{"doi":"10.1098/rstb.1995.0051","title":"Principles of chaperone-mediated protein folding","abstract":"<jats:title>Abstract</jats:title>\n                  <jats:p>The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.</jats:p>","journal":"Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences","year":1995,"id":22652,"datarank":1.1000265686661654,"base_score":2.70805020110221,"endowment":2.70805020110221,"self_citation_contribution":0.40620753016533157,"citation_network_contribution":0.6938190385008338,"self_endowment_contribution":0.40620753016533157,"citer_contribution":0.6938190385008338,"corpus_percentile":null,"corpus_rank":null,"citation_count":14,"citer_count":14,"citers_with_citation_signal":12,"citers_with_endowment":12,"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":141587,"name":"F. Ulrich Hartl","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":2.70805020110221,"endowment":2.70805020110221,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"7770479","pmcid":null,"openalex_id":"https://openalex.org/W2167924958","authors":[],"funders":[],"total_grants":0,"fwci":0.0,"citation_percentile":0.13157074,"influential_citations":1,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":1},{"year":2022,"count":1},{"year":2023,"count":2},{"year":2024,"count":1}],"oa_status":"closed","license":"https://royalsociety.org/journals/ethics-policies/data-sharing-mining/","oa_locations":[{"url":"https://royalsocietypublishing.org/doi/pdf/10.1098/rstb.1995.0051","host_type":"publisher"},{"url":"https://royalsocietypublishing.org/rstb/article-pdf/348/1323/107/83533/rstb.1995.0051.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1098/rstb.1995.0051","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/7770479","host_type":"repository"}],"fields_of_study":["Heat shock proteins research","Protein Structure and Dynamics","Enzyme Structure and Function","Biology","Medicine","Chemistry","Chaperonin 60","HSP70 Heat-Shock Proteins","Molecular Chaperones","Protein Conformation","Protein Folding"],"mesh_terms":["Protein Conformation","Protein Folding","Molecular Chaperones","Chaperonin 60","HSP70 Heat-Shock Proteins"],"keywords":["Co-chaperone","Chaperone (clinical)","Protein folding","HSP60","Heat shock protein","Hsp70","Chaperonin","Chemical chaperone","GroEL","Folding (DSP implementation)","Biology","Cell biology","Hsp90","Computational biology","Foldase","Chemistry","Biochemistry","Unfolded protein response","Gene","Endoplasmic reticulum"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-07T15:01:38.405466Z","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":[]}