{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T14:18:05Z","timestamp":1790518685657,"version":"4.1.0"},"reference-count":70,"publisher":"Public Library of Science (PLoS)","issue":"3","license":[{"start":{"date-parts":[[2017,3,31]],"date-time":"2017-03-31T00:00:00Z","timestamp":1490918400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Ministry of Science and Technology, Taiwan (TW)","award":["MOST 103-2113-M-001 -015"],"award-info":[{"award-number":["MOST 103-2113-M-001 -015"]}]},{"DOI":"10.13039\/501100004663","name":"Ministry of Science and Technology, Taiwan","doi-asserted-by":"publisher","award":["104-2321-B-001-071"],"award-info":[{"award-number":["104-2321-B-001-071"]}],"id":[{"id":"10.13039\/501100004663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004663","name":"Ministry of Science and Technology, Taiwan","doi-asserted-by":"publisher","award":["104-2320-B-001 -013 -MY3"],"award-info":[{"award-number":["104-2320-B-001 -013 -MY3"]}],"id":[{"id":"10.13039\/501100004663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004663","name":"Ministry of Science and Technology, Taiwan","doi-asserted-by":"publisher","award":["104-2745-B-001-002"],"award-info":[{"award-number":["104-2745-B-001-002"]}],"id":[{"id":"10.13039\/501100004663","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0174561","type":"journal-article","created":{"date-parts":[[2017,3,31]],"date-time":"2017-03-31T14:35:28Z","timestamp":1490970928000},"page":"e0174561","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":27,"title":["Alzheimer\u2019s amyloid-\u03b2 A2T variant and its N-terminal peptides inhibit amyloid-\u03b2 fibrillization and rescue the induced cytotoxicity"],"prefix":"10.1371","volume":"12","author":[{"given":"Tien-Wei","family":"Lin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chi-Fon","family":"Chang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu-Jen","family":"Chang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yi-Hung","family":"Liao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hui-Ming","family":"Yu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yun-Ru","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2017,3,31]]},"reference":[{"issue":"4","key":"ref1","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1056\/NEJMra0909142","article-title":"Alzheimer's disease","volume":"362","author":"HW Querfurth","year":"2010","journal-title":"N Engl J Med"},{"issue":"1","key":"ref2","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1053\/j.semnuclmed.2016.09.006","article-title":"Abeta-amyloid and Tau Imaging in Dementia","volume":"47","author":"VL Villemagne","year":"2017","journal-title":"Seminars in nuclear medicine"},{"issue":"6","key":"ref3","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1016\/j.neuron.2013.12.003","article-title":"Biomarker modeling of Alzheimer's disease","volume":"80","author":"CR Jack Jr.","year":"2013","journal-title":"Neuron"},{"key":"ref4","article-title":"Is there correlation between Abeta-heme peroxidase activity and the peptide aggregation state? A literature review combined with hypothesis","author":"R Khodarahmi","year":"2016","journal-title":"International journal of biological macromolecules"},{"issue":"7266","key":"ref5","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1038\/nature08538","article-title":"Multimodal techniques for diagnosis and prognosis of Alzheimer's disease","volume":"461","author":"RJ Perrin","year":"2009","journal-title":"Nature"},{"issue":"4","key":"ref6","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1001\/jamaneurol.2013.5847","article-title":"Amyloid-beta and tau: the trigger and bullet in Alzheimer disease pathogenesis","volume":"71","author":"GS Bloom","year":"2014","journal-title":"JAMA neurology"},{"issue":"2","key":"ref7","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/S1474-4422(12)70291-0","article-title":"Tracking pathophysiological processes in Alzheimer's disease: an updated hypothetical model of dynamic biomarkers","volume":"12","author":"CR Jack Jr.","year":"2013","journal-title":"Lancet Neurol"},{"issue":"6","key":"ref8","doi-asserted-by":"crossref","first-page":"595","DOI":"10.15252\/emmm.201606210","article-title":"The amyloid hypothesis of Alzheimer's disease at 25 years","volume":"8","author":"DJ Selkoe","year":"2016","journal-title":"EMBO Mol Med"},{"issue":"22","key":"ref9","doi-asserted-by":"crossref","first-page":"5930","DOI":"10.1046\/j.0014-2956.2001.02537.x","article-title":"NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1\u201340)(ox) and A beta(1\u201342)(ox)","volume":"268","author":"R Riek","year":"2001","journal-title":"Eur J Biochem"},{"issue":"35","key":"ref10","doi-asserted-by":"crossref","first-page":"24143","DOI":"10.1074\/jbc.M114.576256","article-title":"The peculiar role of the A2V mutation in amyloid-beta (Abeta) 1\u201342 molecular assembly","volume":"289","author":"M Messa","year":"2014","journal-title":"The Journal of biological chemistry"},{"issue":"3","key":"ref11","doi-asserted-by":"crossref","first-page":"112","DOI":"10.4161\/pri.2.3.7488","article-title":"Amyloid fibrils: abnormal protein assembly","volume":"2","author":"RN Rambaran","year":"2008","journal-title":"Prion"},{"issue":"3","key":"ref12","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1073\/pnas.93.3.1125","article-title":"On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants","volume":"93","author":"A Lomakin","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"11","key":"ref13","doi-asserted-by":"crossref","first-page":"2334","DOI":"10.1110\/ps.073164107","article-title":"Protein aggregation processes: In search of the mechanism","volume":"16","author":"C Frieden","year":"2007","journal-title":"Protein Sci"},{"issue":"8","key":"ref14","doi-asserted-by":"crossref","first-page":"4749","DOI":"10.1074\/jbc.R800036200","article-title":"Amyloid beta-protein assembly and Alzheimer disease","volume":"284","author":"R Roychaudhuri","year":"2009","journal-title":"J Biol Chem"},{"issue":"7","key":"ref15","doi-asserted-by":"crossref","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":"M Biancalana","year":"2010","journal-title":"Biochim Biophys Acta"},{"issue":"1","key":"ref16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S0033583506004173","article-title":"Molecular structure of amyloid fibrils: insights from solid-state NMR","volume":"39","author":"R Tycko","year":"2006","journal-title":"Q Rev Biophys"},{"issue":"43","key":"ref17","doi-asserted-by":"crossref","first-page":"40810","DOI":"10.1074\/jbc.M205659200","article-title":"Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling","volume":"277","author":"M Torok","year":"2002","journal-title":"J Biol Chem"},{"issue":"3","key":"ref18","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/j.jmb.2003.11.008","article-title":"Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis","volume":"335","author":"AD Williams","year":"2004","journal-title":"J Mol Biol"},{"issue":"6","key":"ref19","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nsmb.2991","article-title":"Abeta(1\u201342) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease","volume":"22","author":"Y Xiao","year":"2015","journal-title":"Nat Struct Mol Biol"},{"issue":"9","key":"ref20","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1021\/bi802046n","article-title":"Structural Characterization of a Soluble Amyloid \u03b2-Peptide Oligomer","volume":"48","author":"L Yu","year":"2009","journal-title":"Biochemistry"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1146\/annurev.genom.3.022502.103022","article-title":"Deciphering the genetic basis of Alzheimer's disease","volume":"3","author":"DJ Selkoe","year":"2002","journal-title":"Annu Rev Genomics Hum Genet"},{"issue":"30","key":"ref22","doi-asserted-by":"crossref","first-page":"23186","DOI":"10.1074\/jbc.M109.086496","article-title":"Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity","volume":"285","author":"K Ono","year":"2010","journal-title":"The Journal of biological chemistry"},{"issue":"7","key":"ref23","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1136\/jnnp.2003.010611","article-title":"Novel amyloid precursor protein gene missense mutation (D678N) in probable familial Alzheimer's disease","volume":"75","author":"Y Wakutani","year":"2004","journal-title":"Journal of neurology, neurosurgery, and psychiatry"},{"issue":"4","key":"ref24","doi-asserted-by":"crossref","first-page":"e35807","DOI":"10.1371\/journal.pone.0035807","article-title":"Amyloid-beta (Abeta) D7H mutation increases oligomeric Abeta42 and alters properties of Abeta-zinc\/copper assemblies","volume":"7","author":"WT Chen","year":"2012","journal-title":"PLoS One"},{"issue":"10","key":"ref25","doi-asserted-by":"crossref","first-page":"3829","DOI":"10.1529\/biophysj.106.090993","article-title":"Impact of the mutation A21G (Flemish variant) on Alzheimer's beta-amyloid dimers by molecular dynamics simulations","volume":"91","author":"A Huet","year":"2006","journal-title":"Biophys J"},{"issue":"9","key":"ref26","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1038\/nn0901-887","article-title":"The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation","volume":"4","author":"C Nilsberth","year":"2001","journal-title":"Nature neuroscience"},{"issue":"4959","key":"ref27","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1126\/science.2111584","article-title":"Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type","volume":"248","author":"E Levy","year":"1990","journal-title":"Science"},{"issue":"4959","key":"ref28","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1126\/science.1971458","article-title":"Amyloid beta protein precursor gene and hereditary cerebral hemorrhage with amyloidosis (Dutch)","volume":"248","author":"C Van Broeckhoven","year":"1990","journal-title":"Science"},{"issue":"3","key":"ref29","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1212\/WNL.50.3.688","article-title":"Fatal familial insomnia: genetic, neuropathologic, and biochemical study of a patient from a new Italian kindred","volume":"50","author":"G Rossi","year":"1998","journal-title":"Neurology"},{"issue":"6","key":"ref30","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1002\/ana.1009","article-title":"Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy","volume":"49","author":"TJ Grabowski","year":"2001","journal-title":"Ann Neurol"},{"issue":"7","key":"ref31","doi-asserted-by":"crossref","first-page":"4916","DOI":"10.1074\/jbc.M608220200","article-title":"The Tottori (D7N) and English (H6R) familial Alzheimer disease mutations accelerate Abeta fibril formation without increasing protofibril formation","volume":"282","author":"Y Hori","year":"2007","journal-title":"The Journal of biological chemistry"},{"issue":"5920","key":"ref32","doi-asserted-by":"crossref","first-page":"1473","DOI":"10.1126\/science.1168979","article-title":"A recessive mutation in the APP gene with dominant-negative effect on amyloidogenesis","volume":"323","author":"G Di Fede","year":"2009","journal-title":"Science"},{"issue":"6","key":"ref33","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1007\/s00401-010-0747-1","article-title":"Neuropathology of the recessive A673V APP mutation: Alzheimer disease with distinctive features","volume":"120","author":"G Giaccone","year":"2010","journal-title":"Acta Neuropathol"},{"issue":"7409","key":"ref34","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/nature11283","article-title":"A mutation in APP protects against Alzheimer's disease and age-related cognitive decline","volume":"488","author":"T Jonsson","year":"2012","journal-title":"Nature"},{"issue":"45","key":"ref35","doi-asserted-by":"crossref","first-page":"30977","DOI":"10.1074\/jbc.M114.599027","article-title":"The Alzheimer disease protective mutation A2T modulates kinetic and thermodynamic properties of amyloid-beta (Abeta) aggregation","volume":"289","author":"I Benilova","year":"2014","journal-title":"The Journal of biological chemistry"},{"issue":"10","key":"ref36","doi-asserted-by":"crossref","first-page":"5193","DOI":"10.1021\/cr300009x","article-title":"Bioinorganic chemistry of Alzheimer's disease","volume":"112","author":"KP Kepp","year":"2012","journal-title":"Chemical reviews"},{"issue":"4","key":"ref37","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/S0733-8619(05)70227-9","article-title":"Treatment of Alzheimer's disease: rationale and strategies","volume":"18","author":"M Grundman","year":"2000","journal-title":"Neurol Clin"},{"issue":"3","key":"ref38","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1080\/13506120701461020","article-title":"Small molecule inhibitors of Abeta assembly","volume":"14","author":"H LeVine 3rd","year":"2007","journal-title":"Amyloid"},{"issue":"34","key":"ref39","doi-asserted-by":"crossref","first-page":"9019","DOI":"10.1021\/acs.jpcb.6b03892","article-title":"Action of Caffeine as an Amyloid Inhibitor in the Aggregation of Abeta16-22 Peptides","volume":"120","author":"B Sharma","year":"2016","journal-title":"J Phys Chem B"},{"issue":"9","key":"ref40","doi-asserted-by":"crossref","first-page":"1300","DOI":"10.1021\/acschemneuro.6b00175","article-title":"Natural Tripeptide-Based Inhibitor of Multifaceted Amyloid beta Toxicity","volume":"7","author":"K Rajasekhar","year":"2016","journal-title":"Acs Chem Neurosci"},{"issue":"24","key":"ref41","doi-asserted-by":"crossref","first-page":"5621","DOI":"10.1016\/j.bmcl.2014.10.076","article-title":"Structure activity relationship study of curcumin analogues toward the amyloid-beta aggregation inhibitor","volume":"24","author":"H Endo","year":"2014","journal-title":"Bioorg Med Chem Lett"},{"issue":"6","key":"ref42","doi-asserted-by":"crossref","first-page":"755","DOI":"10.2174\/138161212799277752","article-title":"Peptides for therapy and diagnosis of Alzheimer's disease","volume":"18","author":"SA Funke","year":"2012","journal-title":"Curr Pharm Des"},{"issue":"8","key":"ref43","doi-asserted-by":"crossref","first-page":"1615","DOI":"10.1021\/acs.jpcb.5b08177","article-title":"Mechanism of C-Terminal Fragments of Amyloid beta-Protein as Abeta Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?","volume":"120","author":"X Zheng","year":"2016","journal-title":"J Phys Chem B"},{"issue":"16","key":"ref44","doi-asserted-by":"crossref","first-page":"13905","DOI":"10.1074\/jbc.M211976200","article-title":"Pharmacological profiles of peptide drug candidates for the treatment of Alzheimer's disease","volume":"278","author":"C Adessi","year":"2003","journal-title":"J Biol Chem"},{"issue":"37","key":"ref45","doi-asserted-by":"crossref","first-page":"14175","DOI":"10.1073\/pnas.0807163105","article-title":"C-terminal peptides coassemble into Abeta42 oligomers and protect neurons against Abeta42-induced neurotoxicity","volume":"105","author":"EA Fradinger","year":"2008","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"issue":"5580","key":"ref46","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1126\/science.1072994","article-title":"The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics","volume":"297","author":"J Hardy","year":"2002","journal-title":"Science"},{"issue":"11","key":"ref47","doi-asserted-by":"crossref","first-page":"1662","DOI":"10.1002\/cbic.200600270","article-title":"A weakly clustered N terminus inhibits Abeta(1\u201340) amyloidogenesis","volume":"7","author":"KH Lim","year":"2006","journal-title":"Chembiochem: a European journal of chemical biology"},{"issue":"5","key":"ref48","doi-asserted-by":"crossref","first-page":"3417","DOI":"10.1074\/jbc.M109.045187","article-title":"Structural correlates of antibodies associated with acute reversal of amyloid beta-related behavioral deficits in a mouse model of Alzheimer disease","volume":"285","author":"GS Basi","year":"2010","journal-title":"The Journal of biological chemistry"},{"issue":"7","key":"ref49","doi-asserted-by":"crossref","first-page":"1948","DOI":"10.1021\/bi00859a010","article-title":"Spectroscopic determination of tryptophan and tyrosine in proteins","volume":"6","author":"H Edelhoch","year":"1967","journal-title":"Biochemistry"},{"issue":"4","key":"ref50","doi-asserted-by":"crossref","first-page":"1390","DOI":"10.1096\/fj.10-175539","article-title":"Folding stability of amyloid-\u03b2 40 monomer is an important determinant of the nucleation kinetics in fibrillization","volume":"25","author":"C-L Ni","year":"2011","journal-title":"The FASEB Journal"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.pep.2015.05.002","article-title":"A novel method for expression and purification of authentic amyloid-beta with and without (15)N labels","volume":"113","author":"YH Liao","year":"2015","journal-title":"Protein expression and purification"},{"issue":"7","key":"ref52","doi-asserted-by":"crossref","first-page":"1992","DOI":"10.1021\/ja036813f","article-title":"Solution NMR studies of the A beta(1\u201340) and A beta(1\u201342) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation","volume":"126","author":"L Hou","year":"2004","journal-title":"J Am Chem Soc"},{"issue":"10","key":"ref53","doi-asserted-by":"crossref","first-page":"2328","DOI":"10.1016\/j.bbamem.2013.04.012","article-title":"ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins","volume":"1828","author":"R Sarroukh","year":"2013","journal-title":"Biochim Biophys Acta"},{"issue":"11","key":"ref54","doi-asserted-by":"crossref","first-page":"6448","DOI":"10.1073\/pnas.95.11.6448","article-title":"Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins","volume":"95","author":"MP Lambert","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"35","key":"ref55","doi-asserted-by":"crossref","first-page":"32046","DOI":"10.1074\/jbc.M201750200","article-title":"Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability","volume":"277","author":"KN Dahlgren","year":"2002","journal-title":"J Biol Chem"},{"issue":"10","key":"ref56","doi-asserted-by":"crossref","first-page":"1732","DOI":"10.1021\/acschemneuro.5b00171","article-title":"Amyloid beta-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation","volume":"6","author":"X Zheng","year":"2015","journal-title":"Acs Chem Neurosci"},{"issue":"3","key":"ref57","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1016\/j.bpj.2014.12.013","article-title":"Alzheimer's protective A2T mutation changes the conformational landscape of the Abeta(1)(-)(4)(2) monomer differently than does the A2V mutation","volume":"108","author":"P Das","year":"2015","journal-title":"Biophys J"},{"issue":"40","key":"ref58","doi-asserted-by":"crossref","first-page":"16013","DOI":"10.1021\/ja2035859","article-title":"A new structural model of Abeta40 fibrils","volume":"133","author":"I Bertini","year":"2011","journal-title":"J Am Chem Soc"},{"issue":"1","key":"ref59","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1002\/anie.201408598","article-title":"Atomic-resolution three-dimensional structure of amyloid beta fibrils bearing the Osaka mutation","volume":"54","author":"AK Schutz","year":"2015","journal-title":"Angew Chem Int Ed Engl"},{"issue":"6","key":"ref60","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.cell.2013.08.035","article-title":"Molecular structure of beta-amyloid fibrils in Alzheimer's disease brain tissue","volume":"154","author":"JX Lu","year":"2013","journal-title":"Cell"},{"issue":"4","key":"ref61","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1002\/cbic.201402595","article-title":"Solution NMR studies of recombinant Abeta(1\u201342): from the presence of a micellar entity to residual beta-sheet structure in the soluble species","volume":"16","author":"MA Walti","year":"2015","journal-title":"Chembiochem"},{"issue":"41","key":"ref62","doi-asserted-by":"crossref","first-page":"23895","DOI":"10.1074\/jbc.270.41.23895","article-title":"Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro","volume":"270","author":"CJ Pike","year":"1995","journal-title":"J Biol Chem"},{"issue":"29","key":"ref63","doi-asserted-by":"crossref","first-page":"7072","DOI":"10.1021\/bi900818a","article-title":"Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides","volume":"48","author":"D Schlenzig","year":"2009","journal-title":"Biochemistry"},{"issue":"11","key":"ref64","doi-asserted-by":"crossref","first-page":"9646","DOI":"10.1074\/jbc.M110.177246","article-title":"Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formation","volume":"286","author":"WT Chen","year":"2011","journal-title":"J Biol Chem"},{"issue":"5177","key":"ref65","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1126\/science.8073293","article-title":"Rapid Induction of Alzheimer Abeta Amyloid Formation by Zinc","volume":"265","author":"AI Bush","year":"1994","journal-title":"Science"},{"issue":"34","key":"ref66","doi-asserted-by":"crossref","first-page":"32293","DOI":"10.1074\/jbc.M010706200","article-title":"New insights on how metals disrupt amyloid beta-aggregation and their effects on amyloid-beta cytotoxicity","volume":"276","author":"Y Yoshiike","year":"2001","journal-title":"J Biol Chem"},{"issue":"4","key":"ref67","doi-asserted-by":"crossref","first-page":"1376","DOI":"10.1021\/ja076282l","article-title":"Zinc-amyloid beta interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species","volume":"130","author":"D Noy","year":"2008","journal-title":"J Am Chem Soc"},{"issue":"10","key":"ref68","doi-asserted-by":"crossref","first-page":"2881","DOI":"10.1021\/bi0620961","article-title":"Concentration Dependent Cu2+ Induced Aggregation and Dityrosine Formation of the Alzheimer's Disease Amyloid-beta Peptide","volume":"46","author":"DP Smith","year":"2007","journal-title":"Biochemistry"},{"issue":"37","key":"ref69","doi-asserted-by":"crossref","first-page":"10655","DOI":"10.1021\/bi700798b","article-title":"Zinc lowers amyloid-beta toxicity by selectively precipitating aggregation intermediates","volume":"46","author":"K Garai","year":"2007","journal-title":"Biochemistry"},{"issue":"6","key":"ref70","doi-asserted-by":"crossref","first-page":"1784","DOI":"10.1111\/j.1471-4159.2009.06269.x","article-title":"Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-beta (1\u201342) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators","volume":"110","author":"V Tougu","year":"2009","journal-title":"J Neurochem"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0174561","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,10,24]],"date-time":"2018-10-24T00:12:51Z","timestamp":1540339971000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0174561"}},"subtitle":[],"editor":[{"given":"Jaya","family":"Padmanabhan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2017,3,31]]},"references-count":70,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2017,3,31]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0174561","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,3,31]]}}}