{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T11:05:40Z","timestamp":1790679940271,"version":"4.1.0"},"reference-count":45,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2015,11,4]],"date-time":"2015-11-04T00:00:00Z","timestamp":1446595200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000864","name":"The Michael J. Fox Foundation for Parkinson\u2019s Research","doi-asserted-by":"crossref","award":["130-012\/2310"],"award-info":[{"award-number":["130-012\/2310"]}],"id":[{"id":"10.13039\/100000864","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Neurodegeneration"],"published-print":{"date-parts":[[2015,12]]},"DOI":"10.1186\/s13024-015-0055-2","type":"journal-article","created":{"date-parts":[[2015,11,4]],"date-time":"2015-11-04T15:51:56Z","timestamp":1446652316000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":45,"title":["Ceruloplasmin functional changes in Parkinson\u2019s disease-cerebrospinal fluid"],"prefix":"10.1186","volume":"10","author":[{"given":"Marco","family":"Barbariga","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Flavio","family":"Curnis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annapaola","family":"Andolfo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alan","family":"Zanardi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Massimo","family":"Lazzaro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonio","family":"Conti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giuseppe","family":"Magnani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria Antonietta","family":"Volont\u00e8","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura","family":"Ferrari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giancarlo","family":"Comi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angelo","family":"Corti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Massimo","family":"Alessio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2015,11,4]]},"reference":[{"key":"55_CR1","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1146\/annurev.nutr.22.012502.114457","volume":"22","author":"NE Hellman","year":"2002","unstructured":"Hellman NE, Gitlin JD. Ceruloplasmin metabolism and function. Annu Rev Nutr. 2002;22:439\u201358.","journal-title":"Annu Rev Nutr"},{"key":"55_CR2","doi-asserted-by":"publisher","first-page":"2823","DOI":"10.1038\/sj.emboj.7601735","volume":"26","author":"I Domenico De","year":"2007","unstructured":"De Domenico I, Ward DM, di Patti MC, Jeong SY, David S, Musci G, et al. Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin. EMBO J. 2007;26:2823\u201331.","journal-title":"EMBO J"},{"key":"55_CR3","doi-asserted-by":"publisher","first-page":"18568","DOI":"10.1523\/JNEUROSCI.3768-11.2011","volume":"31","author":"S Olivieri","year":"2011","unstructured":"Olivieri S, Conti A, Iannaccone S, Cannistraci CV, Campanella A, Barbariga M, et al. Ceruloplasmin oxidation, a feature of Parkinson\u2019s disease CSF, inhibits ferroxidase activity and promotes cellular iron retention. J Neurosci. 2011;31:18568\u201377.","journal-title":"J Neurosci"},{"key":"55_CR4","doi-asserted-by":"publisher","first-page":"1717","DOI":"10.1007\/s11064-008-9610-3","volume":"33","author":"MC Boll","year":"2008","unstructured":"Boll MC, Alcaraz-Zubeldia M, Montes S, Rios C. Free copper, ferroxidase and SOD1 activities, lipid peroxidation and NO(x) content in the CSF. A different marker profile in four neurodegenerative diseases. Neurochem Res. 2008;33:1717\u201323.","journal-title":"Neurochem Res"},{"key":"55_CR5","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1016\/S0304-3940(99)00221-9","volume":"265","author":"MC Boll","year":"1999","unstructured":"Boll MC, Sotelo J, Otero E, Alcaraz-Zubeldia M, Rios C. Reduced ferroxidase activity in the cerebrospinal fluid from patients with Parkinson\u2019s disease. Neurosci Lett. 1999;265:155\u20138.","journal-title":"Neurosci Lett"},{"key":"55_CR6","doi-asserted-by":"publisher","first-page":"1277","DOI":"10.1042\/BST0361277","volume":"36","author":"SJ Texel","year":"2008","unstructured":"Texel SJ, Xu X, Harris ZL. Ceruloplasmin in neurodegenerative diseases. Biochem Soc Trans. 2008;36:1277\u201381.","journal-title":"Biochem Soc Trans"},{"key":"55_CR7","doi-asserted-by":"publisher","first-page":"554","DOI":"10.1002\/ana.23817","volume":"73","author":"S Ayton","year":"2013","unstructured":"Ayton S, Lei P, Duce JA, Wong BX, Sedjahtera A, Adlard PA, et al. Ceruloplasmin dysfunction and therapeutic potential for parkinson disease. Ann Neurol. 2013;73:554\u201359.","journal-title":"Ann Neurol"},{"key":"55_CR8","doi-asserted-by":"crossref","first-page":"6578","DOI":"10.1523\/JNEUROSCI.22-15-06578.2002","volume":"22","author":"BN Patel","year":"2002","unstructured":"Patel BN, Dunn RJ, Jeong SY, Zhu Q, Julien JP, David S. Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury. J Neurosci. 2002;22:6578\u201386.","journal-title":"J Neurosci"},{"key":"55_CR9","doi-asserted-by":"crossref","first-page":"972S","DOI":"10.1093\/ajcn\/67.5.972S","volume":"67","author":"ZL Harris","year":"1998","unstructured":"Harris ZL, Klomp LW, Gitlin JD. Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis. Am J Clin Nutr. 1998;67:972S\u20137S.","journal-title":"Am J Clin Nutr"},{"key":"55_CR10","doi-asserted-by":"publisher","first-page":"200","DOI":"10.1159\/000148691","volume":"60","author":"A McNeill","year":"2008","unstructured":"McNeill A, Pandolfo M, Kuhn J, Shang H, Miyajima H. The neurological presentation of ceruloplasmin gene mutations. Eur Neurol. 2008;60:200\u20135.","journal-title":"Eur Neurol"},{"key":"55_CR11","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1186\/1750-1326-9-27","volume":"9","author":"S Ayton","year":"2014","unstructured":"Ayton S, Lei P, Adlard PA, Volitakis I, Cherny RA, Bush AI, et al. Iron accumulation confers neurotoxicity to a vulnerable population of nigral neurons: implications for Parkinson\u2019s disease. Mol Neurodegener. 2014;9:27.","journal-title":"Mol Neurodegener"},{"key":"55_CR12","doi-asserted-by":"publisher","first-page":"73","DOI":"10.3109\/10715762.2010.512040","volume":"45","author":"S Grimm","year":"2011","unstructured":"Grimm S, Hoehn A, Davies KJ, Grune T. Protein oxidative modifications in the ageing brain: consequence for the onset of neurodegenerative disease. Free Radic Res. 2011;45:73\u201388.","journal-title":"Free Radic Res"},{"key":"55_CR13","doi-asserted-by":"publisher","first-page":"863","DOI":"10.1038\/nrn1537","volume":"5","author":"L Zecca","year":"2004","unstructured":"Zecca L, Youdim MB, Riederer P, Connor JR, Crichton RR. Iron, brain ageing and neurodegenerative disorders. Nat Rev Neurosci. 2004;5:863\u201373.","journal-title":"Nat Rev Neurosci"},{"key":"55_CR14","doi-asserted-by":"publisher","first-page":"3736","DOI":"10.1074\/jbc.M113.520981","volume":"289","author":"M Barbariga","year":"2014","unstructured":"Barbariga M, Curnis F, Spitaleri A, Andolfo A, Zucchelli C, Lazzaro M, et al. Oxidation-induced structural changes of ceruloplasmin foster NGR-motifs deamidation that promote integrin binding and signalling. J Biol Chem. 2014;289:3736\u201348.","journal-title":"J Biol Chem"},{"key":"55_CR15","doi-asserted-by":"publisher","first-page":"36466","DOI":"10.1074\/jbc.M604812200","volume":"281","author":"F Curnis","year":"2006","unstructured":"Curnis F, Longhi R, Crippa L, Cattaneo A, Dondossola E, Bachi A, et al. Spontaneous formation of L-isoaspartate and gain of function in fibronectin. J Biol Chem. 2006;281:36466\u201376.","journal-title":"J Biol Chem"},{"key":"55_CR16","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1242\/jcs.077172","volume":"124","author":"A Corti","year":"2011","unstructured":"Corti A, Curnis F. Isoaspartate-dependent molecular switches for integrin-ligand recognition. J Cell Sci. 2011;124:515\u201322.","journal-title":"J Cell Sci"},{"key":"55_CR17","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1016\/B978-141602908-3.50013-3","volume-title":"Cerebrospinal fluid in clinical practice","author":"DN Irani","year":"2009","unstructured":"Irani DN. Properties and composition of normal cerebrospinal fluid. In: Irani DN, editor. Cerebrospinal fluid in clinical practice. Philadelphia: Saunders-Elsevier; 2009. p. 69\u201392."},{"key":"55_CR18","doi-asserted-by":"crossref","first-page":"13388","DOI":"10.1016\/S0021-9258(19)38663-6","volume":"268","author":"G Musci","year":"1993","unstructured":"Musci G, di Patti MC B, Fagiolo U, Calabrese L. Age-related changes in human ceruloplasmin. Evidence for oxidative modifications. J Biol Chem. 1993;268:13388\u201395.","journal-title":"J Biol Chem"},{"key":"55_CR19","doi-asserted-by":"crossref","unstructured":"Weintraub SJ, Deverman BE. Chronoregulation by asparagine deamidation. Sci STKE. 2007;409:re7.","DOI":"10.1126\/stke.4092007re7"},{"key":"55_CR20","doi-asserted-by":"publisher","first-page":"426","DOI":"10.1111\/j.1399-3011.2004.00151.x","volume":"63","author":"NE Robinson","year":"2004","unstructured":"Robinson NE, Robinson ZW, Robinson BR, Robinson AL, Robinson JA, Robinson ML, et al. Structure-dependent nonenzymatic deamidation of glutaminyl and asparaginyl pentapeptides. J Pept Res. 2004;63:426\u201336.","journal-title":"J Pept Res"},{"key":"55_CR21","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1016\/j.parkreldis.2012.07.002","volume":"19","author":"S Iannaccone","year":"2013","unstructured":"Iannaccone S, Cerami C, Alessio M, Garibotto V, Panzacchi A, Olivieri S, et al. In vivo microglia activation in very early dementia with Lewy bodies, comparison with Parkinson's disease. Parkinsonism Relat Disord. 2013;19:47\u201352.","journal-title":"Parkinsonism Relat Disord"},{"key":"55_CR22","doi-asserted-by":"publisher","first-page":"2032","DOI":"10.1046\/j.1432-1033.2002.02838.x","volume":"269","author":"D Ingrosso","year":"2002","unstructured":"Ingrosso D, Cimmino A, D'Angelo S, Alfinito F, Zappia V, Galletti P. Protein methylation as a marker of aspartate damage in glucose-6-phosphate dehydrogenase-deficient erythrocytes: role of oxidative stress. Eur J Biochem. 2002;269:2032\u20139.","journal-title":"Eur J Biochem"},{"key":"55_CR23","doi-asserted-by":"crossref","first-page":"17047","DOI":"10.1016\/S0021-9258(18)41890-X","volume":"267","author":"M Hasegawa","year":"1992","unstructured":"Hasegawa M, Morishima-Kawashima M, Takio K, Suzuki M, Titani K, Ihara Y. Protein sequence and mass spectrometric analyses of tau in the Alzheimer\u2019s disease brain. J Biol Chem. 1992;267:17047\u201354.","journal-title":"J Biol Chem"},{"key":"55_CR24","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1006\/abbi.2000.1955","volume":"381","author":"T Shimizu","year":"2000","unstructured":"Shimizu T, Watanabe A, Ogawara M, Mori H, Shirasawa T. Isoaspartate formation and neurodegeneration in Alzheimer\u2019s disease. Arch Biochem Biophys. 2000;381:225\u201334.","journal-title":"Arch Biochem Biophys"},{"key":"55_CR25","doi-asserted-by":"publisher","first-page":"7368","DOI":"10.1074\/jbc.274.11.7368","volume":"274","author":"A Watanabe","year":"1999","unstructured":"Watanabe A, Takio K, Ihara Y. Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau. J Biol Chem. 1999;274:7368\u201378.","journal-title":"J Biol Chem"},{"key":"55_CR26","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1523\/JNEUROSCI.23-02-00493.2003","volume":"23","author":"EA Grace","year":"2003","unstructured":"Grace EA, Busciglio J. Aberrant activation of focal adhesion proteins mediates fibrillar amyloid beta-induced neuronal dystrophy. J Neurosci. 2003;23:493\u2013502.","journal-title":"J Neurosci"},{"key":"55_CR27","first-page":"438","volume":"2007","author":"J Caltagarone","year":"1772","unstructured":"Caltagarone J, Jing Z, Bowser R. Focal adhesions regulate Abeta signaling and cell death in Alzheimer\u2019s disease. Biochim Biophys Acta. 1772;2007:438\u201345.","journal-title":"Biochim Biophys Acta"},{"key":"55_CR28","doi-asserted-by":"publisher","first-page":"226","DOI":"10.1016\/j.neurobiolaging.2005.12.002","volume":"28","author":"S Wright","year":"2007","unstructured":"Wright S, Malinin NL, Powell KA, Yednock T, Rydel RE, Griswold-Prenner I. Alpha2beta1 and alphaVbeta1 integrin signaling pathways mediate amyloid-beta-induced neurotoxicity. Neurobiol Aging. 2007;28:226\u201337.","journal-title":"Neurobiol Aging"},{"key":"55_CR29","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. 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. 2005;280:35789\u201392.","journal-title":"J Biol Chem"},{"key":"55_CR30","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1016\/j.redox.2012.12.004","volume":"1","author":"RH Gottfredsen","year":"2013","unstructured":"Gottfredsen RH, Larsen UG, Enghild JJ, Petersen SV. Hydrogen peroxide induce modifications of human extracellular superoxide dismutase that results in enzyme inhibition. Redox biology. 2013;1:24\u201331.","journal-title":"Redox biology"},{"key":"55_CR31","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0061442","volume":"8","author":"V Vigneswara","year":"2013","unstructured":"Vigneswara V, Cass S, Wayne D, Bolt EL, Ray DE, Carter WG. Molecular ageing of alpha- and Beta-synucleins: protein damage and repair mechanisms. PLoS One. 2013;8, e61442.","journal-title":"PLoS One"},{"key":"55_CR32","doi-asserted-by":"publisher","first-page":"1766","DOI":"10.1212\/WNL.0b013e3181fd613b","volume":"75","author":"T Tokuda","year":"2010","unstructured":"Tokuda T, Qureshi MM, Ardah MT, Varghese S, Shehab SA, Kasai T, et al. Detection of elevated levels of alpha-synuclein oligomers in CSF from patients with Parkinson disease. Neurology. 2010;75:1766\u201372.","journal-title":"Neurology"},{"key":"55_CR33","doi-asserted-by":"publisher","first-page":"215","DOI":"10.3988\/jcn.2011.7.4.215","volume":"7","author":"MJ Park","year":"2011","unstructured":"Park MJ, Cheon SM, Bae HR, Kim SH, Kim JW. Elevated levels of alpha-synuclein oligomer in the cerebrospinal fluid of drug-naive patients with Parkinson\u2019s disease. J Clin Neurol. 2011;7:215\u201322.","journal-title":"J Clin Neurol"},{"key":"55_CR34","doi-asserted-by":"publisher","first-page":"1188","DOI":"10.1039\/c1ib00018g","volume":"3","author":"MR Sierks","year":"2011","unstructured":"Sierks MR, Chatterjee G, McGraw C, Kasturirangan S, Schulz P, Prasad S. CSF levels of oligomeric alpha-synuclein and beta-amyloid as biomarkers for neurodegenerative disease. Integr Biol (Camb). 2011;3:1188\u201396.","journal-title":"Integr Biol (Camb)"},{"key":"55_CR35","doi-asserted-by":"publisher","first-page":"1255555","DOI":"10.1126\/science.1255555","volume":"349","author":"M Goedert","year":"2015","unstructured":"Goedert M. NEURODEGENERATION. Alzheimer\u2019s and Parkinson\u2019s diseases: the prion concept in relation to assembled abeta, tau, and alpha-synuclein. Science. 2015;349:1255555.","journal-title":"Science"},{"key":"55_CR36","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1016\/j.freeradbiomed.2015.05.025","volume":"86","author":"S Dev","year":"2015","unstructured":"Dev S, Kumari S, Singh N, Kumar Bal S, Seth P, Mukhopadhyay CK. Role of extracellular hydrogen peroxide in regulation of iron homeostasis genes in neuronal cells: implication in iron accumulation. Free Radic Biol Med. 2015;86:78\u201389.","journal-title":"Free Radic Biol Med"},{"key":"55_CR37","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1016\/j.redox.2014.02.006","volume":"2","author":"HS Marinho","year":"2014","unstructured":"Marinho HS, Real C, Cyrne L, Soares H, Antunes F. Hydrogen peroxide sensing, signaling and regulation of transcription factors. Redox biology. 2014;2:535\u201362.","journal-title":"Redox biology"},{"key":"55_CR38","doi-asserted-by":"publisher","first-page":"3130","DOI":"10.1038\/emboj.2013.233","volume":"32","author":"KK Patel","year":"2013","unstructured":"Patel KK, Miyoshi H, Beatty WL, Head RD, Malvin NP, Cadwell K, et al. Autophagy proteins control goblet cell function by potentiating reactive oxygen species production. EMBO J. 2013;32:3130\u201344.","journal-title":"EMBO J"},{"key":"55_CR39","doi-asserted-by":"publisher","first-page":"304","DOI":"10.1016\/j.redox.2013.04.005","volume":"1","author":"CL Quinlan","year":"2013","unstructured":"Quinlan CL, Perevoshchikova IV, Hey-Mogensen M, Orr AL, Brand MD. Sites of reactive oxygen species generation by mitochondria oxidizing different substrates. Redox biology. 2013;1:304\u201312.","journal-title":"Redox biology"},{"key":"55_CR40","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1111\/ene.12022","volume":"20","author":"A Berardelli","year":"2013","unstructured":"Berardelli A, Wenning GK, Antonini A, Berg D, Bloem BR, Bonifati V, et al. EFNS\/MDS-ES\/ENS recommendations for the diagnosis of Parkinson\u2019s disease. Eur J Neurol. 2013;20:16\u201334.","journal-title":"Eur J Neurol"},{"key":"55_CR41","unstructured":"Thomas PK, Dyck P. Peripheral Neuropathy. 4th ed. Saunders; 2005."},{"key":"55_CR42","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1136\/jcp.49.3.249","volume":"49","author":"JG Cunniffe","year":"1996","unstructured":"Cunniffe JG, Whitby-Strevens S, Wilcox MH. Effect of pH changes in cerebrospinal fluid specimens on bacterial survival and antigen test results. J Clin Pathol. 1996;49:249\u201353.","journal-title":"J Clin Pathol"},{"key":"55_CR43","doi-asserted-by":"publisher","first-page":"9114","DOI":"10.1074\/jbc.M109.044297","volume":"285","author":"F Curnis","year":"2010","unstructured":"Curnis F, Cattaneo A, Longhi R, Sacchi A, Gasparri AM, Pastorino F, et al. Critical role of flanking residues in NGR-to-isoDGR transition and CD13\/integrin receptor switching. J Biol Chem. 2010;285:9114\u201323.","journal-title":"J Biol Chem"},{"key":"55_CR44","doi-asserted-by":"publisher","first-page":"966","DOI":"10.1093\/bioinformatics\/btq054","volume":"26","author":"B MacLean","year":"2010","unstructured":"MacLean B, Tomazela DM, Shulman N, Chambers M, Finney GL, Frewen B, et al. Skyline: an open source document editor for creating and analyzing targeted proteomics experiments. Bioinformatics. 2010;26:966\u20138.","journal-title":"Bioinformatics"},{"key":"55_CR45","doi-asserted-by":"publisher","first-page":"3467","DOI":"10.1021\/pr201240a","volume":"11","author":"SD Sherrod","year":"2012","unstructured":"Sherrod SD, Myers MV, Li M, Myers JS, Carpenter KL, Maclean B, et al. Label-free quantitation of protein modifications by pseudo selected reaction monitoring with internal reference peptides. J Proteome Res. 2012;11:3467\u201379.","journal-title":"J Proteome Res"}],"container-title":["Molecular Neurodegeneration"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1186\/s13024-015-0055-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1186\/s13024-015-0055-2\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1186\/s13024-015-0055-2","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1186\/s13024-015-0055-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,5,25]],"date-time":"2022-05-25T04:59:46Z","timestamp":1653454786000},"score":1,"resource":{"primary":{"URL":"https:\/\/molecularneurodegeneration.biomedcentral.com\/articles\/10.1186\/s13024-015-0055-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,11,4]]},"references-count":45,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2015,12]]}},"alternative-id":["55"],"URL":"https:\/\/doi.org\/10.1186\/s13024-015-0055-2","relation":{},"ISSN":["1750-1326"],"issn-type":[{"value":"1750-1326","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,11,4]]},"assertion":[{"value":"28 August 2015","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 October 2015","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 November 2015","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}],"article-number":"59"}}