{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T19:25:55Z","timestamp":1791141955836,"version":"4.1.0"},"reference-count":187,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2013,10,1]],"date-time":"2013-10-01T00:00:00Z","timestamp":1380585600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100012166","name":"National Basic Research Program of China","doi-asserted-by":"crossref","award":["2009BC918304"],"award-info":[{"award-number":["2009BC918304"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100012166","name":"National Basic Research Program of China","doi-asserted-by":"crossref","award":["2012CB524901"],"award-info":[{"award-number":["2012CB524901"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["30970607"],"award-info":[{"award-number":["30970607"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["31271370"],"award-info":[{"award-number":["31271370"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81100687"],"award-info":[{"award-number":["81100687"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81172971"],"award-info":[{"award-number":["81172971"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81222043"],"award-info":[{"award-number":["81222043"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100004602","name":"Program for New Century Excellent Talents in University","doi-asserted-by":"crossref","award":["NECT10-0623"],"award-info":[{"award-number":["NECT10-0623"]}],"id":[{"id":"10.13039\/501100004602","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100004602","name":"Program for New Century Excellent Talents in University","doi-asserted-by":"crossref","award":["NECT11-0170"],"award-info":[{"award-number":["NECT11-0170"]}],"id":[{"id":"10.13039\/501100004602","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"published-print":{"date-parts":[[2013,10]]},"DOI":"10.1016\/j.bbagen.2013.06.029","type":"journal-article","created":{"date-parts":[[2013,6,29]],"date-time":"2013-06-29T10:47:09Z","timestamp":1372502829000},"page":"4860-4871","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":190,"title":["Inhibiting toxic aggregation of amyloidogenic proteins: A therapeutic strategy for protein misfolding diseases"],"prefix":"10.1016","volume":"1830","author":[{"given":"Biao","family":"Cheng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hao","family":"Gong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hongwen","family":"Xiao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert B.","family":"Petersen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ling","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kun","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbagen.2013.06.029_bb0005","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1146\/annurev.neuro.26.010302.081142","article-title":"Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders","volume":"26","author":"Caughey","year":"2003","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0010","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1021\/cb400080f","article-title":"Untangling amyloid-beta, tau, and metals in Alzheimer's disease","volume":"8","author":"Savelieff","year":"2013","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0015","first-page":"630182","article-title":"Amyloid beta and tau proteins as therapeutic targets for Alzheimer's disease treatment: rethinking the current strategy","volume":"2012","author":"Mondragon-Rodriguez","year":"2012","journal-title":"Int. J. Alzheimers Dis."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0020","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1001\/archneur.55.2.151","article-title":"Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: implications for the pathogenesis of Parkinson disease and Lewy body dementia","volume":"55","author":"Trojanowski","year":"1998","journal-title":"Arch. Neurol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0025","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/362553a0","article-title":"Human lysozyme gene mutations cause hereditary systemic amyloidosis","volume":"362","author":"Pepys","year":"1993","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0030","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1073\/pnas.84.11.3881","article-title":"Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells","volume":"84","author":"Westermark","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0035","doi-asserted-by":"crossref","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":"10.1016\/j.bbagen.2013.06.029_bb0040","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1146\/annurev.neuro.29.051605.113042","article-title":"Trinucleotide repeat disorders","volume":"30","author":"Orr","year":"2007","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0045","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S0959-440X(96)80089-3","article-title":"Alternative conformations of amyloidogenic proteins govern their behavior","volume":"6","author":"Kelly","year":"1996","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0050","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/0092-8674(93)90635-4","article-title":"Seeding \u201cone-dimensional crystallization\u201d of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?","volume":"73","author":"Jarrett","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0055","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1126\/science.1178250","article-title":"An analytical solution to the kinetics of breakable filament assembly","volume":"326","author":"Knowles","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0060","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1016\/j.bbapap.2005.10.021","article-title":"Probing the pressure\u2013temperature stability of amyloid fibrils provides new insights into their molecular properties","volume":"1764","author":"Meersman","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0065","doi-asserted-by":"crossref","first-page":"12142","DOI":"10.1016\/S0021-9258(17)38998-6","article-title":"Effect of divalent metal ions and pH upon the binding reactivity of human serum amyloid P component, a C-reactive protein homologue, for zymosan. Preferential reactivity in the presence of copper and acidic pH","volume":"260","author":"Potempa","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0940","doi-asserted-by":"crossref","DOI":"10.1002\/prot.24338","article-title":"Disulfide bonds in amyloidogenesis diseases related proteins","author":"Li","year":"2013","journal-title":"Proteins"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0075","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.sbi.2006.01.011","article-title":"Protein aggregation and amyloidosis: confusion of the kinds?","volume":"16","author":"Rousseau","year":"2006","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0080","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1006\/jmbi.2001.4970","article-title":"Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis","volume":"312","author":"Kirkitadze","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0085","doi-asserted-by":"crossref","first-page":"40186","DOI":"10.1074\/jbc.M305326200","article-title":"The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation","volume":"278","author":"Zhu","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0090","doi-asserted-by":"crossref","first-page":"9496","DOI":"10.1021\/bi060579z","article-title":"Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide","volume":"45","author":"Knight","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0095","doi-asserted-by":"crossref","first-page":"18223","DOI":"10.1021\/ja1069882","article-title":"Mechanistic studies of peptide self-assembly: transient alpha-helices to stable beta-sheets","volume":"132","author":"Liu","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0100","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1093\/protein\/gzp036","article-title":"A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides","volume":"22","author":"Abedini","year":"2009","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0105","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.bbrc.2012.05.013","article-title":"Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling alpha-helix","volume":"422","author":"Sparks","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0110","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1146\/annurev.biochem.66.1.385","article-title":"Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins","volume":"66","author":"Harper","year":"1997","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0115","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S0033583598003400","article-title":"From the globular to the fibrous state: protein structure and structural conversion in amyloid formation","volume":"31","author":"Sunde","year":"1998","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0120","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0968-0004(99)01445-0","article-title":"Protein misfolding, evolution and disease","volume":"24","author":"Dobson","year":"1999","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0125","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1096\/fj.01-0442hyp","article-title":"A possible role for pi-stacking in the self-assembly of amyloid fibrils","volume":"16","author":"Gazit","year":"2002","journal-title":"FASEB J."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0130","doi-asserted-by":"crossref","first-page":"8545","DOI":"10.1074\/jbc.271.15.8545","article-title":"Arrest of beta-amyloid fibril formation by a pentapeptide ligand","volume":"271","author":"Tjernberg","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0135","doi-asserted-by":"crossref","first-page":"1898","DOI":"10.1002\/pro.5560070906","article-title":"Effects of salt bridges on protein structure and design","volume":"7","author":"Sindelar","year":"1998","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0140","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1016\/0022-2836(92)90835-8","article-title":"Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides","volume":"228","author":"Hilbich","year":"1992","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0145","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1021\/cn3000247","article-title":"A key role for lysine residues in amyloid beta-protein folding, assembly, and toxicity","volume":"3","author":"Sinha","year":"2012","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0150","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1111\/j.1432-1033.1997.t01-2-00355.x","article-title":"Characterization of the interactions of Alzheimer beta-amyloid peptides with phospholipid membranes","volume":"245","author":"McLaurin","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0155","doi-asserted-by":"crossref","first-page":"1380","DOI":"10.1111\/j.1742-4658.2010.07571.x","article-title":"Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states","volume":"277","author":"Lindgren","year":"2010","journal-title":"FEBS J."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0160","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1016\/j.bbamem.2007.01.022","article-title":"Membrane interaction of islet amyloid polypeptide","volume":"1768","author":"Jayasinghe","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0165","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1002\/(SICI)1097-0282(1998)47:6<451::AID-BIP4>3.0.CO;2-F","article-title":"Mode of action of linear amphipathic alpha-helical antimicrobial peptides","volume":"47","author":"Oren","year":"1998","journal-title":"Biopolymers"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0170","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1016\/j.biochi.2010.12.012","article-title":"A mechanistic approach for islet amyloid polypeptide aggregation to develop anti-amyloidogenic agents for type-2 diabetes","volume":"93","author":"Ahmad","year":"2011","journal-title":"Biochimie"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0175","doi-asserted-by":"crossref","first-page":"11479","DOI":"10.1021\/bi00036a021","article-title":"Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles","volume":"34","author":"Gazit","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0180","doi-asserted-by":"crossref","first-page":"12416","DOI":"10.1021\/bi00164a017","article-title":"Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes","volume":"31","author":"Pouny","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0185","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/0006-8993(95)00148-J","article-title":"Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium","volume":"676","author":"Mattson","year":"1995","journal-title":"Brain Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0190","doi-asserted-by":"crossref","first-page":"507","DOI":"10.2174\/1568026013394822","article-title":"Production of reactive oxygen species from aggregating proteins implicated in Alzheimer's disease, Parkinson's disease and other neurodegenerative diseases","volume":"1","author":"Tabner","year":"2001","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0195","doi-asserted-by":"crossref","first-page":"7609","DOI":"10.1021\/bi990438f","article-title":"The A beta peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction","volume":"38","author":"Huang","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0945","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1016\/S0891-5849(01)00513-5","article-title":"Alpha-synuclein implicated in Parkinson's disease catalyses the formation of hydrogen peroxide in vitro","volume":"30","author":"Turnbull","year":"2001","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0205","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S0304-3940(02)01254-5","article-title":"Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126","volume":"336","author":"Turnbull","year":"2003","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0210","doi-asserted-by":"crossref","first-page":"1570","DOI":"10.1016\/j.bbapap.2008.08.007","article-title":"Polyphenol-induced dissociation of various amyloid fibrils results in a methionine-independent formation of ROS","volume":"1784","author":"Shoval","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0215","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1042\/BST0361293","article-title":"Metal-dependent generation of reactive oxygen species from amyloid proteins implicated in neurodegenerative disease","volume":"36","author":"Allsop","year":"2008","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0220","doi-asserted-by":"crossref","first-page":"e54198","DOI":"10.1371\/journal.pone.0054198","article-title":"Bisphenol A accelerates toxic amyloid formation of human islet amyloid polypeptide: a possible link between bisphenol A exposure and type 2 diabetes","volume":"8","author":"Gong","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0225","doi-asserted-by":"crossref","first-page":"8134","DOI":"10.1021\/bi1010909","article-title":"Redox reactions of the alpha-synuclein-Cu(2+) complex and their effects on neuronal cell viability","volume":"49","author":"Wang","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0230","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.jinorgbio.2009.11.005","article-title":"Binding of alpha-synuclein with Fe(III) and with Fe(II) and biological implications of the resultant complexes","volume":"104","author":"Peng","year":"2010","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0235","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1097\/01.jnen.0000228136.58062.bf","article-title":"Involvement of oxidative stress in Alzheimer disease","volume":"65","author":"Nunomura","year":"2006","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0240","doi-asserted-by":"crossref","first-page":"12737","DOI":"10.1021\/bi701079z","article-title":"Three histidine residues of amyloid-beta peptide control the redox activity of copper and iron","volume":"46","author":"Nakamura","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0245","doi-asserted-by":"crossref","first-page":"114","DOI":"10.2174\/138945013804806532","article-title":"Molecular mechanism aspect of ER stress in Alzheimer's disease: current approaches and future strategies","volume":"14","author":"Ansari","year":"2013","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0250","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.molmed.2012.12.005","article-title":"An ERcentric view of Parkinson's disease","volume":"19","author":"Mercado","year":"2013","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0255","doi-asserted-by":"crossref","first-page":"E1656","DOI":"10.1152\/ajpendo.00318.2007","article-title":"Induction of endoplasmic reticulum stress-induced beta-cell apoptosis and accumulation of polyubiquitinated proteins by human islet amyloid polypeptide","volume":"293","author":"Huang","year":"2007","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0260","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1002\/jnr.22640","article-title":"Intraneuronal amyloid beta oligomers cause cell death via endoplasmic reticulum stress, endosomal\/lysosomal leakage, and mitochondrial dysfunction in vivo","volume":"89","author":"Umeda","year":"2011","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0265","doi-asserted-by":"crossref","first-page":"467","DOI":"10.3233\/JAD-2011-110326","article-title":"Caspase-12 activation is involved in amyloid-beta protein-induced synaptic toxicity","volume":"26","author":"Quiroz-Baez","year":"2011","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0270","doi-asserted-by":"crossref","first-page":"735206","DOI":"10.1155\/2012\/735206","article-title":"Mitochondrial- and endoplasmic reticulum-associated oxidative stress in Alzheimer's disease: from pathogenesis to biomarkers","volume":"2012","author":"Ferreiro","year":"2012","journal-title":"Int. J. Cell Biol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0275","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/j.biocel.2010.12.008","article-title":"Involvement of mitochondrial dysfunction in human islet amyloid polypeptide-induced apoptosis in INS-1E pancreatic beta cells: an effect attenuated by phycocyanin","volume":"43","author":"Li","year":"2011","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0280","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1002\/biof.159","article-title":"Mitochondria, calcium, and endoplasmic reticulum stress in Parkinson's disease","volume":"37","author":"Cali","year":"2011","journal-title":"Biofactors"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0285","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/j.bbagen.2009.08.003","article-title":"Mitochondrial mechanisms in amyloid beta peptide-induced cerebrovascular degeneration","volume":"1800","author":"Hsu","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0290","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1385\/NMM:4:1-2:21","article-title":"Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases","volume":"4","author":"Hashimoto","year":"2003","journal-title":"Neuromolecular Med."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0295","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1096\/fj.00-0561fje","article-title":"Functional mitochondria are required for amyloid beta-mediated neurotoxicity","volume":"15","author":"Cardoso","year":"2001","journal-title":"FASEB J."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0950","series-title":"World Alzheimer Report 2009","author":"Ferri","year":"2009"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0305","series-title":"Diabetes Mellitus","author":"Global Burden of Disease","year":"2008"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0310","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1080\/15228940802142720","article-title":"Polyphenol and phytosterol composition in an antibacterial extract from Rhizophora mangle L. bark","volume":"7","author":"Sanchez Perera","year":"2007","journal-title":"J. Herb. Pharmacother."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0315","doi-asserted-by":"crossref","first-page":"3664","DOI":"10.1529\/biophysj.106.081877","article-title":"Phenol red interacts with the protofibril-like oligomers of an amyloidogenic hexapeptide NFGAIL through both hydrophobic and aromatic contacts","volume":"91","author":"Wu","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0320","doi-asserted-by":"crossref","first-page":"11879","DOI":"10.1021\/jp202640b","article-title":"Molecular insight into conformational transition of amyloid beta-peptide 42 inhibited by (\u2212)-epigallocatechin-3-gallate probed by molecular simulations","volume":"115","author":"Liu","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0325","doi-asserted-by":"crossref","first-page":"2115","DOI":"10.1096\/fj.07-099671","article-title":"Molecular and cellular aspects of protein misfolding and disease","volume":"22","author":"Herczenik","year":"2008","journal-title":"FASEB J."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0330","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.brainresbull.2011.11.014","article-title":"Antioxidant properties of natural polyphenols and their therapeutic potentials for Alzheimer's disease","volume":"87","author":"Choi","year":"2012","journal-title":"Brain Res. Bull."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0335","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/j.jnutbio.2004.05.002","article-title":"Neurological mechanisms of green tea polyphenols in Alzheimer's and Parkinson's diseases","volume":"15","author":"Weinreb","year":"2004","journal-title":"J. Nutr. Biochem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0340","doi-asserted-by":"crossref","first-page":"34933","DOI":"10.1074\/jbc.M204672200","article-title":"Epigallocatechin gallate, a constituent of green tea, represses hepatic glucose production","volume":"277","author":"Waltner-Law","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0345","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1002\/mnfr.200500102","article-title":"Anti-obesity effects of green tea: from bedside to bench","volume":"50","author":"Wolfram","year":"2006","journal-title":"Mol. Nutr. Food Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0350","doi-asserted-by":"crossref","first-page":"211","DOI":"10.3233\/JAD-2008-15207","article-title":"Cell signaling pathways and iron chelation in the neurorestorative activity of green tea polyphenols: special reference to epigallocatechin gallate (EGCG)","volume":"15","author":"Mandel","year":"2008","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0355","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.bbagen.2013.06.029_bb0360","doi-asserted-by":"crossref","first-page":"8127","DOI":"10.1021\/bi100939a","article-title":"The flavanol (\u2212)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity","volume":"49","author":"Meng","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0365","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1111\/j.1747-0285.2005.00318.x","article-title":"Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism","volume":"67","author":"Porat","year":"2006","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0370","doi-asserted-by":"crossref","first-page":"e29933","DOI":"10.1371\/journal.pone.0029933","article-title":"Epigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidosis: \u201cin vivo\u201d evidence from FAP mice models","volume":"7","author":"Ferreira","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0375","doi-asserted-by":"crossref","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":"10.1016\/j.bbagen.2013.06.029_bb0380","doi-asserted-by":"crossref","first-page":"1987","DOI":"10.3945\/jn.109.109785","article-title":"Green tea (\u2212)-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. Nutr."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0385","doi-asserted-by":"crossref","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":"10.1016\/j.bbagen.2013.06.029_bb0390","doi-asserted-by":"crossref","first-page":"4627","DOI":"10.1158\/1078-0432.CCR-04-2549","article-title":"Effects of dosing condition on the oral bioavailability of green tea catechins after single-dose administration of Polyphenon E in healthy individuals","volume":"11","author":"Chow","year":"2005","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0955","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.ejphar.2005.12.024","article-title":"(\u2212)-Epigallocatechin gallate attenuates acute stress responses through GABAergic system in the brain","volume":"531","author":"Adachi","year":"2006","journal-title":"Eur. J. Pharmacol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0400","doi-asserted-by":"crossref","first-page":"679","DOI":"10.3177\/jnsv.43.679","article-title":"Absorption and distribution of tea catechin, (\u2212)-epigallocatechin-3-gallate, in the rat","volume":"43","author":"Nakagawa","year":"1997","journal-title":"J. Nutr. Sci. Vitaminol. (Tokyo)"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0405","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1007\/s00018-008-7452-4","article-title":"Curcumin: from ancient medicine to current clinical trials","volume":"65","author":"Hatcher","year":"2008","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0410","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1093\/aje\/kwj267","article-title":"Curry consumption and cognitive function in the elderly","volume":"164","author":"Ng","year":"2006","journal-title":"Am. J. Epidemiol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0415","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1002\/jnr.20025","article-title":"Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro","volume":"75","author":"Ono","year":"2004","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0420","doi-asserted-by":"crossref","first-page":"118","DOI":"10.3109\/13506129.2010.530008","article-title":"The effect of curcumin on human islet amyloid polypeptide misfolding and toxicity","volume":"17","author":"Daval","year":"2010","journal-title":"Amyloid"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0425","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1007\/s00401-007-0332-4","article-title":"Curcumin inhibits aggregation of alpha-synuclein","volume":"115","author":"Pandey","year":"2008","journal-title":"Acta Neuropathol."},{"issue":"Suppl. 1","key":"10.1016\/j.bbagen.2013.06.029_bb0430","doi-asserted-by":"crossref","first-page":"39","DOI":"10.3109\/13506129.2012.668502","article-title":"Natural polyphenols as modulators of TTR amyloidogenesis: in vitro and in vivo evidences towards therapy","volume":"19","author":"Ferreira","year":"2012","journal-title":"Amyloid"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0435","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.bpc.2009.06.010","article-title":"Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme","volume":"144","author":"Wang","year":"2009","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0440","doi-asserted-by":"crossref","first-page":"5967","DOI":"10.1016\/j.bmc.2011.08.052","article-title":"Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid beta-protein fibrils","volume":"19","author":"Masuda","year":"2011","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0445","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.jchromb.2007.03.010","article-title":"Oral bioavailability of curcumin in rat and the herbal analysis from Curcuma longa by LC\u2212MS\/MS","volume":"853","author":"Yang","year":"2007","journal-title":"J. Chromatogr. B Analyt. Technol. Biomed. Life Sci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0450","doi-asserted-by":"crossref","first-page":"5892","DOI":"10.1074\/jbc.M404751200","article-title":"Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo","volume":"280","author":"Yang","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0455","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1046\/j.1471-4159.2003.01976.x","article-title":"Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease","volume":"87","author":"Ono","year":"2003","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0460","doi-asserted-by":"crossref","first-page":"14631","DOI":"10.1074\/jbc.M111.325456","article-title":"Phenolic compounds prevent amyloid beta-protein oligomerization and synaptic dysfunction by site-specific binding","volume":"287","author":"Ono","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0465","doi-asserted-by":"crossref","first-page":"2557","DOI":"10.2353\/ajpath.2009.090417","article-title":"Phenolic compounds prevent Alzheimer's pathology through different effects on the amyloid-beta aggregation pathway","volume":"175","author":"Hamaguchi","year":"2009","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0960","doi-asserted-by":"crossref","first-page":"349","DOI":"10.33588\/rn.5406.2011611","article-title":"Resveratrol: a neuroprotective polyphenol in the Mediterranean diet","volume":"54","author":"Lopez-Miranda","year":"2012","journal-title":"Rev. Neurol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0475","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1016\/j.neuro.2009.08.013","article-title":"Resveratrol inhibits beta-amyloid oligomeric cytotoxicity but does not prevent oligomer formation","volume":"30","author":"Feng","year":"2009","journal-title":"Neurotoxicology"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0480","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1016\/j.febslet.2009.03.059","article-title":"Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol","volume":"583","author":"Radovan","year":"2009","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0485","doi-asserted-by":"crossref","first-page":"1550","DOI":"10.1016\/j.bpj.2011.02.010","article-title":"Resveratrol inhibits the formation of multiple-layered beta-sheet oligomers of the human islet amyloid polypeptide segment 22\u201327","volume":"100","author":"Jiang","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0490","doi-asserted-by":"crossref","first-page":"24228","DOI":"10.1074\/jbc.M110.133108","article-title":"Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Abeta into off-pathway conformers","volume":"285","author":"Ladiwala","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0495","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.jpba.2011.10.023","article-title":"Determination of resveratrol and its sulfate and glucuronide metabolites in plasma by LC\u2013MS\/MS and their pharmacokinetics in dogs","volume":"59","author":"Muzzio","year":"2012","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0500","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1001\/jama.291.10.1213","article-title":"Coffee consumption and risk of type 2 diabetes mellitus among middle-aged Finnish men and women","volume":"291","author":"Tuomilehto","year":"2004","journal-title":"JAMA"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0505","doi-asserted-by":"crossref","first-page":"2196","DOI":"10.1093\/jn\/137.10.2196","article-title":"Chlorogenic acid compounds from coffee are differentially absorbed and metabolized in humans","volume":"137","author":"Monteiro","year":"2007","journal-title":"J. Nutr."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0510","doi-asserted-by":"crossref","first-page":"13147","DOI":"10.1021\/jf201702h","article-title":"Coffee components inhibit amyloid formation of human islet amyloid polypeptide in vitro: possible link between coffee consumption and diabetes mellitus","volume":"59","author":"Cheng","year":"2011","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0515","doi-asserted-by":"crossref","first-page":"14454","DOI":"10.1021\/bi048582a","article-title":"Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions","volume":"43","author":"Porat","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0520","doi-asserted-by":"crossref","first-page":"210","DOI":"10.4161\/isl.1.3.9609","article-title":"Targeting insulin amyloid assembly by small aromatic molecules: toward rational design of aggregation inhibitors","volume":"1","author":"Levy-Sakin","year":"2009","journal-title":"Islets"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0525","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1002\/med.1028","article-title":"Antioxidant and other biological activities of phenols from olives and olive oil","volume":"22","author":"Visioli","year":"2002","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0530","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/S0024-3205(97)01150-8","article-title":"Oleuropein, the bitter principle of olives, enhances nitric oxide production by mouse macrophages","volume":"62","author":"Visioli","year":"1998","journal-title":"Life Sci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0535","doi-asserted-by":"crossref","first-page":"2213","DOI":"10.1093\/jn\/136.8.2213","article-title":"The olive constituent oleuropein exhibits anti-ischemic, antioxidative, and hypolipidemic effects in anesthetized rabbits","volume":"136","author":"Andreadou","year":"2006","journal-title":"J. Nutr."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0540","doi-asserted-by":"crossref","first-page":"841","DOI":"10.2174\/156720511798192682","article-title":"Abeta(1\u201342) aggregates into non-toxic amyloid assemblies in the presence of the natural polyphenol oleuropein aglycon","volume":"8","author":"Rigacci","year":"2011","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0545","doi-asserted-by":"crossref","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. Neurodegener."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0550","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1016\/j.jnutbio.2009.04.010","article-title":"Oleuropein aglycon prevents cytotoxic amyloid aggregation of human amylin","volume":"21","author":"Rigacci","year":"2010","journal-title":"J. Nutr. Biochem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0555","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1002\/mnfr.201100436","article-title":"Distribution of olive oil phenolic compounds in rat tissues after administration of a phenolic extract from olive cake","volume":"56","author":"Serra","year":"2012","journal-title":"Mol. Nutr. Food Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0560","doi-asserted-by":"crossref","first-page":"26846","DOI":"10.1074\/jbc.M403129200","article-title":"The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils","volume":"279","author":"Zhu","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0565","doi-asserted-by":"crossref","first-page":"767","DOI":"10.3233\/JAD-2011-111061","article-title":"Identification of polyphenolic compounds and black tea extract as potent inhibitors of lipid membrane destabilization by Abeta(4)(2) aggregates","volume":"27","author":"Gauci","year":"2011","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0570","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1002\/cbic.201000604","article-title":"Baicalein inhibits formation of alpha-synuclein oligomers within living cells and prevents Abeta peptide fibrillation and oligomerisation","volume":"12","author":"Lu","year":"2011","journal-title":"ChemBioChem"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0575","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.neulet.2011.01.055","article-title":"Baicalin prevents the production of hydrogen peroxide and oxidative stress induced by Abeta aggregation in SH-SY5Y cells","volume":"492","author":"Yin","year":"2011","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0580","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1016\/j.fitote.2011.12.019","article-title":"Pharmacokinetic study of baicalein after oral administration in monkeys","volume":"83","author":"Tian","year":"2012","journal-title":"Fitoterapia"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0585","doi-asserted-by":"crossref","first-page":"7516","DOI":"10.1016\/j.bmc.2008.04.067","article-title":"Baicalin, a prodrug able to reach the CNS, is a prolyl oligopeptidase inhibitor","volume":"16","author":"Tarrago","year":"2008","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0590","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/sj.bjp.0704911","article-title":"A novel beta-sheet breaker, RS-0406, reverses amyloid beta-induced cytotoxicity and impairment of long-term potentiation in vitro","volume":"137","author":"Nakagami","year":"2002","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0595","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.1523\/JNEUROSCI.4391-04.2005","article-title":"Certain inhibitors of synthetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation","volume":"25","author":"Walsh","year":"2005","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0600","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.bbr.2010.01.044","article-title":"RS-0406 arrests amyloid-beta oligomer-induced behavioural deterioration in vivo","volume":"210","author":"O'Hare","year":"2010","journal-title":"Behav. Brain Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0605","doi-asserted-by":"crossref","first-page":"29","DOI":"10.5507\/bp.2005.002","article-title":"Silybin and silymarin \u2014 new effects and applications","volume":"149","author":"Kren","year":"2005","journal-title":"Biomed. Pap. Med. Fac. Univ. Palacky Olomouc Czech. Republic"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0610","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/j.neuint.2010.12.017","article-title":"Silibinin: a novel inhibitor of Abeta aggregation","volume":"58","author":"Yin","year":"2011","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0615","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/j.bbrc.2012.02.042","article-title":"Silibinin inhibits the toxic aggregation of human islet amyloid polypeptide","volume":"419","author":"Cheng","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0620","first-page":"380","article-title":"Salvianolic acid B inhibits fibril formation and neurotoxicity of amyloid beta-protein in vitro","volume":"22","author":"Tang","year":"2001","journal-title":"Acta Pharmacol. Sin."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0625","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1002\/prot.24216","article-title":"Salvianolic acid B inhibits the amyloid formation of human islet amyloid polypeptide and protects pancreatic beta-cells against cytotoxicity","volume":"81","author":"Cheng","year":"2013","journal-title":"Proteins"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0630","first-page":"159","article-title":"Proanthocyanidins and polymeric flavonoids from sorghum","volume":"213","author":"Gujer","year":"1986","journal-title":"Prog. Clin. Biol. Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0635","doi-asserted-by":"crossref","first-page":"798","DOI":"10.1093\/ajcn\/76.4.798","article-title":"Procyanidin dimer B2 [epicatechin-(4beta-8)-epicatechin] in human plasma after the consumption of a flavanol-rich cocoa","volume":"76","author":"Holt","year":"2002","journal-title":"Am. J. Clin. Nutr."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0640","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1016\/j.fct.2013.02.049","article-title":"Proanthocyanidins are the major anti-diabetic components of cinnamon water extract","volume":"56","author":"Jiao","year":"2013","journal-title":"Food Chem. Toxicol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0645","doi-asserted-by":"crossref","first-page":"1962","DOI":"10.1002\/prot.24080","article-title":"Generic inhibition of amyloidogenic proteins by two naphthoquinone-tryptophan hybrid molecules","volume":"80","author":"Scherzer-Attali","year":"2012","journal-title":"Proteins"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0650","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1016\/j.nbd.2012.03.005","article-title":"Naphthoquinone-tyrptophan reduces neurotoxic Abeta*56 levels and improves cognition in Alzheimer's disease animal model","volume":"46","author":"Scherzer-Attali","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0655","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1016\/j.bmc.2011.12.042","article-title":"A review on coumarins as acetylcholinesterase inhibitors for Alzheimer's disease","volume":"20","author":"Anand","year":"2012","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0660","doi-asserted-by":"crossref","first-page":"2596","DOI":"10.1016\/j.bmc.2011.03.010","article-title":"Inhibition of amyloid-beta aggregation by coumarin analogs can be manipulated by functionalization of the aromatic center","volume":"19","author":"Soto-Ortega","year":"2011","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0665","doi-asserted-by":"crossref","first-page":"18495","DOI":"10.1074\/jbc.M906994199","article-title":"Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid beta peptide and inhibit abeta-induced toxicity","volume":"275","author":"McLaurin","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0670","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1111\/j.1460-9568.2009.07052.x","article-title":"Small molecule beta-amyloid inhibitors that stabilize protofibrillar structures in vitro improve cognition and pathology in a mouse model of Alzheimer's disease","volume":"31","author":"Hawkes","year":"2010","journal-title":"Eur. J. Neurosci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0675","doi-asserted-by":"crossref","first-page":"2313","DOI":"10.1093\/hmg\/ddl157","article-title":"Mapping genetic modulators of amyloid plaque deposition in TgCRND8 transgenic mice","volume":"15","author":"Sebastiani","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0680","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1007\/BF00971603","article-title":"Myo-inositol transport through the blood\u2013brain barrier","volume":"13","author":"Spector","year":"1988","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0685","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.neuropharm.2010.07.013","article-title":"Calpain inhibition prevents amyloid-beta-induced neurodegeneration and associated behavioral dysfunction in rats","volume":"59","author":"Granic","year":"2010","journal-title":"Neuropharmacology"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0690","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.brainres.2010.05.013","article-title":"Characterization of the 3\u00d7Tg-AD mouse model of Alzheimer's disease: part 1. Circadian changes","volume":"1348","author":"Sterniczuk","year":"2010","journal-title":"Brain Res."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0695","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1016\/j.ajpath.2012.04.020","article-title":"Calpain inhibitor A-705253 mitigates Alzheimer's disease-like pathology and cognitive decline in aged 3\u00d7TgAD mice","volume":"181","author":"Medeiros","year":"2012","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0700","doi-asserted-by":"crossref","first-page":"49","DOI":"10.3233\/JAD-2009-0925","article-title":"Identification of antihypertensive drugs which inhibit amyloid-beta protein oligomerization","volume":"16","author":"Zhao","year":"2009","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0705","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nrd3675","article-title":"Tafamidis","volume":"11","author":"Said","year":"2012","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0710","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1358\/dot.2012.48.5.1808486","article-title":"Tafamidis for transthyretin amyloidosis","volume":"48","author":"de Lartigue","year":"2012","journal-title":"Drugs Today (Barc)"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0715","doi-asserted-by":"crossref","first-page":"9629","DOI":"10.1073\/pnas.1121005109","article-title":"Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade","volume":"109","author":"Bulawa","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0720","doi-asserted-by":"crossref","first-page":"38992","DOI":"10.1074\/jbc.M112.348037","article-title":"A novel inhibitor of amyloid beta (Abeta) peptide aggregation: from high throughput screening to efficacy in an animal model of Alzheimer disease","volume":"287","author":"McKoy","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0725","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1111\/j.1747-0285.2007.00557.x","article-title":"Structure\u2013activity relationships of amyloid beta-aggregation inhibitors based on curcumin: influence of linker length and flexibility","volume":"70","author":"Reinke","year":"2007","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0730","doi-asserted-by":"crossref","first-page":"e31869","DOI":"10.1371\/journal.pone.0031869","article-title":"A chemical analog of curcumin as an improved inhibitor of amyloid Abeta oligomerization","volume":"7","author":"Orlando","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0735","doi-asserted-by":"crossref","first-page":"2670","DOI":"10.1021\/bi2015162","article-title":"Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols","volume":"51","author":"Cao","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0740","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1002\/pro.2023","article-title":"Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers","volume":"21","author":"Noor","year":"2012","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0745","doi-asserted-by":"crossref","first-page":"3439","DOI":"10.1021\/ja209829m","article-title":"Mechanisms of protein oligomerization: inhibitor of functional amyloids templates alpha-synuclein fibrillation","volume":"134","author":"Horvath","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0750","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.febslet.2010.11.050","article-title":"Porcine islet amyloid polypeptide fragments are refractory to amyloid formation","volume":"585","author":"Zhang","year":"2011","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0755","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1046\/j.1471-4159.1995.64010253.x","article-title":"Structure\u2013activity analyses of beta-amyloid peptides: contributions of the beta 25\u201335 region to aggregation and neurotoxicity","volume":"64","author":"Pike","year":"1995","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0760","doi-asserted-by":"crossref","first-page":"7882","DOI":"10.1021\/bi002734u","article-title":"Structure\u2013function relationships for inhibitors of beta-amyloid toxicity containing the recognition sequence KLVFF","volume":"40","author":"Lowe","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0765","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1006\/bbrc.1996.1413","article-title":"Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation","volume":"226","author":"Soto","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0770","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1038\/nm0798-822","article-title":"Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy","volume":"4","author":"Soto","year":"1998","journal-title":"Nat. Med."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0775","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1096\/fj.01-0841fje","article-title":"Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide","volume":"16","author":"Permanne","year":"2002","journal-title":"FASEB J."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0780","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1002\/(SICI)1097-4695(19990605)39:3<371::AID-NEU4>3.0.CO;2-E","article-title":"Beta-sheet breaker peptide inhibitor of Alzheimer's amyloidogenesis with increased blood\u2013brain barrier permeability and resistance to proteolytic degradation in plasma","volume":"39","author":"Poduslo","year":"1999","journal-title":"J. Neurobiol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0785","doi-asserted-by":"crossref","first-page":"13203","DOI":"10.1074\/jbc.273.21.13203","article-title":"Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides","volume":"273","author":"Chabry","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0790","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1096\/fj.03-1346fje","article-title":"A strategy for designing inhibitors of alpha-synuclein aggregation and toxicity as a novel treatment for Parkinson's disease and related disorders","volume":"18","author":"El-Agnaf","year":"2004","journal-title":"FASEB J."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0795","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/S0022-2836(02)00164-X","article-title":"Design of peptide-based inhibitors of human islet amyloid polypeptide fibrillogenesis","volume":"318","author":"Scrocchi","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0800","doi-asserted-by":"crossref","first-page":"10437","DOI":"10.1074\/jbc.275.14.10437","article-title":"Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening","volume":"275","author":"Nagai","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0805","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1110\/ps.051879606","article-title":"Inhibition of insulin fibrillogenesis with targeted peptides","volume":"15","author":"Gibson","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0965","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1007\/s13311-013-0184-7","article-title":"Inhibition of protein misfolding\/aggregation using polyglutamine binding peptide QBP1 as a therapy for the polyglutamine diseases","volume":"10","author":"Popiel","year":"2013","journal-title":"Neurotherapeutics"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0815","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1002\/anie.200901694","article-title":"Synthetic alpha-helix mimetics as agonists and antagonists of islet amyloid polypeptide aggregation","volume":"49","author":"Saraogi","year":"2010","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0820","doi-asserted-by":"crossref","first-page":"4749","DOI":"10.1039\/c3cc41452c","article-title":"A foldamer approach to targeting membrane bound helical states of islet amyloid polypeptide","volume":"49","author":"Kumar","year":"2013","journal-title":"Chem. Commun. (Camb)"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0825","doi-asserted-by":"crossref","first-page":"1943","DOI":"10.1002\/bip.1980.360191103","article-title":"Conformational energy studies on N-methylated analogs of thyrotropin releasing hormone, enkephalin, and luteinizing hormone-releasing hormone","volume":"19","author":"Manavalan","year":"1980","journal-title":"Biopolymers"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0830","doi-asserted-by":"crossref","first-page":"25109","DOI":"10.1074\/jbc.M003554200","article-title":"Inhibition of toxicity in the beta-amyloid peptide fragment beta-(25\u201335) using N-methylated derivatives: a general strategy to prevent amyloid formation","volume":"275","author":"Hughes","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0835","first-page":"P2","article-title":"\u03b2-amyloid aggregation inhibitors for the treatment of Alzheimer's disease","volume":"4","author":"Hozefa Amijee","year":"2008","journal-title":"Alzheimers Dement."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0840","doi-asserted-by":"crossref","first-page":"2046","DOI":"10.1073\/pnas.0507471103","article-title":"Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis","volume":"103","author":"Yan","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0845","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1152\/physrev.2001.81.2.741","article-title":"Alzheimer's disease: genes, proteins, and therapy","volume":"81","author":"Selkoe","year":"2001","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0850","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/nature10154","article-title":"Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation","volume":"475","author":"Sievers","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0855","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1073\/pnas.93.1.452","article-title":"Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide","volume":"93","author":"Solomon","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0860","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1038\/nature01870","article-title":"A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme","volume":"424","author":"Dumoulin","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0865","doi-asserted-by":"crossref","first-page":"e27230","DOI":"10.1371\/journal.pone.0027230","article-title":"Antibodies against alpha-synuclein reduce oligomerization in living cells","volume":"6","author":"Nasstrom","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0870","doi-asserted-by":"crossref","first-page":"19232","DOI":"10.1073\/pnas.0703793104","article-title":"Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils","volume":"104","author":"Habicht","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0875","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1126\/science.1079469","article-title":"Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis","volume":"300","author":"Kayed","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0880","doi-asserted-by":"crossref","first-page":"2052","DOI":"10.1212\/WNL.0b013e3181c6784a","article-title":"APOE {epsilon}4 and bapineuzumab: infusing pharmacogenomics into Alzheimer disease therapeutics","volume":"73","author":"Kaufer","year":"2009","journal-title":"Neurology"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0885","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1097\/WNF.0b013e3181cb577a","article-title":"Safety and changes in plasma and cerebrospinal fluid amyloid beta after a single administration of an amyloid beta monoclonal antibody in subjects with Alzheimer disease","volume":"33","author":"Siemers","year":"2010","journal-title":"Clin. Neuropharmacol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0890","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/j.jmb.2011.11.047","article-title":"Structural basis of C-terminal beta-amyloid peptide binding by the antibody ponezumab for the treatment of Alzheimer's disease","volume":"421","author":"La Porte","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0895","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1001\/archneurol.2011.1538","article-title":"Mechanism of amyloid removal in patients with Alzheimer disease treated with gantenerumab","volume":"69","author":"Ostrowitzki","year":"2012","journal-title":"Arch. Neurol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0900","first-page":"89","article-title":"Bapineuzumab, an investigational agent for Alzheimer's disease","volume":"38","author":"Khorassani","year":"2013","journal-title":"P. T."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0905","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1097\/WNF.0b013e31827db49b","article-title":"Safety and pharmacology of a single intravenous dose of ponezumab in subjects with mild-to-moderate Alzheimer disease: a phase I, randomized, placebo-controlled, double-blind, dose-escalation study","volume":"36","author":"Landen","year":"2013","journal-title":"Clin. Neuropharmacol."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0970","doi-asserted-by":"crossref","first-page":"84ra43","DOI":"10.1126\/scitranslmed.3002254","article-title":"A therapeutic antibody targeting BACE1 inhibits amyloid-beta production in vivo","volume":"3","author":"Atwal","year":"2011","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0915","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.tibs.2006.12.005","article-title":"How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?","volume":"32","author":"Shaw","year":"2007","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0920","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1080\/13506120412331272287","article-title":"Amyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragments","volume":"11","author":"Reches","year":"2004","journal-title":"Amyloid"},{"key":"10.1016\/j.bbagen.2013.06.029_bb0925","doi-asserted-by":"crossref","first-page":"35475","DOI":"10.1074\/jbc.M206039200","article-title":"Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin","volume":"277","author":"Reches","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0930","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/S0006-291X(05)80107-X","article-title":"The N-terminal segment of protein AA determines its fibrillogenic property","volume":"182","author":"Westermark","year":"1992","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbagen.2013.06.029_bb0935","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1038\/aps.2011.14","article-title":"Small molecule inhibitors of amyloid beta peptide aggregation as a potential therapeutic strategy for Alzheimer's disease","volume":"32","author":"Nie","year":"2011","journal-title":"Acta Pharmacol. Sin."}],"container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416513002894?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416513002894?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,4,30]],"date-time":"2025-04-30T08:42:46Z","timestamp":1746002566000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0304416513002894"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,10]]},"references-count":187,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2013,10]]}},"alternative-id":["S0304416513002894"],"URL":"https:\/\/doi.org\/10.1016\/j.bbagen.2013.06.029","relation":{},"ISSN":["0304-4165"],"issn-type":[{"value":"0304-4165","type":"print"}],"subject":[],"published":{"date-parts":[[2013,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Inhibiting toxic aggregation of amyloidogenic proteins: A therapeutic strategy for protein misfolding diseases","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - General Subjects","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbagen.2013.06.029","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2013 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}