{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T21:32:31Z","timestamp":1793223151068,"version":"4.5.0"},"reference-count":111,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T00:00:00Z","timestamp":1787529600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2021\/10925-8"],"award-info":[{"award-number":["2021\/10925-8"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008353","name":"Funda\u00e7\u00e3o de Apoio ao Ensino, Pesquisa e Assist\u00eancia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008353","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01AG061708"],"award-info":[{"award-number":["R01AG061708"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007059","name":"Northwestern University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007059","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100017393","name":"Chemistry of Life Processes Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100017393","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.jbc.2026.113499","type":"journal-article","created":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T23:25:54Z","timestamp":1787786754000},"page":"113499","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Use of high-affinity scFv antibody NUsc1 for isolation and sensitive detection of Alzheimer\u2019s-associated amyloid beta oligomers"],"prefix":"10.1016","volume":"302","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7475-0259","authenticated-orcid":false,"given":"Raquel Maria de","family":"Campos","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1774-2719","authenticated-orcid":false,"given":"Mariane F\u00e1vero","family":"Carraro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andr\u00e9 Luiz Brand\u00e3o","family":"Bitencourt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2534-4593","authenticated-orcid":false,"given":"Joshua J.","family":"Jerisha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5546-912X","authenticated-orcid":false,"given":"Navid Jubaer","family":"Ayon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vuslat B.","family":"Juska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1693-2534","authenticated-orcid":false,"given":"Nathalia Reges","family":"Pinheiro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth A.","family":"Johnson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raghad N.","family":"Nowar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0527-8904","authenticated-orcid":false,"given":"John P.","family":"McGee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-9106-6382","authenticated-orcid":false,"given":"Mauro Exequiel","family":"Alfaro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9994-9296","authenticated-orcid":false,"given":"Maria Victoria","family":"Oberholzer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8058-615X","authenticated-orcid":false,"given":"Vanina","family":"Grippo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8062-4312","authenticated-orcid":false,"given":"Erika N.","family":"Cline","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9862-6436","authenticated-orcid":false,"given":"Kirsten L.","family":"Viola","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neil L.","family":"Kelleher","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Habif","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0407-7518","authenticated-orcid":false,"given":"Diana Alicia","family":"Jerusalinsky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gajendra S.","family":"Shekhawat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Morgan B.","family":"Elmor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8810-620X","authenticated-orcid":false,"given":"James J.","family":"Lah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Allan I.","family":"Levey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William L.","family":"Klein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adriano","family":"Sebollela","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.113499_bib1","first-page":"152","article-title":"2025 alzheimer\u2019s disease facts and figures","volume":"21","year":"2025","journal-title":"Alzheimer's Demen."},{"key":"10.1016\/j.jbc.2026.113499_bib2","doi-asserted-by":"crossref","first-page":"10417","DOI":"10.1073\/pnas.1834302100","article-title":"Alzheimer\u2019s disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss","volume":"100","author":"Gong","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113499_bib3","doi-asserted-by":"crossref","first-page":"6448","DOI":"10.1073\/pnas.95.11.6448","article-title":"Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins","volume":"95","author":"Lambert","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113499_bib4","doi-asserted-by":"crossref","first-page":"S567","DOI":"10.3233\/JAD-179941","article-title":"The amyloid-beta oligomer hypothesis: beginning of the third decade","volume":"64","author":"Cline","year":"2018","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.jbc.2026.113499_bib5","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1006\/exnr.1995.1080","article-title":"Clusterin (apoJ) alters the aggregation of amyloid beta-peptide (A beta 1-42) and forms slowly sedimenting A beta complexes that cause oxidative stress","volume":"136","author":"Oda","year":"1995","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.jbc.2026.113499_bib6","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1126\/science.1072994","article-title":"The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics","volume":"297","author":"Hardy","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113499_bib7","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1039\/C6CS00731G","article-title":"Towards an understanding of amyloid-beta oligomers: characterization, toxicity mechanisms, and inhibitors","volume":"46","author":"Lee","year":"2017","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jbc.2026.113499_bib8","doi-asserted-by":"crossref","first-page":"8920","DOI":"10.3390\/ijms21238920","article-title":"Antibody fragments as tools for elucidating structure-toxicity relationships and for diagnostic\/therapeutic targeting of neurotoxic amyloid oligomers","volume":"21","author":"Bitencourt","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.113499_bib9","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1111\/jnc.14118","article-title":"A human scFv antibody that targets and neutralizes high molecular weight pathogenic amyloid-beta oligomers","volume":"142","author":"Sebollela","year":"2017","journal-title":"J. Neurochem."},{"key":"10.1016\/j.jbc.2026.113499_bib10","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.ymthe.2022.11.002","article-title":"AAV-mediated neuronal expression of an scFv antibody selective for Abeta oligomers protects synapses and rescues memory in Alzheimer models","volume":"31","author":"Selles","year":"2023","journal-title":"Mol. Ther."},{"key":"10.1016\/j.jbc.2026.113499_bib11","first-page":"1","article-title":"Memory recovery through gene therapy with a single chain antibody fragment selective for A\u03b2 oligomers in a model of Alzheimer\u2019s disease in rats","volume":"4","author":"Colettis","year":"2023","journal-title":"J. Appl. Cogn. Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib12","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1021\/cn300122k","article-title":"Synapse-binding subpopulations of Abeta oligomers sensitive to peptide assembly blockers and scFv antibodies","volume":"3","author":"Velasco","year":"2012","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib13","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.imlet.2019.06.009","article-title":"Trends in therapeutic antibody affinity maturation: from in-vitro towards next-generation sequencing approaches","volume":"212","author":"Tabasinezhad","year":"2019","journal-title":"Immunol. Lett."},{"key":"10.1016\/j.jbc.2026.113499_bib14","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.jsb.2004.08.002","article-title":"The binding of thioflavin-T to amyloid fibrils: localisation and implications","volume":"149","author":"Krebs","year":"2005","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jbc.2026.113499_bib15","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/nsmb.1799","article-title":"Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils","volume":"17","author":"Ahmed","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113499_bib16","doi-asserted-by":"crossref","first-page":"7509","DOI":"10.1021\/jacs.5b03997","article-title":"High resolution structural characterization of Abeta42 amyloid fibrils by magic angle spinning NMR","volume":"137","author":"Colvin","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2026.113499_bib17","doi-asserted-by":"crossref","first-page":"25945","DOI":"10.1074\/jbc.274.36.25945","article-title":"Amyloid \u03b2-protein fibrillogenesis -: structure and biological activity of protofibrillar intermediates","volume":"274","author":"Walsh","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113499_bib18","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nsmb.2991","article-title":"Abeta(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer\u2019s disease","volume":"22","author":"Xiao","year":"2015","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113499_bib19","doi-asserted-by":"crossref","first-page":"4197","DOI":"10.1021\/acs.biochem.5b00467","article-title":"Mechanism of nucleated conformational conversion of Abeta42","volume":"54","author":"Fu","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.113499_bib20","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1038\/nchembio.624","article-title":"Amyloid-beta forms fibrils by nucleated conformational conversion of oligomers","volume":"7","author":"Lee","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2026.113499_bib21","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1111\/jnc.14647","article-title":"A novel crosslinking protocol stabilizes amyloid beta oligomers capable of inducing alzheimer\u2019s-associated pathologies","volume":"148","author":"Cline","year":"2019","journal-title":"J. Neurochem."},{"key":"10.1016\/j.jbc.2026.113499_bib22","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1016\/j.bbamem.2017.05.012","article-title":"Lipid membranes catalyse the fibril formation of the amyloid-beta (1-42) peptide through lipid-fibril interactions that reinforce secondary pathways","volume":"1859","author":"Lindberg","year":"2017","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.jbc.2026.113499_bib23","doi-asserted-by":"crossref","first-page":"445","DOI":"10.4161\/mabs.20776","article-title":"Molecular engineering of antibodies for therapeutic and diagnostic purposes","volume":"4","author":"Ducancel","year":"2012","journal-title":"MAbs"},{"key":"10.1016\/j.jbc.2026.113499_bib24","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1007\/s13311-013-0187-4","article-title":"Developing therapeutic antibodies for neurodegenerative disease","volume":"10","author":"Yu","year":"2013","journal-title":"Neurotherapeutics"},{"key":"10.1016\/j.jbc.2026.113499_bib25","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1038\/s41573-022-00501-8","article-title":"Avidity in antibody effector functions and biotherapeutic drug design","volume":"21","author":"Oostindie","year":"2022","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.jbc.2026.113499_bib26","doi-asserted-by":"crossref","first-page":"12202","DOI":"10.1021\/acsnano.7b05434","article-title":"Nanoscale dynamics of amyloid beta-42 oligomers as revealed by high-speed atomic force microscopy","volume":"11","author":"Banerjee","year":"2017","journal-title":"ACS Nano"},{"key":"10.1016\/j.jbc.2026.113499_bib27","doi-asserted-by":"crossref","first-page":"7831","DOI":"10.1073\/pnas.1916452117","article-title":"Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy","volume":"117","author":"Konno","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113499_bib28","doi-asserted-by":"crossref","first-page":"22829","DOI":"10.1038\/srep22829","article-title":"Quantitative thermophoretic study of disease-related protein aggregates","volume":"6","author":"Wolff","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2026.113499_bib29","doi-asserted-by":"crossref","first-page":"1896","DOI":"10.1021\/jasms.0c00160","article-title":"Internal fragments generated by electron ionization dissociation enhance protein top-down mass spectrometry","volume":"31","author":"Zenaidee","year":"2020","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.jbc.2026.113499_bib30","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1111\/joim.12816","article-title":"Biomarkers for Alzheimer's disease: current status and prospects for the future","volume":"284","author":"Blennow","year":"2018","journal-title":"J. Intern. Med."},{"key":"10.1016\/j.jbc.2026.113499_bib31","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1586\/14737159.2015.1002469","article-title":"Genetic diagnosis and prognosis of Alzheimer's disease: challenges and opportunities","volume":"15","author":"Reitz","year":"2015","journal-title":"Expert Rev. Mol. Diagn."},{"key":"10.1016\/j.jbc.2026.113499_bib32","doi-asserted-by":"crossref","DOI":"10.1016\/j.lanhl.2024.07.013","article-title":"Challenges in the practical implementation of blood biomarkers for Alzheimer\u2019s disease","volume":"5","author":"Scholl","year":"2024","journal-title":"Lancet Healthy Longev."},{"key":"10.1016\/j.jbc.2026.113499_bib33","doi-asserted-by":"crossref","DOI":"10.1016\/j.heliyon.2022.e09239","article-title":"Nucleic acid liquid biopsies in Alzheimer\u2019s disease: current state, challenges, and opportunities","volume":"8","author":"Soelter","year":"2022","journal-title":"Heliyon"},{"key":"10.1016\/j.jbc.2026.113499_bib34","doi-asserted-by":"crossref","first-page":"6412","DOI":"10.1038\/s41598-018-24501-0","article-title":"Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-beta","volume":"8","author":"Arndt","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2026.113499_bib35","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1007\/s13311-022-01308-6","article-title":"Lecanemab, aducanumab, and gantenerumab - binding profiles to different forms of amyloid-beta might explain efficacy and side effects in clinical trials for Alzheimer\u2019s disease","volume":"20","author":"S\u00f6derberg","year":"2023","journal-title":"Neurotherapeutics"},{"key":"10.1016\/j.jbc.2026.113499_bib36","doi-asserted-by":"crossref","DOI":"10.1016\/j.mcn.2024.103949","article-title":"Lecanemab demonstrates highly selective binding to Abeta protofibrils isolated from Alzheimer\u2019s disease brains","volume":"130","author":"Johannesson","year":"2024","journal-title":"Mol. Cell Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib37","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1016\/j.neuron.2012.10.029","article-title":"A plaque-specific antibody clears existing beta-amyloid plaques in Alzheimer\u2019s disease mice","volume":"76","author":"Demattos","year":"2012","journal-title":"Neuron"},{"key":"10.1016\/j.jbc.2026.113499_bib38","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.omto.2021.08.005","article-title":"Extending traditional antibody therapies: novel discoveries in immunotherapy and clinical applications","volume":"22","author":"Shin","year":"2021","journal-title":"Mol. Ther. Oncolytics"},{"key":"10.1016\/j.jbc.2026.113499_bib39","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1080\/19420862.2015.1113360","article-title":"Pharmacokinetic properties of IgG and various Fc fusion proteins in mice","volume":"8","author":"Unverdorben","year":"2016","journal-title":"MAbs"},{"key":"10.1016\/j.jbc.2026.113499_bib40","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/alzrt36","article-title":"The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?","volume":"2","author":"Broersen","year":"2010","journal-title":"Alzheimers Res. Ther."},{"key":"10.1016\/j.jbc.2026.113499_bib41","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1002\/alz.12084","article-title":"The biogenesis and biology of amyloid beta oligomers in the brain","volume":"16","author":"Ashe","year":"2020","journal-title":"Alzheimers Dement."},{"key":"10.1016\/j.jbc.2026.113499_bib42","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.jmb.2012.01.055","article-title":"Turn nucleation perturbs amyloid beta self-assembly and cytotoxicity","volume":"421","author":"Doran","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113499_bib43","doi-asserted-by":"crossref","first-page":"e2404916","DOI":"10.1002\/advs.202404916","article-title":"Secondary nucleation of abeta revealed by single-molecule and computational approaches","volume":"11","author":"Meyer","year":"2024","journal-title":"Adv. Sci. (Weinh)"},{"key":"10.1016\/j.jbc.2026.113499_bib44","doi-asserted-by":"crossref","first-page":"9384","DOI":"10.1073\/pnas.1401564111","article-title":"Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Abeta40 and Abeta42 peptides","volume":"111","author":"Meisl","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113499_bib45","doi-asserted-by":"crossref","first-page":"8876","DOI":"10.1523\/JNEUROSCI.19-20-08876.1999","article-title":"Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons","volume":"19","author":"Hartley","year":"1999","journal-title":"J. Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib46","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1111\/j.1742-4658.2007.05647.x","article-title":"Docosahexaenoic acid stabilizes soluble amyloid-beta protofibrils and sustains amyloid-beta-induced neurotoxicity in vitro","volume":"274","author":"Johansson","year":"2007","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2026.113499_bib47","doi-asserted-by":"crossref","first-page":"952","DOI":"10.3390\/ijms21030952","article-title":"Protofibrils of amyloid-beta are important targets of a disease-modifying approach for Alzheimer's disease","volume":"21","author":"Ono","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.113499_bib48","doi-asserted-by":"crossref","first-page":"5481","DOI":"10.1038\/s41380-021-01249-0","article-title":"The amyloid-beta pathway in Alzheimer\u2019s disease","volume":"26","author":"Hampel","year":"2021","journal-title":"Mol. Psychiatry"},{"key":"10.1016\/j.jbc.2026.113499_bib49","article-title":"A possible mechanism for the enhanced toxicity of beta-amyloid protofibrils in Alzheimer\u2019s disease","volume":"120","author":"Chen","year":"2023","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113499_bib50","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.bbrc.2012.10.129","article-title":"Soluble oligomers and fibrillar species of amyloid beta-peptide differentially affect cognitive functions and hippocampal inflammatory response","volume":"429","author":"He","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2026.113499_bib51","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/0197-4580(95)02020-9","article-title":"Deposits of A beta fibrils are not toxic to cortical and hippocampal neurons in vitro","volume":"17","author":"Wujek","year":"1996","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.jbc.2026.113499_bib52","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1186\/s12974-015-0379-4","article-title":"An N-terminal antibody promotes the transformation of amyloid fibrils into oligomers and enhances the neurotoxicity of amyloid-beta: the dust-raising effect","volume":"12","author":"Liu","year":"2015","journal-title":"J. Neuroinflammation"},{"key":"10.1016\/j.jbc.2026.113499_bib53","doi-asserted-by":"crossref","first-page":"4109","DOI":"10.1073\/pnas.94.8.4109","article-title":"Disaggregation of Alzheimer beta-amyloid by site-directed mAb","volume":"94","author":"Solomon","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113499_bib54","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2023.1208059","article-title":"Amyloid fibrils degradation: the pathway to recovery or aggravation of the disease?","volume":"10","author":"Sulatsky","year":"2023","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jbc.2026.113499_bib55","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-024-66970-6","article-title":"Targeting soluble amyloid-beta oligomers with a novel nanobody","volume":"14","author":"Haynes","year":"2024","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2026.113499_bib56","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2023.1108715","article-title":"Methods for the isolation and analysis of Abeta from postmortem brain","volume":"17","author":"Hong","year":"2023","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib57","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1038\/nm1782","article-title":"Amyloid-beta protein dimers isolated directly from Alzheimer\u2019s brains impair synaptic plasticity and memory","volume":"14","author":"Shankar","year":"2008","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2026.113499_bib58","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/978-1-60761-744-0_3","article-title":"Isolation of low-n amyloid beta-protein oligomers from cultured cells, CSF, and brain","volume":"670","author":"Shankar","year":"2011","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113499_bib59","doi-asserted-by":"crossref","first-page":"10831","DOI":"10.1021\/bi001048s","article-title":"The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain","volume":"39","author":"Walsh","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.113499_bib60","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1038\/416535a","article-title":"Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo","volume":"416","author":"Walsh","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113499_bib61","doi-asserted-by":"crossref","first-page":"5814","DOI":"10.1038\/s41467-022-33030-4","article-title":"IgG-like bispecific antibodies with potent and synergistic neutralization against circulating SARS-CoV-2 variants of concern","volume":"13","author":"Chang","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113499_bib62","doi-asserted-by":"crossref","first-page":"5255","DOI":"10.1038\/s41467-024-49625-y","article-title":"The binding mechanism of an anti-multiple myeloma antibody to the human GPRC5D homodimer","volume":"15","author":"Yan","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113499_bib63","doi-asserted-by":"crossref","first-page":"2301","DOI":"10.1038\/s41467-019-10247-4","article-title":"Atomic resolution cryo-EM structure of a native-like CENP-A nucleosome aided by an antibody fragment","volume":"10","author":"Zhou","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113499_bib64","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1080\/13506120500106958","article-title":"Neurotoxic protein oligomers--what you see is not always what you get","volume":"12","author":"Bitan","year":"2005","journal-title":"Amyloid"},{"key":"10.1016\/j.jbc.2026.113499_bib65","doi-asserted-by":"crossref","first-page":"4215","DOI":"10.1021\/ac400023c","article-title":"Analysis of protein aggregation in neurodegenerative disease","volume":"85","author":"Pedersen","year":"2013","journal-title":"Anal. Chem."},{"key":"10.1016\/j.jbc.2026.113499_bib66","doi-asserted-by":"crossref","first-page":"3038","DOI":"10.3390\/ijms13033038","article-title":"Unraveling the early events of amyloid-beta protein (Abeta) aggregation: techniques for the determination of Abeta aggregate size","volume":"13","author":"Pryor","year":"2012","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.113499_bib67","doi-asserted-by":"crossref","DOI":"10.1038\/srep14809","article-title":"SDS-PAGE analysis of Abeta oligomers is disserving research into Alzheimer s disease: appealing for ESI-IM-MS","volume":"5","author":"Pujol-Pina","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2026.113499_bib68","doi-asserted-by":"crossref","first-page":"1238","DOI":"10.1021\/cn500156r","article-title":"Elucidating molecular mass and shape of a neurotoxic Abeta oligomer","volume":"5","author":"Sebollela","year":"2014","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib69","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1111\/j.1471-4159.2005.03407.x","article-title":"Globular amyloid beta-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer\u2019s disease","volume":"95","author":"Barghorn","year":"2005","journal-title":"J. Neurochem."},{"key":"10.1016\/j.jbc.2026.113499_bib70","doi-asserted-by":"crossref","first-page":"15938","DOI":"10.1073\/pnas.0908176106","article-title":"Reelin signaling antagonizes beta-amyloid at the synapse","volume":"106","author":"Durakoglugil","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113499_bib71","doi-asserted-by":"crossref","first-page":"191","DOI":"10.3389\/fncel.2015.00191","article-title":"Soluble amyloid-beta oligomers as synaptotoxins leading to cognitive impairment in Alzheimer\u2019s disease","volume":"9","author":"Ferreira","year":"2015","journal-title":"Front Cell Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib72","doi-asserted-by":"crossref","first-page":"2716","DOI":"10.1096\/fj.09-150359","article-title":"High-molecular-weight beta-amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients","volume":"24","author":"Fukumoto","year":"2010","journal-title":"FASEB J."},{"key":"10.1016\/j.jbc.2026.113499_bib73","doi-asserted-by":"crossref","first-page":"10191","DOI":"10.1523\/JNEUROSCI.3432-04.2004","article-title":"Synaptic targeting by alzheimer\u2019s-related amyloid beta oligomers","volume":"24","author":"Lacor","year":"2004","journal-title":"J. Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib74","doi-asserted-by":"crossref","first-page":"32895","DOI":"10.1074\/jbc.M109.000208","article-title":"Isolation and characterization of patient-derived, toxic, high mass amyloid beta-protein (Abeta) assembly from Alzheimer disease brains","volume":"284","author":"Noguchi","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113499_bib75","doi-asserted-by":"crossref","first-page":"9220","DOI":"10.1096\/fj.201900604R","article-title":"High molecular weight amyloid beta(1-42) oligomers induce neurotoxicity via plasma membrane damage","volume":"33","author":"Yasumoto","year":"2019","journal-title":"FASEB J."},{"key":"10.1016\/j.jbc.2026.113499_bib76","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1111\/j.1582-4934.2011.01306.x","article-title":"High-molecular weight Abeta oligomers and protofibrils are the predominant Abeta species in the native soluble protein fraction of the AD brain","volume":"16","author":"Upadhaya","year":"2012","journal-title":"J. Cell Mol. Med."},{"key":"10.1016\/j.jbc.2026.113499_bib77","doi-asserted-by":"crossref","first-page":"12749","DOI":"10.1021\/bi030029q","article-title":"Self-assembly of Abeta(1-42) into globular neurotoxins","volume":"42","author":"Chromy","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.113499_bib78","doi-asserted-by":"crossref","first-page":"69","DOI":"10.3389\/fmolb.2020.00069","article-title":"AFM probing of amyloid-beta 42 dimers and trimers","volume":"7","author":"Maity","year":"2020","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jbc.2026.113499_bib79","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.jmb.2006.01.042","article-title":"High-resolution atomic force microscopy of soluble Abeta42 oligomers","volume":"358","author":"Mastrangelo","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113499_bib80","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0035443","article-title":"The influence of spin-labeled fluorene compounds on the assembly and toxicity of the abeta peptide","volume":"7","author":"Petrlova","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.113499_bib81","doi-asserted-by":"crossref","first-page":"1690","DOI":"10.1016\/j.bpj.2024.05.012","article-title":"Protective effect of trehalose sugar on amyloid-membrane interactions using BLM electrophysiology","volume":"123","author":"Xu","year":"2024","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2026.113499_bib82","doi-asserted-by":"crossref","first-page":"8422","DOI":"10.1021\/acs.analchem.9b01316","article-title":"Binary structure of amyloid beta oligomers revealed by dual recognition mapping","volume":"91","author":"Yoon","year":"2019","journal-title":"Anal. Chem."},{"key":"10.1016\/j.jbc.2026.113499_bib83","doi-asserted-by":"crossref","DOI":"10.3390\/ijms232315036","article-title":"Synthetic, cell-derived, brain-derived, and recombinant beta-Amyloid: modelling Alzheimer\u2019s disease for research and drug development","volume":"23","author":"Varshavskaya","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.113499_bib84","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1038\/nchem.247","article-title":"Amyloid-beta protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer\u2019s disease","volume":"1","author":"Bernstein","year":"2009","journal-title":"Nat. Chem."},{"key":"10.1016\/j.jbc.2026.113499_bib85","doi-asserted-by":"crossref","first-page":"3014","DOI":"10.1038\/s41467-020-16566-1","article-title":"Abeta(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage","volume":"11","author":"Ciudad","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113499_bib86","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2219216120","article-title":"Probing differences among Abeta oligomers with two triangular trimers derived from Abeta","volume":"120","author":"Kreutzer","year":"2023","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113499_bib87","doi-asserted-by":"crossref","first-page":"15595","DOI":"10.1073\/pnas.1001740107","article-title":"Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering","volume":"107","author":"Sandberg","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113499_bib88","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1021\/acs.biochem.1c00739","article-title":"A disulfide-stabilized abeta that forms dimers but does not form fibrils","volume":"61","author":"Zhang","year":"2022","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.113499_bib89","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/S1474-4422(21)00066-1","article-title":"Clinical diagnosis of Alzheimer\u2019s disease: recommendations of the International Working Group","volume":"20","author":"Dubois","year":"2021","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.jbc.2026.113499_bib90","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1212\/WNL.0000000000002923","article-title":"A\/T\/N: an unbiased descriptive classification scheme for Alzheimer disease biomarkers","volume":"87","author":"Jack","year":"2016","journal-title":"Neurology"},{"key":"10.1016\/j.jbc.2026.113499_bib91","doi-asserted-by":"crossref","first-page":"61","DOI":"10.3390\/jpm10030061","article-title":"Molecular and imaging biomarkers in Alzheimer\u2019s disease: a focus on recent insights","volume":"10","author":"Villa","year":"2020","journal-title":"J. Pers. Med."},{"key":"10.1016\/j.jbc.2026.113499_bib92","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/s12987-025-00620-5","article-title":"Exploring the ability of plasma pTau217, pTau181 and beta-amyloid in mirroring cerebrospinal fluid biomarker profile of mild cognitive impairment by the fully automated Lumipulse((R)) platform","volume":"22","author":"Catania","year":"2025","journal-title":"Fluids Barriers CNS"},{"key":"10.1016\/j.jbc.2026.113499_bib93","doi-asserted-by":"crossref","first-page":"26801","DOI":"10.1038\/srep26801","article-title":"Plasma beta-amyloid in alzheimer\u2019s disease and vascular disease","volume":"6","author":"Janelidze","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2026.113499_bib94","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1016\/j.jalz.2019.05.002","article-title":"Concordance between the assessment of Abeta42, T-tau, and P-T181-tau in peripheral blood neuronal-derived exosomes and cerebrospinal fluid","volume":"15","author":"Jia","year":"2019","journal-title":"Alzheimers Dement."},{"key":"10.1016\/j.jbc.2026.113499_bib95","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1038\/nature25456","article-title":"High performance plasma amyloid-beta biomarkers for Alzheimer\u2019s disease","volume":"554","author":"Nakamura","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113499_bib96","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/j.jalz.2017.06.2266","article-title":"Amyloid beta concentrations and stable isotope labeling kinetics of human plasma specific to central nervous system amyloidosis","volume":"13","author":"Ovod","year":"2017","journal-title":"Alzheimers Dement."},{"key":"10.1016\/j.jbc.2026.113499_bib97","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1002\/ana.25334","article-title":"Plasma amyloid as prescreener for the earliest alzheimer pathological changes","volume":"84","author":"Verberk","year":"2018","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.jbc.2026.113499_bib98","doi-asserted-by":"crossref","first-page":"18008","DOI":"10.1523\/JNEUROSCI.1402-13.2013","article-title":"Changes in brain function occur years before the onset of cognitive impairment","volume":"33","author":"Beason-Held","year":"2013","journal-title":"J. Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib99","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1038\/s41467-017-01150-x","article-title":"Earliest accumulation of beta-amyloid occurs within the default-mode network and concurrently affects brain connectivity","volume":"8","author":"Palmqvist","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113499_bib100","series-title":"Phage Display : A Laboratory Manual","author":"Barbas","year":"2001"},{"key":"10.1016\/j.jbc.2026.113499_bib101","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1002\/j.1460-2075.1994.tb06308.x","article-title":"Antibody fragments from a \u2018single pot\u2019 phage display library as immunochemical reagents","volume":"13","author":"Nissim","year":"1994","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.113499_bib102","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jbc.2026.113499_bib103","doi-asserted-by":"crossref","first-page":"10129","DOI":"10.1523\/JNEUROSCI.1202-06.2006","article-title":"Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation","volume":"26","author":"Oakley","year":"2006","journal-title":"J. Neurosci."},{"key":"10.1016\/j.jbc.2026.113499_bib104","doi-asserted-by":"crossref","first-page":"113","DOI":"10.3233\/JAD-2010-1349","article-title":"A novel transgenic rat model with a full alzheimer\u2019s-like amyloid pathology displays pre-plaque intracellular amyloid-beta-associated cognitive impairment","volume":"20","author":"Leon","year":"2010","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.jbc.2026.113499_bib105","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1186\/1750-1326-8-37","article-title":"Modeling Alzheimer's disease in transgenic rats","volume":"8","author":"Do Carmo","year":"2013","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.jbc.2026.113499_bib106","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.jneumeth.2008.12.001","article-title":"A simple and rapid method to collect the cerebrospinal fluid of rats and its application for the assessment of drug penetration into the central nervous system","volume":"178","author":"Nirogi","year":"2009","journal-title":"J. Neurosci. Methods"},{"key":"10.1016\/j.jbc.2026.113499_bib107","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1159\/000501856","article-title":"Rationale and design of the emory healthy aging and emory healthy brain studies","volume":"53","author":"Goetz","year":"2019","journal-title":"Neuroepidemiology"},{"key":"10.1016\/j.jbc.2026.113499_bib108","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1515\/cclm-2022-0516","article-title":"Second-generation Elecsys cerebrospinal fluid immunoassays aid diagnosis of early Alzheimer\u2019s disease","volume":"61","author":"Blennow","year":"2023","journal-title":"Clin. Chem. Lab. Med."},{"key":"10.1016\/j.jbc.2026.113499_bib109","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1002\/jnr.490350513","article-title":"Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination","volume":"35","author":"Brewer","year":"1993","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.jbc.2026.113499_bib110","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1097\/00001756-199606170-00014","article-title":"Viable cultured neurons in ambient carbon dioxide and hibernation storage for a month","volume":"7","author":"Brewer","year":"1996","journal-title":"Neuroreport"},{"key":"10.1016\/j.jbc.2026.113499_bib111","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1038\/s41592-020-0764-5","article-title":"Multiplexed mass spectrometry of individual ions improves measurement of proteoforms and their complexes","volume":"17","author":"Kafader","year":"2020","journal-title":"Nat. Methods"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826023719?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826023719?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T20:38:33Z","timestamp":1793219913000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826023719"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":111,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2026,10]]}},"alternative-id":["S0021925826023719"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113499","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Use of high-affinity scFv antibody NUsc1 for isolation and sensitive detection of Alzheimer\u2019s-associated amyloid beta oligomers","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113499","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"113499"}}