{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T03:07:11Z","timestamp":1793156831132,"version":"4.5.0"},"reference-count":170,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2021,9,14]],"date-time":"2021-09-14T00:00:00Z","timestamp":1631577600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Neurosci."],"abstract":"<jats:p>\n                    The accumulation of protein aggregates in human tissues is a hallmark of more than 40 diseases called amyloidoses. In seven of these disorders, the aggregation is associated with neurodegenerative processes in the central nervous system such as Alzheimer\u2019s disease (AD), Parkinson\u2019s disease (PD), and Huntington\u2019s disease (HD). The aggregation occurs when certain soluble proteins lose their physiological function and become toxic amyloid species. The amyloid assembly consists of protein filament interactions, which can form fibrillar structures rich in \u03b2-sheets. Despite the frequent incidence of these diseases among the elderly, the available treatments are limited and at best palliative, and new therapeutic approaches are needed. Among the many natural compounds that have been evaluated for their ability to prevent or delay the amyloidogenic process is epigallocatechin-3-gallate (EGCG), an abundant and potent polyphenolic molecule present in green tea that has extensive biological activity. There is evidence for EGCG\u2019s ability to inhibit the aggregation of \u03b1-synuclein, amyloid-\u03b2, and huntingtin proteins, respectively associated with PD, AD, and HD. It prevents fibrillogenesis (\n                    <jats:italic>in vitro<\/jats:italic>\n                    and\n                    <jats:italic>in vivo<\/jats:italic>\n                    ), reduces amyloid cytotoxicity, and remodels fibrils to form non-toxic amorphous species that lack seed propagation. Although it is an antioxidant, EGCG in an oxidized state can promote fibrils\u2019 remodeling through formation of Schiff bases and crosslinking the fibrils. Moreover, microparticles to drug delivery were synthesized from oxidized EGCG and loaded with a second anti-amyloidogenic molecule, obtaining a synergistic therapeutic effect. Here, we describe several pre-clinical and clinical studies involving EGCG and neurodegenerative diseases and their related mechanisms.\n                  <\/jats:p>","DOI":"10.3389\/fnins.2021.718188","type":"journal-article","created":{"date-parts":[[2021,9,14]],"date-time":"2021-09-14T08:30:26Z","timestamp":1631608226000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":112,"title":["Green Tea Polyphenol Epigallocatechin-Gallate in Amyloid Aggregation and Neurodegenerative Diseases"],"prefix":"10.3389","volume":"15","author":[{"given":"Luiza","family":"Fernandes","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thyago R.","family":"Cardim-Pires","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Debora","family":"Foguel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fernando L.","family":"Palhano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2021,9,14]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"902","DOI":"10.1016\/j.phymed.2010.03.008","article-title":"Epigallocatechin gallate inhibits beta amyloid oligomerization in Caenorhabditis elegans and affects the daf-2\/insulin-like signaling pathway.","volume":"17","author":"Abbas","year":"2010","journal-title":"Phytomedicine"},{"key":"B2","doi-asserted-by":"publisher","first-page":"750","DOI":"10.1002\/dneu.22713","article-title":"Neuropathological correlates of amyloid PET imaging in Down syndrome.","volume":"79","author":"Abrahamson","year":"2019","journal-title":"Dev. Neurobiol."},{"key":"B3","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1016\/j.bpj.2020.05.033","article-title":"The effect of (-)-epigallocatechin-3-gallate on the amyloid-\u03b2 secondary structure.","volume":"119","author":"Acharya","year":"2020","journal-title":"Biophys. J."},{"key":"B4","doi-asserted-by":"publisher","first-page":"13720","DOI":"10.1021\/jacs.7b05012","article-title":"Molecular Mechanism for the (-)-epigallocatechin gallate-induced toxic to nontoxic remodeling of A\u03b2 oligomers.","volume":"139","author":"Ahmed","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"B5","doi-asserted-by":"publisher","first-page":"3005","DOI":"10.1002\/jps.21205","article-title":"High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. aggregation kinetics.","volume":"97","author":"Alford","year":"2008","journal-title":"J. Pharmaceut. Sci."},{"key":"B6","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1016\/j.redox.2016.12.016","article-title":"Oxidized epigallocatechin gallate inhibited lysozyme fibrillation more strongly than the native form.","volume":"11","author":"An","year":"2017","journal-title":"Redox Biol."},{"key":"B7","doi-asserted-by":"publisher","first-page":"6319","DOI":"10.2147\/DDDT.S96893","article-title":"Green tea extract as a treatment for patients with wild-type transthyretin amyloidosis: an observational study.","volume":"9","author":"Aus dem Siepen","year":"2015","journal-title":"Drug Design Dev. Ther."},{"key":"B8","doi-asserted-by":"publisher","first-page":"22393","DOI":"10.1002\/jbt.22393","article-title":"Mitigative effects of epigallocatechin gallate in terms of diminishing apoptosis and oxidative stress generated by the combination of lead and amyloid peptides in human neuronal cells.","volume":"33","author":"Ayyalasomayajula","year":"2019","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"B9","doi-asserted-by":"publisher","first-page":"1369","DOI":"10.1186\/s12883-019-1369-4","article-title":"Inflammatory profiling of patients with familial amyloid polyneuropathy.","volume":"19","author":"Azevedo","year":"2019","journal-title":"BMC Neurol."},{"key":"B10","doi-asserted-by":"publisher","first-page":"37206","DOI":"10.1074\/jbc.M112.369942","article-title":"Amyloid fibrils trigger the release of neutrophil extracellular traps (NETs), causing fibril fragmentation by NET-associated elastase.","volume":"287","author":"Azevedo","year":"2012","journal-title":"J. Biol. Chem."},{"key":"B11","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1016\/j.bbrc.2010.08.088","article-title":"Amyloid formation and disaggregation of \u03b1-synuclein and its tandem repeat (\u03b1-TR).","volume":"400","author":"Bae","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"B12","doi-asserted-by":"publisher","first-page":"693","DOI":"10.1080\/10408399709527797","article-title":"The chemistry of tea flavonoids.","volume":"37","author":"Balentine","year":"1997","journal-title":"Crit. Rev. Food Sci. Nutrit."},{"key":"B13","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1007\/s11596-020-2142-z","article-title":"Epigallocatechin-3-gallate alleviates cognitive deficits in APP\/PS1 mice.","volume":"40","author":"Bao","year":"2020","journal-title":"Curr. Med. Sci."},{"key":"B14","doi-asserted-by":"publisher","first-page":"4361","DOI":"10.1021\/acs.biochem.9b00739","article-title":"Lipid membranes influence the ability of small molecules to inhibit huntingtin fibrillization.","volume":"58","author":"Beasley","year":"2019","journal-title":"Biochemistry"},{"key":"B15","doi-asserted-by":"publisher","first-page":"1405","DOI":"10.1016\/j.bbapap.2010.04.001","article-title":"Molecular mechanism of thioflavin-T binding to amyloid fibrils.","volume":"1804","author":"Biancalana","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"B16","doi-asserted-by":"publisher","first-page":"7710","DOI":"10.1073\/pnas.0910723107","article-title":"EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity.","volume":"107","author":"Bieschke","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B17","doi-asserted-by":"publisher","first-page":"16926","DOI":"10.1021\/ja406197f","article-title":"Ion mobility spectrometry reveals the mechanism of amyloid formation of A\u03b2(25-35) and its modulation by inhibitors at the molecular level: epigallocatechin gallate and scyllo-inositol.","volume":"135","author":"Bleiholder","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"B18","doi-asserted-by":"publisher","first-page":"505","DOI":"10.1001\/jamaneurol.2013.5847","article-title":"Amyloid-\u03b2 and tau: the trigger and bullet in Alzheimer disease pathogenesis.","volume":"71","author":"Bloom","year":"2014","journal-title":"JAMA Neurol."},{"key":"B19","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1023\/a:1015887001987","article-title":"Chemical stability of insulin. 2. Formation of higher molecular weight transformation products during storage of pharmaceutical preparations.","volume":"9","author":"Brange","year":"1992","journal-title":"Pharmaceut. Res."},{"key":"B20","doi-asserted-by":"publisher","first-page":"e4274","DOI":"10.1073\/pnas.1416598111","article-title":"\u03b1-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation.","volume":"111","author":"Burr\u00e9","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B21","doi-asserted-by":"publisher","first-page":"1183","DOI":"10.1038\/s41593-020-0687-6","article-title":"Synergy between amyloid-\u03b2 and tau in Alzheimer\u2019s disease.","volume":"23","author":"Busche","year":"2020","journal-title":"Nat. Neurosci."},{"key":"B22","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/j.jconrel.2019.03.010","article-title":"Dual-drug loaded nanoparticles of epigallocatechin-3-gallate (EGCG)\/ascorbic acid enhance therapeutic efficacy of EGCG in a APPswe\/PS1dE9 Alzheimer\u2019s disease mice model.","volume":"301","author":"Cano","year":"2019","journal-title":"J. Control. Rel."},{"key":"B23","doi-asserted-by":"publisher","first-page":"1113","DOI":"10.1016\/j.febslet.2011.03.046","article-title":"Inhibition and disaggregation of \u03b1-synuclein oligomers by natural polyphenolic compounds.","volume":"585","author":"Caruana","year":"2011","journal-title":"FEBS Lett."},{"key":"B24","doi-asserted-by":"publisher","first-page":"21937","DOI":"10.1038\/s41467-021-21937-3","article-title":"The release of toxic oligomers from \u03b1-synuclein fibrils induces dysfunction in neuronal cells.","volume":"12","author":"Cascella","year":"2021","journal-title":"Nat. Commun."},{"key":"B25","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1016\/j.foodchem.2015.11.118","article-title":"Metal chelation, radical scavenging and inhibition of A\u03b242 fibrillation by food constituents in relation to Alzheimer\u2019s disease.","volume":"199","author":"Chan","year":"2016","journal-title":"Food Chem."},{"key":"B26","doi-asserted-by":"publisher","first-page":"004","DOI":"10.1016\/j.yexcr.2015.04.004","article-title":"(-)-Epigallocatechin-3-gallate attenuates cognitive deterioration in Alzheimer\u2019s disease model mice by upregulating neprilysin expression.","volume":"334","author":"Chang","year":"2015","journal-title":"Exp. Cell Res."},{"key":"B27","doi-asserted-by":"publisher","first-page":"383","DOI":"10.1016\/j.neuroscience.2014.12.003","article-title":"Tea polyphenols alleviate motor impairments, dopaminergic neuronal injury, and cerebral \u03b1-synuclein aggregation in MPTP-intoxicated parkinsonian monkeys.","volume":"286","author":"Chen","year":"2015","journal-title":"Neuroscience"},{"key":"B28","doi-asserted-by":"publisher","first-page":"ja311374b","DOI":"10.1021\/ja311374b","article-title":"Biocompatible, functional spheres based on oxidative coupling assembly of green tea polyphenols.","volume":"135","author":"Chen","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"B29","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1016\/j.ejphar.2015.11.048","article-title":"Epigallocatechin gallate attenuates amyloid \u03b2-induced inflammation and neurotoxicity in EOC 13.31 microglia.","volume":"770","author":"Cheng-Chung Wei","year":"2016","journal-title":"Eur. J. Pharmacol."},{"key":"B30","doi-asserted-by":"publisher","first-page":"a:1025771421906","DOI":"10.1023\/a:1025771421906","article-title":"Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation.","volume":"20","author":"Chi","year":"2003","journal-title":"Pharmaceut. Res."},{"key":"B31","doi-asserted-by":"publisher","first-page":"1218424110","DOI":"10.1073\/pnas.1218424110","article-title":"Large \u03b1-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.","volume":"110","author":"Choi","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B32","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1016\/s0024-3205(01)01438-2","article-title":"The green tea polyphenol (-)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons.","volume":"70","author":"Choi","year":"2001","journal-title":"Life Sci."},{"key":"B33","doi-asserted-by":"publisher","first-page":"20315","DOI":"10.1074\/jbc.M601016200","article-title":"ERK1\/2 activation mediates Abeta oligomer-induced neurotoxicity via caspase-3 activation and tau cleavage in rat organotypic hippocampal slice cultures.","volume":"281","author":"Chong","year":"2006","journal-title":"J. Biol. Chem."},{"key":"B34","first-page":"3312","article-title":"Pharmacokinetics and safety of green tea polyphenols after multiple-dose administration of epigallocatechin gallate and polyphenon E in healthy individuals.","volume":"9","author":"Chow","year":"2003","journal-title":"Clin. Cancer Res."},{"key":"B35","doi-asserted-by":"publisher","first-page":"785","DOI":"10.1212\/WNL.0b013e3182661eb1","article-title":"Tafamidis for transthyretin familial amyloid polyneuropathy: a randomized, controlled trial.","volume":"79","author":"Coelho","year":"2012","journal-title":"Neurology"},{"key":"B36","doi-asserted-by":"publisher","first-page":"a006833","DOI":"10.1101\/cshperspect.a006833","article-title":"Prions.","volume":"3","author":"Colby","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"B37","doi-asserted-by":"publisher","first-page":"4790","DOI":"10.1007\/s12035-020-02064-4","article-title":"Guanosine neuroprotection of presynaptic mitochondrial calcium homeostasis in a mouse study with amyloid-\u03b2 oligomers.","volume":"57","author":"da Silva","year":"2020","journal-title":"Mol. Neurobiol."},{"key":"B38","doi-asserted-by":"publisher","first-page":"9220","DOI":"10.1523\/JNEUROSCI.2617-07.2007","article-title":"Different species of alpha-synuclein oligomers induce calcium influx and seeding.","volume":"27","author":"Danzer","year":"2007","journal-title":"J. Neurosci."},{"key":"B39","doi-asserted-by":"publisher","first-page":"104997","DOI":"10.1016\/j.phrs.2020.104997","article-title":"The flavonoid agathisflavone modulates the microglial neuroinflammatory response and enhances remyelination.","volume":"159","author":"de Almeida","year":"2020","journal-title":"Pharmacol. Res."},{"key":"B40","doi-asserted-by":"publisher","first-page":"1921","DOI":"10.1007\/s00210-020-01905-2","article-title":"Agathisflavone modulates astrocytic responses and increases the population of neurons in an in vitro model of traumatic brain injury.","volume":"393","author":"de Amorim","year":"2020","journal-title":"Naunyn-Schmiedeberg\u2019s Archiv. Pharmacol."},{"key":"B41","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1016\/j.clnu.2019.02.028","article-title":"A phase 1, randomized double-blind, placebo controlled trial to evaluate safety and efficacy of epigallocatechin-3-gallate and cognitive training in adults with Fragile X syndrome.","volume":"39","author":"de la Torre","year":"2020","journal-title":"Clin. Nutrit."},{"key":"B42","doi-asserted-by":"publisher","first-page":"801","DOI":"10.1016\/S1474-4422(16)30034-5","article-title":"Safety and efficacy of cognitive training plus epigallocatechin-3-gallate in young adults with Down\u2019s syndrome (TESDAD): a double-blind, randomised, placebo-controlled, phase 2 trial.","volume":"15","author":"de la Torre","year":"2016","journal-title":"Lancet Neurol."},{"key":"B43","doi-asserted-by":"publisher","first-page":"278","DOI":"10.1002\/mnfr.201300325","article-title":"Epigallocatechin-3-gallate, a DYRK1A inhibitor, rescues cognitive deficits in Down Syndrome mouse models and in humans.","volume":"58","author":"de la Torre","year":"2014","journal-title":"Mol. Nutrit. Food Res."},{"key":"B44","doi-asserted-by":"publisher","first-page":"376","DOI":"10.1089\/ars.2015.6343","article-title":"Alpha-synuclein oligomers interact with metal ions to induce oxidative stress and neuronal death in Parkinson\u2019s Disease.","volume":"24","author":"Deas","year":"2016","journal-title":"Antioxidants Redox Signal."},{"key":"B45","doi-asserted-by":"publisher","first-page":"20309","DOI":"10.1021\/acsami.6b06853","article-title":"Efficient Inhibition of Protein Aggregation, Disintegration of Aggregates, and Lowering of Cytotoxicity by Green Tea Polyphenol-Based Self-Assembled Polymer Nanoparticles.","volume":"8","author":"Debnath","year":"2016","journal-title":"ACS Appl. Mater. Interf."},{"key":"B46","doi-asserted-by":"publisher","first-page":"842","DOI":"10.1002\/ajmg.a.38494","article-title":"Therapy development in Huntington disease: from current strategies to emerging opportunities.","volume":"176","author":"Dickey","year":"2018","journal-title":"Am. J. Med. Genet. Part A"},{"key":"B47","doi-asserted-by":"publisher","first-page":"1990","DOI":"10.1126\/science.277.5334.1990","article-title":"Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain.","volume":"277","author":"DiFiglia","year":"1997","journal-title":"Science"},{"key":"B48","doi-asserted-by":"publisher","first-page":"12827","DOI":"10.1038\/s41598-020-69744-y","article-title":"Effects of pharmacological modulators of \u03b1-synuclein and tau aggregation and internalization.","volume":"10","author":"Dominguez-Meijide","year":"2020","journal-title":"Sci. Rep."},{"key":"B49","doi-asserted-by":"publisher","first-page":"507","DOI":"10.3233\/JAD-2011-101629","article-title":"Green tea epigallocatechin-3-gallate (EGCG) and other flavonoids reduce Alzheimer\u2019s amyloid-induced mitochondrial dysfunction.","volume":"26","author":"Dragicevic","year":"2011","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"B50","doi-asserted-by":"publisher","first-page":"201700890","DOI":"10.1002\/mnfr.201700890","article-title":"Epigallocatechin gallate reduces amyloid \u03b2-induced neurotoxicity via inhibiting endoplasmic reticulum stress-mediated apoptosis.","volume":"62","author":"Du","year":"2018","journal-title":"Mol. Nutrit. Food Res."},{"key":"B51","doi-asserted-by":"publisher","first-page":"244","DOI":"10.4161\/pri.4.4.13597","article-title":"Countering amyloid polymorphism and drug resistance with minimal drug cocktails.","volume":"4","author":"Duennwald","year":"2010","journal-title":"Prion"},{"key":"B52","doi-asserted-by":"publisher","first-page":"558","DOI":"10.1038\/nsmb.1437","article-title":"EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers.","volume":"15","author":"Ehrnhoefer","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B53","doi-asserted-by":"publisher","first-page":"2743","DOI":"10.1093\/hmg\/ddl210","article-title":"Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington\u2019s disease models.","volume":"15","author":"Ehrnhoefer","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"B54","doi-asserted-by":"publisher","first-page":"4414","DOI":"10.1021\/acsbiomaterials.0c00188","article-title":"Green Tea Polyphenol Microparticles Based on the Oxidative Coupling of EGCG Inhibit Amyloid Aggregation\/Cytotoxicity and Serve as a Platform for Drug Delivery.","volume":"6","author":"Fernandes","year":"2020","journal-title":"ACS Biomater. Sci. Engine."},{"key":"B55","doi-asserted-by":"publisher","first-page":"1704","DOI":"10.1021\/acschemneuro.7b00017","article-title":"An ortho-iminoquinone compound reacts with lysine inhibiting aggregation while remodeling mature amyloid fibrils.","volume":"8","author":"Fernandes","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"B56","doi-asserted-by":"publisher","first-page":"4259","DOI":"10.1016\/j.febslet.2010.09.022","article-title":"EGCG functions through estrogen receptor-mediated activation of ADAM10 in the promotion of non-amyloidogenic processing of APP.","volume":"584","author":"Fernandez","year":"2010","journal-title":"FEBS Lett."},{"key":"B57","doi-asserted-by":"publisher","first-page":"9626","DOI":"10.1523\/JNEUROSCI.0482-13.2013","article-title":"Memantine rescues transient cognitive impairment caused by high-molecular-weight a\u03b2 oligomers but not the persistent impairment induced by low-molecular-weight oligomers.","volume":"33","author":"Figueiredo","year":"2013","journal-title":"J. Neurosci."},{"key":"B58","doi-asserted-by":"publisher","first-page":"23117","DOI":"10.1002\/bip.23117","article-title":"Molecular determinants of the interaction of EGCG with ordered and disordered proteins.","volume":"109","author":"Fusco","year":"2018","journal-title":"Biopolymers"},{"key":"B59","doi-asserted-by":"publisher","first-page":"589","DOI":"10.1016\/j.bbapap.2017.02.014","article-title":"Polyphenols in combination with \u03b2-cyclodextrin can inhibit and disaggregate \u03b1-synuclein amyloids under cell mimicking conditions: A promising therapeutic alternative.","volume":"1865","author":"Gautam","year":"2017","journal-title":"Biochim. Biophys. Acta Prot. Proteom."},{"key":"B60","doi-asserted-by":"publisher","first-page":"a023747","DOI":"10.1101\/cshperspect.a023747","article-title":"Developing Therapeutics for PrP Prion Diseases.","volume":"7","author":"Giles","year":"2017","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"B61","doi-asserted-by":"publisher","first-page":"5813793","DOI":"10.1155\/2017\/5813793","article-title":"Therapeutic potential of epigallocatechin gallate nanodelivery systems.","volume":"2017","author":"Granja","year":"2017","journal-title":"BioMed Res. Int."},{"key":"B62","doi-asserted-by":"publisher","first-page":"312","DOI":"10.1016\/j.bbadis.2005.11.009","article-title":"A yeast-based model of alpha-synucleinopathy identifies compounds with therapeutic potential.","volume":"1762","author":"Griffioen","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"B63","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1021\/acs.biochem.6b01060","article-title":"Site-specific fluorescence polarization for studying the disaggregation of \u03b1-synuclein fibrils by small molecules.","volume":"56","author":"Haney","year":"2017","journal-title":"Biochemistry"},{"key":"B64","doi-asserted-by":"publisher","first-page":"AN20100025","DOI":"10.1042\/AN20100025","article-title":"Prolonged exposure of cortical neurons to oligomeric amyloid-\u03b2 impairs NMDA receptor function via NADPH oxidase-mediated ROS production: protective effect of green tea (-)-epigallocatechin-3-gallate.","volume":"3","author":"He","year":"2011","journal-title":"ASN Neuro"},{"key":"B65","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1111\/j.1365-3083.1986.tb01966.x","article-title":"Chemical and clinical classification of amyloidosis.","volume":"23","author":"Husby","year":"1986","journal-title":"Scand. J. Immunol."},{"key":"B66","doi-asserted-by":"publisher","first-page":"3743","DOI":"10.1073\/pnas.1220326110","article-title":"Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-\u03b2 species.","volume":"110","author":"Hyung","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B67","doi-asserted-by":"publisher","first-page":"3905","DOI":"10.1016\/j.bmcl.2003.09.018","article-title":"Green tea catechins as a BACE1 (beta-secretase) inhibitor.","volume":"13","author":"Jeon","year":"2003","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"B68","doi-asserted-by":"publisher","first-page":"2722","DOI":"10.1021\/acschemneuro.7b00261","article-title":"Comparison of \u03b1-synuclein fibril inhibition by four different amyloid inhibitors.","volume":"8","author":"Jha","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"B69","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1007\/s11010-013-1675-x","article-title":"(-)-Epigallocatechin-3-gallate alleviates spatial memory impairment in APP\/PS1 mice by restoring IRS-1 signaling defects in the hippocampus.","volume":"380","author":"Jia","year":"2013","journal-title":"Mol. Cell. Biochem."},{"key":"B70","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1002\/pro.2180","article-title":"Characterizing antiprion compounds based on their binding properties to prion proteins: implications as medical chaperones.","volume":"22","author":"Kamatari","year":"2013","journal-title":"Prot. Sci."},{"key":"B71","doi-asserted-by":"publisher","first-page":"129001","DOI":"10.3233\/JAD-2012-129001","article-title":"Molecular mechanisms of amyloid oligomers toxicity.","volume":"33","author":"Kayed","year":"2013","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"B72","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1186\/1750-1326-2-18","article-title":"Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers.","volume":"2","author":"Kayed","year":"2007","journal-title":"Mol. Neurodegenerat."},{"key":"B73","doi-asserted-by":"publisher","first-page":"8700","DOI":"10.1021\/acsomega.1c00680","article-title":"Pentameric Thiophene as a Probe to Monitor EGCG\u2019s Remodeling Activity of Mature Amyloid Fibrils: Overcoming Signal Artifacts of Thioflavin T.","volume":"6","author":"Kelley","year":"2021","journal-title":"ACS Omega"},{"key":"B74","doi-asserted-by":"publisher","first-page":"869","DOI":"10.1007\/s12272-009-1609-z","article-title":"Neuroprotective effect of epigallocatechin-3-gallate against beta-amyloid-induced oxidative and nitrosative cell death via augmentation of antioxidant defense capacity.","volume":"32","author":"Kim","year":"2009","journal-title":"Archiv. Pharmacal. Res."},{"key":"B75","doi-asserted-by":"publisher","first-page":"10288","DOI":"10.1128\/jvi.77.19.10288-10294.2003","article-title":"New inhibitors of scrapie-associated prion protein formation in a library of 2000 drugs and natural products.","volume":"77","author":"Kocisko","year":"2003","journal-title":"J. Virol."},{"key":"B76","doi-asserted-by":"publisher","first-page":"2479","DOI":"10.1099\/vir.0.80082-0","article-title":"Evaluation of new cell culture inhibitors of protease-resistant prion protein against scrapie infection in mice.","volume":"85","author":"Kocisko","year":"2004","journal-title":"J. General Virol."},{"key":"B77","doi-asserted-by":"publisher","first-page":"4012","DOI":"10.1073\/pnas.0811698106","article-title":"Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques.","volume":"106","author":"Koffie","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B78","doi-asserted-by":"publisher","first-page":"8468","DOI":"10.1021\/acs.analchem.6b00731","article-title":"Opposite structural effects of epigallocatechin-3-gallate and dopamine binding to \u03b1-synuclein.","volume":"88","author":"Konijnenberg","year":"2016","journal-title":"Analyt. Chem."},{"key":"B79","doi-asserted-by":"publisher","first-page":"805","DOI":"10.1007\/s00392-012-0463-z","article-title":"Green tea halts progression of cardiac transthyretin amyloidosis: an observational report.","volume":"101","author":"Kristen","year":"2012","journal-title":"Clin. Res. Cardiol."},{"key":"B80","doi-asserted-by":"publisher","first-page":"70794","DOI":"10.18632\/oncotarget.12222","article-title":"Randomized, placebo-controlled trial evaluating the safety of one-year administration of green tea catechins.","volume":"7","author":"Kumar","year":"2016","journal-title":"Oncotarget"},{"key":"B81","doi-asserted-by":"publisher","first-page":"2522","DOI":"10.1016\/j.fct.2009.07.011","article-title":"Effect of lycopene and epigallocatechin-3-gallate against 3-nitropropionic acid induced cognitive dysfunction and glutathione depletion in rat: A novel nitric oxide mechanism.","volume":"47","author":"Kumar","year":"2009","journal-title":"Food Chem. Toxicol."},{"key":"B82","doi-asserted-by":"publisher","first-page":"162750","DOI":"10.1155\/2013\/162750","article-title":"Chemistry and biological activities of flavonoids: an overview.","volume":"29","author":"Kumar","year":"2013","journal-title":"Sci. World J."},{"key":"B83","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1016\/j.actbio.2020.11.015","article-title":"Use of leptin-conjugated phosphatidic acid liposomes with resveratrol and epigallocatechin gallate to protect dopaminergic neurons against apoptosis for Parkinson\u2019s disease therapy.","volume":"119","author":"Kuo","year":"2021","journal-title":"Acta Biomaterial."},{"key":"B84","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1111\/nan.12644","article-title":"Peripheral inflammation exacerbates \u03b1-synuclein toxicity and neuropathology in Parkinson\u2019s models.","volume":"47","author":"La Vitola","year":"2021","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"B85","doi-asserted-by":"publisher","first-page":"108620","DOI":"10.1016\/j.abb.2020.108620","article-title":"The tea catechin epigallocatechin gallate inhibits NF-\u03baB-mediated transcriptional activation by covalent modification.","volume":"695","author":"Lakshmi","year":"2020","journal-title":"Arch. Biochem. Biophys."},{"key":"B86","doi-asserted-by":"publisher","first-page":"5409","DOI":"10.1002\/anie.201200587","article-title":"A biologically inspired Cu(I)\/topaquinone-like co-catalytic system for the highly atom-economical aerobic oxidation of primary amines to imines.","volume":"51","author":"Largeron","year":"2012","journal-title":"Angewandte Chemie"},{"key":"B87","doi-asserted-by":"publisher","first-page":"9701","DOI":"10.18632\/oncotarget.3832","article-title":"EGCG-mediated autophagy flux has a neuroprotection effect via a class III histone deacetylase in primary neuron cells.","volume":"6","author":"Lee","year":"2015","journal-title":"Oncotarget"},{"key":"B88","doi-asserted-by":"publisher","first-page":"1987","DOI":"10.3945\/jn.109.109785","article-title":"Green tea (-)-epigallocatechin-3-gallate inhibits beta-amyloid-induced cognitive dysfunction through modification of secretase activity via inhibition of ERK and NF-kappaB pathways in mice.","volume":"139","author":"Lee","year":"2009","journal-title":"J. Nutrit."},{"key":"B89","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1080\/1028415X.2018.1507618","article-title":"Effect of catechins and high-temperature-processed green tea extract on scavenging reactive oxygen species and preventing A\u03b21\u201342 fibrils\u2019 formation in brain microvascular endothelium.","volume":"23","author":"Lee","year":"2020","journal-title":"Nutrit. Neurosci."},{"key":"B90","doi-asserted-by":"publisher","first-page":"724","DOI":"10.1016\/S1474-4422(19)30141-3","article-title":"Safety and efficacy of epigallocatechin gallate in multiple system atrophy (PROMESA): a randomised, double-blind, placebo-controlled trial.","volume":"18","author":"Levin","year":"2019","journal-title":"Lancet Neurol."},{"key":"B91","doi-asserted-by":"publisher","first-page":"952","DOI":"10.1096\/fj.02-0881fje","article-title":"Neuroprotection and neurorescue against Abeta toxicity and PKC-dependent release of nonamyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate.","volume":"17","author":"Levites","year":"2003","journal-title":"Federat. Am. Soc. Exp. Biol."},{"key":"B92","doi-asserted-by":"publisher","first-page":"5469","DOI":"10.7150\/thno.28295","article-title":"\u201cCell-addictive\u201d dual-target traceable nanodrug for Parkinson\u2019s disease treatment via flotillins pathway.","volume":"8","author":"Li","year":"2018","journal-title":"Theranostics"},{"key":"B93","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/j.neurobiolaging.2007.05.012","article-title":"Epigallocatechin gallate (EGCG) suppresses beta-amyloid-induced neurotoxicity through inhibiting c-Abl\/FE65 nuclear translocation and GSK3 beta activation.","volume":"30","author":"Lin","year":"2009","journal-title":"Neurobiol. Aging"},{"key":"B94","doi-asserted-by":"publisher","first-page":"11879","DOI":"10.1021\/jp202640b","article-title":"Molecular insight into conformational transition of amyloid \u03b2-peptide 42 inhibited by (-)-epigallocatechin-3-gallate probed by molecular simulations.","volume":"115","author":"Liu","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"B95","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1016\/j.jcis.2016.12.038","article-title":"Synergistic effects of negatively charged hydrophobic nanoparticles and (-)-epigallocatechin-3-gallate on inhibiting amyloid \u03b2-protein aggregation.","volume":"491","author":"Liu","year":"2017","journal-title":"J. Colloid Interf. Sci."},{"key":"B96","doi-asserted-by":"publisher","first-page":"1350","DOI":"10.1007\/s12035-013-8608-2","article-title":"(-)-Epigallocatechin-3-gallate ameliorates learning and memory deficits by adjusting the balance of TrkA\/p75NTR signaling in APP\/PS1 transgenic mice.","volume":"49","author":"Liu","year":"2014","journal-title":"Mol. Neurobiol."},{"key":"B97","doi-asserted-by":"publisher","first-page":"162","DOI":"10.1111\/cbdd.13067","article-title":"Influence of EGCG on \u03b1-synuclein (\u03b1S) aggregation and identification of their possible binding mode: A computational study using molecular dynamics simulation.","volume":"91","author":"Liu","year":"2018","journal-title":"Chem. Biol. Drug Design"},{"key":"B98","doi-asserted-by":"publisher","first-page":"517","DOI":"10.1016\/j.jmb.2012.01.013","article-title":"Structural properties of EGCG-induced, nontoxic Alzheimer\u2019s disease A\u03b2 oligomers.","volume":"421","author":"Lopez del Amo","year":"2012","journal-title":"J. Mol. Biol."},{"key":"B99","doi-asserted-by":"publisher","first-page":"21299","DOI":"10.1074\/jbc.M114.554667","article-title":"How epigallocatechin gallate can inhibit \u03b1-synuclein oligomer toxicity in vitro.","volume":"289","author":"Lorenzen","year":"2014","journal-title":"J. Biol. Chem."},{"key":"B100","doi-asserted-by":"publisher","first-page":"2293","DOI":"10.1038\/s41467-018-04422-2","article-title":"\u03b1-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson\u2019s disease.","volume":"9","author":"Ludtmann","year":"2018","journal-title":"Nat. Commun."},{"key":"B101","doi-asserted-by":"publisher","first-page":"21490","DOI":"10.1074\/jbc.M113.545749","article-title":"Soluble, prefibrillar \u03b1-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction.","volume":"289","author":"Luth","year":"2014","journal-title":"J. Biol. Chem."},{"key":"B102","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1007\/s11064-009-0038-1","article-title":"Genome-wide microarray analysis of the differential neuroprotective effects of antioxidants in neuroblastoma cells overexpressing the familial Parkinson\u2019s disease alpha-synuclein A53T mutation.","volume":"35","author":"Ma","year":"2010","journal-title":"Neurochem. Res."},{"key":"B103","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1093\/ajcn\/79.5.727","article-title":"Polyphenols: food sources and bioavailability.","volume":"79","author":"Manach","year":"2004","journal-title":"Am. J. Clin. Nutrit."},{"key":"B104","doi-asserted-by":"publisher","first-page":"2183","DOI":"10.1113\/JP279345","article-title":"Amyloid Beta42 oligomers up-regulate the excitatory synapses by potentiating presynaptic release while impairing postsynaptic NMDA receptors.","volume":"598","author":"Marcantoni","year":"2020","journal-title":"J. Physiol."},{"key":"B105","doi-asserted-by":"publisher","first-page":"1007","DOI":"10.1056\/NEJMoa1805689","article-title":"Tafamidis treatment for patients with transthyretin amyloid cardiomyopathy.","volume":"379","author":"Maurer","year":"2018","journal-title":"N. Engl. J. Med."},{"key":"B106","doi-asserted-by":"publisher","first-page":"1214","DOI":"10.1111\/ejn.12507","article-title":"Tau phosphorylation and tau mislocalization mediate soluble A\u03b2 oligomer-induced AMPA glutamate receptor signaling deficits.","volume":"39","author":"Miller","year":"2014","journal-title":"Eur. J. Neurosci."},{"key":"B107","doi-asserted-by":"publisher","first-page":"936","DOI":"10.1002\/iub.1094","article-title":"Fe65 matters: new light on an old molecule.","volume":"64","author":"Minopoli","year":"2012","journal-title":"IUBMB Life"},{"key":"B108","doi-asserted-by":"publisher","first-page":"2714","DOI":"10.1074\/jbc.RA118.004280","article-title":"Combined treatment with the phenolics (-)-epigallocatechin-3-gallate and ferulic acid improves cognition and reduces Alzheimer-like pathology in mice.","volume":"294","author":"Mori","year":"2019","journal-title":"J. Biol. Chem."},{"key":"B109","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/s0896-6273(02)00761-4","article-title":"Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones?","volume":"35","author":"Muchowski","year":"2002","journal-title":"Neuron"},{"key":"B110","doi-asserted-by":"publisher","first-page":"1981","DOI":"10.1271\/bbb.61.1981","article-title":"Dose-dependent incorporation of tea catechins, (-)-epigallocatechin-3-gallate and (-)-epigallocatechin, into human plasma.","volume":"61","author":"Nakagawa","year":"1997","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"B111","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1016\/s0025-7125(03)00072-5","article-title":"Traditional Chinese medicine.","volume":"86","author":"Nestler","year":"2002","journal-title":"Med. Clin. North Am."},{"key":"B112","doi-asserted-by":"publisher","first-page":"16419","DOI":"10.1074\/jbc.M600617200","article-title":"ADAM10 activation is required for green tea (-)-epigallocatechin-3-gallate-induced alpha-secretase cleavage of amyloid precursor protein.","volume":"281","author":"Obregon","year":"2006","journal-title":"J. Biol. Chem."},{"key":"B113","doi-asserted-by":"publisher","first-page":"1648","DOI":"10.1002\/asia.201600259","article-title":"Cyclodextrins as protective agents of protein aggregation: an overview.","volume":"11","author":"Oliveri","year":"2016","journal-title":"Chemis. Asian J."},{"key":"B114","doi-asserted-by":"publisher","first-page":"7503","DOI":"10.1021\/ja3115696","article-title":"Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils.","volume":"135","author":"Palhano","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"B115","doi-asserted-by":"publisher","first-page":"10962","DOI":"10.1073\/pnas.90.23.10962","article-title":"Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.","volume":"90","author":"Pan","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B116","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1126\/science.277.5324.381","article-title":"In vitro propagation of the prion-like state of yeast Sup35 protein.","volume":"277","author":"Paushkin","year":"1997","journal-title":"Science"},{"key":"B117","doi-asserted-by":"publisher","first-page":"5657","DOI":"10.1074\/jbc.RA118.001907","article-title":"Methionine oxidation in \u03b1-synuclein inhibits its propensity for ordered secondary structure.","volume":"294","author":"Ponzini","year":"2019","journal-title":"J. Biol. Chem."},{"key":"B118","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1016\/s0092-8674(00)81163-0","article-title":"Prion protein biology.","volume":"93","author":"Prusiner","year":"1998","journal-title":"Cell"},{"key":"B119","doi-asserted-by":"publisher","first-page":"218","DOI":"10.1111\/j.1471-4159.2008.05611.x","article-title":"Green tea extracts interfere with the stress-protective activity of PrP and the formation of PrP.","volume":"107","author":"Rambold","year":"2008","journal-title":"J. Neurochem."},{"key":"B120","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1016\/j.brainres.2008.02.107","article-title":"Green tea epigallocatechin-3-gallate (EGCG) reduces beta-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice.","volume":"1214","author":"Rezai-Zadeh","year":"2008","journal-title":"Brain Res."},{"key":"B121","doi-asserted-by":"publisher","first-page":"8807","DOI":"10.1523\/JNEUROSCI.1521-05.2005","article-title":"Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice.","volume":"25","author":"Rezai-Zadeh","year":"2005","journal-title":"J. Neurosci."},{"key":"B122","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1111\/j.1471-4159.2006.03770.x","article-title":"Reduction of iron-regulated amyloid precursor protein and beta-amyloid peptide by (-)-epigallocatechin-3-gallate in cell cultures: implications for iron chelation in Alzheimer\u2019s disease.","volume":"97","author":"Reznichenko","year":"2006","journal-title":"J. Neurochem."},{"key":"B123","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/j.phytochem.2018.12.013","article-title":"Identification of fermented tea (Camellia sinensis) polyphenols and their inhibitory activities against amyloid-beta aggregation.","volume":"160","author":"Rho","year":"2019","journal-title":"Phytochemistry"},{"key":"B124","doi-asserted-by":"publisher","first-page":"936","DOI":"10.1038\/nchembio.246","article-title":"A synergistic small-molecule combination directly eradicates diverse prion strain structures.","volume":"5","author":"Roberts","year":"2009","journal-title":"Nat. Chem. Biol."},{"key":"B125","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1016\/j.nbd.2017.04.004","article-title":"Alpha-synuclein: Pathology, mitochondrial dysfunction and neuroinflammation in Parkinson\u2019s disease.","volume":"109","author":"Rocha","year":"2018","journal-title":"Neurobiol. Dis."},{"key":"B126","doi-asserted-by":"publisher","first-page":"780","DOI":"10.1038\/nature05291","article-title":"The roles of intracellular protein-degradation pathways in neurodegeneration.","volume":"443","author":"Rubinsztein","year":"2006","journal-title":"Nature"},{"key":"B127","doi-asserted-by":"publisher","first-page":"254","DOI":"10.4103\/2249-4863.192322","article-title":"Physicians of ancient India.","volume":"5","author":"Saini","year":"2016","journal-title":"J. Fam. Med. Primary Care"},{"key":"B128","doi-asserted-by":"publisher","first-page":"5284","DOI":"10.3390\/ijms14035284","article-title":"Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis.","volume":"14","author":"Sant\u2019anna","year":"2013","journal-title":"Int. J. Mol. Sci."},{"key":"B129","doi-asserted-by":"publisher","first-page":"1501","DOI":"10.1212\/01.wnl.0000260698.46517.8f","article-title":"Synaptic alterations in CA1 in mild Alzheimer disease and mild cognitive impairment.","volume":"68","author":"Scheff","year":"2007","journal-title":"Neurology"},{"key":"B130","doi-asserted-by":"publisher","first-page":"442","DOI":"10.1016\/j.foodres.2017.07.026","article-title":"Green tea supplementation produces better neuroprotective effects than red and black tea in Alzheimer-like rat model.","volume":"100","author":"Schimidt","year":"2017","journal-title":"Food Res. Int."},{"key":"B131","doi-asserted-by":"publisher","first-page":"767","DOI":"10.1016\/j.appet.2011.11.016","article-title":"Acute neurocognitive effects of epigallocatechin gallate (EGCG).","volume":"58","author":"Scholey","year":"2012","journal-title":"Appetite"},{"key":"B132","doi-asserted-by":"publisher","first-page":"1329","DOI":"10.1097\/WNR.0b013e32830b8ae1","article-title":"Epigallocatechin-3-gallate and curcumin suppress amyloid beta-induced beta-site APP cleaving enzyme-1 upregulation.","volume":"19","author":"Shimmyo","year":"2008","journal-title":"Neuroreport"},{"key":"B133","doi-asserted-by":"publisher","first-page":"244","DOI":"10.3389\/fnagi.2018.00244","article-title":"EGCG Nanoparticles attenuate aluminum chloride induced neurobehavioral deficits, beta amyloid and tau pathology in a rat model of Alzheimer\u2019s Disease.","volume":"10","author":"Singh","year":"2018","journal-title":"Front. Aging Neurosci."},{"key":"B134","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1021\/cn200133x","article-title":"Comparison of three amyloid assembly inhibitors: the sugar scyllo-inositol, the polyphenol epigallocatechin gallate, and the molecular tweezer CLR01.","volume":"3","author":"Sinha","year":"2012","journal-title":"ACS Chem. Neurosci."},{"key":"B135","doi-asserted-by":"publisher","first-page":"13793","DOI":"10.1002\/chem.201403188","article-title":"Natural compounds against neurodegenerative diseases: molecular characterization of the interaction of catechins from green tea with A\u03b21-42, PrP106-126, and ataxin-3 oligomers.","volume":"20","author":"Sironi","year":"2014","journal-title":"Chemistry"},{"key":"B136","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1016\/j.ijpharm.2010.01.012","article-title":"Nanolipidic particles improve the bioavailability and alpha-secretase inducing ability of epigallocatechin-3-gallate (EGCG) for the treatment of Alzheimer\u2019s disease.","volume":"389","author":"Smith","year":"2010","journal-title":"Int. J. Pharmaceut."},{"key":"B137","doi-asserted-by":"publisher","first-page":"e1271","DOI":"10.7717\/peerj.1271","article-title":"Looking for a generic inhibitor of amyloid-like fibril formation among flavone derivatives.","volume":"3","author":"\u0160neideris","year":"2015","journal-title":"PeerJ"},{"key":"B138","doi-asserted-by":"publisher","first-page":"855","DOI":"10.3390\/biom9120855","article-title":"The environment is a key factor in determining the anti-amyloid efficacy of EGCG.","volume":"9","author":"\u0160neideris","year":"2019","journal-title":"Biomolecules"},{"key":"B139","doi-asserted-by":"publisher","first-page":"1995","DOI":"10.3390\/ijms21061995","article-title":"The aggregation conditions define whether EGCG is an inhibitor or enhancer of \u03b1-synuclein amyloid fibril formation.","volume":"21","author":"Sternke-Hoffmann","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"B140","doi-asserted-by":"publisher","first-page":"5462","DOI":"10.3390\/ijms21155462","article-title":"Insights into the effect of curcumin and (-)-epigallocatechin-3-gallate on the aggregation of A\u03b2(1-40) monomers by means of molecular dynamics.","volume":"21","author":"Tavanti","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"B141","doi-asserted-by":"publisher","first-page":"2940","DOI":"10.3390\/molecules24162940","article-title":"Complex of EGCG with Cu(II) suppresses amyloid aggregation and Cu(II)-induced cytotoxicity of \u03b1-synuclein.","volume":"24","author":"Teng","year":"2019","journal-title":"Molecules"},{"key":"B142","doi-asserted-by":"publisher","first-page":"881","DOI":"10.1016\/j.jagp.2016.07.009","article-title":"Green tea consumption and the risk of incident dementia in elderly japanese: the Ohsaki Cohort 2006 Study.","volume":"24","author":"Tomata","year":"2016","journal-title":"Am. J. Geriatr. Psychiatry"},{"key":"B143","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1016\/j.jsb.2012.07.008","article-title":"Flavonoid interactions with human transthyretin: combined structural and thermodynamic analysis.","volume":"180","author":"Trivella","year":"2012","journal-title":"J. Struct. Biol."},{"key":"B144","doi-asserted-by":"publisher","first-page":"356","DOI":"10.1038\/sj.ejcn.1600568","article-title":"Bioavailability of catechins from tea: the effect of milk.","volume":"52","author":"van het Hof","year":"1998","journal-title":"Eur. J. Clin. Nutrit."},{"key":"B145","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1080\/1028415X.2018.1484021","article-title":"Green tea infusion alleviates neurodegeneration induced by mutant Huntingtin in Drosophila.","volume":"23","author":"Varga","year":"2020","journal-title":"Nutrit. Neurosci."},{"key":"B146","doi-asserted-by":"publisher","first-page":"173554","DOI":"10.1016\/j.ejphar.2020.173554","article-title":"Alzheimer\u2019s disease: recent treatment strategies.","volume":"887","author":"Vaz","year":"2020","journal-title":"Eur. J. Pharmacol."},{"key":"B147","doi-asserted-by":"publisher","first-page":"138","DOI":"10.4103\/0972-2327.144284","article-title":"Toxic species in amyloid disorders: oligomers or mature fibrils.","volume":"18","author":"Verma","year":"2015","journal-title":"Ann. Ind. Acad. Neurol."},{"key":"B148","doi-asserted-by":"publisher","first-page":"104727","DOI":"10.1016\/j.archoralbio.2020.104727","article-title":"Efficacy of green tea and its extract, epigallocatechin-3-gallate, in the reduction of cariogenic microbiota in children: a randomized clinical trial.","volume":"114","author":"Vilela","year":"2020","journal-title":"Arch. Oral Biol."},{"key":"B149","doi-asserted-by":"publisher","first-page":"2694","DOI":"10.1021\/jf0730338","article-title":"Reaction kinetics of degradation and epimerization of epigallocatechin gallate (EGCG) in aqueous system over a wide temperature range.","volume":"56","author":"Wang","year":"2008","journal-title":"J. Agricult. Food Chem."},{"key":"B150","doi-asserted-by":"publisher","first-page":"5803","DOI":"10.1021\/jp209406t","article-title":"Thermodynamic analysis of the molecular interactions between amyloid \u03b2-protein fragments and (-)-epigallocatechin-3-gallate.","volume":"116","author":"Wang","year":"2012","journal-title":"J. Physic. Chem. B"},{"key":"B151","doi-asserted-by":"publisher","first-page":"11576","DOI":"10.1021\/jp1001435","article-title":"Thermodynamic analysis of the molecular interactions between amyloid beta-peptide 42 and (-)-epigallocatechin-3-gallate.","volume":"114","author":"Wang","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"B152","doi-asserted-by":"publisher","first-page":"3893","DOI":"10.1016\/j.jmb.2017.10.006","article-title":"Aggregation of A\u03b2(17-36) in the presence of naturally occurring phenolic inhibitors using coarse-grained simulations.","volume":"429","author":"Wang","year":"2017","journal-title":"J. Mol. Biol."},{"key":"B153","doi-asserted-by":"publisher","first-page":"2641","DOI":"10.1016\/S0140-6736(15)01274-X","article-title":"Systemic amyloidosis.","volume":"387","author":"Wechalekar","year":"2016","journal-title":"Lancet"},{"key":"B154","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1111\/nyas.13350","article-title":"Structure, bioactivity, and synthesis of methylated flavonoids.","volume":"1398","author":"Wen","year":"2017","journal-title":"Ann. N Y. Acad. Sci."},{"key":"B155","doi-asserted-by":"publisher","first-page":"33313","DOI":"10.1074\/jbc.M706024200","article-title":"Fe65 stimulates proteolytic liberation of the beta-amyloid precursor protein intracellular domain.","volume":"282","author":"Wiley","year":"2007","journal-title":"J. Biol. Chem."},{"key":"B156","doi-asserted-by":"publisher","first-page":"2788","DOI":"10.1007\/s11064-016-1995-9","article-title":"epigallocatechin gallate (egcg) inhibits alpha-synuclein aggregation: a potential agent for Parkinson\u2019s Disease.","volume":"41","author":"Xu","year":"2016","journal-title":"Neurochem. Res."},{"key":"B157","doi-asserted-by":"publisher","first-page":"1511","DOI":"10.1248\/bpb.b20-00262","article-title":"oroxylin a exerts its antitumor effects in human gallbladder cancer via inhibition of the PTEN\/PI3K\/AKT signaling pathway.","volume":"43","author":"Xuan","year":"2020","journal-title":"Biol. Pharmaceut. Bull."},{"key":"B158","doi-asserted-by":"publisher","first-page":"BSR20181415","DOI":"10.1042\/BSR20181415","article-title":"Congo Red and amyloids: history and relationship.","volume":"39","author":"Yakupova","year":"2019","journal-title":"Biosci. Rep."},{"key":"B159","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1016\/j.aninu.2020.01.001","article-title":"Antioxidant mechanism of tea polyphenols and its impact on health benefits.","volume":"6","author":"Yan","year":"2020","journal-title":"Anim. Nutrit."},{"key":"B160","doi-asserted-by":"publisher","first-page":"17945","DOI":"10.1038\/s41598-017-18349-z","article-title":"EGCG-mediated protection of the membrane disruption and cytotoxicity caused by the \u2018active oligomer\u2019 of \u03b1-synuclein.","volume":"7","author":"Yang","year":"2017","journal-title":"Sci. Rep."},{"key":"B161","doi-asserted-by":"publisher","first-page":"4351","DOI":"10.1021\/acschemneuro.0c00598","article-title":"epigallocatechin gallate destabilizes \u03b1-synuclein fibril by disrupting the E46-K80 salt-bridge and inter-protofibril interface.","volume":"11","author":"Yao","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"B162","doi-asserted-by":"publisher","first-page":"2590","DOI":"10.3390\/ijms14022590","article-title":"Partial peptide of \u03b1-synuclein modified with small-molecule inhibitors specifically inhibits amyloid fibrillation of \u03b1-synuclein.","volume":"14","author":"Yoshida","year":"2013","journal-title":"Int. J. Mol. Sci."},{"key":"B163","doi-asserted-by":"publisher","first-page":"1437","DOI":"10.1073\/pnas.94.4.1437","article-title":"Regulation of DNA damage-induced apoptosis by the c-Abl tyrosine kinase.","volume":"94","author":"Yuan","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"B164","doi-asserted-by":"publisher","first-page":"1841","DOI":"10.1021\/acschemneuro.0c00277","article-title":"Green tea extracts EGCG and EGC display distinct mechanisms in disrupting A\u03b242 protofibril.","volume":"11","author":"Zhan","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"B165","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1039\/c3mt20106f","article-title":"Electroanalysis of the interaction between (-)-epigallocatechin-3-gallate (EGCG) and amyloid-\u03b2 in the presence of copper.","volume":"5","author":"Zhang","year":"2013","journal-title":"Metallomics Integr. Biomet. Sci."},{"key":"B166","doi-asserted-by":"publisher","first-page":"8475","DOI":"10.1021\/am501341u","article-title":"Epigallocatechin-3-gallate (EGCG)-stabilized selenium nanoparticles coated with Tet-1 peptide to reduce amyloid-\u03b2 aggregation and cytotoxicity.","volume":"6","author":"Zhang","year":"2014","journal-title":"ACS Appl. Mater. Interf."},{"key":"B167","doi-asserted-by":"publisher","first-page":"3993","DOI":"10.1021\/jp312573y","article-title":"Molecular mechanism of the inhibition of EGCG on the Alzheimer A\u03b2(1-42) dimer.","volume":"117","author":"Zhang","year":"2013","journal-title":"J. Phys. Chemist. B"},{"key":"B168","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1007\/s12035-013-8491-x","article-title":"Involvement of \u03b17 nAChR signaling cascade in epigallocatechin gallate suppression of \u03b2-amyloid-induced apoptotic cortical neuronal insults.","volume":"49","author":"Zhang","year":"2014","journal-title":"Mol. Neurobiol."},{"key":"B169","doi-asserted-by":"publisher","first-page":"468","DOI":"10.1007\/s11064-016-2093-8","article-title":"Epigallocatechin gallate attenuates \u03b2-amyloid generation and oxidative stress involvement of PPAR\u03b3 in N2a\/APP695 cells.","volume":"42","author":"Zhang","year":"2017","journal-title":"Neurochemic. Res."},{"key":"B170","doi-asserted-by":"publisher","first-page":"136","DOI":"10.1111\/jnc.14142","article-title":"Metal chelator EGCG attenuates Fe(III)-induced conformational transition of \u03b1-synuclein and protects AS-PC12 cells against Fe(III)-induced death.","volume":"143","author":"Zhao","year":"2017","journal-title":"J. Neurochem."}],"container-title":["Frontiers in Neuroscience"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fnins.2021.718188\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,14]],"date-time":"2021-09-14T08:30:30Z","timestamp":1631608230000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fnins.2021.718188\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,9,14]]},"references-count":170,"alternative-id":["10.3389\/fnins.2021.718188"],"URL":"https:\/\/doi.org\/10.3389\/fnins.2021.718188","relation":{},"ISSN":["1662-453X"],"issn-type":[{"value":"1662-453X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,9,14]]},"article-number":"718188"}}