{"doi":"10.1038/ncomms2909","title":"Mechanistic and environmental control of the prevalence and lifetime of amyloid oligomers","abstract":null,"journal":"Nature Communications","year":2013,"id":589232,"datarank":2.105621386075994,"base_score":3.6888794541139363,"endowment":3.6888794541139363,"self_citation_contribution":0.5533319181170905,"citation_network_contribution":1.5522894679589034,"self_endowment_contribution":0.5533319181170905,"citer_contribution":1.5522894679589034,"corpus_percentile":null,"corpus_rank":null,"citation_count":39,"citer_count":36,"citers_with_citation_signal":34,"citers_with_endowment":34,"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":1507548,"name":"Kym Eden","orcid":null,"position":1,"is_corresponding":false},{"id":1507549,"name":"Reuben Yarwood","orcid":null,"position":2,"is_corresponding":false},{"id":1507550,"name":"Line Jourdain","orcid":null,"position":3,"is_corresponding":false},{"id":995528,"name":"Rosalind J. Allen","orcid":"0000-0003-4110-2962","position":4,"is_corresponding":false},{"id":1213585,"name":"Cait E. MacPhee","orcid":"0000-0001-8313-8387","position":5,"is_corresponding":false},{"id":1507547,"name":"Ryan J. Morris","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Mechanistic and environmental control of the prevalence and lifetime of amyloid oligomers","abstract":"Amyloid fibrils are self-assembled protein aggregates implicated in a number of human diseases. Fragmentation-dominated models for the self-assembly of amyloid fibrils have had important successes in explaining the kinetics of amyloid fibril formation but predict fibril length distributions that do not match experiments. Here we resolve this inconsistency using a combination of experimental kinetic measurements and computer simulations. We provide evidence for a structural transition that occurs at a critical fibril mass concentration, or CFC, above which fragmentation of fibrils is suppressed. Our simulations predict the formation of distinct fibril length distributions above and below the CFC, which we confirm by electron microscopy. These results point to a new picture of amyloid fibril growth in which structural transitions that occur during self-assembly have strong effects on the final population of aggregate species with small, and potentially cytotoxic, oligomers dominating for long periods of time at protein concentrations below the CFC.","is_dataset_classified":null,"base_score":3.6888794541139363,"endowment":3.6888794541139363,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23695685","pmcid":null,"openalex_id":"https://openalex.org/W2025753714","authors":[],"funders":[{"funder_name":"UK Research and Innovation","grant_id":"BB/H013636/1","title":"Biophysical dissection of protein nucleation using a combined experimental and computational approach"},{"funder_name":"UK Research and Innovation","grant_id":"EP/J007404/1","title":"Design Principles for New Soft Materials"}],"total_grants":2,"fwci":2.6582,"citation_percentile":0.89826258,"influential_citations":0,"citation_trend":[{"year":2013,"count":2},{"year":2014,"count":3},{"year":2015,"count":7},{"year":2016,"count":4},{"year":2017,"count":4},{"year":2018,"count":4},{"year":2019,"count":1},{"year":2020,"count":7},{"year":2021,"count":3},{"year":2023,"count":2},{"year":2025,"count":2}],"oa_status":"bronze","license":"Springer Nature TDM","oa_locations":[{"url":"https://www.nature.com/articles/ncomms2909.pdf","host_type":"journal"},{"url":"https://www.nature.com/articles/ncomms2909.pdf","host_type":"publisher"},{"url":"https://www.nature.com/articles/ncomms2909","host_type":"publisher"},{"url":"https://doi.org/10.1038/ncomms2909","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/23695685","host_type":"repository"},{"url":"https://insu.hal.science/insu-02782113","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3796876","host_type":"repository"},{"url":"http://dx.doi.org/10.1038/ncomms2909","host_type":""},{"url":"https://dx.doi.org/10.1038/ncomms2909","host_type":""},{"url":"https://insu.hal.science/insu-02782113v1","host_type":""},{"url":"https://insu.hal.science/insu-02782113v1/document","host_type":""},{"url":"https://doi.org/https://doi.org/10.1038/ncomms2909","host_type":""}],"fields_of_study":["Alzheimer's disease research and treatments","Prion Diseases and Protein Misfolding","Supramolecular Self-Assembly in Materials","0301 basic medicine","0303 health sciences","03 medical and health sciences","Amyloid","Animals","Cattle","Computer Simulation","Humans","Insulin","Kinetics","Models, Molecular","Molecular Weight","Protein Structure, Quaternary","Sodium Chloride","Time Factors"],"mesh_terms":["Amyloid","Animals","Cattle","Computer Simulation","Humans","Insulin","Kinetics","Models, Molecular","Molecular Weight","Sodium Chloride","Time Factors","Protein Structure, Quaternary"],"keywords":["Fibril","Amyloid fibril","Fragmentation (computing)","Amyloid (mycology)","Biophysics","Kinetics","Chemistry","Protein aggregation","Amyloid β","Biochemistry","Biology","Medicine","Physics","Models, Molecular","Amyloid","Time Factors","[SDV.BBM]Life Sciences [q-bio]/Biochemistry","500","Sodium Chloride","530","Article","Molecular Weight","[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology","Animals","Humans","Insulin","Cattle","Computer Simulation","Protein Structure, Quaternary","Molecular Biology"],"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":"2026-07-23T14:56:18.723781Z","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":[]}