{"doi":"10.1073/pnas.1600749113","title":"Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril","abstract":"<jats:title>Significance</jats:title>\n                  <jats:p>Alzheimer’s disease is the most prevalent neurodegenerative disease still with no known cure. The disease is characterized by the development of extracellular plaques and intracellular neurofibrillary tangles. The senile plaques consist mainly of the peptide amyloid-β (Aβ) in aggregated form, called amyloid fibrils. It is believed that the Aβ amyloid fibrils play an important role in disease progression and cell-to-cell transmissibility, and small Aβ oligomers are often assumed to be the most neurotoxic species. Here, we determined the 3D structure of a disease-relevant Aβ(1–42) fibril polymorph combining data from solid-state NMR spectroscopy and mass-per-length measurements from EM. The 3D structure is composed of two molecules per fibril layer, forming a double-horseshoe–like cross–β-sheet entity with maximally buried hydrophobic side chains.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2016,"id":661913,"datarank":1.0082138551185966,"base_score":6.721425700790643,"endowment":6.721425700790643,"self_citation_contribution":1.0082138551185966,"citation_network_contribution":0.0,"self_endowment_contribution":1.0082138551185966,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":829,"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":1727989,"name":"Francesco Ravotti","orcid":null,"position":1,"is_corresponding":false},{"id":1727990,"name":"Hiromi Arai","orcid":null,"position":2,"is_corresponding":false},{"id":1727993,"name":"Charles G. Glabe","orcid":null,"position":3,"is_corresponding":false},{"id":1727996,"name":"Joseph S. Wall","orcid":null,"position":4,"is_corresponding":false},{"id":677248,"name":"Anja Böckmann","orcid":"0000-0001-8149-7941","position":5,"is_corresponding":false},{"id":813436,"name":"Peter Güntert","orcid":"0000-0002-2911-7574","position":6,"is_corresponding":false},{"id":77130,"name":"Beat H. Meier","orcid":"0000-0002-9107-4464","position":7,"is_corresponding":false},{"id":85202,"name":"Roland Riek","orcid":"0000-0002-6333-066X","position":8,"is_corresponding":false},{"id":693556,"name":"Marielle Aulikki Wälti","orcid":"0000-0002-2458-9062","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril","abstract":"<jats:title>Significance</jats:title>\n                  <jats:p>Alzheimer’s disease is the most prevalent neurodegenerative disease still with no known cure. The disease is characterized by the development of extracellular plaques and intracellular neurofibrillary tangles. The senile plaques consist mainly of the peptide amyloid-β (Aβ) in aggregated form, called amyloid fibrils. It is believed that the Aβ amyloid fibrils play an important role in disease progression and cell-to-cell transmissibility, and small Aβ oligomers are often assumed to be the most neurotoxic species. Here, we determined the 3D structure of a disease-relevant Aβ(1–42) fibril polymorph combining data from solid-state NMR spectroscopy and mass-per-length measurements from EM. The 3D structure is composed of two molecules per fibril layer, forming a double-horseshoe–like cross–β-sheet entity with maximally buried hydrophobic side chains.</jats:p>","is_dataset_classified":null,"base_score":6.721425700790643,"endowment":6.721425700790643,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"27469165","pmcid":"PMC5003276","openalex_id":"https://openalex.org/W2487730443","authors":[],"funders":[{"funder_name":"Swiss National Science Foundation","grant_id":"200020_159707","title":null},{"funder_name":"Swiss National Science Foundation","grant_id":"200020_146757","title":null},{"funder_name":"Agence Nationale de la Recherche","grant_id":"ANR-11-BSV8-021-01","title":null},{"funder_name":"Agence Nationale de la Recherche","grant_id":"ANR-14-CE09-0024B","title":null},{"funder_name":"Swiss National Science Foundation","grant_id":"159707","title":"NMR studies in the Solid State"},{"funder_name":"Swiss National Science Foundation","grant_id":"200020","title":null},{"funder_name":"NIA NIH HHS","grant_id":"P01 AG000538","title":null},{"funder_name":"Swiss National Science Foundation","grant_id":"146757","title":"NMR studies in the Solid State"}],"total_grants":8,"fwci":71.9827,"citation_percentile":0.99977242,"influential_citations":0,"citation_trend":[{"year":2016,"count":20},{"year":2017,"count":114},{"year":2018,"count":120},{"year":2019,"count":100},{"year":2020,"count":112},{"year":2021,"count":93},{"year":2022,"count":82},{"year":2023,"count":64},{"year":2024,"count":49},{"year":2025,"count":57},{"year":2026,"count":17}],"oa_status":"bronze","license":"http://www.pnas.org/preview_site/misc/userlicense.xhtml","oa_locations":[{"url":"https://www.pnas.org/content/pnas/113/34/E4976.full.pdf","host_type":"journal"},{"url":"https://www.pnas.org/content/pnas/113/34/E4976.full.pdf","host_type":"publisher"},{"url":"http://www.pnas.org/syndication/doi/10.1073/pnas.1600749113","host_type":"publisher"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.1600749113","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.1600749113","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/27469165","host_type":"repository"},{"url":"https://www.osti.gov/biblio/1351799","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/5003276","host_type":"repository"},{"url":"https://hal.science/hal-03347517","host_type":"repository"},{"url":"https://escholarship.org/uc/item/9fh2c7xf","host_type":"repository"},{"url":"https://dx.doi.org/10.1073/pnas.1600749113","host_type":""},{"url":"https://sonar.ch/global/documents/181116","host_type":""},{"url":"https://escholarship.org/content/qt9fh2c7xf/qt9fh2c7xf.pdf","host_type":""},{"url":"https://doi.org/https://doi.org/10.1073/pnas.1600749113","host_type":""}],"fields_of_study":["Advanced NMR Techniques and Applications","Alzheimer's disease research and treatments","Advanced Neuroimaging Techniques and Applications","0301 basic medicine","03 medical and health sciences","Amyloid beta-Peptides","Cloning, Molecular","Escherichia coli","Gene Expression","Genetic Vectors","Humans","Microscopy, Electron","Models, Molecular","Nuclear Magnetic Resonance, Biomolecular","Peptide Fragments","Protein Conformation, beta-Strand","Recombinant Proteins"],"mesh_terms":["Protein Conformation, beta-Strand","Cloning, Molecular","Escherichia coli","Genetic Vectors","Humans","Microscopy, Electron","Models, Molecular","Peptide Fragments","Recombinant Proteins","Gene Expression","Amyloid beta-Peptides","Nuclear Magnetic Resonance, Biomolecular"],"keywords":["Fibril","Chemistry","Senile plaques","Amyloid (mycology)","Amyloid fibril","Biophysics","Crystallography","Residue (chemistry)","Biochemistry","Alzheimer's disease","Amyloid β","Biology","Pathology","Disease","Medicine","Amyloid","Alzheimer’s disease","Solid-state NMR","protein structure","Models, Molecular","570","Aging","Protein Conformation","1.1 Normal biological development and functioning","Nuclear Magnetic Resonance","Genetic Vectors","Gene Expression","Neurodegenerative","Electron","Models","616","Acquired Cognitive Impairment","Escherichia coli","2.1 Biological and endogenous factors","Humans","Cloning, Molecular","Nuclear Magnetic Resonance, Biomolecular","Microscopy","Amyloid beta-Peptides","Neurosciences","Alzheimer's Disease including Alzheimer's Disease Related Dementias (AD/ADRD)","Molecular","Biological Sciences","Peptide Fragments","Recombinant Proteins","Brain Disorders","Microscopy, Electron","Physical Sciences","Dementia","beta-Strand","Protein Conformation, beta-Strand","Biochemistry and Cell Biology","Cloning","Biomolecular"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. Good health"},{"sdg_number":13,"sdg_label":"13. Climate action"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T11:57:39.271317Z","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":[]}