{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T07:50:51Z","timestamp":1793260251831,"version":"4.5.0"},"reference-count":87,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2018,4,27]],"date-time":"2018-04-27T00:00:00Z","timestamp":1524787200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/academic.oup.com\/journals\/pages\/about_us\/legal\/notices"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2018,6,1]]},"DOI":"10.1093\/jnen\/nly024","type":"journal-article","created":{"date-parts":[[2018,4,27]],"date-time":"2018-04-27T10:24:39Z","timestamp":1524824679000},"page":"443-453","source":"Crossref","is-referenced-by-count":155,"title":["Increased Oxidative Stress Exacerbates \u03b1-Synuclein Aggregation In Vivo"],"prefix":"10.1093","volume":"77","author":[{"given":"Owen","family":"Scudamore","sequence":"first","affiliation":[{"name":"CNS Disease Research, Boehringer Ingelheim GmbH & Co. KG, Biberach an der Riss, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Ciossek","sequence":"additional","affiliation":[{"name":"CNS Disease Research, Boehringer Ingelheim GmbH & Co. KG, Biberach an der Riss, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2018,4,27]]},"reference":[{"key":"key\n\t\t\t\t20180516101549_nly024-B1","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1126\/science.276.5321.2045","article-title":"Mutation in the alpha-synuclein gene identified in families with Parkinson\u2019s disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"key\n\t\t\t\t20180516101549_nly024-B2","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1038\/ng0298-106","article-title":"Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson\u2019s disease","volume":"18","author":"Kruger","year":"1998","journal-title":"Nat Genet"},{"key":"key\n\t\t\t\t20180516101549_nly024-B3","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1002\/ana.10795","article-title":"The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia","volume":"55","author":"Zarranz","year":"2004","journal-title":"Ann Neurol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B4","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1016\/S0140-6736(04)17103-1","article-title":"Alpha-synuclein locus duplication as a cause of familial Parkinson\u2019s disease","volume":"364","author":"Chartier-Harlin","year":"2004","journal-title":"Lancet"},{"key":"key\n\t\t\t\t20180516101549_nly024-B5","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1016\/S0140-6736(04)17104-3","article-title":"Causal relation between alpha-synuclein gene duplication and familial Parkinson\u2019s disease","volume":"364","author":"Ibanez","year":"2004","journal-title":"Lancet"},{"key":"key\n\t\t\t\t20180516101549_nly024-B6","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1002\/ana.20753","article-title":"Clinical heterogeneity of alpha-synuclein gene duplication in Parkinson\u2019s disease","volume":"59","author":"Nishioka","year":"2006","journal-title":"Ann Neurol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B7","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1212\/01.wnl.0000254458.17630.c5","article-title":"Phenotypic variation in a large Swedish pedigree due to SNCA duplication and triplication","volume":"68","author":"Fuchs","year":"2007","journal-title":"Neurology"},{"key":"key\n\t\t\t\t20180516101549_nly024-B8","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1126\/science.1090278","article-title":"alpha-Synuclein locus triplication causes Parkinson\u2019s disease","volume":"302","author":"Singleton","year":"2003","journal-title":"Science"},{"key":"key\n\t\t\t\t20180516101549_nly024-B9","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1002\/ana.10846","article-title":"Comparison of kindreds with Parkinsonism and alpha-synuclein genomic multiplications","volume":"55","author":"Farrer","year":"2004","journal-title":"Ann Neurol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B10","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1038\/77060","article-title":"Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase","volume":"25","author":"Shimura","year":"2000","journal-title":"Nat Genet"},{"key":"key\n\t\t\t\t20180516101549_nly024-B11","doi-asserted-by":"crossref","first-page":"3477","DOI":"10.1093\/hmg\/ddi377","article-title":"Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive Parkinsonism","volume":"14","author":"Silvestri","year":"2005","journal-title":"Hum Mol Genet"},{"key":"key\n\t\t\t\t20180516101549_nly024-B12","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1038\/sj.embor.7400074","article-title":"DJ-1 has a role in antioxidative stress to prevent cell death","volume":"5","author":"Taira","year":"2004","journal-title":"EMBO Rep"},{"key":"key\n\t\t\t\t20180516101549_nly024-B13","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1523\/JNEUROSCI.4308-05.2006","article-title":"Parkinson\u2019s disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death","volume":"26","author":"Martin","year":"2006","journal-title":"J Neurosci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B14","doi-asserted-by":"crossref","first-page":"2377","DOI":"10.1093\/hmg\/ddm083","article-title":"Mono- and double-mutant mouse models of Parkinson\u2019s disease display severe mitochondrial damage","volume":"16","author":"Stichel","year":"2007","journal-title":"Hum Mol Genet"},{"key":"key\n\t\t\t\t20180516101549_nly024-B15","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1016\/j.neurobiolaging.2005.04.010","article-title":"Increased sensitivity to MPTP in human alpha-synuclein A30P transgenic mice","volume":"27","author":"Nieto","year":"2006","journal-title":"Neurobiol Aging"},{"key":"key\n\t\t\t\t20180516101549_nly024-B16","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/S0014-4886(03)00342-X","article-title":"Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP","volume":"186","author":"Song","year":"2004","journal-title":"Exp Neurol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B17","doi-asserted-by":"crossref","first-page":"14524","DOI":"10.1073\/pnas.172514599","article-title":"Resistance of alpha-synuclein null mice to the Parkinsonian neurotoxin MPTP","volume":"99","author":"Dauer","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180516101549_nly024-B18","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/j.neuro.2004.05.002","article-title":"Mice lacking alpha-synuclein have an attenuated loss of striatal dopamine following prolonged chronic MPTP administration","volume":"25","author":"Drolet","year":"2004","journal-title":"Neurotoxicology"},{"key":"key\n\t\t\t\t20180516101549_nly024-B19","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1073\/pnas.0409713102","article-title":"Parkinson-like syndrome induced by continuous MPTP infusion: convergent roles of the ubiquitin-proteasome system and alpha-synuclein","volume":"102","author":"Fornai","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180516101549_nly024-B20","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1016\/j.nbd.2005.12.003","article-title":"Intersecting pathways to neurodegeneration in Parkinson\u2019s disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system","volume":"22","author":"Betarbet","year":"2006","journal-title":"Neurobiol Dis"},{"key":"key\n\t\t\t\t20180516101549_nly024-B21","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1097\/00001756-199903170-00011","article-title":"Oxidative stress induces amyloid-like aggregate formation of NACP\/alpha-synuclein in vitro","volume":"10","author":"Hashimoto","year":"1999","journal-title":"Neuroreport"},{"key":"key\n\t\t\t\t20180516101549_nly024-B22","doi-asserted-by":"crossref","first-page":"18344","DOI":"10.1074\/jbc.M000206200","article-title":"Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies","volume":"275","author":"Souza","year":"2000","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B23","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1046\/j.1471-4159.2002.00821.x","article-title":"Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures","volume":"81","author":"McNaught","year":"2002","journal-title":"J Neurochem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B24","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1097\/00001756-200208070-00018","article-title":"Proteasome inhibition causes nigral degeneration with inclusion bodies in rats","volume":"13","author":"McNaught","year":"2002","journal-title":"Neuroreport"},{"key":"key\n\t\t\t\t20180516101549_nly024-B25","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1023\/A:1027335217774","article-title":"The role of reactive oxygen species in mitochondrial permeability transition","volume":"17","author":"Vercesi","year":"1997","journal-title":"Biosci Rep"},{"key":"key\n\t\t\t\t20180516101549_nly024-B26","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1111\/j.1749-6632.2002.tb02094.x","article-title":"Role of mitochondria in oxidative stress and aging","volume":"959","author":"Lenaz","year":"2002","journal-title":"Ann N Y Acad Sci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B27","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1042\/bj1560435","article-title":"Role of ubiquinone in the mitochondrial generation of hydrogen peroxide","volume":"156","author":"Boveris","year":"1976","journal-title":"Biochem J"},{"key":"key\n\t\t\t\t20180516101549_nly024-B28","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-9861(77)90035-2","article-title":"Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria","volume":"180","author":"Cadenas","year":"1977","journal-title":"Arch Biochem Biophys"},{"key":"key\n\t\t\t\t20180516101549_nly024-B29","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1042\/bj1910421","article-title":"Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria","volume":"191","author":"Turrens","year":"1980","journal-title":"Biochem J"},{"key":"key\n\t\t\t\t20180516101549_nly024-B30","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1016\/S0896-6273(03)00568-3","article-title":"Parkinson\u2019s disease: mechanisms and models","volume":"39","author":"Dauer","year":"2003","journal-title":"Neuron"},{"key":"key\n\t\t\t\t20180516101549_nly024-B31","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1146\/annurev.bi.64.070195.000525","article-title":"Superoxide radical and superoxide dismutases","volume":"64","author":"Fridovich","year":"1995","journal-title":"Annu Rev Biochem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B32","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1159\/000111433","article-title":"Modulation of oxygen-radical-scavenging enzymes by oxidative stress in primary cultures of rat astroglial cells","volume":"18","author":"Pinteaux","year":"1996","journal-title":"Dev Neurosci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B33","first-page":"L150","article-title":"Redox regulation of manganese superoxide dismutase","volume":"271","author":"Warner","year":"1996","journal-title":"Am J Physiol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B34","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/0306-4522(94)90234-8","article-title":"Distribution of manganese-dependent superoxide dismutase in the human brain","volume":"61","author":"Zhang","year":"1994","journal-title":"Neuroscience"},{"key":"key\n\t\t\t\t20180516101549_nly024-B35","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1016\/S0891-5849(01)00694-3","article-title":"Genetic modification of prenatal lethality and dilated cardiomyopathy in Mn superoxide dismutase mutant mice","volume":"31","author":"Huang","year":"2001","journal-title":"Free Radic Biol Med"},{"key":"key\n\t\t\t\t20180516101549_nly024-B36","doi-asserted-by":"crossref","first-page":"2278","DOI":"10.1073\/pnas.051627098","article-title":"Increased mitochondrial oxidative stress in the Sod2 (+\/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis","volume":"98","author":"Kokoszka","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180516101549_nly024-B37","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1152\/physiolgenomics.00122.2003","article-title":"Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging","volume":"16","author":"Van Remmen","year":"2003","journal-title":"Physiol Genomics"},{"key":"key\n\t\t\t\t20180516101549_nly024-B38","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1038\/ng1295-376","article-title":"Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase","volume":"11","author":"Li","year":"1995","journal-title":"Nat Genet"},{"key":"key\n\t\t\t\t20180516101549_nly024-B39","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1006\/abbi.1998.1060","article-title":"Characterization of the antioxidant status of the heterozygous manganese superoxide dismutase knockout mouse","volume":"363","author":"Van Remmen","year":"1999","journal-title":"Arch Biochem Biophys"},{"key":"key\n\t\t\t\t20180516101549_nly024-B40","doi-asserted-by":"crossref","first-page":"9782","DOI":"10.1073\/pnas.93.18.9782","article-title":"Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice","volume":"93","author":"Lebovitz","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180516101549_nly024-B41","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1172\/JCI200215777","article-title":"Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies","volume":"110","author":"Neumann","year":"2002","journal-title":"J Clin Invest"},{"key":"key\n\t\t\t\t20180516101549_nly024-B42","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1038\/nn.2928","article-title":"Scale: a chemical approach for fluorescence imaging and reconstruction of transparent mouse brain","volume":"14","author":"Hama","year":"2011","journal-title":"Nat Neurosci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B43","doi-asserted-by":"crossref","first-page":"3942","DOI":"10.1523\/JNEUROSCI.4965-05.2006","article-title":"Pathological changes in dopaminergic nerve cells of the substantia nigra and olfactory bulb in mice transgenic for truncated human alpha-synuclein(1-120): implications for Lewy body disorders","volume":"26","author":"Tofaris","year":"2006","journal-title":"J Neurosci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B44","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1038\/ncb748","article-title":"alpha-Synuclein is phosphorylated in synucleinopathy lesions","volume":"4","author":"Fujiwara","year":"2002","journal-title":"Nat Cell Biol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B45","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1016\/j.neurobiolaging.2006.06.013","article-title":"Age-dependent cognitive decline and amygdala pathology in alpha-synuclein transgenic mice","volume":"28","author":"Freichel","year":"2007","journal-title":"Neurobiol Aging"},{"key":"key\n\t\t\t\t20180516101549_nly024-B46","doi-asserted-by":"crossref","first-page":"6365","DOI":"10.1523\/JNEUROSCI.20-17-06365.2000","article-title":"Subcellular localization of wild-type and Parkinson\u2019s disease-associated mutant alpha-synuclein in human and transgenic mouse brain","volume":"20","author":"Kahle","year":"2000","journal-title":"J Neurosci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B47","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1016\/j.neuroscience.2009.03.002","article-title":"Nuclear and neuritic distribution of serine-129 phosphorylated alpha-synuclein in transgenic mice","volume":"160","author":"Schell","year":"2009","journal-title":"Neuroscience"},{"key":"key\n\t\t\t\t20180516101549_nly024-B48","doi-asserted-by":"crossref","first-page":"S94","DOI":"10.1002\/ana.410320716","article-title":"Alterations in levels of iron, ferritin, and other trace metals in neurodegenerative diseases affecting the basal ganglia. The Royal Kings and Queens Parkinson\u2019s Disease Research Group","volume":"32(Suppl)","author":"Dexter","year":"1992","journal-title":"Ann Neurol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B49","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/S0022-510X(98)00095-1","article-title":"Mitochondrial function, GSH and iron in neurodegeneration and Lewy body diseases","volume":"158","author":"Gu","year":"1998","journal-title":"J Neurol Sci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B50","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1002\/ana.410360612","article-title":"Complex I, iron, and ferritin in Parkinson\u2019s disease substantia nigra","volume":"36","author":"Mann","year":"1994","journal-title":"Ann Neurol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B51","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1111\/j.1749-6632.1996.tb39064.x","article-title":"Oxidative stress and Parkinson\u2019s disease","volume":"786","author":"Owen","year":"1996","journal-title":"Ann N Y Acad Sci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B52","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1365-2990.1995.tb01022.x","article-title":"Oxidative stress in Parkinson\u2019s disease","volume":"21","author":"Schapira","year":"1995","journal-title":"Neuropathol Appl Neurobiol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B53","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1016\/S0140-6736(89)92366-0","article-title":"Mitochondrial complex I deficiency in Parkinson\u2019s disease","volume":"1","author":"Schapira","year":"1989","journal-title":"Lancet"},{"key":"key\n\t\t\t\t20180516101549_nly024-B54","doi-asserted-by":"crossref","first-page":"5167","DOI":"10.1523\/JNEUROSCI.0482-06.2006","article-title":"Reduction in mitochondrial superoxide dismutase modulates Alzheimer\u2019s disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice","volume":"26","author":"Esposito","year":"2006","journal-title":"J Neurosci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B55","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1111\/j.1471-4159.2004.02455.x","article-title":"Increased plaque burden in brains of APP mutant MnSOD heterozygous knockout mice","volume":"89","author":"Li","year":"2004","journal-title":"J Neurochem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B56","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1002\/mus.21049","article-title":"MnSOD deficiency has a differential effect on disease progression in two different ALS mutant mouse models","volume":"38","author":"Muller","year":"2008","journal-title":"Muscle Nerve"},{"key":"key\n\t\t\t\t20180516101549_nly024-B57","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1074\/jbc.275.1.390","article-title":"Constitutive phosphorylation of the Parkinson\u2019s disease associated alpha-synuclein","volume":"275","author":"Okochi","year":"2000","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B58","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1073\/pnas.97.2.571","article-title":"Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson\u2019s disease: implications for pathogenesis and therapy","volume":"97","author":"Conway","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180516101549_nly024-B59","doi-asserted-by":"crossref","first-page":"2162","DOI":"10.1073\/pnas.0406976102","article-title":"Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson\u2019s disease-linked mutations","volume":"102","author":"Li","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180516101549_nly024-B60","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1093\/glycob\/cwj014","article-title":"Agrin binds alpha-synuclein and modulates alpha-synuclein fibrillation","volume":"15","author":"Liu","year":"2005","journal-title":"Glycobiology"},{"key":"key\n\t\t\t\t20180516101549_nly024-B61","doi-asserted-by":"crossref","first-page":"29739","DOI":"10.1074\/jbc.M600933200","article-title":"Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease","volume":"281","author":"Anderson","year":"2006","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B62","doi-asserted-by":"crossref","first-page":"8530","DOI":"10.1021\/bi027363r","article-title":"Role of alpha-synuclein carboxy-terminus on fibril formation in vitro","volume":"42","author":"Murray","year":"2003","journal-title":"Biochemistry"},{"key":"key\n\t\t\t\t20180516101549_nly024-B63","doi-asserted-by":"crossref","first-page":"4897","DOI":"10.1073\/pnas.97.9.4897","article-title":"Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation","volume":"97","author":"Serpell","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180516101549_nly024-B64","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1016\/j.jmb.2008.03.017","article-title":"Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation","volume":"378","author":"Wu","year":"2008","journal-title":"J Mol Biol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B65","doi-asserted-by":"crossref","first-page":"30649","DOI":"10.1074\/jbc.C500288200","article-title":"Familial mutants of alpha-synuclein with increased neurotoxicity have a destabilized conformation","volume":"280","author":"Bertoncini","year":"2005","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B66","doi-asserted-by":"crossref","first-page":"22670","DOI":"10.1074\/jbc.M501508200","article-title":"A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: implications for pathogenesis of Parkinson disease","volume":"280","author":"Liu","year":"2005","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B67","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1111\/j.1460-9568.2010.07284.x","article-title":"Co-expression of C-terminal truncated alpha-synuclein enhances full-length alpha-synuclein-induced pathology","volume":"32","author":"Ulusoy","year":"2010","journal-title":"Eur J Neurosci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B68","doi-asserted-by":"crossref","first-page":"3338","DOI":"10.1523\/JNEUROSCI.0285-07.2007","article-title":"Aggregated alpha-synuclein mediates dopaminergic neurotoxicity in vivo","volume":"27","author":"Periquet","year":"2007","journal-title":"J Neurosci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B69","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1016\/j.neurobiolaging.2006.11.017","article-title":"Selective loss of nigral dopamine neurons induced by overexpression of truncated human alpha-synuclein in mice","volume":"29","author":"Wakamatsu","year":"2008","journal-title":"Neurobiol Aging"},{"key":"key\n\t\t\t\t20180516101549_nly024-B70","doi-asserted-by":"crossref","first-page":"e28033","DOI":"10.1371\/journal.pone.0028033","article-title":"Early induction of oxidative stress in mouse model of Alzheimer disease with reduced mitochondrial superoxide dismutase activity","volume":"7","author":"Lee","year":"2012","journal-title":"PLoS One"},{"key":"key\n\t\t\t\t20180516101549_nly024-B71","doi-asserted-by":"crossref","first-page":"1641","DOI":"10.1074\/jbc.C100560200","article-title":"The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein","volume":"277","author":"Manning-Bog","year":"2002","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B72","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1016\/j.redox.2017.07.008","article-title":"Proteostasis, oxidative stress and aging","volume":"13","author":"Korovila","year":"2017","journal-title":"Redox Biol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B73","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1111\/jnc.13575","article-title":"Walking the tightrope: proteostasis and neurodegenerative disease","volume":"137","author":"Yerbury","year":"2016","journal-title":"J Neurochem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B74","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1126\/science.1227157","article-title":"Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice","volume":"338","author":"Luk","year":"2012","journal-title":"Science"},{"key":"key\n\t\t\t\t20180516101549_nly024-B75","doi-asserted-by":"crossref","first-page":"12368","DOI":"10.1523\/JNEUROSCI.2102-14.2014","article-title":"Brain injection of alpha-synuclein induces multiple proteinopathies, gliosis, and a neuronal injury marker","volume":"34","author":"Sacino","year":"2014","journal-title":"J Neurosci"},{"key":"key\n\t\t\t\t20180516101549_nly024-B76","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/nature14547","article-title":"alpha-Synuclein strains cause distinct synucleinopathies after local and systemic administration","volume":"522","author":"Peelaerts","year":"2015","journal-title":"Nature"},{"key":"key\n\t\t\t\t20180516101549_nly024-B77","doi-asserted-by":"crossref","first-page":"E912","DOI":"10.1073\/pnas.1512876113","article-title":"Induction of de novo alpha-synuclein fibrillization in a neuronal model for Parkinson\u2019s disease","volume":"113","author":"Fares","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"key":"key\n\t\t\t\t20180516101549_nly024-B78","doi-asserted-by":"crossref","first-page":"1835","DOI":"10.1016\/j.biocel.2008.01.017","article-title":"Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein","volume":"40","author":"Lee","year":"2008","journal-title":"Int J Biochem Cell Biol"},{"key":"key\n\t\t\t\t20180516101549_nly024-B79","doi-asserted-by":"crossref","first-page":"13621","DOI":"10.1074\/jbc.M109.074617","article-title":"Lysosomal degradation of alpha-synuclein in vivo","volume":"285","author":"Mak","year":"2010","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B80","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1111\/jnc.13743","article-title":"Proteolysis of alpha-synuclein fibrils in the lysosomal pathway limits induction of inclusion pathology","volume":"140","author":"Sacino","year":"2017","journal-title":"J Neurochem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B81","doi-asserted-by":"crossref","first-page":"7690","DOI":"10.1038\/s41598-017-08149-w","article-title":"Impaired endo-lysosomal membrane integrity accelerates the seeding progression of alpha-synuclein aggregates","volume":"7","author":"Jiang","year":"2017","journal-title":"Sci Rep"},{"key":"key\n\t\t\t\t20180516101549_nly024-B82","doi-asserted-by":"crossref","first-page":"13482","DOI":"10.1074\/jbc.M117.780296","article-title":"Selective imaging of internalized proteopathic alpha-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies","volume":"292","author":"Karpowicz","year":"2017","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20180516101549_nly024-B83","doi-asserted-by":"crossref","first-page":"E8284","DOI":"10.1073\/pnas.1710442114","article-title":"Modeling Parkinson\u2019s disease pathology by combination of fibril seeds and alpha-synuclein overexpression in the rat brain","volume":"114","author":"Thakur","year":"2017","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180516101549_nly024-B84","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1084\/jem.20112457","article-title":"Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice","volume":"209","author":"Luk","year":"2012","journal-title":"J Exp Med"},{"key":"key\n\t\t\t\t20180516101549_nly024-B85","doi-asserted-by":"crossref","first-page":"10732","DOI":"10.1073\/pnas.1321785111","article-title":"Intramuscular injection of alpha-synuclein induces CNS alpha-synuclein pathology and a rapid-onset motor phenotype in transgenic mice","volume":"111","author":"Sacino","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180516101549_nly024-B86","doi-asserted-by":"crossref","first-page":"2459","DOI":"10.1096\/fj.09-132928","article-title":"Reduction of oxidative stress, amyloid deposition, and memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer\u2019s disease","volume":"23","author":"Dumont","year":"2009","journal-title":"FASEB J"},{"key":"key\n\t\t\t\t20180516101549_nly024-B87","doi-asserted-by":"crossref","first-page":"13576","DOI":"10.1073\/pnas.0902714106","article-title":"Overexpression of SOD-2 reduces hippocampal superoxide and prevents memory deficits in a mouse model of Alzheimer\u2019s disease","volume":"106","author":"Massaad","year":"2009","journal-title":"Proc Natl Acad Sci U S A"}],"container-title":["Journal of Neuropathology &amp; Experimental Neurology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/jnen\/article-pdf\/77\/6\/443\/24819412\/nly024.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,10,17]],"date-time":"2019-10-17T01:10:00Z","timestamp":1571274600000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jnen\/article\/77\/6\/443\/4989445"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,4,27]]},"references-count":87,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2018,4,27]]},"published-print":{"date-parts":[[2018,6,1]]}},"URL":"https:\/\/doi.org\/10.1093\/jnen\/nly024","relation":{},"ISSN":["0022-3069","1554-6578"],"issn-type":[{"value":"0022-3069","type":"print"},{"value":"1554-6578","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2018,6]]},"published":{"date-parts":[[2018,4,27]]}}}