{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T13:11:09Z","timestamp":1793970669846,"version":"4.8.0"},"reference-count":356,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2021,8,28]],"date-time":"2021-08-28T00:00:00Z","timestamp":1630108800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2021,8,28]],"date-time":"2021-08-28T00:00:00Z","timestamp":1630108800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Vetenskapsr\u00e5det","doi-asserted-by":"publisher","award":["2016-03952"],"award-info":[{"award-number":["2016-03952"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008599","name":"Alzheimerfonden","doi-asserted-by":"publisher","award":["AF-544641, AF-640331, AF-733821"],"award-info":[{"award-number":["AF-544641, AF-640331, AF-733821"]}],"id":[{"id":"10.13039\/501100008599","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004200","name":"Stiftelsen Olle Engkvist Byggm\u00e4stare","doi-asserted-by":"publisher","award":["199-0446"],"award-info":[{"award-number":["199-0446"]}],"id":[{"id":"10.13039\/501100004200","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Neurodegeneration"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Alzheimer\u2019s disease (AD) is pathologically defined by the presence of fibrillar amyloid \u03b2 (A\u03b2) peptide in extracellular senile plaques and tau filaments in intracellular neurofibrillary tangles. Extensive research has focused on understanding the assembly mechanisms and neurotoxic effects of A\u03b2 during the last decades but still we only have a brief understanding of the disease associated biological processes. This review highlights the many other constituents that, beside A\u03b2, are accumulated in the plaques, with the focus on extracellular proteins. All living organisms rely on a delicate network of protein functionality. Deposition of significant amounts of certain proteins in insoluble inclusions will unquestionably lead to disturbances in the network, which may contribute to AD and copathology. This paper provide a comprehensive overview of extracellular proteins that have been shown to interact with A\u03b2 and a discussion of their potential roles in AD pathology. Methods that can expand the knowledge about <jats:italic>how<\/jats:italic> the proteins are incorporated in plaques are described. Top-down methods to analyze post-mortem tissue and bottom-up approaches with the potential to provide molecular insights on the organization of plaque-like particles are compared. Finally, a network analysis of A\u03b2-interacting partners with enriched functional and structural key words is presented.<\/jats:p>","DOI":"10.1186\/s13024-021-00465-0","type":"journal-article","created":{"date-parts":[[2021,8,28]],"date-time":"2021-08-28T09:02:52Z","timestamp":1630141372000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":248,"title":["Extracellular protein components of amyloid plaques and their roles in Alzheimer\u2019s disease pathology"],"prefix":"10.1186","volume":"16","author":[{"given":"M. Mahafuzur","family":"Rahman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9238-7246","authenticated-orcid":false,"given":"Christofer","family":"Lendel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,8,28]]},"reference":[{"key":"465_CR1","unstructured":"World Alzheimer Report 2019. Attitudes to dementia. London: ADI. 2019."},{"key":"465_CR2","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1016\/S1474-4422(16)00070-3","volume":"15","author":"B Olsson","year":"2016","unstructured":"Olsson B, Lautner R, Andreasson U, \u00d6hrfelt A, Portelius E, Bjerke M, et al. CSF and blood biomarkers for the diagnosis of Alzheimer\u2019s disease: a systematic review and meta-analysis. Lancet Neurol. 2016;15:673\u201384.","journal-title":"Lancet Neurol"},{"key":"465_CR3","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1186\/s13041-019-0448-1","volume":"12","author":"H Zetterberg","year":"2019","unstructured":"Zetterberg H, Burnham SC. Blood-based molecular biomarkers for Alzheimer\u2019s disease. Mol Brain. 2019;12:26.","journal-title":"Mol Brain"},{"key":"465_CR4","doi-asserted-by":"publisher","first-page":"735","DOI":"10.1007\/s11604-019-00867-7","volume":"37","author":"H Matsuda","year":"2019","unstructured":"Matsuda H, Shigemoto Y, Sato N. Neuroimaging of Alzheimer\u2019s disease: focus on amyloid and tau PET. Jpn J Radiol. 2019;37:735\u201349.","journal-title":"Jpn J Radiol"},{"key":"465_CR5","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1186\/s13024-019-0333-5","volume":"14","author":"MA DeTure","year":"2019","unstructured":"DeTure MA, Dickson DW. The neuropathological diagnosis of Alzheimer\u2019s disease. Mol Neurodegener. 2019;14:32.","journal-title":"Mol Neurodegener"},{"key":"465_CR6","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1186\/s13024-019-0325-5","volume":"14","author":"F M\u00e1rquez","year":"2019","unstructured":"M\u00e1rquez F, Yassa MA. Neuroimaging biomarkers for Alzheimer\u2019s disease. Mol Neurodegener. 2019;14:21.","journal-title":"Mol Neurodegener"},{"key":"465_CR7","doi-asserted-by":"publisher","first-page":"1509","DOI":"10.1001\/archneur.65.11.1509","volume":"65","author":"HJ Aizenstein","year":"2008","unstructured":"Aizenstein HJ, Nebes RD, Saxton JA, Price JC, Mathis CA, Tsopelas ND, et al. Frequent amyloid deposition without significant cognitive impairment among the elderly. Arch Neurol. 2008;65:1509\u201317.","journal-title":"Arch Neurol"},{"key":"465_CR8","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1056\/NEJMra0909142","volume":"362","author":"HW Querfurth","year":"2010","unstructured":"Querfurth HW, LaFerla FM. Alzheimer\u2019s disease. N Engl J Med. 2010;362:329\u201344.","journal-title":"N Engl J Med"},{"key":"465_CR9","first-page":"146","volume":"64","author":"A Alzheimer","year":"1907","unstructured":"Alzheimer A. \u00dcber eine eigenartige Erkrankung der Hirnrinde. Allgemeine Zeitschrift fur Psychiatrie und Psychisch-gerichtliche Medizin. 1907;64:146\u20138.","journal-title":"Allgemeine Zeitschrift fur Psychiatrie und Psychisch-gerichtliche Medizin"},{"key":"465_CR10","first-page":"643","volume":"27","author":"P Divry","year":"1927","unstructured":"Divry P. Etude histochimique des plaques. J Belge de Neurologie et de Psychiatrie. 1927;27:643\u201357.","journal-title":"J Belge de Neurologie et de Psychiatrie"},{"key":"465_CR11","doi-asserted-by":"publisher","first-page":"885","DOI":"10.1016\/S0006-291X(84)80190-4","volume":"120","author":"GG Glenner","year":"1984","unstructured":"Glenner GG, Wong CW. Alzheimer\u2019s disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun. 1984;120:885\u201390.","journal-title":"Biochem Biophys Res Commun"},{"key":"465_CR12","doi-asserted-by":"publisher","first-page":"4245","DOI":"10.1073\/pnas.82.12.4245","volume":"82","author":"CL Masters","year":"1985","unstructured":"Masters CL, Simms G, Weinman NA, Multhaup G, McDonald BL, Beyreuther K. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc Natl Acad Sci U S A. 1985;82:4245\u20139.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR13","first-page":"89","volume":"17","author":"JP Brion","year":"1985","unstructured":"Brion JP, Couck AM, Passareiro E, Flament-Durand J. Neurofibrillary tangles of Alzheimer\u2019s disease: an immunohistochemical study. J Submicrosc Cytol. 1985;17:89\u201396.","journal-title":"J Submicrosc Cytol"},{"key":"465_CR14","doi-asserted-by":"publisher","first-page":"5991","DOI":"10.1073\/pnas.84.16.5991","volume":"84","author":"SG van Duinen","year":"1987","unstructured":"van Duinen SG, Casta\u00f1o EM, Prelli F, Bots GT, Luyendijk W, Frangione B. Hereditary cerebral hemorrhage with amyloidosis in patients of Dutch origin is related to Alzheimer disease. Proc Natl Acad Sci U S A. 1987;84:5991\u20134.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR15","doi-asserted-by":"publisher","first-page":"1120","DOI":"10.1126\/science.1971458","volume":"248","author":"C Van Broeckhoven","year":"1990","unstructured":"Van Broeckhoven C, Haan J, Bakker E, Hardy JA, Van Hul W, Wehnert A, et al. Amyloid \u03b2 protein precursor gene and hereditary cerebral hemorrhage with amyloidosis (Dutch). Science. 1990;248:1120\u20132.","journal-title":"Science"},{"key":"465_CR16","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1038\/ng0792-233","volume":"1","author":"J Hardy","year":"1992","unstructured":"Hardy J. Framing \u03b2-amyloid. Nat Genet. 1992;1:233\u20134.","journal-title":"Nat Genet"},{"key":"465_CR17","doi-asserted-by":"publisher","first-page":"18349","DOI":"10.1073\/pnas.0806270105","volume":"105","author":"AK Paravastu","year":"2008","unstructured":"Paravastu AK, Leapman RD, Yau WM, Tycko R. Molecular structural basis for polymorphism in Alzheimer\u2019s \u03b2-amyloid fibrils. Proc Natl Acad Sci U S A. 2008;105:18349\u201354.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR18","doi-asserted-by":"publisher","first-page":"9663","DOI":"10.1021\/jacs.6b05129","volume":"138","author":"MT Colvin","year":"2016","unstructured":"Colvin MT, Silvers R, Ni QZ, Can TV, Sergeyev I, Rosay M, et al. Atomic resolution structure of monomorphic A\u03b242 amyloid fibrils. J Am Chem Soc. 2016;138:9663\u201374.","journal-title":"J Am Chem Soc"},{"key":"465_CR19","doi-asserted-by":"publisher","first-page":"E4976","DOI":"10.1073\/pnas.1600749113","volume":"113","author":"MA W\u00e4lti","year":"2016","unstructured":"W\u00e4lti MA, Ravotti F, Arai H, Glabe CG, Wall JS, B\u00f6ckmann A, et al. Atomic-resolution structure of a disease-relevant A\u03b2(1-42) amyloid fibril. Proc Natl Acad Sci U S A. 2016;113:E4976\u201384.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR20","doi-asserted-by":"publisher","first-page":"116","DOI":"10.1126\/science.aao2825","volume":"358","author":"L Gremer","year":"2017","unstructured":"Gremer L, Sch\u00f6lzel D, Schenk C, Reinartz E, Labahn J, Ravelli RBG, et al. Fibril structure of amyloid-\u03b2(1-42) by cryo-electron microscopy. Science. 2017;358:116\u20139.","journal-title":"Science"},{"key":"465_CR21","doi-asserted-by":"publisher","first-page":"6448","DOI":"10.1073\/pnas.95.11.6448","volume":"95","author":"MP Lambert","year":"1998","unstructured":"Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, et al. Diffusible, nonfibrillar ligands derived from A\u03b21-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A. 1998;95:6448\u201353.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR22","doi-asserted-by":"publisher","first-page":"S567","DOI":"10.3233\/JAD-179941","volume":"64","author":"EN Cline","year":"2018","unstructured":"Cline EN, Bicca MA, Viola KL, Klein WL. The amyloid-\u03b2 oligomer hypothesis: beginning of the third decade. J Alzheimers Dis. 2018;64:S567\u2013s610.","journal-title":"J Alzheimers Dis"},{"key":"465_CR23","doi-asserted-by":"publisher","first-page":"9758","DOI":"10.1073\/pnas.1218402110","volume":"110","author":"SI Cohen","year":"2013","unstructured":"Cohen SI, Linse S, Luheshi LM, Hellstrand E, White DA, Rajah L, et al. Proliferation of amyloid-\u03b242 aggregates occurs through a secondary nucleation mechanism. Proc Natl Acad Sci U S A. 2013;110:9758\u201363.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR24","doi-asserted-by":"publisher","first-page":"9384","DOI":"10.1073\/pnas.1401564111","volume":"111","author":"G Meisl","year":"2014","unstructured":"Meisl G, Yang X, Hellstrand E, Frohm B, Kirkegaard JB, Cohen SI, et al. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the A\u03b240 and A\u03b242 peptides. Proc Natl Acad Sci U S A. 2014;111:9384\u20139.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR25","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1016\/j.cell.2015.12.056","volume":"164","author":"B De Strooper","year":"2016","unstructured":"De Strooper B, Karran E. The cellular phase of Alzheimer\u2019s disease. Cell. 2016;164:603\u201315.","journal-title":"Cell"},{"key":"465_CR26","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1007\/BF00685397","volume":"57","author":"P Eikelenboom","year":"1982","unstructured":"Eikelenboom P, Stam FC. Immunoglobulins and complement factors in senile plaques. An immunoperoxidase study. Acta Neuropathol. 1982;57:239\u201342.","journal-title":"Acta Neuropathol"},{"key":"465_CR27","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1007\/BF00689569","volume":"32","author":"T Ishii","year":"1975","unstructured":"Ishii T, Haga S. Identification of components of immunoglobulins in senile plaques by means of fluorescent antibody technique. Acta Neuropathol. 1975;32:157\u201362.","journal-title":"Acta Neuropathol"},{"key":"465_CR28","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1620\/tjem.174.269","volume":"174","author":"PL McGeer","year":"1994","unstructured":"McGeer PL, Klegeris A, Walker DG, Yasuhara O, McGeer EG. Pathological proteins in senile plaques. Tohoku J Exp Med. 1994;174:269\u201377.","journal-title":"Tohoku J Exp Med"},{"key":"465_CR29","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1016\/0006-8993(91)91092-F","volume":"541","author":"Y Namba","year":"1991","unstructured":"Namba Y, Tomonaga M, Kawasaki H, Otomo E, Ikeda K. Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer\u2019s disease and kuru plaque amyloid in Creutzfeldt-Jakob disease. Brain Res. 1991;541:163\u20136.","journal-title":"Brain Res"},{"key":"465_CR30","doi-asserted-by":"publisher","first-page":"921","DOI":"10.1126\/science.8346443","volume":"261","author":"EH Corder","year":"1993","unstructured":"Corder EH, Saunders AM, Strittmatter WJ, Schmechel DE, Gaskell PC, Small GW, et al. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer\u2019s disease in late onset families. Science. 1993;261:921\u20133.","journal-title":"Science"},{"key":"465_CR31","doi-asserted-by":"publisher","first-page":"37061","DOI":"10.1074\/jbc.M403672200","volume":"279","author":"L Liao","year":"2004","unstructured":"Liao L, Cheng D, Wang J, Duong DM, Losik TG, Gearing M, et al. Proteomic characterization of postmortem amyloid plaques isolated by laser capture microdissection. J Biol Chem. 2004;279:37061\u20138.","journal-title":"J Biol Chem"},{"key":"465_CR32","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1016\/j.jalz.2018.10.006","volume":"15","author":"F Xiong","year":"2019","unstructured":"Xiong F, Ge W, Ma C. Quantitative proteomics reveals distinct composition of amyloid plaques in Alzheimer\u2019s disease. Alzheimers Dement. 2019;15:429\u201340.","journal-title":"Alzheimers Dement"},{"key":"465_CR33","doi-asserted-by":"publisher","first-page":"975","DOI":"10.1016\/j.neuron.2019.12.015","volume":"105","author":"B Bai","year":"2020","unstructured":"Bai B, Wang X, Li Y, Chen PC, Yu K, Dey KK, et al. Deep multilayer brain proteomics identifies molecular networks in Alzheimer\u2019s disease progression. Neuron. 2020;105:975\u201391.e7.","journal-title":"Neuron"},{"key":"465_CR34","doi-asserted-by":"publisher","first-page":"9849","DOI":"10.1021\/bi060331+","volume":"45","author":"L S\u00f6derberg","year":"2006","unstructured":"S\u00f6derberg L, Bogdanovic N, Axelsson B, Winblad B, N\u00e4slund J, Tjernberg LO. Analysis of single Alzheimer solid plaque cores by laser capture microscopy and nanoelectrospray\/tandem mass spectrometry. Biochemistry. 2006;45:9849\u201356.","journal-title":"Biochemistry"},{"key":"465_CR35","doi-asserted-by":"publisher","first-page":"18","DOI":"10.3174\/ajnr.A0781","volume":"29","author":"FJ Wippold 2nd","year":"2008","unstructured":"Wippold FJ 2nd, Cairns N, Vo K, Holtzman DM, Morris JC. Neuropathology for the neuroradiologist: plaques and tangles. AJNR Am J Neuroradiol. 2008;29:18\u201322.","journal-title":"AJNR Am J Neuroradiol"},{"key":"465_CR36","doi-asserted-by":"publisher","first-page":"1000","DOI":"10.1038\/s41594-018-0147-0","volume":"25","author":"FJ O\u2019Reilly","year":"2018","unstructured":"O\u2019Reilly FJ, Rappsilber J. Cross-linking mass spectrometry: methods and applications in structural, molecular and systems biology. Nat Struct Mol Biol. 2018;25:1000\u20138.","journal-title":"Nat Struct Mol Biol"},{"key":"465_CR37","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1016\/j.cbpa.2018.08.006","volume":"48","author":"JD Chavez","year":"2019","unstructured":"Chavez JD, Bruce JE. Chemical cross-linking with mass spectrometry: a tool for systems structural biology. Curr Opin Chem Biol. 2019;48:8\u201318.","journal-title":"Curr Opin Chem Biol"},{"key":"465_CR38","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1074\/mcp.M700077-MCP200","volume":"7","author":"Y Bai","year":"2008","unstructured":"Bai Y, Markham K, Chen F, Weerasekera R, Watts J, Horne P, et al. The in vivo brain interactome of the amyloid precursor protein. Mol Cell Proteomics. 2008;7:15\u201334.","journal-title":"Mol Cell Proteomics"},{"key":"465_CR39","doi-asserted-by":"publisher","first-page":"2429","DOI":"10.1021\/acs.jproteome.0c00137","volume":"19","author":"J Sinsky","year":"2020","unstructured":"Sinsky J, Majerova P, Kovac A, Kotlyar M, Jurisica I, Hanes J. Physiological tau interactome in brain and its link to tauopathies. J Proteome Res. 2020;19:2429\u201342.","journal-title":"J Proteome Res"},{"key":"465_CR40","doi-asserted-by":"crossref","unstructured":"Nystr\u00f6m S, B\u00e4ck M, Nilsson KPR, Hammarstr\u00f6m P. Imaging amyloid tissues stained with luminescent conjugated oligothiophenes by hyperspectral confocal microscopy and fluorescence lifetime imaging. J Vis Exp. 2017;","DOI":"10.3791\/56279"},{"key":"465_CR41","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/j.sbi.2019.05.003","volume":"58","author":"AW Fitzpatrick","year":"2019","unstructured":"Fitzpatrick AW, Saibil HR. Cryo-EM of amyloid fibrils and cellular aggregates. Curr Opin Struct Biol. 2019;58:34\u201342.","journal-title":"Curr Opin Struct Biol"},{"key":"465_CR42","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/j.cell.2017.08.009","volume":"171","author":"FJB B\u00e4uerlein","year":"2017","unstructured":"B\u00e4uerlein FJB, Saha I, Mishra A, Kalemanov M, Mart\u00ednez-S\u00e1nchez A, Klein R, et al. In situ architecture and cellular interactions of PolyQ inclusions. Cell. 2017;171:179\u201387.e10.","journal-title":"Cell"},{"key":"465_CR43","doi-asserted-by":"publisher","first-page":"696","DOI":"10.1016\/j.cell.2017.12.030","volume":"172","author":"Q Guo","year":"2018","unstructured":"Guo Q, Lehmer C, Mart\u00ednez-S\u00e1nchez A, Rudack T, Beck F, Hartmann H, et al. In situ structure of neuronal C9orf72 Poly-GA aggregates reveals proteasome recruitment. Cell. 2018;172:696\u2013705.e12.","journal-title":"Cell"},{"key":"465_CR44","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1038\/s42003-019-0612-2","volume":"2","author":"R Frankel","year":"2019","unstructured":"Frankel R, T\u00f6rnquist M, Meisl G, Hansson O, Andreasson U, Zetterberg H, et al. Autocatalytic amplification of Alzheimer-associated A\u03b242 peptide aggregation in human cerebrospinal fluid. Commun Biol. 2019;2:365.","journal-title":"Commun Biol"},{"key":"465_CR45","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1016\/j.cell.2010.11.050","volume":"144","author":"H Olzscha","year":"2011","unstructured":"Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, et al. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell. 2011;144:67\u201378.","journal-title":"Cell"},{"key":"465_CR46","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1016\/j.cis.2007.04.021","volume":"134\u2013135","author":"I Lynch","year":"2007","unstructured":"Lynch I, Cedervall T, Lundqvist M, Cabaleiro-Lago C, Linse S, Dawson KA. The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century. Adv Colloid Interface Sci. 2007;134\u2013135:167\u201374.","journal-title":"Adv Colloid Interface Sci"},{"key":"465_CR47","volume":"327","author":"I Lynch","year":"2006","unstructured":"Lynch I, Dawson KA, Linse S. Detecting cryptic epitopes created by nanoparticles. Sci STKE. 2006;327:pe14.","journal-title":"Sci STKE"},{"key":"465_CR48","doi-asserted-by":"publisher","first-page":"2331","DOI":"10.1038\/s41467-019-10192-2","volume":"10","author":"K Ezzat","year":"2019","unstructured":"Ezzat K, Pernemalm M, P\u00e5lsson S, Roberts TC, J\u00e4rver P, Dondalska A, et al. The viral protein corona directs viral pathogenesis and amyloid aggregation. Nat Commun. 2019;10:2331.","journal-title":"Nat Commun"},{"key":"465_CR49","doi-asserted-by":"publisher","first-page":"256","DOI":"10.3389\/fnins.2020.00256","volume":"14","author":"M Malmberg","year":"2020","unstructured":"Malmberg M, Malm T, Gustafsson O, Sturchio A, Graff C, Espay AJ, et al. Disentangling the amyloid pathways: a mechanistic approach to etiology. Front Neurosci. 2020;14:256.","journal-title":"Front Neurosci"},{"key":"465_CR50","doi-asserted-by":"publisher","first-page":"766","DOI":"10.1021\/cb5008663","volume":"10","author":"MM Rahman","year":"2015","unstructured":"Rahman MM, Zetterberg H, Lendel C, H\u00e4rd T. Binding of human proteins to amyloid-\u03b2 protofibrils. ACS Chem Biol. 2015;10:766\u201374.","journal-title":"ACS Chem Biol"},{"key":"465_CR51","doi-asserted-by":"publisher","first-page":"1053","DOI":"10.3233\/JAD-180596","volume":"66","author":"MM Rahman","year":"2018","unstructured":"Rahman MM, Westermark GT, Zetterberg H, H\u00e4rd T, Sandgren M. Protofibrillar and fibrillar amyloid-\u03b2 binding proteins in cerebrospinal fluid. J Alzheimers Dis. 2018;66:1053\u201364.","journal-title":"J Alzheimers Dis"},{"key":"465_CR52","doi-asserted-by":"publisher","first-page":"3863","DOI":"10.1038\/s41598-019-40483-z","volume":"9","author":"DW Juhl","year":"2019","unstructured":"Juhl DW, Risor MW, Scavenius C, Rasmussen CB, Otzen D, Nielsen NC, et al. Conservation of the amyloid interactome across diverse fibrillar structures. Sci Rep. 2019;9:3863.","journal-title":"Sci Rep"},{"key":"465_CR53","doi-asserted-by":"publisher","first-page":"988","DOI":"10.1021\/acs.biomac.9b01650","volume":"21","author":"A Nandakumar","year":"2020","unstructured":"Nandakumar A, Xing Y, Aranha RR, Faridi A, Kakinen A, Javed I, et al. Human plasma protein corona of A\u03b2 amyloid and its impact on islet amyloid polypeptide cross-seeding. Biomacromolecules. 2020;21:988\u201398.","journal-title":"Biomacromolecules"},{"key":"465_CR54","doi-asserted-by":"publisher","first-page":"6066","DOI":"10.1021\/acsnano.8b02346","volume":"12","author":"EH Pilkington","year":"2018","unstructured":"Pilkington EH, Gustafsson OJR, Xing Y, Hernandez-Fernaud J, Zampronio C, Kakinen A, et al. Profiling the serum protein corona of fibrillar human islet amyloid polypeptide. ACS Nano. 2018;12:6066\u201378.","journal-title":"ACS Nano"},{"key":"465_CR55","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1016\/j.cca.2014.12.016","volume":"441","author":"S Madasamy","year":"2015","unstructured":"Madasamy S, Chaudhuri V, Kong R, Alderete B, Adams CM, Knaak TD, et al. Plaque array method and proteomics-based identification of biomarkers from Alzheimer\u2019s disease serum. Clin Chim Acta. 2015;441:79\u201385.","journal-title":"Clin Chim Acta"},{"key":"465_CR56","doi-asserted-by":"publisher","first-page":"1447","DOI":"10.1021\/acschemneuro.0c00110","volume":"11","author":"H Chaudhary","year":"2020","unstructured":"Chaudhary H, Meister SW, Zetterberg H, L\u00f6fblom J, Lendel C. Dissecting the structural organization of multiprotein amyloid aggregates using a bottom-up approach. ACS Chem Neurosci. 2020;11:1447\u201357.","journal-title":"ACS Chem Neurosci"},{"key":"465_CR57","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.pneurobio.2015.12.004","volume":"137","author":"SH Han","year":"2016","unstructured":"Han SH, Park JC, Mook-Jung I. Amyloid \u03b2-interacting partners in Alzheimer\u2019s disease: from accomplices to possible therapeutic targets. Prog Neurobiol. 2016;137:17\u201338.","journal-title":"Prog Neurobiol"},{"key":"465_CR58","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1007\/s12551-017-0271-9","volume":"9","author":"KL Stewart","year":"2017","unstructured":"Stewart KL, Radford SE. Amyloid plaques beyond A\u03b2: a survey of the diverse modulators of amyloid aggregation. Biophys Rev. 2017;9:405\u201319.","journal-title":"Biophys Rev"},{"key":"465_CR59","doi-asserted-by":"publisher","first-page":"933","DOI":"10.1007\/s00401-017-1691-0","volume":"133","author":"E Drummond","year":"2017","unstructured":"Drummond E, Nayak S, Faustin A, Pires G, Hickman RA, Askenazi M, et al. Proteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer\u2019s disease. Acta Neuropathol. 2017;133:933\u201354.","journal-title":"Acta Neuropathol"},{"key":"465_CR60","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1186\/s40478-018-0540-2","volume":"6","author":"DC Hondius","year":"2018","unstructured":"Hondius DC, Eigenhuis KN, Morrema THJ, van der Schors RC, van Nierop P, Bugiani M, et al. Proteomics analysis identifies new markers associated with capillary cerebral amyloid angiopathy in Alzheimer\u2019s disease. Acta Neuropathol Commun. 2018;6:46.","journal-title":"Acta Neuropathol Commun"},{"key":"465_CR61","doi-asserted-by":"publisher","first-page":"3042","DOI":"10.1093\/brain\/awl279","volume":"129","author":"A Hye","year":"2006","unstructured":"Hye A, Lynham S, Thambisetty M, Causevic M, Campbell J, Byers HL, et al. Proteome-based plasma biomarkers for Alzheimer\u2019s disease. Brain. 2006;129:3042\u201350.","journal-title":"Brain"},{"key":"465_CR62","doi-asserted-by":"publisher","first-page":"654","DOI":"10.1021\/pr501076j","volume":"14","author":"M H\u00f6ltt\u00e4","year":"2015","unstructured":"H\u00f6ltt\u00e4 M, Minthon L, Hansson O, Holm\u00e9n-Larsson J, Pike I, Ward M, et al. An integrated workflow for multiplex CSF proteomics and peptidomics-identification of candidate cerebrospinal fluid biomarkers of Alzheimer\u2019s disease. J Proteome Res. 2015;14:654\u201363.","journal-title":"J Proteome Res"},{"key":"465_CR63","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1016\/S0167-4838(00)00057-1","volume":"1479","author":"R Oyama","year":"2000","unstructured":"Oyama R, Yamamoto H, Titani K. Glutamine synthetase, hemoglobin \u03b1-chain, and macrophage migration inhibitory factor binding to amyloid \u03b2-protein: their identification in rat brain by a novel affinity chromatography and in Alzheimer\u2019s disease brain by immunoprecipitation. Biochim Biophys Acta. 2000;1479:91\u2013102.","journal-title":"Biochim Biophys Acta"},{"key":"465_CR64","doi-asserted-by":"publisher","first-page":"28360","DOI":"10.1074\/jbc.273.43.28360","volume":"273","author":"S Janciauskiene","year":"1998","unstructured":"Janciauskiene S, Rubin H, Lukacs CM, Wright HT. Alzheimer\u2019s peptide A\u03b21-42 binds to two \u03b2-sheets of \u03b11-antichymotrypsin and transforms it from inhibitor to substrate. J Biol Chem. 1998;273:28360\u20134.","journal-title":"J Biol Chem"},{"key":"465_CR65","doi-asserted-by":"publisher","first-page":"668","DOI":"10.1038\/nsb0896-668","volume":"3","author":"S Janciauskiene","year":"1996","unstructured":"Janciauskiene S, Eriksson S, Wright HT. A specific structural interaction of Alzheimer\u2019s peptide A\u03b2 1-42 with \u03b11-antichymotrypsin. Nat Struct Biol. 1996;3:668\u201371.","journal-title":"Nat Struct Biol"},{"key":"465_CR66","doi-asserted-by":"publisher","first-page":"3042","DOI":"10.1002\/pmic.201600057","volume":"16","author":"CM Hales","year":"2016","unstructured":"Hales CM, Dammer EB, Deng Q, Duong DM, Gearing M, Troncoso JC, et al. Changes in the detergent-insoluble brain proteome linked to amyloid and tau in Alzheimer\u2019s disease progression. Proteomics. 2016;16:3042\u201353.","journal-title":"Proteomics"},{"key":"465_CR67","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1016\/0092-8674(88)90462-X","volume":"52","author":"CR Abraham","year":"1988","unstructured":"Abraham CR, Selkoe DJ, Potter H. Immunochemical identification of the serine protease inhibitor \u03b11-antichymotrypsin in the brain amyloid deposits of Alzheimer\u2019s disease. Cell. 1988;52:487\u2013501.","journal-title":"Cell"},{"key":"465_CR68","doi-asserted-by":"publisher","first-page":"668","DOI":"10.1001\/archneur.61.5.668","volume":"61","author":"MJ Engelhart","year":"2004","unstructured":"Engelhart MJ, Geerlings MI, Meijer J, Kiliaan A, Ruitenberg A, van Swieten JC, et al. Inflammatory proteins in plasma and the risk of dementia: the rotterdam study. Arch Neurol. 2004;61:668\u201372.","journal-title":"Arch Neurol"},{"key":"465_CR69","doi-asserted-by":"publisher","first-page":"1373","DOI":"10.1002\/prca.200600999","volume":"1","author":"Y Hu","year":"2007","unstructured":"Hu Y, Hosseini A, Kauwe JS, Gross J, Cairns NJ, Goate AM, et al. Identification and validation of novel CSF biomarkers for early stages of Alzheimer\u2019s disease. Proteomics Clin Appl. 2007;1:1373\u201384.","journal-title":"Proteomics Clin Appl"},{"key":"465_CR70","doi-asserted-by":"publisher","first-page":"10016","DOI":"10.1073\/pnas.89.21.10016","volume":"89","author":"J Rogers","year":"1992","unstructured":"Rogers J, Cooper NR, Webster S, Schultz J, McGeer PL, Styren SD, et al. Complement activation by \u03b2-amyloid in Alzheimer disease. Proc Natl Acad Sci U S A. 1992;89:10016\u201320.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR71","first-page":"1531","volume":"150","author":"S Webster","year":"1997","unstructured":"Webster S, Bonnell B, Rogers J. Charge-based binding of complement component C1q to the Alzheimer amyloid \u03b2-peptide. Am J Pathol. 1997;150:1531\u20136.","journal-title":"Am J Pathol"},{"key":"465_CR72","doi-asserted-by":"publisher","first-page":"147","DOI":"10.3109\/13506129709014379","volume":"4","author":"MD Watson","year":"1997","unstructured":"Watson MD, Roher AE, Kim KS, Spiegel K, Emmerlin MR. Complement interactions with amyloid \u03b21\u201342: a nidus for inflammation in AD brains. Amyloid. 1997;4:147\u201356.","journal-title":"Amyloid"},{"key":"465_CR73","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1097\/01.wad.0000165506.60370.94","volume":"19","author":"H Zanjani","year":"2005","unstructured":"Zanjani H, Finch CE, Kemper C, Atkinson J, McKeel D, Morris JC, et al. Complement activation in very early Alzheimer disease. Alzheimer Dis Assoc Disord. 2005;19:55\u201366.","journal-title":"Alzheimer Dis Assoc Disord"},{"key":"465_CR74","doi-asserted-by":"crossref","unstructured":"Khoonsari PE, H\u00e4ggmark A, L\u00f6nnberg M, Mikus M, Kilander L, Lannfelt L, et al. Analysis of the cerebrospinal fluid proteome in Alzheimer\u2019s disease. PLoS One. 2016;11:e0150672.","DOI":"10.1371\/journal.pone.0150672"},{"key":"465_CR75","doi-asserted-by":"publisher","first-page":"1397","DOI":"10.1016\/j.jalz.2017.03.010","volume":"13","author":"WD Brubaker","year":"2017","unstructured":"Brubaker WD, Crane A, Johansson JU, Yen K, Garfinkel K, Mastroeni D, et al. Peripheral complement interactions with amyloid \u03b2 peptide: erythrocyte clearance mechanisms. Alzheimers Dement. 2017;13:1397\u2013409.","journal-title":"Alzheimers Dement"},{"key":"465_CR76","doi-asserted-by":"publisher","first-page":"244","DOI":"10.1002\/pmic.200300495","volume":"4","author":"R Zhang","year":"2004","unstructured":"Zhang R, Barker L, Pinchev D, Marshall J, Rasamoelisolo M, Smith C, et al. Mining biomarkers in human sera using proteomic tools. Proteomics. 2004;4:244\u201356.","journal-title":"Proteomics"},{"key":"465_CR77","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0028527","volume":"6","author":"M Thambisetty","year":"2011","unstructured":"Thambisetty M, Simmons A, Hye A, Campbell J, Westman E, Zhang Y, et al. Plasma biomarkers of brain atrophy in Alzheimer\u2019s disease. PLoS One. 2011;6:e28527.","journal-title":"PLoS One"},{"key":"465_CR78","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1002\/ana.21038","volume":"61","author":"EJ Finehout","year":"2007","unstructured":"Finehout EJ, Franck Z, Choe LH, Relkin N, Lee KH. Cerebrospinal fluid proteomic biomarkers for Alzheimer\u2019s disease. Ann Neurol. 2007;61:120\u20139.","journal-title":"Ann Neurol"},{"key":"465_CR79","doi-asserted-by":"publisher","first-page":"500","DOI":"10.1016\/j.ymeth.2012.03.018","volume":"56","author":"D Wijte","year":"2012","unstructured":"Wijte D, McDonnell LA, Balog CI, Bossers K, Deelder AM, Swaab DF, et al. A novel peptidomics approach to detect markers of Alzheimer\u2019s disease in cerebrospinal fluid. Methods. 2012;56:500\u20137.","journal-title":"Methods"},{"key":"465_CR80","doi-asserted-by":"publisher","first-page":"3617","DOI":"10.1016\/j.jprot.2012.04.017","volume":"75","author":"MH Yang","year":"2012","unstructured":"Yang MH, Yang YH, Lu CY, Jong SB, Chen LJ, Lin YF, et al. Activity-dependent neuroprotector homeobox protein: a candidate protein identified in serum as diagnostic biomarker for Alzheimer\u2019s disease. J Proteomics. 2012;75:3617\u201329.","journal-title":"J Proteomics"},{"key":"465_CR81","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1016\/0304-3940(95)11565-7","volume":"191","author":"A Golabek","year":"1995","unstructured":"Golabek A, Marques MA, Lalowski M, Wisniewski T. Amyloid \u03b2 binding proteins in vitro and in normal human cerebrospinal fluid. Neurosci Lett. 1995;191:79\u201382.","journal-title":"Neurosci Lett"},{"key":"465_CR82","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/S0009-8981(97)00207-6","volume":"270","author":"AR Koudinov","year":"1998","unstructured":"Koudinov AR, Berezov TT, Kumar A, Koudinova NV. Alzheimer's amyloid \u03b2 interaction with normal human plasma high density lipoprotein: association with apolipoprotein and lipids. Clin Chim Acta. 1998;270:75\u201384.","journal-title":"Clin Chim Acta"},{"key":"465_CR83","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1007\/978-1-61779-551-0_15","volume":"849","author":"M Calero","year":"2012","unstructured":"Calero M, Rostagno A, Ghiso J. Search for amyloid-binding proteins by affinity chromatography. Methods Mol Biol. 2012;849:213\u201323.","journal-title":"Methods Mol Biol"},{"key":"465_CR84","doi-asserted-by":"crossref","unstructured":"Koldamova RP, Lefterov IM, Lefterova MI, Lazo JS. Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A\u03b2 aggregation and toxicity. Biochemistry. 2001;40:3553\u201360.","DOI":"10.1021\/bi002186k"},{"key":"465_CR85","doi-asserted-by":"publisher","first-page":"755","DOI":"10.1194\/jlr.C500022-JLR200","volume":"47","author":"LM Wilson","year":"2006","unstructured":"Wilson LM, Pham CL, Jenkins AJ, Wade JD, Hill AF, Perugini MA, et al. High density lipoproteins bind A\u03b2 and apolipoprotein C-II amyloid fibrils. J Lipid Res. 2006;47:755\u201360.","journal-title":"J Lipid Res"},{"key":"465_CR86","first-page":"238","volume":"147","author":"T Wisniewski","year":"1995","unstructured":"Wisniewski T, Golabek AA, Kida E, Wisniewski KE, Frangione B. Conformational mimicry in Alzheimer\u2019s disease. Role of apolipoproteins in amyloidogenesis. Am J Pathol. 1995;147:238\u201344.","journal-title":"Am J Pathol"},{"key":"465_CR87","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1159\/000090676","volume":"21","author":"HC Liu","year":"2006","unstructured":"Liu HC, Hu CJ, Chang JG, Sung SM, Lee LS, Yuan RY, et al. Proteomic identification of lower apolipoprotein A-I in Alzheimer\u2019s disease. Dement Geriatr Cogn Disord. 2006;21:155\u201361.","journal-title":"Dement Geriatr Cogn Disord"},{"key":"465_CR88","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1080\/01616412.2017.1281195","volume":"39","author":"Y Kitamura","year":"2017","unstructured":"Kitamura Y, Usami R, Ichihara S, Kida H, Satoh M, Tomimoto H, et al. Plasma protein profiling for potential biomarkers in the early diagnosis of Alzheimer\u2019s disease. Neurol Res. 2017;39:231\u20138.","journal-title":"Neurol Res"},{"key":"465_CR89","doi-asserted-by":"publisher","first-page":"361","DOI":"10.3233\/JAD-160913","volume":"56","author":"L Shen","year":"2017","unstructured":"Shen L, Liao L, Chen C, Guo Y, Song D, Wang Y, et al. Proteomics analysis of blood serums from Alzheimer\u2019s disease patients using iTRAQ labeling technology. J Alzheimers Dis. 2017;56:361\u201378.","journal-title":"J Alzheimers Dis"},{"key":"465_CR90","doi-asserted-by":"publisher","first-page":"639","DOI":"10.3233\/JAD-180855","volume":"67","author":"PE Khoonsari","year":"2019","unstructured":"Khoonsari PE, Shevchenko G, Herman S, Remnestal J, Giedraitis V, Brundin R, et al. Improved differential diagnosis of Alzheimer\u2019s disease by integrating ELISA and mass spectrometry-based cerebrospinal fluid biomarkers. J Alzheimers Dis. 2019;67:639\u201351.","journal-title":"J Alzheimers Dis"},{"key":"465_CR91","doi-asserted-by":"publisher","first-page":"434","DOI":"10.1159\/000110576","volume":"24","author":"AH Simonsen","year":"2007","unstructured":"Simonsen AH, McGuire J, Podust VN, Hagnelius NO, Nilsson TK, Kapaki E, et al. A novel panel of cerebrospinal fluid biomarkers for the differential diagnosis of Alzheimer\u2019s disease versus normal aging and frontotemporal dementia. Dement Geriatr Cogn Disord. 2007;24:434\u201340.","journal-title":"Dement Geriatr Cogn Disord"},{"key":"465_CR92","doi-asserted-by":"publisher","first-page":"855","DOI":"10.3233\/JAD-140111","volume":"41","author":"Y-H Shih","year":"2014","unstructured":"Shih Y-H, Tsai K-J, Lee C-W, Shiesh S-C, Chen W-T, Pai M-C, et al. Apolipoprotein C-III is an amyloid-\u03b2-binding protein and an early marker for Alzheimer\u2019s disease. J Alzheimers Dis. 2014;41:855\u201365.","journal-title":"J Alzheimers Dis"},{"key":"465_CR93","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1179\/his.2001.24.1.45","volume":"24","author":"A Navarro","year":"2001","unstructured":"Navarro A, Astudillo A, Valle E, Rey CG, Tolivia J. Immunohistochemical presence of apolipoprotein D in senile plaques. J Histotechnol. 2001;24:45\u20138.","journal-title":"J Histotechnol"},{"key":"465_CR94","doi-asserted-by":"publisher","first-page":"697","DOI":"10.1016\/S0014-4886(03)00315-7","volume":"184","author":"A Navarro","year":"2003","unstructured":"Navarro A, Del Valle E, Astudillo A, Gonzalez del Rey C, Tolivia J. Immunohistochemical study of distribution of apolipoproteins E and D in human cerebral \u03b2 amyloid deposits. Exp Neurol. 2003;184:697\u2013704.","journal-title":"Exp Neurol"},{"key":"465_CR95","doi-asserted-by":"publisher","first-page":"1303","DOI":"10.3233\/JAD-140141","volume":"44","author":"Z Ol\u00e1h","year":"2015","unstructured":"Ol\u00e1h Z, K\u00e1lm\u00e1n J, Toth ME, Zvara A, S\u00e1ntha M, Ivitz E, et al. Proteomic analysis of cerebrospinal fluid in Alzheimer\u2019s disease: wanted dead or alive. J Alzheimers Dis. 2015;44:1303\u201312.","journal-title":"J Alzheimers Dis"},{"key":"465_CR96","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0018850","volume":"6","author":"R Craig-Schapiro","year":"2011","unstructured":"Craig-Schapiro R, Kuhn M, Xiong C, Pickering EH, Liu J, Misko TP, et al. Multiplexed immunoassay panel identifies novel CSF biomarkers for Alzheimer\u2019s disease diagnosis and prognosis. PLoS One. 2011;6:e18850.","journal-title":"PLoS One"},{"key":"465_CR97","doi-asserted-by":"publisher","DOI":"10.1038\/tp.2016.194","volume":"6","author":"RW Paterson","year":"2016","unstructured":"Paterson RW, Heywood WE, Heslegrave AJ, Magdalinou NK, Andreasson U, Sirka E, et al. A targeted proteomic multiplex CSF assay identifies increased malate dehydrogenase and other neurodegenerative biomarkers in individuals with Alzheimer\u2019s disease pathology. Transl Psychiatry. 2016;6:e952.","journal-title":"Transl Psychiatry"},{"key":"465_CR98","doi-asserted-by":"publisher","first-page":"625","DOI":"10.3233\/JAD-2011-111505","volume":"28","author":"B Vafadar-Isfahani","year":"2012","unstructured":"Vafadar-Isfahani B, Ball G, Coveney C, Lemetre C, Boocock D, Minthon L, et al. Identification of SPARC-like 1 protein as part of a biomarker panel for Alzheimer\u2019s disease in cerebrospinal fluid. J Alzheimers Dis. 2012;28:625\u201336.","journal-title":"J Alzheimers Dis"},{"key":"465_CR99","doi-asserted-by":"publisher","first-page":"18644","DOI":"10.1074\/jbc.272.30.18644","volume":"272","author":"SM Hammad","year":"1997","unstructured":"Hammad SM, Ranganathan S, Loukinova E, Twal WO, Argraves WS. Interaction of apolipoprotein J-amyloid \u03b2-peptide complex with low density lipoprotein receptor-related protein-2\/megalin. A mechanism to prevent pathological accumulation of amyloid \u03b2-peptide. J Biol Chem. 1997;272:18644\u20139.","journal-title":"J Biol Chem"},{"key":"465_CR100","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1002\/1097-0029(20000815)50:4<305::AID-JEMT10>3.0.CO;2-L","volume":"50","author":"M Calero","year":"2000","unstructured":"Calero M, Rostagno A, Matsubara E, Zlokovic B, Frangione B, Ghiso J. Apolipoprotein J (clusterin) and Alzheimer\u2019s disease. Microsc Res Tech. 2000;50:305\u201315.","journal-title":"Microsc Res Tech"},{"key":"465_CR101","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1016\/0006-8993(92)90071-G","volume":"579","author":"PL McGeer","year":"1992","unstructured":"McGeer PL, Kawamata T, Walker DG. Distribution of clusterin in Alzheimer brain tissue. Brain Res. 1992;579:337\u201341.","journal-title":"Brain Res"},{"key":"465_CR102","doi-asserted-by":"publisher","first-page":"506","DOI":"10.1002\/prca.200600684","volume":"1","author":"PC Liao","year":"2007","unstructured":"Liao PC, Yu L, Kuo CC, Lin C, Kuo YM. Proteomics analysis of plasma for potential biomarkers in the diagnosis of Alzheimer\u2019s disease. Proteomics Clin Appl. 2007;1:506\u201312.","journal-title":"Proteomics Clin Appl"},{"key":"465_CR103","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1016\/j.brainres.2009.01.058","volume":"1265","author":"GN Yin","year":"2009","unstructured":"Yin GN, Lee HW, Cho JY, Suk K. Neuronal pentraxin receptor in cerebrospinal fluid as a potential biomarker for neurodegenerative diseases. Brain Res. 2009;1265:158\u201370.","journal-title":"Brain Res"},{"key":"465_CR104","doi-asserted-by":"publisher","first-page":"2240","DOI":"10.1002\/pmic.200300475","volume":"3","author":"HL Yu","year":"2003","unstructured":"Yu HL, Chertkow HM, Bergman H, Schipper HM. Aberrant profiles of native and oxidized glycoproteins in Alzheimer plasma. Proteomics. 2003;3:2240\u20138.","journal-title":"Proteomics"},{"key":"465_CR105","doi-asserted-by":"publisher","first-page":"3275","DOI":"10.1073\/pnas.95.6.3275","volume":"95","author":"SR Hughes","year":"1998","unstructured":"Hughes SR, Khorkova O, Goyal S, Knaeblein J, Heroux J, Riedel NG, et al. \u03b12-macroglobulin associates with \u03b2-amyloid peptide and prevents fibril formation. Proc Natl Acad Sci U S A. 1998;95:3275\u201380.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR106","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1046\/j.1471-4159.1997.69010299.x","volume":"69","author":"Y Du","year":"1997","unstructured":"Du Y, Ni B, Glinn M, Dodel RC, Bales KR, Zhang Z, et al. \u03b12-Macroglobulin as a \u03b2-amyloid peptide-binding plasma protein. J Neurochem. 1997;69:299\u2013305.","journal-title":"J Neurochem"},{"key":"465_CR107","doi-asserted-by":"publisher","first-page":"1077","DOI":"10.1001\/archneurol.2010.215","volume":"67","author":"SE O\u2019Bryant","year":"2010","unstructured":"O\u2019Bryant SE, Xiao G, Barber R, Reisch J, Doody R, Fairchild T, et al. A serum protein-based algorithm for the detection of Alzheimer disease. Arch Neurol. 2010;67:1077\u201381.","journal-title":"Arch Neurol"},{"key":"465_CR108","first-page":"886","volume":"143","author":"RN Kalaria","year":"1993","unstructured":"Kalaria RN, Golde T, Kroon SN, Perry G. Serine protease inhibitor antithrombin III and its messenger RNA in the pathogenesis of Alzheimer\u2019s disease. Am J Pathol. 1993;143:886\u201393.","journal-title":"Am J Pathol"},{"key":"465_CR109","doi-asserted-by":"publisher","first-page":"991","DOI":"10.3233\/JAD-160751","volume":"56","author":"R Salza","year":"2017","unstructured":"Salza R, Lethias C, Ricard-Blum S. The multimerization state of the amyloid-\u03b242 amyloid peptide governs its interaction network with the extracellular matrix. J Alzheimers Dis. 2017;56:991\u20131005.","journal-title":"J Alzheimers Dis"},{"key":"465_CR110","doi-asserted-by":"publisher","first-page":"995","DOI":"10.1111\/jth.13209","volume":"14","author":"D Zamolodchikov","year":"2016","unstructured":"Zamolodchikov D, Renne T, Strickland S. The Alzheimer\u2019s disease peptide \u03b2-amyloid promotes thrombin generation through activation of coagulation factor XII. J Thromb Haemost. 2016;14:995\u20131007.","journal-title":"J Thromb Haemost"},{"key":"465_CR111","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1006\/clim.1998.4621","volume":"90","author":"Y Shibayama","year":"1999","unstructured":"Shibayama Y, Joseph K, Nakazawa Y, Ghebreihiwet B, Peerschke EI, Kaplan AP. Zinc-dependent activation of the plasma kinin-forming cascade by aggregated \u03b2 amyloid protein. Clin Immunol. 1999;90:89\u201399.","journal-title":"Clin Immunol"},{"key":"465_CR112","doi-asserted-by":"publisher","first-page":"21812","DOI":"10.1073\/pnas.1010373107","volume":"107","author":"HJ Ahn","year":"2010","unstructured":"Ahn HJ, Zamolodchikov D, Cortes-Canteli M, Norris EH, Glickman JF, Strickland S. Alzheimer\u2019s disease peptide \u03b2-amyloid interacts with fibrinogen and induces its oligomerization. Proc Natl Acad Sci U S A. 2010;107:21812\u20137.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR113","doi-asserted-by":"publisher","first-page":"695","DOI":"10.1016\/j.neuron.2010.05.014","volume":"66","author":"M Cortes-Canteli","year":"2010","unstructured":"Cortes-Canteli M, Paul J, Norris EH, Bronstein R, Ahn HJ, Zamolodchikov D, et al. Fibrinogen and \u03b2-amyloid association alters thrombosis and fibrinolysis: a possible contributing factor to Alzheimer\u2019s disease. Neuron. 2010;66:695\u2013709.","journal-title":"Neuron"},{"key":"465_CR114","doi-asserted-by":"publisher","first-page":"59","DOI":"10.3233\/JAD-160599","volume":"55","author":"PP Sainaghi","year":"2017","unstructured":"Sainaghi PP, Bellan M, Lombino F, Alciato F, Carecchio M, Galimberti D, et al. Growth arrest specific 6 concentration is increased in the cerebrospinal fluid of patients with Alzheimer\u2019s disease. J Alzheimers Dis. 2017;55:59\u201365.","journal-title":"J Alzheimers Dis"},{"key":"465_CR115","doi-asserted-by":"crossref","unstructured":"Hadley KC, Rakhit R, Guo H, Sun Y, Jonkman JE, McLaurin J, et al. Determining composition of micron-scale protein deposits in neurodegenerative disease by spatially targeted optical microproteomics. Elife. 2015;4","DOI":"10.7554\/eLife.09579"},{"key":"465_CR116","doi-asserted-by":"publisher","first-page":"755","DOI":"10.1002\/psc.998","volume":"14","author":"Y Verdier","year":"2008","unstructured":"Verdier Y, F\u00f6ldi I, Sergeant N, F\u00fcl\u00f6p L, Penke Z, Jan\u00e1ky T, et al. Characterization of the interaction between A\u03b2 1\u201342 and glyceraldehyde phosphodehydrogenase. J Pept Sci. 2008;14:755\u201362.","journal-title":"J Pept Sci"},{"key":"465_CR117","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1016\/j.bpj.2010.11.037","volume":"100","author":"J Milojevic","year":"2011","unstructured":"Milojevic J, Melacini G. Stoichiometry and affinity of the human serum albumin-Alzheimer\u2019s A\u03b2 peptide interactions. Biophys J. 2011;100:183\u201392.","journal-title":"Biophys J"},{"key":"465_CR118","doi-asserted-by":"publisher","first-page":"159","DOI":"10.3233\/JAD-2012-111139","volume":"29","author":"M Costa","year":"2012","unstructured":"Costa M, Ortiz AM, Jorquera JI. Therapeutic albumin binding to remove amyloid-\u03b2. J Alzheimers Dis. 2012;29:159\u201370.","journal-title":"J Alzheimers Dis"},{"key":"465_CR119","doi-asserted-by":"publisher","first-page":"714","DOI":"10.1016\/j.bbrc.2007.10.080","volume":"364","author":"M Rozga","year":"2007","unstructured":"Rozga M, Kloniecki M, Jablonowska A, Dadlez M, Bal W. The binding constant for amyloid A\u03b240 peptide interaction with human serum albumin. Biochem Biophys Res Commun. 2007;364:714\u20138.","journal-title":"Biochem Biophys Res Commun"},{"key":"465_CR120","doi-asserted-by":"publisher","first-page":"17158","DOI":"10.1074\/jbc.M117.792853","volume":"292","author":"M Algamal","year":"2017","unstructured":"Algamal M, Ahmed R, Jafari N, Ahsan B, Ortega J, Melacini G. Atomic-resolution map of the interactions between an amyloid inhibitor protein and amyloid \u03b2 (A\u03b2) peptides in the monomer and protofibril states. J Biol Chem. 2017;292:17158\u201368.","journal-title":"J Biol Chem"},{"key":"465_CR121","doi-asserted-by":"publisher","first-page":"936","DOI":"10.1016\/j.febslet.2008.02.034","volume":"582","author":"R Costa","year":"2008","unstructured":"Costa R, Goncalves A, Saraiva MJ, Cardoso I. Transthyretin binding to A\u03b2 peptide\u2014impact on A\u03b2 fibrillogenesis and toxicity. FEBS Lett. 2008;582:936\u201342.","journal-title":"FEBS Lett"},{"key":"465_CR122","doi-asserted-by":"publisher","first-page":"2681","DOI":"10.1073\/pnas.0712197105","volume":"105","author":"JN Buxbaum","year":"2008","unstructured":"Buxbaum JN, Ye Z, Reixach N, Friske L, Levy C, Das P, et al. Transthyretin protects Alzheimer\u2019s mice from the behavioral and biochemical effects of A\u03b2 toxicity. Proc Natl Acad Sci U S A. 2008;105:2681\u20136.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR123","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1016\/j.jprot.2018.04.027","volume":"182","author":"I Begcevic","year":"2018","unstructured":"Begcevic I, Brinc D, Brown M, Martinez-Morillo E, Goldhardt O, Grimmer T, et al. Brain-related proteins as potential CSF biomarkers of Alzheimer\u2019s disease: a targeted mass spectrometry approach. J Proteomics. 2018;182:12\u201320.","journal-title":"J Proteomics"},{"key":"465_CR124","doi-asserted-by":"crossref","unstructured":"Brinkmalm G, Sj\u00f6din S, Simonsen AH, Hasselbalch SG, Zetterberg H, Brinkmalm A, et al. A parallel reaction monitoring mass spectrometric method for analysis of potential CSF biomarkers for Alzheimer\u2019s disease. Proteomics Clin Appl. 2018;12","DOI":"10.1002\/prca.201700131"},{"key":"465_CR125","doi-asserted-by":"crossref","unstructured":"van Steenoven I, Noli B, Cocco C, Ferri GL, Oeckl P, Otto M, et al. VGF peptides in cerebrospinal fluid of patients with dementia with lewy bodies. Int J Mol Sci. 2019;20","DOI":"10.3390\/ijms20194674"},{"key":"465_CR126","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1006\/mcne.1999.0816","volume":"15","author":"SL Cotman","year":"2000","unstructured":"Cotman SL, Halfter W, Cole GJ. Agrin binds to \u03b2-amyloid (A\u03b2), accelerates a\u03b2 fibril formation, and is localized to A\u03b2 deposits in Alzheimer\u2019s disease brain. Mol Cell Neurosci. 2000;15:183\u201398.","journal-title":"Mol Cell Neurosci"},{"key":"465_CR127","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.dadm.2014.11.008","volume":"1","author":"M Del Campo Milan","year":"2015","unstructured":"Del Campo Milan M, Zuroff L, Jimenez CR, Scheltens P, Teunissen CE. Can agrin cerebrospinal fluid concentration be used as an early biomarker for Alzheimer\u2019s disease? Alzheimers Dement (Amst). 2015;1:75\u201380.","journal-title":"Alzheimers Dement (Amst)"},{"key":"465_CR128","doi-asserted-by":"publisher","first-page":"84","DOI":"10.1006\/abbi.1995.1345","volume":"320","author":"AD Snow","year":"1995","unstructured":"Snow AD, Kinsella MG, Parks E, Sekiguchi RT, Miller JD, Kimata K, et al. Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin, and versican) to the \u03b2-amyloid protein of Alzheimer\u2019s disease. Arch Biochem Biophys. 1995;320:84\u201395.","journal-title":"Arch Biochem Biophys"},{"key":"465_CR129","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1177\/40.1.1370306","volume":"40","author":"AD Snow","year":"1992","unstructured":"Snow AD, Mar H, Nochlin D, Kresse H, Wight TN. Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer\u2019s disease. J Histochem Cytochem. 1992;40:105\u201313.","journal-title":"J Histochem Cytochem"},{"key":"465_CR130","doi-asserted-by":"publisher","first-page":"1013","DOI":"10.1096\/fj.03-1040fje","volume":"18","author":"N Watanabe","year":"2004","unstructured":"Watanabe N, Araki W, Chui D-H, Makifuchi T, Ihara Y, Tabira T. Glypican-1 as an A\u03b2 binding HSPG in the human brain: its localization in DIG domains and possible roles in the pathogenesis of Alzheimer\u2019s disease. FASEB J. 2004;18:1013\u20135.","journal-title":"FASEB J"},{"key":"465_CR131","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/0165-5728(91)90067-H","volume":"32","author":"H Akiyama","year":"1991","unstructured":"Akiyama H, Kawamata T, Dedhar S, McGeer PL. Immunohistochemical localization of vitronectin, its receptor and \u03b2-3 integrin in Alzheimer brain tissue. J Neuroimmunol. 1991;32:19\u201328.","journal-title":"J Neuroimmunol"},{"key":"465_CR132","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1080\/00365510601009738","volume":"67","author":"ML Selenica","year":"2007","unstructured":"Selenica ML, Wang X, Ostergaard-Pedersen L, Westlind-Danielsson A, Grubb A. Cystatin C reduces the in vitro formation of soluble A\u03b21-42 oligomers and protofibrils. Scand J Clin Lab Invest. 2007;67:179\u201390.","journal-title":"Scand J Clin Lab Invest"},{"key":"465_CR133","doi-asserted-by":"publisher","first-page":"1033","DOI":"10.1016\/j.neurobiolaging.2003.11.006","volume":"25","author":"M Sastre","year":"2004","unstructured":"Sastre M, Calero M, Pawlik M, Mathews PM, Kumar A, Danilov V, et al. Binding of cystatin C to Alzheimer\u2019s amyloid \u03b2 inhibits in vitro amyloid fibril formation. Neurobiol Aging. 2004;25:1033\u201343.","journal-title":"Neurobiol Aging"},{"key":"465_CR134","doi-asserted-by":"publisher","first-page":"1152","DOI":"10.1111\/jnc.13216","volume":"134","author":"KA Bruggink","year":"2015","unstructured":"Bruggink KA, Kuiperij HB, Gloerich J, Otte-H\u00f6ller I, Rozemuller AJM, Claassen JAHR, et al. Dickkopf-related protein 3 is a potential A\u03b2-associated protein in Alzheimer\u2019s disease. J Neurochem. 2015;134:1152\u201362.","journal-title":"J Neurochem"},{"key":"465_CR135","doi-asserted-by":"publisher","first-page":"241","DOI":"10.1006\/bbrc.1999.0623","volume":"258","author":"VP Chauhan","year":"1999","unstructured":"Chauhan VP, Ray I, Chauhan A, Wisniewski HM. Binding of gelsolin, a secretory protein, to amyloid \u03b2-protein. Biochem Biophys Res Commun. 1999;258:241\u20136.","journal-title":"Biochem Biophys Res Commun"},{"key":"465_CR136","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1016\/j.bios.2014.12.041","volume":"68","author":"Y Yu","year":"2015","unstructured":"Yu Y, Sun X, Tang D, Li C, Zhang L, Nie D, et al. Gelsolin bound \u03b2-amyloid peptides(1-40\/1-42): electrochemical evaluation of levels of soluble peptide associated with Alzheimer\u2019s disease. Biosens Bioelectron. 2015;68:115\u201321.","journal-title":"Biosens Bioelectron"},{"key":"465_CR137","doi-asserted-by":"publisher","first-page":"12832","DOI":"10.1002\/anie.201405001","volume":"53","author":"Y Yu","year":"2014","unstructured":"Yu Y, Zhang L, Li C, Sun X, Tang D, Shi G. A method for evaluating the level of soluble \u03b2-amyloid(1-40\/1-42) in Alzheimer\u2019s disease based on the binding of gelsolin to \u03b2-amyloid peptides. Angew Chem Int Ed Engl. 2014;53:12832\u20135.","journal-title":"Angew Chem Int Ed Engl"},{"key":"465_CR138","doi-asserted-by":"publisher","first-page":"7423","DOI":"10.1038\/s41598-020-64461-y","volume":"10","author":"SA Park","year":"2020","unstructured":"Park SA, Jung JM, Park JS, Lee JH, Park B, Kim HJ, et al. SWATH-MS analysis of cerebrospinal fluid to generate a robust battery of biomarkers for Alzheimer\u2019s disease. Sci Rep. 2020;10:7423.","journal-title":"Sci Rep"},{"key":"465_CR139","doi-asserted-by":"publisher","first-page":"10392","DOI":"10.1074\/jbc.270.18.10392","volume":"270","author":"H Hamazaki","year":"1995","unstructured":"Hamazaki H. Ca(2+)-dependent binding of human serum amyloid P component to Alzheimer\u2019s \u03b2-amyloid peptide. J Biol Chem. 1995;270:10392\u20134.","journal-title":"J Biol Chem"},{"key":"465_CR140","doi-asserted-by":"publisher","first-page":"1181","DOI":"10.1084\/jem.177.4.1181","volume":"177","author":"F Gaskin","year":"1993","unstructured":"Gaskin F, Finley J, Fang Q, Xu S, Fu SM. Human antibodies reactive with \u03b2-amyloid protein in Alzheimer\u2019s disease. J Exp Med. 1993;177:1181\u20136.","journal-title":"J Exp Med"},{"key":"465_CR141","doi-asserted-by":"publisher","first-page":"801","DOI":"10.1212\/WNL.57.5.801","volume":"57","author":"Y Du","year":"2001","unstructured":"Du Y, Dodel R, Hampel H, Buerger K, Lin S, Eastwood B, et al. Reduced levels of amyloid \u03b2-peptide antibody in Alzheimer disease. Neurology. 2001;57:801\u20135.","journal-title":"Neurology"},{"key":"465_CR142","doi-asserted-by":"publisher","first-page":"943","DOI":"10.1016\/S0531-5565(02)00029-3","volume":"37","author":"ME Weksler","year":"2002","unstructured":"Weksler ME, Relkin N, Turkenich R, LaRusse S, Zhou L, Szabo P. Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals. Exp Gerontol. 2002;37:943\u20138.","journal-title":"Exp Gerontol"},{"key":"465_CR143","doi-asserted-by":"publisher","first-page":"4714","DOI":"10.1074\/jbc.M707983200","volume":"283","author":"H Taguchi","year":"2008","unstructured":"Taguchi H, Planque S, Nishiyama Y, Symersky J, Boivin S, Szabo P, et al. Autoantibody-catalyzed hydrolysis of amyloid \u03b2 peptide. J Biol Chem. 2008;283:4714\u201322.","journal-title":"J Biol Chem"},{"key":"465_CR144","doi-asserted-by":"publisher","first-page":"807","DOI":"10.1016\/j.autrev.2010.07.008","volume":"9","author":"T Colasanti","year":"2010","unstructured":"Colasanti T, Barbati C, Rosano G, Malorni W, Ortona E. Autoantibodies in patients with Alzheimer\u2019s disease: pathogenetic role and potential use as biomarkers of disease progression. Autoimmun Rev. 2010;9:807\u201311.","journal-title":"Autoimmun Rev"},{"key":"465_CR145","doi-asserted-by":"publisher","first-page":"13460","DOI":"10.1523\/JNEUROSCI.1333-13.2013","volume":"33","author":"AH Stephan","year":"2013","unstructured":"Stephan AH, Madison DV, Mateos JM, Fraser DA, Lovelett EA, Coutellier L, et al. A dramatic increase of C1q protein in the CNS during normal aging. J Neurosci. 2013;33:13460\u201374.","journal-title":"J Neurosci"},{"key":"465_CR146","doi-asserted-by":"publisher","first-page":"712","DOI":"10.1126\/science.aad8373","volume":"352","author":"S Hong","year":"2016","unstructured":"Hong S, Beja-Glasser VF, Nfonoyim BM, Frouin A, Li S, Ramakrishnan S, et al. Complement and microglia mediate early synapse loss in Alzheimer mouse models. Science. 2016;352:712\u20136.","journal-title":"Science"},{"key":"465_CR147","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1016\/S0165-5728(03)00040-7","volume":"137","author":"M S\u00e1rv\u00e1ri","year":"2003","unstructured":"S\u00e1rv\u00e1ri M, V\u00e1g\u00f3 I, W\u00e9ber CS, Nagy J, G\u00e1l P, M\u00e1k M, et al. Inhibition of C1q-\u03b2-amyloid binding protects hippocampal cells against complement mediated toxicity. J Neuroimmunol. 2003;137:12\u20138.","journal-title":"J Neuroimmunol"},{"key":"465_CR148","doi-asserted-by":"publisher","first-page":"448","DOI":"10.1002\/jnr.490390412","volume":"39","author":"S Webster","year":"1994","unstructured":"Webster S, O\u2019Barr S, Rogers J. Enhanced aggregation and \u03b2 structure of amyloid \u03b2 peptide after coincubation with C1q. J Neurosci Res. 1994;39:448\u201356.","journal-title":"J Neurosci Res"},{"key":"465_CR149","doi-asserted-by":"publisher","first-page":"526","DOI":"10.1046\/j.1365-2249.1999.00835.x","volume":"115","author":"L Bergamaschini","year":"1999","unstructured":"Bergamaschini L, Canziani S, Bottasso B, Cugno M, Braidotti P, Agostoni A. Alzheimer\u2019s \u03b2-amyloid peptides can activate the early components of complement classical pathway in a C1q-independent manner. Clin Exp Immunol. 1999;115:526\u201333.","journal-title":"Clin Exp Immunol"},{"key":"465_CR150","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1016\/S0006-8993(98)00346-1","volume":"796","author":"Y Shen","year":"1998","unstructured":"Shen Y, Sullivan T, Lee CM, Meri S, Shiosaki K, Lin CW. Induced expression of neuronal membrane attack complex and cell death by Alzheimer\u2019s \u03b2-amyloid peptide. Brain Res. 1998;796:187\u201397.","journal-title":"Brain Res"},{"key":"465_CR151","doi-asserted-by":"publisher","first-page":"2111","DOI":"10.1016\/j.celrep.2019.07.060","volume":"28","author":"T Wu","year":"2019","unstructured":"Wu T, Dejanovic B, Gandham VD, Gogineni A, Edmonds R, Schauer S, et al. Complement C3 is activated in human AD brain and is required for neurodegeneration in mouse models of amyloidosis and tauopathy. Cell Rep. 2019;28:2111\u201323.e6.","journal-title":"Cell Rep"},{"key":"465_CR152","doi-asserted-by":"publisher","first-page":"13029","DOI":"10.1523\/JNEUROSCI.1698-15.2015","volume":"35","author":"Q Shi","year":"2015","unstructured":"Shi Q, Colodner KJ, Matousek SB, Merry K, Hong S, Kenison JE, et al. Complement C3-deficient mice fail to display age-related hippocampal decline. J Neurosci. 2015;35:13029\u201342.","journal-title":"J Neurosci"},{"key":"465_CR153","doi-asserted-by":"publisher","first-page":"577","DOI":"10.1523\/JNEUROSCI.2117-15.2016","volume":"36","author":"H Lian","year":"2016","unstructured":"Lian H, Litvinchuk A, Chiang AC, Aithmitti N, Jankowsky JL, Zheng H. Astrocyte-microglia cross talk through complement activation modulates amyloid pathology in mouse models of Alzheimer\u2019s disease. J Neurosci. 2016;36:577\u201389.","journal-title":"J Neurosci"},{"key":"465_CR154","doi-asserted-by":"publisher","first-page":"6333","DOI":"10.1523\/JNEUROSCI.0829-08.2008","volume":"28","author":"M Maier","year":"2008","unstructured":"Maier M, Peng Y, Jiang L, Seabrook TJ, Carroll MC, Lemere CA. Complement C3 deficiency leads to accelerated amyloid \u03b2 plaque deposition and neurodegeneration and modulation of the microglia\/macrophage phenotype in amyloid precursor protein transgenic mice. J Neurosci. 2008;28:6333\u201341.","journal-title":"J Neurosci"},{"key":"465_CR155","doi-asserted-by":"crossref","unstructured":"Shi Q, Chowdhury S, Ma R, Le KX, Hong S, Caldarone BJ, et al. Complement C3 deficiency protects against neurodegeneration in aged plaque-rich APP\/PS1 mice. Sci Transl Med. 2017;9","DOI":"10.1126\/scitranslmed.aaf6295"},{"key":"465_CR156","doi-asserted-by":"publisher","first-page":"3020","DOI":"10.1093\/brain\/awl255","volume":"129","author":"J Padmanabhan","year":"2006","unstructured":"Padmanabhan J, Levy M, Dickson DW, Potter H. \u03b11-antichymotrypsin, an inflammatory protein overexpressed in Alzheimer\u2019s disease brain, induces tau phosphorylation in neurons. Brain. 2006;129:3020\u201334.","journal-title":"Brain"},{"key":"465_CR157","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1002\/ana.10414","volume":"53","author":"ST DeKosky","year":"2003","unstructured":"DeKosky ST, Ikonomovic MD, Wang X, Farlow M, Wisniewski S, Lopez OL, et al. Plasma and cerebrospinal fluid \u03b11-antichymotrypsin levels in Alzheimer\u2019s disease: correlation with cognitive impairment. Ann Neurol. 2003;53:81\u201390.","journal-title":"Ann Neurol"},{"key":"465_CR158","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1016\/j.neuron.2020.02.034","volume":"106","author":"N Zhao","year":"2020","unstructured":"Zhao N, Ren Y, Yamazaki Y, Qiao W, Li F, Felton LM, et al. Alzheimer\u2019s risk factors age, APOE genotype, and sex drive distinct molecular pathways. Neuron. 2020;106:727\u201342.e6.","journal-title":"Neuron"},{"key":"465_CR159","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1038\/372092a0","volume":"372","author":"J Ma","year":"1994","unstructured":"Ma J, Yee A, Brewer HB Jr, Das S, Potter H. Amyloid-associated proteins \u03b11-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer \u03b2-protein into filaments. Nature. 1994;372:92\u20134.","journal-title":"Nature"},{"key":"465_CR160","doi-asserted-by":"publisher","first-page":"1444","DOI":"10.1523\/JNEUROSCI.21-05-01444.2001","volume":"21","author":"LN Nilsson","year":"2001","unstructured":"Nilsson LN, Bales KR, DiCarlo G, Gordon MN, Morgan D, Paul SM, et al. \u03b1-1-antichymotrypsin promotes \u03b2-sheet amyloid plaque deposition in a transgenic mouse model of Alzheimer\u2019s disease. J Neurosci. 2001;21:1444\u201351.","journal-title":"J Neurosci"},{"key":"465_CR161","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1007\/s12031-007-0060-1","volume":"33","author":"JA Hamilton","year":"2007","unstructured":"Hamilton JA, Hillard CJ, Spector AA, Watkins PA. Brain uptake and utilization of fatty acids, lipids and lipoproteins: application to neurological disorders. J Mol Neurosci. 2007;33:2\u201311.","journal-title":"J Mol Neurosci"},{"key":"465_CR162","doi-asserted-by":"publisher","first-page":"808","DOI":"10.1021\/bi301070v","volume":"52","author":"KA Burke","year":"2013","unstructured":"Burke KA, Yates EA, Legleiter J. Amyloid-forming proteins alter the local mechanical properties of lipid membranes. Biochemistry. 2013;52:808\u201317.","journal-title":"Biochemistry"},{"key":"465_CR163","doi-asserted-by":"publisher","first-page":"3991","DOI":"10.1039\/c3an00295k","volume":"138","author":"CR Liao","year":"2013","unstructured":"Liao CR, Rak M, Lund J, Unger M, Platt E, Albensi BC, et al. Synchrotron FTIR reveals lipid around and within amyloid plaques in transgenic mice and Alzheimer\u2019s disease brain. Analyst. 2013;138:3991\u20137.","journal-title":"Analyst"},{"key":"465_CR164","doi-asserted-by":"publisher","first-page":"13489","DOI":"10.1038\/srep13489","volume":"5","author":"J Kiskis","year":"2015","unstructured":"Kiskis J, Fink H, Nyberg L, Thyr J, Li JY, Enejder A. Plaque-associated lipids in Alzheimer\u2019s diseased brain tissue visualized by nonlinear microscopy. Sci Rep. 2015;5:13489.","journal-title":"Sci Rep"},{"key":"465_CR165","doi-asserted-by":"publisher","first-page":"1094","DOI":"10.1038\/ng.439","volume":"41","author":"JC Lambert","year":"2009","unstructured":"Lambert JC, Heath S, Even G, Campion D, Sleegers K, Hiltunen M, et al. Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer\u2019s disease. Nat Genet. 2009;41:1094\u20139.","journal-title":"Nat Genet"},{"key":"465_CR166","doi-asserted-by":"publisher","first-page":"1088","DOI":"10.1038\/ng.440","volume":"41","author":"D Harold","year":"2009","unstructured":"Harold D, Abraham R, Hollingworth P, Sims R, Gerrish A, Hamshere ML, et al. Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer\u2019s disease. Nat Genet. 2009;41:1088\u201393.","journal-title":"Nat Genet"},{"key":"465_CR167","doi-asserted-by":"publisher","first-page":"759","DOI":"10.1038\/s41577-018-0051-1","volume":"18","author":"Y Shi","year":"2018","unstructured":"Shi Y, Holtzman DM. Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight. Nat Rev Immunol. 2018;18:759\u201372.","journal-title":"Nat Rev Immunol"},{"key":"465_CR168","doi-asserted-by":"publisher","first-page":"1467","DOI":"10.1212\/WNL.43.8.1467","volume":"43","author":"AM Saunders","year":"1993","unstructured":"Saunders AM, Strittmatter WJ, Schmechel D, George-Hyslop PH, Pericak-Vance MA, Joo SH, et al. Association of apolipoprotein E allele epsilon 4 with late-onset familial and sporadic Alzheimer\u2019s disease. Neurology. 1993;43:1467\u201372.","journal-title":"Neurology"},{"key":"465_CR169","doi-asserted-by":"publisher","first-page":"1977","DOI":"10.1073\/pnas.90.5.1977","volume":"90","author":"WJ Strittmatter","year":"1993","unstructured":"Strittmatter WJ, Saunders AM, Schmechel D, Pericak-Vance M, Enghild J, Salvesen GS, et al. Apolipoprotein E: high-avidity binding to \u03b2-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc Natl Acad Sci U S A. 1993;90:1977\u201381.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR170","doi-asserted-by":"publisher","first-page":"8098","DOI":"10.1073\/pnas.90.17.8098","volume":"90","author":"WJ Strittmatter","year":"1993","unstructured":"Strittmatter WJ, Weisgraber KH, Huang DY, Dong LM, Salvesen GS, Pericak-Vance M, et al. Binding of human apolipoprotein E to synthetic amyloid \u03b2 peptide: isoform-specific effects and implications for late-onset Alzheimer disease. Proc Natl Acad Sci U S A. 1993;90:8098\u2013102.","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"Pt 2","key":"465_CR171","doi-asserted-by":"publisher","first-page":"359","DOI":"10.1042\/bj3480359","volume":"348","author":"T Tokuda","year":"2000","unstructured":"Tokuda T, Calero M, Matsubara E, Vidal R, Kumar A, Permanne B, et al. Lipidation of apolipoprotein E influences its isoform-specific interaction with Alzheimer\u2019s amyloid \u03b2 peptides. Biochem J. 2000;348(Pt 2):359\u201365.","journal-title":"Biochem J"},{"key":"465_CR172","doi-asserted-by":"publisher","first-page":"824","DOI":"10.1194\/jlr.R075481","volume":"58","author":"TV Huynh","year":"2017","unstructured":"Huynh TV, Davis AA, Ulrich JD, Holtzman DM. Apolipoprotein E and Alzheimer\u2019s disease: the influence of apolipoprotein E on amyloid-\u03b2 and other amyloidogenic proteins. J Lipid Res. 2017;58:824\u201336.","journal-title":"J Lipid Res"},{"key":"465_CR173","doi-asserted-by":"publisher","first-page":"15181","DOI":"10.1523\/JNEUROSCI.1542-12.2012","volume":"32","author":"T Hashimoto","year":"2012","unstructured":"Hashimoto T, Serrano-Pozo A, Hori Y, Adams KW, Takeda S, Banerji AO, et al. Apolipoprotein E, especially apolipoprotein E4, increases the oligomerization of amyloid \u03b2 peptide. J Neurosci. 2012;32:15181\u201392.","journal-title":"J Neurosci"},{"issue":"Pt 2","key":"465_CR174","doi-asserted-by":"publisher","first-page":"599","DOI":"10.1042\/bj3060599","volume":"306","author":"EM Castano","year":"1995","unstructured":"Castano EM, Prelli F, Wisniewski T, Golabek A, Kumar RA, Soto C, et al. Fibrillogenesis in Alzheimer\u2019s disease of amyloid \u03b2 peptides and apolipoprotein E. Biochem J. 1995;306(Pt 2):599\u2013604.","journal-title":"Biochem J"},{"key":"465_CR175","first-page":"1030","volume":"145","author":"T Wisniewski","year":"1994","unstructured":"Wisniewski T, Casta\u00f1o EM, Golabek A, Vogel T, Frangione B. Acceleration of Alzheimer\u2019s fibril formation by apolipoprotein E in vitro. Am J Pathol. 1994;145:1030\u20135.","journal-title":"Am J Pathol"},{"key":"465_CR176","doi-asserted-by":"publisher","first-page":"41774","DOI":"10.1074\/jbc.M112.407957","volume":"287","author":"KL Youmans","year":"2012","unstructured":"Youmans KL, Tai LM, Nwabuisi-Heath E, Jungbauer L, Kanekiyo T, Gan M, et al. APOE4-specific changes in A\u03b2 accumulation in a new transgenic mouse model of Alzheimer disease. J Biol Chem. 2012;287:41774\u201386.","journal-title":"J Biol Chem"},{"key":"465_CR177","doi-asserted-by":"publisher","first-page":"1024","DOI":"10.1016\/j.neuron.2017.11.013","volume":"96","author":"CC Liu","year":"2017","unstructured":"Liu CC, Zhao N, Fu Y, Wang N, Linares C, Tsai CW, et al. ApoE4 accelerates early seeding of amyloid pathology. Neuron. 2017;96:1024\u201332.e3.","journal-title":"Neuron"},{"key":"465_CR178","doi-asserted-by":"publisher","first-page":"523","DOI":"10.1038\/nature24016","volume":"549","author":"Y Shi","year":"2017","unstructured":"Shi Y, Yamada K, Liddelow SA, Smith ST, Zhao L, Luo W, et al. ApoE4 markedly exacerbates tau-mediated neurodegeneration in a mouse model of tauopathy. Nature. 2017;549:523\u20137.","journal-title":"Nature"},{"key":"465_CR179","doi-asserted-by":"publisher","first-page":"1585","DOI":"10.1096\/fj.10-175976","volume":"25","author":"E Cerf","year":"2011","unstructured":"Cerf E, Gustot A, Goormaghtigh E, Ruysschaert JM, Raussens V. High ability of apolipoprotein E4 to stabilize amyloid-\u03b2 peptide oligomers, the pathological entities responsible for Alzheimer\u2019s disease. FASEB J. 2011;25:1585\u201395.","journal-title":"FASEB J"},{"key":"465_CR180","doi-asserted-by":"publisher","first-page":"949","DOI":"10.1016\/S1074-5521(96)90183-0","volume":"3","author":"SJ Wood","year":"1996","unstructured":"Wood SJ, Chan W, Wetzel R. An ApoE-A\u03b2 inhibition complex in A\u03b2 fibril extension. Chem Biol. 1996;3:949\u201356.","journal-title":"Chem Biol"},{"key":"465_CR181","doi-asserted-by":"publisher","first-page":"6323","DOI":"10.1021\/bi5008172","volume":"53","author":"K Garai","year":"2014","unstructured":"Garai K, Verghese PB, Baban B, Holtzman DM, Frieden C. The binding of apolipoprotein E to oligomers and fibrils of amyloid-\u03b2 alters the kinetics of amyloid aggregation. Biochemistry. 2014;53:6323\u201331.","journal-title":"Biochemistry"},{"key":"465_CR182","doi-asserted-by":"publisher","first-page":"12623","DOI":"10.1021\/bi961074j","volume":"35","author":"SJ Wood","year":"1996","unstructured":"Wood SJ, Chan W, Wetzel R. Seeding of A\u03b2 fibril formation is inhibited by all three isotypes of apolipoprotein E. Biochemistry. 1996;35:12623\u20138.","journal-title":"Biochemistry"},{"key":"465_CR183","doi-asserted-by":"publisher","first-page":"104784","DOI":"10.1016\/j.nbd.2020.104784","volume":"138","author":"T Wisniewski","year":"2020","unstructured":"Wisniewski T, Drummond E. APOE-amyloid interaction: therapeutic targets. Neurobiol Dis. 2020;138:104784.","journal-title":"Neurobiol Dis"},{"key":"465_CR184","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.aau3112","volume":"5","author":"T Scheidt","year":"2019","unstructured":"Scheidt T, \u0141api\u0144ska U, Kumita JR, Whiten DR, Klenerman D, Wilson MR, et al. Secondary nucleation and elongation occur at different sites on Alzheimer\u2019s amyloid-\u03b2 aggregates. Sci Adv. 2019;5:eaau3112.","journal-title":"Sci Adv"},{"key":"465_CR185","doi-asserted-by":"publisher","first-page":"831","DOI":"10.1016\/0896-6273(90)90342-D","volume":"5","author":"PC May","year":"1990","unstructured":"May PC, Lampert-Etchells M, Johnson SA, Poirier J, Masters JN, Finch CE. Dynamics of gene expression for a hippocampal glycoprotein elevated in Alzheimer\u2019s disease and in response to experimental lesions in rat. Neuron. 1990;5:831\u20139.","journal-title":"Neuron"},{"key":"465_CR186","doi-asserted-by":"publisher","first-page":"164","DOI":"10.3389\/fnins.2019.00164","volume":"13","author":"EM Foster","year":"2019","unstructured":"Foster EM, Dangla-Valls A, Lovestone S, Ribe EM, Buckley NJ. Clusterin in Alzheimer\u2019s disease: mechanisms, genetics, and lessons from other pathologies. Front Neurosci. 2019;13:164.","journal-title":"Front Neurosci"},{"key":"465_CR187","doi-asserted-by":"publisher","first-page":"9270","DOI":"10.1021\/bi301277k","volume":"51","author":"P Narayan","year":"2012","unstructured":"Narayan P, Meehan S, Carver JA, Wilson MR, Dobson CM, Klenerman D. Amyloid-\u03b2 oligomers are sequestered by both intracellular and extracellular chaperones. Biochemistry. 2012;51:9270\u20136.","journal-title":"Biochemistry"},{"key":"465_CR188","doi-asserted-by":"publisher","first-page":"2312","DOI":"10.1096\/fj.06-7986com","volume":"21","author":"JJ Yerbury","year":"2007","unstructured":"Yerbury JJ, Poon S, Meehan S, Thompson B, Kumita JR, Dobson CM, et al. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J. 2007;21:2312\u201322.","journal-title":"FASEB J"},{"issue":"Pt 2","key":"465_CR189","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1042\/bj3160671","volume":"316","author":"E Matsubara","year":"1996","unstructured":"Matsubara E, Soto C, Governale S, Frangione B, Ghiso J. Apolipoprotein J and Alzheimer\u2019s amyloid \u03b2 solubility. Biochem J. 1996;316(Pt 2):671\u20139.","journal-title":"Biochem J"},{"key":"465_CR190","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1186\/s13024-020-00416-1","volume":"15","author":"AM Wojtas","year":"2020","unstructured":"Wojtas AM, Sens JP, Kang SS, Baker KE, Berry TJ, Kurti A, et al. Astrocyte-derived clusterin suppresses amyloid formation in vivo. Mol Neurodegener. 2020;15:71.","journal-title":"Mol Neurodegener"},{"key":"465_CR191","doi-asserted-by":"publisher","first-page":"E6962","DOI":"10.1073\/pnas.1701137114","volume":"114","author":"AM Wojtas","year":"2017","unstructured":"Wojtas AM, Kang SS, Olley BM, Gatherer M, Shinohara M, Lozano PA, et al. Loss of clusterin shifts amyloid deposition to the cerebrovasculature via disruption of perivascular drainage pathways. Proc Natl Acad Sci U S A. 2017;114:E6962\u2013e71.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR192","doi-asserted-by":"publisher","first-page":"909","DOI":"10.1038\/sj.jcbfm.9600419","volume":"27","author":"RD Bell","year":"2007","unstructured":"Bell RD, Sagare AP, Friedman AE, Bedi GS, Holtzman DM, Deane R, et al. Transport pathways for clearance of human Alzheimer\u2019s amyloid \u03b2-peptide and apolipoproteins E and J in the mouse central nervous system. J Cereb Blood Flow Metab. 2007;27:909\u201318.","journal-title":"J Cereb Blood Flow Metab"},{"key":"465_CR193","doi-asserted-by":"publisher","first-page":"1361","DOI":"10.1016\/j.biocel.2008.12.003","volume":"41","author":"AC Paula-Lima","year":"2009","unstructured":"Paula-Lima AC, Tricerri MA, Brito-Moreira J, Bomfim TR, Oliveira FF, Magdesian MH, et al. Human apolipoprotein A-I binds amyloid-\u03b2 and prevents A\u03b2-induced neurotoxicity. Int J Biochem Cell Biol. 2009;41:1361\u201370.","journal-title":"Int J Biochem Cell Biol"},{"key":"465_CR194","first-page":"11","volume":"2016","author":"ER Padayachee","year":"1651","unstructured":"Padayachee ER, Zetterberg H, Portelius E, Bor\u00e9n J, Molinuevo JL, Andreasen N, et al. Cerebrospinal fluid-induced retardation of amyloid \u03b2 aggregation correlates with Alzheimer\u2019s disease and the APOE \u03b54 allele. Brain Res. 1651;2016:11\u20136.","journal-title":"Brain Res"},{"key":"465_CR195","doi-asserted-by":"publisher","first-page":"608","DOI":"10.1002\/1097-4547(20001115)62:4<608::AID-JNR16>3.0.CO;2-4","volume":"62","author":"K Yamauchi","year":"2000","unstructured":"Yamauchi K, Tozuka M, Hidaka H, Nakabayashi T, Sugano M, Kondo Y, et al. Effect of apolipoprotein AII on the interaction of apolipoprotein E with \u03b2-amyloid: some apo(E-AII) complexes inhibit the internalization of \u03b2-amyloid in cultures of neuroblastoma cells. J Neurosci Res. 2000;62:608\u201314.","journal-title":"J Neurosci Res"},{"key":"465_CR196","doi-asserted-by":"publisher","first-page":"1298","DOI":"10.1016\/j.ajpath.2010.11.057","volume":"178","author":"Y Cui","year":"2011","unstructured":"Cui Y, Huang M, He Y, Zhang S, Luo Y. Genetic ablation of apolipoprotein A-IV accelerates Alzheimer\u2019s disease pathogenesis in a mouse model. Am J Pathol. 2011;178:1298\u2013308.","journal-title":"Am J Pathol"},{"key":"465_CR197","doi-asserted-by":"publisher","first-page":"593","DOI":"10.1016\/j.nbd.2015.08.014","volume":"82","author":"LY Di Marco","year":"2015","unstructured":"Di Marco LY, Venneri A, Farkas E, Evans PC, Marzo A, Frangi AF. Vascular dysfunction in the pathogenesis of Alzheimer\u2019s disease\u2014a review of endothelium-mediated mechanisms and ensuing vicious circles. Neurobiol Dis. 2015;82:593\u2013606.","journal-title":"Neurobiol Dis"},{"key":"465_CR198","doi-asserted-by":"publisher","first-page":"2547","DOI":"10.1182\/blood-2016-11-753202","volume":"129","author":"ZL Chen","year":"2017","unstructured":"Chen ZL, Revenko AS, Singh P, MacLeod AR, Norris EH, Strickland S. Depletion of coagulation factor XII ameliorates brain pathology and cognitive impairment in Alzheimer disease mice. Blood. 2017;129:2547\u201356.","journal-title":"Blood"},{"key":"465_CR199","doi-asserted-by":"publisher","first-page":"1099","DOI":"10.1016\/j.neuron.2019.01.014","volume":"101","author":"M Merlini","year":"2019","unstructured":"Merlini M, Rafalski VA, Rios Coronado PE, Gill TM, Ellisman M, Muthukumar G, et al. Fibrinogen induces microglia-mediated spine elimination and cognitive impairment in an Alzheimer\u2019s disease model. Neuron. 2019;101:1099\u2013108.e6.","journal-title":"Neuron"},{"key":"465_CR200","doi-asserted-by":"publisher","first-page":"1144","DOI":"10.1182\/blood-2016-03-705228","volume":"128","author":"D Zamolodchikov","year":"2016","unstructured":"Zamolodchikov D, Berk-Rauch HE, Oren DA, Stor DS, Singh PK, Kawasaki M, et al. Biochemical and structural analysis of the interaction between \u03b2-amyloid and fibrinogen. Blood. 2016;128:1144\u201351.","journal-title":"Blood"},{"key":"465_CR201","doi-asserted-by":"publisher","first-page":"427","DOI":"10.1097\/MOH.0000000000000368","volume":"24","author":"HJ Ahn","year":"2017","unstructured":"Ahn HJ, Chen ZL, Zamolodchikov D, Norris EH, Strickland S. Interactions of \u03b2-amyloid peptide with fibrinogen and coagulation factor XII may contribute to Alzheimer\u2019s disease. Curr Opin Hematol. 2017;24:427\u201331.","journal-title":"Curr Opin Hematol"},{"key":"465_CR202","doi-asserted-by":"publisher","first-page":"1488","DOI":"10.1111\/jth.13358","volume":"14","author":"D Gurwitz","year":"2016","unstructured":"Gurwitz D. The Alzheimer\u2019s disease peptide \u03b2-amyloid promotes thrombin generation through activation of coagulation factor XII: comment. J Thromb Haemost. 2016;14:1488\u20139.","journal-title":"J Thromb Haemost"},{"key":"465_CR203","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1186\/s12974-014-0165-8","volume":"11","author":"M Gold","year":"2014","unstructured":"Gold M, Dolga AM, Koepke J, Mengel D, Culmsee C, Dodel R, et al. \u03b11-antitrypsin modulates microglial-mediated neuroinflammation and protects microglial cells from amyloid-\u03b2-induced toxicity. J Neuroinflammation. 2014;11:165.","journal-title":"J Neuroinflammation"},{"key":"465_CR204","doi-asserted-by":"publisher","first-page":"4246","DOI":"10.1074\/jbc.M807242200","volume":"284","author":"JJ Yerbury","year":"2009","unstructured":"Yerbury JJ, Kumita JR, Meehan S, Dobson CM, Wilson MR. \u03b12-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species. J Biol Chem. 2009;284:4246\u201354.","journal-title":"J Biol Chem"},{"key":"465_CR205","doi-asserted-by":"publisher","first-page":"1356","DOI":"10.1212\/01.wnl.0000210535.20297.ae","volume":"66","author":"C Cordonnier","year":"2006","unstructured":"Cordonnier C, van der Flier WM, Sluimer JD, Leys D, Barkhof F, Scheltens P. Prevalence and severity of microbleeds in a memory clinic setting. Neurology. 2006;66:1356\u201360.","journal-title":"Neurology"},{"key":"465_CR206","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1046\/j.1365-2559.2001.01082.x","volume":"38","author":"MR D\u2019Andrea","year":"2001","unstructured":"D\u2019Andrea MR, Nagele RG, Wang HY, Peterson PA, Lee DH. Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer\u2019s disease. Histopathology. 2001;38:120\u201334.","journal-title":"Histopathology"},{"key":"465_CR207","doi-asserted-by":"publisher","first-page":"369","DOI":"10.3233\/JAD-2010-1375","volume":"20","author":"DA Butterfield","year":"2010","unstructured":"Butterfield DA, Hardas SS, Lange MLB. Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer\u2019s disease: many pathways to neurodegeneration. J Alzheimers Dis. 2010;20:369\u201393.","journal-title":"J Alzheimers Dis"},{"key":"465_CR208","doi-asserted-by":"publisher","first-page":"869","DOI":"10.1096\/fj.04-3210fje","volume":"19","author":"Q Wang","year":"2005","unstructured":"Wang Q, Woltjer RL, Cimino PJ, Pan C, Montine KS, Zhang J, et al. Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J. 2005;19:869\u201371.","journal-title":"FASEB J"},{"key":"465_CR209","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1016\/j.bbagen.2005.07.013","volume":"1726","author":"R Yamaji","year":"2005","unstructured":"Yamaji R, Chatani E, Harada N, Sugimoto K, Inui H, Nakano Y. Glyceraldehyde-3-phosphate dehydrogenase in the extracellular space inhibits cell spreading. Biochim Biophys Acta. 2005;1726:261\u201371.","journal-title":"Biochim Biophys Acta"},{"key":"465_CR210","doi-asserted-by":"publisher","first-page":"3816","DOI":"10.1016\/j.bbagen.2013.03.019","volume":"1830","author":"N Sheokand","year":"2013","unstructured":"Sheokand N, Kumar S, Malhotra H, Tillu V, Raje CI, Raje M. Secreted glyceraldehye-3-phosphate dehydrogenase is a multifunctional autocrine transferrin receptor for cellular iron acquisition. Biochim Biophys Acta. 2013;1830:3816\u201327.","journal-title":"Biochim Biophys Acta"},{"key":"465_CR211","doi-asserted-by":"publisher","first-page":"26562","DOI":"10.1074\/jbc.M704199200","volume":"282","author":"H Nakajima","year":"2007","unstructured":"Nakajima H, Amano W, Fujita A, Fukuhara A, Azuma YT, Hata F, et al. The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death. J Biol Chem. 2007;282:26562\u201374.","journal-title":"J Biol Chem"},{"key":"465_CR212","doi-asserted-by":"publisher","first-page":"1066","DOI":"10.1016\/j.bbrc.2009.10.118","volume":"390","author":"H Nakajima","year":"2009","unstructured":"Nakajima H, Amano W, Fukuhara A, Kubo T, Misaki S, Azuma YT, et al. An aggregate-prone mutant of human glyceraldehyde-3-phosphate dehydrogenase augments oxidative stress-induced cell death in SH-SY5Y cells. Biochem Biophys Res Commun. 2009;390:1066\u201371.","journal-title":"Biochem Biophys Res Commun"},{"key":"465_CR213","doi-asserted-by":"publisher","first-page":"14493","DOI":"10.1074\/jbc.M115.669291","volume":"290","author":"M Itakura","year":"2015","unstructured":"Itakura M, Nakajima H, Kubo T, Semi Y, Kume S, Higashida S, et al. Glyceraldehyde-3-phosphate dehydrogenase aggregates accelerate amyloid-\u03b2 amyloidogenesis in Alzheimer disease. J Biol Chem. 2015;290:14493\u2013503.","journal-title":"J Biol Chem"},{"key":"465_CR214","doi-asserted-by":"publisher","first-page":"156795","DOI":"10.1155\/2012\/156795","volume":"2012","author":"A D\u00edaz-Ramos","year":"2012","unstructured":"D\u00edaz-Ramos A, Roig-Borrellas A, Garc\u00eda-Melero A, L\u00f3pez-Alemany R. \u03b1-Enolase, a multifunctional protein: its role on pathophysiological situations. J Biomed Biotechnol. 2012;2012:156795.","journal-title":"J Biomed Biotechnol"},{"key":"465_CR215","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1111\/j.1471-4159.2009.06397.x","volume":"111","author":"DA Butterfield","year":"2009","unstructured":"Butterfield DA, Lange ML. Multifunctional roles of enolase in Alzheimer\u2019s disease brain: beyond altered glucose metabolism. J Neurochem. 2009;111:915\u201333.","journal-title":"J Neurochem"},{"key":"465_CR216","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jchromb.2006.05.019","volume":"840","author":"O Carrette","year":"2006","unstructured":"Carrette O, Burgess JA, Burkhard PR, Lang C, C\u00f4te M, Rodrigo N, et al. Changes of the cortex proteome and Apolipoprotein E in transgenic mouse models of Alzheimer\u2019s disease. J Chromatogr B Analyt Technol Biomed Life Sci. 2006;840:1\u20139.","journal-title":"J Chromatogr B Analyt Technol Biomed Life Sci"},{"key":"465_CR217","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1111\/j.1471-4159.2009.06397.x","volume":"111","author":"DA Butterfield","year":"2009","unstructured":"Butterfield DA, Lange MLB. Multifunctional roles of enolase in Alzheimer\u2019s disease brain: beyond altered glucose metabolism. J Neurochem. 2009;111:915\u201333.","journal-title":"J Neurochem"},{"key":"465_CR218","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1016\/j.jprot.2015.04.005","volume":"123","author":"L Shen","year":"2015","unstructured":"Shen L, Chen C, Yang A, Chen Y, Liu Q, Ni J. Redox proteomics identification of specifically carbonylated proteins in the hippocampi of triple transgenic Alzheimer\u2019s disease mice at its earliest pathological stage. J Proteomics. 2015;123:101\u201313.","journal-title":"J Proteomics"},{"key":"465_CR219","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1042\/BJ20130295","volume":"457","author":"R Salza","year":"2014","unstructured":"Salza R, Peysselon F, Chautard E, Faye C, Moschcovich L, Weiss T, et al. Extended interaction network of procollagen C-proteinase enhancer-1 in the extracellular matrix. Biochem J. 2014;457:137\u201349.","journal-title":"Biochem J"},{"key":"465_CR220","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1016\/j.matbio.2007.11.005","volume":"27","author":"H Morimoto","year":"2008","unstructured":"Morimoto H, Wada J, Font B, Mott JD, Hulmes DJ, Ookoshi T, et al. Procollagen C-proteinase enhancer-1 (PCPE-1) interacts with \u03b22-microglobulin (\u03b22-m) and may help initiate \u03b22-m amyloid fibril formation in connective tissues. Matrix Biol. 2008;27:211\u20139.","journal-title":"Matrix Biol"},{"key":"465_CR221","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1002\/cne.22062","volume":"515","author":"F Richter","year":"2009","unstructured":"Richter F, Meurers BH, Zhu C, Medvedeva VP, Chesselet MF. Neurons express hemoglobin \u03b1- and \u03b2-chains in rat and human brains. J Comp Neurol. 2009;515:538\u201347.","journal-title":"J Comp Neurol"},{"key":"465_CR222","doi-asserted-by":"publisher","first-page":"15454","DOI":"10.1073\/pnas.0813216106","volume":"106","author":"M Biagioli","year":"2009","unstructured":"Biagioli M, Pinto M, Cesselli D, Zaninello M, Lazarevic D, Roncaglia P, et al. Unexpected expression of \u03b1- and \u03b2-globin in mesencephalic dopaminergic neurons and glial cells. Proc Natl Acad Sci U S A. 2009;106:15454.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR223","doi-asserted-by":"publisher","first-page":"585","DOI":"10.1038\/jcbfm.2008.152","volume":"29","author":"DW Schelshorn","year":"2009","unstructured":"Schelshorn DW, Schneider A, Kuschinsky W, Weber D, Kr\u00fcger C, Dittgen T, et al. Expression of hemoglobin in rodent neurons. J Cereb Blood Flow Metab. 2009;29:585\u201395.","journal-title":"J Cereb Blood Flow Metab"},{"key":"465_CR224","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0033120","volume":"7","author":"JY Chuang","year":"2012","unstructured":"Chuang JY, Lee CW, Shih YH, Yang T, Yu L, Kuo YM. Interactions between amyloid-\u03b2 and hemoglobin: implications for amyloid plaque formation in Alzheimer\u2019s disease. PLoS One. 2012;7:e33120.","journal-title":"PLoS One"},{"key":"465_CR225","doi-asserted-by":"publisher","first-page":"1519","DOI":"10.1002\/1615-9861(200111)1:12<1519::AID-PROT1519>3.0.CO;2-L","volume":"1","author":"SJ Schonberger","year":"2001","unstructured":"Schonberger SJ, Edgar PF, Kydd R, Faull RL, Cooper GJ. Proteomic analysis of the brain in Alzheimer\u2019s disease: molecular phenotype of a complex disease process. Proteomics. 2001;1:1519\u201328.","journal-title":"Proteomics"},{"key":"465_CR226","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1016\/j.nbd.2004.08.014","volume":"17","author":"CW Wu","year":"2004","unstructured":"Wu CW, Liao PC, Yu L, Wang ST, Chen ST, Wu CM, et al. Hemoglobin promotes A\u03b2 oligomer formation and localizes in neurons and amyloid deposits. Neurobiol Dis. 2004;17:367\u201377.","journal-title":"Neurobiol Dis"},{"key":"465_CR227","first-page":"286","volume":"43","author":"A Gregory","year":"2005","unstructured":"Gregory A, Hayflick SJ. Neurodegeneration with brain iron accumulation. Folia Neuropathol. 2005;43:286\u201396.","journal-title":"Folia Neuropathol"},{"key":"465_CR228","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1097\/01.rmr.0000245461.90406.ad","volume":"17","author":"D Berg","year":"2006","unstructured":"Berg D, Youdim MB. Role of iron in neurodegenerative disorders. Top Magn Reson Imaging. 2006;17:5\u201317.","journal-title":"Top Magn Reson Imaging"},{"key":"465_CR229","doi-asserted-by":"publisher","first-page":"11153","DOI":"10.1073\/pnas.0404349101","volume":"101","author":"H Atamna","year":"2004","unstructured":"Atamna H, Frey WH 2nd. A role for heme in Alzheimer\u2019s disease: heme binds amyloid \u03b2 and has altered metabolism. Proc Natl Acad Sci U S A. 2004;101:11153\u20138.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR230","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1016\/j.abb.2009.05.003","volume":"487","author":"H Atamna","year":"2009","unstructured":"Atamna H, Frey WH 2nd, Ko N. Human and rodent amyloid-\u03b2 peptides differentially bind heme: relevance to the human susceptibility to Alzheimer\u2019s disease. Arch Biochem Biophys. 2009;487:59\u201365.","journal-title":"Arch Biochem Biophys"},{"key":"465_CR231","doi-asserted-by":"publisher","first-page":"3381","DOI":"10.1073\/pnas.0600134103","volume":"103","author":"H Atamna","year":"2006","unstructured":"Atamna H, Boyle K. Amyloid-\u03b2 peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer\u2019s disease. Proc Natl Acad Sci U S A. 2006;103:3381\u20136.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR232","doi-asserted-by":"publisher","first-page":"1170","DOI":"10.4103\/1673-5374.235021","volume":"13","author":"J Flemmig","year":"2018","unstructured":"Flemmig J, Z\u00e1mock\u00fd M, Alia A. Amyloid \u03b2 and free heme: bloody new insights into the pathogenesis of Alzheimer\u2019s disease. Neural Regen Res. 2018;13:1170\u20134.","journal-title":"Neural Regen Res"},{"key":"465_CR233","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1186\/2051-5960-1-83","volume":"1","author":"YK Al-Hilaly","year":"2013","unstructured":"Al-Hilaly YK, Williams TL, Stewart-Parker M, Ford L, Skaria E, Cole M, et al. A central role for dityrosine crosslinking of Amyloid-\u03b2 in Alzheimer\u2019s disease. Acta Neuropathol Commun. 2013;1:83.","journal-title":"Acta Neuropathol Commun"},{"key":"465_CR234","first-page":"547","volume":"46","author":"J Wassell","year":"2000","unstructured":"Wassell J. Haptoglobin: function and polymorphism. Clinical laboratory. 2000;46:547\u201352.","journal-title":"Clinical laboratory"},{"key":"465_CR235","doi-asserted-by":"publisher","first-page":"4192","DOI":"10.1111\/j.1582-4934.2008.00611.x","volume":"13","author":"N Morello","year":"2009","unstructured":"Morello N, Tonoli E, Logrand F, Fiorito V, Fagoonee S, Turco E, et al. Haemopexin affects iron distribution and ferritin expression in mouse brain. J Cell Mol Med. 2009;13:4192\u2013204.","journal-title":"J Cell Mol Med"},{"key":"465_CR236","doi-asserted-by":"publisher","first-page":"10914","DOI":"10.1021\/bi050764x","volume":"44","author":"JJ Yerbury","year":"2005","unstructured":"Yerbury JJ, Rybchyn MS, Easterbrook-Smith SB, Henriques C, Wilson MR. The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin. Biochemistry. 2005;44:10914\u201325.","journal-title":"Biochemistry"},{"key":"465_CR237","doi-asserted-by":"publisher","first-page":"837","DOI":"10.1021\/cn500099f","volume":"5","author":"MS Spagnuolo","year":"2014","unstructured":"Spagnuolo MS, Maresca B, La Marca V, Carrizzo A, Veronesi C, Cupidi C, et al. Haptoglobin interacts with apolipoprotein E and \u03b2-amyloid and influences their crosstalk. ACS Chem Neurosci. 2014;5:837\u201347.","journal-title":"ACS Chem Neurosci"},{"key":"465_CR238","doi-asserted-by":"publisher","first-page":"18292","DOI":"10.1074\/jbc.M109.017202","volume":"284","author":"J Watanabe","year":"2009","unstructured":"Watanabe J, Grijalva V, Hama S, Barbour K, Berger FG, Navab M, et al. Hemoglobin and its scavenger protein haptoglobin associate with apoA-1-containing particles and influence the inflammatory properties and function of high density lipoprotein. J Biol Chem. 2009;284:18292\u2013301.","journal-title":"J Biol Chem"},{"key":"465_CR239","doi-asserted-by":"publisher","first-page":"28163","DOI":"10.1074\/jbc.C112.360800","volume":"287","author":"HF Stanyon","year":"2012","unstructured":"Stanyon HF, Viles JH. Human serum albumin can regulate amyloid-\u03b2 peptide fiber growth in the brain interstitium: implications for Alzheimer disease. J Biol Chem. 2012;287:28163\u20138.","journal-title":"J Biol Chem"},{"key":"465_CR240","doi-asserted-by":"publisher","first-page":"32916","DOI":"10.1074\/jbc.271.51.32916","volume":"271","author":"AL Biere","year":"1996","unstructured":"Biere AL, Ostaszewski B, Stimson ER, Hyman BT, Maggio JE, Selkoe DJ. Amyloid \u03b2-peptide is transported on lipoproteins and albumin in human plasma. J Biol Chem. 1996;271:32916\u201322.","journal-title":"J Biol Chem"},{"key":"465_CR241","doi-asserted-by":"publisher","first-page":"2585","DOI":"10.1016\/j.bpj.2009.08.028","volume":"97","author":"J Milojevic","year":"2009","unstructured":"Milojevic J, Raditsis A, Melacini G. Human serum albumin inhibits A\u03b2 fibrillization through a \u201cmonomer-competitor\u201d mechanism. Biophys J. 2009;97:2585\u201394.","journal-title":"Biophys J"},{"key":"465_CR242","doi-asserted-by":"publisher","first-page":"919","DOI":"10.1016\/j.jmb.2018.01.008","volume":"430","author":"DC Bode","year":"2018","unstructured":"Bode DC, Stanyon HF, Hirani T, Baker MD, Nield J, Viles JH. Serum albumin\u2019s protective inhibition of amyloid-\u03b2 fiber formation is suppressed by cholesterol, fatty acids and warfarin. J Mol Biol. 2018;430:919\u201334.","journal-title":"J Mol Biol"},{"key":"465_CR243","doi-asserted-by":"publisher","first-page":"175","DOI":"10.3233\/JAD-150694","volume":"50","author":"A Ezra","year":"2016","unstructured":"Ezra A, Rabinovich-Nikitin I, Rabinovich-Toidman P, Solomon B. Multifunctional effect of human serum albumin reduces Alzheimer\u2019s disease related pathologies in the 3xTg mouse model. J Alzheimers Dis. 2016;50:175\u201388.","journal-title":"J Alzheimers Dis"},{"key":"465_CR244","doi-asserted-by":"publisher","first-page":"91","DOI":"10.2174\/156720510790274392","volume":"7","author":"DJ Llewellyn","year":"2010","unstructured":"Llewellyn DJ, Langa KM, Friedland RP, Lang IA. Serum albumin concentration and cognitive impairment. Curr Alzheimer Res. 2010;7:91\u20136.","journal-title":"Curr Alzheimer Res"},{"key":"465_CR245","doi-asserted-by":"publisher","first-page":"716","DOI":"10.1111\/ggi.12147","volume":"14","author":"K Yamamoto","year":"2014","unstructured":"Yamamoto K, Shimada H, Koh H, Ataka S, Miki T. Serum levels of albumin-amyloid \u03b2 complexes are decreased in Alzheimer\u2019s disease. Geriatr Gerontol Int. 2014;14:716\u201323.","journal-title":"Geriatr Gerontol Int"},{"key":"465_CR246","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1358\/dnp.2009.22.6.1395256","volume":"22","author":"M Boada","year":"2009","unstructured":"Boada M, Ortiz P, Anaya F, Hern\u00e1ndez I, Mu\u00f1oz J, N\u00fa\u00f1ez L, et al. Amyloid-targeted therapeutics in Alzheimer\u2019s disease: use of human albumin in plasma exchange as a novel approach for A\u03b2 mobilization. Drug News Perspect. 2009;22:325\u201339.","journal-title":"Drug News Perspect"},{"key":"465_CR247","doi-asserted-by":"publisher","first-page":"1412","DOI":"10.1002\/alz.12137","volume":"16","author":"M Boada","year":"2020","unstructured":"Boada M, L\u00f3pez OL, Olazar\u00e1n J, N\u00fa\u00f1ez L, Pfeffer M, Paricio M, et al. A randomized, controlled clinical trial of plasma exchange with albumin replacement for Alzheimer\u2019s disease: primary results of the AMBAR Study. Alzheimers Dement. 2020;16:1412\u201325.","journal-title":"Alzheimers Dement"},{"key":"465_CR248","doi-asserted-by":"publisher","first-page":"1183","DOI":"10.1515\/CCLM.2002.208","volume":"40","author":"J Robbins","year":"2002","unstructured":"Robbins J. Transthyretin from discovery to now. Clin Chem Lab Med. 2002;40:1183\u201390.","journal-title":"Clin Chem Lab Med"},{"key":"465_CR249","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1093\/protein\/gzs026","volume":"25","author":"J Du","year":"2012","unstructured":"Du J, Cho PY, Yang DT, Murphy RM. Identification of \u03b2-amyloid-binding sites on transthyretin. Protein Eng Des Sel. 2012;25:337\u201345.","journal-title":"Protein Eng Des Sel"},{"key":"465_CR250","first-page":"146","volume":"199","author":"AL Schwarzman","year":"1996","unstructured":"Schwarzman AL, Goldgaber D. Interaction of transthyretin with amyloid \u03b2-protein: binding and inhibition of amyloid formation. Ciba Found Symp. 1996;199:146\u201360. discussion 60\u20134","journal-title":"Ciba Found Symp"},{"key":"465_CR251","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1006\/bbrc.1999.0552","volume":"257","author":"YM Kuo","year":"1999","unstructured":"Kuo YM, Emmerling MR, Lampert HC, Hempelman SR, Kokjohn TA, Woods AS, et al. High levels of circulating A\u03b242 are sequestered by plasma proteins in Alzheimer\u2019s disease. Biochem Biophys Res Commun. 1999;257:787\u201391.","journal-title":"Biochem Biophys Res Commun"},{"key":"465_CR252","doi-asserted-by":"publisher","first-page":"357","DOI":"10.3233\/JAD-131355","volume":"39","author":"CA Ribeiro","year":"2014","unstructured":"Ribeiro CA, Oliveira SM, Guido LF, Magalhaes A, Valencia G, Arsequell G, et al. Transthyretin stabilization by iododiflunisal promotes amyloid-\u03b2 peptide clearance, decreases its deposition, and ameliorates cognitive deficits in an Alzheimer\u2019s disease mouse model. J Alzheimers Dis. 2014;39:357\u201370.","journal-title":"J Alzheimers Dis"},{"key":"465_CR253","doi-asserted-by":"publisher","first-page":"389","DOI":"10.3233\/JAD-2009-0966","volume":"16","author":"SF Hansson","year":"2009","unstructured":"Hansson SF, Andreasson U, Wall M, Skoog I, Andreasen N, Wallin A, et al. Reduced levels of amyloid-\u03b2-binding proteins in cerebrospinal fluid from Alzheimer\u2019s disease patients. J Alzheimers Dis. 2009;16:389\u201397.","journal-title":"J Alzheimers Dis"},{"key":"465_CR254","doi-asserted-by":"publisher","first-page":"1112","DOI":"10.1021\/acs.biomac.9b01475","volume":"21","author":"SA Ghadami","year":"2020","unstructured":"Ghadami SA, Chia S, Ruggeri FS, Meisl G, Bemporad F, Habchi J, et al. Transthyretin inhibits primary and secondary nucleations of amyloid-\u03b2 peptide aggregation and reduces the toxicity of its oligomers. Biomacromolecules. 2020;21:1112\u201325.","journal-title":"Biomacromolecules"},{"key":"465_CR255","doi-asserted-by":"publisher","first-page":"91","DOI":"10.3233\/JAD-180797","volume":"67","author":"MJ Reed","year":"2019","unstructured":"Reed MJ, Damodarasamy M, Pathan JL, Chan CK, Spiekerman C, Wight TN, et al. Increased hyaluronan and TSG-6 in association with neuropathologic changes of Alzheimer\u2019s disease. J Alzheimers Dis. 2019;67:91\u2013102.","journal-title":"J Alzheimers Dis"},{"key":"465_CR256","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1007\/978-981-13-9589-5_5","volume":"1173","author":"T Wang","year":"2019","unstructured":"Wang T, Xu SF, Fan YG, Li LB, Guo C. Iron pathophysiology in Alzheimer\u2019s diseases. Adv Exp Med Biol. 2019;1173:67\u2013104.","journal-title":"Adv Exp Med Biol"},{"key":"465_CR257","doi-asserted-by":"publisher","first-page":"764","DOI":"10.1016\/j.bbrc.2020.01.111","volume":"524","author":"K Cho","year":"2020","unstructured":"Cho K, Jang YJ, Lee SJ, Jeon YN, Shim YL, Lee JY, et al. TLQP-21 mediated activation of microglial BV2 cells promotes clearance of extracellular fibril amyloid-\u03b2. Biochem Biophys Res Commun. 2020;524:764\u201371.","journal-title":"Biochem Biophys Res Commun"},{"key":"465_CR258","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1186\/s13024-020-0357-x","volume":"15","author":"F El Gaamouch","year":"2020","unstructured":"El Gaamouch F, Audrain M, Lin WJ, Beckmann N, Jiang C, Hariharan S, et al. VGF-derived peptide TLQP-21 modulates microglial function through C3aR1 signaling pathways and reduces neuropathology in 5xFAD mice. Mol Neurodegener. 2020;15:4.","journal-title":"Mol Neurodegener"},{"key":"465_CR259","doi-asserted-by":"publisher","first-page":"3942","DOI":"10.1038\/s41467-020-17405-z","volume":"11","author":"ND Beckmann","year":"2020","unstructured":"Beckmann ND, Lin WJ, Wang M, Cohain AT, Charney AW, Wang P, et al. Multiscale causal networks identify VGF as a key regulator of Alzheimer\u2019s disease. Nat Commun. 2020;11:3942.","journal-title":"Nat Commun"},{"key":"465_CR260","doi-asserted-by":"publisher","first-page":"639","DOI":"10.1523\/JNEUROSCI.20-02-00639.2000","volume":"20","author":"LD Fricker","year":"2000","unstructured":"Fricker LD, McKinzie AA, Sun J, Curran E, Qian Y, Yan L, et al. Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing. J Neurosci. 2000;20:639\u201348.","journal-title":"J Neurosci"},{"key":"465_CR261","doi-asserted-by":"publisher","first-page":"1114","DOI":"10.1074\/jbc.M112.417071","volume":"288","author":"M Helwig","year":"2013","unstructured":"Helwig M, Hoshino A, Berridge C, Lee SN, Lorenzen N, Otzen DE, et al. The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins. J Biol Chem. 2013;288:1114\u201324.","journal-title":"J Biol Chem"},{"key":"465_CR262","doi-asserted-by":"publisher","first-page":"646","DOI":"10.1016\/S0006-291X(03)01391-3","volume":"308","author":"K Kikuchi","year":"2003","unstructured":"Kikuchi K, Arawaka S, Koyama S, Kimura H, Ren CH, Wada M, et al. An N-terminal fragment of ProSAAS (a granin-like neuroendocrine peptide precursor) is associated with tau inclusions in Pick\u2019s disease. Biochem Biophys Res Commun. 2003;308:646\u201354.","journal-title":"Biochem Biophys Res Commun"},{"key":"465_CR263","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1016\/j.neulet.2003.11.028","volume":"356","author":"M Wada","year":"2004","unstructured":"Wada M, Ren CH, Koyama S, Arawaka S, Kawakatsu S, Kimura H, et al. A human granin-like neuroendocrine peptide precursor (proSAAS) immunoreactivity in tau inclusions of Alzheimer\u2019s disease and parkinsonism-dementia complex on Guam. Neurosci Lett. 2004;356:49\u201352.","journal-title":"Neurosci Lett"},{"key":"465_CR264","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1111\/jnc.12454","volume":"128","author":"A Hoshino","year":"2014","unstructured":"Hoshino A, Helwig M, Rezaei S, Berridge C, Eriksen JL, Lindberg I. A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer\u2019s disease. J Neurochem. 2014;128:419\u201330.","journal-title":"J Neurochem"},{"key":"465_CR265","doi-asserted-by":"publisher","first-page":"3406","DOI":"10.1016\/j.febslet.2013.09.006","volume":"587","author":"JR Peinado","year":"2013","unstructured":"Peinado JR, Sami F, Rajpurohit N, Lindberg I. Blockade of islet amyloid polypeptide fibrillation and cytotoxicity by the secretory chaperones 7B2 and proSAAS. FEBS Lett. 2013;587:3406\u201311.","journal-title":"FEBS Lett"},{"key":"465_CR266","doi-asserted-by":"publisher","first-page":"E4708","DOI":"10.1073\/pnas.1601091113","volume":"113","author":"TS Jarvela","year":"2016","unstructured":"Jarvela TS, Lam HA, Helwig M, Lorenzen N, Otzen DE, McLean PJ, et al. The neural chaperone proSAAS blocks \u03b1-synuclein fibrillation and neurotoxicity. Proc Natl Acad Sci U S A. 2016;113:E4708\u201315.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR267","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1016\/j.msard.2012.08.002","volume":"2","author":"S Gnanapavan","year":"2013","unstructured":"Gnanapavan S, Giovannoni G. Neural cell adhesion molecules in brain plasticity and disease. Mult Scler Relat Disord. 2013;2:13\u201320.","journal-title":"Mult Scler Relat Disord"},{"key":"465_CR268","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1007\/s12031-011-9578-3","volume":"46","author":"KP Chen","year":"2012","unstructured":"Chen KP, Dou F. Selective interaction of amyloid precursor protein with different isoforms of neural cell adhesion molecule. J Mol Neurosci. 2012;46:203\u20139.","journal-title":"J Mol Neurosci"},{"key":"465_CR269","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1002\/jnr.490330406","volume":"33","author":"SG Kallapur","year":"1992","unstructured":"Kallapur SG, Akeson RA. The neural cell adhesion molecule (NCAM) heparin binding domain binds to cell surface heparan sulfate proteoglycans. J Neurosci Res. 1992;33:538\u201348.","journal-title":"J Neurosci Res"},{"key":"465_CR270","doi-asserted-by":"publisher","first-page":"8836","DOI":"10.1038\/ncomms9836","volume":"6","author":"I Leshchys\u2019ka","year":"2015","unstructured":"Leshchys\u2019ka I, Liew HT, Shepherd C, Halliday GM, Stevens CH, Ke YD, et al. A\u03b2-dependent reduction of NCAM2-mediated synaptic adhesion contributes to synapse loss in Alzheimer\u2019s disease. Nat Commun. 2015;6:8836.","journal-title":"Nat Commun"},{"key":"465_CR271","doi-asserted-by":"publisher","first-page":"1051","DOI":"10.1016\/j.biocel.2012.03.022","volume":"44","author":"R Frischknecht","year":"2012","unstructured":"Frischknecht R, Seidenbecher CI. Brevican: a key proteoglycan in the perisynaptic extracellular matrix of the brain. Int J Biochem Cell Biol. 2012;44:1051\u20134.","journal-title":"Int J Biochem Cell Biol"},{"key":"465_CR272","doi-asserted-by":"crossref","unstructured":"Mohamedi Y, Fontanil T, Cobo T, Cal S, Obaya AJ. New insights into ADAMTS metalloproteases in the central nervous system. Biomolecules. 2020;10","DOI":"10.3390\/biom10030403"},{"key":"465_CR273","doi-asserted-by":"publisher","first-page":"784","DOI":"10.1111\/j.1471-4159.2010.06647.x","volume":"113","author":"JM Ajmo","year":"2010","unstructured":"Ajmo JM, Bailey LA, Howell MD, Cortez LK, Pennypacker KR, Mehta HN, et al. Abnormal post-translational and extracellular processing of brevican in plaque-bearing mice over-expressing APPsw. J Neurochem. 2010;113:784\u201395.","journal-title":"J Neurochem"},{"key":"465_CR274","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1038\/nrn.2017.29","volume":"18","author":"UC M\u00fcller","year":"2017","unstructured":"M\u00fcller UC, Deller T, Korte M. Not just amyloid: physiological functions of the amyloid precursor protein family. Nat Rev Neurosci. 2017;18:281\u201398.","journal-title":"Nat Rev Neurosci"},{"key":"465_CR275","doi-asserted-by":"publisher","first-page":"10542","DOI":"10.1074\/jbc.M310001200","volume":"279","author":"Q Li","year":"2004","unstructured":"Li Q, S\u00fcdhof TC. Cleavage of amyloid-\u03b2 precursor protein and amyloid-\u03b2 precursor-like protein by BACE 1. J Biol Chem. 2004;279:10542\u201350.","journal-title":"J Biol Chem"},{"key":"465_CR276","doi-asserted-by":"publisher","first-page":"18146","DOI":"10.1074\/jbc.M311601200","volume":"279","author":"S Eggert","year":"2004","unstructured":"Eggert S, Paliga K, Soba P, Evin G, Masters CL, Weidemann A, et al. The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves \u03b1 -, \u03b2-, \u03b3-, and \u03b5-like cleavages: modulation of APLP-1 processing by n-glycosylation. J Biol Chem. 2004;279:18146\u201356.","journal-title":"J Biol Chem"},{"key":"465_CR277","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1007\/s004010050745","volume":"94","author":"TA Bayer","year":"1997","unstructured":"Bayer TA, Paliga K, Weggen S, Wiestler OD, Beyreuther K, Multhaup G. Amyloid precursor-like protein 1 accumulates in neuritic plaques in Alzheimer\u2019s disease. Acta Neuropathol. 1997;94:519\u201324.","journal-title":"Acta Neuropathol"},{"key":"465_CR278","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1016\/S0006-8993(98)00653-2","volume":"804","author":"MJ McNamara","year":"1998","unstructured":"McNamara MJ, Ruff CT, Wasco W, Tanzi RE, Thinakaran G, Hyman BT. Immunohistochemical and in situ analysis of amyloid precursor-like protein-1 and amyloid precursor-like protein-2 expression in Alzheimer disease and aged control brains. Brain Res. 1998;804:45\u201351.","journal-title":"Brain Res"},{"key":"465_CR279","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/S0006-8993(02)04173-2","volume":"966","author":"AR White","year":"2003","unstructured":"White AR, Maher F, Brazier MW, Jobling MF, Thyer J, Stewart LR, et al. Diverse fibrillar peptides directly bind the Alzheimer\u2019s amyloid precursor protein and amyloid precursor-like protein 2 resulting in cellular accumulation. Brain Res. 2003;966:231\u201344.","journal-title":"Brain Res"},{"key":"465_CR280","doi-asserted-by":"publisher","first-page":"545","DOI":"10.1111\/j.1365-2958.2010.07373.x","volume":"78","author":"B Singh","year":"2010","unstructured":"Singh B, Su YC, Riesbeck K. Vitronectin in bacterial pathogenesis: a host protein used in complement escape and cellular invasion. Mol Microbiol. 2010;78:545\u201360.","journal-title":"Mol Microbiol"},{"key":"465_CR281","doi-asserted-by":"publisher","first-page":"533","DOI":"10.1093\/glycob\/cwp205","volume":"20","author":"E Sandwall","year":"2010","unstructured":"Sandwall E, O\u2019Callaghan P, Zhang X, Lindahl U, Lannfelt L, Li JP. Heparan sulfate mediates amyloid-\u03b2 internalization and cytotoxicity. Glycobiology. 2010;20:533\u201341.","journal-title":"Glycobiology"},{"key":"465_CR282","doi-asserted-by":"publisher","first-page":"5053","DOI":"10.1074\/jbc.M114.600569","volume":"290","author":"CB Jendresen","year":"2015","unstructured":"Jendresen CB, Cui H, Zhang X, Vlodavsky I, Nilsson LN, Li JP. Overexpression of heparanase lowers the amyloid burden in amyloid-\u03b2 precursor protein transgenic mice. J Biol Chem. 2015;290:5053\u201364.","journal-title":"J Biol Chem"},{"key":"465_CR283","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.aad3650","volume":"8","author":"CC Liu","year":"2016","unstructured":"Liu CC, Zhao N, Yamaguchi Y, Cirrito JR, Kanekiyo T, Holtzman DM, et al. Neuronal heparan sulfates promote amyloid pathology by modulating brain amyloid-\u03b2 clearance and aggregation in Alzheimer\u2019s disease. Sci Transl Med. 2016;8:332ra44.","journal-title":"Sci Transl Med"},{"key":"465_CR284","doi-asserted-by":"publisher","first-page":"6468","DOI":"10.1073\/pnas.96.11.6468","volume":"96","author":"JE Donahue","year":"1999","unstructured":"Donahue JE, Berzin TM, Rafii MS, Glass DJ, Yancopoulos GD, Fallon JR, et al. Agrin in Alzheimer\u2019s disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma. Proc Natl Acad Sci U S A. 1999;96:6468\u201372.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR285","doi-asserted-by":"publisher","first-page":"1124","DOI":"10.1097\/NEN.0b013e31823b0b12","volume":"70","author":"SM Rauch","year":"2011","unstructured":"Rauch SM, Huen K, Miller MC, Chaudry H, Lau M, Sanes JR, et al. Changes in brain \u03b2-amyloid deposition and aquaporin 4 levels in response to altered agrin expression in mice. J Neuropathol Exp Neurol. 2011;70:1124\u201337.","journal-title":"J Neuropathol Exp Neurol"},{"key":"465_CR286","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1016\/S0197-4580(00)00121-4","volume":"21","author":"TM Berzin","year":"2000","unstructured":"Berzin TM, Zipser BD, Rafii MS, Kuo-Leblanc V, Yancopoulos GD, Glass DJ, et al. Agrin and microvascular damage in Alzheimer\u2019s disease. Neurobiol Aging. 2000;21:349\u201355.","journal-title":"Neurobiol Aging"},{"key":"465_CR287","doi-asserted-by":"publisher","first-page":"537","DOI":"10.1016\/S0197-4580(02)00010-6","volume":"23","author":"J van Horssen","year":"2002","unstructured":"van Horssen J, Kleinnijenhuis J, Maass CN, Rensink AA, Otte-H\u00f6ller I, David G, et al. Accumulation of heparan sulfate proteoglycans in cerebellar senile plaques. Neurobiol Aging. 2002;23:537\u201345.","journal-title":"Neurobiol Aging"},{"key":"465_CR288","doi-asserted-by":"publisher","first-page":"604","DOI":"10.1007\/s004010100414","volume":"102","author":"J van Horssen","year":"2001","unstructured":"van Horssen J, Otte-H\u00f6ller I, David G, Maat-Schieman ML, van den Heuvel LP, Wesseling P, et al. Heparan sulfate proteoglycan expression in cerebrovascular amyloid \u03b2 deposits in Alzheimer\u2019s disease and hereditary cerebral hemorrhage with amyloidosis (Dutch) brains. Acta Neuropathol. 2001;102:604\u201314.","journal-title":"Acta Neuropathol"},{"key":"465_CR289","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1016\/j.brainres.2008.12.063","volume":"1260","author":"NM Timmer","year":"2009","unstructured":"Timmer NM, van Horssen J, Otte-Holler I, Wilhelmus MM, David G, van Beers J, et al. Amyloid \u03b2 induces cellular relocalization and production of agrin and glypican-1. Brain Res. 2009;1260:38\u201346.","journal-title":"Brain Res"},{"key":"465_CR290","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1000666","volume":"5","author":"DR Taylor","year":"2009","unstructured":"Taylor DR, Whitehouse IJ, Hooper NM. Glypican-1 mediates both prion protein lipid raft association and disease isoform formation. PLoS Pathog. 2009;5:e1000666.","journal-title":"PLoS Pathog"},{"key":"465_CR291","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1016\/j.matbio.2006.09.006","volume":"26","author":"E Steck","year":"2007","unstructured":"Steck E, Br\u00e4un J, Pelttari K, Kadel S, Kalbacher H, Richter W. Chondrocyte secreted CRTAC1: a glycosylated extracellular matrix molecule of human articular cartilage. Matrix Biol. 2007;26:30\u201341.","journal-title":"Matrix Biol"},{"key":"465_CR292","doi-asserted-by":"publisher","first-page":"242","DOI":"10.1002\/prot.25210","volume":"85","author":"L Anjos","year":"2017","unstructured":"Anjos L, Morgado I, Guerreiro M, Cardoso JC, Melo EP, Power DM. Cartilage acidic protein 1, a new member of the \u03b2-propeller protein family with amyloid propensity. Proteins. 2017;85:242\u201355.","journal-title":"Proteins"},{"key":"465_CR293","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1186\/1750-1326-3-16","volume":"3","author":"TM Shin","year":"2008","unstructured":"Shin TM, Isas JM, Hsieh CL, Kayed R, Glabe CG, Langen R, et al. Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin. Mol Neurodegener. 2008;3:16.","journal-title":"Mol Neurodegener"},{"key":"465_CR294","doi-asserted-by":"publisher","first-page":"67","DOI":"10.2174\/156720507779939869","volume":"4","author":"JK Wung","year":"2007","unstructured":"Wung JK, Perry G, Kowalski A, Harris PL, Bishop GM, Trivedi MA, et al. Increased expression of the remodeling- and tumorigenic-associated factor osteopontin in pyramidal neurons of the Alzheimer's disease brain. Curr Alzheimer Res. 2007;4:67\u201372.","journal-title":"Curr Alzheimer Res"},{"key":"465_CR295","doi-asserted-by":"publisher","first-page":"179","DOI":"10.3233\/JAD-2011-102151","volume":"25","author":"M Carecchio","year":"2011","unstructured":"Carecchio M, Comi C. The role of osteopontin in neurodegenerative diseases. J Alzheimers Dis. 2011;25:179\u201385.","journal-title":"J Alzheimers Dis"},{"key":"465_CR296","doi-asserted-by":"publisher","first-page":"288","DOI":"10.2478\/s13380-012-0028-7","volume":"3","author":"A Brown","year":"2012","unstructured":"Brown A. Osteopontin: a key link between immunity, inflammation and the central nervous system. Transl Neurosci. 2012;3:288\u201393.","journal-title":"Transl Neurosci"},{"key":"465_CR297","doi-asserted-by":"publisher","first-page":"793","DOI":"10.1111\/bpa.12721","volume":"29","author":"L Grand Moursel","year":"2019","unstructured":"Grand Moursel L, van der Graaf LM, Bulk M, van Roon-Mom WMC, van der Weerd L. Osteopontin and phospho-SMAD2\/3 are associated with calcification of vessels in D-CAA, an hereditary cerebral amyloid angiopathy. Brain Pathol. 2019;29:793\u2013802.","journal-title":"Brain Pathol"},{"key":"465_CR298","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1016\/j.bbi.2017.08.019","volume":"67","author":"A Rentsendorj","year":"2018","unstructured":"Rentsendorj A, Sheyn J, Fuchs DT, Daley D, Salumbides BC, Schubloom HE, et al. A novel role for osteopontin in macrophage-mediated amyloid-\u03b2 clearance in Alzheimer\u2019s models. Brain Behav Immun. 2018;67:163\u201380.","journal-title":"Brain Behav Immun"},{"key":"465_CR299","doi-asserted-by":"publisher","first-page":"3678","DOI":"10.1074\/jbc.RA119.008703","volume":"295","author":"T Seki","year":"2020","unstructured":"Seki T, Kanagawa M, Kobayashi K, Kowa H, Yahata N, Maruyama K, et al. Galectin 3-binding protein suppresses amyloid-\u03b2 production by modulating \u03b2-cleavage of amyloid precursor protein. J Biol Chem. 2020;295:3678\u201391.","journal-title":"J Biol Chem"},{"key":"465_CR300","doi-asserted-by":"publisher","first-page":"1411","DOI":"10.1046\/j.1471-4159.2001.00144.x","volume":"76","author":"I Ohsawa","year":"2001","unstructured":"Ohsawa I, Takamura C, Kohsaka S. Fibulin-1 binds the amino-terminal head of \u03b2-amyloid precursor protein and modulates its physiological function. J Neurochem. 2001;76:1411\u201320.","journal-title":"J Neurochem"},{"key":"465_CR301","doi-asserted-by":"publisher","first-page":"1372","DOI":"10.1172\/JCI114581","volume":"85","author":"E Asch","year":"1990","unstructured":"Asch E, Podack E. Vitronectin binds to activated human platelets and plays a role in platelet aggregation. J Clin Invest. 1990;85:1372\u20138.","journal-title":"J Clin Invest"},{"key":"465_CR302","doi-asserted-by":"publisher","first-page":"19458","DOI":"10.1074\/jbc.270.33.19458","volume":"270","author":"H Tran","year":"1995","unstructured":"Tran H, Tanaka A, Litvinovich SV, Medved LV, Haudenschild CC, Argraves WS. The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis. J Biol Chem. 1995;270:19458\u201364.","journal-title":"J Biol Chem"},{"key":"465_CR303","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1008002","volume":"15","author":"G Xu","year":"2019","unstructured":"Xu G, Xia Z, Deng F, Liu L, Wang Q, Yu Y, et al. Inducible LGALS3BP\/90K activates antiviral innate immune responses by targeting TRAF6 and TRAF3 complex. PLoS Pathog. 2019;15:e1008002.","journal-title":"PLoS Pathog"},{"key":"465_CR304","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1177\/10454411920030040101","volume":"3","author":"LA Bobek","year":"1992","unstructured":"Bobek LA, Levine MJ. Cystatins\u2014inhibitors of cysteine proteinases. Crit Rev Oral Biol Med. 1992;3:307\u201332.","journal-title":"Crit Rev Oral Biol Med"},{"key":"465_CR305","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1016\/0305-0491(96)00025-9","volume":"114","author":"K H\u00e5kansson","year":"1996","unstructured":"H\u00e5kansson K, Huh C, Grubb A, Karlsson S, Abrahamson M. Mouse and rat cystatin C: Escherichia coli production, characterization and tissue distribution. Comp Biochem Physiol B Biochem Mol Biol. 1996;114:303\u201311.","journal-title":"Comp Biochem Physiol B Biochem Mol Biol"},{"key":"465_CR306","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1111\/j.1750-3639.2006.tb00562.x","volume":"16","author":"E Levy","year":"2006","unstructured":"Levy E, Jaskolski M, Grubb A. The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology and animal models. Brain Pathol. 2006;16:60\u201370.","journal-title":"Brain Pathol"},{"key":"465_CR307","doi-asserted-by":"publisher","first-page":"1437","DOI":"10.1038\/ng.2007.23","volume":"39","author":"SA Kaeser","year":"2007","unstructured":"Kaeser SA, Herzig MC, Coomaraswamy J, Kilger E, Selenica ML, Winkler DT, et al. Cystatin C modulates cerebral \u03b2-amyloidosis. Nat Genet. 2007;39:1437\u20139.","journal-title":"Nat Genet"},{"key":"465_CR308","doi-asserted-by":"publisher","first-page":"885","DOI":"10.3233\/JAD-2010-1291","volume":"19","author":"B Tizon","year":"2010","unstructured":"Tizon B, Ribe EM, Mi W, Troy CM, Levy E. Cystatin C protects neuronal cells from amyloid-\u03b2-induced toxicity. J Alzheimers Dis. 2010;19:885\u201394.","journal-title":"J Alzheimers Dis"},{"key":"465_CR309","doi-asserted-by":"publisher","first-page":"387","DOI":"10.1093\/brain\/95.2.387","volume":"95","author":"G Gudmundsson","year":"1972","unstructured":"Gudmundsson G, Hallgr\u00edmsson J, J\u00f3nasson TA, Bjarnason O. Hereditary cerebral haemorrhage with amyloidosis. Brain. 1972;95:387\u2013404.","journal-title":"Brain"},{"key":"465_CR310","doi-asserted-by":"publisher","first-page":"9700","DOI":"10.1021\/bi960920n","volume":"35","author":"D Wen","year":"1996","unstructured":"Wen D, Corina K, Chow EP, Miller S, Janmey PA, Pepinsky RB. The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure. Biochemistry. 1996;35:9700\u20139.","journal-title":"Biochemistry"},{"key":"465_CR311","doi-asserted-by":"publisher","first-page":"80","DOI":"10.3109\/13506129409148629","volume":"1","author":"T Paunio","year":"1994","unstructured":"Paunio T, Kiuru S, Karonen S-L, Palo J, Peltonen L. Quantification of serum and cerebrospinal fluid gelsolin in familial amyloidosis, Finnish type (AGel). Amyloid. 1994;1:80\u20139.","journal-title":"Amyloid"},{"key":"465_CR312","first-page":"314","volume":"1","author":"J Meretoja","year":"1969","unstructured":"Meretoja J. Familial systemic paramyloidosis with lattice dystrophy of the cornea, progressive cranial neuropathy, skin changes and various internal symptoms. A previously unrecognized heritable syndrome. Ann Clin Res. 1969;1:314\u201324.","journal-title":"Ann Clin Res"},{"key":"465_CR313","doi-asserted-by":"publisher","DOI":"10.1016\/B978-0-444-52902-2.00039-4","volume-title":"Hereditary gelsolin amyloidosis","author":"MH Sari Kiuru-Enari","year":"2013","unstructured":"Sari Kiuru-Enari MH. Hereditary gelsolin amyloidosis. Amsterdam: Elsevier; 2013."},{"key":"465_CR314","doi-asserted-by":"publisher","first-page":"344","DOI":"10.1016\/S0006-8993(99)02315-X","volume":"853","author":"I Ray","year":"2000","unstructured":"Ray I, Chauhan A, Wegiel J, Chauhan VP. Gelsolin inhibits the fibrillization of amyloid \u03b2-protein, and also defibrillizes its preformed fibrils. Brain Res. 2000;853:344\u201351.","journal-title":"Brain Res"},{"key":"465_CR315","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1523\/JNEUROSCI.23-01-00029.2003","volume":"23","author":"Y Matsuoka","year":"2003","unstructured":"Matsuoka Y, Saito M, LaFrancois J, Saito M, Gaynor K, Olm V, et al. Novel therapeutic approach for the treatment of Alzheimer\u2019s disease by peripheral administration of agents with an affinity to \u03b2-amyloid. J Neurosci. 2003;23:29\u201333.","journal-title":"J Neurosci"},{"key":"465_CR316","doi-asserted-by":"publisher","first-page":"1623","DOI":"10.1038\/sj.mt.6300253","volume":"15","author":"AC Hirko","year":"2007","unstructured":"Hirko AC, Meyer EM, King MA, Hughes JA. Peripheral transgene expression of plasma gelsolin reduces amyloid in transgenic mouse models of Alzheimer\u2019s disease. Mol Ther. 2007;15:1623\u20139.","journal-title":"Mol Ther"},{"key":"465_CR317","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1111\/j.1365-2990.1984.tb00340.x","volume":"10","author":"IF Rowe","year":"1984","unstructured":"Rowe IF, Jensson O, Lewis PD, Candy J, Tennent GA, Pepys MB. Immunohistochemical demonstration of amyloid P component in cerebro-vascular amyloidosis. Neuropathol Appl Neurobiol. 1984;10:53\u201361.","journal-title":"Neuropathol Appl Neurobiol"},{"key":"465_CR318","first-page":"454","volume":"58","author":"F Coria","year":"1988","unstructured":"Coria F, Casta\u00f1o E, Prelli F, Larrondo-Lillo M, van Duinen S, Shelanski ML, et al. Isolation and characterization of amyloid P component from Alzheimer\u2019s disease and other types of cerebral amyloidosis. Lab Invest. 1988;58:454\u20138.","journal-title":"Lab Invest"},{"key":"465_CR319","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1007\/BF00688180","volume":"78","author":"T Duong","year":"1989","unstructured":"Duong T, Pommier EC, Scheibel AB. Immunodetection of the amyloid P component in Alzheimer\u2019s disease. Acta Neuropathol. 1989;78:429\u201337.","journal-title":"Acta Neuropathol"},{"key":"465_CR320","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1038\/nm0897-855","volume":"3","author":"M Botto","year":"1997","unstructured":"Botto M, Hawkins PN, Bickerstaff MCM, Herbert J, Bygrave AE, McBride A, et al. Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene. Nat Med. 1997;3:855\u20139.","journal-title":"Nat Med"},{"key":"465_CR321","doi-asserted-by":"publisher","first-page":"875","DOI":"10.3233\/JAD-2012-120076","volume":"29","author":"M Mold","year":"2012","unstructured":"Mold M, Shrive AK, Exley C. Serum amyloid P component accelerates the formation and enhances the stability of amyloid fibrils in a physiologically significant under-saturated solution of amyloid-\u03b2 42. J Alzheimers Dis. 2012;29:875\u201381.","journal-title":"J Alzheimers Dis"},{"key":"465_CR322","doi-asserted-by":"publisher","first-page":"4299","DOI":"10.1073\/pnas.92.10.4299","volume":"92","author":"GA Tennent","year":"1995","unstructured":"Tennent GA, Lovat LB, Pepys MB. Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proc Natl Acad Sci U S A. 1995;92:4299\u2013303.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR323","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1002\/glia.22619","volume":"62","author":"SD Mulder","year":"2014","unstructured":"Mulder SD, Nielsen HM, Blankenstein MA, Eikelenboom P, Veerhuis R. Apolipoproteins E and J interfere with amyloid-\u03b2 uptake by primary human astrocytes and microglia in vitro. Glia. 2014;62:493\u2013503.","journal-title":"Glia"},{"key":"465_CR324","first-page":"375","volume":"270","author":"Z Urb\u00e1nyi","year":"1994","unstructured":"Urb\u00e1nyi Z, Lakics V, Erd\u00f6 SL. Serum amyloid P component-induced cell death in primary cultures of rat cerebral cortex. Eur J Pharmacol. 1994;270:375\u20138.","journal-title":"Eur J Pharmacol"},{"key":"465_CR325","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1016\/S0006-8993(98)00966-4","volume":"813","author":"T Duong","year":"1998","unstructured":"Duong T, Acton PJ, Johnson RA. The in vitro neuronal toxicity of pentraxins associated with Alzheimer\u2019s disease brain lesions. Brain Res. 1998;813:303\u201312.","journal-title":"Brain Res"},{"key":"465_CR326","doi-asserted-by":"publisher","first-page":"150202","DOI":"10.1098\/rsob.150202","volume":"6","author":"R Al-Shawi","year":"2016","unstructured":"Al-Shawi R, Tennent GA, Millar DJ, Richard-Londt A, Brandner S, Werring DJ, et al. Pharmacological removal of serum amyloid P component from intracerebral plaques and cerebrovascular A\u03b2 amyloid deposits in vivo. Open Biol. 2016;6:150202.","journal-title":"Open Biol"},{"key":"465_CR327","doi-asserted-by":"publisher","first-page":"621","DOI":"10.1111\/joim.12175","volume":"275","author":"ET Askevold","year":"2014","unstructured":"Askevold ET, Aukrust P, Nymo SH, Lunde IG, Kaasb\u00f8ll OJ, Aakhus S, et al. The cardiokine secreted frizzled-related protein 3, a modulator of Wnt signalling, in clinical and experimental heart failure. J Int Med. 2014;275:621\u201330.","journal-title":"J Int Med"},{"key":"465_CR328","doi-asserted-by":"crossref","unstructured":"Ng LF, Kaur P, Bunnag N, Suresh J, Sung ICH, Tan QH, et al. WNT signaling in disease. Cells. 2019;8","DOI":"10.3390\/cells8080826"},{"key":"465_CR329","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1038\/sj.mp.4001208","volume":"8","author":"GV De Ferrari","year":"2003","unstructured":"De Ferrari GV, Chac\u00f3n MA, Barr\u00eda MI, Garrido JL, Godoy JA, Olivares G, et al. Activation of Wnt signaling rescues neurodegeneration and behavioral impairments induced by \u03b2-amyloid fibrils. Mol Psychiatry. 2003;8:195\u2013208.","journal-title":"Mol Psychiatry"},{"key":"465_CR330","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1186\/s13024-019-0320-x","volume":"14","author":"D Twohig","year":"2019","unstructured":"Twohig D, Nielsen HM. \u03b1-synuclein in the pathophysiology of Alzheimer\u2019s disease. Mol Neurodegener. 2019;14:23.","journal-title":"Mol Neurodegener"},{"key":"465_CR331","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1038\/nrn.2015.1","volume":"17","author":"Y Wang","year":"2016","unstructured":"Wang Y, Mandelkow E. Tau in physiology and pathology. Nat Rev Neurosci. 2016;17:5\u201321.","journal-title":"Nat Rev Neurosci"},{"key":"465_CR332","doi-asserted-by":"publisher","first-page":"11282","DOI":"10.1073\/pnas.90.23.11282","volume":"90","author":"K U\u00e9da","year":"1993","unstructured":"U\u00e9da K, Fukushima H, Masliah E, Xia Y, Iwai A, Yoshimoto M, et al. Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proc Natl Acad Sci U S A. 1993;90:11282\u20136.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR333","first-page":"201","volume":"148","author":"E Masliah","year":"1996","unstructured":"Masliah E, Iwai A, Mallory M, U\u00e9da K, Saitoh T. Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer\u2019s disease. Am J Pathol. 1996;148:201\u201310.","journal-title":"Am J Pathol"},{"key":"465_CR334","doi-asserted-by":"publisher","first-page":"492","DOI":"10.1038\/35081564","volume":"2","author":"M Goedert","year":"2001","unstructured":"Goedert M. \u03b1-synuclein and neurodegenerative diseases. Nat Rev Neurosci. 2001;2:492\u2013501.","journal-title":"Nat Rev Neurosci"},{"key":"465_CR335","doi-asserted-by":"publisher","first-page":"D607","DOI":"10.1093\/nar\/gky1131","volume":"47","author":"D Szklarczyk","year":"2019","unstructured":"Szklarczyk D, Gable AL, Lyon D, Junge A, Wyder S, Huerta-Cepas J, et al. STRING v11: protein-protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets. Nucleic Acids Res. 2019;47:D607\u2013d13.","journal-title":"Nucleic Acids Res"},{"key":"465_CR336","doi-asserted-by":"publisher","first-page":"499","DOI":"10.1038\/nrn2168","volume":"8","author":"FM LaFerla","year":"2007","unstructured":"LaFerla FM, Green KN, Oddo S. Intracellular amyloid-\u03b2 in Alzheimer\u2019s disease. Nat Rev Neurosci. 2007;8:499\u2013509.","journal-title":"Nat Rev Neurosci"},{"key":"465_CR337","doi-asserted-by":"publisher","first-page":"3339","DOI":"10.1242\/jcs.00643","volume":"116","author":"A Kinoshita","year":"2003","unstructured":"Kinoshita A, Fukumoto H, Shah T, Whelan CM, Irizarry MC, Hyman BT. Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes. J Cell Sci. 2003;116:3339\u201346.","journal-title":"J Cell Sci"},{"key":"465_CR338","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1146\/annurev-neuro-061010-113613","volume":"34","author":"RJ O\u2019Brien","year":"2011","unstructured":"O\u2019Brien RJ, Wong PC. Amyloid precursor protein processing and Alzheimer\u2019s disease. Annu Rev Neurosci. 2011;34:185\u2013204.","journal-title":"Annu Rev Neurosci"},{"key":"465_CR339","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1126\/science.abb8587","volume":"370","author":"T Bartels","year":"2020","unstructured":"Bartels T, De Schepper S, Hong S. Microglia modulate neurodegeneration in Alzheimer\u2019s and Parkinson\u2019s diseases. Science. 2020;370:66\u20139.","journal-title":"Science"},{"key":"465_CR340","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1186\/s40035-020-00221-2","volume":"9","author":"HS Kwon","year":"2020","unstructured":"Kwon HS, Koh SH. Neuroinflammation in neurodegenerative disorders: the roles of microglia and astrocytes. Transl Neurodegener. 2020;9:42.","journal-title":"Transl Neurodegener"},{"key":"465_CR341","doi-asserted-by":"publisher","first-page":"609073","DOI":"10.3389\/fnmol.2020.609073","volume":"13","author":"MR Brown","year":"2020","unstructured":"Brown MR, Radford SE, Hewitt EW. Modulation of \u03b2-amyloid fibril formation in Alzheimer\u2019s disease by microglia and infection. Front Mol Neurosci. 2020;13:609073.","journal-title":"Front Mol Neurosci"},{"key":"465_CR342","doi-asserted-by":"publisher","first-page":"2665","DOI":"10.1523\/JNEUROSCI.23-07-02665.2003","volume":"23","author":"ME Bamberger","year":"2003","unstructured":"Bamberger ME, Harris ME, McDonald DR, Husemann J, Landreth GE. A cell surface receptor complex for fibrillar \u03b2-amyloid mediates microglial activation. J Neurosci. 2003;23:2665\u201374.","journal-title":"J Neurosci"},{"key":"465_CR343","doi-asserted-by":"publisher","first-page":"7254","DOI":"10.4049\/jimmunol.181.10.7254","volume":"181","author":"M Jana","year":"2008","unstructured":"Jana M, Palencia CA, Pahan K. Fibrillar amyloid-\u03b2 peptides activate microglia via TLR2: implications for Alzheimer\u2019s disease. J Immunol. 2008;181:7254\u201362.","journal-title":"J Immunol"},{"key":"465_CR344","doi-asserted-by":"publisher","first-page":"1023","DOI":"10.1016\/j.neuron.2018.01.031","volume":"97","author":"Y Zhao","year":"2018","unstructured":"Zhao Y, Wu X, Li X, Jiang LL, Gui X, Liu Y, et al. TREM2 is a receptor for \u03b2-amyloid that mediates microglial function. Neuron. 2018;97:1023\u201331.e7.","journal-title":"Neuron"},{"key":"465_CR345","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1007\/s11481-012-9427-3","volume":"8","author":"RS Jones","year":"2013","unstructured":"Jones RS, Minogue AM, Connor TJ, Lynch MA. Amyloid-\u03b2-induced astrocytic phagocytosis is mediated by CD36, CD47 and RAGE. J Neuroimmune Pharmacol. 2013;8:301\u201311.","journal-title":"J Neuroimmune Pharmacol"},{"key":"465_CR346","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1186\/s13024-016-0098-z","volume":"11","author":"S S\u00f6llvander","year":"2016","unstructured":"S\u00f6llvander S, Nikitidou E, Brolin R, S\u00f6derberg L, Sehlin D, Lannfelt L, et al. Accumulation of amyloid-\u03b2 by astrocytes result in enlarged endosomes and microvesicle-induced apoptosis of neurons. Mol Neurodegener. 2016;11:38.","journal-title":"Mol Neurodegener"},{"key":"465_CR347","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1038\/382685a0","volume":"382","author":"SD Yan","year":"1996","unstructured":"Yan SD, Chen X, Fu J, Chen M, Zhu H, Roher A, et al. RAGE and amyloid-\u03b2 peptide neurotoxicity in Alzheimer\u2019s disease. Nature. 1996;382:685\u201391.","journal-title":"Nature"},{"key":"465_CR348","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1016\/S0306-4522(01)00460-2","volume":"110","author":"RG Nagele","year":"2002","unstructured":"Nagele RG, D'Andrea MR, Anderson WJ, Wang HY. Intracellular accumulation of \u03b2-amyloid(1-42) in neurons is facilitated by the \u03b17 nicotinic acetylcholine receptor in Alzheimer\u2019s disease. Neuroscience. 2002;110:199\u2013211.","journal-title":"Neuroscience"},{"key":"465_CR349","doi-asserted-by":"publisher","first-page":"1051","DOI":"10.1038\/nn1503","volume":"8","author":"EM Snyder","year":"2005","unstructured":"Snyder EM, Nong Y, Almeida CG, Paul S, Moran T, Choi EY, et al. Regulation of NMDA receptor trafficking by amyloid-\u03b2. Nat Neurosci. 2005;8:1051\u20138.","journal-title":"Nat Neurosci"},{"key":"465_CR350","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1196\/annals.1377.005","volume":"1086","author":"G Bu","year":"2006","unstructured":"Bu G, Cam J, Zerbinatti C. LRP in amyloid-\u03b2 production and metabolism. Ann N Y Acad Sci. 2006;1086:35\u201353.","journal-title":"Ann N Y Acad Sci"},{"key":"465_CR351","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1016\/S0002-9440(10)64700-1","volume":"156","author":"GK Gouras","year":"2000","unstructured":"Gouras GK, Tsai J, N\u00e4slund J, Vincent B, Edgar M, Checler F, et al. Intraneuronal A\u03b242 accumulation in human brain. Am J Pathol. 2000;156:15\u201320.","journal-title":"Am J Pathol"},{"key":"465_CR352","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1016\/S0140-6736(99)04937-5","volume":"355","author":"A Mochizuki","year":"2000","unstructured":"Mochizuki A, Tamaoka A, Shimohata A, Komatsuzaki Y, Shoji S. A\u03b242-positive non-pyramidal neurons around amyloid plaques in Alzheimer\u2019s disease. Lancet. 2000;355:42\u20133.","journal-title":"Lancet"},{"key":"465_CR353","doi-asserted-by":"publisher","first-page":"1942","DOI":"10.1073\/pnas.0904532106","volume":"107","author":"RP Friedrich","year":"2010","unstructured":"Friedrich RP, Tepper K, R\u00f6nicke R, Soom M, Westermann M, Reymann K, et al. Mechanism of amyloid plaque formation suggests an intracellular basis of A\u03b2 pathogenicity. Proc Natl Acad Sci U S A. 2010;107:1942\u20137.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"465_CR354","doi-asserted-by":"publisher","first-page":"1148","DOI":"10.1016\/j.lfs.2012.02.001","volume":"91","author":"O Wirths","year":"2012","unstructured":"Wirths O, Bayer TA. Intraneuronal A\u03b2 accumulation and neurodegeneration: lessons from transgenic models. Life Sci. 2012;91:1148\u201352.","journal-title":"Life Sci"},{"key":"465_CR355","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0024909","volume":"6","author":"C Manzoni","year":"2011","unstructured":"Manzoni C, Colombo L, Bigini P, Diana V, Cagnotto A, Messa M, et al. The molecular assembly of amyloid A\u03b2 controls its neurotoxicity and binding to cellular proteins. PLoS One. 2011;6:e24909.","journal-title":"PLoS One"},{"key":"465_CR356","doi-asserted-by":"publisher","first-page":"8667","DOI":"10.1039\/C8CC02204F","volume":"54","author":"M T\u00f6rnquist","year":"2018","unstructured":"T\u00f6rnquist M, Michaels TCT, Sanagavarapu K, Yang X, Meisl G, Cohen SIA, et al. Secondary nucleation in amyloid formation. Chem Commun (Camb). 2018;54:8667\u201384.","journal-title":"Chem Commun (Camb)"}],"container-title":["Molecular Neurodegeneration"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s13024-021-00465-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s13024-021-00465-0\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s13024-021-00465-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,2,6]],"date-time":"2023-02-06T01:06:03Z","timestamp":1675645563000},"score":1,"resource":{"primary":{"URL":"https:\/\/molecularneurodegeneration.biomedcentral.com\/articles\/10.1186\/s13024-021-00465-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,8,28]]},"references-count":356,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2021,12]]}},"alternative-id":["465"],"URL":"https:\/\/doi.org\/10.1186\/s13024-021-00465-0","relation":{},"ISSN":["1750-1326"],"issn-type":[{"value":"1750-1326","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,8,28]]},"assertion":[{"value":"17 October 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 June 2021","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"28 August 2021","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"The authors declare that they have no competing interests.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"59"}}