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Biol."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0365","first-page":"2515","article-title":"Tetrazolium-based assays for cellular viability: a critical examination of selected parameters affecting formazan production","volume":"51","author":"Vistica","year":"1991","journal-title":"Cancer Res."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0370","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/s12551-021-00778-w","article-title":"Protein aggregation: in silico algorithms and applications","volume":"13","author":"Prabakaran","year":"2021","journal-title":"Biophys. 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Sin."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0400","doi-asserted-by":"crossref","DOI":"10.1063\/1.4921071","article-title":"In vitro fibrillization of Alzheimer\u2019s amyloid-\u03b2 peptide (1\u201342)","volume":"5","author":"Tiiman","year":"2015","journal-title":"AIP Adv."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0405","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1002\/psc.2513","article-title":"Effect of agitation on the peptide fibrillization: Alzheimer\u2019s amyloid- \u03b2 peptide 1\u201342 but not amylin and insulin fibrils can grow under quiescent conditions","volume":"19","author":"Tiiman","year":"2013","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0410","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1146\/annurev-pathol-011110-130242","article-title":"Parkinson\u2019s disease: genetics and pathogenesis","volume":"6","author":"Shulman","year":"2011","journal-title":"Annu. Rev. Pathol. Mech. Dis."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0415","doi-asserted-by":"crossref","first-page":"6469","DOI":"10.1073\/pnas.95.11.6469","article-title":"Alpha-synuclein in filamentous inclusions of lewy bodies from Parkinson\u2019s disease and dementia with lewy bodies","volume":"95","author":"Spillantini","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0420","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1136\/jnnp.51.6.745","article-title":"The relevance of the lewy body to the pathogenesis of idiopathic Parkinson\u2019s disease","volume":"51","author":"Gibb","year":"1988","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0425","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/nrn3406","article-title":"The many faces of \u03b1-synuclein: from structure and toxicity to therapeutic target","volume":"14","author":"Lashuel","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0430","doi-asserted-by":"crossref","first-page":"32486","DOI":"10.1074\/jbc.M110.139576","article-title":"Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins","volume":"285","author":"Varkey","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0435","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1186\/s13024-019-0329-1","article-title":"Alpha-synuclein structure and Parkinson\u2019s disease \u2013 lessons and emerging principles","volume":"14","author":"Meade","year":"2019","journal-title":"Mol. 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Pharm. Anal."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0460","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.3390\/molecules27031021","article-title":"Molecular mechanisms of amylin turnover, misfolding and toxicity in the pancreas","volume":"27","author":"Bhowmick","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0465","doi-asserted-by":"crossref","first-page":"2154","DOI":"10.1210\/me.2004-0407","article-title":"Processing of pro-islet amyloid polypeptide in the constitutive and regulated secretory pathways of \u03b2 cells","volume":"19","author":"Marzban","year":"2005","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0470","doi-asserted-by":"crossref","first-page":"181","DOI":"10.2174\/1389450053174596","article-title":"Pancreatic amylin as a centrally acting satiating hormone","volume":"6","author":"Lutz","year":"2005","journal-title":"Curr. 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Med."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0490","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2020.00035","article-title":"Islet amyloid polypeptide: a partner in crime with A\u03b2 in the pathology of Alzheimer\u2019s disease","volume":"13","author":"Raimundo","year":"2020","journal-title":"Front. Mol. 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Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0520","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1021\/ar050070g","article-title":"Normal and aberrant biological self-assembly: insights from studies of human lysozyme and its amyloidogenic variants","volume":"39","author":"Dumoulin","year":"2006","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0525","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/B978-0-12-386483-3.00003-3","article-title":"Lysozyme: a model protein for amyloid research","volume":"84","author":"Swaminathan","year":"2011","journal-title":"Adv. Protein Chem. Struct. Biol."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0530","doi-asserted-by":"crossref","first-page":"1362","DOI":"10.1021\/bm0498979","article-title":"Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme","volume":"5","author":"Vernaglia","year":"2004","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0535","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/385787a0","article-title":"Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis","volume":"385","author":"Booth","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0540","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.ejmech.2018.02.035","article-title":"Secretase inhibitors for the treatment of Alzheimer\u2019s disease: long road ahead","volume":"148","author":"Kumar","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0545","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/nrd1468","article-title":"Drug repositioning: identifying and developing new uses for existing drugs","volume":"3","author":"Ashburn","year":"2004","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0550","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1007\/s13311-014-0325-7","article-title":"Drug repositioning approaches for the discovery of new therapeutics for Alzheimer\u2019s disease","volume":"12","author":"Kim","year":"2015","journal-title":"Neurotherapeutics"},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0555","doi-asserted-by":"crossref","DOI":"10.4155\/fso.15.73","article-title":"The case of galantamine: repurposing and late blooming of a cholinergic drug","volume":"1","author":"Mucke","year":"2015","journal-title":"Futur. Sci. OA"},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0560","doi-asserted-by":"crossref","first-page":"183","DOI":"10.2174\/1567205016666190228123923","article-title":"Synthesis of new galanthamine-peptide derivatives designed for prevention and treatment of Alzheimer\u2019s disease","volume":"16","author":"Vezenkov","year":"2019","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0565","article-title":"Amantadine in Parkinson\u2019s disease","author":"Crosby","year":"2003","journal-title":"Cochrane Database Syst. 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Treat."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0585","article-title":"Tamoxifen for amyotrophic lateral sclerosis: a randomized double-blind clinical trial","volume":"99","author":"Chen","year":"2020","journal-title":"Medicine (Baltimore)"},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0590","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1002\/jnr.10611","article-title":"Glucagon-like peptide-1 decreases endogenous amyloid-beta peptide (Abeta) levels and protects hippocampal neurons from death induced by abeta and iron","volume":"72","author":"Perry","year":"2003","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0595","doi-asserted-by":"crossref","first-page":"6587","DOI":"10.1523\/JNEUROSCI.0529-11.2011","article-title":"The diabetes drug liraglutide prevents degenerative processes in a mouse model of Alzheimer\u2019s disease","volume":"31","author":"McClean","year":"2011","journal-title":"J. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0600","doi-asserted-by":"crossref","first-page":"623","DOI":"10.3233\/JAD-130584","article-title":"The neuroprotection of liraglutide on alzheimer-like learning and memory impairment by modulating the hyperphosphorylation of tau and neurofilament proteins and insulin signaling pathways in mice","volume":"37","author":"Xiong","year":"2013","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0605","doi-asserted-by":"crossref","first-page":"451","DOI":"10.3233\/JPD-171192","article-title":"Is exenatide a treatment for Parkinson\u2019s disease?","volume":"7","author":"Athauda","year":"2017","journal-title":"J. Parkinsons. Dis."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0610","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2018.00224","article-title":"Can an infection hypothesis explain the Beta amyloid hypothesis of Alzheimer\u2019s disease?","volume":"10","author":"Fulop","year":"2018","journal-title":"Front. 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Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0640","doi-asserted-by":"crossref","first-page":"1568","DOI":"10.1093\/brain\/aww042","article-title":"Rifampicin is a candidate preventive medicine against amyloid-\u03b2 and tau oligomers","volume":"139","author":"Umeda","year":"2016","journal-title":"Brain"},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0645","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/j.1532-5415.2004.52109.x","article-title":"A randomized, controlled trial of doxycycline and rifampin for patients with Alzheimer\u2019s disease","volume":"52","author":"Loeb","year":"2004","journal-title":"J. Am. Geriatr. Soc."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0650","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.bcp.2017.04.004","article-title":"Natural product-based amyloid inhibitors","volume":"139","author":"Velander","year":"2017","journal-title":"Biochem. 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Chem."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0665","doi-asserted-by":"crossref","DOI":"10.1016\/j.brainres.2019.146476","article-title":"The effect of curcumin on cognition in Alzheimer\u2019s disease and healthy aging: a systematic review of pre-clinical and clinical studies","volume":"1725","author":"Voulgaropoulou","year":"2019","journal-title":"Brain Res."},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0670","doi-asserted-by":"crossref","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":"10.1016\/j.ijbiomac.2022.11.031_bb0675","doi-asserted-by":"crossref","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":"10.1016\/j.ijbiomac.2022.11.031_bb0680","doi-asserted-by":"crossref","first-page":"330","DOI":"10.3390\/life12030330","article-title":"Impact of caffeine on Alzheimer\u2019s disease pathogenesis\u2014protective or risk factor?","volume":"12","author":"Schreiner","year":"2022","journal-title":"Life"},{"key":"10.1016\/j.ijbiomac.2022.11.031_bb0685","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20081829","article-title":"Recent developments in metal-based drugs and chelating agents for neurodegenerative diseases treatments","volume":"20","author":"Sales","year":"2019","journal-title":"Int. J. Mol. 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