{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,6]],"date-time":"2026-05-06T04:07:07Z","timestamp":1778040427079,"version":"3.51.4"},"reference-count":286,"publisher":"Springer Science and Business Media LLC","issue":"4","license":[{"start":{"date-parts":[[2024,10,24]],"date-time":"2024-10-24T00:00:00Z","timestamp":1729728000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2024,10,24]],"date-time":"2024-10-24T00:00:00Z","timestamp":1729728000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["UIDB\/00313\/2020"],"award-info":[{"award-number":["UIDB\/00313\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["UIDB\/00313\/2020"],"award-info":[{"award-number":["UIDB\/00313\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["UIDB\/00313\/2020"],"award-info":[{"award-number":["UIDB\/00313\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005727","name":"Universidade de Coimbra","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100005727","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Neurobiol"],"published-print":{"date-parts":[[2025,4]]},"abstract":"<jats:title>Abstract<\/jats:title>\n          <jats:p>Alzheimer\u2019s disease (AD) is the most common form of dementia around the world (~\u200965%). Here, we portray the neuropathology of AD, biomarkers, and classification of amyloid plaques (diffuse, non-cored, dense core, compact). Tau pathology and its involvement with A\u03b2 plaques and cell death are discussed. Amyloid cascade hypotheses, aggregation mechanisms, and molecular species formed in vitro and in vivo (on- and off-pathways) are described. A\u03b242\/A\u03b240 monomers, dimers, trimers, A\u03b2\u2010derived diffusible ligands, globulomers, dodecamers, amylospheroids, amorphous aggregates, protofibrils, fibrils, and plaques are characterized (structure, size, morphology, solubility, toxicity, mechanistic steps). An update on AD-approved drugs by regulatory agencies, along with new A\u03b2-based therapies, is presented. Beyond prescribing A\u03b2 plaque disruptors, cholinergic agonists, or NMDA receptor antagonists, other therapeutic strategies (RNAi, glutaminyl cyclase inhibitors, monoclonal antibodies, secretase modulators, A\u03b2 aggregation inhibitors, and anti-amyloid vaccines) are already under clinical trials. New drug discovery approaches based on \u201cdesigned multiple ligands\u201d, \u201chybrid molecules\u201d, or \u201cmultitarget-directed ligands\u201d are also being put forward and may contribute to tackling this highly debilitating and fatal form of human dementia.<\/jats:p>","DOI":"10.1007\/s12035-024-04543-4","type":"journal-article","created":{"date-parts":[[2024,10,24]],"date-time":"2024-10-24T15:03:02Z","timestamp":1729782182000},"page":"4391-4419","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["Morphological and Molecular Profiling of Amyloid-\u03b2 Species in Alzheimer\u2019s Pathogenesis"],"prefix":"10.1007","volume":"62","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4097-2766","authenticated-orcid":false,"given":"Zaida L.","family":"Almeida","sequence":"first","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7562-4676","authenticated-orcid":false,"given":"Daniela C.","family":"Vaz","sequence":"additional","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9128-2557","authenticated-orcid":false,"given":"Rui M. M.","family":"Brito","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2024,10,24]]},"reference":[{"key":"4543_CR1","doi-asserted-by":"publisher","first-page":"12924","DOI":"10.3390\/IJMS232112924","volume":"23","author":"U Sehar","year":"2022","unstructured":"Sehar U, Rawat P, Reddy AP et al (2022) Amyloid beta in aging and Alzheimer\u2019s disease. Int J Mol Sci 23:12924. https:\/\/doi.org\/10.3390\/IJMS232112924","journal-title":"Int J Mol Sci"},{"key":"4543_CR2","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/J.ARTMED.2016.06.003","volume":"71","author":"A Alberdi","year":"2016","unstructured":"Alberdi A, Aztiria A, Basarab A (2016) On the early diagnosis of Alzheimer\u2019s disease from multimodal signals: a survey. Artif Intell Med 71:1\u201329. https:\/\/doi.org\/10.1016\/J.ARTMED.2016.06.003","journal-title":"Artif Intell Med"},{"key":"4543_CR3","doi-asserted-by":"publisher","unstructured":"Duncan BB, Schmidt MI, Collaborators G 2019 (2022) Global, regional, and national burden of diseases and injuries for adults 70 years and older: systematic analysis for the Global Burden of Disease 2019 Study. BMJ 376:e068208.\u00a0https:\/\/doi.org\/10.1136\/bmj-2021-068208","DOI":"10.1136\/bmj-2021-068208"},{"key":"4543_CR4","doi-asserted-by":"publisher","first-page":"425","DOI":"10.12688\/f1000research.50786.1","volume":"10","author":"SF Javaid","year":"2021","unstructured":"Javaid SF, Giebel C, Khan MA, Hashim MJ (2021) Epidemiology of Alzheimer\u2019s disease and other dementias: rising global burden and forecasted trends. F1000Research 10:425. https:\/\/doi.org\/10.12688\/f1000research.50786.1","journal-title":"F1000Research"},{"key":"4543_CR5","doi-asserted-by":"publisher","unstructured":"(2022) 2022 Alzheimer\u2019s disease facts and figures. Alzheimers Dement 18(4):700\u2013789. https:\/\/doi.org\/10.1002\/ALZ.12638","DOI":"10.1002\/ALZ.12638"},{"key":"4543_CR6","doi-asserted-by":"publisher","first-page":"38","DOI":"10.3978\/J.ISSN.2305-5839.2015.01.19","volume":"3","author":"XC Zhu","year":"2015","unstructured":"Zhu XC, Tan L, Wang HF et al (2015) Rate of early onset Alzheimer\u2019s disease: a systematic review and meta-analysis. Ann Transl Med 3:38. https:\/\/doi.org\/10.3978\/J.ISSN.2305-5839.2015.01.19","journal-title":"Ann Transl Med"},{"key":"4543_CR7","doi-asserted-by":"publisher","first-page":"167","DOI":"10.2741\/E605","volume":"5","author":"I Piaceri","year":"2013","unstructured":"Piaceri I, Nacmias B, Sorbi S (2013) Genetics of familial and sporadic Alzheimer\u2019s disease. Front Biosci (Elite Ed) 5:167\u2013177. https:\/\/doi.org\/10.2741\/E605","journal-title":"Front Biosci (Elite Ed)"},{"key":"4543_CR8","doi-asserted-by":"publisher","first-page":"5789","DOI":"10.3390\/MOLECULES25245789","volume":"25","author":"Z Breijyeh","year":"2020","unstructured":"Breijyeh Z, Karaman R, Mu\u00f1oz-Torrero D, Dembinski R (2020) Comprehensive review on Alzheimer\u2019s disease: causes and treatment. Mol 25:5789. https:\/\/doi.org\/10.3390\/MOLECULES25245789","journal-title":"Mol"},{"key":"4543_CR9","doi-asserted-by":"publisher","first-page":"412","DOI":"10.1038\/s41588-022-01024-z","volume":"54","author":"C Bellenguez","year":"2022","unstructured":"Bellenguez C, K\u00fc\u00e7\u00fckali F, Jansen IE et al (2022) New insights into the genetic etiology of Alzheimer\u2019s disease and related dementias. Nat Genet 54:412\u2013436. https:\/\/doi.org\/10.1038\/s41588-022-01024-z","journal-title":"Nat Genet"},{"issue":"26","key":"4543_CR10","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/S12929-019-0524-Y","volume":"261","author":"MVF Silva","year":"2019","unstructured":"Silva MVF, Loures CDMG, Alves LCV et al (2019) (2019) Alzheimer\u2019s disease: risk factors and potentially protective measures. J Biomed Sci 261(26):1\u201311. https:\/\/doi.org\/10.1186\/S12929-019-0524-Y","journal-title":"J Biomed Sci"},{"key":"4543_CR11","doi-asserted-by":"publisher","first-page":"917","DOI":"10.1016\/J.JAGP.2020.12.031","volume":"29","author":"D Kim","year":"2021","unstructured":"Kim D, Wang RD, Kiss A et al (2021) Depression and increased risk of Alzheimer\u2019s dementia: longitudinal analyses of modifiable risk and sex-related factors. Am J Geriatr Psychiatry 29:917\u2013926. https:\/\/doi.org\/10.1016\/J.JAGP.2020.12.031","journal-title":"Am J Geriatr Psychiatry"},{"key":"4543_CR12","doi-asserted-by":"publisher","first-page":"725241","DOI":"10.3389\/FCELL.2021.725241\/BIBTEX","volume":"9","author":"CA Sallaberry","year":"2021","unstructured":"Sallaberry CA, Voss BJ, Majewski J et al (2021) Tau and membranes: interactions that promote folding and condensation. Front Cell Dev Biol 9:725241. https:\/\/doi.org\/10.3389\/FCELL.2021.725241\/BIBTEX","journal-title":"Front Cell Dev Biol"},{"key":"4543_CR13","doi-asserted-by":"publisher","first-page":"3617","DOI":"10.1007\/S12035-022-02809-3","volume":"59","author":"SY Liang","year":"2022","unstructured":"Liang SY, Wang ZT, Tan L, Yu JT (2022) Tau toxicity in neurodegeneration. Mol Neurobiol 59:3617\u20133634. https:\/\/doi.org\/10.1007\/S12035-022-02809-3","journal-title":"Mol Neurobiol"},{"key":"4543_CR14","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1016\/J.JALZ.2018.02.018","volume":"14","author":"CR Jack","year":"2018","unstructured":"Jack CR, Bennett DA, Blennow K et al (2018) NIA-AA research framework: toward a biological definition of Alzheimer\u2019s disease. Alzheimer\u2019s Dement 14:535\u2013562. https:\/\/doi.org\/10.1016\/J.JALZ.2018.02.018","journal-title":"Alzheimer\u2019s Dement"},{"key":"4543_CR15","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/J.JALZ.2011.10.007","volume":"8","author":"BT Hyman","year":"2012","unstructured":"Hyman BT, Phelps CH, Beach TG et al (2012) National Institute on Aging\u2013Alzheimer\u2019s Association guidelines for the neuropathologic assessment of Alzheimer\u2019s disease. Alzheimer\u2019s Dement 8:1\u201313. https:\/\/doi.org\/10.1016\/J.JALZ.2011.10.007","journal-title":"Alzheimer\u2019s Dement"},{"key":"4543_CR16","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/S00401-011-0910-3","volume":"123","author":"TJ Montine","year":"2012","unstructured":"Montine TJ, Phelps CH, Beach TG et al (2012) National Institute on Aging-Alzheimer\u2019s Association guidelines for the neuropathologic assessment of Alzheimer\u2019s disease: a practical approach. Acta Neuropathol 123:1\u201311. https:\/\/doi.org\/10.1007\/S00401-011-0910-3","journal-title":"Acta Neuropathol"},{"issue":"27","key":"4543_CR17","doi-asserted-by":"publisher","first-page":"954","DOI":"10.1038\/s41591-021-01382-x","volume":"276","author":"O Hansson","year":"2021","unstructured":"Hansson O (2021) (2021) Biomarkers for neurodegenerative diseases. Nat Med 276(27):954\u2013963. https:\/\/doi.org\/10.1038\/s41591-021-01382-x","journal-title":"Nat Med"},{"key":"4543_CR18","doi-asserted-by":"publisher","first-page":"e13122","DOI":"10.1111\/BPA.13122","volume":"33","author":"I Ferrer","year":"2023","unstructured":"Ferrer I (2023) Hypothesis review: Alzheimer\u2019s overture guidelines. Brain Pathol 33:e13122. https:\/\/doi.org\/10.1111\/BPA.13122","journal-title":"Brain Pathol"},{"key":"4543_CR19","doi-asserted-by":"publisher","first-page":"280","DOI":"10.1016\/J.JALZ.2011.03.003","volume":"7","author":"RA Sperling","year":"2011","unstructured":"Sperling RA, Aisen PS, Beckett LA et al (2011) Toward defining the preclinical stages of Alzheimer\u2019s disease: recommendations from the National Institute on Aging-Alzheimer\u2019s Association workgroups on diagnostic guidelines for Alzheimer\u2019s disease. Alzheimer\u2019s Dement 7:280\u2013292. https:\/\/doi.org\/10.1016\/J.JALZ.2011.03.003","journal-title":"Alzheimer\u2019s Dement"},{"key":"4543_CR20","doi-asserted-by":"publisher","first-page":"270","DOI":"10.1016\/J.JALZ.2011.03.008","volume":"7","author":"MS Albert","year":"2011","unstructured":"Albert MS, DeKosky ST, Dickson D et al (2011) The diagnosis of mild cognitive impairment due to Alzheimer\u2019s disease: recommendations from the National Institute on Aging-Alzheimer\u2019s Association workgroups on diagnostic guidelines for Alzheimer\u2019s disease. Alzheimers Dement 7:270\u2013279. https:\/\/doi.org\/10.1016\/J.JALZ.2011.03.008","journal-title":"Alzheimers Dement"},{"key":"4543_CR21","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1016\/J.JALZ.2011.03.005","volume":"7","author":"GM McKhann","year":"2011","unstructured":"McKhann GM, Knopman DS, Chertkow H et al (2011) The diagnosis of dementia due to Alzheimer\u2019s disease: recommendations from the National Institute on Aging-Alzheimer\u2019s Association workgroups on diagnostic guidelines for Alzheimer\u2019s disease. Alzheimer\u2019s Dement 7:263\u2013269. https:\/\/doi.org\/10.1016\/J.JALZ.2011.03.005","journal-title":"Alzheimer\u2019s Dement"},{"key":"4543_CR22","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1093\/BRAIN\/AWZ403","volume":"143","author":"M Teylan","year":"2020","unstructured":"Teylan M, Mock C, Gauthreaux K et al (2020) Cognitive trajectory in mild cognitive impairment due to primary age-related tauopathy. Brain 143:611\u2013621. https:\/\/doi.org\/10.1093\/BRAIN\/AWZ403","journal-title":"Brain"},{"key":"4543_CR23","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/S11910-020-01063-1\/TABLES\/2","volume":"20","author":"RA Hickman","year":"2020","unstructured":"Hickman RA, Flowers XE, Wisniewski T (2020) Primary age-related tauopathy (PART): addressing the spectrum of neuronal tauopathic changes in the aging brain. Curr Neurol Neurosci Rep 20:1\u201311. https:\/\/doi.org\/10.1007\/S11910-020-01063-1\/TABLES\/2","journal-title":"Curr Neurol Neurosci Rep"},{"key":"4543_CR24","doi-asserted-by":"publisher","first-page":"1356","DOI":"10.1176\/AJP.141.11.1356","volume":"141","author":"WG Rosen","year":"1984","unstructured":"Rosen WG, Mohs RC, Davis KL (1984) A new rating scale for Alzheimer\u2019s disease. Am J Psychiatry 141:1356\u20131364. https:\/\/doi.org\/10.1176\/AJP.141.11.1356","journal-title":"Am J Psychiatry"},{"key":"4543_CR25","doi-asserted-by":"publisher","first-page":"922","DOI":"10.1111\/J.1532-5415.1992.TB01992.X","volume":"40","author":"TN Tombaugh","year":"1992","unstructured":"Tombaugh TN, McIntyre NJ (1992) The mini-mental state examination: a comprehensive review. J Am Geriatr Soc 40:922\u2013935. https:\/\/doi.org\/10.1111\/J.1532-5415.1992.TB01992.X","journal-title":"J Am Geriatr Soc"},{"key":"4543_CR26","doi-asserted-by":"publisher","first-page":"566","DOI":"10.1192\/BJP.140.6.566","volume":"140","author":"CP Hughes","year":"1982","unstructured":"Hughes CP, Berg L, Danziger WL et al (1982) A new clinical scale for the staging of dementia. Br J Psychiatry 140:566\u2013572. https:\/\/doi.org\/10.1192\/BJP.140.6.566","journal-title":"Br J Psychiatry"},{"key":"4543_CR27","doi-asserted-by":"publisher","first-page":"7501","DOI":"10.1073\/PNAS.1504081112\/SUPPL_FILE\/PNAS.1504081112.SAPP.PDF","volume":"112","author":"H Kadavath","year":"2015","unstructured":"Kadavath H, Hofele RV, Biernat J et al (2015) Tau stabilizes microtubules by binding at the interface between tubulin heterodimers. Proc Natl Acad Sci U S A 112:7501\u20137506. https:\/\/doi.org\/10.1073\/PNAS.1504081112\/SUPPL_FILE\/PNAS.1504081112.SAPP.PDF","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"17","key":"4543_CR28","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1038\/nrn.2015.1","volume":"171","author":"Y Wang","year":"2015","unstructured":"Wang Y (2015) Mandelkow E (2015) Tau in physiology and pathology. Nat Rev Neurosci 171(17):22\u201335. https:\/\/doi.org\/10.1038\/nrn.2015.1","journal-title":"Nat Rev Neurosci"},{"key":"4543_CR29","doi-asserted-by":"publisher","first-page":"5155","DOI":"10.1007\/S12035-023-03387-8\/TABLES\/1","volume":"60","author":"Z Waheed","year":"2023","unstructured":"Waheed Z, Choudhary J, Jatala FH et al (2023) The role of Tau proteoforms in health and disease. Mol Neurobiol 60:5155\u20135166. https:\/\/doi.org\/10.1007\/S12035-023-03387-8\/TABLES\/1","journal-title":"Mol Neurobiol"},{"key":"4543_CR30","doi-asserted-by":"publisher","first-page":"272","DOI":"10.1016\/0006-8993(95)01264-8","volume":"707","author":"J Savory","year":"1996","unstructured":"Savory J, Huang Y, Herman MM, Wills MR (1996) Quantitative image analysis of temporal changes in Tau and neurofilament proteins during the course of acute experimental neurofibrillary degeneration; non-phosphorylated epitopes precede phosphorylation. Brain Res 707:272\u2013281. https:\/\/doi.org\/10.1016\/0006-8993(95)01264-8","journal-title":"Brain Res"},{"key":"4543_CR31","doi-asserted-by":"publisher","first-page":"410","DOI":"10.1016\/J.NEURON.2011.04.009","volume":"70","author":"M Morris","year":"2011","unstructured":"Morris M, Maeda S, Vossel K, Mucke L (2011) The many faces of Tau. Neuron 70:410\u2013426. https:\/\/doi.org\/10.1016\/J.NEURON.2011.04.009","journal-title":"Neuron"},{"key":"4543_CR32","doi-asserted-by":"publisher","first-page":"eabm4295","DOI":"10.1126\/SCIADV.ABM4295","volume":"8","author":"M Lacomme","year":"2022","unstructured":"Lacomme M, Hales SC, Brown TW et al (2022) Numb regulates Tau levels and prevents neurodegeneration in tauopathy mouse models. Sci Adv 8:eabm4295. https:\/\/doi.org\/10.1126\/SCIADV.ABM4295","journal-title":"Sci Adv"},{"key":"4543_CR33","doi-asserted-by":"publisher","first-page":"5129","DOI":"10.1073\/PNAS.97.10.5129","volume":"97","author":"M Von Bergen","year":"2000","unstructured":"Von Bergen M, Friedhoff P, Biernat J et al (2000) Assembly of Tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. Proc Natl Acad Sci U S A 97:5129\u20135134. https:\/\/doi.org\/10.1073\/PNAS.97.10.5129","journal-title":"Proc Natl Acad Sci U S A"},{"key":"4543_CR34","doi-asserted-by":"publisher","first-page":"48165","DOI":"10.1074\/JBC.M105196200","volume":"276","author":"M Von Bergen","year":"2001","unstructured":"Von Bergen M, Barghorn S, Li L et al (2001) Mutations of Tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure. J Biol Chem 276:48165\u201348174. https:\/\/doi.org\/10.1074\/JBC.M105196200","journal-title":"J Biol Chem"},{"key":"4543_CR35","doi-asserted-by":"publisher","first-page":"1694","DOI":"10.1021\/BI0357006","volume":"43","author":"S Barghorn","year":"2004","unstructured":"Barghorn S, Davies P, Mandelkow E (2004) Tau paired helical filaments from Alzheimer\u2019s disease brain and assembled in vitro are based on beta-structure in the core domain. Biochemistry 43:1694\u20131703. https:\/\/doi.org\/10.1021\/BI0357006","journal-title":"Biochemistry"},{"key":"4543_CR36","doi-asserted-by":"publisher","first-page":"1121","DOI":"10.1146\/ANNUREV.NEURO.24.1.1121","volume":"24","author":"VMY Lee","year":"2003","unstructured":"Lee VMY, Goedert M, Trojanowski JQ (2003) Neurodegenerative tauopathies. Annu Rev Neurosci 24:1121\u20131159. https:\/\/doi.org\/10.1146\/ANNUREV.NEURO.24.1.1121","journal-title":"Annu Rev Neurosci"},{"key":"4543_CR37","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1146\/ANNUREV-NEURO-072116-031153","volume":"40","author":"M Goedert","year":"2017","unstructured":"Goedert M, Eisenberg DS, Crowther RA (2017) Propagation of Tau aggregates and neurodegeneration. Annu Rev Neurosci 40:189\u2013210. https:\/\/doi.org\/10.1146\/ANNUREV-NEURO-072116-031153","journal-title":"Annu Rev Neurosci"},{"key":"4543_CR38","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1016\/J.BBADIS.2004.09.008","volume":"1739","author":"K Iqbal","year":"2005","unstructured":"Iqbal K, Del C, Alonso A, Chen S et al (2005) Tau pathology in Alzheimer disease and other tauopathies. Biochim Biophys Acta - Mol Basis Dis 1739:198\u2013210. https:\/\/doi.org\/10.1016\/J.BBADIS.2004.09.008","journal-title":"Biochim Biophys Acta - Mol Basis Dis"},{"key":"4543_CR39","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1007\/BF00308809\/METRICS","volume":"82","author":"H Braak","year":"1991","unstructured":"Braak H, Braak E (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 82:239\u2013259. https:\/\/doi.org\/10.1007\/BF00308809\/METRICS","journal-title":"Acta Neuropathol"},{"key":"4543_CR40","doi-asserted-by":"publisher","first-page":"15317","DOI":"10.1074\/JBC.M110.209296","volume":"286","author":"JL Guo","year":"2011","unstructured":"Guo JL, Lee VMY (2011) Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem 286:15317\u201315331. https:\/\/doi.org\/10.1074\/JBC.M110.209296","journal-title":"J Biol Chem"},{"key":"4543_CR41","doi-asserted-by":"publisher","first-page":"19855","DOI":"10.1074\/JBC.R114.549295","volume":"289","author":"BB Holmes","year":"2014","unstructured":"Holmes BB, Diamond MI (2014) Prion-like properties of Tau protein: the importance of extracellular Tau as a therapeutic target. J Biol Chem 289:19855\u201319861. https:\/\/doi.org\/10.1074\/JBC.R114.549295","journal-title":"J Biol Chem"},{"key":"4543_CR42","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1007\/S00401-006-0127-Z\/FIGURES\/5","volume":"112","author":"H Braak","year":"2006","unstructured":"Braak H, Alafuzoff I, Arzberger T et al (2006) Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry. Acta Neuropathol 112:389\u2013404. https:\/\/doi.org\/10.1007\/S00401-006-0127-Z\/FIGURES\/5","journal-title":"Acta Neuropathol"},{"key":"4543_CR43","doi-asserted-by":"publisher","first-page":"479","DOI":"10.1212\/WNL.41.4.479","volume":"41","author":"SS Mirra","year":"1991","unstructured":"Mirra SS, Heyman A, McKeel D et al (1991) The consortium to establish a registry for Alzheimer\u2019s disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer\u2019s disease. Neurology 41:479\u2013486. https:\/\/doi.org\/10.1212\/WNL.41.4.479","journal-title":"Neurology"},{"key":"4543_CR44","doi-asserted-by":"publisher","DOI":"10.3389\/FNAGI.2020.00272\/BIBTEX","volume":"12","author":"C Bjorkli","year":"2020","unstructured":"Bjorkli C, Sandvig A, Sandvig I (2020) Bridging the gap between fluid biomarkers for Alzheimer\u2019s disease, model systems, and patients. Front Aging Neurosci 12:568023. https:\/\/doi.org\/10.3389\/FNAGI.2020.00272\/BIBTEX","journal-title":"Front Aging Neurosci"},{"key":"4543_CR45","doi-asserted-by":"publisher","first-page":"2031","DOI":"10.1212\/WNL.0000000000004643\/SUPPL_FILE\/TABLE_E-2.PDF","volume":"89","author":"MJ Grothe","year":"2017","unstructured":"Grothe MJ, Barthel H, Sepulcre J et al (2017) In vivo staging of regional amyloid deposition. Neurology 89:2031\u20132038. https:\/\/doi.org\/10.1212\/WNL.0000000000004643\/SUPPL_FILE\/TABLE_E-2.PDF","journal-title":"Neurology"},{"key":"4543_CR46","doi-asserted-by":"publisher","unstructured":"Braak H, Del Tredici K (2015) Neuroanatomy and pathology of sporadic Alzheimer\u2019s disease. Adv Anat Embryol Cell Biol 215:1\u2013162. https:\/\/doi.org\/10.1007\/978-3-319-12679-1\/COVER","DOI":"10.1007\/978-3-319-12679-1\/COVER"},{"key":"4543_CR47","doi-asserted-by":"publisher","first-page":"e7280","DOI":"10.1371\/JOURNAL.PONE.0007280","volume":"4","author":"T Jaworski","year":"2009","unstructured":"Jaworski T, Dewachter I, Lechat B et al (2009) AAV-Tau mediates pyramidal neurodegeneration by cell-cycle re-entry without neurofibrillary tangle formation in wild-type mice. PLoS ONE 4:e7280. https:\/\/doi.org\/10.1371\/JOURNAL.PONE.0007280","journal-title":"PLoS ONE"},{"key":"4543_CR48","doi-asserted-by":"publisher","first-page":"808","DOI":"10.1016\/J.BBADIS.2010.03.005","volume":"1802","author":"T Jaworski","year":"2010","unstructured":"Jaworski T, Dewachter I, Seymour CM et al (2010) Alzheimer\u2019s disease: old problem, new views from transgenic and viral models. Biochim Biophys Acta - Mol Basis Dis 1802:808\u2013818. https:\/\/doi.org\/10.1016\/J.BBADIS.2010.03.005","journal-title":"Biochim Biophys Acta - Mol Basis Dis"},{"key":"4543_CR49","doi-asserted-by":"publisher","first-page":"3286","DOI":"10.1093\/BRAIN\/AWX243","volume":"140","author":"A Bejanin","year":"2017","unstructured":"Bejanin A, Schonhaut DR, La Joie R et al (2017) Tau pathology and neurodegeneration contribute to cognitive impairment in Alzheimer\u2019s disease. Brain 140:3286\u20133300. https:\/\/doi.org\/10.1093\/BRAIN\/AWX243","journal-title":"Brain"},{"key":"4543_CR50","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1016\/S1474-4422(14)70252-2","volume":"14","author":"VL Villemagne","year":"2015","unstructured":"Villemagne VL, Fodero-Tavoletti MT, Masters CL, Rowe CC (2015) Tau imaging: early progress and future directions. Lancet Neurol 14:114\u2013124. https:\/\/doi.org\/10.1016\/S1474-4422(14)70252-2","journal-title":"Lancet Neurol"},{"key":"4543_CR51","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1097\/NEN.0B013E31825018F7","volume":"71","author":"PT Nelson","year":"2012","unstructured":"Nelson PT, Alafuzoff I, Bigio EH et al (2012) Correlation of Alzheimer disease neuropathologic changes with cognitive status: a review of the literature. J Neuropathol Exp Neurol 71:362\u2013381. https:\/\/doi.org\/10.1097\/NEN.0B013E31825018F7","journal-title":"J Neuropathol Exp Neurol"},{"key":"4543_CR52","doi-asserted-by":"publisher","first-page":"1680","DOI":"10.1038\/s41591-019-0611-3","volume":"25","author":"JF Arboleda-Velasquez","year":"2019","unstructured":"Arboleda-Velasquez JF, Lopera F, O\u2019Hare M et al (2019) Resistance to autosomal dominant Alzheimer\u2019s disease in an APOE3 Christchurch homozygote: a case report. Nat Med 25:1680\u20131683. https:\/\/doi.org\/10.1038\/s41591-019-0611-3","journal-title":"Nat Med"},{"key":"4543_CR53","doi-asserted-by":"publisher","first-page":"1928","DOI":"10.1016\/J.AJPATH.2012.08.012","volume":"181","author":"K Leroy","year":"2012","unstructured":"Leroy K, Ando K, Laporte V et al (2012) Lack of Tau proteins rescues neuronal cell death and decreases amyloidogenic processing of APP in APP\/PS1 mice. Am J Pathol 181:1928\u20131940. https:\/\/doi.org\/10.1016\/J.AJPATH.2012.08.012","journal-title":"Am J Pathol"},{"key":"4543_CR54","doi-asserted-by":"publisher","first-page":"750","DOI":"10.1126\/SCIENCE.1141736","volume":"316","author":"ED Roberson","year":"2007","unstructured":"Roberson ED, Scearce-Levie K, Palop JJ et al (2007) Reducing endogenous Tau ameliorates amyloid beta-induced deficits in an Alzheimer\u2019s disease mouse model. Science 316:750\u2013754. https:\/\/doi.org\/10.1126\/SCIENCE.1141736","journal-title":"Science"},{"key":"4543_CR55","doi-asserted-by":"publisher","first-page":"1487","DOI":"10.1126\/SCIENCE.1058189\/SUPPL_FILE\/1058189S2_THUMB.GIF","volume":"293","author":"J Lewis","year":"2001","unstructured":"Lewis J, Dickson DW, Lin WL et al (2001) Enhanced neurofibrillary degeneration in transgenic mice expressing mutant Tau and APP. Science (80-) 293:1487\u20131491. https:\/\/doi.org\/10.1126\/SCIENCE.1058189\/SUPPL_FILE\/1058189S2_THUMB.GIF","journal-title":"Science (80-)"},{"key":"4543_CR56","doi-asserted-by":"publisher","first-page":"814","DOI":"10.1016\/J.NBD.2005.05.027","volume":"20","author":"EM Rib\u00e9","year":"2005","unstructured":"Rib\u00e9 EM, P\u00e9rez M, Puig B et al (2005) Accelerated amyloid deposition, neurofibrillary degeneration and neuronal loss in double mutant APP\/Tau transgenic mice. Neurobiol Dis 20:814\u2013822. https:\/\/doi.org\/10.1016\/J.NBD.2005.05.027","journal-title":"Neurobiol Dis"},{"key":"4543_CR57","doi-asserted-by":"publisher","first-page":"733","DOI":"10.1038\/325733a0","volume":"325","author":"J Kang","year":"1987","unstructured":"Kang J, Lemaire HG, Unterbeck A et al (1987) The precursor of Alzheimer\u2019s disease amyloid A4 protein resembles a cell-surface receptor. Nat 325:733\u2013736. https:\/\/doi.org\/10.1038\/325733a0","journal-title":"Nat"},{"key":"4543_CR58","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1038\/nrn.2017.29","volume":"18","author":"UC M\u00fcller","year":"2017","unstructured":"M\u00fcller UC, Deller T, Korte M (2017) Not just amyloid: physiological functions of the amyloid precursor protein family. Nat Rev Neurosci 18:281\u2013298. https:\/\/doi.org\/10.1038\/nrn.2017.29","journal-title":"Nat Rev Neurosci"},{"key":"4543_CR59","doi-asserted-by":"publisher","first-page":"eaao4827","DOI":"10.1126\/SCIENCE.AAO4827","volume":"363","author":"HC Rice","year":"2019","unstructured":"Rice HC, De Malmazet D, Schreurs A et al (2019) Secreted amyloid-\u03b2 precursor protein functions as a GABABR1a ligand to modulate synaptic transmission. Science 363:eaao4827. https:\/\/doi.org\/10.1126\/SCIENCE.AAO4827","journal-title":"Science"},{"key":"4543_CR60","doi-asserted-by":"publisher","first-page":"10836","DOI":"10.1073\/PNAS.90.22.10836","volume":"90","author":"AE Roher","year":"1993","unstructured":"Roher AE, Lowenson JD, Clarke S et al (1993) beta-Amyloid-(1\u201342) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc Natl Acad Sci 90:10836\u201310840. https:\/\/doi.org\/10.1073\/PNAS.90.22.10836","journal-title":"Proc Natl Acad Sci"},{"key":"4543_CR61","doi-asserted-by":"publisher","first-page":"311","DOI":"10.3233\/JAD-2010-1221","volume":"19","author":"MP Murphy","year":"2010","unstructured":"Murphy MP, Levine H (2010) Alzheimer\u2019s disease and the amyloid-\u03b2 peptide. J Alzheimer\u2019s Dis 19:311\u2013323. https:\/\/doi.org\/10.3233\/JAD-2010-1221","journal-title":"J Alzheimer\u2019s Dis"},{"key":"4543_CR62","doi-asserted-by":"publisher","first-page":"292","DOI":"10.15698\/CST2018.11.162","volume":"2","author":"H Steiner","year":"2018","unstructured":"Steiner H, Fukumori A, Tagami S, Okochi M (2018) Making the final cut: pathogenic amyloid-\u03b2 peptide generation by \u03b3-secretase. Cell Stress 2:292. https:\/\/doi.org\/10.15698\/CST2018.11.162","journal-title":"Cell Stress"},{"key":"4543_CR63","doi-asserted-by":"publisher","first-page":"4693","DOI":"10.1021\/BI00069A001\/ASSET\/BI00069A001.FP.PNG_V03","volume":"32","author":"JT Jarrett","year":"1993","unstructured":"Jarrett JT, Berger EP, Lansbury PT (1993) The carboxy terminus of the \u03b2 amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer\u2019s disease. Biochemistry 32:4693\u20134697. https:\/\/doi.org\/10.1021\/BI00069A001\/ASSET\/BI00069A001.FP.PNG_V03","journal-title":"Biochemistry"},{"key":"4543_CR64","first-page":"452","volume":"145","author":"N Suzuki","year":"1994","unstructured":"Suzuki N, Iwatsubo T, Odaka A et al (1994) High tissue content of soluble beta 1\u201340 is linked to cerebral amyloid angiopathy. Am J Pathol 145:452","journal-title":"Am J Pathol"},{"key":"4543_CR65","doi-asserted-by":"publisher","first-page":"172","DOI":"10.1016\/S0925-4439(00)00043-0","volume":"1502","author":"TE Golde","year":"2000","unstructured":"Golde TE, Eckman CB, Younkin SG (2000) Biochemical detection of Abeta isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer\u2019s disease. Biochim Biophys Acta 1502:172\u2013187. https:\/\/doi.org\/10.1016\/S0925-4439(00)00043-0","journal-title":"Biochim Biophys Acta"},{"key":"4543_CR66","doi-asserted-by":"publisher","first-page":"11993","DOI":"10.1073\/PNAS.91.25.11993","volume":"91","author":"M Citron","year":"1994","unstructured":"Citron M, Vigo-Pelfrey C, Teplow DB et al (1994) Excessive production of amyloid beta-protein by peripheral cells of symptomatic and presymptomatic patients carrying the Swedish familial Alzheimer disease mutation. Proc Natl Acad Sci U S A 91:11993\u201311997. https:\/\/doi.org\/10.1073\/PNAS.91.25.11993","journal-title":"Proc Natl Acad Sci U S A"},{"key":"4543_CR67","doi-asserted-by":"publisher","first-page":"1336","DOI":"10.1126\/SCIENCE.8191290","volume":"264","author":"N Suzuki","year":"1994","unstructured":"Suzuki N, Cheung TT, Cai XD et al (1994) An increased percentage of long amyloid \u03b2 protein secreted by familial amyloid \u03b2 protein precursor (\u03b2App717) mutants. Science (80-) 264:1336\u20131340. https:\/\/doi.org\/10.1126\/SCIENCE.8191290","journal-title":"Science (80-)"},{"key":"4543_CR68","doi-asserted-by":"publisher","first-page":"864","DOI":"10.1038\/NM0896-864","volume":"2","author":"D Scheuner","year":"1996","unstructured":"Scheuner D, Eckman C, Jensen M et al (1996) Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer\u2019s disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer\u2019s disease. Nat Med 2:864\u2013870. https:\/\/doi.org\/10.1038\/NM0896-864","journal-title":"Nat Med"},{"key":"4543_CR69","doi-asserted-by":"publisher","first-page":"eabc6184","DOI":"10.1126\/SCITRANSLMED.ABC6184\/SUPPL_FILE\/SCITRANSLMED.ABC6184_DATA_FILES_S1_AND_S2.ZIP","volume":"13","author":"MP De la Vega","year":"2021","unstructured":"De la Vega MP, Giedraitis V, Michno W et al (2021) The Uppsala APP deletion causes early onset autosomal dominant Alzheimer\u2019s disease by altering APP processing and increasing amyloid \u03b2 fibril formation. Sci Transl Med 13:eabc6184. https:\/\/doi.org\/10.1126\/SCITRANSLMED.ABC6184\/SUPPL_FILE\/SCITRANSLMED.ABC6184_DATA_FILES_S1_AND_S2.ZIP","journal-title":"Sci Transl Med"},{"key":"4543_CR70","doi-asserted-by":"publisher","first-page":"969547","DOI":"10.3389\/FCELL.2022.969547\/BIBTEX","volume":"10","author":"G Pfundstein","year":"2022","unstructured":"Pfundstein G, Nikonenko AG, Sytnyk V (2022) Amyloid precursor protein (APP) and amyloid \u03b2 (A\u03b2) interact with cell adhesion molecules: Implications in Alzheimer\u2019s disease and normal physiology. Front Cell Dev Biol 10:969547. https:\/\/doi.org\/10.3389\/FCELL.2022.969547\/BIBTEX","journal-title":"Front Cell Dev Biol"},{"key":"4543_CR71","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1007\/S00401-020-02196-W","volume":"140","author":"SA Kent","year":"2020","unstructured":"Kent SA, Spires-Jones TL, Durrant CS (2020) The physiological roles of Tau and A\u03b2: implications for Alzheimer\u2019s disease pathology and therapeutics. Acta Neuropathol 140:417\u2013447. https:\/\/doi.org\/10.1007\/S00401-020-02196-W","journal-title":"Acta Neuropathol"},{"key":"4543_CR72","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1159\/000008156","volume":"43","author":"R Fukuyama","year":"2000","unstructured":"Fukuyama R, Mizuno T, Mizuno T et al (2000) Age-dependent change in the levels of Abeta40 and Abeta42 in cerebrospinal fluid from control subjects, and a decrease in the ratio of Abeta42 to Abeta40 level in cerebrospinal fluid from Alzheimer\u2019s disease patients. Eur Neurol 43:155\u2013160. https:\/\/doi.org\/10.1159\/000008156","journal-title":"Eur Neurol"},{"key":"4543_CR73","doi-asserted-by":"publisher","first-page":"2338","DOI":"10.1007\/S12035-016-9826-1\/TABLES\/2","volume":"54","author":"YR Wang","year":"2017","unstructured":"Wang YR, Wang QH, Zhang T et al (2017) Associations between hepatic functions and plasma amyloid-beta levels\u2014implications for the capacity of liver in peripheral amyloid-beta clearance. Mol Neurobiol 54:2338\u20132344. https:\/\/doi.org\/10.1007\/S12035-016-9826-1\/TABLES\/2","journal-title":"Mol Neurobiol"},{"key":"4543_CR74","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1007\/S12035-014-8854-Y\/FIGURES\/2","volume":"52","author":"YH Liu","year":"2015","unstructured":"Liu YH, Xiang Y, Wang YR et al (2015) Association between serum amyloid-beta and renal functions: implications for roles of kidney in amyloid-beta clearance. Mol Neurobiol 52:115\u2013119. https:\/\/doi.org\/10.1007\/S12035-014-8854-Y\/FIGURES\/2","journal-title":"Mol Neurobiol"},{"key":"4543_CR75","doi-asserted-by":"publisher","first-page":"13354","DOI":"10.18632\/ONCOTARGET.7997","volume":"7","author":"M Bosch-Morat\u00f3","year":"2016","unstructured":"Bosch-Morat\u00f3 M, Iriondo C, Guivernau B et al (2016) Increased amyloid \u03b2-peptide uptake in skeletal muscle is induced by hyposialylation and may account for apoptosis in GNE myopathy. Oncotarget 7:13354. https:\/\/doi.org\/10.18632\/ONCOTARGET.7997","journal-title":"Oncotarget"},{"key":"4543_CR76","doi-asserted-by":"publisher","first-page":"1495","DOI":"10.3233\/JAD-171133","volume":"62","author":"ML Gosztyla","year":"2018","unstructured":"Gosztyla ML, Brothers HM, Robinson SR (2018) Alzheimer\u2019s amyloid-\u03b2 is an antimicrobial peptide: a review of the evidence. J Alzheimers Dis 62:1495\u20131506. https:\/\/doi.org\/10.3233\/JAD-171133","journal-title":"J Alzheimers Dis"},{"key":"4543_CR77","doi-asserted-by":"publisher","first-page":"8368","DOI":"10.1073\/PNAS.91.18.8368","volume":"91","author":"AL Schwarzman","year":"1994","unstructured":"Schwarzman AL, Gregori L, Vitek MP et al (1994) Transthyretin sequesters amyloid beta protein and prevents amyloid formation. Proc Natl Acad Sci 91:8368\u20138372. https:\/\/doi.org\/10.1073\/PNAS.91.18.8368","journal-title":"Proc Natl Acad Sci"},{"key":"4543_CR78","doi-asserted-by":"publisher","DOI":"10.1080\/10408363.2024.2350379","author":"ZL Almeida","year":"2024","unstructured":"Almeida ZL, Vaz DC, Brito RMM (2024) Transthyretin mutagenesis: impact on amyloidogenesis and disease. Crit Rev Clin Lab Sci. https:\/\/doi.org\/10.1080\/10408363.2024.2350379","journal-title":"Crit Rev Clin Lab Sci"},{"key":"4543_CR79","doi-asserted-by":"publisher","first-page":"184","DOI":"10.1126\/SCIENCE.1566067\/ASSET\/74A758CB-215F-4A8E-9AAA-05F4D89DA62A\/ASSETS\/SCIENCE.1566067.FP.PNG","volume":"256","author":"JA Hardy","year":"1992","unstructured":"Hardy JA, Higgins GA (1992) Alzheimer\u2019s disease: the amyloid cascade hypothesis. Science (80-) 256:184\u2013185. https:\/\/doi.org\/10.1126\/SCIENCE.1566067\/ASSET\/74A758CB-215F-4A8E-9AAA-05F4D89DA62A\/ASSETS\/SCIENCE.1566067.FP.PNG","journal-title":"Science (80-)"},{"key":"4543_CR80","doi-asserted-by":"publisher","first-page":"755","DOI":"10.1007\/S00401-014-1349-0\/TABLES\/2","volume":"128","author":"JF Crary","year":"2014","unstructured":"Crary JF, Trojanowski JQ, Schneider JA et al (2014) Primary age-related tauopathy (PART): a common pathology associated with human aging. Acta Neuropathol 128:755\u2013766. https:\/\/doi.org\/10.1007\/S00401-014-1349-0\/TABLES\/2","journal-title":"Acta Neuropathol"},{"key":"4543_CR81","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1016\/0022-510X(77)90073-9","volume":"34","author":"EK Perry","year":"1977","unstructured":"Perry EK, Gibson PH, Blessed G et al (1977) Neurotransmitter enzyme abnormalities in senile dementia: choline acetyltransferase and glutamic acid decarboxylase activities in necropsy brain tissue. J Neurol Sci 34:247\u2013265. https:\/\/doi.org\/10.1016\/0022-510X(77)90073-9","journal-title":"J Neurol Sci"},{"key":"4543_CR82","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1111\/J.1365-2990.1978.TB00545.X","volume":"4","author":"EK Perry","year":"1978","unstructured":"Perry EK, Perry RH, Blessed G, Tomlinson BE (1978) Changes in brain cholinesterases in senile dementia of Alzheimer type. Neuropathol Appl Neurobiol 4:273\u2013277. https:\/\/doi.org\/10.1111\/J.1365-2990.1978.TB00545.X","journal-title":"Neuropathol Appl Neurobiol"},{"key":"4543_CR83","doi-asserted-by":"publisher","first-page":"1234","DOI":"10.1001\/ARCHNEUR.1997.00550220042012","volume":"54","author":"JW Olney","year":"1997","unstructured":"Olney JW, Wozniak DF, Farber NB (1997) Excitotoxic neurodegeneration in Alzheimer disease: new hypothesis and new therapeutic strategies. Arch Neurol 54:1234\u20131240. https:\/\/doi.org\/10.1001\/ARCHNEUR.1997.00550220042012","journal-title":"Arch Neurol"},{"key":"4543_CR84","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1126\/SCIENCE.7901908","volume":"262","author":"JT Coyle","year":"1993","unstructured":"Coyle JT, Puttfarcken P (1993) Oxidative Stress, Glutamate, and Neurodegenerative Disorders. Science (80-) 262:689\u2013695. https:\/\/doi.org\/10.1126\/SCIENCE.7901908","journal-title":"Science (80-)"},{"key":"4543_CR85","doi-asserted-by":"publisher","first-page":"214","DOI":"10.1016\/J.NEURON.2008.06.008","volume":"59","author":"KV Kuchibhotla","year":"2008","unstructured":"Kuchibhotla KV, Goldman ST, Lattarulo CR et al (2008) Abeta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks. Neuron 59:214\u2013225. https:\/\/doi.org\/10.1016\/J.NEURON.2008.06.008","journal-title":"Neuron"},{"key":"4543_CR86","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1016\/J.PNEUROBIO.2009.07.009","volume":"89","author":"JT Yu","year":"2009","unstructured":"Yu JT, Chang RCC, Tan L (2009) Calcium dysregulation in Alzheimer\u2019s disease: from mechanisms to therapeutic opportunities. Prog Neurobiol 89:240\u2013255. https:\/\/doi.org\/10.1016\/J.PNEUROBIO.2009.07.009","journal-title":"Prog Neurobiol"},{"key":"4543_CR87","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1039\/C0MT00074D","volume":"3","author":"DJ Bonda","year":"2011","unstructured":"Bonda DJ, Lee HG, Blair JA et al (2011) Role of metal dyshomeostasis in Alzheimer\u2019s disease. Metallomics 3:267\u2013270. https:\/\/doi.org\/10.1039\/C0MT00074D","journal-title":"Metallomics"},{"key":"4543_CR88","doi-asserted-by":"publisher","first-page":"1467","DOI":"10.1212\/WNL.43.8.1467","volume":"43","author":"AM Saunders","year":"1993","unstructured":"Saunders AM, Strittmatter WJ, Schmechel D et al (1993) Association of apolipoprotein E allele \u03f54 with late-onset familial and sporadic Alzheimer\u2019s disease. Neurology 43:1467\u20131472. https:\/\/doi.org\/10.1212\/WNL.43.8.1467","journal-title":"Neurology"},{"key":"4543_CR89","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1097\/00005072-199701000-00007","volume":"56","author":"JJ Pei","year":"1997","unstructured":"Pei JJ, Tanaka T, Tung YC et al (1997) Distribution, levels, and activity of glycogen synthase kinase-3 in the Alzheimer disease brain. J Neuropathol Exp Neurol 56:70\u201378. https:\/\/doi.org\/10.1097\/00005072-199701000-00007","journal-title":"J Neuropathol Exp Neurol"},{"key":"4543_CR90","doi-asserted-by":"publisher","first-page":"13217","DOI":"10.1073\/PNAS.172504199","volume":"99","author":"OV Vitolo","year":"2002","unstructured":"Vitolo OV, Sant\u2019Angelo A, Costanzo V et al (2002) Amyloid \u03b2-peptide inhibition of the PKA\/CREB pathway and long-term potentiation: reversibility by drugs that enhance cAMP signaling. Proc Natl Acad Sci 99:13217\u201313221. https:\/\/doi.org\/10.1073\/PNAS.172504199","journal-title":"Proc Natl Acad Sci"},{"key":"4543_CR91","doi-asserted-by":"publisher","first-page":"878","DOI":"10.1016\/J.BBADIS.2015.12.023","volume":"1862","author":"A Kapasi","year":"2016","unstructured":"Kapasi A, Schneider JA (2016) Vascular contributions to cognitive impairment, clinical Alzheimer\u2019s disease, and dementia in older persons. Biochim Biophys Acta - Mol Basis Dis 1862:878\u2013886. https:\/\/doi.org\/10.1016\/J.BBADIS.2015.12.023","journal-title":"Biochim Biophys Acta - Mol Basis Dis"},{"key":"4543_CR92","doi-asserted-by":"publisher","first-page":"1101","DOI":"10.1177\/193229680800200619","volume":"2","author":"SM De La Monte","year":"2008","unstructured":"De La Monte SM, Wands JR (2008) Alzheimer\u2019s disease is type 3 diabetes\u2014evidence reviewed. J Diabetes Sci Technol 2:1101\u20131113. https:\/\/doi.org\/10.1177\/193229680800200619","journal-title":"J Diabetes Sci Technol"},{"key":"4543_CR93","doi-asserted-by":"publisher","first-page":"460","DOI":"10.1038\/74833","volume":"3","author":"A Lorenzo","year":"2000","unstructured":"Lorenzo A, Yuan M, Zhang Z et al (2000) Amyloid \u03b2 interacts with the amyloid precursor protein: a potential toxic mechanism in Alzheimer\u2019s disease. Nat Neurosci 3:460\u2013464. https:\/\/doi.org\/10.1038\/74833","journal-title":"Nat Neurosci"},{"key":"4543_CR94","doi-asserted-by":"publisher","first-page":"8501693","DOI":"10.1155\/2016\/8501693","volume":"2016","author":"J Folch","year":"2016","unstructured":"Folch J, Petrov D, Ettcheto M et al (2016) Current research therapeutic strategies for Alzheimer\u2019s disease treatment. Neural Plast 2016:8501693. https:\/\/doi.org\/10.1155\/2016\/8501693","journal-title":"Neural Plast"},{"key":"4543_CR95","doi-asserted-by":"publisher","first-page":"7361613","DOI":"10.1155\/2016\/7361613","volume":"2016","author":"SK Singh","year":"2016","unstructured":"Singh SK, Srivastav S, Yadav AK et al (2016) Overview of Alzheimer\u2019s disease and some therapeutic approaches targeting A \u03b2 by using several synthetic and herbal compounds. Oxid Med Cell Longev 2016:7361613. https:\/\/doi.org\/10.1155\/2016\/7361613","journal-title":"Oxid Med Cell Longev"},{"key":"4543_CR96","doi-asserted-by":"publisher","first-page":"451","DOI":"10.2119\/2007-00100.IRVINE","volume":"14","author":"GB Irvine","year":"2008","unstructured":"Irvine GB, El-Agnaf OM, Shankar GM, Walsh DM (2008) Protein aggregation in the brain: the molecular basis for Alzheimer\u2019s and Parkinson\u2019s diseases. Mol Med 14:451\u2013464. https:\/\/doi.org\/10.2119\/2007-00100.IRVINE","journal-title":"Mol Med"},{"key":"4543_CR97","doi-asserted-by":"publisher","first-page":"672","DOI":"10.1038\/360672A0","volume":"360","author":"M Citron","year":"1992","unstructured":"Citron M, Oltersdorf T, Haass C et al (1992) Mutation of the beta-amyloid precursor protein in familial Alzheimer\u2019s disease increases beta-protein production. Nature 360:672\u2013674. https:\/\/doi.org\/10.1038\/360672A0","journal-title":"Nature"},{"key":"4543_CR98","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1006\/nbdi.1996.0016","volume":"3","author":"RE Tanzi","year":"1996","unstructured":"Tanzi RE, Kovacs DM, Kim TW et al (1996) The gene defects responsible for familial Alzheimer\u2019s disease. Neurobiol Dis 3:159\u2013168. https:\/\/doi.org\/10.1006\/nbdi.1996.0016","journal-title":"Neurobiol Dis"},{"key":"4543_CR99","first-page":"1633","volume":"152","author":"H Funato","year":"1998","unstructured":"Funato H, Yoshimura M, Kusui K et al (1998) Quantitation of amyloid beta-protein (A beta) in the cortex during aging and in Alzheimer\u2019s disease. Am J Pathol 152:1633","journal-title":"Am J Pathol"},{"key":"4543_CR100","doi-asserted-by":"publisher","first-page":"a006338","DOI":"10.1101\/CSHPERSPECT.A006338","volume":"2","author":"L Mucke","year":"2012","unstructured":"Mucke L, Selkoe DJ (2012) Neurotoxicity of amyloid \u03b2-protein: synaptic and network dysfunction. Cold Spring Harb Perspect Med 2:a006338. https:\/\/doi.org\/10.1101\/CSHPERSPECT.A006338","journal-title":"Cold Spring Harb Perspect Med"},{"key":"4543_CR101","doi-asserted-by":"publisher","first-page":"142972","DOI":"10.3389\/FNCEL.2015.00191\/BIBTEX","volume":"9","author":"ST Ferreira","year":"2015","unstructured":"Ferreira ST, Lourenco MV, Oliveira MM, De Felice FG (2015) Soluble amyloid-\u03b2 oligomers as synaptotoxins leading to cognitive impairment in Alzheimer\u2019s disease. Front Cell Neurosci 9:142972. https:\/\/doi.org\/10.3389\/FNCEL.2015.00191\/BIBTEX","journal-title":"Front Cell Neurosci"},{"key":"4543_CR102","doi-asserted-by":"publisher","first-page":"1984","DOI":"10.1212\/01.WNL.0000129697.01779.0A","volume":"62","author":"P Tiraboschi","year":"2004","unstructured":"Tiraboschi P, Hansen LA, Thal LJ, Corey-Bloom J (2004) The importance of neuritic plaques and tangles to the development and evolution of AD. Neurology 62:1984\u20131989. https:\/\/doi.org\/10.1212\/01.WNL.0000129697.01779.0A","journal-title":"Neurology"},{"key":"4543_CR103","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1007\/S00401-015-1525-X\/FIGURES\/9","volume":"131","author":"B Vasconcelos","year":"2016","unstructured":"Vasconcelos B, Stancu IC, Buist A et al (2016) Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo. Acta Neuropathol 131:549\u2013569. https:\/\/doi.org\/10.1007\/S00401-015-1525-X\/FIGURES\/9","journal-title":"Acta Neuropathol"},{"key":"4543_CR104","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1016\/S0014-5793(02)02376-1","volume":"514","author":"KB Rank","year":"2002","unstructured":"Rank KB, Pauley AM, Bhattacharya K et al (2002) Direct interaction of soluble human recombinant Tau protein with A\u03b2 1\u201342 results in Tau aggregation and hyperphosphorylation by Tau protein kinase II. FEBS Lett 514:263\u2013268. https:\/\/doi.org\/10.1016\/S0014-5793(02)02376-1","journal-title":"FEBS Lett"},{"key":"4543_CR105","doi-asserted-by":"publisher","first-page":"1491","DOI":"10.1126\/SCIENCE.1062097","volume":"293","author":"J G\u00f6tz","year":"2001","unstructured":"G\u00f6tz J, Chen F, Van Dorpe J, Nitsch RM (2001) Formation of neurofibrillary tangles in P301l Tau transgenic mice induced by Abeta 42 fibrils. Science 293:1491\u20131495. https:\/\/doi.org\/10.1126\/SCIENCE.1062097","journal-title":"Science"},{"issue":"664\u2013683","key":"4543_CR106","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1038\/sj.mp.4001508","volume":"9","author":"J G\u00f6tz","year":"2004","unstructured":"G\u00f6tz J, Streffer JR, David D et al (2004) Transgenic animal models of Alzheimer\u2019s disease and related disorders: histopathology, behavior and therapy. Mol Psychiatry 9(664\u2013683):683. https:\/\/doi.org\/10.1038\/sj.mp.4001508","journal-title":"Mol Psychiatry"},{"key":"4543_CR107","doi-asserted-by":"publisher","first-page":"328460","DOI":"10.3389\/FNINS.2018.00025\/BIBTEX","volume":"12","author":"F Kametani","year":"2018","unstructured":"Kametani F, Hasegawa M (2018) Reconsideration of amyloid hypothesis and Tau hypothesis in Alzheimer\u2019s disease. Front Neurosci 12:328460. https:\/\/doi.org\/10.3389\/FNINS.2018.00025\/BIBTEX","journal-title":"Front Neurosci"},{"key":"4543_CR108","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1001\/ARCHNEUROL.2011.1538","volume":"69","author":"S Ostrowitzki","year":"2012","unstructured":"Ostrowitzki S, Deptula D, Thurfjell L et al (2012) Mechanism of amyloid removal in patients with Alzheimer disease treated with gantenerumab. Arch Neurol 69:198\u2013207. https:\/\/doi.org\/10.1001\/ARCHNEUROL.2011.1538","journal-title":"Arch Neurol"},{"key":"4543_CR109","doi-asserted-by":"publisher","first-page":"677","DOI":"10.1038\/NRNEUROL.2013.223","volume":"9","author":"E Giacobini","year":"2013","unstructured":"Giacobini E, Gold G (2013) Alzheimer disease therapy\u2013moving from amyloid-\u03b2 to Tau. Nat Rev Neurol 9:677\u2013686. https:\/\/doi.org\/10.1038\/NRNEUROL.2013.223","journal-title":"Nat Rev Neurol"},{"key":"4543_CR110","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1056\/NEJMOA1312889","volume":"370","author":"RS Doody","year":"2014","unstructured":"Doody RS, Thomas RG, Farlow M et al (2014) Phase 3 trials of solanezumab for mild-to-moderate Alzheimer\u2019s disease. N Engl J Med 370:311\u2013321. https:\/\/doi.org\/10.1056\/NEJMOA1312889","journal-title":"N Engl J Med"},{"key":"4543_CR111","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1056\/NEJMOA1304839\/SUPPL_FILE\/NEJMOA1304839_DISCLOSURES.PDF","volume":"370","author":"S Salloway","year":"2014","unstructured":"Salloway S, Sperling R, Fox NC et al (2014) Two phase 3 trials of bapineuzumab in mild-to-moderate Alzheimer\u2019s disease. N Engl J Med 370:322\u2013333. https:\/\/doi.org\/10.1056\/NEJMOA1304839\/SUPPL_FILE\/NEJMOA1304839_DISCLOSURES.PDF","journal-title":"N Engl J Med"},{"key":"4543_CR112","doi-asserted-by":"publisher","first-page":"1026","DOI":"10.1016\/J.NEUROBIOLAGING.2009.04.002","volume":"30","author":"JL Price","year":"2009","unstructured":"Price JL, McKeel DW, Buckles VD et al (2009) Neuropathology of nondemented aging: presumptive evidence for preclinical Alzheimer disease. Neurobiol Aging 30:1026\u20131036. https:\/\/doi.org\/10.1016\/J.NEUROBIOLAGING.2009.04.002","journal-title":"Neurobiol Aging"},{"key":"4543_CR113","doi-asserted-by":"publisher","first-page":"356","DOI":"10.1016\/J.NICL.2013.02.006","volume":"2","author":"G Ch\u00e9telat","year":"2013","unstructured":"Ch\u00e9telat G, La Joie R, Villain N et al (2013) Amyloid imaging in cognitively normal individuals, at-risk populations and preclinical Alzheimer\u2019s disease. NeuroImage Clin 2:356\u2013365. https:\/\/doi.org\/10.1016\/J.NICL.2013.02.006","journal-title":"NeuroImage Clin"},{"key":"4543_CR114","doi-asserted-by":"publisher","first-page":"1924","DOI":"10.1001\/JAMA.2015.4668","volume":"313","author":"WJ Jansen","year":"2015","unstructured":"Jansen WJ, Ossenkoppele R, Knol DL et al (2015) Prevalence of cerebral amyloid pathology in persons without dementia: A Meta-analysis. JAMA 313:1924\u20131938. https:\/\/doi.org\/10.1001\/JAMA.2015.4668","journal-title":"JAMA"},{"key":"4543_CR115","doi-asserted-by":"publisher","first-page":"745","DOI":"10.1016\/J.NEUROSCIENCE.2007.10.054","volume":"151","author":"S Lesn\u00e9","year":"2008","unstructured":"Lesn\u00e9 S, Kotilinek L, Ashe KH (2008) Plaque-bearing mice with reduced levels of oligomeric amyloid-\u03b2 assemblies have intact memory function. Neuroscience 151:745\u2013749. https:\/\/doi.org\/10.1016\/J.NEUROSCIENCE.2007.10.054","journal-title":"Neuroscience"},{"key":"4543_CR116","doi-asserted-by":"publisher","first-page":"1791","DOI":"10.1212\/WNL.58.12.1791","volume":"58","author":"DR Thal","year":"2002","unstructured":"Thal DR, R\u00fcb U, Orantes M, Braak H (2002) Phases of A beta-deposition in the human brain and its relevance for the development of AD. Neurology 58:1791\u20131800. https:\/\/doi.org\/10.1212\/WNL.58.12.1791","journal-title":"Neurology"},{"key":"4543_CR117","doi-asserted-by":"publisher","first-page":"re1","DOI":"10.1126\/SAGEKE.2006.6.RE1\/ASSET\/01189700-5FAD-4ACF-8ED0-F057B38E2ED5\/ASSETS\/GRAPHIC\/62006RE1F5.JPEG","volume":"2006","author":"DR Thal","year":"2006","unstructured":"Thal DR, Capetillo-Zarate E, Del Tredici K, Braak H (2006) The development of amyloid beta protein deposits in the aged brain. Sci Aging Knowledge Environ 2006:re1. https:\/\/doi.org\/10.1126\/SAGEKE.2006.6.RE1\/ASSET\/01189700-5FAD-4ACF-8ED0-F057B38E2ED5\/ASSETS\/GRAPHIC\/62006RE1F5.JPEG","journal-title":"Sci Aging Knowledge Environ"},{"key":"4543_CR118","doi-asserted-by":"publisher","first-page":"4491","DOI":"10.1523\/JNEUROSCI.16-14-04491.1996","volume":"16","author":"T G\u00f3mez-Isla","year":"1996","unstructured":"G\u00f3mez-Isla T, Price JL, McKeel DW et al (1996) Profound loss of layer II entorhinal cortex neurons occurs in very mild Alzheimer\u2019s disease. J Neurosci 16:4491\u20134500. https:\/\/doi.org\/10.1523\/JNEUROSCI.16-14-04491.1996","journal-title":"J Neurosci"},{"key":"4543_CR119","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1016\/0304-3940(88)90080-8","volume":"93","author":"F Tagliavini","year":"1988","unstructured":"Tagliavini F, Giaccone G, Frangione B, Bugiani O (1988) Preamyloid deposits in the cerebral cortex of patients with Alzheimer\u2019s disease and nondemented individuals. Neurosci Lett 93:191\u2013196. https:\/\/doi.org\/10.1016\/0304-3940(88)90080-8","journal-title":"Neurosci Lett"},{"key":"4543_CR120","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1159\/000017051","volume":"9","author":"RA Armstrong","year":"1998","unstructured":"Armstrong RA (1998) \u03b2-amyloid plaques: stages in life history or independent origin? Dement Geriatr Cogn Disord 9:227\u2013238. https:\/\/doi.org\/10.1159\/000017051","journal-title":"Dement Geriatr Cogn Disord"},{"key":"4543_CR121","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/IJMS22010007","volume":"22","author":"N Jankovska","year":"2020","unstructured":"Jankovska N, Olejar T, Matej R (2020) Extracellular amyloid deposits in Alzheimer\u2019s and Creutzfeldt-Jakob disease: similar behavior of different proteins? Int J Mol Sci 22:1\u201319. https:\/\/doi.org\/10.3390\/IJMS22010007","journal-title":"Int J Mol Sci"},{"key":"4543_CR122","doi-asserted-by":"publisher","first-page":"a006189","DOI":"10.1101\/CSHPERSPECT.A006189","volume":"1","author":"A Serrano-Pozo","year":"2011","unstructured":"Serrano-Pozo A, Frosch MP, Masliah E, Hyman BT (2011) Neuropathological alterations in Alzheimer disease. Cold Spring Harb Perspect Med 1:a006189. https:\/\/doi.org\/10.1101\/CSHPERSPECT.A006189","journal-title":"Cold Spring Harb Perspect Med"},{"key":"4543_CR123","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/S11910-014-0499-8","volume":"14","author":"JM Ringman","year":"2014","unstructured":"Ringman JM, Goate A, Masters CL et al (2014) Genetic heterogeneity in Alzheimer disease and implications for treatment strategies. Curr Neurol Neurosci Rep 14:1. https:\/\/doi.org\/10.1007\/S11910-014-0499-8","journal-title":"Curr Neurol Neurosci Rep"},{"key":"4543_CR124","doi-asserted-by":"publisher","first-page":"960","DOI":"10.1097\/NEN.0B013E318232A379","volume":"70","author":"H Braak","year":"2011","unstructured":"Braak H, Thal DR, Ghebremedhin E, Del Tredici K (2011) Stages of the pathologic process in Alzheimer disease: age categories from 1 to 100 years. J Neuropathol Exp Neurol 70:960\u2013969. https:\/\/doi.org\/10.1097\/NEN.0B013E318232A379","journal-title":"J Neuropathol Exp Neurol"},{"key":"4543_CR125","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1016\/0304-3940(90)90391-L","volume":"116","author":"P Dela\u00e8re","year":"1990","unstructured":"Dela\u00e8re P, Duyckaerts C, Masters C et al (1990) Large amounts of neocortical \u03b2A4 deposits without neuritic plaques nor tangles in a psychometrically assessed, non-demented person. Neurosci Lett 116:87\u201393. https:\/\/doi.org\/10.1016\/0304-3940(90)90391-L","journal-title":"Neurosci Lett"},{"key":"4543_CR126","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/0197-4580(92)90027-U","volume":"13","author":"DW Dickson","year":"1992","unstructured":"Dickson DW, Crystal HA, Mattiace LA et al (1992) Identification of normal and pathological aging in prospectively studied nondemented elderly humans. Neurobiol Aging 13:179\u2013189. https:\/\/doi.org\/10.1016\/0197-4580(92)90027-U","journal-title":"Neurobiol Aging"},{"key":"4543_CR127","doi-asserted-by":"crossref","unstructured":"Dawbarn D, Allen SJ (2007) Neurobiology of alzheimer\u2019s disease,\u00a03rd edn. Oxford University Press","DOI":"10.1093\/oso\/9780198566618.001.0001"},{"key":"4543_CR128","doi-asserted-by":"publisher","first-page":"987","DOI":"10.1016\/S0002-9440(10)63360-3","volume":"165","author":"T Bussi\u00e8re","year":"2004","unstructured":"Bussi\u00e8re T, Bard F, Barbour R et al (2004) Morphological characterization of thioflavin-S-positive amyloid plaques in transgenic alzheimer mice and effect of passive A\u03b2 immunotherapy on their clearance. Am J Pathol 165:987\u2013995. https:\/\/doi.org\/10.1016\/S0002-9440(10)63360-3","journal-title":"Am J Pathol"},{"key":"4543_CR129","doi-asserted-by":"publisher","first-page":"2607","DOI":"10.1093\/BRAIN\/AWM191","volume":"130","author":"A Lockhart","year":"2007","unstructured":"Lockhart A, Lamb JR, Osredkar T et al (2007) PIB is a non-specific imaging marker of amyloid-beta (A\u03b2) peptide-related cerebral amyloidosis. Brain 130:2607\u20132615. https:\/\/doi.org\/10.1093\/BRAIN\/AWM191","journal-title":"Brain"},{"key":"4543_CR130","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1007\/BF00692843\/METRICS","volume":"74","author":"A Probst","year":"1987","unstructured":"Probst A, Brunnschweiler H, Lautenschlager C, Ulrich J (1987) A special type of senile plaque, possibly an initial stage. Acta Neuropathol 74:133\u2013141. https:\/\/doi.org\/10.1007\/BF00692843\/METRICS","journal-title":"Acta Neuropathol"},{"key":"4543_CR131","doi-asserted-by":"publisher","first-page":"10424","DOI":"10.1021\/BI990718V","volume":"38","author":"BP Tseng","year":"1999","unstructured":"Tseng BP, Esler WP, Clish CB et al (1999) Deposition of monomeric, not oligomeric, Abeta mediates growth of Alzheimer\u2019s disease amyloid plaques in human brain preparations. Biochemistry 38:10424\u201310431. https:\/\/doi.org\/10.1021\/BI990718V","journal-title":"Biochemistry"},{"key":"4543_CR132","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/S0306-4522(01)00169-5","volume":"105","author":"TC Dickson","year":"2001","unstructured":"Dickson TC, Vickers JC (2001) The morphological phenotype of beta-amyloid plaques and associated neuritic changes in Alzheimer\u2019s disease. Neuroscience 105:99\u2013107. https:\/\/doi.org\/10.1016\/S0306-4522(01)00169-5","journal-title":"Neuroscience"},{"key":"4543_CR133","doi-asserted-by":"publisher","first-page":"461","DOI":"10.1016\/J.NEUROSCIENCE.2006.08.027","volume":"143","author":"A G\u00fcntert","year":"2006","unstructured":"G\u00fcntert A, D\u00f6beli H, Bohrmann B (2006) High sensitivity analysis of amyloid-beta peptide composition in amyloid deposits from human and PS2APP mouse brain. Neuroscience 143:461\u2013475. https:\/\/doi.org\/10.1016\/J.NEUROSCIENCE.2006.08.027","journal-title":"Neuroscience"},{"key":"4543_CR134","first-page":"1293","volume":"137","author":"E Masliah","year":"1990","unstructured":"Masliah E, Terry RD, Mallory M et al (1990) Diffuse plaques do not accentuate synapse loss in Alzheimer\u2019s disease. Am J Pathol 137:1293","journal-title":"Am J Pathol"},{"key":"4543_CR135","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/S13024-019-0333-5","volume":"14","author":"MA Deture","year":"2019","unstructured":"Deture MA, Dickson DW (2019) The neuropathological diagnosis of Alzheimer\u2019s disease. Mol Neurodegener 14:1\u201318. https:\/\/doi.org\/10.1186\/S13024-019-0333-5","journal-title":"Mol Neurodegener"},{"key":"4543_CR136","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1016\/0165-5728(89)90115-X","volume":"24","author":"S Itagaki","year":"1989","unstructured":"Itagaki S, McGeer PL, Akiyama H et al (1989) Relationship of microglia and astrocytes to amyloid deposits of Alzheimer disease. J Neuroimmunol 24:173\u2013182. https:\/\/doi.org\/10.1016\/0165-5728(89)90115-X","journal-title":"J Neuroimmunol"},{"key":"4543_CR137","unstructured":"Perry A, Brat DJ (2018) Practical surgical neuropathology: a diagnostic approach, 2nd edn. Elsevier"},{"key":"4543_CR138","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/srep43477","volume":"7","author":"B Baumann","year":"2017","unstructured":"Baumann B, Woehrer A, Ricken G et al (2017) Visualization of neuritic plaques in Alzheimer\u2019s disease by polarization-sensitive optical coherence microscopy. Sci Reports 7:1\u201312. https:\/\/doi.org\/10.1038\/srep43477","journal-title":"Sci Reports"},{"key":"4543_CR139","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1002\/MSJ.20157","volume":"77","author":"DP Perl","year":"2010","unstructured":"Perl DP (2010) Neuropathology of Alzheimer\u2019s disease. Mt Sinai J Med A J Transl Pers Med 77:32\u201342. https:\/\/doi.org\/10.1002\/MSJ.20157","journal-title":"Mt Sinai J Med A J Transl Pers Med"},{"key":"4543_CR140","doi-asserted-by":"publisher","first-page":"13S","DOI":"10.2967\/JNUMED.121.263195","volume":"63","author":"M Chapleau","year":"2022","unstructured":"Chapleau M, Iaccarino L, Soleimani-Meigooni D, Rabinovici GD (2022) The role of amyloid PET in imaging neurodegenerative disorders: a review. J Nucl Med 63:13S-19S. https:\/\/doi.org\/10.2967\/JNUMED.121.263195","journal-title":"J Nucl Med"},{"key":"4543_CR141","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1002\/ANA.410300503","volume":"30","author":"JPG Vonsattel","year":"1991","unstructured":"Vonsattel JPG, Myers RH, Tessa Hedley-Whyte E et al (1991) Cerebral amyloid angiopathy without and with cerebral hemorrhages: a comparative histological study. Ann Neurol 30:637\u2013649. https:\/\/doi.org\/10.1002\/ANA.410300503","journal-title":"Ann Neurol"},{"key":"4543_CR142","doi-asserted-by":"publisher","first-page":"1418","DOI":"10.1161\/01.STR.28.7.1418","volume":"28","author":"SM Greenberg","year":"1997","unstructured":"Greenberg SM, Vonsattel JPG (1997) Diagnosis of cerebral amyloid angiopathy. Stroke 28:1418\u20131422. https:\/\/doi.org\/10.1161\/01.STR.28.7.1418","journal-title":"Stroke"},{"key":"4543_CR143","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1073\/PNAS.222681699","volume":"100","author":"GB Marina","year":"2003","unstructured":"Marina GB, Kirkitadze D, Lomakin A et al (2003) Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci U S A 100:330\u2013335. https:\/\/doi.org\/10.1073\/PNAS.222681699","journal-title":"Proc Natl Acad Sci U S A"},{"key":"4543_CR144","doi-asserted-by":"publisher","first-page":"4766","DOI":"10.1073\/PNAS.91.11.4766","volume":"91","author":"MP Vitek","year":"1994","unstructured":"Vitek MP, Bhattacharya K, Glendening JM et al (1994) Advanced glycation end products contribute to amyloidosis in Alzheimer disease. Proc Natl Acad Sci 91:4766\u20134770. https:\/\/doi.org\/10.1073\/PNAS.91.11.4766","journal-title":"Proc Natl Acad Sci"},{"key":"4543_CR145","doi-asserted-by":"publisher","first-page":"10039","DOI":"10.1021\/BI1016233\/SUPPL_FILE\/BI1016233_SI_001.PDF","volume":"49","author":"CA Lasagna-Reeves","year":"2010","unstructured":"Lasagna-Reeves CA, Castillo-Carranza DL, Guerrero-Mu\u00f1oz MJ et al (2010) Preparation and characterization of neurotoxic Tau oligomers. Biochemistry 49:10039\u201310041. https:\/\/doi.org\/10.1021\/BI1016233\/SUPPL_FILE\/BI1016233_SI_001.PDF","journal-title":"Biochemistry"},{"key":"4543_CR146","doi-asserted-by":"publisher","first-page":"594","DOI":"10.1111\/JNC.13443","volume":"136","author":"MK Jana","year":"2016","unstructured":"Jana MK, Cappai R, Pham CLL, Ciccotosto GD (2016) Membrane-bound tetramer and trimer A\u03b2 oligomeric species correlate with toxicity towards cultured neurons. J Neurochem 136:594\u2013608. https:\/\/doi.org\/10.1111\/JNC.13443","journal-title":"J Neurochem"},{"key":"4543_CR147","doi-asserted-by":"publisher","first-page":"20631","DOI":"10.1074\/JBC.271.34.20631","volume":"271","author":"AE Roher","year":"1996","unstructured":"Roher AE, Chaney MO, Kuo YM et al (1996) Morphology and toxicity of Abeta-(1\u201342) dimer derived from neuritic and vascular amyloid deposits of Alzheimer\u2019s disease. J Biol Chem 271:20631\u201320635. https:\/\/doi.org\/10.1074\/JBC.271.34.20631","journal-title":"J Biol Chem"},{"key":"4543_CR148","doi-asserted-by":"publisher","first-page":"837","DOI":"10.1038\/NM1782","volume":"14","author":"GM Shankar","year":"2008","unstructured":"Shankar GM, Li S, Mehta TH et al (2008) Amyloid-beta protein dimers isolated directly from Alzheimer\u2019s brains impair synaptic plasticity and memory. Nat Med 14:837\u2013842. https:\/\/doi.org\/10.1038\/NM1782","journal-title":"Nat Med"},{"key":"4543_CR149","doi-asserted-by":"publisher","first-page":"6150","DOI":"10.1021\/ACS.BIOCHEM.6B00453\/ASSET\/IMAGES\/LARGE\/BI-2016-00453C_0007.JPEG","volume":"55","author":"TT O\u2019Malley","year":"2016","unstructured":"O\u2019Malley TT, Witbold WM, Linse S, Walsh DM (2016) The aggregation paths and products of A\u03b242 dimers are distinct from those of the A\u03b242 monomer. Biochemistry 55:6150\u20136161. https:\/\/doi.org\/10.1021\/ACS.BIOCHEM.6B00453\/ASSET\/IMAGES\/LARGE\/BI-2016-00453C_0007.JPEG","journal-title":"Biochemistry"},{"key":"4543_CR150","doi-asserted-by":"publisher","first-page":"5819","DOI":"10.1073\/PNAS.1017033108","volume":"108","author":"M Jin","year":"2011","unstructured":"Jin M, Shepardson N, Yang T et al (2011) Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration. Proc Natl Acad Sci U S A 108:5819\u20135824. https:\/\/doi.org\/10.1073\/PNAS.1017033108","journal-title":"Proc Natl Acad Sci U S A"},{"key":"4543_CR151","doi-asserted-by":"publisher","first-page":"1441","DOI":"10.1093\/BRAIN\/AWZ066","volume":"142","author":"G Brinkmalm","year":"2019","unstructured":"Brinkmalm G, Hong W, Wang Z et al (2019) Identification of neurotoxic cross-linked amyloid-\u03b2 dimers in the Alzheimer\u2019s brain. Brain 142:1441\u20131457. https:\/\/doi.org\/10.1093\/BRAIN\/AWZ066","journal-title":"Brain"},{"key":"4543_CR152","doi-asserted-by":"publisher","first-page":"10831","DOI":"10.1021\/BI001048S","volume":"39","author":"DM Walsh","year":"2000","unstructured":"Walsh DM, Tseng BP, Rydel RE et al (2000) The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry 39:10831\u201310839. https:\/\/doi.org\/10.1021\/BI001048S","journal-title":"Biochemistry"},{"key":"4543_CR153","doi-asserted-by":"publisher","first-page":"352","DOI":"10.1038\/nature04533","volume":"440","author":"S Lesn\u00e9","year":"2006","unstructured":"Lesn\u00e9 S, Ming TK, Kotilinek L et al (2006) A specific amyloid-\u03b2 protein assembly in the brain impairs memory. Nat 440:352\u2013357. https:\/\/doi.org\/10.1038\/nature04533","journal-title":"Nat"},{"key":"4543_CR154","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1113\/JPHYSIOL.2005.103754","volume":"572","author":"M Townsend","year":"2006","unstructured":"Townsend M, Shankar GM, Mehta T et al (2006) Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: a potent role for trimers. J Physiol 572:477\u2013492. https:\/\/doi.org\/10.1113\/JPHYSIOL.2005.103754","journal-title":"J Physiol"},{"key":"4543_CR155","doi-asserted-by":"publisher","first-page":"11555","DOI":"10.1074\/JBC.M110.181313","volume":"286","author":"S Matsumura","year":"2011","unstructured":"Matsumura S, Shinoda K, Yamada M et al (2011) Two distinct amyloid beta-protein (Abeta) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses. J Biol Chem 286:11555\u201311562. https:\/\/doi.org\/10.1074\/JBC.M110.181313","journal-title":"J Biol Chem"},{"key":"4543_CR156","doi-asserted-by":"publisher","first-page":"1383","DOI":"10.1093\/BRAIN\/AWT062","volume":"136","author":"SE Lesn\u00e9","year":"2013","unstructured":"Lesn\u00e9 SE, Sherman MA, Grant M et al (2013) Brain amyloid-\u03b2 oligomers in ageing and Alzheimer\u2019s disease. Brain 136:1383\u20131398. https:\/\/doi.org\/10.1093\/BRAIN\/AWT062","journal-title":"Brain"},{"key":"4543_CR157","doi-asserted-by":"publisher","first-page":"6448","DOI":"10.1073\/PNAS.95.11.6448","volume":"95","author":"MP Lambert","year":"1998","unstructured":"Lambert MP, Barlow AK, Chromy BA et al (1998) Diffusible, nonfibrillar ligands derived from A\u03b21\u201342 are potent central nervous system neurotoxins. Proc Natl Acad Sci 95:6448\u20136453. https:\/\/doi.org\/10.1073\/PNAS.95.11.6448","journal-title":"Proc Natl Acad Sci"},{"key":"4543_CR158","doi-asserted-by":"publisher","first-page":"10417","DOI":"10.1073\/PNAS.1834302100","volume":"100","author":"Y Gong","year":"2003","unstructured":"Gong Y, Chang L, Viola KL et al (2003) Alzheimer\u2019s disease-affected brain: Presence of oligomeric A\u03b2 ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc Natl Acad Sci 100:10417\u201310422. https:\/\/doi.org\/10.1073\/PNAS.1834302100","journal-title":"Proc Natl Acad Sci"},{"key":"4543_CR159","doi-asserted-by":"publisher","first-page":"10191","DOI":"10.1523\/JNEUROSCI.3432-04.2004","volume":"24","author":"PN Lacor","year":"2004","unstructured":"Lacor PN, Buniel MC, Chang L et al (2004) Synaptic targeting by Alzheimer\u2019s-related amyloid \u03b2 oligomers. J Neurosci 24:10191\u201310200. https:\/\/doi.org\/10.1523\/JNEUROSCI.3432-04.2004","journal-title":"J Neurosci"},{"key":"4543_CR160","doi-asserted-by":"publisher","first-page":"15157","DOI":"10.1021\/BI061850F\/ASSET\/IMAGES\/LARGE\/BI061850FF00005.JPEG","volume":"45","author":"RW Hepler","year":"2006","unstructured":"Hepler RW, Grimm KM, Nahas DD et al (2006) Solution state characterization of amyloid \u03b2-derived diffusible ligands. Biochemistry 45:15157\u201315167. https:\/\/doi.org\/10.1021\/BI061850F\/ASSET\/IMAGES\/LARGE\/BI061850FF00005.JPEG","journal-title":"Biochemistry"},{"key":"4543_CR161","doi-asserted-by":"publisher","first-page":"230","DOI":"10.1016\/J.NEUROPHARM.2010.07.012","volume":"59","author":"GA Krafft","year":"2010","unstructured":"Krafft GA, Klein WL (2010) ADDLs and the signaling web that leads to Alzheimer\u2019s disease. Neuropharmacology 59:230\u2013242. https:\/\/doi.org\/10.1016\/J.NEUROPHARM.2010.07.012","journal-title":"Neuropharmacology"},{"key":"4543_CR162","doi-asserted-by":"publisher","first-page":"834","DOI":"10.1111\/J.1471-4159.2005.03407.X","volume":"95","author":"S Barghorn","year":"2005","unstructured":"Barghorn S, Nimmrich V, Striebinger A et al (2005) Globular amyloid \u03b2-peptide1\u221242 oligomer\u2212a homogenous and stable neuropathological protein in Alzheimer\u2019s disease. J Neurochem 95:834\u2013847. https:\/\/doi.org\/10.1111\/J.1471-4159.2005.03407.X","journal-title":"J Neurochem"},{"key":"4543_CR163","doi-asserted-by":"publisher","first-page":"212","DOI":"10.1016\/J.NBD.2008.01.010","volume":"30","author":"GP Gellermann","year":"2008","unstructured":"Gellermann GP, Byrnes H, Striebinger A et al (2008) Abeta-globulomers are formed independently of the fibril pathway. Neurobiol Dis 30:212\u2013220. https:\/\/doi.org\/10.1016\/J.NBD.2008.01.010","journal-title":"Neurobiol Dis"},{"key":"4543_CR164","doi-asserted-by":"publisher","first-page":"788","DOI":"10.1523\/JNEUROSCI.4771-07.2008","volume":"28","author":"V Nimmrich","year":"2008","unstructured":"Nimmrich V, Grimm C, Draguhn A et al (2008) Amyloid \u03b2 oligomers (A\u03b21\u201342 globulomer) suppress spontaneous synaptic activity by inhibition of P\/Q-type calcium currents. J Neurosci 28:788\u2013797. https:\/\/doi.org\/10.1523\/JNEUROSCI.4771-07.2008","journal-title":"J Neurosci"},{"key":"4543_CR165","doi-asserted-by":"publisher","first-page":"1870","DOI":"10.1021\/BI802046N\/SUPPL_FILE\/BI802046N_SI_001.PDF","volume":"48","author":"L Yu","year":"2009","unstructured":"Yu L, Edalji R, Harlan JE et al (2009) Structural characterization of a soluble amyloid \u03b2-peptide oligomer. Biochemistry 48:1870\u20131877. https:\/\/doi.org\/10.1021\/BI802046N\/SUPPL_FILE\/BI802046N_SI_001.PDF","journal-title":"Biochemistry"},{"key":"4543_CR166","doi-asserted-by":"publisher","first-page":"e49375","DOI":"10.1371\/JOURNAL.PONE.0049375","volume":"7","author":"SL Gallion","year":"2012","unstructured":"Gallion SL (2012) Modeling amyloid-beta as homogeneous dodecamers and in complex with cellular prion protein. PLoS ONE 7:e49375. https:\/\/doi.org\/10.1371\/JOURNAL.PONE.0049375","journal-title":"PLoS ONE"},{"key":"4543_CR167","doi-asserted-by":"publisher","first-page":"1760","DOI":"10.1016\/J.CELREP.2015.05.021","volume":"11","author":"P Liu","year":"2015","unstructured":"Liu P, Reed MN, Kotilinek LA et al (2015) Quaternary structure defines a large class of amyloid-\u03b2 oligomers neutralized by sequestration. Cell Rep 11:1760\u20131771. https:\/\/doi.org\/10.1016\/J.CELREP.2015.05.021","journal-title":"Cell Rep"},{"key":"4543_CR168","doi-asserted-by":"publisher","first-page":"326","DOI":"10.1038\/nchem.247","volume":"1","author":"SL Bernstein","year":"2009","unstructured":"Bernstein SL, Dupuis NF, Lazo ND et al (2009) Amyloid-\u03b2 protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer\u2019s disease. Nat Chem 1:326\u2013331. https:\/\/doi.org\/10.1038\/nchem.247","journal-title":"Nat Chem"},{"key":"4543_CR169","doi-asserted-by":"publisher","first-page":"eaal2021","DOI":"10.1126\/SCISIGNAL.AAL2021","volume":"10","author":"F Amar","year":"2017","unstructured":"Amar F, Sherman MA, Rush T et al (2017) The amyloid-\u03b2 oligomer A\u03b2*56 induces specific alterations in neuronal signaling that lead to Tau phosphorylation and aggregation. Sci Signal 10:eaal2021. https:\/\/doi.org\/10.1126\/SCISIGNAL.AAL2021","journal-title":"Sci Signal"},{"key":"4543_CR170","doi-asserted-by":"publisher","first-page":"6370","DOI":"10.1073\/PNAS.1237107100","volume":"100","author":"M Hoshi","year":"2003","unstructured":"Hoshi M, Sato M, Matsumoto S et al (2003) Spherical aggregates of \u03b2-amyloid (amylospheroid) show high neurotoxicity and activate Tau protein kinase I\/glycogen synthase kinase-3\u03b2. Proc Natl Acad Sci 100:6370\u20136375. https:\/\/doi.org\/10.1073\/PNAS.1237107100","journal-title":"Proc Natl Acad Sci"},{"key":"4543_CR171","doi-asserted-by":"publisher","first-page":"1157","DOI":"10.1038\/NSMB1345","volume":"14","author":"S Chimon","year":"2007","unstructured":"Chimon S, Shaibat MA, Jones CR et al (2007) Evidence of fibril-like \u03b2-sheet structures in a neurotoxic amyloid intermediate of Alzheimer\u2019s \u03b2-amyloid. Nat Struct Mol Biol 14:1157\u20131164. https:\/\/doi.org\/10.1038\/NSMB1345","journal-title":"Nat Struct Mol Biol"},{"key":"4543_CR172","doi-asserted-by":"publisher","first-page":"32895","DOI":"10.1074\/jbc.M109.000208","volume":"284","author":"A Noguchi","year":"2009","unstructured":"Noguchi A, Matsumura S, Dezawa M et al (2009) Isolation and characterization of patient-derived, toxic, high mass amyloid \u03b2-protein (A\u03b2) assembly from Alzheimer disease brains. J Biol Chem 284:32895\u201332905. https:\/\/doi.org\/10.1074\/jbc.M109.000208","journal-title":"J Biol Chem"},{"key":"4543_CR173","doi-asserted-by":"publisher","first-page":"6480","DOI":"10.1021\/JACS.5B03373\/SUPPL_FILE\/JA5B03373_SI_001.PDF","volume":"137","author":"S Parthasarathy","year":"2015","unstructured":"Parthasarathy S, Inoue M, Xiao Y et al (2015) Structural insight into an Alzheimer\u2019s brain-derived spherical assembly of amyloid \u03b2 by solid-state NMR. J Am Chem Soc 137:6480\u20136483. https:\/\/doi.org\/10.1021\/JACS.5B03373\/SUPPL_FILE\/JA5B03373_SI_001.PDF","journal-title":"J Am Chem Soc"},{"key":"4543_CR174","doi-asserted-by":"publisher","first-page":"E4465","DOI":"10.1073\/PNAS.1421182112\/-\/DCSUPPLEMENTAL","volume":"112","author":"T Ohnishi","year":"2015","unstructured":"Ohnishi T, Yanazawa M, Sasahara T et al (2015) Na, K-ATPase \u03b13 is a death target of Alzheimer patient amyloid-\u03b2 assembly. Proc Natl Acad Sci U S A 112:E4465\u2013E4474. https:\/\/doi.org\/10.1073\/PNAS.1421182112\/-\/DCSUPPLEMENTAL","journal-title":"Proc Natl Acad Sci U S A"},{"key":"4543_CR175","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41598-018-23122-x","volume":"8","author":"MC Lee","year":"2018","unstructured":"Lee MC, Yu WC, Shih YH et al (2018) Zinc ion rapidly induces toxic, off-pathway amyloid-\u03b2 oligomers distinct from amyloid-\u03b2 derived diffusible ligands in Alzheimer\u2019s disease. Sci Reports 8:1\u201316. https:\/\/doi.org\/10.1038\/s41598-018-23122-x","journal-title":"Sci Reports"},{"key":"4543_CR176","doi-asserted-by":"publisher","first-page":"452","DOI":"10.1016\/J.ISCI.2019.01.018","volume":"13","author":"H Komura","year":"2019","unstructured":"Komura H, Kakio S, Sasahara T et al (2019) Alzheimer A\u03b2 assemblies accumulate in excitatory neurons upon proteasome inhibition and kill nearby NAK\u03b13 neurons by secretion. iScience 13:452\u2013477. https:\/\/doi.org\/10.1016\/J.ISCI.2019.01.018","journal-title":"iScience"},{"key":"4543_CR177","doi-asserted-by":"publisher","first-page":"558","DOI":"10.1038\/nsmb.1437","volume":"15","author":"DE Ehrnhoefer","year":"2008","unstructured":"Ehrnhoefer DE, Bieschke J, Boeddrich A et al (2008) EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol 15:558\u2013566. https:\/\/doi.org\/10.1038\/nsmb.1437","journal-title":"Nat Struct Mol Biol"},{"key":"4543_CR178","doi-asserted-by":"publisher","first-page":"8134","DOI":"10.1038\/S41598-024-58773-6","volume":"14","author":"M Kuramochi","year":"2024","unstructured":"Kuramochi M, Nakamura M, Takahashi H et al (2024) Adenosine triphosphate induces amorphous aggregation of amyloid \u03b2 by increasing A\u03b2 dynamics. Sci Rep 14:8134. https:\/\/doi.org\/10.1038\/S41598-024-58773-6","journal-title":"Sci Rep"},{"key":"4543_CR179","doi-asserted-by":"publisher","first-page":"13816","DOI":"10.1021\/JP4079986\/ASSET\/IMAGES\/MEDIUM\/JP-2013-079986_0009.GIF","volume":"117","author":"E Bramanti","year":"2013","unstructured":"Bramanti E, Fulgentini L, Bizzarri R et al (2013) \u03b2-amyloid amorphous aggregates induced by the small natural molecule ferulic acid. J Phys Chem B 117:13816\u201313821. https:\/\/doi.org\/10.1021\/JP4079986\/ASSET\/IMAGES\/MEDIUM\/JP-2013-079986_0009.GIF","journal-title":"J Phys Chem B"},{"key":"4543_CR180","doi-asserted-by":"publisher","first-page":"1202","DOI":"10.1016\/J.BPJ.2011.06.062","volume":"101","author":"N Rezaei-Ghaleh","year":"2011","unstructured":"Rezaei-Ghaleh N, Giller K, Becker S, Zweckstetter M (2011) Effect of zinc binding on \u03b2-amyloid structure and dynamics: implications for A\u03b2 aggregation. Biophys J 101:1202. https:\/\/doi.org\/10.1016\/J.BPJ.2011.06.062","journal-title":"Biophys J"},{"key":"4543_CR181","doi-asserted-by":"publisher","first-page":"1197","DOI":"10.1007\/S00775-019-01727-5","volume":"24","author":"MGM Weibull","year":"2019","unstructured":"Weibull MGM, Simonsen S, Oksbjerg CR et al (2019) Effects of Cu(II) on the aggregation of amyloid-\u03b2. JBIC J Biol Inorg Chem 24:1197\u20131215. https:\/\/doi.org\/10.1007\/S00775-019-01727-5","journal-title":"JBIC J Biol Inorg Chem"},{"key":"4543_CR182","doi-asserted-by":"publisher","first-page":"10624","DOI":"10.1021\/BI2012383\/SUPPL_FILE\/BI2012383_SI_001.PDF","volume":"50","author":"G Grelle","year":"2011","unstructured":"Grelle G, Otto A, Lorenz M et al (2011) Black tea theaflavins inhibit formation of toxic amyloid-\u03b2 and \u03b1-synuclein fibrils. Biochemistry 50:10624\u201310636. https:\/\/doi.org\/10.1021\/BI2012383\/SUPPL_FILE\/BI2012383_SI_001.PDF","journal-title":"Biochemistry"},{"key":"4543_CR183","doi-asserted-by":"publisher","first-page":"12243","DOI":"10.1073\/PNAS.91.25.12243","volume":"91","author":"A Lorenzo","year":"1994","unstructured":"Lorenzo A, Yankner BA (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc Natl Acad Sci 91:12243\u201312247. https:\/\/doi.org\/10.1073\/PNAS.91.25.12243","journal-title":"Proc Natl Acad Sci"},{"key":"4543_CR184","doi-asserted-by":"publisher","first-page":"15595","DOI":"10.1073\/PNAS.1001740107\/SUPPL_FILE\/PNAS.201001740SI.PDF","volume":"107","author":"A Sandberg","year":"2010","unstructured":"Sandberg A, Luheshi LM, S\u00f6llvander S et al (2010) Stabilization of neurotoxic Alzheimer amyloid-\u03b2 oligomers by protein engineering. Proc Natl Acad Sci U S A 107:15595\u201315600. https:\/\/doi.org\/10.1073\/PNAS.1001740107\/SUPPL_FILE\/PNAS.201001740SI.PDF","journal-title":"Proc Natl Acad Sci U S A"},{"key":"4543_CR185","doi-asserted-by":"publisher","first-page":"2433","DOI":"10.1096\/FJ.01-0377COM","volume":"15","author":"H Lin","year":"2001","unstructured":"Lin H, Bhatia R, Lal R (2001) Amyloid \u03b2 protein forms ion channels: implications for Alzheimer\u2019s disease pathophysiology. FASEB J 15:2433\u20132444. https:\/\/doi.org\/10.1096\/FJ.01-0377COM","journal-title":"FASEB J"},{"key":"4543_CR186","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1038\/418291a","volume":"418","author":"HA Lashuel","year":"2002","unstructured":"Lashuel HA, Hartley D, Petre BM et al (2002) Amyloid pores from pathogenic mutations. Nat 418:291\u2013291. https:\/\/doi.org\/10.1038\/418291a","journal-title":"Nat"},{"key":"4543_CR187","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1016\/S0143-4160(03)00128-3","volume":"34","author":"MP Mattson","year":"2003","unstructured":"Mattson MP, Chan SL (2003) Neuronal and glial calcium signaling in Alzheimer\u2019s disease. Cell Calcium 34:385\u2013397. https:\/\/doi.org\/10.1016\/S0143-4160(03)00128-3","journal-title":"Cell Calcium"},{"key":"4543_CR188","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1016\/S0022-2836(03)00927-6","volume":"332","author":"HA Lashuel","year":"2003","unstructured":"Lashuel HA, Hartley DM, Petre BM et al (2003) Mixtures of wild-type and a pathogenic (E22G) form of A\u03b240 in vitro accumulate protofibrils, including amyloid pores. J Mol Biol 332:795\u2013808. https:\/\/doi.org\/10.1016\/S0022-2836(03)00927-6","journal-title":"J Mol Biol"},{"key":"4543_CR189","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1017\/S0033583506004422","volume":"39","author":"HA Lashuel","year":"2006","unstructured":"Lashuel HA, Lansbury PT (2006) Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q Rev Biophys 39:167\u2013201. https:\/\/doi.org\/10.1017\/S0033583506004422","journal-title":"Q Rev Biophys"},{"key":"4543_CR190","doi-asserted-by":"publisher","first-page":"4230","DOI":"10.1074\/jbc.M808591200","volume":"284","author":"R Kayed","year":"2009","unstructured":"Kayed R, Pensalfini A, Margol L et al (2009) Annular protofibrils area structurally and functionally distinct type of amyloid oligomer. J Biol Chem 284:4230\u20134237. https:\/\/doi.org\/10.1074\/jbc.M808591200","journal-title":"J Biol Chem"},{"key":"4543_CR191","doi-asserted-by":"publisher","first-page":"6538","DOI":"10.1073\/PNAS.0914251107","volume":"107","author":"H Jang","year":"2010","unstructured":"Jang H, Arce FT, Ramachandran S et al (2010) Truncated beta-amyloid peptide channels provide an alternative mechanism for Alzheimer\u2019s disease and down syndrome. Proc Natl Acad Sci U S A 107:6538\u20136543. https:\/\/doi.org\/10.1073\/PNAS.0914251107","journal-title":"Proc Natl Acad Sci U S A"},{"key":"4543_CR192","doi-asserted-by":"publisher","first-page":"3052","DOI":"10.1016\/J.FEBSLET.2011.08.027","volume":"585","author":"CA Lasagna-Reeves","year":"2011","unstructured":"Lasagna-Reeves CA, Kayed R (2011) Astrocytes contain amyloid-\u03b2 annular protofibrils in Alzheimer\u2019s disease brains. FEBS Lett 585:3052\u20133057. https:\/\/doi.org\/10.1016\/J.FEBSLET.2011.08.027","journal-title":"FEBS Lett"},{"key":"4543_CR193","doi-asserted-by":"publisher","first-page":"22364","DOI":"10.1074\/JBC.272.35.22364","volume":"272","author":"DM Walsh","year":"1997","unstructured":"Walsh DM, Lomakin A, Benedek GB et al (1997) Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J Biol Chem 272:22364\u201322372. https:\/\/doi.org\/10.1074\/JBC.272.35.22364","journal-title":"J Biol Chem"},{"key":"4543_CR194","doi-asserted-by":"publisher","first-page":"995","DOI":"10.1111\/J.1742-4658.2008.06836.X","volume":"276","author":"A Lord","year":"2009","unstructured":"Lord A, Englund H, S\u00f6derberg L et al (2009) Amyloid-beta protofibril levels correlate with spatial learning in Arctic Alzheimer\u2019s disease transgenic mice. FEBS J 276:995\u20131006. https:\/\/doi.org\/10.1111\/J.1742-4658.2008.06836.X","journal-title":"FEBS J"},{"key":"4543_CR195","doi-asserted-by":"publisher","DOI":"10.1371\/JOURNAL.PONE.0032014","volume":"7","author":"D Sehlin","year":"2012","unstructured":"Sehlin D, Englund H, Simu B et al (2012) Large aggregates are the major soluble A\u03b2 species in AD brain fractionated with density gradient ultracentrifugation. PLoS ONE 7:e32014. https:\/\/doi.org\/10.1371\/JOURNAL.PONE.0032014","journal-title":"PLoS ONE"},{"key":"4543_CR196","doi-asserted-by":"publisher","first-page":"1416","DOI":"10.1021\/ACSCHEMNEURO.8B00029","volume":"9","author":"LK Gouwens","year":"2018","unstructured":"Gouwens LK, Ismail MS, Rogers VA et al (2018) A\u03b242 protofibrils interact with and are trafficked through microglial-derived microvesicles. ACS Chem Neurosci 9:1416\u20131425. https:\/\/doi.org\/10.1021\/ACSCHEMNEURO.8B00029","journal-title":"ACS Chem Neurosci"},{"key":"4543_CR197","doi-asserted-by":"publisher","first-page":"720","DOI":"10.1038\/NATURE06616","volume":"451","author":"M Meyer-Luehmann","year":"2008","unstructured":"Meyer-Luehmann M, Spires-Jones TL, Prada C et al (2008) Rapid appearance and local toxicity of amyloid-beta plaques in a mouse model of Alzheimer\u2019s disease. Nature 451:720\u2013724. https:\/\/doi.org\/10.1038\/NATURE06616","journal-title":"Nature"},{"key":"4543_CR198","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1042\/BJ20090379","volume":"421","author":"E Cerf","year":"2009","unstructured":"Cerf E, Sarroukh R, Tamamizu-Kato S et al (2009) Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide. Biochem J 421:415\u2013423. https:\/\/doi.org\/10.1042\/BJ20090379","journal-title":"Biochem J"},{"key":"4543_CR199","doi-asserted-by":"publisher","unstructured":"Walker LC (2020) A\u03b2 plaques. Free Neuropathol 1:1\u201331. https:\/\/doi.org\/10.17879\/FREENEUROPATHOLOGY-2020-3025","DOI":"10.17879\/FREENEUROPATHOLOGY-2020-3025"},{"key":"4543_CR200","doi-asserted-by":"publisher","DOI":"10.1016\/J.BBAPAP.2019.07.010","volume":"1867","author":"L Lutter","year":"2019","unstructured":"Lutter L, Serpell CJ, Tuite MF, Xue WF (2019) The molecular lifecycle of amyloid \u2013 mechanism of assembly, mesoscopic organisation, polymorphism, suprastructures, and biological consequences. Biochim Biophys Acta - Proteins Proteomics 1867:140257. https:\/\/doi.org\/10.1016\/J.BBAPAP.2019.07.010","journal-title":"Biochim Biophys Acta - Proteins Proteomics"},{"key":"4543_CR201","doi-asserted-by":"publisher","first-page":"1195","DOI":"10.3390\/MOLECULES25051195","volume":"25","author":"ZL Almeida","year":"2020","unstructured":"Almeida ZL, Brito RMM (2020) Structure and aggregation mechanisms in amyloids. Molecules 25:1195. https:\/\/doi.org\/10.3390\/MOLECULES25051195","journal-title":"Molecules"},{"key":"4543_CR202","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1186\/1750-1326-2-18","volume":"2","author":"R Kayed","year":"2007","unstructured":"Kayed R, Head E, Sarsoza F et al (2007) Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener 2:18. https:\/\/doi.org\/10.1186\/1750-1326-2-18","journal-title":"Mol Neurodegener"},{"key":"4543_CR203","doi-asserted-by":"publisher","first-page":"6071","DOI":"10.1074\/JBC.M109.069542","volume":"285","author":"JW Wu","year":"2010","unstructured":"Wu JW, Breydo L, Isas JM et al (2010) Fibrillar oligomers nucleate the oligomerization of monomeric amyloid \u03b2 but do not seed fibril formation. J Biol Chem 285:6071. https:\/\/doi.org\/10.1074\/JBC.M109.069542","journal-title":"J Biol Chem"},{"key":"4543_CR204","doi-asserted-by":"publisher","first-page":"1691","DOI":"10.1056\/NEJMOA2100708","volume":"384","author":"MA Mintun","year":"2021","unstructured":"Mintun MA, Lo AC, Evans CD et al (2021) Donanemab in early Alzheimer\u2019s disease. N Engl J Med 384:1691\u20131704. https:\/\/doi.org\/10.1056\/NEJMOA2100708","journal-title":"N Engl J Med"},{"key":"4543_CR205","doi-asserted-by":"publisher","first-page":"755","DOI":"10.1016\/J.IJBIOMAC.2022.11.049","volume":"223","author":"N Admane","year":"2022","unstructured":"Admane N, Srivastava A, Jamal S et al (2022) Molecular insights into the critical role of gallate moiety of green tea catechins in modulating prion fibrillation, cellular internalization, and neuronal toxicity. Int J Biol Macromol 223:755\u2013765. https:\/\/doi.org\/10.1016\/J.IJBIOMAC.2022.11.049","journal-title":"Int J Biol Macromol"},{"key":"4543_CR206","doi-asserted-by":"publisher","first-page":"5481","DOI":"10.1038\/s41380-021-01249-0","volume":"26","author":"H Hampel","year":"2021","unstructured":"Hampel H, Hardy J, Blennow K et al (2021) The amyloid-\u03b2 pathway in Alzheimer\u2019s disease. Mol Psychiatry 26:5481\u20135503. https:\/\/doi.org\/10.1038\/s41380-021-01249-0","journal-title":"Mol Psychiatry"},{"key":"4543_CR207","doi-asserted-by":"publisher","first-page":"1594","DOI":"10.1002\/JCB.30141","volume":"122","author":"P Madhu","year":"2021","unstructured":"Madhu P, Mukhopadhyay S (2021) Distinct types of amyloid-\u03b2 oligomers displaying diverse neurotoxicity mechanisms in Alzheimer\u2019s disease. J Cell Biochem 122:1594\u20131608. https:\/\/doi.org\/10.1002\/JCB.30141","journal-title":"J Cell Biochem"},{"key":"4543_CR208","doi-asserted-by":"publisher","DOI":"10.1016\/J.NEUINT.2021.105208","volume":"151","author":"K Ono","year":"2021","unstructured":"Ono K, Watanabe-Nakayama T (2021) Aggregation and structure of amyloid \u03b2-protein. Neurochem Int 151:105208. https:\/\/doi.org\/10.1016\/J.NEUINT.2021.105208","journal-title":"Neurochem Int"},{"key":"4543_CR209","doi-asserted-by":"publisher","first-page":"4477","DOI":"10.3390\/IJMS21124477","volume":"21","author":"YR Huang","year":"2020","unstructured":"Huang YR, Liu RT (2020) The toxicity and polymorphism of \u03b2-amyloid oligomers. Int J Mol Sci 21:4477. https:\/\/doi.org\/10.3390\/IJMS21124477","journal-title":"Int J Mol Sci"},{"key":"4543_CR210","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/J.EJMECH.2016.02.065","volume":"114","author":"P Salahuddin","year":"2016","unstructured":"Salahuddin P, Fatima MT, Abdelhameed AS et al (2016) Structure of amyloid oligomers and their mechanisms of toxicities: targeting amyloid oligomers using novel therapeutic approaches. Eur J Med Chem 114:41\u201358. https:\/\/doi.org\/10.1016\/J.EJMECH.2016.02.065","journal-title":"Eur J Med Chem"},{"key":"4543_CR211","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1111\/J.1471-4159.2011.07478.X","volume":"120","author":"ME Larson","year":"2012","unstructured":"Larson ME, Lesn\u00e9 SE (2012) Soluble A\u03b2 oligomer production and toxicity. J Neurochem 120:125\u2013139. https:\/\/doi.org\/10.1111\/J.1471-4159.2011.07478.X","journal-title":"J Neurochem"},{"key":"4543_CR212","doi-asserted-by":"publisher","first-page":"338","DOI":"10.1016\/j.tibs.2011.02.002","volume":"36","author":"M F\u00e4ndrich","year":"2011","unstructured":"F\u00e4ndrich M, Schmidt M, Grigorieff N (2011) Recent progress in understanding Alzheimer\u2019s \u03b2-amyloid structures. Trends Biochem Sci 36:338\u2013345. https:\/\/doi.org\/10.1016\/j.tibs.2011.02.002","journal-title":"Trends Biochem Sci"},{"key":"4543_CR213","doi-asserted-by":"publisher","first-page":"1022","DOI":"10.1016\/J.IJBIOMAC.2019.05.109","volume":"134","author":"M Zaman","year":"2019","unstructured":"Zaman M, Khan AN, Wahiduzzaman et al (2019) Protein misfolding, aggregation and mechanism of amyloid cytotoxicity: an overview and therapeutic strategies to inhibit aggregation. Int J Biol Macromol 134:1022\u20131037. https:\/\/doi.org\/10.1016\/J.IJBIOMAC.2019.05.109","journal-title":"Int J Biol Macromol"},{"key":"4543_CR214","doi-asserted-by":"publisher","first-page":"13365","DOI":"10.1021\/BI0508284\/ASSET\/IMAGES\/LARGE\/BI0508284F00007.JPEG","volume":"44","author":"SK Maji","year":"2005","unstructured":"Maji SK, Amsden JJ, Rothschild KJ et al (2005) Conformational dynamics of amyloid \u03b2-protein assembly probed using intrinsic fluorescence. Biochemistry 44:13365\u201313376. https:\/\/doi.org\/10.1021\/BI0508284\/ASSET\/IMAGES\/LARGE\/BI0508284F00007.JPEG","journal-title":"Biochemistry"},{"key":"4543_CR215","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1111\/J.1471-4159.2005.03188.X","volume":"94","author":"M Lotz","year":"2005","unstructured":"Lotz M, Ebert S, Esselmann H et al (2005) Amyloid beta peptide 1\u201340 enhances the action of Toll-like receptor-2 and -4 agonists but antagonizes Toll-like receptor-9-induced inflammation in primary mouse microglial cell cultures. J Neurochem 94:289\u2013298. https:\/\/doi.org\/10.1111\/J.1471-4159.2005.03188.X","journal-title":"J Neurochem"},{"key":"4543_CR216","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41598-018-19961-3","volume":"8","author":"M Novo","year":"2018","unstructured":"Novo M, Freire S, Al-Soufi W (2018) Critical aggregation concentration for the formation of early Amyloid-\u03b2 (1\u201342) oligomers. Sci Reports 8:1\u20138. https:\/\/doi.org\/10.1038\/s41598-018-19961-3","journal-title":"Sci Reports"},{"key":"4543_CR217","doi-asserted-by":"publisher","first-page":"1216","DOI":"10.1016\/S0006-3495(94)80591-0","volume":"67","author":"SW Snyder","year":"1994","unstructured":"Snyder SW, Ladror US, Wade WS et al (1994) Amyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths. Biophys J 67:1216\u20131228. https:\/\/doi.org\/10.1016\/S0006-3495(94)80591-0","journal-title":"Biophys J"},{"key":"4543_CR218","doi-asserted-by":"publisher","first-page":"23518","DOI":"10.1074\/jbc.M113.470450","volume":"288","author":"A Abelein","year":"2013","unstructured":"Abelein A, Kaspersen JD, Nielsen SB et al (2013) Formation of dynamic soluble surfactant-induced amyloid \u03b2 peptide aggregation intermediates. J Biol Chem 288:23518\u201323528. https:\/\/doi.org\/10.1074\/jbc.M113.470450","journal-title":"J Biol Chem"},{"key":"4543_CR219","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1002\/PSC.2535","volume":"19","author":"JA Loureiro","year":"2013","unstructured":"Loureiro JA, Rocha S, Pereira MDC (2013) Charged surfactants induce a non-fibrillar aggregation pathway of amyloid-beta peptide. J Pept Sci 19:581\u2013587. https:\/\/doi.org\/10.1002\/PSC.2535","journal-title":"J Pept Sci"},{"key":"4543_CR220","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1016\/J.BPC.2017.05.004","volume":"228","author":"A Campos-Ram\u00edrez","year":"2017","unstructured":"Campos-Ram\u00edrez A, M\u00e1rquez M, Quintanar L, Rojas-Ochoa LF (2017) Effect of ionic strength on the aggregation kinetics of the amidated amyloid beta peptide A\u03b2 (1\u201340) in aqueous solutions. Biophys Chem 228:98\u2013107. https:\/\/doi.org\/10.1016\/J.BPC.2017.05.004","journal-title":"Biophys Chem"},{"key":"4543_CR221","doi-asserted-by":"publisher","first-page":"1321","DOI":"10.1016\/J.JMB.2007.08.068","volume":"373","author":"K Klement","year":"2007","unstructured":"Klement K, Wieligmann K, Meinhardt J et al (2007) Effect of different salt ions on the propensity of aggregation and on the structure of alzheimer\u2019s A\u03b2(1\u201340) amyloid fibrils. J Mol Biol 373:1321\u20131333. https:\/\/doi.org\/10.1016\/J.JMB.2007.08.068","journal-title":"J Mol Biol"},{"key":"4543_CR222","doi-asserted-by":"publisher","first-page":"12711","DOI":"10.1021\/LA3021436\/SUPPL_FILE\/LA3021436_SI_001.PDF","volume":"28","author":"D Jiang","year":"2012","unstructured":"Jiang D, Rauda I, Han S et al (2012) Aggregation pathways of the amyloid \u03b2(1 42) peptide depend on its colloidal stability and ordered \u03b2-sheet stacking. Langmuir 28:12711\u201312721. https:\/\/doi.org\/10.1021\/LA3021436\/SUPPL_FILE\/LA3021436_SI_001.PDF","journal-title":"Langmuir"},{"key":"4543_CR223","doi-asserted-by":"publisher","first-page":"1190","DOI":"10.1016\/S0006-3495(91)82154-3","volume":"60","author":"PE Fraser","year":"1991","unstructured":"Fraser PE, Nguyen JT, Surewicz WK, Kirschner DA (1991) pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys J 60:1190. https:\/\/doi.org\/10.1016\/S0006-3495(91)82154-3","journal-title":"Biophys J"},{"key":"4543_CR224","doi-asserted-by":"publisher","first-page":"870","DOI":"10.1006\/JMBI.1996.0133","volume":"256","author":"SJ Wood","year":"1996","unstructured":"Wood SJ, Maleeff B, Hart T, Wetzel R (1996) Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer\u2019s amyloid peptide A \u03b2. J Mol Biol 256:870\u2013877. https:\/\/doi.org\/10.1006\/JMBI.1996.0133","journal-title":"J Mol Biol"},{"key":"4543_CR225","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1146\/ANNUREV.BIOCHEM.66.1.385","volume":"66","author":"JD Harper","year":"1997","unstructured":"Harper JD, Lansbury PT (1997) Models of amyloid seeding in Alzheimer\u2019s disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 66:385\u2013407. https:\/\/doi.org\/10.1146\/ANNUREV.BIOCHEM.66.1.385","journal-title":"Annu Rev Biochem"},{"key":"4543_CR226","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/0304-3940(95)12089-M","volume":"200","author":"C Soto","year":"1995","unstructured":"Soto C, Casta\u00f1o EM, Asok Kumar R et al (1995) Fibrillogenesis of synthetic amyloid-\u03b2 peptides is dependent on their initial secondary structure. Neurosci Lett 200:105\u2013108. https:\/\/doi.org\/10.1016\/0304-3940(95)12089-M","journal-title":"Neurosci Lett"},{"key":"4543_CR227","doi-asserted-by":"publisher","first-page":"3938","DOI":"10.1111\/J.1742-4658.2005.04812.X","volume":"272","author":"J Danielsson","year":"2005","unstructured":"Danielsson J, Jarvet J, Damberg P, Gr\u00e4slund A (2005) The Alzheimer \u03b2-peptide shows temperature-dependent transitions between left-handed 31-helix, \u03b2-strand and random coil secondary structures. FEBS J 272:3938\u20133949. https:\/\/doi.org\/10.1111\/J.1742-4658.2005.04812.X","journal-title":"FEBS J"},{"key":"4543_CR228","doi-asserted-by":"publisher","first-page":"12277","DOI":"10.1073\/PNAS.95.21.12277","volume":"95","author":"Y Kusumoto","year":"1998","unstructured":"Kusumoto Y, Lomakin A, Teplow DB, Benedek GB (1998) Temperature dependence of amyloid beta-protein fibrillization. Proc Natl Acad Sci U S A 95:12277\u201312282. https:\/\/doi.org\/10.1073\/PNAS.95.21.12277","journal-title":"Proc Natl Acad Sci U S A"},{"key":"4543_CR229","doi-asserted-by":"publisher","first-page":"386","DOI":"10.1002\/PSC.2513","volume":"19","author":"A Tiiman","year":"2013","unstructured":"Tiiman A, Noorm\u00e4gi A, Friedemann M et al (2013) Effect of agitation on the peptide fibrillization: Alzheimer\u2019s amyloid-\u03b2 peptide 1\u201342 but not amylin and insulin fibrils can grow under quiescent conditions. J Pept Sci 19:386\u2013391. https:\/\/doi.org\/10.1002\/PSC.2513","journal-title":"J Pept Sci"},{"key":"4543_CR230","doi-asserted-by":"publisher","first-page":"e59005","DOI":"10.1371\/JOURNAL.PONE.0059005","volume":"8","author":"F Hane","year":"2013","unstructured":"Hane F, Tran G, Attwood SJ, Leonenko Z (2013) Cu2+ affects amyloid-\u03b2 (1\u201342) aggregation by increasing peptide-peptide binding forces. PLoS ONE 8:e59005. https:\/\/doi.org\/10.1371\/JOURNAL.PONE.0059005","journal-title":"PLoS ONE"},{"key":"4543_CR231","doi-asserted-by":"publisher","first-page":"3909","DOI":"10.1021\/ACS.JPCB.6B12187\/ASSET\/IMAGES\/LARGE\/JP-2016-12187U_0007.JPEG","volume":"121","author":"J Guo","year":"2017","unstructured":"Guo J, Yu L, Sun Y, Dong X (2017) Kinetic insights into Zn2+-induced amyloid \u03b2-protein aggregation revealed by stopped-flow fluorescence spectroscopy. J Phys Chem B 121:3909\u20133917. https:\/\/doi.org\/10.1021\/ACS.JPCB.6B12187\/ASSET\/IMAGES\/LARGE\/JP-2016-12187U_0007.JPEG","journal-title":"J Phys Chem B"},{"key":"4543_CR232","doi-asserted-by":"publisher","first-page":"14411","DOI":"10.1523\/JNEUROSCI.3537-10.2010","volume":"30","author":"B O\u2019Nuallain","year":"2010","unstructured":"O\u2019Nuallain B, Freir DB, Nicoll AJ et al (2010) Amyloid \u03b2-protein dimers rapidly form stable synaptotoxic protofibrils. J Neurosci 30:14411\u201314419. https:\/\/doi.org\/10.1523\/JNEUROSCI.3537-10.2010","journal-title":"J Neurosci"},{"key":"4543_CR233","doi-asserted-by":"publisher","first-page":"e939","DOI":"10.1038\/cddis.2013.492","volume":"4","author":"VA Mitkevich","year":"2013","unstructured":"Mitkevich VA, Petrushanko IY, Yegorov YE et al (2013) Isomerization of Asp7 leads to increased toxic effect of amyloid-\u03b242 on human neuronal cells. Cell Death Dis 4:e939\u2013e939. https:\/\/doi.org\/10.1038\/cddis.2013.492","journal-title":"Cell Death Dis"},{"key":"4543_CR234","doi-asserted-by":"publisher","first-page":"1182","DOI":"10.1016\/J.ELECTACTA.2017.11.173","volume":"258","author":"EV Suprun","year":"2017","unstructured":"Suprun EV, Radko SP, Farafonova TE et al (2017) Electrochemical detection of protein post-translational modifications: phosphorylation and nitration of amyloid-beta (1\u201316). Electrochim Acta 258:1182\u20131190. https:\/\/doi.org\/10.1016\/J.ELECTACTA.2017.11.173","journal-title":"Electrochim Acta"},{"key":"4543_CR235","doi-asserted-by":"publisher","first-page":"1545","DOI":"10.1039\/C7MB00249A","volume":"13","author":"E Jamasbi","year":"2017","unstructured":"Jamasbi E, Separovic F, Hossain MA, Ciccotosto GD (2017) Phosphorylation of a full length amyloid-\u03b2 peptide modulates its amyloid aggregation, cell binding and neurotoxic properties. Mol Biosyst 13:1545\u20131551. https:\/\/doi.org\/10.1039\/C7MB00249A","journal-title":"Mol Biosyst"},{"key":"4543_CR236","doi-asserted-by":"publisher","first-page":"10205","DOI":"10.1016\/S0021-9258(17)34045-0","volume":"269","author":"T Tomiyama","year":"1994","unstructured":"Tomiyama T, Asano S, Furiya Y et al (1994) Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues. J Biol Chem 269:10205\u201310208. https:\/\/doi.org\/10.1016\/S0021-9258(17)34045-0","journal-title":"J Biol Chem"},{"key":"4543_CR237","doi-asserted-by":"publisher","first-page":"31446","DOI":"10.1039\/C6CP05041G","volume":"18","author":"AK Jana","year":"2016","unstructured":"Jana AK, Batkulwar KB, Kulkarni MJ, Sengupta N (2016) Glycation induces conformational changes in the amyloid-\u03b2 peptide and enhances its aggregation propensity: molecular insights. Phys Chem Chem Phys 18:31446\u201331458. https:\/\/doi.org\/10.1039\/C6CP05041G","journal-title":"Phys Chem Chem Phys"},{"key":"4543_CR238","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1016\/J.BBREP.2015.07.017","volume":"3","author":"M Friedemann","year":"2015","unstructured":"Friedemann M, Helk E, Tiiman A et al (2015) Effect of methionine-35 oxidation on the aggregation of amyloid-\u03b2 peptide. Biochem Biophys Reports 3:94\u201399. https:\/\/doi.org\/10.1016\/J.BBREP.2015.07.017","journal-title":"Biochem Biophys Reports"},{"key":"4543_CR239","doi-asserted-by":"publisher","first-page":"142","DOI":"10.1002\/JMS.732","volume":"40","author":"W Hosia","year":"2005","unstructured":"Hosia W, Griffiths WJ, Johansson J (2005) Hydrolysis of the amyloid \u03b2-peptide (A\u03b2) 1\u201340 between Asp23\u2013Val24 produces non-aggregating fragments. An electrospray mass spectrometric study. J Mass Spectrom 40:142\u2013145. https:\/\/doi.org\/10.1002\/JMS.732","journal-title":"J Mass Spectrom"},{"key":"4543_CR240","doi-asserted-by":"publisher","first-page":"110029","DOI":"10.1016\/J.CBI.2022.110029","volume":"363","author":"S Onder","year":"2022","unstructured":"Onder S, Biberoglu K, Tacal O, Schopfer LM (2022) Chlorpyrifos oxon crosslinking of amyloid beta 42 peptides is a new route for generation of self-aggregating amyloidogenic oligomers that promote Alzheimer\u2019s disease. Chem Biol Interact 363:110029. https:\/\/doi.org\/10.1016\/J.CBI.2022.110029","journal-title":"Chem Biol Interact"},{"key":"4543_CR241","doi-asserted-by":"publisher","first-page":"883","DOI":"10.1111\/J.1471-4159.2012.07847.X","volume":"122","author":"K Ono","year":"2012","unstructured":"Ono K, Takahashi R, Ikeda T, Yamada M (2012) Cross-seeding effects of amyloid \u03b2-protein and \u03b1-synuclein. J Neurochem 122:883\u2013890. https:\/\/doi.org\/10.1111\/J.1471-4159.2012.07847.X","journal-title":"J Neurochem"},{"key":"4543_CR242","doi-asserted-by":"publisher","first-page":"967","DOI":"10.1021\/ACSCHEMNEURO.7B00396\/ASSET\/IMAGES\/MEDIUM\/CN-2017-00396A_M002.GIF","volume":"9","author":"X Ge","year":"2018","unstructured":"Ge X, Yang Y, Sun Y et al (2018) Islet amyloid polypeptide promotes amyloid-beta aggregation by binding-induced helix-unfolding of the amyloidogenic core. ACS Chem Neurosci 9:967\u2013975. https:\/\/doi.org\/10.1021\/ACSCHEMNEURO.7B00396\/ASSET\/IMAGES\/MEDIUM\/CN-2017-00396A_M002.GIF","journal-title":"ACS Chem Neurosci"},{"key":"4543_CR243","doi-asserted-by":"publisher","first-page":"1398","DOI":"10.1111\/J.1471-4159.2004.02828.X","volume":"91","author":"J Fung","year":"2004","unstructured":"Fung J, Frost D, Chakrabartty A, McLaurin JA (2004) Interaction of human and mouse A\u03b2 peptides. J Neurochem 91:1398\u20131403. https:\/\/doi.org\/10.1111\/J.1471-4159.2004.02828.X","journal-title":"J Neurochem"},{"key":"4543_CR244","doi-asserted-by":"publisher","first-page":"5650","DOI":"10.1074\/jbc.M111.264473","volume":"287","author":"K Pauwels","year":"2012","unstructured":"Pauwels K, Williams TL, Morris KL et al (2012) Structural basis for increased toxicity of pathological A\u03b242:A\u03b240 ratios in Alzheimer disease. J Biol Chem 287:5650\u20135660. https:\/\/doi.org\/10.1074\/jbc.M111.264473","journal-title":"J Biol Chem"},{"key":"4543_CR245","doi-asserted-by":"publisher","first-page":"29268","DOI":"10.1074\/jbc.M600690200","volume":"281","author":"KJ Kinghorn","year":"2006","unstructured":"Kinghorn KJ, Crowther DC, Sharp LK et al (2006) Neuroserpin binds A\u03b2 and is a neuroprotective component of amyloid plaques in Alzheimer disease. J Biol Chem 281:29268\u201329277. https:\/\/doi.org\/10.1074\/jbc.M600690200","journal-title":"J Biol Chem"},{"key":"4543_CR246","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1038\/nature11060","volume":"485","author":"JM Nussbaum","year":"2012","unstructured":"Nussbaum JM, Schilling S, Cynis H et al (2012) Prion-like behaviour and Tau-dependent cytotoxicity of pyroglutamylated amyloid-\u03b2. Nat 485:651\u2013655. https:\/\/doi.org\/10.1038\/nature11060","journal-title":"Nat"},{"key":"4543_CR247","doi-asserted-by":"publisher","first-page":"2781","DOI":"10.1021\/JACS.7B13660","volume":"140","author":"BK Yoo","year":"2018","unstructured":"Yoo BK, Xiao Y, McElheny D, Ishii Y (2018) E22G Pathogenic mutation of \u03b2-amyloid (A\u03b2) enhances misfolding of A\u03b240 by unexpected prion-like cross talk between A\u03b242 and A\u03b240. J Am Chem Soc 140:2781\u20132784. https:\/\/doi.org\/10.1021\/JACS.7B13660","journal-title":"J Am Chem Soc"},{"key":"4543_CR248","doi-asserted-by":"publisher","first-page":"1953","DOI":"10.1073\/PNAS.0509386103\/SUPPL_FILE\/09386TABLE4.JPG","volume":"103","author":"JP Guo","year":"2006","unstructured":"Guo JP, Arai T, Miklossy J, McGeer PL (2006) A\u03b2 and Tau form soluble complexes that may promote self aggregation of both into the insoluble forms in Alzheimer\u2019s diseases. Proc Natl Acad Sci U S A 103:1953\u20131958. https:\/\/doi.org\/10.1073\/PNAS.0509386103\/SUPPL_FILE\/09386TABLE4.JPG","journal-title":"Proc Natl Acad Sci U S A"},{"key":"4543_CR249","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1016\/J.BRAINRESREV.2005.04.001","volume":"50","author":"EA Kiyatkin","year":"2005","unstructured":"Kiyatkin EA (2005) Brain hyperthermia as physiological and pathological phenomena. Brain Res Rev 50:27\u201356. https:\/\/doi.org\/10.1016\/J.BRAINRESREV.2005.04.001","journal-title":"Brain Res Rev"},{"key":"4543_CR250","doi-asserted-by":"publisher","first-page":"1183","DOI":"10.1152\/PHYSREV.00010.2003\/ASSET\/IMAGES\/LARGE\/9J0430270004.JPEG","volume":"83","author":"M Chesler","year":"2003","unstructured":"Chesler M (2003) Regulation and modulation of pH in the brain. Physiol Rev 83:1183\u20131221. https:\/\/doi.org\/10.1152\/PHYSREV.00010.2003\/ASSET\/IMAGES\/LARGE\/9J0430270004.JPEG","journal-title":"Physiol Rev"},{"key":"4543_CR251","doi-asserted-by":"publisher","DOI":"10.1016\/J.BIOPHA.2021.111623","volume":"139","author":"TT Nguyen","year":"2021","unstructured":"Nguyen TT, Nguyen TD, Nguyen TKO et al (2021) Advances in developing therapeutic strategies for Alzheimer\u2019s disease. Biomed Pharmacother 139:111623. https:\/\/doi.org\/10.1016\/J.BIOPHA.2021.111623","journal-title":"Biomed Pharmacother"},{"key":"4543_CR252","doi-asserted-by":"publisher","first-page":"744","DOI":"10.1177\/106002809402800612","volume":"28","author":"ML Crismon","year":"1994","unstructured":"Crismon ML (1994) Tacrine: first drug approved for Alzheimer\u2019s disease. Ann Pharmacother 28:744\u2013751. https:\/\/doi.org\/10.1177\/106002809402800612","journal-title":"Ann Pharmacother"},{"key":"4543_CR253","doi-asserted-by":"publisher","first-page":"1916","DOI":"10.1016\/J.BMCL.2013.02.017","volume":"23","author":"A Romero","year":"2013","unstructured":"Romero A, Cacabelos R, Oset-Gasque MJ et al (2013) Novel tacrine-related drugs as potential candidates for the treatment of Alzheimer\u2019s disease. Bioorg Med Chem Lett 23:1916\u20131922. https:\/\/doi.org\/10.1016\/J.BMCL.2013.02.017","journal-title":"Bioorg Med Chem Lett"},{"key":"4543_CR254","doi-asserted-by":"publisher","first-page":"521","DOI":"10.3233\/JAD-2011-110417","volume":"27","author":"S Kavanagh","year":"2011","unstructured":"Kavanagh S, Van Baelen B, Sch\u00e4uble B (2011) Long-term effects of galantamine on cognitive function in Alzheimer\u2019s disease: a large-scale international retrospective study. J Alzheimers Dis 27:521\u2013530. https:\/\/doi.org\/10.3233\/JAD-2011-110417","journal-title":"J Alzheimers Dis"},{"key":"4543_CR255","doi-asserted-by":"publisher","first-page":"769","DOI":"10.1002\/GPS.2788","volume":"27","author":"D Wilkinson","year":"2012","unstructured":"Wilkinson D (2012) A review of the effects of memantine on clinical progression in Alzheimer\u2019s disease. Int J Geriatr Psychiatry 27:769\u2013776. https:\/\/doi.org\/10.1002\/GPS.2788","journal-title":"Int J Geriatr Psychiatry"},{"key":"4543_CR256","doi-asserted-by":"publisher","first-page":"925702","DOI":"10.1155\/2013\/925702","volume":"2013","author":"I Molino","year":"2013","unstructured":"Molino I, Colucci L, Fasanaro AM et al (2013) Efficacy of memantine, donepezil, or their association in moderate-severe Alzheimer\u2019s disease: a review of clinical trials. Sci World J 2013:925702. https:\/\/doi.org\/10.1155\/2013\/925702","journal-title":"Sci World J"},{"key":"4543_CR257","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41598-018-24501-0","volume":"8","author":"JW Arndt","year":"2018","unstructured":"Arndt JW, Qian F, Smith BA et al (2018) Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-\u03b2. Sci Reports 8:1\u201316. https:\/\/doi.org\/10.1038\/s41598-018-24501-0","journal-title":"Sci Reports"},{"key":"4543_CR258","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/S13195-021-00813-8\/TABLES\/3","volume":"13","author":"CJ Swanson","year":"2021","unstructured":"Swanson CJ, Zhang Y, Dhadda S et al (2021) A randomized, double-blind, phase 2b proof-of-concept clinical trial in early Alzheimer\u2019s disease with lecanemab, an anti-A\u03b2 protofibril antibody. Alzheimer\u2019s Res Ther 13:1\u201314. https:\/\/doi.org\/10.1186\/S13195-021-00813-8\/TABLES\/3","journal-title":"Alzheimer\u2019s Res Ther"},{"key":"4543_CR259","doi-asserted-by":"publisher","first-page":"336","DOI":"10.1093\/AGEING\/AFL027","volume":"35","author":"N Tabet","year":"2006","unstructured":"Tabet N (2006) Acetylcholinesterase inhibitors for Alzheimer\u2019s disease: anti-inflammatories in acetylcholine clothing! Age Ageing 35:336\u2013338. https:\/\/doi.org\/10.1093\/AGEING\/AFL027","journal-title":"Age Ageing"},{"key":"4543_CR260","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1016\/0166-2236(87)90025-7","volume":"10","author":"WF Maragos","year":"1987","unstructured":"Maragos WF, Greenamyre JT, Penney JB, Young AB (1987) Glutamate dysfunction in Alzheimer\u2019s disease: an hypothesis. Trends Neurosci 10:65\u201368. https:\/\/doi.org\/10.1016\/0166-2236(87)90025-7","journal-title":"Trends Neurosci"},{"key":"4543_CR261","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1007\/BF03033787\/METRICS","volume":"2","author":"W Danysz","year":"2000","unstructured":"Danysz W, Parsons CG, M\u00d6bius H-J\u00f6, et al (2000) Neuroprotective and symptomatological action of memantine relevant for alzheimer\u2019s disease \u2014 a unified glutamatergic hypothesis on the mechanism of action. Neurotox Res 2:85\u201397. https:\/\/doi.org\/10.1007\/BF03033787\/METRICS","journal-title":"Neurotox Res"},{"key":"4543_CR262","doi-asserted-by":"publisher","first-page":"613","DOI":"10.1056\/NEJM199403033300907","volume":"330","author":"FH Epstein","year":"1994","unstructured":"Epstein FH, Lipton SA, Rosenberg PA (1994) Excitatory amino acids as a final common pathway for neurologic disorders. N Engl J Med 330:613\u2013622. https:\/\/doi.org\/10.1056\/NEJM199403033300907","journal-title":"N Engl J Med"},{"key":"4543_CR263","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/S13195-021-00813-8","volume":"13","author":"CJ Swanson","year":"2021","unstructured":"Swanson CJ, Zhang Y, Dhadda S et al (2021) A randomized, double-blind, phase 2b proof-of-concept clinical trial in early Alzheimer\u2019s disease with lecanemab, an anti-A\u03b2 protofibril antibody. Alzheimers Res Ther 13:1. https:\/\/doi.org\/10.1186\/S13195-021-00813-8","journal-title":"Alzheimers Res Ther"},{"key":"4543_CR264","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/S40001-023-01512-W\/FIGURES\/5","volume":"28","author":"W Wu","year":"2023","unstructured":"Wu W, Ji Y, Wang Z et al (2023) The FDA-approved anti-amyloid-\u03b2 monoclonal antibodies for the treatment of Alzheimer\u2019s disease: a systematic review and meta-analysis of randomized controlled trials. Eur J Med Res 28:1\u201313. https:\/\/doi.org\/10.1186\/S40001-023-01512-W\/FIGURES\/5","journal-title":"Eur J Med Res"},{"key":"4543_CR265","doi-asserted-by":"publisher","first-page":"943","DOI":"10.17219\/ACEM\/171379","volume":"32","author":"M Kurkinen","year":"2023","unstructured":"Kurkinen M (2023) Lecanemab (Leqembi) is not the right drug for patients with Alzheimer\u2019s disease. Adv Clin Exp Med 32:943\u2013947. https:\/\/doi.org\/10.17219\/ACEM\/171379","journal-title":"Adv Clin Exp Med"},{"key":"4543_CR266","first-page":"110","volume":"7","author":"YE Wang","year":"1986","unstructured":"Wang YE, Yue DX, Tang XC (1986) Anti-cholinesterase activity of huperzine A. Zhongguo Yao Li Xue Bao 7:110\u2013113","journal-title":"Zhongguo Yao Li Xue Bao"},{"key":"4543_CR267","doi-asserted-by":"publisher","DOI":"10.1002\/14651858.CD005592.PUB2\/INFORMATION\/EN","author":"J Li","year":"2008","unstructured":"Li J, Wu HM, Zhou RL et al (2008) Huperzine a for Alzheimer\u2019s disease. Cochrane Database Syst Rev. https:\/\/doi.org\/10.1002\/14651858.CD005592.PUB2\/INFORMATION\/EN","journal-title":"Cochrane Database Syst Rev"},{"key":"4543_CR268","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1007\/S40265-020-01268-1\/TABLES\/3","volume":"80","author":"YY Syed","year":"2020","unstructured":"Syed YY (2020) Sodium oligomannate: first approval. Drugs 80:441\u2013444. https:\/\/doi.org\/10.1007\/S40265-020-01268-1\/TABLES\/3","journal-title":"Drugs"},{"key":"4543_CR269","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1038\/s41422-019-0216-x","volume":"29","author":"X Wang","year":"2019","unstructured":"Wang X, Sun G, Feng T et al (2019) Sodium oligomannate therapeutically remodels gut microbiota and suppresses gut bacterial amino acids-shaped neuroinflammation to inhibit Alzheimer\u2019s disease progression. Cell Res 29:787\u2013803. https:\/\/doi.org\/10.1038\/s41422-019-0216-x","journal-title":"Cell Res"},{"key":"4543_CR270","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1179\/174313206X152483","volume":"29","author":"S Wang","year":"2007","unstructured":"Wang S, Li J, Xia W, Geng M (2007) A marine-derived acidic oligosaccharide sugar chain specifically inhibits neuronal cell injury mediated by \u03b2-amyloid-induced astrocyte activation in vitro. Neurol Res 29:96\u2013102. https:\/\/doi.org\/10.1179\/174313206X152483","journal-title":"Neurol Res"},{"key":"4543_CR271","doi-asserted-by":"publisher","first-page":"394","DOI":"10.1007\/S00343-008-0394-8\/METRICS","volume":"26","author":"M Liu","year":"2008","unstructured":"Liu M, Nie Q, Xin X, Geng M (2008) Identification of AOSC-binding proteins in neurons. Chinese J Oceanol Limnol 26:394\u2013399. https:\/\/doi.org\/10.1007\/S00343-008-0394-8\/METRICS","journal-title":"Chinese J Oceanol Limnol"},{"key":"4543_CR272","doi-asserted-by":"publisher","first-page":"e12465","DOI":"10.1002\/TRC2.12465","volume":"10","author":"J Cummings","year":"2024","unstructured":"Cummings J, Zhou Y, Lee G et al (2024) Alzheimer\u2019s disease drug development pipeline: 2024. Alzheimer\u2019s Dement Transl Res Clin Interv 10:e12465. https:\/\/doi.org\/10.1002\/TRC2.12465","journal-title":"Alzheimer\u2019s Dement Transl Res Clin Interv"},{"key":"4543_CR273","doi-asserted-by":"publisher","first-page":"e12385","DOI":"10.1002\/TRC2.12385","volume":"9","author":"J Cummings","year":"2023","unstructured":"Cummings J, Zhou Y, Lee G et al (2023) Alzheimer\u2019s disease drug development pipeline: 2023. Alzheimer\u2019s Dement Transl Res Clin Interv 9:e12385. https:\/\/doi.org\/10.1002\/TRC2.12385","journal-title":"Alzheimer\u2019s Dement Transl Res Clin Interv"},{"key":"4543_CR274","doi-asserted-by":"publisher","first-page":"1745","DOI":"10.14336\/AD.2022.0412","volume":"13","author":"T Wu","year":"2022","unstructured":"Wu T, Lin D, Cheng Y et al (2022) Amyloid cascade hypothesis for the treatment of Alzheimer\u2019s disease: progress and challenges. Aging Dis 13:1745. https:\/\/doi.org\/10.14336\/AD.2022.0412","journal-title":"Aging Dis"},{"key":"4543_CR275","doi-asserted-by":"publisher","first-page":"101496","DOI":"10.1016\/J.ARR.2021.101496","volume":"72","author":"D Jeremic","year":"2021","unstructured":"Jeremic D, Jim\u00e9nez-D\u00edaz L, Navarro-L\u00f3pez JD (2021) Past, present and future of therapeutic strategies against amyloid-\u03b2 peptides in Alzheimer\u2019s disease: a systematic review. Ageing Res Rev 72:101496. https:\/\/doi.org\/10.1016\/J.ARR.2021.101496","journal-title":"Ageing Res Rev"},{"issue":"10","key":"4543_CR276","doi-asserted-by":"publisher","first-page":"3276","DOI":"10.3390\/BIOMEDICINES10123276","volume":"3276","author":"ZL Almeida","year":"2022","unstructured":"Almeida ZL, Brito RMM (2022) Amyloid disassembly: what can we learn from chaperones? Biomed 2022, Vol 10. Page 3276(10):3276. https:\/\/doi.org\/10.3390\/BIOMEDICINES10123276","journal-title":"Page"},{"key":"4543_CR277","doi-asserted-by":"publisher","first-page":"192017","DOI":"10.3389\/FNINS.2016.00177\/BIBTEX","volume":"10","author":"RE Hughes","year":"2016","unstructured":"Hughes RE, Nikolic K, Ramsay RR (2016) One for all? Hitting multiple Alzheimer\u2019s disease targets with one drug. Front Neurosci 10:192017. https:\/\/doi.org\/10.3389\/FNINS.2016.00177\/BIBTEX","journal-title":"Front Neurosci"},{"key":"4543_CR278","doi-asserted-by":"publisher","first-page":"3512","DOI":"10.1007\/S12035-022-02779-6\/TABLES\/1","volume":"59","author":"A Jana","year":"2022","unstructured":"Jana A, Bhattacharjee A, Das SS et al (2022) Molecular insights into therapeutic potentials of hybrid compounds targeting Alzheimer\u2019s disease. Mol Neurobiol 59:3512\u20133528. https:\/\/doi.org\/10.1007\/S12035-022-02779-6\/TABLES\/1","journal-title":"Mol Neurobiol"},{"key":"4543_CR279","doi-asserted-by":"publisher","first-page":"1243","DOI":"10.3390\/MOLECULES21091243","volume":"21","author":"G Mazzanti","year":"2016","unstructured":"Mazzanti G, Di Giacomo S (2016) Curcumin and resveratrol in the management of cognitive disorders: what is the clinical evidence? Mol 21:1243. https:\/\/doi.org\/10.3390\/MOLECULES21091243","journal-title":"Mol"},{"key":"4543_CR280","doi-asserted-by":"publisher","first-page":"24228","DOI":"10.1074\/JBC.M110.133108","volume":"285","author":"A Reza","year":"2010","unstructured":"Reza A, Ladiwala A, Lin JC et al (2010) Resveratrol selectively remodels soluble oligomers and fibrils of amyloid A\u03b2 into off-pathway conformers *. J Biol Chem 285:24228\u201324237. https:\/\/doi.org\/10.1074\/JBC.M110.133108","journal-title":"J Biol Chem"},{"key":"4543_CR281","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/J.MCN.2017.12.003","volume":"88","author":"E Vion","year":"2018","unstructured":"Vion E, Page G, Bourdeaud E et al (2018) Trans \u03b5-viniferin is an amyloid-\u03b2 disaggregating and anti-inflammatory drug in a mouse primary cellular model of Alzheimer\u2019s disease. Mol Cell Neurosci 88:1\u20136. https:\/\/doi.org\/10.1016\/J.MCN.2017.12.003","journal-title":"Mol Cell Neurosci"},{"key":"4543_CR282","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1016\/J.DYEPIG.2017.07.071","volume":"147","author":"P Dao","year":"2017","unstructured":"Dao P, Ye F, Du ZY et al (2017) Design and synthesis of new theranostic agents for near-infrared imaging of \u03b2-amyloid plaques and inhibition of \u03b2-amyloid aggregation in Alzheimer\u2019s disease. Dye Pigment 147:130\u2013140. https:\/\/doi.org\/10.1016\/J.DYEPIG.2017.07.071","journal-title":"Dye Pigment"},{"key":"4543_CR283","doi-asserted-by":"publisher","first-page":"953","DOI":"10.1111\/CNS.12472","volume":"21","author":"SQ Hu","year":"2015","unstructured":"Hu SQ, Wang R, Cui W et al (2015) Dimeric bis (heptyl)-cognitin blocks Alzheimer\u2019s \u03b2-amyloid neurotoxicity via the inhibition of A\u03b2 fibrils formation and disaggregation of preformed fibrils. CNS Neurosci Ther 21:953\u2013961. https:\/\/doi.org\/10.1111\/CNS.12472","journal-title":"CNS Neurosci Ther"},{"key":"4543_CR284","doi-asserted-by":"publisher","first-page":"5892","DOI":"10.1074\/jbc.M404751200","volume":"280","author":"F Yang","year":"2005","unstructured":"Yang F, Lim GP, Begum AN et al (2005) Curcumin inhibits formation of amyloid \u03b2 oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem 280:5892\u20135901. https:\/\/doi.org\/10.1074\/jbc.M404751200","journal-title":"J Biol Chem"},{"key":"4543_CR285","doi-asserted-by":"publisher","first-page":"1570","DOI":"10.1016\/J.BBAPAP.2008.08.007","volume":"1784","author":"H Shoval","year":"2008","unstructured":"Shoval H, Weiner L, Gazit E et al (2008) Polyphenol-induced dissociation of various amyloid fibrils results in a methionine-independent formation of ROS. Biochim Biophys Acta - Proteins Proteomics 1784:1570\u20131577. https:\/\/doi.org\/10.1016\/J.BBAPAP.2008.08.007","journal-title":"Biochim Biophys Acta - Proteins Proteomics"},{"key":"4543_CR286","doi-asserted-by":"publisher","first-page":"1097","DOI":"10.1111\/J.1471-4159.2008.05866.X","volume":"108","author":"HS Hong","year":"2009","unstructured":"Hong HS, Rana S, Barrigan L et al (2009) Inhibition of Alzheimer\u2019s amyloid toxicity with a tricyclic pyrone molecule in vitro and in vivo. J Neurochem 108:1097\u20131108. https:\/\/doi.org\/10.1111\/J.1471-4159.2008.05866.X","journal-title":"J Neurochem"}],"container-title":["Molecular Neurobiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-024-04543-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12035-024-04543-4\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-024-04543-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,3,4]],"date-time":"2025-03-04T10:10:14Z","timestamp":1741083014000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s12035-024-04543-4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,10,24]]},"references-count":286,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2025,4]]}},"alternative-id":["4543"],"URL":"https:\/\/doi.org\/10.1007\/s12035-024-04543-4","relation":{},"ISSN":["0893-7648","1559-1182"],"issn-type":[{"value":"0893-7648","type":"print"},{"value":"1559-1182","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,10,24]]},"assertion":[{"value":"5 March 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"8 October 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"24 October 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics Approval"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to Participate"}},{"value":"Not applicable.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for Publication"}},{"value":"The authors declare no competing interests.","order":5,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of Interest"}}]}}