Scientific References

 

  • 1.Selkoe, D. J. & Hardy, J. The amyloid hypothesis of Alzheimer’s disease at 25 years. EMBO Mol Med (2016). [DOI] [PMC free article] [PubMed]
  • 2.Harrison JR, Owen MJ. Alzheimer’s disease: the amyloid hypothesis on trial. Br J Psychiatry. 2016;208:1–3. doi: 10.1192/bjp.bp.115.167569. [DOI] [PubMed] [Google Scholar]
  • 3.Kang J, et al. The precursor of Alzheimer’s disease amyloid A4 protein resembles a cell-surface receptor. Nature. 1987;325:733–736. doi: 10.1038/325733a0. [DOI] [PubMed] [Google Scholar]
  • 4.Thinakaran G, Koo EH. Amyloid precursor protein trafficking, processing, and function. J Biol Chem. 2008;283:29615–29619. doi: 10.1074/jbc.R800019200. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 5.Bibl M, et al. Blood-based neurochemical diagnosis of vascular dementia: a pilot study. J Neurochem. 2007;103:467–474. doi: 10.1111/j.1471-4159.2007.04763.x. [DOI] [PubMed] [Google Scholar]
  • 6.Schoonenboom NS, et al. Amyloid beta 38, 40, and 42 species in cerebrospinal fluid: more of the same? Ann Neurol. 2005;58:139–142. doi: 10.1002/ana.20508. [DOI] [PubMed] [Google Scholar]
  • 7.Roychaudhuri R, Yang M, Hoshi MM, Teplow DB. Amyloid beta-protein assembly and Alzheimer disease. J Biol Chem. 2009;284:4749–4753. doi: 10.1074/jbc.R800036200. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 8.Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science. 2002;297:353–356. doi: 10.1126/science.1072994. [DOI] [PubMed] [Google Scholar]
  • 9.Selkoe DJ. Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior. Behavioural brain research. 2008;192:106–113. doi: 10.1016/j.bbr.2008.02.016. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 10.Hamley IW. The amyloid beta peptide: a chemist’s perspective. Role in Alzheimer’s and fibrillization. Chemical reviews. 2012;112:5147–5192. doi: 10.1021/cr3000994. [DOI] [PubMed] [Google Scholar]
  • 11.Glabe CG. Structural classification of toxic amyloid oligomers. J Biol Chem. 2008;283:29639–29643. doi: 10.1074/jbc.R800016200. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 12.Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nat Rev Mol Cell Biol. 2007;8:101–112. doi: 10.1038/nrm2101. [DOI] [PubMed] [Google Scholar]
  • 13.Chimon S, et al. Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer’s beta-amyloid. Nat Struct Mol Biol. 2007;14:1157–1164. doi: 10.1038/nsmb1345. [DOI] [PubMed] [Google Scholar]
  • 14.Liang C, et al. Kinetic intermediates in amyloid assembly. J Am Chem Soc. 2014;136:15146–15149. doi: 10.1021/ja508621b. [DOI] [PubMed] [Google Scholar]
  • 15.Parthasarathy S, et al. Structural Insight into an Alzheimer’s Brain-Derived Spherical Assembly of Amyloid beta by Solid-State NMR. J Am Chem Soc. 2015;137:6480–6483. doi: 10.1021/jacs.5b03373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 16.Chandra B, et al. Curcumin Dictates Divergent Fates for the Central Salt Bridges in Amyloid-beta40 and Amyloid-beta42. Biophys J. 2017;112:1597–1608. doi: 10.1016/j.bpj.2017.02.043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 17.Biancalana M, Koide S. Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochimica et biophysica acta. 2010;1804:1405–1412. doi: 10.1016/j.bbapap.2010.04.001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 18.Chen YR, Glabe CG. Distinct early folding and aggregation properties of Alzheimer amyloid-beta peptides Abeta40 and Abeta42: stable trimer or tetramer formation by Abeta42. J Biol Chem. 2006;281:24414–24422. doi: 10.1074/jbc.M602363200. [DOI] [PubMed] [Google Scholar]
  • 19.Bitan G, et al. Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci USA. 2003;100:330–335. doi: 10.1073/pnas.222681699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 20.Bernstein SL, et al. Amyloid-beta protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer’s disease. Nature chemistry. 2009;1:326–331. doi: 10.1038/nchem.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 21.Tycko R. Molecular structure of amyloid fibrils: insights from solid-state NMR. Q Rev Biophys. 2006;39:1–55. doi: 10.1017/S0033583506004173. [DOI] [PubMed] [Google Scholar]
  • 22.Torok M, et al. Structural and dynamic features of Alzheimer’s Abeta peptide in amyloid fibrils studied by site-directed spin labeling. J Biol Chem. 2002;277:40810–40815. doi: 10.1074/jbc.M205659200. [DOI] [PubMed] [Google Scholar]
  • 23.Williams AD, et al. Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis. J Mol Biol. 2004;335:833–842. doi: 10.1016/j.jmb.2003.11.008. [DOI] [PubMed] [Google Scholar]
  • 24.Gremer L, et al. Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy. Science. 2017;358:116–119. doi: 10.1126/science.aao2825. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 25.Dahlgren KN, et al. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. The Journal of biological chemistry. 2002;277:32046–32053. doi: 10.1074/jbc.M201750200. [DOI] [PubMed] [Google Scholar]
  • 26.McGowan E, et al. Abeta42 is essential for parenchymal and vascular amyloid deposition in mice. Neuron. 2005;47:191–199. doi: 10.1016/j.neuron.2005.06.030. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 27.Seubert P, et al. Isolation and quantification of soluble Alzheimer’s beta-peptide from biological fluids. Nature. 1992;359:325–327. doi: 10.1038/359325a0. [DOI] [PubMed] [Google Scholar]
  • 28.Ayton S, Lei P, Bush AI. Metallostasis in Alzheimer’s disease. Free Radic Biol Med. 2013;62:76–89. doi: 10.1016/j.freeradbiomed.2012.10.558. [DOI] [PubMed] [Google Scholar]
  • 29.Lovell MA, Robertson JD, Teesdale WJ, Campbell JL, Markesbery WR. Copper, iron and zinc in Alzheimer’s disease senile plaques. J Neurol Sci. 1998;158:47–52. doi: 10.1016/S0022-510X(98)00092-6. [DOI] [PubMed] [Google Scholar]
  • 30.Frederickson CJ, Koh JY, Bush AI. The neurobiology of zinc in health and disease. Nat Rev Neurosci. 2005;6:449–462. doi: 10.1038/nrn1671. [DOI] [PubMed] [Google Scholar]
  • 31.Bush AI. The metallobiology of Alzheimer’s disease. Trends Neurosci. 2003;26:207–214. doi: 10.1016/S0166-2236(03)00067-5. [DOI] [PubMed] [Google Scholar]
  • 32.Zatta P, Drago D, Bolognin S, Sensi SL. Alzheimer’s disease, metal ions and metal homeostatic therapy. Trends Pharmacol Sci. 2009;30:346–355. doi: 10.1016/j.tips.2009.05.002. [DOI] [PubMed] [Google Scholar]
  • 33.Chen WT, Liao YH, Yu HM, Cheng IH, Chen YR. Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formation. J Biol Chem. 2011;286:9646–9656. doi: 10.1074/jbc.M110.177246. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 34.Tougu V, Tiiman A, Palumaa P. Interactions of Zn(II) and Cu(II) ions with Alzheimer’s amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity. Metallomics. 2011;3:250–261. doi: 10.1039/c0mt00073f. [DOI] [PubMed] [Google Scholar]
  • 35.Solomonov I, et al. Zn2+ -Abeta40 complexes form metastable quasi-spherical oligomers that are cytotoxic to cultured hippocampal neurons. J Biol Chem. 2012;287:20555–20564. doi: 10.1074/jbc.M112.344036. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 36.Chen WT, et al. Amyloid-beta (Abeta) D7H mutation increases oligomeric Abeta42 and alters properties of Abeta-zinc/copper assemblies. PloS one. 2012;7:e35807. doi: 10.1371/journal.pone.0035807. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 37.Minicozzi V, et al. Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides. J Biol Chem. 2008;283:10784–10792. doi: 10.1074/jbc.M707109200. [DOI] [PubMed] [Google Scholar]
  • 38.Nair NG, Perry G, Smith MA, Reddy VP. NMR studies of zinc, copper, and iron binding to histidine, the principal metal ion complexing site of amyloid-beta peptide. J Alzheimers Dis. 2010;20:57–66. doi: 10.3233/JAD-2010-1346. [DOI] [PubMed] [Google Scholar]
  • 39.Danielsson J, Pierattelli R, Banci L, Graslund A. High-resolution NMR studies of the zinc-binding site of the Alzheimer’s amyloid beta-peptide. FEBS J. 2007;274:46–59. doi: 10.1111/j.1742-4658.2006.05563.x. [DOI] [PubMed] [Google Scholar]
  • 40.Syme CD, Viles JH. Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Abeta) of Alzheimer’s disease. Biochim Biophys Acta. 2006;1764:246–256. doi: 10.1016/j.bbapap.2005.09.012. [DOI] [PubMed] [Google Scholar]
  • 41.Klug GM, et al. Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH. Eur J Biochem. 2003;270:4282–4293. doi: 10.1046/j.1432-1033.2003.03815.x. [DOI] [PubMed] [Google Scholar]
  • 42.Garai K, Sahoo B, Kaushalya SK, Desai R, Maiti S. Zinc lowers amyloid-beta toxicity by selectively precipitating aggregation intermediates. Biochemistry. 2007;46:10655–10663. doi: 10.1021/bi700798b. [DOI] [PubMed] [Google Scholar]
  • 43.Ayton S, Lei P, Bush AI. Biometals and their therapeutic implications in Alzheimer’s disease. Neurotherapeutics. 2015;12:109–120. doi: 10.1007/s13311-014-0312-z. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 44.Bush AI. The metal theory of Alzheimer’s disease. J Alzheimers Dis. 2013;33(Suppl 1):S277–281. doi: 10.3233/JAD-2012-129011. [DOI] [PubMed] [Google Scholar]
  • 45.Faux NG, et al. PBT2 rapidly improves cognition in Alzheimer’s Disease: additional phase II analyses. Journal of Alzheimer’s disease: JAD. 2010;20:509–516. doi: 10.3233/JAD-2010-1390. [DOI] [PubMed] [Google Scholar]
  • 46.Lannfelt L, et al. Safety, efficacy, and biomarker findings of PBT2 in targeting Abeta as a modifying therapy for Alzheimer’s disease: a phase IIa, double-blind, randomised, placebo-controlled trial. Lancet Neurol. 2008;7:779–786. doi: 10.1016/S1474-4422(08)70167-4. [DOI] [PubMed] [Google Scholar]
  • 47.Chromy BA, et al. Self-assembly of Abeta(1-42) into globular neurotoxins. Biochemistry. 2003;42:12749–12760. doi: 10.1021/bi030029q. [DOI] [PubMed] [Google Scholar]
  • 48.Reinke AA, Seh HY, Gestwicki JE. A chemical screening approach reveals that indole fluorescence is quenched by pre-fibrillar but not fibrillar amyloid-beta. Bioorg Med Chem Lett. 2009;19:4952–4957. doi: 10.1016/j.bmcl.2009.07.082. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 49.Chen RJ, Chang WW, Lin YC, Cheng PL, Chen YR. Alzheimer’s amyloid-beta oligomers rescue cellular prion protein induced tau reduction via the Fyn pathway. ACS chemical neuroscience. 2013;4:1287–1296. doi: 10.1021/cn400085q. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 50.Brand L, Gohlke JR. Fluorescence probes for structure. Annu Rev Biochem. 1972;41:843–868. doi: 10.1146/annurev.bi.41.070172.004211. [DOI] [PubMed] [Google Scholar]
  • 51.LeVine H., 3rd 4,4(′)-Dianilino-1,1(′)-binaphthyl-5,5(′)-disulfonate: report on non-beta-sheet conformers of Alzheimer’s peptide beta(1-40) Arch Biochem Biophys. 2002;404:106–115. doi: 10.1016/S0003-9861(02)00246-1. [DOI] [PubMed] [Google Scholar]
  • 52.Kayed R, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 2003;300:486–489. doi: 10.1126/science.1079469. [DOI] [PubMed] [Google Scholar]
  • 53.Kayed R, et al. Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener. 2007;2:18. doi: 10.1186/1750-1326-2-18. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 54.Wu JW, et al. Fibrillar oligomers nucleate the oligomerization of monomeric amyloid beta but do not seed fibril formation. The Journal of biological chemistry. 2010;285:6071–6079. doi: 10.1074/jbc.M109.069542. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 55.Saito H, Ando I, Ramamoorthy A. Chemical shift tensor – the heart of NMR: Insights into biological aspects of proteins. Progress in nuclear magnetic resonance spectroscopy. 2010;57:181–228. doi: 10.1016/j.pnmrs.2010.04.005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 56.Wishart DS. Advances in metabolite identification. Bioanalysis. 2011;3:1769–1782. doi: 10.4155/bio.11.155. [DOI] [PubMed] [Google Scholar]
  • 57.Wishart DS. Interpreting protein chemical shift data. Progress in nuclear magnetic resonance spectroscopy. 2011;58:62–87. doi: 10.1016/j.pnmrs.2010.07.004. [DOI] [PubMed] [Google Scholar]
  • 58.Bertini I, Gonnelli L, Luchinat C, Mao J, Nesi A. A new structural model of Abeta40 fibrils. J Am Chem Soc. 2011;133:16013–16022. doi: 10.1021/ja2035859. [DOI] [PubMed] [Google Scholar]
  • 59.Adamo AM, Oteiza PI. Zinc deficiency and neurodevelopment: the case of neurons. Biofactors. 2010;36:117–124. doi: 10.1002/biof.91. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 60.Kim YH, Kim EY, Gwag BJ, Sohn S, Koh JY. Zinc-induced cortical neuronal death with features of apoptosis and necrosis: mediation by free radicals. Neuroscience. 1999;89:175–182. doi: 10.1016/S0306-4522(98)00313-3. [DOI] [PubMed] [Google Scholar]
  • 61.Lal R, Lin H, Quist AP. Amyloid beta ion channel: 3D structure and relevance to amyloid channel paradigm. Biochim Biophys Acta. 2007;1768:1966–1975. doi: 10.1016/j.bbamem.2007.04.021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 62.Lambert MP, et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proceedings of the National Academy of Sciences of the United States of America. 1998;95:6448–6453. doi: 10.1073/pnas.95.11.6448. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 63.Wang HW, et al. Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus. Brain research. 2002;924:133–140. doi: 10.1016/S0006-8993(01)03058-X. [DOI] [PubMed] [Google Scholar]
  • 64.Cullen WK, Suh YH, Anwyl R, Rowan MJ. Block of LTP in rat hippocampus in vivo by beta-amyloid precursor protein fragments. Neuroreport. 1997;8:3213–3217. doi: 10.1097/00001756-199710200-00006. [DOI] [PubMed] [Google Scholar]
  • 65.Lee JY, Cole TB, Palmiter RD, Suh SW, Koh JY. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc Natl Acad Sci USA. 2002;99:7705–7710. doi: 10.1073/pnas.092034699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 66.Yu WH, Lukiw WJ, Bergeron C, Niznik HB, Fraser PE. Metallothionein III is reduced in Alzheimer’s disease. Brain Res. 2001;894:37–45. doi: 10.1016/S0006-8993(00)03196-6. [DOI] [PubMed] [Google Scholar]
  • 67.Xie XM, Smart TG. A physiological role for endogenous zinc in rat hippocampal synaptic neurotransmission. Nature. 1991;349:521–524. doi: 10.1038/349521a0. [DOI] [PubMed] [Google Scholar]
  • 68.Lovell MA, Xie C, Markesbery WR. Protection against amyloid beta peptide toxicity by zinc. Brain research. 1999;823:88–95. doi: 10.1016/S0006-8993(99)01114-2. [DOI] [PubMed] [Google Scholar]
  • 69.Bishop GM, Robinson SR. The amyloid paradox: amyloid-beta-metal complexes can be neurotoxic and neuroprotective. Brain Pathol. 2004;14:448–452. doi: 10.1111/j.1750-3639.2004.tb00089.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 70.Cuajungco MP, et al. Evidence that the beta-amyloid plaques of Alzheimer’s disease represent the redox-silencing and entombment of abeta by zinc. J Biol Chem. 2000;275:19439–19442. doi: 10.1074/jbc.C000165200. [DOI] [PubMed] [Google Scholar]
  • 71.Petkova AT, et al. A structural model for Alzheimer’s beta -amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA. 2002;99:16742–16747. doi: 10.1073/pnas.262663499. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 72.Mithu VS, et al. Zn(++) binding disrupts the Asp(23)-Lys(28) salt bridge without altering the hairpin-shaped cross-beta Structure of Abeta(42) amyloid aggregates. Biophys J. 2011;101:2825–2832. doi: 10.1016/j.bpj.2011.10.023. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 73.Ehrnhoefer DE, et al. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol. 2008;15:558–566. doi: 10.1038/nsmb.1437. [DOI] [PubMed] [Google Scholar]
  • 74.Freir DB, et al. Interaction between prion protein and toxic amyloid beta assemblies can be therapeutically targeted at multiple sites. Nature communications. 2011;2:336. doi: 10.1038/ncomms1341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 75.Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature. 2009;457:1128–1132. doi: 10.1038/nature07761. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 76.De Felice FG, et al. Alzheimer’s disease-type neuronal tau hyperphosphorylation induced by A beta oligomers. Neurobiol Aging. 2008;29:1334–1347. doi: 10.1016/j.neurobiolaging.2007.02.029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 77.Minicozzi V, et al. Identifying the Minimal Copper- and Zinc-binding Site Sequence in Amyloid-{beta} Peptides. J. Biol. Chem. 2008;283:10784–10792. doi: 10.1074/jbc.M707109200. [DOI] [PubMed] [Google Scholar]
  • 78.Syme CD, Viles JH. Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (A[beta]) of Alzheimer’s disease. Biochimica et Biophysica Acta (BBA) – Proteins & Proteomics. 2006;1764:246–256. doi: 10.1016/j.bbapap.2005.09.012. [DOI] [PubMed] [Google Scholar]
  • 79.Danielsson J, Pierattelli R, Banci L, Graslund A. High-resolution NMR studies of the zinc-binding site of the Alzheimer’s amyloid beta peptide. FEBS Journal. 2007;274:46–59. doi: 10.1111/j.1742-4658.2006.05563.x. [DOI] [PubMed] [Google Scholar]
  • 80.Stellato F, et al. Metal binding in amyloid β-peptides shows intra- and inter-peptide coordination modes. European Biophysics Journal. 2006;35:340–351. doi: 10.1007/s00249-005-0041-7. [DOI] [PubMed] [Google Scholar]
  • 81.Jonsson T, et al. A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline. Nature. 2012;488:96–99. doi: 10.1038/nature11283. [DOI] [PubMed] [Google Scholar]
  • 82.Di Fede G, et al. A recessive mutation in the APP gene with dominant-negative effect on amyloidogenesis. Science. 2009;323:1473–1477. doi: 10.1126/science.1168979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 83.Giaccone G, et al. Neuropathology of the recessive A673V APP mutation: Alzheimer disease with distinctive features. Acta Neuropathol. 2010;120:803–812. doi: 10.1007/s00401-010-0747-1. [DOI] [PubMed] [Google Scholar]
  • 84.Lin TW, et al. Alzheimer’s amyloid-beta A2T variant and its N-terminal peptides inhibit amyloid-beta fibrillization and rescue the induced cytotoxicity. PLoS One. 2017;12:e0174561. doi: 10.1371/journal.pone.0174561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 85.Basi GS, et al. Structural correlates of antibodies associated with acute reversal of amyloid beta-related behavioral deficits in a mouse model of Alzheimer disease. The Journal of biological chemistry. 2010;285:3417–3427. doi: 10.1074/jbc.M109.045187. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 86.Deshpande A, Kawai H, Metherate R, Glabe CG, Busciglio J. A role for synaptic zinc in activity-dependent Abeta oligomer formation and accumulation at excitatory synapses. J Neurosci. 2009;29:4004–4015. doi: 10.1523/JNEUROSCI.5980-08.2009. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 87.Takeda A, et al. Amyloid beta-mediated Zn2+ influx into dentate granule cells transiently induces a short-term cognitive deficit. PloS one. 2014;9:e115923. doi: 10.1371/journal.pone.0115923. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 88.Takeda A, et al. Extracellular Zn2+ Is Essential for Amyloid beta1-42-Induced Cognitive Decline in the Normal Brain and Its Rescue. The Journal of neuroscience: the official journal of the Society for Neuroscience. 2017;37:7253–7262. doi: 10.1523/JNEUROSCI.0954-17.2017. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 89.Sevigny J, et al. The antibody aducanumab reduces Abeta plaques in Alzheimer’s disease. Nature. 2016;537:50–56. doi: 10.1038/nature19323. [DOI] [PubMed] [Google Scholar]
  • 90.Burdick D, et al. Assembly and aggregation properties of synthetic Alzheimer’s A4/beta amyloid peptide analogs. J Biol Chem. 1992;267:546–554. [PubMed] [Google Scholar]
  • 91.Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry. 1967;6:1948–1954. doi: 10.1021/bi00859a010. [DOI] [PubMed] [Google Scholar]
  • 92.Chang YJ, Chen YR. The coexistence of an equal amount of Alzheimer’s amyloid-beta 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway. The FEBS journal. 2014;281:2674–2687. doi: 10.1111/febs.12813. [DOI] [PubMed] [Google Scholar]
  • 93.Liao YH, Chen YR. A novel method for expression and purification of authentic amyloid-beta with and without (15)N labels. Protein expression and purification. 2015;113:63–71. doi: 10.1016/j.pep.2015.05.002. [DOI] [PubMed] [Google Scholar]
  • 94.Tsai KJ, Tsai YC, Shen CK. G-CSF rescues the memory impairment of animal models of Alzheimer’s disease. J Exp Med. 2007;204:1273–1280. doi: 10.1084/jem.20062481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 95.Morroni F, Sita G, Tarozzi A, Rimondini R, Hrelia P. Early effects of Abeta1-42 oligomers injection in mice: Involvement of PI3K/Akt/GSK3 and MAPK/ERK1/2 pathways. Behavioural brain research. 2016;314:106–115. doi: 10.1016/j.bbr.2016.08.002. [DOI] [PubMed] [Google Scholar]
  • 96.Chen JH, Ke KF, Lu JH, Qiu YH, Peng YP. Protection of TGF-beta1 against neuroinflammation and neurodegeneration in Abeta1-42-induced Alzheimer’s disease model rats. PloS one. 2015;10:e0116549. doi: 10.1371/journal.pone.0116549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 97.Tsukuda K, et al. Cognitive deficit in amyloid-beta-injected mice was improved by pretreatment with a low dose of telmisartan partly because of peroxisome proliferator-activated receptor-gamma activation. Hypertension. 2009;54:782–787. doi: 10.1161/HYPERTENSIONAHA.109.136879. [DOI] [PubMed] [Google Scholar]
  • 98.Cascella R, et al. Extracellular chaperones prevent Abeta42-induced toxicity in rat brains. Biochimica et biophysica acta. 2013;1832:1217–1226. doi: 10.1016/j.bbadis.2013.04.012. [DOI] [PubMed] [Google Scholar]