","Mutagenesis, Site-Directed","Mutation","Protein Folding","Protein Precursors","Protein Refolding","Protein Structure, Secondary","Protein Structure, Tertiary","Sequence Alignment","Sequence Homology, Amino Acid","Subtilisins"],"mesh_terms":["Amino Acid Sequence","Bacillus subtilis","Kinetics","Molecular Sequence Data","Mutation","Protein Precursors","Subtilisins","Mutagenesis, Site-Directed","Sequence Alignment","Conserved Sequence","Sequence Homology, Amino Acid","Protein Structure, Secondary","Protein Structure, Tertiary","Protein Folding","Molecular Chaperones","Molecular Dynamics Simulation","Protein Refolding"],"keywords":["Nattokinase","Subtilisin","Chaperone (clinical)","Chemistry","Protein precursor","Protein folding","Intramolecular force","In vivo","Biochemistry","Biology","Stereochemistry","Enzyme","Medicine"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-06T21:59:50.861805Z","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":[]}