{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T07:23:30Z","timestamp":1787988210460,"version":"build-2784847793"},"reference-count":219,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2022,9,22]],"date-time":"2022-09-22T00:00:00Z","timestamp":1663804800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Horizon-Euratom-2021-NRT-01-11 project","award":["101061694"],"award-info":[{"award-number":["101061694"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Alzheimer\u2019s disease (AD) is the most common neurodegenerative disorder in the elderly. The two cardinal neuropathological hallmarks of AD are the senile plaques, which are extracellular deposits mainly constituted by beta-amyloids, and neurofibrillary tangles formed by abnormally phosphorylated Tau (p-Tau) located in the cytoplasm of neurons. Although the research has made relevant progress in the management of the disease, the treatment is still lacking. Only symptomatic medications exist for the disease, and, in the meantime, laboratories worldwide are investigating disease-modifying treatments for AD. In the present review, results centered on the use of peptides of different sizes involved in AD are presented.<\/jats:p>","DOI":"10.3390\/biom12101344","type":"journal-article","created":{"date-parts":[[2022,9,22]],"date-time":"2022-09-22T05:33:14Z","timestamp":1663824794000},"page":"1344","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["From Small Peptides to Large Proteins against Alzheimer\u2019sDisease"],"prefix":"10.3390","volume":"12","author":[{"given":"Pasquale","family":"Picone","sequence":"first","affiliation":[{"name":"Istituto per la Ricerca e l\u2019Innovazione Biomedica, Consiglio Nazionale delle Ricerche, Via U. La Malfa 153, 90146 Palermo, Italy"},{"name":"Dipartmento of Scienze Biologiche, Chimiche, Farmaceutiche e Tecnologiche (STEBICEF), University of Palermo, 90128 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tiziana","family":"Sanfilippo","sequence":"additional","affiliation":[{"name":"Ambulatorio di Nutrizione Clinica ASP Palermo, Via G. Cusmano 24, 90141 Palermo, Italy"},{"name":"Anestesia e Rianimazione, Presidio Ospedaliero \u201cS. Cimino\u201d, 90141 Termini Imerese, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6033-4745","authenticated-orcid":false,"given":"Sonya","family":"Vasto","sequence":"additional","affiliation":[{"name":"Dipartmento of Scienze Biologiche, Chimiche, Farmaceutiche e Tecnologiche (STEBICEF), University of Palermo, 90128 Palermo, Italy"},{"name":"Istituti Euro-Mediterranei di Scienza e Tecnologia (IEMEST), Via M. Miraglia 20, 90139 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5160-5865","authenticated-orcid":false,"given":"Sara","family":"Baldassano","sequence":"additional","affiliation":[{"name":"Dipartmento of Scienze Biologiche, Chimiche, Farmaceutiche e Tecnologiche (STEBICEF), University of Palermo, 90128 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rossella","family":"Guggino","sequence":"additional","affiliation":[{"name":"Ambulatorio di Nutrizione Clinica ASP Palermo, Via G. Cusmano 24, 90141 Palermo, Italy"},{"name":"Anestesia e Rianimazione, Presidio Ospedaliero \u201cS. Cimino\u201d, 90141 Termini Imerese, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4325-417X","authenticated-orcid":false,"given":"Domenico","family":"Nuzzo","sequence":"additional","affiliation":[{"name":"Istituto per la Ricerca e l\u2019Innovazione Biomedica, Consiglio Nazionale delle Ricerche, Via U. La Malfa 153, 90146 Palermo, Italy"},{"name":"Dipartmento of Scienze Biologiche, Chimiche, Farmaceutiche e Tecnologiche (STEBICEF), University of Palermo, 90128 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5841-9133","authenticated-orcid":false,"given":"Donatella","family":"Bulone","sequence":"additional","affiliation":[{"name":"Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Via U. La. Malfa 153, 90146 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4622-7361","authenticated-orcid":false,"given":"Pier Luigi","family":"San Biagio","sequence":"additional","affiliation":[{"name":"Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Via U. La. Malfa 153, 90146 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3098-4915","authenticated-orcid":false,"given":"Emanuela","family":"Muscolino","sequence":"additional","affiliation":[{"name":"Dipartimento di Ingegneria, Universit\u00e0 degli Studi di Palermo, Viale delle Scienze, Bldg 6, 90128 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2829-523X","authenticated-orcid":false,"given":"Roberto","family":"Monastero","sequence":"additional","affiliation":[{"name":"Dipartimento di Biomedicina, Neuroscienze e Diagnostica Avanzata, Universit\u00e0 degli Studi di Palermo, Via del Vespro 129, 90127 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0076-5161","authenticated-orcid":false,"given":"Clelia","family":"Dispenza","sequence":"additional","affiliation":[{"name":"Dipartimento di Ingegneria, Universit\u00e0 degli Studi di Palermo, Viale delle Scienze, Bldg 6, 90128 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6667-0205","authenticated-orcid":false,"given":"Daniela","family":"Giacomazza","sequence":"additional","affiliation":[{"name":"Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Via U. La. Malfa 153, 90146 Palermo, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,9,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3944","DOI":"10.1111\/ejn.14758","article-title":"Obesity and Alzheimer\u2019s disease: Molecular bases","volume":"52","author":"Picone","year":"2020","journal-title":"Eur. J. Neurosci."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1275","DOI":"10.1007\/s10072-013-1424-7","article-title":"Non-cognitive symptoms and related conditions in the Alzheimer\u2019s Disease: A literature review","volume":"34","author":"Raudino","year":"2013","journal-title":"Neurol. Sci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1016\/j.jalz.2014.01.001","article-title":"A conceptual framework for research on subjective cognitive decline in preclinical Alzheimer\u2019s disease","volume":"10","author":"Jessen","year":"2014","journal-title":"Alzheimers Dement."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"23","DOI":"10.3233\/JAD-2007-12104","article-title":"Mild cognitive impairment: A systematic review","volume":"12","author":"Mariani","year":"2007","journal-title":"J. Alzheimers Dis."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1577","DOI":"10.1016\/S0140-6736(20)32205-4","article-title":"Alzheimer\u2019s disease","volume":"397","author":"Scheltens","year":"2021","journal-title":"Lancet"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1212\/WNL.0000000000002923","article-title":"A\/T\/N: An unbiased descriptive classification scheme for Alzheimer disease biomarkers","volume":"87","author":"Jack","year":"2016","journal-title":"Neurology"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1186\/s13195-021-00817-4","article-title":"Prognostic value of amyloid\/tau\/neurodegeneration (ATN) classification based on diagnostic cerebrospinal fluid samples for Alzheimer\u2019s disease","volume":"13","author":"Delmotte","year":"2021","journal-title":"Alzheimers Res. Ther."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0197-4580(95)00021-6","article-title":"Staging of Alzheimer\u2019s disease-related neurofibrillary changes","volume":"16","author":"Braak","year":"1995","journal-title":"Neurobiol. Aging"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"244102","DOI":"10.1088\/0953-8984\/24\/24\/244102","article-title":"Alzheimer\u2019s Disease: Biological aspects, therapeutic perspectives and diagnostic tools","volume":"24","author":"Giacomazza","year":"2012","journal-title":"J. Phys. Condens. Matter"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"11339","DOI":"10.1074\/jbc.271.19.11339","article-title":"APP-BP1, a novel protein that binds to the carboxyl-terminal region of the Amyloid Precursor Protein","volume":"271","author":"Chow","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1016\/j.conb.2004.08.001","article-title":"Amyloid-beta precursor protein processing in neurodegeneration","volume":"14","author":"Wilquet","year":"2004","journal-title":"Curr. Opin. Neurobiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1111\/jnc.12675","article-title":"Insights into the physiological function of the \u03b2-amyloid precursor protein: Beyond Alzheimer\u2019s disease","volume":"129","author":"Dawkins","year":"2014","journal-title":"J. Neurochem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1007\/s12603-019-1162-5","article-title":"What is the physiological function of amyloid-beta protein?","volume":"23","author":"Morley","year":"2019","journal-title":"J. Nutr. Health Aging"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"3363","DOI":"10.1073\/pnas.88.8.3363","article-title":"Amnestic effects in mice of four synthetic peptides homologous to amyloid beta protein from patients with Alzheimer disease","volume":"88","author":"Flood","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1113\/jphysiol.2006.111203","article-title":"Physiological roles for amyloid \u03b2 peptide","volume":"575","author":"Pearson","year":"2006","journal-title":"J. Physiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"145","DOI":"10.3233\/JAD-2012-112186","article-title":"Evidence that the amyloid-\u03b2 protein precursor intracellular domain, AICD, derives from \u03b2-secretase-generated C-terminal fragment","volume":"30","author":"Flammang","year":"2012","journal-title":"J. Alzheimers Dis."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"a006270","DOI":"10.1101\/cshperspect.a006270","article-title":"Trafficking and proteolytic processing of APP","volume":"2","author":"Haass","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_18","first-page":"159","article-title":"The metalloprotease meprin \u03b2 is an alternative \u03b2-secretase of APP","volume":"9","author":"Pietrzik","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.bbrc.2006.10.181","article-title":"ADAM19 is tightly associated with constitutive Alzheimer\u2019s disease APP alpha-secretase in A172 cells","volume":"352","author":"Tanabe","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1172\/JCI20864","article-title":"A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model","volume":"113","author":"Postina","year":"2004","journal-title":"J. Clin. Investig."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/sj.emboj.7600061","article-title":"Take five\u2013BACE and the gamma-secretase quartet conduct Alzheimer\u2019s amyloid beta-peptide generation","volume":"23","author":"Haass","year":"2004","journal-title":"EMBO J."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1002\/med.21622","article-title":"BACE1 inhibitors: Current status and future directions in treating Alzheimer\u2019s disease","volume":"40","author":"Abdin","year":"2020","journal-title":"Med. Res. Rev."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"178","DOI":"10.3389\/fchem.2018.00178","article-title":"Highlights in BACE1 inhibitors for Alzheimer\u2019s disease treatment","volume":"6","author":"Coimbra","year":"2018","journal-title":"Front. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"51654","DOI":"10.1074\/jbc.M404500200","article-title":"Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria","volume":"279","author":"Hansson","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1126\/science.1566067","article-title":"Alzheimer\u2019s disease: The amyloid cascade hypothesis","volume":"256","author":"Hardy","year":"1992","journal-title":"Science"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1001\/archneurol.2011.221","article-title":"Autosomal recessive causes likely in early-onset Alzheimer disease","volume":"69","author":"Wingo","year":"2012","journal-title":"Arch. Neurol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2677","DOI":"10.1042\/BCJ20160868","article-title":"The growth of amyloid fibrils: Rates and mechanisms","volume":"476","author":"Buell","year":"2019","journal-title":"Biochem. J."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"6523","DOI":"10.1021\/acs.analchem.1c00527","article-title":"Unraveling the speciation of b-amyloid peptides during the aggregation process by Taylor dispersion analysis","volume":"93","author":"Deleanu","year":"2021","journal-title":"Anal. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1073\/pnas.84.11.3881","article-title":"Amyloid fibrils in human insulinoma and islets of Langherans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells","volume":"84","author":"Westermark","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Akter, R., Cao, P., Noor, H., Ridgway, Z., Tu, L.-T., Wang, H., Wong, A.G., Zhang, X., Abedini, A., and Schmidt, A.M. (2016). Islet amyloid polypeptide: Structure, function, and pathology. J. Diab. Res., 2798269.","DOI":"10.1155\/2016\/2798269"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.jmb.2012.01.048","article-title":"The Effect of A\u03b2 on IAPP Aggregation in the Presence of an Isolated \u03b2-Cell Membrane","volume":"421","author":"Seeliger","year":"2012","journal-title":"J. Mol. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2101301","DOI":"10.1002\/adbi.202101301","article-title":"Recent advances in the discovery of the therapeutics to curtail islet amyloid polypeptide aggregation in Type 2 Diabetes treatment","volume":"2022","author":"Smith","year":"2022","journal-title":"Advanced Biology"},{"key":"ref_33","first-page":"140772","article-title":"Silybins inhibit human IAPP amyloid growth and toxicity through stereospecific interactions","volume":"1870","author":"Ilie","year":"2021","journal-title":"Biochim. Biophys. Acta-Proteins Proteom."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"5235","DOI":"10.1074\/jbc.M111.327817","article-title":"Fibril structure of human islet amyloid polypeptide","volume":"287","author":"Bedrood","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1016\/j.bbamem.2018.03.015","article-title":"Role of the cell membrane interface in modulating production and uptake of Alzheimer\u2019s beta amyloid protein","volume":"1860","author":"Bharadwaj","year":"2018","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"10356","DOI":"10.1038\/s41598-020-66602-9","article-title":"Amylin and beta amyloid proteins interact to form amorphous heterocomplexes with enhanced toxicity in neuronal cells","volume":"10","author":"Bharadwaj","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1021\/acschemneuro.6b00247","article-title":"Molecular understanding of A\u03b2-hIAPP cross-seeding assemblies on lipid membranes","volume":"8","author":"Zhang","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Simic, G., Babic Leko, M., Wray, S., Harrington, C., Delalle, I., Jovanov-Milosevic, N., Bazadona, D., Bu\u00e9e, L., da Silva, R.R., and Di Giovanni, G. (2016). Tau protein hyperphoshorilation and aggregation in Alzheimer\u2019s Disease and other tauopathies, and possible neuroprotective strategies. Biomolecules, 6.","DOI":"10.3390\/biom6010006"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.1039\/C7CS00706J","article-title":"Shedding light on tau protein aggregation: The progress in developing highly selective fluorophores","volume":"47","author":"Verwilst","year":"2018","journal-title":"Chem. Soc. Rev."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2219","DOI":"10.1007\/s00018-007-7220-x","article-title":"Tauopathies","volume":"64","author":"Hernandez","year":"2007","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1038\/nrn.2015.1","article-title":"Tau in physiology and pathology","volume":"17","author":"Wang","year":"2016","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"24374","DOI":"10.1016\/S0021-9258(20)80536-5","article-title":"Microtubule-associated protein tau: Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease","volume":"268","author":"Kopke","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1111\/j.1755-5949.2010.00177.x","article-title":"The role of Tau in Alzheimer\u2019s Disease and related disorders","volume":"17","author":"Madeiros","year":"2011","journal-title":"CNS Neurosci. Ther."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/978-981-32-9358-8_2","article-title":"Structure of NTF: Biochemical approach","volume":"1184","author":"Hasegawa","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"e98049","DOI":"10.15252\/embj.201798049","article-title":"Tau protein liquid-liquid phase separation can initiate Tau aggregation","volume":"37","author":"Wegmann","year":"2018","journal-title":"EMBO J."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"e202006054","DOI":"10.1083\/jcb.202006054","article-title":"The prolin-rich domain promotes Tau liquid-liquid phase separation in cells","volume":"219","author":"Zhang","year":"2020","journal-title":"J. Cell Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/j.neuron.2010.08.044","article-title":"Acetylation of tau inhibits its degradation and contributes to tauopathy","volume":"67","author":"Min","year":"2010","journal-title":"Neuron"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1093\/hmg\/ddt402","article-title":"Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance","volume":"23","author":"Cook","year":"2014","journal-title":"Human. Mol. Genet."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S0022-510X(98)00092-6","article-title":"Copper, iron and zinc in Alzheimer\u2019s disease senile plaques","volume":"158","author":"Lovell","year":"1998","journal-title":"J. Neurol. Sci."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2026","DOI":"10.1021\/acs.accounts.9b00248","article-title":"Metal Ions in Alzheimer\u2019s Disease: A Key Role or Not?","volume":"52","author":"Liu","year":"2019","journal-title":"ACC Chem. Res."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"9812178","DOI":"10.1155\/2016\/9812178","article-title":"Metals and neuronal metal bindind proteins implicated in Alzheimer\u2019s disease","volume":"2016","author":"Cristovao","year":"2016","journal-title":"Oxidative Med. Cell. Long."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.bbamcr.2006.08.039","article-title":"Protein oxidation and cellular homeostasis: Enphasis on metabolism","volume":"1773","author":"Cecarini","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"151","DOI":"10.3164\/jcbn.14-10","article-title":"The role of lipid peroxidation in neurological disorders","volume":"54","author":"Shichiri","year":"2014","journal-title":"J. Clin. Biochem. Nutr."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"9646","DOI":"10.1074\/jbc.M110.177246","article-title":"Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-\u03b2 stability, oligomerization, and aggregation: Amyloid-\u03b2 destabilization promotes annular protofibril formation","volume":"286","author":"Chen","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1007\/s10534-009-9277-5","article-title":"Serum zinc is decreased in Alzheimer\u2019s disease and serum arsenic correlates positively with cognitive ability","volume":"23","author":"Baum","year":"2010","journal-title":"BioMetals"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1159\/000065696","article-title":"Iron: A pathological mediator of Alzheimer disease?","volume":"24","author":"Bishop","year":"2002","journal-title":"Dev. Neurosci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1784","DOI":"10.1111\/j.1471-4159.2009.06269.x","article-title":"Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-\u03b2 (1\u201342) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators","volume":"110","author":"Tougu","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"41533","DOI":"10.1074\/jbc.M110.171355","article-title":"Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-\u03b2 from Alzheimer disease","volume":"285","author":"Sarell","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"21","DOI":"10.3389\/fnmol.2017.00021","article-title":"Structure and synaptic function of metal binding to amyloid precursor protein and its proteolytic fragments","volume":"10","author":"Wild","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"7268","DOI":"10.1002\/chem.201600286","article-title":"Histidine-Rich Oligopeptides to Lessen Copper-Mediated Amyloid-\u03b2 Toxicity","volume":"22","author":"Caballero","year":"2016","journal-title":"Chemistry"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1777","DOI":"10.1002\/chem.202003949","article-title":"Impact of N-Truncated A\u03b2 Peptides on Cu- and Cu(A\u03b2)-Generated ROS: Cu I Matters!","volume":"27","author":"Esmieu","year":"2021","journal-title":"Chemistry"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1186\/s13041-020-00654-w","article-title":"Metallothionein-3 as a multifunctional player in the control of cellular processes and diseases","volume":"13","author":"Koh","year":"2020","journal-title":"Mol. Brain"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"7683","DOI":"10.1039\/C7CS00448F","article-title":"Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins","volume":"46","author":"Santoro","year":"2017","journal-title":"Chem. Soc. Rev."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"13763","DOI":"10.1038\/s41598-017-12800-x","article-title":"The efficacy and pharmacological mechanism of Zn7MT3 to protect against Alzheimer\u2019s disease","volume":"7","author":"Xu","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"463","DOI":"10.3389\/fnins.2019.00463","article-title":"S100 proteins in Alzheimer\u2019s disease","volume":"13","author":"Cristovao","year":"2019","journal-title":"Front. Neurosci."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.neubiorev.2017.06.006","article-title":"Zinc transporter 3 (ZnT3) and vescicular zinc in central nervous system function","volume":"80","author":"McAllister","year":"2017","journal-title":"Neurosci. Biobehav. Rev."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1523\/JNEUROSCI.5255-09.2010","article-title":"Cognitive loss in zinc transporter-3 knock-out mice: A phenocopy for the synaptic and memory deficits of Alzheimer\u2019s disease?","volume":"30","author":"Adlard","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/S0197-4580(01)00293-7","article-title":"The role of activated astrocytes and of the neurotrophic cytokine S100B in the pathogenesis of Alzheimer\u2019s disease","volume":"22","author":"Mrak","year":"2001","journal-title":"Neurobiol. Aging"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1046\/j.1471-4159.2002.t01-1-01061.x","article-title":"Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: Implications in the formation of neurofibrillary tangles of Alzheimer\u2019s disease","volume":"82","author":"Yamamoto","year":"2002","journal-title":"J. Neurochem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1021\/acs.chemrev.8b00138","article-title":"Development of Multifunctional Molecules as Potential Therapeutic Candidates for Alzheimer\u2019s Disease, Parkinson\u2019s Disease, and Amyotrophic Lateral Sclerosis in the Last Decade","volume":"119","author":"Savelieff","year":"2019","journal-title":"Chem. Rev."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"715","DOI":"10.2174\/0929867324666171026163144","article-title":"Peptides and their Metal Complexes in Neurodegenerative Diseases: From Structural Studies to Nanomedicine Prospects","volume":"25","author":"Trapani","year":"2018","journal-title":"Curr. Med. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"101792","DOI":"10.1016\/j.isci.2020.101792","article-title":"Designed Metal-ATCUN Derivatives: Redox- and Non-redox-Based Applications Relevant for Chemistry, Biology, and Medicine","volume":"23","author":"Maiti","year":"2020","journal-title":"iScience"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"4994","DOI":"10.1021\/ja100943r","article-title":"A prochelator activated by beta-secretase inhibits Abeta aggregation and suppresses copper-induced reactive oxygen species formation","volume":"132","author":"Folk","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1021\/acschemneuro.6b00145","article-title":"Tripeptide GGH as the Inhibitor of Copper-Amyloid-\u03b2-Mediated Redox Reaction and Toxicity","volume":"7","author":"Hu","year":"2016","journal-title":"ACS Chem. Neurosci."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1266","DOI":"10.2174\/092986709787846578","article-title":"Mitochondrial respiratory complex I: Structure, function and implication in human diseases","volume":"16","author":"Sharma","year":"2009","journal-title":"Curr. Med. Chem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.biocel.2006.07.001","article-title":"Free radicals and antioxidants in normal physiological functions and human diseases","volume":"39","author":"Valko","year":"2007","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1159\/000136357","article-title":"Oxidative innate immune defenses by Nox\/Duox family NADPH oxidases","volume":"15","author":"Rada","year":"2008","journal-title":"Contrib. Microbiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"714370","DOI":"10.3389\/fcell.2021.714370","article-title":"Physiological signaling functions of reactive oxygen species in stem cells: From flies to man","volume":"9","author":"Sinenko","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.3109\/10715762.2012.714466","article-title":"Are oxidative stress and mitochondrial dysfunction the key players in the neurodegenerative diseases?","volume":"46","author":"Giacomazza","year":"2012","journal-title":"Free Ras. Res."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"757","DOI":"10.2147\/CIA.S158513","article-title":"Oxidative stress, aging and diseases","volume":"13","author":"Liguori","year":"2018","journal-title":"Clin. Interv. Aging"},{"key":"ref_81","first-page":"2105607","article-title":"Oxidative stress in neurodegenerative diseases: From a mitochondrial point of view","volume":"2019","author":"Cenini","year":"2019","journal-title":"Oxidative Med. Cell. Long."},{"key":"ref_82","first-page":"977","article-title":"Review of oxidative stress products and related genes in early Alzheimer\u2019s disease","volume":"83","author":"Cioffi","year":"2021","journal-title":"J. Alz. Dis."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"7497","DOI":"10.1093\/nar\/gkm821","article-title":"Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer\u2019s disease","volume":"35","author":"Lovell","year":"2007","journal-title":"Nucleic Acid Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"201","DOI":"10.2217\/bmm-2017-0456","article-title":"Oxidative stress as a biomarker for Alzheimer\u2019s disease","volume":"12","author":"Collin","year":"2018","journal-title":"Biomark. Med."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1016\/j.bbadis.2013.09.010","article-title":"The Alzheimer\u2019s disease mitochondrial cascade hypothesis: Progress and perspectives","volume":"1842","author":"Swerdlow","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.redox.2017.10.014","article-title":"Oxidative stress and the amyloid beta peptide in Alzheimer\u2019s disease","volume":"14","author":"Cheignon","year":"2018","journal-title":"Redox Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.neurobiolaging.2021.07.014","article-title":"Emerging roles of oxidative stress in brain aging and Alzheimer\u2019s disease","volume":"107","author":"Cotman","year":"2021","journal-title":"Neurobiol. Aging"},{"key":"ref_88","first-page":"1105","article-title":"Oxidative stress, synaptic dysfunction, and Alzheimer\u2019s disease","volume":"57","author":"Tonnies","year":"2017","journal-title":"J. Alz. Dis."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1021\/cn100057j","article-title":"Oral treatment with the d-enantiomeric peptide D3 improves the pathology and behavior of Alzheimer\u2019s Disease transgenic mice","volume":"1","author":"Funke","year":"2010","journal-title":"ACS Chem. Neurosci."},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Bened\u00e9, S., and Molina, E. (2020). Chicken egg proteins and derived peptides with antioxidant properties. Foods, 9.","DOI":"10.3390\/foods9060735"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1462","DOI":"10.3382\/ps\/pex399","article-title":"Antioxidant, angiotensin-converting enzyme inhibitory activity and other functional properties of egg white proteins and their derived peptides\u2014A review","volume":"97","author":"Abeyrathne","year":"2018","journal-title":"Poult. Sci."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"8274","DOI":"10.3390\/nu7105394","article-title":"Hen egg as an antioxidant food commodity: A review","volume":"7","author":"Nimalaratne","year":"2015","journal-title":"Nutrients"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.foodchem.2015.05.014","article-title":"Purification and characterization of antioxidant peptides from enzymatically hydrolyzed chicken egg white","volume":"188","author":"Nimalaratne","year":"2015","journal-title":"Food Chem."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1016\/j.foodchem.2014.11.142","article-title":"Purification and identification of novel antioxidant peptides from egg white protein and their antioxidant activities","volume":"175","author":"Liu","year":"2015","journal-title":"Food Chem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1939","DOI":"10.4315\/0362-028X-67.9.1939","article-title":"Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis","volume":"67","author":"Davalos","year":"2004","journal-title":"J. Food Prot."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1016\/j.foodchem.2012.05.093","article-title":"Effects of addition of egg ovotransferrin-derived peptides on the oxygen radical absorbance capacity of different teas","volume":"135","author":"Huang","year":"2012","journal-title":"Food Chem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"2604","DOI":"10.1002\/jsfa.3015","article-title":"Antioxidant activity of tryptic digests of hen egg yolk phosvitin: Antioxidant activity of phosvitin peptides","volume":"87","author":"Xu","year":"2007","journal-title":"J. Sci. Food Agric."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"2648","DOI":"10.1002\/jsfa.10295","article-title":"Identification of ovalbumin-derived peptides as multi-target inhibitors of AChE, BChE, and BACE1","volume":"100","author":"Yu","year":"2020","journal-title":"J. Sci. Food Agric."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1039\/C7FO01462G","article-title":"Anti-Alzheimers activity and molecular mechanism of albumin-derived peptides against AChE and BChE","volume":"9","author":"Yu","year":"2018","journal-title":"Food Funct."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Nuzzo, D., Frinchi, F., Giardina, C., Scordino, M., Zuccarini, M., De Simone, C., Di Carlo, M., Belluardo, N., Mud\u00f2, G., and Di Liberto, V. (2022). Neuroprotective and Antioxidant Role of Oxotremorine-M, a Non-selective Muscarinic Acetylcholine Receptors Agonist, in a Cellular Model of Alzheimer Disease. Cell Mol. Neurobiol., 1\u201316.","DOI":"10.1007\/s10571-022-01274-9"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.fshw.2020.01.004","article-title":"Biological evaluation and interaction mechanism of beta-site APP cleaving enzyme 1 inhibitory pentapeptide from egg albumin","volume":"9","author":"Yu","year":"2020","journal-title":"Food Sci. Hum. Wellness"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1016\/S0959-440X(03)00100-3","article-title":"Design strategies for anti-amyloid agents","volume":"13","author":"Mason","year":"2003","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1021\/acscombsci.6b00116","article-title":"Rationally designed peptides and peptidomimetics as inhibitors of amyloid-\u03b2 (Ab) aggregation: Potential therapeutics of Alzheimer\u2019s Disease","volume":"19","author":"Goyal","year":"2017","journal-title":"ACS Comb. Sci."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1517\/13543776.2013.772983","article-title":"Small-molecule inhibitors\/modulators of amyloid-\u03b2 peptide aggregation and toxicity for the treatment of Alzheimer\u2019s disease: A patent review (2010\u20132012)","volume":"23","author":"Belluti","year":"2013","journal-title":"Expert Opin. Ther. Pat."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1006\/bbrc.1996.1413","article-title":"Inhibition of Alzheimer\u2019s amyloidosis by peptides that prevent \u03b2-sheet conformation","volume":"116","author":"Soto","year":"1996","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1038\/372092a0","article-title":"Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments","volume":"372","author":"Ma","year":"1994","journal-title":"Nature"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1023\/A:1021600212829","article-title":"Increased fibrillar beta-amyloid in response to human C1q injections into hippocampus and cortex of APP + PS1 transgenic mice","volume":"28","author":"Boyett","year":"2003","journal-title":"Neurochem. Res."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1016\/j.bbamem.2007.05.026","article-title":"A mechanistic link between oxidative stress and membrane mediated amyloidogenesis revealed by infrared spectroscopy","volume":"1768","author":"Komatsu","year":"2007","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.bpc.2017.05.005","article-title":"The effect of \u03b2-sheet breaker peptides on metal associated Amyloid-\u03b2 peptide aggregation process","volume":"229","author":"Stellato","year":"2017","journal-title":"Biophys. Chem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/0197-4580(89)90108-5","article-title":"Proteoglycans in the pathogenesis of Alzheimer\u2019s disease and other amyloidosis","volume":"10","author":"Snow","year":"1989","journal-title":"Neurobiol. Aging"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1111\/j.1471-4159.2006.04426.x","article-title":"Abeta oligomers\u2014A decade of discovery","volume":"101","author":"Walsh","year":"2007","journal-title":"J. Neurochem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"15659","DOI":"10.1073\/pnas.0705888104","article-title":"Molecular basis for passive immunotherapy of Alzheimer\u2019s disease","volume":"104","author":"Gardberg","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1523","DOI":"10.1126\/science.1151839","article-title":"Amyloid fibrils of the HET-s (218\u2013289) prion form a beta solenoid with a triangular hydrophobic core","volume":"319","author":"Wasmer","year":"2008","journal-title":"Science"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"23580","DOI":"10.1074\/jbc.M109.038133","article-title":"Amino acid position-specific contributions to amyloid beta-protein oligomerization","volume":"284","author":"Maji","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"14175","DOI":"10.1073\/pnas.0807163105","article-title":"C-terminal peptides coassemble into Abeta42 oligomers and protect neurons against Abeta42-induced neurotoxicity","volume":"105","author":"Fradinger","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1007\/s00894-016-2960-x","article-title":"Investigation of the effect of erythrosine B on amyloid beta peptide using molecular modeling","volume":"22","author":"Lee","year":"2016","journal-title":"J. Mol. Model."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"15998","DOI":"10.1038\/s41598-020-72989-2","article-title":"Hyaluronan-carnosine conjugates inhibit A\u03b2 aggregation and toxicity","volume":"10","author":"Greco","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"7673","DOI":"10.1039\/C7CC03102E","article-title":"Stabilizing amyloid-\u03b2 peptide by the N-terminus capture is capable of preventing and eliminating amyloid-\u03b2 oligomers","volume":"53","author":"Wen","year":"2017","journal-title":"Chem. Commun."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"553","DOI":"10.2174\/1389450043345290","article-title":"Beta-sheet breakers for Alzheimer\u2019s disease therapy","volume":"5","author":"Bieler","year":"2004","journal-title":"Curr. Drug Targets"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1038\/nm0798-822","article-title":"Beta-sheet breaker peptides inhibit fibrillogenesis ia rat brain model of amyloidosis: Implications for Alzheimer\u2019s therapy","volume":"4","author":"Soto","year":"1998","journal-title":"Nat. Med."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"23557","DOI":"10.1039\/D1RA03609B","article-title":"Destabilization potential of beta sheet breaker peptides on Abeta fibril structure: An insight from molecular dynamics simulation study","volume":"11","author":"Jani","year":"2021","journal-title":"RSC Adv."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1002\/prot.26057","article-title":"\u03b2-sheet breakers with consecutive phenylalanines: Insights into mechanism of dissolution of \u03b2-amyloid fibrils","volume":"89","author":"Jamula","year":"2021","journal-title":"Proteins"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1021\/acschemneuro.6b00154","article-title":"Modulation of amyloid \u03b2-protein (A\u03b2) assembly by homologous C-terminal fragments as a strategy for inhibiting A\u03b2 toxicity","volume":"7","author":"Li","year":"2016","journal-title":"ACS Chem. Neurosci."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"405","DOI":"10.3389\/fncel.2019.00405","article-title":"The evolving concept pf the blood brain barrier (BBB): From a single static barrier to a heterogeneous and dynamic relay center","volume":"13","author":"Erice","year":"2019","journal-title":"Front. Cell. Neurosci."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"a020412","DOI":"10.1101\/cshperspect.a020412","article-title":"The Blood-Brain Barrier","volume":"7","author":"Daneman","year":"2015","journal-title":"Cold Spring Harbor. Perspect. Biol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"2000068","DOI":"10.1002\/anbr.202000068","article-title":"Biochemical- and biophysical-induced barrigenesis in the blood-brain barrier: A review of barrigenic factor for use in vitro models","volume":"1","author":"Schofield","year":"2021","journal-title":"Adv. NanoBiomed. Res."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"695479","DOI":"10.3389\/fncel.2021.695479","article-title":"Relationship between amyloid-\u03b2 deposition and blood-brain barrier dysfunction in Alheimer\u2019s disease","volume":"15","author":"Wang","year":"2021","journal-title":"Front. Cell. Neurosci."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"2232","DOI":"10.2337\/db14-0568","article-title":"Insulin action in brain regulates systemic metabolism and brain function","volume":"63","author":"Kleinridders","year":"2014","journal-title":"Diabetes"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1609","DOI":"10.1007\/s00125-016-3996-2","article-title":"Cerebral cortex: A target and source of insulin?","volume":"59","author":"Csajbok","year":"2016","journal-title":"Diabetologia"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1038\/2151375a0","article-title":"Insulin in the cerebrospinal fluid","volume":"215","author":"Margolis","year":"1967","journal-title":"Nature"},{"key":"ref_131","first-page":"E331","article-title":"Relationship between plasma and cerebrospinal fluid insulin levels of dogs","volume":"233","author":"Woods","year":"1977","journal-title":"Am. J. Physiol"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"161","DOI":"10.3389\/fendo.2014.00161","article-title":"Insulin in the brain: Its pathophysiological implications for states related with central insulin resistance, Type 2 Diabetes and Alzheimer\u2019s disease","volume":"5","author":"Blazquez","year":"2014","journal-title":"Front. Endocrinol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"E8478","DOI":"10.1073\/pnas.1710625114","article-title":"Endothelial insulin receptors differentially control insulin signaling kinetics in peripheral tissues and brain of mice","volume":"114","author":"Konishi","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Sartorius, T., Peter, A., Heni, M., Maetzeler, W., Fritsche, A., Haring, H.-U., and Hennige, A.M. (2015). The brain response to peripheral insulin declines with age: A contribution of the blood\u2014brain barrier?. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0126804"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"723","DOI":"10.2174\/1567205012666150710115506","article-title":"Insulin resistance as common molecular denominator linking obesity to Alzheimer\u2019s disease","volume":"12","author":"Nuzzo","year":"2015","journal-title":"Curr. Alzheimer Res."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1016\/S1474-4422(20)30231-3","article-title":"Brain insulin resistance in Alzheimer\u2019s disease and related disorders: Mechanisms and therapeutic approaches","volume":"19","author":"Kellar","year":"2020","journal-title":"Lancet Neurol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1089\/rej.2011.1289","article-title":"Can Alzheimer disease be a form of type 3 diabetes?","volume":"15","author":"Accardi","year":"2012","journal-title":"Rejuvenation Res."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1016\/j.jalz.2014.03.011","article-title":"Insulin resistance predicts brain amyloid deposition in late middle-aged adults","volume":"11","author":"Willette","year":"2015","journal-title":"Alzheimers Dement."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"e1150","DOI":"10.1212\/WNL.0000000000005214","article-title":"Midlife insulin resistance, APOE genotype, and late-life brain amyloid accumulation","volume":"90","author":"Ekblad","year":"2018","journal-title":"Neurology"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"63","DOI":"10.3233\/JAD-2005-7107","article-title":"Impaired insulin and insulin-like growth factor expression and signaling mechanisms in Alzheimer\u2019s disease\u2014Is this type 3 diabetes?","volume":"7","author":"Steen","year":"2005","journal-title":"J. Alzheimers Dis."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1096\/fj.06-7703com","article-title":"Amyloid beta oligomers induce impairment of neuronal insulin receptors","volume":"22","author":"Zhao","year":"2008","journal-title":"FASEB J."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1091\/mbc.e08-07-0777","article-title":"The insulin\/AKT signaling pathway is targeted by intracellular \u03b2-amyloid","volume":"20","author":"Lee","year":"2009","journal-title":"Mol. Biol. Cell"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/j.bbadis.2008.10.014","article-title":"Insulin resistance and amyloidogenesis as common molecular foundation for type 2 diabetes and Alzheimer\u2019s disease","volume":"1792","author":"Zhao","year":"2009","journal-title":"Biochim. Biophys. Acta-Mol. Basis Disease"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"4519","DOI":"10.1021\/acs.biochem.9b00696","article-title":"Insulin inhibits A\u03b242 aggregation and prevents A\u03b242-induced membrane disruption","volume":"58","author":"Long","year":"2019","journal-title":"Biochemistry"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"104739","DOI":"10.1016\/j.nbd.2020.104739","article-title":"Insulin deficiency promotes formation of toxic amyloid-\u03b242 conformer co-aggregating with hyper-phosphorylated tau oligomer in an Alzheimer\u2019s disease model","volume":"137","author":"Imamura","year":"2020","journal-title":"Neurobiol. Dis."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1111\/j.1474-9726.2011.00724.x","article-title":"Insulin-activated Akt rescues A\u03b2 oxidative stress-induced cell death by orchestrating molecular trafficking","volume":"10","author":"Picone","year":"2011","journal-title":"Aging Cell"},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Galizzi, G., and Di Carlo, M. (2022). Insulin and its key role for mitochondrial function\/dysfunction and quality control: A shared link between dysmetabolism and neurodegeneration. Biology, 11.","DOI":"10.3390\/biology11060943"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.biomaterials.2015.11.057","article-title":"Ionizing radiation-engineered nanogels as insulin nanocarriers for the development of a new strategy for the treatment of Alzheimer\u2019s disease","volume":"80","author":"Picone","year":"2016","journal-title":"Biomaterials"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.jconrel.2017.11.040","article-title":"Nose-to-brain delivery of insulin enhanced by a nanogel carrier","volume":"270","author":"Picone","year":"2018","journal-title":"J. Control. Release"},{"key":"ref_150","first-page":"147835","article-title":"Insulin promotes survival of amyloid-beta oligomers neuroblastoma damaged cells via caspase 9 inhibition and Hsp70 upregulation","volume":"2010","author":"Picone","year":"2010","journal-title":"J. Biomed. Biotechnol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1111\/acel.12498","article-title":"Intranasal insulin alleviates cognitive deficits and amyloid pathology in young adult APPswe\/PS1dE9 mice","volume":"15","author":"Mao","year":"2016","journal-title":"Aging Cell"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1210\/en.2012-1661","article-title":"Insulin has multiple antiamyloidogenic effects on human neuronal cells","volume":"154","author":"Pandini","year":"2013","journal-title":"Endocrinology"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1016\/j.psyneuen.2004.04.003","article-title":"Intranasal insulin improves memory in humans","volume":"29","author":"Benedict","year":"2009","journal-title":"Psyconeuroendocrinology"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1001\/archpsyc.56.12.1135","article-title":"Enhancement of memory in Alzheimer disease with insulin and somatostatin, but not glucose","volume":"56","author":"Craft","year":"1999","journal-title":"Arch. Gen. Psychiatry"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"897","DOI":"10.3233\/JAD-141791","article-title":"Long-acting intranasal insulin Detemir improves cognition for adults with mild cognitive impairment or early-stage Alzheimer\u2019s disease dementia","volume":"44","author":"Claxton","year":"2015","journal-title":"J. Alzheimers Dis."},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Nuzzo, D., and Picone, P. (2021). Multiple Sclerosis: Focus on extracellular and artificial vesicles, nanoparticles as potential therapeutic approaches. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22168866"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.ijpharm.2019.01.056","article-title":"Advances in nanocarriers enabled brain targeted drug delivery across blood brain barrier","volume":"559","author":"Sharma","year":"2019","journal-title":"Int. J. Pharm."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"100146","DOI":"10.1016\/j.mtbio.2021.100146","article-title":"Nano-structured myelin: New nanovesicles for targeted delivery to white matter and microglia, from brain-to-brain","volume":"12","author":"Picone","year":"2021","journal-title":"Mater. Today Bio."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/j.jconrel.2017.12.015","article-title":"Crossing the blood-brain barrier with nanoparticles","volume":"28","author":"Zhou","year":"2018","journal-title":"J. Contr. Release"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"1654","DOI":"10.1002\/jps.21924","article-title":"Intranasal delivery to the central nervous system: Mechanisms and experimental considerations","volume":"99","author":"Dhuria","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/j.addr.2011.11.002","article-title":"Intranasal delivery of biologics to the central nervous system","volume":"64","author":"Lochhead","year":"2012","journal-title":"Adv. Drug Deliv. Rev."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.neulet.2008.10.090","article-title":"Direct transport of VEGF from the nasal cavity to brain","volume":"449","author":"Yang","year":"2009","journal-title":"Neurosci. Lett."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"25","DOI":"10.2174\/187221108783331429","article-title":"Recent patents review on intranasal administration for CNS drug delivery","volume":"2","author":"Jogani","year":"2008","journal-title":"Recent Patents Drug Deliv. Formul."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.jconrel.2014.11.004","article-title":"Brain delivery of insulin boosted by intranasal coadministration with cell-penetrating peptides","volume":"197","author":"Kamei","year":"2015","journal-title":"J. Control. Release"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.2165\/00003088-200342130-00003","article-title":"Absorption enhancers for nasal drug delivery","volume":"42","author":"Illum","year":"2003","journal-title":"Clin. Pharmacokinet."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1002\/jps.2600760709","article-title":"Analysis of structural requirements for the absorption of drugs and macromolecules from the nasal cavity","volume":"76","author":"McMartin","year":"1987","journal-title":"J. Pharm. Sci."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1146\/annurev.bi.62.070193.002025","article-title":"Molecular chaperone functions of Heat-Shock Proteins","volume":"62","author":"Hendrick","year":"1993","journal-title":"Ann. Rev. Biochem."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"aac4354","DOI":"10.1126\/science.aac4354","article-title":"In Vivo aspects of protein folding and quality control","volume":"353","author":"Balchin","year":"2016","journal-title":"Science"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"2770","DOI":"10.1002\/1873-3468.13844","article-title":"Recent advances in understanding catalysis of protein folding by molecular chaperones","volume":"594","author":"Balchin","year":"2020","journal-title":"FEBS Lett."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1152\/physrev.1999.79.2.425","article-title":"Chaperone-mediated protein folding","volume":"79","author":"Fink","year":"1993","journal-title":"Physiol. Rev."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1038\/nrm3658","article-title":"Chaperone machines for protein folding, unfolding and disaggregation","volume":"14","author":"Saibil","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1379\/1466-1268(2003)008<0309:MFROHF>2.0.CO;2","article-title":"Mechanisms for regulating Hsp70 function by Hsp40","volume":"8","author":"Fan","year":"2003","journal-title":"Cell Stress Chaperon"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1007\/s00239-004-0013-z","article-title":"Evolutionary diversity of vertebrate small heat shock proteins","volume":"59","author":"Frank","year":"2004","journal-title":"J. Mol. Evol."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"2007","DOI":"10.1073\/pnas.0910126107","article-title":"Quaternary dynamics and plasticity underlie small heat shock protein chaperone function","volume":"107","author":"Stengel","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1083\/jcb.200104079","article-title":"Hsp90: A specialized but essential protein-folding tool","volume":"154","author":"Young","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/S0092-8674(00)80928-9","article-title":"The Hsp70 and Hsp60 chaperones machines","volume":"92","author":"Bukau","year":"1998","journal-title":"Cell"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.molcel.2018.01.004","article-title":"Cellular handling of protein aggregates by disaggregation machines","volume":"69","author":"Mogk","year":"2018","journal-title":"Mol. Cell."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/nrn1587","article-title":"Modulation of neurodegeneration by molecular chaperones","volume":"6","author":"Muchowski","year":"2005","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_179","doi-asserted-by":"crossref","unstructured":"(2012). Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. Proc. Natl. Acad. Sci. USA, 109, 12479\u201312484.","DOI":"10.1073\/pnas.1117799109"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1016\/j.ijbiomac.2019.02.148","article-title":"Molecular chaperones biochemistry and role in neurodegenerative diseases","volume":"131","author":"Chaari","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"581374","DOI":"10.3389\/fnagi.2020.581374","article-title":"Molecular chaperones: A double-edged sword in neurodegenerative diseases","volume":"12","author":"Tittelmeier","year":"2020","journal-title":"Front. Aging Neurosci."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.freeradbiomed.2021.11.015","article-title":"Mitochondrial chaperones in human health and disease","volume":"179","author":"Bahr","year":"2021","journal-title":"Free Rad. Biomed."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"9676","DOI":"10.1074\/jbc.RA120.013478","article-title":"Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding competent species","volume":"295","author":"Nachman","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"e13952","DOI":"10.15252\/emmm.202113952","article-title":"The Hsp40 chaperone Ydj1 drives amiloyd beta 42 toxicity","volume":"14","author":"Ring","year":"2022","journal-title":"EMBO Mol. Med."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"10948","DOI":"10.1038\/ncomms10948","article-title":"Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation","volume":"7","author":"Arosio","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1007\/s12035-007-0029-7","article-title":"Heat Shock proteins and amateur chaperones in amyloid accumulation and clearance in Alzheimer\u2019s Disease","volume":"35","author":"Wilhelmus","year":"2007","journal-title":"Mol. Neurobiol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"16006","DOI":"10.1073\/pnas.1516131112","article-title":"Exogenous Hsp70 delays senescence and improves cognitive function in aging mice","volume":"112","author":"Bobkova","year":"2015","journal-title":"PNAS"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.3389\/fphar.2019.01047","article-title":"Small heat shock proteins, big impact on protein aggregation in neurodegenerative disease","volume":"10","author":"Webster","year":"2019","journal-title":"Front. Pharmacol."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1007\/s12192-020-01101-4","article-title":"Small heat shock proteins in neurodegenerative diseases","volume":"25","author":"Vendredy","year":"2020","journal-title":"Cell Stress Chaperon"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"2474","DOI":"10.1016\/j.bbagen.2016.07.019","article-title":"Hsp60, amateur chaperon in amyloid-beta fibrillogenesis","volume":"1860","author":"Mangione","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"2858","DOI":"10.1021\/acschemneuro.9b00086","article-title":"Hsp60 protects against Amyloid \u03b2 oligomers synaptic toxicity via modification of toxic oligomer conformation","volume":"10","author":"Marino","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"435203","DOI":"10.1155\/2014\/435203","article-title":"Heat shock protein 70 in Alzheimer\u2019s disease","volume":"2014","author":"Lu","year":"2014","journal-title":"Biomed. Res. Int."},{"key":"ref_193","first-page":"33182","article-title":"Heat shock proteins 70 and 90 inhibit early stages of amyloid \u03b2-(1.42) aggregation in vitro","volume":"44","author":"Evans","year":"2006","journal-title":"J. Mol. Biol."},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Franco, A., Velasco-Carneros, L., Alvarez, N., Orozco, N., Moro, F., Prado, A., and Muga, A. (2021). Unzipping the secrets of amyloid disassembly by the human disaggregase. Cells, 10.","DOI":"10.3390\/cells10102745"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"5359","DOI":"10.1111\/febs.16441","article-title":"Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation","volume":"289","author":"Harari","year":"2022","journal-title":"FEBS J."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.jare.2021.05.007","article-title":"Molecular mechanism of amyloid disaggregation","volume":"36","author":"Low","year":"2022","journal-title":"J. Adv. Res."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"100567","DOI":"10.1016\/j.jbc.2021.100567","article-title":"Suppression of aggregate and amyloid formation by novel intrinsically disordered region in metazoan Hsp110 chaperones","volume":"296","author":"Yakubu","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"2687","DOI":"10.1074\/jbc.M117.803411","article-title":"HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation","volume":"293","author":"Baughman","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1002\/pro.4060","article-title":"Small heat shock protein 22 kDa can modulate the aggregation and liquid-liquid phase separation behavior of tau","volume":"7","author":"Darling","year":"2021","journal-title":"Protein Sci."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"e69601","DOI":"10.7554\/eLife.69601","article-title":"Hsp40s play complementary roles in the prevention of tau amyloid formation","volume":"10","author":"Irvin","year":"2021","journal-title":"eLife"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1021\/acschembio.7b01039","article-title":"Hsp70 inhibits the nucleation and elongation of tau and sequesters tau aggregates with high affinity","volume":"13","author":"Kundel","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"3029","DOI":"10.1016\/j.jmb.2018.05.026","article-title":"Dancing with the diva: Hsp90-client interactions","volume":"430","author":"Radli","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"4956","DOI":"10.1074\/jbc.RA118.005980","article-title":"Heat shock protein 104 (Hsp104) chaperones soluble Tau via a mechanism distinct from its disaggregase activity","volume":"294","author":"Zhang","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.neuroscience.2020.11.020","article-title":"Hsp90-interacting co-chaperones and their family proteins in Tau regulation: Introducing a novel role for Cdc37L1","volume":"453","author":"Peak","year":"2021","journal-title":"Neuroscience"},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1016\/j.neuron.2011.04.009","article-title":"The many faces of tau","volume":"70","author":"Morris","year":"2011","journal-title":"Neuron"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.tibs.2021.12.009","article-title":"Chaperoning shape-shifting tau in disease","volume":"47","author":"Ryder","year":"2022","journal-title":"Trends Biochim. Sci."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"10300","DOI":"10.1021\/bi2009147","article-title":"Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport","volume":"50","author":"Patterson","year":"2011","journal-title":"Biochemistry"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"eaax6999","DOI":"10.1126\/sciadv.aax6999","article-title":"The mechanism of Hsp90-induced oligomerizaton of Tau","volume":"6","author":"Weickert","year":"2020","journal-title":"Sci. Adv."},{"key":"ref_209","first-page":"319","article-title":"Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein","volume":"17","author":"Tortosa","year":"2009","journal-title":"J. Alz. Dis."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"4158","DOI":"10.1172\/JCI69003","article-title":"Accelerated neurodegeneration through chaperone-mediated oligomerization of tau","volume":"123","author":"Blair","year":"2013","journal-title":"J. Clin. Investig."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"9707","DOI":"10.1073\/pnas.1707039114","article-title":"Hsp90 activator Aha1 drives production of pathological tau aggregates","volume":"114","author":"Shelton","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1016\/S1474-4422(10)70119-8","article-title":"Alzheimer\u2019s disease: Clinical trials and drug development","volume":"9","author":"Mangialasche","year":"2010","journal-title":"Lancet Neurol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"1589","DOI":"10.1001\/jama.2019.4782","article-title":"Diagnosis and management of dementia: Review","volume":"322","author":"Arvanitakis","year":"2019","journal-title":"JAMA"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"797","DOI":"10.2147\/CIA.S325026","article-title":"Role of aducanumab in the treatment of Alzheimer\u2019s Disease: Challenges and opportunities","volume":"17","author":"Vaz","year":"2022","journal-title":"Clin. Interv. Aging"},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"e069780","DOI":"10.1136\/bmj-2021-069780","article-title":"Regulatory decisions diverge over aducanumab for Alzheimer\u2019s disease","volume":"376","author":"Lythgoe","year":"2022","journal-title":"BMJ"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/s40263-020-00781-x","article-title":"Intranasal insulin for Alzheimer\u2019s disease","volume":"35","author":"Hallschmid","year":"2021","journal-title":"CNS Drug"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/j.nbd.2009.03.007","article-title":"Oral apolipoprotein a-i mimetic peptide improves cognitive function and reduces amyloid burden in a mouse model of Alzheimer\u2019s disease","volume":"34","author":"Handattu","year":"2009","journal-title":"Neurobiol. Dis."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1038\/nrd2896","article-title":"Alzheimer\u2019s disease: Strategies for disease modification","volume":"9","author":"Citron","year":"2010","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1186\/s13195-021-00927-z","article-title":"The Alzheimer\u2019s disease drug development landscape","volume":"13","author":"Vermunt","year":"2021","journal-title":"Alzheimers Res. Ther."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/12\/10\/1344\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:37:09Z","timestamp":1760143029000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/12\/10\/1344"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9,22]]},"references-count":219,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2022,10]]}},"alternative-id":["biom12101344"],"URL":"https:\/\/doi.org\/10.3390\/biom12101344","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,9,22]]}}}