{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T18:47:11Z","timestamp":1780426031010,"version":"3.54.1"},"reference-count":71,"publisher":"Springer Science and Business Media LLC","issue":"8","license":[{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["19K16919"],"award-info":[{"award-number":["19K16919"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["19KK0410"],"award-info":[{"award-number":["19KK0410"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008735","name":"Japan Foundation of Applied Enzymology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008735","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008880","name":"Kanae Foundation for the Promotion of Medical Science","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008880","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008732","name":"Uehara Memorial Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008732","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006679","name":"Kobayashi Magobe Memorial Medical Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100006679","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007449","name":"Takeda Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007449","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Daiwa Health Foundation"},{"DOI":"10.13039\/501100008665","name":"Osaka Medical Research Foundation for Intractable Diseases","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005865","name":"Mochida Memorial Foundation for Medical and Pharmaceutical Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005865","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008667","name":"SENSHIN Medical Research Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008667","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Cell. Mol. Life Sci."],"published-print":{"date-parts":[[2022,8]]},"DOI":"10.1007\/s00018-022-04493-x","type":"journal-article","created":{"date-parts":[[2022,8,2]],"date-time":"2022-08-02T10:02:46Z","timestamp":1659434566000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["\u03b1-Enolase reduces cerebrovascular A\u03b2 deposits by protecting A\u03b2 amyloid formation"],"prefix":"10.1007","volume":"79","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4180-5908","authenticated-orcid":false,"given":"Yasuteru","family":"Inoue","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masayoshi","family":"Tasaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Teruaki","family":"Masuda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yohei","family":"Misumi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toshiya","family":"Nomura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yukio","family":"Ando","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mitsuharu","family":"Ueda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2022,8,2]]},"reference":[{"key":"4493_CR1","first-page":"249","volume":"141","author":"H Yamaguchi","year":"1992","unstructured":"Yamaguchi H, Yamazaki T, Lemere CA, Frosch MP, Selkoe DJ (1992) Beta amyloid is focally deposited within the outer basement membrane in the amyloid angiopathy of Alzheimer\u2019s disease. An immunoelectron microscopic study. Am J Pathol 141:249\u2013259","journal-title":"Am J Pathol"},{"key":"4493_CR2","doi-asserted-by":"publisher","first-page":"871","DOI":"10.1002\/ana.22516","volume":"70","author":"A Viswanathan","year":"2011","unstructured":"Viswanathan A, Greenberg SM (2011) Cerebral amyloid angiopathy in the elderly. Ann Neurol 70:871\u2013880","journal-title":"Ann Neurol"},{"key":"4493_CR3","doi-asserted-by":"publisher","first-page":"813","DOI":"10.1007\/s007020200068","volume":"109","author":"KA Jellinger","year":"2002","unstructured":"Jellinger KA (2002) Alzheimer disease and cerebrovascular pathology: an update. J Neural Transm (Vienna) 109:813\u2013836","journal-title":"J Neural Transm (Vienna)"},{"key":"4493_CR4","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1074\/mcp.R115.053330","volume":"15","author":"G Moya-Alvarado","year":"2016","unstructured":"Moya-Alvarado G, Gershoni-Emek N, Perlson E, Bronfman FC (2016) Neurodegeneration and Alzheimer\u2019s disease (AD). What can proteomics tell us about the Alzheimer\u2019s brain? Mol Cell Proteomics 15:409\u2013425","journal-title":"Mol Cell Proteomics"},{"key":"4493_CR5","doi-asserted-by":"publisher","first-page":"912","DOI":"10.4103\/1673-5374.208570","volume":"12","author":"E Drummond","year":"2017","unstructured":"Drummond E, Wisniewski T (2017) The use of localized proteomics to identify the drivers of Alzheimer\u2019s disease pathogenesis. Neural Regen Res 12:912\u2013913","journal-title":"Neural Regen Res"},{"key":"4493_CR6","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1111\/jnc.14603","volume":"151","author":"KW Li","year":"2019","unstructured":"Li KW, Ganz AB, Smit AB (2019) Proteomics of neurodegenerative diseases: analysis of human post-mortem brain. J Neurochem 151:435\u2013445","journal-title":"J Neurochem"},{"key":"4493_CR7","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 (2001) Proteomic analysis of the brain in Alzheimer\u2019s disease: molecular phenotype of a complex disease process. Proteomics 1:1519\u20131528","journal-title":"Proteomics"},{"key":"4493_CR8","doi-asserted-by":"publisher","first-page":"1564","DOI":"10.1016\/j.neurobiolaging.2005.09.021","volume":"27","author":"R Sultana","year":"2006","unstructured":"Sultana R, Boyd-Kimball D, Poon HF, Cai J, Pierce WM, Klein JB et al (2006) Redox proteomics identification of oxidized proteins in Alzheimer\u2019s disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD. Neurobiol Aging 27:1564\u20131576","journal-title":"Neurobiol Aging"},{"key":"4493_CR9","doi-asserted-by":"publisher","first-page":"153","DOI":"10.3233\/JAD-2007-11203","volume":"11","author":"R Sultana","year":"2007","unstructured":"Sultana R, Boyd-Kimball D, Cai J, Pierce WM, Klein JB, Merchant M et al (2007) Proteomics analysis of the Alzheimer\u2019s disease hippocampal proteome. J Alzheimers Dis 11:153\u2013164","journal-title":"J Alzheimers Dis"},{"key":"4493_CR10","doi-asserted-by":"publisher","first-page":"682","DOI":"10.1002\/prca.200800161","volume":"3","author":"M Perluigi","year":"2009","unstructured":"Perluigi M, Sultana R, Cenini G, Di Domenico F, Memo M, Pierce WM et al (2009) Redox proteomics identification of 4-hydroxynonenal-modified brain proteins in Alzheimer\u2019s disease: role of lipid peroxidation in Alzheimer\u2019s disease pathogenesis. Proteomics Clin Appl 3:682\u2013693","journal-title":"Proteomics Clin Appl"},{"key":"4493_CR11","doi-asserted-by":"publisher","first-page":"1091","DOI":"10.1016\/j.jprot.2011.03.033","volume":"74","author":"F Di Domenico","year":"2011","unstructured":"Di Domenico F, Sultana R, Barone E, Perluigi M, Cini C, Mancuso C et al (2011) Quantitative proteomics analysis of phosphorylated proteins in the hippocampus of Alzheimer\u2019s disease subjects. J Proteomics 74:1091\u20131103","journal-title":"J Proteomics"},{"key":"4493_CR12","doi-asserted-by":"publisher","first-page":"954","DOI":"10.1111\/j.1471-4159.2012.07737.x","volume":"121","author":"S Zahid","year":"2012","unstructured":"Zahid S, Oellerich M, Asif AR, Ahmed N (2012) Phosphoproteome profiling of substantia nigra and cortex regions of Alzheimer\u2019s disease patients. J Neurochem 121:954\u2013963","journal-title":"J Neurochem"},{"key":"4493_CR13","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 (2009) Multifunctional roles of enolase in Alzheimer\u2019s disease brain: beyond altered glucose metabolism. J Neurochem 111:915\u2013933","journal-title":"J Neurochem"},{"key":"4493_CR14","doi-asserted-by":"publisher","first-page":"605","DOI":"10.1007\/s00401-017-1720-z","volume":"134","author":"Y Inoue","year":"2017","unstructured":"Inoue Y, Ueda M, Tasaki M, Takeshima A, Nagatoshi A, Masuda T et al (2017) Sushi repeat-containing protein 1: a novel disease-associated molecule in cerebral amyloid angiopathy. Acta Neuropathol 134:605\u2013617","journal-title":"Acta Neuropathol"},{"key":"4493_CR15","doi-asserted-by":"publisher","first-page":"902","DOI":"10.1007\/PL00000910","volume":"58","author":"V Pancholi","year":"2001","unstructured":"Pancholi V (2001) Multifunctional \u03b1-enolase: its role in diseases. Cell Mol Life Sci 58:902\u2013920","journal-title":"Cell Mol Life Sci"},{"key":"4493_CR16","doi-asserted-by":"publisher","first-page":"503","DOI":"10.1038\/nature06281","volume":"450","author":"K Kobayakawa","year":"2007","unstructured":"Kobayakawa K, Kobayakawa R, Matsumoto H, Oka Y, Imai T, Ikawa M et al (2007) Innate versus learned odour processing in the mouse olfactory bulb. Nature 450:503\u2013508","journal-title":"Nature"},{"key":"4493_CR17","doi-asserted-by":"publisher","first-page":"202","DOI":"10.1002\/ana.1095","volume":"50","author":"GP Comi","year":"2001","unstructured":"Comi GP, Fortunato F, Lucchiari S, Bordoni A, Prelle A, Jann S et al (2001) \u03b2-Enolase deficiency, a new metabolic myopathy of distal glycolysis. Ann Neurol 50:202\u2013207","journal-title":"Ann Neurol"},{"key":"4493_CR18","doi-asserted-by":"publisher","first-page":"14503","DOI":"10.1074\/jbc.273.23.14503","volume":"273","author":"V Pancholi","year":"1998","unstructured":"Pancholi V, Fischetti VA (1998) \u03b1-Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 273:14503\u201314515","journal-title":"J Biol Chem"},{"key":"4493_CR19","doi-asserted-by":"publisher","first-page":"1178","DOI":"10.1111\/j.1471-4159.1991.tb08277.x","volume":"57","author":"N Takei","year":"1991","unstructured":"Takei N, Kondo J, Nagaike K, Ohsawa K, Kato K, Kohsaka S (1991) Neuronal survival factor from bovine brain is identical to neuron-specific enolase. J Neurochem 57:1178\u20131184","journal-title":"J Neurochem"},{"key":"4493_CR20","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1038\/315688a0","volume":"315","author":"H Iida","year":"1985","unstructured":"Iida H, Yahara I (1985) Yeast heat-shock protein of Mr 48,000 is an isoprotein of enolase. Nature 315:688\u2013690","journal-title":"Nature"},{"key":"4493_CR21","doi-asserted-by":"publisher","first-page":"27752","DOI":"10.1074\/jbc.270.46.27752","volume":"270","author":"RM Aaronson","year":"1995","unstructured":"Aaronson RM, Graven KK, Tucci M, McDonald RJ, Farber HW (1995) Non-neuronal enolase is an endothelial hypoxic stress protein. J Biol Chem 270:27752\u201327757","journal-title":"J Biol Chem"},{"key":"4493_CR22","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1111\/j.1432-1033.1995.tb20403.x","volume":"227","author":"A Redlitz","year":"1995","unstructured":"Redlitz A, Fowler BJ, Plow EF, Miles LA (1995) The role of an enolase-related molecule in plasminogen binding to cells. Eur J Biochem 227:407\u2013415","journal-title":"Eur J Biochem"},{"key":"4493_CR23","doi-asserted-by":"publisher","first-page":"8573","DOI":"10.1007\/s12035-019-01678-7","volume":"56","author":"Y Inoue","year":"2019","unstructured":"Inoue Y, Ueda M, Masuda T, Misumi Y, Yamashita T, Ando Y (2019) Memantine, a noncompetitive N-methyl-D-aspartate receptor antagonist, attenuates cerebral amyloid angiopathy by increasing insulin-degrading enzyme expression. Mol Neurobiol 56:8573\u20138588","journal-title":"Mol Neurobiol"},{"key":"4493_CR24","doi-asserted-by":"publisher","first-page":"883","DOI":"10.1111\/j.1471-4159.2012.07847.x","volume":"122","author":"K Ono","year":"2012","unstructured":"Ono K, Takahashi R, Ikeda T, Yamada M (2012) Cross-seeding effects of amyloid \u03b2-protein and \u03b1-synuclein. J Neurochem 122:883\u2013890","journal-title":"J Neurochem"},{"key":"4493_CR25","doi-asserted-by":"publisher","first-page":"444","DOI":"10.1002\/path.5203","volume":"247","author":"M Tasaki","year":"2019","unstructured":"Tasaki M, Ueda M, Hoshii Y, Mizukami M, Matsumoto S, Nakamura M et al (2019) A novel age-related venous amyloidosis derived from EGF-containing fibulin-like extracellular matrix protein 1. J Pathol 247:444\u2013455","journal-title":"J Pathol"},{"key":"4493_CR26","doi-asserted-by":"publisher","first-page":"553","DOI":"10.1016\/0006-291X(82)91146-9","volume":"106","author":"SG Spencer","year":"1982","unstructured":"Spencer SG, Brewer JM (1982) Substrate-dependent inhibition of yeast enolase by fluoride. Biochem Biophys Res Commun 106:553\u2013558","journal-title":"Biochem Biophys Res Commun"},{"key":"4493_CR27","first-page":"1","volume":"23","author":"S Shenolikar","year":"1991","unstructured":"Shenolikar S, Nairn AC (1991) Protein phosphatases: recent progress. Adv Second Messenger Phosphoprotein Res 23:1\u2013121","journal-title":"Adv Second Messenger Phosphoprotein Res"},{"key":"4493_CR28","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1016\/S0003-9861(71)80053-X","volume":"146","author":"JA Kanapka","year":"1971","unstructured":"Kanapka JA, Hamilton IR (1971) Fluoride inhibition of enolase activity in vivo and its relationship to the inhibition of glucose-6-P formation in Streptococcus salivarius. Arch Biochem Biophys 146:167\u2013171","journal-title":"Arch Biochem Biophys"},{"key":"4493_CR29","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1159\/000260304","volume":"11","author":"IR Hamilton","year":"1977","unstructured":"Hamilton IR (1977) Effects of fluoride on enzymatic regulation of bacterial carbohydrate metabolism. Caries Res 11:262\u2013291","journal-title":"Caries Res"},{"key":"4493_CR30","volume":"105","author":"AC Boulay","year":"2015","unstructured":"Boulay AC, Saubam\u00e9a B, Decl\u00e8ves X, Cohen-Salmon M (2015) Purification of mouse brain vessels. J Vis Exp 105:e53208","journal-title":"J Vis Exp"},{"key":"4493_CR31","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1038\/nprot.2006.4","volume":"1","author":"H Sch\u00e4gger","year":"2006","unstructured":"Sch\u00e4gger H (2006) Tricine-SDS-PAGE. Nat Protoc 1:16\u201322","journal-title":"Nat Protoc"},{"key":"4493_CR32","doi-asserted-by":"publisher","first-page":"1429","DOI":"10.1007\/s00018-010-0529-x","volume":"68","author":"R Sarroukh","year":"2011","unstructured":"Sarroukh R, Cerf E, Derclaye S, Dufr\u00eane YF, Goormaghtigh E, Ruysschaert JM, Raussens V (2011) Transformation of amyloid \u03b2(1\u201340) oligomers into fibrils is characterized by a major change in secondary structure. Cell Mol Life Sci 68:1429\u20131438","journal-title":"Cell Mol Life Sci"},{"key":"4493_CR33","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1042\/BJ20090379","volume":"421","author":"E Cerf","year":"2009","unstructured":"Cerf E, Sarroukh R, Tamamizu-Kato S, Breydo L, Derclaye S, Dufr\u00eane YF, Narayanaswami V, Goormaghtigh E, Ruysschaert JM, Raussens V (2009) Antiparallel \u03b2-sheet: a signature structure of the oligomeric amyloid \u03b2-peptide. Biochem J 421:415\u2013423","journal-title":"Biochem J"},{"key":"4493_CR34","doi-asserted-by":"publisher","first-page":"776","DOI":"10.1186\/s12864-019-6158-3","volume":"20","author":"XY Zhang","year":"2019","unstructured":"Zhang XY, Sun XZ, Zhang S, Yang JH, Liu FF, Fan J (2019) Comprehensive transcriptome analysis of grafting onto Artemisia scoparia W. to affect the aphid resistance of chrysanthemum (Chrysanthemum morifolium T.). BMC Genomics 20:776","journal-title":"BMC Genomics"},{"key":"4493_CR35","doi-asserted-by":"publisher","first-page":"353","DOI":"10.1016\/0005-2760(95)00226-X","volume":"1299","author":"C Dentan","year":"1996","unstructured":"Dentan C, Tselepis AD, Chapman MJ, Ninio E (1996) Pefabloc, 4-[2-aminoethyl]benzenesulfonyl fluoride, is a new, potent nontoxic and irreversible inhibitor of PAF-degrading acetylhydrolase. Biochim Biophys Acta 1299:353\u2013357","journal-title":"Biochim Biophys Acta"},{"key":"4493_CR36","doi-asserted-by":"publisher","first-page":"C413","DOI":"10.1111\/j.1750-3841.2008.00777.x","volume":"73","author":"S Nalinanon","year":"2008","unstructured":"Nalinanon S, Benjakul S, Visessanguan W, Kishimura H (2008) Tuna pepsin: characteristics and its use for collagen extraction from the skin of threadfin bream (Nemipterus spp.). J Food Sci 73:C413-419","journal-title":"J Food Sci"},{"key":"4493_CR37","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1016\/S0166-6851(01)00452-2","volume":"120","author":"J Li","year":"2002","unstructured":"Li J, Matsuoka H, Mitamura T, Horii T (2002) Characterization of proteases involved in the processing of Plasmodium falciparum serine repeat antigen (SERA). Mol Biochem Parasitol 120:177\u2013186","journal-title":"Mol Biochem Parasitol"},{"key":"4493_CR38","doi-asserted-by":"publisher","first-page":"708","DOI":"10.1016\/j.foodchem.2016.07.029","volume":"213","author":"Q Sun","year":"2016","unstructured":"Sun Q, Zhang B, Yan QJ, Jiang ZQ (2016) Comparative analysis on the distribution of protease activities among fruits and vegetable resources. Food Chem 213:708\u2013713","journal-title":"Food Chem"},{"key":"4493_CR39","doi-asserted-by":"publisher","first-page":"921","DOI":"10.1152\/jappl.1995.78.3.921","volume":"78","author":"H Tsukagoshi","year":"1995","unstructured":"Tsukagoshi H, Sun J, Kwon O, Barnes PJ, Chung KF (1995) Role of neutral endopeptidase in bronchial hyperresponsiveness to bradykinin induced by IL-1 beta. J Appl Physiol 78:921\u2013927","journal-title":"J Appl Physiol"},{"key":"4493_CR40","doi-asserted-by":"publisher","first-page":"13287","DOI":"10.1073\/pnas.94.24.13287","volume":"94","author":"C Sturchler-Pierrat","year":"1997","unstructured":"Sturchler-Pierrat C, Abramowski D, Duke M, Wiederhold KH, Mistl C, Rothacher S et al (1997) Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology. Proc Natl Acad Sci USA 94:13287\u201313292","journal-title":"Proc Natl Acad Sci USA"},{"key":"4493_CR41","doi-asserted-by":"publisher","first-page":"873","DOI":"10.1016\/j.freeradbiomed.2010.01.010","volume":"48","author":"N Lu","year":"2010","unstructured":"Lu N, Zhang Y, Li H, Gao Z (2010) Oxidative and nitrative modifications of \u03b1-enolase in cardiac proteins from diabetic rats. Free Radic Biol Med 48:873\u2013881","journal-title":"Free Radic Biol Med"},{"key":"4493_CR42","doi-asserted-by":"publisher","first-page":"481","DOI":"10.1538\/expanim.60.481","volume":"60","author":"S Kawai","year":"2011","unstructured":"Kawai S, Takagi Y, Kaneko S, Kurosawa T (2011) Effect of three types of mixed anesthetic agents alternate to ketamine in mice. Exp Anim 60:481\u2013487","journal-title":"Exp Anim"},{"key":"4493_CR43","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1186\/s12868-018-0402-7","volume":"19","author":"XM Qi","year":"2018","unstructured":"Qi XM, Wang C, Chu XK, Li G, Ma JF (2018) Intraventricular infusion of clusterin ameliorated cognition and pathology in Tg6799 model of Alzheimer\u2019s disease. BMC Neurosci 19:2","journal-title":"BMC Neurosci"},{"key":"4493_CR44","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1111\/j.1601-183X.2008.00439.x","volume":"8","author":"BM de Castro","year":"2009","unstructured":"de Castro BM, Pereira GS, Magalh\u00e3es V, Rossato JI, De Jaeger X, Martins-Silva C et al (2009) Reduced expression of the vesicular acetylcholine transporter causes learning deficits in mice. Genes Brain Behav 8:23\u201335","journal-title":"Genes Brain Behav"},{"key":"4493_CR45","doi-asserted-by":"publisher","first-page":"17941","DOI":"10.1074\/jbc.M601372200","volume":"281","author":"SM Huang","year":"2006","unstructured":"Huang SM, Mouri A, Kokubo H, Nakajima R, Suemoto T, Higuchi M et al (2006) Neprilysin-sensitive synapse-associated amyloid-\u03b2 peptide oligomers impair neuronal plasticity and cognitive function. J Biol Chem 281:17941\u201317951","journal-title":"J Biol Chem"},{"key":"4493_CR46","doi-asserted-by":"publisher","first-page":"157","DOI":"10.3109\/13506129909007321","volume":"6","author":"J Davis","year":"1999","unstructured":"Davis J, Cribbs DH, Cotman CW, Van Nostrand WE (1999) Pathogenic amyloid \u03b2-protein induces apoptosis in cultured human cerebrovascular smooth muscle cells. Amyloid 6:157\u2013164","journal-title":"Amyloid"},{"key":"4493_CR47","doi-asserted-by":"publisher","first-page":"50120","DOI":"10.1074\/jbc.M402299200","volume":"279","author":"Y Mizukami","year":"2004","unstructured":"Mizukami Y, Iwamatsu A, Aki T, Kimura M, Nakamura K, Nao T et al (2004) ERK1\/2 regulates intracellular ATP levels through \u03b1-enolase expression in cardiomyocytes exposed to ischemic hypoxia and reoxygenation. J Biol Chem 279:50120\u201350131","journal-title":"J Biol Chem"},{"key":"4493_CR48","doi-asserted-by":"publisher","first-page":"3850","DOI":"10.1038\/s41467-018-06376-x","volume":"9","author":"J Dai","year":"2018","unstructured":"Dai J, Zhou Q, Chen J, Rexius-Hall ML, Rehman J, Zhou G (2018) Alpha-enolase regulates the malignant phenotype of pulmonary artery smooth muscle cells via the AMPK-Akt pathway. Nat Commun 9:3850","journal-title":"Nat Commun"},{"key":"4493_CR49","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1016\/S0076-6879(99)09022-9","volume":"309","author":"H Naiki","year":"1999","unstructured":"Naiki H, Gejyo F (1999) Kinetic analysis of amyloid fibril formation. Methods Enzymol 309:305\u2013318","journal-title":"Methods Enzymol"},{"key":"4493_CR50","doi-asserted-by":"publisher","first-page":"404","DOI":"10.1002\/pro.5560020312","volume":"2","author":"H LeVine 3rd","year":"1993","unstructured":"LeVine H 3rd (1993) Thioflavine T interaction with synthetic Alzheimer\u2019s disease \u03b2-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 2:404\u2013410","journal-title":"Protein Sci"},{"key":"4493_CR51","doi-asserted-by":"publisher","first-page":"36499","DOI":"10.1038\/srep36499","volume":"6","author":"OH Bastidas","year":"2016","unstructured":"Bastidas OH, Green B, Sprague M, Peters MH (2016) Few Ramachandran angle changes provide interaction strength increase in A\u03b242 versus A\u03b240 amyloid fibrils. Sci Rep 6:36499","journal-title":"Sci Rep"},{"key":"4493_CR52","doi-asserted-by":"publisher","first-page":"2405","DOI":"10.1007\/s00018-004-4256-z","volume":"61","author":"P Wang","year":"2004","unstructured":"Wang P, Mariman E, Keijer J, Bouwman F, Noben JP, Robben J et al (2004) Profiling of the secreted proteins during 3T3-L1 adipocyte differentiation leads to the identification of novel adipokines. Cell Mol Life Sci 61:2405\u20132417","journal-title":"Cell Mol Life Sci"},{"key":"4493_CR53","doi-asserted-by":"publisher","first-page":"8443","DOI":"10.1074\/jbc.271.14.8443","volume":"271","author":"WQ Qiu","year":"1996","unstructured":"Qiu WQ, Borth W, Ye Z, Haass C, Teplow DB, Selkoe DJ (1996) Degradation of amyloid \u03b2-protein by a serine protease-\u03b12-macroglobulin complex. J Biol Chem 271:8443\u20138451","journal-title":"J Biol Chem"},{"key":"4493_CR54","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1007\/s11010-011-1028-6","volume":"359","author":"CY Wu","year":"2012","unstructured":"Wu CY, Tang ZH, Jiang L, Li XF, Jiang ZS, Liu LS (2012) PCSK9 siRNA inhibits HUVEC apoptosis induced by ox-LDL via Bcl\/Bax-caspase9-caspase3 pathway. Mol Cell Biochem 359:347\u2013358","journal-title":"Mol Cell Biochem"},{"key":"4493_CR55","doi-asserted-by":"publisher","first-page":"1815","DOI":"10.1016\/j.neurobiolaging.2007.05.001","volume":"29","author":"RC Li","year":"2008","unstructured":"Li RC, Pouranfar F, Lee SK, Morris MW, Wang Y, Gozal D (2008) Neuroglobin protects PC12 cells against \u03b2-amyloid-induced cell injury. Neurobiol Aging 29:1815\u20131822","journal-title":"Neurobiol Aging"},{"key":"4493_CR56","doi-asserted-by":"publisher","first-page":"905","DOI":"10.1016\/j.freeradbiomed.2011.05.036","volume":"51","author":"Y Oh","year":"2011","unstructured":"Oh Y, Kim EY, Kim Y, Jin J, Jin BK, Jahng GH et al (2011) Neuroprotective effects of overexpressed cyclophilin B against A\u03b2-induced neurotoxicity in PC12 cells. Free Radic Biol Med 51:905\u2013920","journal-title":"Free Radic Biol Med"},{"key":"4493_CR57","doi-asserted-by":"publisher","first-page":"334","DOI":"10.1097\/01.WCB.0000105800.49957.1E","volume":"24","author":"L Park","year":"2004","unstructured":"Park L, Anrather J, Forster C, Kazama K, Carlson GA, Iadecola C (2004) A\u03b2-induced vascular oxidative stress and attenuation of functional hyperemia in mouse somatosensory cortex. J Cereb Blood Flow Metab 24:334\u2013342","journal-title":"J Cereb Blood Flow Metab"},{"key":"4493_CR58","doi-asserted-by":"publisher","first-page":"35789","DOI":"10.1074\/jbc.C500238200","volume":"280","author":"BJ Tabner","year":"2005","unstructured":"Tabner BJ, El-Agnaf OM, Turnbull S, German MJ, Paleologou KE, Hayashi Y et al (2005) Hydrogen peroxide is generated during the very early stages of aggregation of the amyloid peptides implicated in Alzheimer disease and familial British dementia. J Biol Chem 280:35789\u201335792","journal-title":"J Biol Chem"},{"key":"4493_CR59","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1016\/j.jprot.2012.12.020","volume":"79","author":"NK Sharma","year":"2013","unstructured":"Sharma NK, Sethy NK, Bhargava K (2013) Comparative proteome analysis reveals differential regulation of glycolytic and antioxidant enzymes in cortex and hippocampus exposed to short-term hypobaric hypoxia. J Proteomics 79:277\u2013298","journal-title":"J Proteomics"},{"key":"4493_CR60","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1016\/j.nbd.2005.11.002","volume":"22","author":"DA Butterfield","year":"2006","unstructured":"Butterfield DA, Poon HF, St Clair D, Keller JN, Pierce WM, Klein JB et al (2006) Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer\u2019s disease. Neurobiol Dis 22:223\u2013232","journal-title":"Neurobiol Dis"},{"key":"4493_CR61","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/S0165-0173(00)00051-5","volume":"35","author":"A Law","year":"2001","unstructured":"Law A, Gauthier S, Quirion R (2001) Say NO to Alzheimer\u2019s disease: the putative links between nitric oxide and dementia of the Alzheimer\u2019s type. Brain Res Brain Res Rev 35:73\u201396","journal-title":"Brain Res Brain Res Rev"},{"key":"4493_CR62","doi-asserted-by":"publisher","first-page":"268","DOI":"10.1007\/s12035-014-8672-2","volume":"51","author":"QF Zhao","year":"2015","unstructured":"Zhao QF, Yu JT, Tan L (2015) S-Nitrosylation in Alzheimer\u2019s disease. Mol Neurobiol 51:268\u2013280","journal-title":"Mol Neurobiol"},{"key":"4493_CR63","doi-asserted-by":"publisher","first-page":"596","DOI":"10.1016\/j.neuron.2013.05.005","volume":"78","author":"T Nakamura","year":"2013","unstructured":"Nakamura T, Tu S, Akhtar MW, Sunico CR, Okamoto S, Lipton SA (2013) Aberrant protein S-nitrosylation in neurodegenerative diseases. Neuron 78:596\u2013614","journal-title":"Neuron"},{"key":"4493_CR64","doi-asserted-by":"publisher","DOI":"10.1088\/0022-3727\/45\/26\/263001","volume":"45","author":"DB Graves","year":"2012","unstructured":"Graves DB (2012) The emerging role of reactive oxygen and nitrogen species in redox biology and some implications for plasma applications to medicine and biology. J Phys D Appl Phys 45:263001","journal-title":"J Phys D Appl Phys"},{"key":"4493_CR65","doi-asserted-by":"publisher","first-page":"1969","DOI":"10.2967\/jnumed.109.062315","volume":"50","author":"YA Chung","year":"2009","unstructured":"Chung YA, Hyun O J, Kim JY, Kim KJ, Ahn KJ (2009) Hypoperfusion and ischemia in cerebral amyloid angiopathy documented by 99mTc-ECD brain perfusion SPECT. J Nucl Med 50:1969\u20131974","journal-title":"J Nucl Med"},{"key":"4493_CR66","doi-asserted-by":"publisher","first-page":"334","DOI":"10.1097\/00006123-199908000-00028","volume":"45","author":"AM Malek","year":"1999","unstructured":"Malek AM, Izumo S, Alper SL (1999) Modulation by pathophysiological stimuli of the shear stress-induced up-regulation of endothelial nitric oxide synthase expression in endothelial cells. Neurosurgery 45:334\u2013344 (discussion 344\u2013345)","journal-title":"Neurosurgery"},{"key":"4493_CR67","doi-asserted-by":"publisher","first-page":"755","DOI":"10.1038\/27351","volume":"395","author":"ME Calhoun","year":"1998","unstructured":"Calhoun ME, Wiederhold KH, Abramowski D, Phinney AL, Probst A, Sturchler-Pierrat C, Staufenbiel M, Sommer B, Jucker M (1998) Neuron loss in APP transgenic mice. Nature 395:755\u2013775","journal-title":"Nature"},{"key":"4493_CR68","doi-asserted-by":"publisher","first-page":"7013","DOI":"10.1074\/jbc.270.13.7013","volume":"270","author":"SA Gravina","year":"1995","unstructured":"Gravina SA, Ho L, Eckman CB, Long KE, Otvos L Jr, Younkin LH, Suzuki N, Younkin SG (1995) Amyloid \u03b2 protein (A\u03b2) in Alzheimer\u2019s disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at A\u03b240 or A\u03b242(43). J Biol Chem 270:7013\u20137016","journal-title":"J Biol Chem"},{"key":"4493_CR69","doi-asserted-by":"publisher","first-page":"2363","DOI":"10.1021\/acs.biomac.5b00603","volume":"16","author":"H Liu","year":"2015","unstructured":"Liu H, Ojha B, Morris C, Jiang M, Wojcikiewicz EP, Rao PP, Du D (2015) Positively charged chitosan and N-trimethyl chitosan inhibit A\u03b240 fibrillogenesis. Biomacromol 16:2363\u20132373","journal-title":"Biomacromol"},{"key":"4493_CR70","doi-asserted-by":"publisher","first-page":"352","DOI":"10.1016\/j.nbd.2009.05.024","volume":"35","author":"JL Tomic","year":"2009","unstructured":"Tomic JL, Pensalfini A, Head E, Glabe CG (2009) Soluble fibrillar oligomer levels are elevated in Alzheimer\u2019s disease brain and correlate with cognitive dysfunction. Neurobiol Dis 35:352\u2013358","journal-title":"Neurobiol Dis"},{"key":"4493_CR71","doi-asserted-by":"publisher","first-page":"796","DOI":"10.1007\/s12035-013-8562-z","volume":"49","author":"GS Jeon","year":"2014","unstructured":"Jeon GS, Nakamura T, Lee JS, Choi WJ, Ahn SW, Lee KW, Sung JJ, Lipton SA (2014) Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis. Mol Neurobiol 49:796\u2013807","journal-title":"Mol Neurobiol"}],"container-title":["Cellular and Molecular Life Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00018-022-04493-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00018-022-04493-x\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00018-022-04493-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,10,24]],"date-time":"2022-10-24T19:08:21Z","timestamp":1666638501000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00018-022-04493-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,8]]},"references-count":71,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2022,8]]}},"alternative-id":["4493"],"URL":"https:\/\/doi.org\/10.1007\/s00018-022-04493-x","relation":{},"ISSN":["1420-682X","1420-9071"],"issn-type":[{"value":"1420-682X","type":"print"},{"value":"1420-9071","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,8]]},"assertion":[{"value":"17 February 2022","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 June 2022","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 July 2022","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"2 August 2022","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors have no conflicts of interest to disclose.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"The Animal Care and Use Committee of Kumamoto University School of Medicine approved the protocols for the animal experiments.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"Not applicable.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}}],"article-number":"462"}}