{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T21:29:36Z","timestamp":1790890176029,"version":"4.1.0"},"reference-count":152,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2021,8,31]],"date-time":"2021-08-31T00:00:00Z","timestamp":1630368000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012190","name":"Ministry of Science and Higher Education of the Russian Federation","doi-asserted-by":"publisher","award":["075-15-2020-926"],"award-info":[{"award-number":["075-15-2020-926"]}],"id":[{"id":"10.13039\/501100012190","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000066","name":"National Institute of Environmental Health Sciences","doi-asserted-by":"publisher","award":["R01ES07331 and R01ES10563"],"award-info":[{"award-number":["R01ES07331 and R01ES10563"]}],"id":[{"id":"10.13039\/100000066","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Kamprad Research Foundation, the Ulla-Carin Lindquist Foundation for ALS Research and the Karolinska Institutet IMM strategic grants","award":["n\/a"],"award-info":[{"award-number":["n\/a"]}]},{"DOI":"10.13039\/501100013398","name":"Sykehuset Innlandet HF","doi-asserted-by":"publisher","award":["n\/a"],"award-info":[{"award-number":["n\/a"]}],"id":[{"id":"10.13039\/501100013398","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The aim of the present review is to discuss traditional hypotheses on the etiopathogenesis of Alzheimer\u2019s disease (AD), as well as the role of metabolic-syndrome-related mechanisms in AD development with a special focus on advanced glycation end-products (AGEs) and their role in metal-induced neurodegeneration in AD. Persistent hyperglycemia along with oxidative stress results in increased protein glycation and formation of AGEs. The latter were shown to possess a wide spectrum of neurotoxic effects including increased A\u03b2 generation and aggregation. In addition, AGE binding to receptor for AGE (RAGE) induces a variety of pathways contributing to neuroinflammation. The existing data also demonstrate that AGE toxicity seems to mediate the involvement of copper (Cu) and potentially other metals in AD pathogenesis. Specifically, Cu promotes AGE formation, AGE-A\u03b2 cross-linking and up-regulation of RAGE expression. Moreover, A\u03b2 glycation was shown to increase prooxidant effects of Cu through Fenton chemistry. Given the role of AGE and RAGE, as well as metal toxicity in AD pathogenesis, it is proposed that metal chelation and\/or incretins may slow down oxidative damage. In addition, selenium (Se) compounds seem to attenuate the intracellular toxicity of the deranged tau and A\u03b2, as well as inhibiting AGE accumulation and metal-induced neurotoxicity.<\/jats:p>","DOI":"10.3390\/ijms22179461","type":"journal-article","created":{"date-parts":[[2021,8,31]],"date-time":"2021-08-31T08:42:32Z","timestamp":1630399352000},"page":"9461","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":53,"title":["Copper, Iron, Selenium and Lipo-Glycemic Dysmetabolism in Alzheimer\u2019s Disease"],"prefix":"10.3390","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7518-5703","authenticated-orcid":false,"given":"Jan","family":"Aaseth","sequence":"first","affiliation":[{"name":"Department of Research, Innlandet Hospital Trust, P.O. Box 104, N-2381 Brumunddal, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anatoly V.","family":"Skalny","sequence":"additional","affiliation":[{"name":"World-Class Research Center \u201cDigital Biodesign and Personalized Healthcare\u201d, IM Sechenov First Moscow State Medical University (Sechenov University), Bolshaya Pirogovskaya St., 2\u20134, 119146 Moscow, Russia"},{"name":"Department of Bioelementology, K.G. Razumovsky Moscow State University of Technologies and Management, Zemlyanoi Val St., 73, 109004 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Per M.","family":"Roos","sequence":"additional","affiliation":[{"name":"Institute of Environmental Medicine, Karolinska Institute, 171 77 Stockholm, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6381-5720","authenticated-orcid":false,"given":"Jan","family":"Alexander","sequence":"additional","affiliation":[{"name":"Norwegian Institute of Public Health, P.O. Box 222 Sk\u00f8yen, 0213 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2619-1656","authenticated-orcid":false,"given":"Michael","family":"Aschner","sequence":"additional","affiliation":[{"name":"Department of Molecular Pharmacology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA"},{"name":"Laboratory of Molecular Dietetics, IM Sechenov First Moscow State Medical University (Sechenov University), Bolshaya Pirogovskaya St., 2\u20134, 119146 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexey A.","family":"Tinkov","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Dietetics, IM Sechenov First Moscow State Medical University (Sechenov University), Bolshaya Pirogovskaya St., 2\u20134, 119146 Moscow, Russia"},{"name":"Laboratory of Ecobiomonitoring and Quality Control, Yaroslavl State University, Sovetskaya Str. 14, 150000 Yaroslavl, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,8,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Alzheimer\u2019s Association (2021). 2021 Alzheimers disease facts and figures. Alzheimers Dement., 17, 327\u2013406.","DOI":"10.1002\/alz.12328"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.cell.2019.09.001","article-title":"Alzheimer Disease: An Update on Pathobiology and Treatment Strategies","volume":"179","author":"Long","year":"2019","journal-title":"Cell"},{"key":"ref_3","first-page":"321","article-title":"Association of apolipoprotein E epsilon 4 allele with sporadic late onset Alzheimer\u2019s disease. A meta-analysis","volume":"17","author":"Talebi","year":"2012","journal-title":"Neurosciences"},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Jacobs, E.G., Kroenke, C., Lin, J., Epel, E.S., Kenna, H.A., Blackburn, E.H., and Rasgon, N.L. (2013). Accelerated cell aging in female APOE-epsilon4 carriers: Implications for hormone therapy use. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0054713"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.neuron.2007.08.008","article-title":"Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1","volume":"56","author":"Liu","year":"2007","journal-title":"Neuron"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"652099","DOI":"10.3389\/fnins.2021.652099","article-title":"The Neurobiology of Selenium: Looking Back and to the Future","volume":"15","author":"Schweizer","year":"2021","journal-title":"Front. Neurosci"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"16","DOI":"10.2174\/187152709787601867","article-title":"Clearance of amyloid-beta peptide across the blood-brain barrier: Implication for therapies in Alzheimer\u2019s disease","volume":"8","author":"Deane","year":"2009","journal-title":"CNS Neurol. Disord. Drug Targets"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1159\/000337231","article-title":"A multifaceted role for apoE in the clearance of beta-amyloid across the blood-brain barrier","volume":"11","author":"Bachmeier","year":"2013","journal-title":"Neurodegener. Dis."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1016\/j.jalz.2013.11.003","article-title":"The amyloid hypothesis, time to move on: Amyloid is the downstream result, not cause, of Alzheimer\u2019s disease","volume":"10","author":"Drachman","year":"2014","journal-title":"Alzheimers Dement."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"445","DOI":"10.31887\/DCNS.2013.15.4\/hjahn","article-title":"Memory loss in Alzheimer\u2019s disease","volume":"15","author":"Jahn","year":"2013","journal-title":"Dialogues Clin. Neurosci."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.neulet.2012.03.072","article-title":"Relationships between hippocampal shape and cognitive performances in drug-naive patients with Alzheimer\u2019s disease","volume":"516","author":"Lim","year":"2012","journal-title":"Neurosci. Lett."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1159\/000381511","article-title":"Hypothesis of Endogenous Anticholinergic Activity in Alzheimer\u2019s Disease","volume":"15","author":"Konishi","year":"2015","journal-title":"Neurodegener. Dis."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1016\/j.bcp.2013.04.001","article-title":"Importance of the nicotinic acetylcholine receptor system in the prefrontal cortex","volume":"85","author":"Wallace","year":"2013","journal-title":"Biochem. Pharm."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/j.neuropharm.2007.07.013","article-title":"Memantine: A NMDA receptor antagonist that improves memory by restoration of homeostasis in the glutamatergic system\u2014Too little activation is bad, too much is even worse","volume":"53","author":"Parsons","year":"2007","journal-title":"Neuropharmacology"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1007\/s10571-020-00796-4","article-title":"Caveolin: A New Link Between Diabetes and AD","volume":"40","author":"Surguchov","year":"2020","journal-title":"Cell Mol. Neurobiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1016\/j.bbadis.2016.04.017","article-title":"Common neurodegenerative pathways in obesity, diabetes, and Alzheimer\u2019s disease","volume":"1863","author":"Pugazhenthi","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"e21990","DOI":"10.1002\/syn.21990","article-title":"Alzheimer\u2019s disease and metabolic syndrome: A link from oxidative stress and inflammation to neurodegeneration","volume":"71","author":"Trevino","year":"2017","journal-title":"Synapse"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.lfs.2016.02.002","article-title":"Oxidative stress and metabolic disorders: Pathogenesis and therapeutic strategies","volume":"148","author":"Rani","year":"2016","journal-title":"Life Sci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1093\/jn\/134.5.1003","article-title":"Intracellular copper transport in mammals","volume":"134","author":"Prohaska","year":"2004","journal-title":"J. Nutr."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/nrn.2017.29","article-title":"Not just amyloid: Physiological functions of the amyloid precursor protein family","volume":"18","author":"Muller","year":"2017","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"30","DOI":"10.3389\/fnmol.2017.00030","article-title":"Therapeutic Potential of Secreted Amyloid Precursor Protein APPsalpha","volume":"10","author":"Mockett","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1038\/cr.2011.116","article-title":"APP physiological and pathophysiological functions: Insights from animal models","volume":"22","author":"Guo","year":"2012","journal-title":"Cell Res."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Richter, M.C., Ludewig, S., Winschel, A., Abel, T., Bold, C., Salzburger, L.R., Klein, S., Han, K., Weyer, S.W., and Fritz, A.K. (2018). Distinct in vivo roles of secreted APP ectodomain variants APPsalpha and APPsbeta in regulation of spine density, synaptic plasticity, and cognition. EMBO J., 37.","DOI":"10.15252\/embj.201798335"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1007\/s12603-019-1162-5","article-title":"Editorial: What is the Physiological Function of Amyloid-Beta Protein?","volume":"23","author":"Morley","year":"2019","journal-title":"J. Nutr. Health Aging"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1007\/s00401-020-02196-w","article-title":"The physiological roles of tau and Abeta: Implications for Alzheimer\u2019s disease pathology and therapeutics","volume":"140","author":"Kent","year":"2020","journal-title":"Acta Neuropathol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3905","DOI":"10.1111\/j.1742-4658.2011.08228.x","article-title":"Membrane and surface interactions of Alzheimer\u2019s Abeta peptide\u2014Insights into the mechanism of cytotoxicity","volume":"278","author":"Williams","year":"2011","journal-title":"FEBS J."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1692","DOI":"10.1002\/cbic.201300262","article-title":"Biophysical studies of the amyloid beta-peptide: Interactions with metal ions and small molecules","volume":"14","author":"Warmlander","year":"2013","journal-title":"ChemBioChem"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1553","DOI":"10.1212\/01.WNL.0000159740.16984.3C","article-title":"Clinical effects of Abeta immunization (AN1792) in patients with AD in an interrupted trial","volume":"64","author":"Gilman","year":"2005","journal-title":"Neurology"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1586\/1744666X.2014.883921","article-title":"Amyloid-based immunotherapy for Alzheimer\u2019s disease in the time of prevention trials: The way forward","volume":"10","author":"Panza","year":"2014","journal-title":"Expert Rev. Clin. Immunol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/j.trci.2017.04.005","article-title":"Phase II clinical trials of anti-amyloid beta antibodies: When is enough, enough?","volume":"3","author":"Gold","year":"2017","journal-title":"Alzheimers Dement. N. Y."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"491","DOI":"10.2174\/1570159X11311050004","article-title":"Pyroglutamate-Modified Amyloid Beta Peptides: Emerging Targets for Alzheimer\u2019s Disease Immunotherapy","volume":"11","author":"Gevorkian","year":"2013","journal-title":"Curr. Neuropharmacol."},{"key":"ref_32","first-page":"122","article-title":"Biological Basis for Amyloidogenesis in Alzheimer\u2019s Disease","volume":"82","author":"Andreeva","year":"2017","journal-title":"Biochemistry"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"18367","DOI":"10.1073\/pnas.0907652106","article-title":"Alzheimer\u2019s disease-like pathological features in transgenic mice expressing the APP intracellular domain","volume":"106","author":"Ghosal","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1111\/j.1742-4658.2010.07568.x","article-title":"Amyloid oligomers: Formation and toxicity of Abeta oligomers","volume":"277","author":"Sakono","year":"2010","journal-title":"FEBS J."},{"key":"ref_35","unstructured":"Alsunusi, S., Kumosani, T.A., Glabe, C.G., Huwait, E.A., and Moselhy, S.S. (2020). In vitro study of the mechanism of intraneuronal beta-amyloid aggregation in Alzheimer\u2019s disease. Arch. Physiol. Biochem., 1\u20138."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.freeradbiomed.2011.03.031","article-title":"Ubiquitin-proteasome pathway and cellular responses to oxidative stress","volume":"51","author":"Shang","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1002\/iub.1271","article-title":"Slipping up: Partial substrate degradation by ATP-dependent proteases","volume":"66","author":"Nassif","year":"2014","journal-title":"IUBMB Life"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"38","DOI":"10.2174\/138920291501140306113344","article-title":"The Mechanistic Links Between Proteasome Activity, Aging and Age-related Diseases","volume":"15","author":"Saez","year":"2014","journal-title":"Curr. Genom."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1046\/j.1471-4159.2003.01642.x","article-title":"Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer\u2019s disease","volume":"85","author":"Keck","year":"2003","journal-title":"J. Neurochem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"3622","DOI":"10.1073\/pnas.0709180105","article-title":"Akt and CHIP coregulate tau degradation through coordinated interactions","volume":"105","author":"Dickey","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1016\/j.neurobiolaging.2007.04.014","article-title":"Abeta inhibits the proteasome and enhances amyloid and tau accumulation","volume":"29","author":"Tseng","year":"2008","journal-title":"Neurobiol. Aging"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"7032","DOI":"10.1007\/s12035-019-1563-9","article-title":"Molecular Targets in Alzheimer\u2019s Disease","volume":"56","author":"Bjorklund","year":"2019","journal-title":"Mol. Neurobiol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1089\/ars.2014.6062","article-title":"Protein Oxidation in Aging: Does It Play a Role in Aging Progression?","volume":"23","author":"Reeg","year":"2015","journal-title":"Antioxid. Redox Signal."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1007\/s10534-016-9959-8","article-title":"Treatment strategies in Alzheimer\u2019s disease: A review with focus on selenium supplementation","volume":"29","author":"Aaseth","year":"2016","journal-title":"Biometals"},{"key":"ref_45","first-page":"517","article-title":"Mitochondrial ROS Metabolism: 10 Years Later","volume":"80","author":"Andreyev","year":"2015","journal-title":"Biochemistry"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1093\/jnen\/64.2.113","article-title":"Extensive involvement of autophagy in Alzheimer disease: An immuno-electron microscopy study","volume":"64","author":"Nixon","year":"2005","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.celrep.2013.08.042","article-title":"Abeta secretion and plaque formation depend on autophagy","volume":"5","author":"Nilsson","year":"2013","journal-title":"Cell Rep."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Leal, N.S., and Martins, L.M. (2021). Mind the Gap: Mitochondria and the Endoplasmic Reticulum in Neurodegenerative Diseases. Biomedicines, 9.","DOI":"10.3390\/biomedicines9020227"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1080\/15548627.2019.1596497","article-title":"Mitophagy and NAD+ inhibit Alzheimer disease","volume":"15","author":"Fang","year":"2019","journal-title":"Autophagy"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.pneurobio.2008.03.002","article-title":"Microtubule-associated protein tau in development, degeneration and protection of neurons","volume":"85","author":"Wang","year":"2008","journal-title":"Prog. Neurobiol."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Aaseth, J., Buha, A., Wallace, D.R., and Bjorklund, G. (2020). Xenobiotics, Trace Metals and Genetics in the Pathogenesis of Tauopathies. Int. J. Environ. Res. Public Health, 17.","DOI":"10.3390\/ijerph17041269"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1016\/j.arcmed.2012.10.015","article-title":"Deregulated Cdk5 activity is involved in inducing Alzheimer\u2019s disease","volume":"43","author":"Shukla","year":"2012","journal-title":"Arch. Med. Res."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"527","DOI":"10.2174\/1381612822666151124235028","article-title":"Neuroprotective Mechanisms Mediated by CDK5 Inhibition","volume":"22","author":"Mushtaq","year":"2016","journal-title":"Curr. Pharm. Des."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/s41582-018-0070-3","article-title":"Lifestyle interventions to prevent cognitive impairment, dementia and Alzheimer disease","volume":"14","author":"Kivipelto","year":"2018","journal-title":"Nat. Rev. Neurol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1152\/physrev.00001.2019","article-title":"Methylglyoxal, a Highly Reactive Dicarbonyl Compound, in Diabetes, Its Vascular Complications, and Other Age-Related Diseases","volume":"100","author":"Schalkwijk","year":"2020","journal-title":"Physiol. Rev."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.3233\/JAD-180903","article-title":"Present Algorithms and Future Treatments for Alzheimer\u2019s Disease","volume":"67","author":"Grossberg","year":"2019","journal-title":"J. Alzheimers Dis."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1001\/jama.1997.03550160069041","article-title":"Effects of age, sex, and ethnicity on the association between apolipoprotein E genotype and Alzheimer disease. A meta-analysis. APOE and Alzheimer Disease Meta Analysis Consortium","volume":"278","author":"Farrer","year":"1997","journal-title":"JAMA"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.cmet.2018.08.014","article-title":"The Role of Advanced Glycation End Products in Aging and Metabolic Diseases: Bridging Association and Causality","volume":"28","author":"Chaudhuri","year":"2018","journal-title":"Cell Metab."},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Brings, S., Fleming, T., Freichel, M., Muckenthaler, M.U., Herzig, S., and Nawroth, P.P. (2017). Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18050984"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/s12276-021-00561-7","article-title":"Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury","volume":"53","author":"Rungratanawanich","year":"2021","journal-title":"Exp. Mol. Med."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"108886","DOI":"10.1016\/j.abb.2021.108886","article-title":"Detecting beta-amyloid glycation by intrinsic fluorescence\u2014Understanding the link between diabetes and Alzheimer\u2019s disease","volume":"704","author":"Alghamdi","year":"2021","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"e673","DOI":"10.1038\/cddis.2013.180","article-title":"Glycation exacerbates the neuronal toxicity of beta-amyloid","volume":"4","author":"Li","year":"2013","journal-title":"Cell Death Dis."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/j.freeradbiomed.2010.05.005","article-title":"Advanced glycation end products enhance amyloid precursor protein expression by inducing reactive oxygen species","volume":"49","author":"Ko","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"63","DOI":"10.3233\/JAD-2012-112114","article-title":"Amyloid-beta metabolite sensing: Biochemical linking of glycation modification and misfolding","volume":"30","author":"Fawver","year":"2012","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1021\/acschemneuro.7b00410","article-title":"Advanced Glycation End Products Modulate Amyloidogenic APP Processing and Tau Phosphorylation: A Mechanistic Link between Glycation and the Development of Alzheimer\u2019s Disease","volume":"9","author":"Batkulwar","year":"2018","journal-title":"ACS Chem. Neurosci."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"224","DOI":"10.5808\/GI.2013.11.4.224","article-title":"Receptor for Advanced Glycation Endproducts (RAGE), Its Ligands, and Soluble RAGE: Potential Biomarkers for Diagnosis and Therapeutic Targets for Human Renal Diseases","volume":"11","author":"Lee","year":"2013","journal-title":"Genom. Inf."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1007\/s10571-015-0233-3","article-title":"Role of RAGE in Alzheimer\u2019s Disease","volume":"36","author":"Cai","year":"2016","journal-title":"Cell Mol. Neurobiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"75","DOI":"10.3109\/00207454.2013.825258","article-title":"The potential mechanisms of Abeta-receptor for advanced glycation end-products interaction disrupting tight junctions of the blood-brain barrier in Alzheimer\u2019s disease","volume":"124","author":"Wan","year":"2014","journal-title":"Int. J. Neurosci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.neuropharm.2017.12.026","article-title":"Targeted inhibition of RAGE reduces amyloid-beta influx across the blood-brain barrier and improves cognitive deficits in db\/db mice","volume":"131","author":"Wang","year":"2018","journal-title":"Neuropharmacology"},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Zeng, F., Liu, Y., Huang, W., Qing, H., Kadowaki, T., Kashiwazaki, H., Ni, J., and Wu, Z. (2020). Receptor for advanced glycation end products up-regulation in cerebral endothelial cells mediates cerebrovascular-related amyloid beta accumulation after Porphyromonas gingivalis infection. J. Neurochem.","DOI":"10.1111\/jnc.15096"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"e047199","DOI":"10.1002\/alz.047199","article-title":"Receptor for advanced glycation end products mediates meningitis-triggered amyloid-\u03b2 accumulation and cognitive impairment","volume":"16","author":"Barichello","year":"2020","journal-title":"Alzheimers Dement."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.neubiorev.2015.12.006","article-title":"RAGE axis in neuroinflammation, neurodegeneration and its emerging role in the pathogenesis of amyotrophic lateral sclerosis","volume":"62","author":"Ray","year":"2016","journal-title":"Neurosci. Biobehav. Rev."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1615","DOI":"10.2174\/1871527313666140806144831","article-title":"Receptor for AGEs (RAGE) as mediator of NF-kB pathway activation in neuroinflammation and oxidative stress","volume":"13","author":"Cuevas","year":"2014","journal-title":"CNS Neurol. Disord. Drug Targets"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1097\/00002093-200307000-00005","article-title":"Copper, zinc, and the metallobiology of Alzheimer disease","volume":"17","author":"Bush","year":"2003","journal-title":"Alzheimer Dis. Assoc. Disord."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.jtemb.2014.12.012","article-title":"Neurodegenerative diseases and therapeutic strategies using iron chelators","volume":"31","author":"Ward","year":"2015","journal-title":"J. Trace Elem. Med. Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1159\/000330467","article-title":"Ceruloplasmin and iron proteins in the serum of patients with Alzheimer\u2019s disease","volume":"1","author":"Torsdottir","year":"2011","journal-title":"Dement. Geriatr. Cogn. Dis. Extra"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.jtemb.2017.11.005","article-title":"Copper dyshomeostasis in Wilson disease and Alzheimer\u2019s disease as shown by serum and urine copper indicators","volume":"45","author":"Squitti","year":"2018","journal-title":"J. Trace Elem. Med. Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/B978-0-12-410502-7.00007-7","article-title":"Aceruloplasminemia: An update","volume":"110","author":"Kono","year":"2013","journal-title":"Int. Rev. Neurobiol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1007\/s00775-017-1497-5","article-title":"Glycation of Lys-16 and Arg-5 in amyloid-beta and the presence of Cu2+ play a major role in the oxidative stress mechanism of Alzheimer\u2019s disease","volume":"22","author":"Shuster","year":"2017","journal-title":"J. Biol. Inorg. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"11065","DOI":"10.1073\/pnas.1832769100","article-title":"Trace amounts of copper in water induce beta-amyloid plaques and learning deficits in a rabbit model of Alzheimer\u2019s disease","volume":"100","author":"Sparks","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1001\/archneur.63.8.1085","article-title":"Dietary copper and high saturated and trans fat intakes associated with cognitive decline","volume":"63","author":"Morris","year":"2006","journal-title":"Arch. Neurol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1002\/ana.24136","article-title":"Value of serum nonceruloplasmin copper for prediction of mild cognitive impairment conversion to Alzheimer disease","volume":"75","author":"Squitti","year":"2014","journal-title":"Ann. Neurol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.jocn.2006.07.017","article-title":"Wilson\u2019s disease: A clinico-neuropathological autopsy study","volume":"15","author":"Mahadevan","year":"2008","journal-title":"J. Clin. Neurosci."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1053\/j.gastro.2008.04.007","article-title":"Copper availability contributes to iron perturbations in human nonalcoholic fatty liver disease","volume":"135","author":"Aigner","year":"2008","journal-title":"Gastroenterology"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"6760","DOI":"10.1038\/ncomms7760","article-title":"Ferritin levels in the cerebrospinal fluid predict Alzheimer\u2019s disease outcomes and are regulated by APOE","volume":"6","author":"Ayton","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1001\/jamaneurol.2016.4406","article-title":"Association of Cerebrospinal Fluid Ferritin Level with Preclinical Cognitive Decline in APOE-epsilon4 Carriers","volume":"74","author":"Ayton","year":"2017","journal-title":"JAMA Neurol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.jinorgbio.2019.02.007","article-title":"Interaction of metal ions with tau protein. The case for a metal-mediated tau aggregation","volume":"194","author":"Ahmadi","year":"2019","journal-title":"J. Inorg. Biochem."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"129","DOI":"10.3233\/BSI-130041","article-title":"Elevated copper in the amyloid plaques and iron in the cortex are observed in mouse models of Alzheimer\u2019s disease that exhibit neurodegeneration","volume":"2","author":"Bourassa","year":"2013","journal-title":"Biomed. Spectrosc. Imaging"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/j.freeradbiomed.2018.09.033","article-title":"Striking while the iron is hot: Iron metabolism and ferroptosis in neurodegeneration","volume":"133","author":"Masaldan","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1006\/bbrc.1998.9326","article-title":"Transition metals bind to glycated proteins forming redox active \u201cglycochelates\u201d: Implications for the pathogenesis of certain diabetic complications","volume":"250","author":"Qian","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.mrgentox.2017.10.005","article-title":"Generation of Advanced Glycation End-Products (AGEs) by glycoxidation mediated by copper and ROS in a human serum albumin (HSA) model peptide: Reaction mechanism and damage in motor neuron cells","volume":"824","author":"Marques","year":"2017","journal-title":"Mutat. Res."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.ccr.2018.05.020","article-title":"Copper imbalance in Alzheimer\u2019s disease: Overview of the exchangeable copper component in plasma and the intriguing role albumin plays","volume":"371","author":"Siotto","year":"2018","journal-title":"Coord. Chem. Rev."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"4171","DOI":"10.1046\/j.1432-1327.2000.01452.x","article-title":"Transition metal-mediated glycoxidation accelerates cross-linking of beta-amyloid peptide","volume":"267","author":"Loske","year":"2000","journal-title":"Eur J. Biochem."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1039\/C4MT00323C","article-title":"Small angle X-ray scattering analysis of Cu2+-induced oligomers of the Alzheimer\u2019s amyloid beta peptide","volume":"7","author":"Ryan","year":"2015","journal-title":"Metallomics"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1515\/CCLM.2011.079","article-title":"Advanced glycation endproducts as gerontotoxins and biomarkers for carbonyl-based degenerative processes in Alzheimer\u2019s disease","volume":"49","author":"Rahmadi","year":"2011","journal-title":"Clin. Chem. Lab. Med."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.abb.2007.08.035","article-title":"Fe2+-catalyzed non-enzymatic glycosylation alters collagen conformation during AGE-collagen formation in vitro","volume":"468","author":"Xiao","year":"2007","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1007\/s00277-017-3223-3","article-title":"Increased levels of advanced glycation end products positively correlate with iron overload and oxidative stress markers in patients with beta-thalassemia major","volume":"97","author":"Mirlohi","year":"2018","journal-title":"Ann. Hematol."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Chen, S.H., Yuan, K.C., Lee, Y.C., Shih, C.K., Tseng, S.H., Tinkov, A.A., Skalny, A.V., and Chang, J.S. (2020). Iron and Advanced Glycation End Products: Emerging Role of Iron in Androgen Deficiency in Obesity. Antioxidants, 9.","DOI":"10.3390\/antiox9030261"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.cbi.2014.06.012","article-title":"Immunogenicity of DNA-advanced glycation end product fashioned through glyoxal and arginine in the presence of Fe3+: Its potential role in prompt recognition of diabetes mellitus auto-antibodies","volume":"219","author":"Shahab","year":"2014","journal-title":"Chem. Biol. Interact."},{"key":"ref_100","first-page":"277","article-title":"Antidiabetic drugs and their potential role in treating mild cognitive impairment and Alzheimer\u2019s disease","volume":"16","author":"Alagiakrishnan","year":"2013","journal-title":"Discov. Med."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.pnpbp.2017.06.002","article-title":"Effects of metformin exposure on neurodegenerative diseases in elderly patients with type 2 diabetes mellitus","volume":"79","author":"Kuan","year":"2017","journal-title":"Prog. Neuropsychopharmacol. Biol. Psychiatry"},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Feinkohl, I., Janke, J., Hadzidiakos, D., Slooter, A., Winterer, G., Spies, C., and Pischon, T. (2019). Associations of the metabolic syndrome and its components with cognitive impairment in older adults. BMC Geriatr., 19.","DOI":"10.1186\/s12877-019-1073-7"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1001\/jamaneurol.2014.2013","article-title":"Is apolipoprotein e required for cognitive function in humans? Implications for Alzheimer drug development","volume":"71","author":"Herz","year":"2014","journal-title":"JAMA Neurol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1111\/jgs.16342","article-title":"Benefits and Harms of Statins in People with Dementia: A Systematic Review and Meta-Analysis","volume":"68","author":"Davis","year":"2020","journal-title":"J. Am. Geriatr. Soc."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.2174\/1567205013666160401114751","article-title":"Glucagon-Like Peptide-1-Mediated Modulation of Inflammatory Pathways in the Diabetic Brain: Relevance to Alzheimer\u2019s Disease","volume":"13","author":"Qin","year":"2016","journal-title":"Curr. Alzheimer Res."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Wicinski, M., Socha, M., Malinowski, B., Wodkiewicz, E., Walczak, M., Gorski, K., Slupski, M., and Pawlak-Osinska, K. (2019). Liraglutide and its Neuroprotective Properties-Focus on Possible Biochemical Mechanisms in Alzheimer\u2019s Disease and Cerebral Ischemic Events. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20051050"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.bbr.2018.08.006","article-title":"Neural correlates of liraglutide effects in persons at risk for Alzheimer\u2019s disease","volume":"356","author":"Watson","year":"2019","journal-title":"Behav. Brain Res."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1498","DOI":"10.1111\/dom.13672","article-title":"Routine clinical use of liraglutide 3 mg for the treatment of obesity: Outcomes in non-surgical and bariatric surgery patients","volume":"21","author":"Suliman","year":"2019","journal-title":"Diabetes Obes. Metab."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.nut.2015.08.017","article-title":"Beneficial action of resveratrol: How and why?","volume":"32","author":"Repossi","year":"2016","journal-title":"Nutrition"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"2197","DOI":"10.1021\/jm400658e","article-title":"Dipeptidyl peptidase IV and its inhibitors: Therapeutics for type 2 diabetes and what else?","volume":"57","year":"2014","journal-title":"J. Med. Chem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.neuint.2018.01.005","article-title":"Dipeptidyl peptidase IV, which probably plays important roles in Alzheimer disease (AD) pathology, is upregulated in AD brain neurons and associates with amyloid plaques","volume":"114","author":"Bernstein","year":"2018","journal-title":"Neurochem. Int."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.exger.2009.12.004","article-title":"Long-term inhibition of dipeptidyl peptidase-4 in Alzheimer\u2019s prone mice","volume":"45","author":"Marfella","year":"2010","journal-title":"Exp. Gerontol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1097\/00007691-199312000-00027","article-title":"Desferrioxamine and Alzheimer\u2019s disease: Video home behavior assessment of clinical course and measures of brain aluminum","volume":"15","author":"McLachlan","year":"1993","journal-title":"Ther. Drug Monit."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.3233\/JAD-209009","article-title":"The Iron Chelator Deferiprone Improves the Phenotype in a Mouse Model of Tauopathy","volume":"78","author":"Rao","year":"2020","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"101271","DOI":"10.1016\/j.arr.2021.101271","article-title":"The pleiotropic neuroprotective effects of resveratrol in cognitive decline and Alzheimer\u2019s disease pathology: From antioxidant to epigenetic therapy","volume":"67","author":"Izquierdo","year":"2021","journal-title":"Ageing Res. Rev."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.ifset.2009.07.002","article-title":"Antioxidant properties of resveratrol: A structure-activity insight","volume":"11","year":"2010","journal-title":"Innov. Food Sci. Emerg. Technol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1016\/S0197-4580(02)00120-3","article-title":"Metal complexing agents as therapies for Alzheimer\u2019s disease","volume":"23","author":"Bush","year":"2002","journal-title":"Neurobiol. Aging"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"509","DOI":"10.3233\/JAD-2010-1390","article-title":"PBT2 rapidly improves cognition in Alzheimer\u2019s Disease: Additional phase II analyses","volume":"20","author":"Faux","year":"2010","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.phrs.2004.08.003","article-title":"Neuropsychiatric reactions to drugs: An analysis of spontaneous reports from general practitioners in Italy","volume":"51","author":"Galatti","year":"2005","journal-title":"Pharm. Res."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1016\/j.bbagen.2009.03.026","article-title":"Selenoprotein P-expression, functions, and roles in mammals","volume":"1790","author":"Burk","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.brainresrev.2004.03.004","article-title":"Selenium and brain function: A poorly recognized liaison","volume":"45","author":"Schweizer","year":"2004","journal-title":"Brain Res. Brain Res. Rev."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.freeradbiomed.2011.03.017","article-title":"A study of the relative importance of the peroxiredoxin-, catalase-, and glutathione-dependent systems in neural peroxide metabolism","volume":"51","author":"Mitozo","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.abb.2013.02.021","article-title":"Selenium homeostasis and antioxidant selenoproteins in brain: Implications for disorders in the central nervous system","volume":"536","author":"Steinbrenner","year":"2013","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1093\/jn\/137.3.690","article-title":"All regions of mouse brain are dependent on selenoprotein P for maintenance of selenium","volume":"137","author":"Nakayama","year":"2007","journal-title":"J. Nutr."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.brainres.2011.04.046","article-title":"Progression of neurodegeneration and morphologic changes in the brains of juvenile mice with selenoprotein P deleted","volume":"1398","author":"Caito","year":"2011","journal-title":"Brain Res."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.1002\/mds.23218","article-title":"Plasma selenium is positively related to performance in neurological tasks assessing coordination and motor speed","volume":"25","author":"Shahar","year":"2010","journal-title":"Mov. Disord."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1111\/j.1532-5415.2000.tb02603.x","article-title":"Cognitive decline is associated with systemic oxidative stress: The EVA study. Etude du Vieillissement Arteriel","volume":"48","author":"Berr","year":"2000","journal-title":"J. Am. Geriatr. Soc."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1007\/s10534-014-9728-5","article-title":"Homeostasis of metals in the progression of Alzheimer\u2019s disease","volume":"27","year":"2014","journal-title":"Biometals"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1039\/c5mt00075k","article-title":"Selenium, selenoproteins and neurodegenerative diseases","volume":"7","author":"Cardoso","year":"2015","journal-title":"Metallomics"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1001\/jamaneurol.2016.5778","article-title":"Association of Antioxidant Supplement Use and Dementia in the Prevention of Alzheimer\u2019s Disease by Vitamin E and Selenium Trial (PREADViSE)","volume":"74","author":"Kryscio","year":"2017","journal-title":"JAMA Neurol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1007\/s12011-018-1492-x","article-title":"Brain Selenium in Alzheimer\u2019s Disease (BRAIN SEAD Study): A Systematic Review and Meta-Analysis","volume":"189","author":"Varikasuvu","year":"2019","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"126541","DOI":"10.1016\/j.jtemb.2020.126541","article-title":"Supplemental selenium and coenzyme Q10 reduce glycation along with cardiovascular mortality in an elderly population with low selenium status\u2014A four-year, prospective, randomised, double-blind placebo-controlled trial","volume":"61","author":"Alehagen","year":"2020","journal-title":"J. Trace Elem. Med. Biol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1186\/s12950-019-0210-6","article-title":"Decrease in inflammatory biomarker concentration by intervention with selenium and coenzyme Q10: A subanalysis of osteopontin, osteoprotergerin, TNFr1, TNFr2 and TWEAK","volume":"16","author":"Alehagen","year":"2019","journal-title":"J. Inflamm."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/j.neulet.2009.12.035","article-title":"Selenium attenuates A beta production and A beta-induced neuronal death","volume":"469","author":"Gwon","year":"2010","journal-title":"Neurosci. Lett."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1039\/C8MT00041G","article-title":"Selenium-enriched yeast inhibited beta-amyloid production and modulated autophagy in a triple transgenic mouse model of Alzheimer\u2019s disease","volume":"10","author":"Song","year":"2018","journal-title":"Metallomics"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"6485","DOI":"10.1007\/s00216-020-02644-2","article-title":"Ability of selenium species to inhibit metal-induced Abeta aggregation involved in the development of Alzheimer\u2019s disease","volume":"412","author":"Madrid","year":"2020","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1007\/s12011-017-1162-4","article-title":"Selenium and Zinc against Abeta25-35-Induced Cytotoxicity and Tau Phosphorylation in PC12 Cells and Inhibits gamma-cleavage of APP","volume":"184","author":"Li","year":"2018","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1007\/s13311-018-0662-z","article-title":"Supranutritional Sodium Selenate Supplementation Delivers Selenium to the Central Nervous System: Results from a Randomized Controlled Pilot Trial in Alzheimer\u2019s Disease","volume":"16","author":"Cardoso","year":"2019","journal-title":"Neurotherapeutics"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1016\/j.neuropharm.2016.05.001","article-title":"Sodium selenate, a protein phosphatase 2A activator, mitigates hyperphosphorylated tau and improves repeated mild traumatic brain injury outcomes","volume":"108","author":"Tan","year":"2016","journal-title":"Neuropharmacology"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1007\/BF02916538","article-title":"Vitamin E and selenium supplementation in geriatric patients: A double-blind preliminary clinical trial","volume":"7","author":"Tolonen","year":"1985","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"4970","DOI":"10.1021\/acs.jafc.7b01465","article-title":"Long-Term Dietary Supplementation with Selenium-Enriched Yeast Improves Cognitive Impairment, Reverses Synaptic Deficits, and Mitigates Tau Pathology in a Triple Transgenic Mouse Model of Alzheimer\u2019s Disease","volume":"65","author":"Zhang","year":"2017","journal-title":"J. Agric. Food Chem."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"13888","DOI":"10.1073\/pnas.1009038107","article-title":"Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer\u2019s disease models","volume":"107","author":"Ke","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1007\/s00775-017-1463-2","article-title":"Ebselen ameliorates beta-amyloid pathology, tau pathology, and cognitive impairment in triple-transgenic Alzheimer\u2019s disease mice","volume":"22","author":"Xie","year":"2017","journal-title":"J. Biol. Inorg. Chem."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.1007\/s11064-013-1147-4","article-title":"Selenium compounds prevent amyloid beta-peptide neurotoxicity in rat primary hippocampal neurons","volume":"38","author":"Godoi","year":"2013","journal-title":"Neurochem. Res."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"6431","DOI":"10.1038\/s41598-018-24741-0","article-title":"Reversal of memory and neuropsychiatric symptoms and reduced tau pathology by selenium in 3xTg-AD mice","volume":"8","author":"Ahmed","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"145703","DOI":"10.1088\/0957-4484\/26\/14\/145703","article-title":"The inhibitory effect of selenium nanoparticles on protein glycation in vitro","volume":"26","author":"Yu","year":"2015","journal-title":"Nanotechnology"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"2301","DOI":"10.1007\/s11033-010-0362-1","article-title":"Selenium inhibits high glucose-induced cyclooxygenase-2 and P-selectin expression in vascular endothelial cells","volume":"38","author":"Li","year":"2011","journal-title":"Mol. Biol. Rep."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/s12011-012-9401-1","article-title":"Selenium downregulates RAGE and NFkappaB expression in diabetic rats","volume":"149","author":"Pillai","year":"2012","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.jinorgbio.2014.12.020","article-title":"Sulfur and selenium antioxidants: Challenging radical scavenging mechanisms and developing structure-activity relationships based on metal binding","volume":"145","author":"Zimmerman","year":"2015","journal-title":"J. Inorg. Biochem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1021\/ic051594f","article-title":"The central role of metal coordination in selenium antioxidant activity","volume":"45","author":"Battin","year":"2006","journal-title":"Inorg. Chem."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1672","DOI":"10.1021\/ic4028282","article-title":"Inhibitory effect of selenoprotein P on Cu+\/Cu2+-induced Abeta42 aggregation and toxicity","volume":"53","author":"Du","year":"2014","journal-title":"Inorg. Chem."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"11221","DOI":"10.1021\/ic501788v","article-title":"Inhibitory act of selenoprotein P on Cu+\/Cu2+-induced tau aggregation and neurotoxicity","volume":"53","author":"Du","year":"2014","journal-title":"Inorg. 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