{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,20]],"date-time":"2026-03-20T02:36:56Z","timestamp":1773974216503,"version":"3.50.1"},"reference-count":64,"publisher":"Oxford University Press (OUP)","issue":"1","license":[{"start":{"date-parts":[[2018,9,13]],"date-time":"2018-09-13T00:00:00Z","timestamp":1536796800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["SFRH\/BD\/80884\/2011"],"award-info":[{"award-number":["SFRH\/BD\/80884\/2011"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["SFRH\/BD\/74881\/2010"],"award-info":[{"award-number":["SFRH\/BD\/74881\/2010"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"name":"German Science Foundation"},{"DOI":"10.13039\/501100001659","name":"German Research Foundation","doi-asserted-by":"publisher","award":["SFB1286"],"award-info":[{"award-number":["SFB1286"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002347","name":"Federal Ministry of Education and Research","doi-asserted-by":"publisher","award":["01KU1503B"],"award-info":[{"award-number":["01KU1503B"]}],"id":[{"id":"10.13039\/501100002347","id-type":"DOI","asserted-by":"publisher"}]},{"name":"EU Joint Programme\u2013Neurodegenerative Disease Research"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019,1,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Alpha-synuclein (aSyn) is a central player in Parkinson\u2019s disease (PD) but the precise molecular mechanisms underlying its pathogenicity remain unclear. It has recently been suggested that nuclear aSyn may modulate gene expression, possibly via interactions with DNA. However, the biological behavior of aSyn in the nucleus and the factors affecting its transcriptional role are not known. Here, we investigated the mechanisms underlying aSyn-mediated transcription deregulation by assessing its effects in the nucleus and the impact of phosphorylation in these dynamics. We found that aSyn induced severe transcriptional deregulation, including the downregulation of important cell cycle-related genes. Importantly, transcriptional deregulation was concomitant with reduced binding of aSyn to DNA. By forcing the nuclear presence of aSyn in the nucleus (aSyn-NLS), we found the accumulation of high molecular weight aSyn species altered gene expression and reduced toxicity when compared with the wild-type or exclusively cytosolic protein. Interestingly, nuclear localization of aSyn, and the effect on gene expression and cytotoxicity, was also modulated by phosphorylation on serine 129. Thus, we hypothesize that the role of aSyn on gene expression and, ultimately, toxicity, may be modulated by the phosphorylation status and nuclear presence of different aSyn species. Our findings shed new light onto the subcellular dynamics of aSyn and unveil an intricate interplay between subcellular location, phosphorylation and toxicity, opening novel avenues for the design of future strategies for therapeutic intervention in PD and other synucleinopathies.<\/jats:p>","DOI":"10.1093\/hmg\/ddy326","type":"journal-article","created":{"date-parts":[[2018,9,11]],"date-time":"2018-09-11T20:19:02Z","timestamp":1536697142000},"page":"31-50","source":"Crossref","is-referenced-by-count":168,"title":["Nuclear localization and phosphorylation modulate pathological effects of alpha-synuclein"],"prefix":"10.1093","volume":"28","author":[{"given":"Raquel","family":"Pinho","sequence":"first","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"},{"name":"Faculty of Medicine, University of Porto, Porto, Portugal"}]},{"given":"Isabel","family":"Paiva","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"Kristina Gotovac","family":"Jer\u010di\u0107","sequence":"additional","affiliation":[{"name":"Department for Functional Genomics, Center for Translational and Clinical Research, University Hospital Center Zagreb, University of Zagreb School of Medicine, Zagreb, Croatia"}]},{"given":"Luis","family":"Fonseca-Ornelas","sequence":"additional","affiliation":[{"name":"Max Planck Institute for Biophysical Chemistry, G\u00f6ttingen, Germany"}]},{"given":"Ellen","family":"Gerhardt","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"Christiane","family":"Fahlbusch","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"Paula","family":"Garcia-Esparcia","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, Bellvitge University Hospital, University of Barcelona, Bellvitge Biomedical Research Institute, Hospitalet de Llobregat; Biomedical Research Center of Neurodegenerative Diseases, Barcelona, Spain"}]},{"given":"Cemil","family":"Kerimoglu","sequence":"additional","affiliation":[{"name":"Department for Psychiatry and Psychotherapy, University Medical Center, G\u00f6ttingen, Germany"}]},{"given":"Maria A S","family":"Pavlou","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"Anna","family":"Villar-Piqu\u00e9","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"\u00c9va","family":"Szeg\u0151","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"Tom\u00e1s","family":"Lopes da Fonseca","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"Francesca","family":"Odoardi","sequence":"additional","affiliation":[{"name":"Institute of Neuroimmunology and Institute for Multiple Sclerosis Research, University Medical Centre G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"Szabolcs","family":"Soeroes","sequence":"additional","affiliation":[{"name":"Max Planck Institute for Biophysical Chemistry, Laboratory of Chromatin Biochemistry, G\u00f6ttingen, Germany"},{"name":"Oxford Nanopore Technologies LTD, Oxford, United Kingdom"}]},{"given":"Ana Cristina","family":"Rego","sequence":"additional","affiliation":[{"name":"Center for Neuroscience and Cell Biology and Faculty of Medicine, University of Coimbra, Coimbra, Portugal"}]},{"given":"Wolfgang","family":"Fischle","sequence":"additional","affiliation":[{"name":"Max Planck Institute for Biophysical Chemistry, Laboratory of Chromatin Biochemistry, G\u00f6ttingen, Germany"},{"name":"King Abdullah University of Science and Technology, Environmental Epigenetics Program, Thuwal, Saudi Arabia"}]},{"given":"Jens C","family":"Schwamborn","sequence":"additional","affiliation":[{"name":"Development and Cellular Biology, Luxembourg Centre for Systems Biomedicine (LCSB), University of Luxembourg, Esch-sur-Alzette, Luxembourg"}]},{"given":"Thomas","family":"Meyer","sequence":"additional","affiliation":[{"name":"Klinik f\u00fcr Psychosomatische Medizin und Psychotherapie, Universit\u00e4tsmedizin G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"Sebastian","family":"K\u00fcgler","sequence":"additional","affiliation":[{"name":"Department of Neurology, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"}]},{"given":"Isidre","family":"Ferrer","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, Bellvitge University Hospital, University of Barcelona, Bellvitge Biomedical Research Institute, Hospitalet de Llobregat; Biomedical Research Center of Neurodegenerative Diseases, Barcelona, Spain"}]},{"given":"Johannes","family":"Attems","sequence":"additional","affiliation":[{"name":"Institute of Neuroscience, Newcastle University, Campus for Ageing and Vitality, Newcastle upon Tyne, United Kingdom"}]},{"given":"Andr\u00e9","family":"Fischer","sequence":"additional","affiliation":[{"name":"Department for Psychiatry and Psychotherapy, University Medical Center, G\u00f6ttingen, Germany"},{"name":"Department of Epigenetics and Systems Medicine in Neurodegenerative Diseases, German Center for Neurodegenerative Diseases, G\u00f6ttingen Germany"}]},{"given":"Stefan","family":"Becker","sequence":"additional","affiliation":[{"name":"Max Planck Institute for Biophysical Chemistry, G\u00f6ttingen, Germany"}]},{"given":"Markus","family":"Zweckstetter","sequence":"additional","affiliation":[{"name":"Max Planck Institute for Biophysical Chemistry, G\u00f6ttingen, Germany"},{"name":"Department of Neurology, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"},{"name":"Structural Biology in Dementia, German Center for Neurodegenerative Diseases, G\u00f6ttingen, Germany"}]},{"given":"Fran","family":"Borovecki","sequence":"additional","affiliation":[{"name":"Department for Functional Genomics, Center for Translational and Clinical Research, University Hospital Center Zagreb, University of Zagreb School of Medicine, Zagreb, Croatia"},{"name":"Department of Neurology, University Hospital Center Zagreb, Zagreb, Croatia"}]},{"given":"Tiago F","family":"Outeiro","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center G\u00f6ttingen, G\u00f6ttingen, Germany"},{"name":"Institute of Neuroscience, Newcastle University, Campus for Ageing and Vitality, Newcastle upon Tyne, United Kingdom"},{"name":"Chronic Disease Research Center, NOVA Medical School, Lisboa, Portugal"},{"name":"Max Planck Institute for Experimental Medicine, G\u00f6ttingen, Germany"}]}],"member":"286","published-online":{"date-parts":[[2018,9,13]]},"reference":[{"key":"2019102302291620500_ref1","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's disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"2019102302291620500_ref2","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1038\/ng.487","article-title":"Genome-wide association study reveals genetic risk underlying Parkinson's disease","volume":"41","author":"Simon-Sanchez","year":"2009","journal-title":"Nat. Genet."},{"key":"2019102302291620500_ref3","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"Alpha-synuclein in Lewy bodies","volume":"388","author":"Spillantini","year":"1997","journal-title":"Nature"},{"key":"2019102302291620500_ref4","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.nbd.2007.11.008","article-title":"Transcriptional dysregulation in a transgenic model of Parkinson disease","volume":"29","author":"Yacoubian","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"2019102302291620500_ref5","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.expneurol.2006.12.005","article-title":"Wild-type and mutant alpha-synuclein induce a multi-component gene expression profile consistent with shared pathophysiology in different transgenic mouse models of PD","volume":"204","author":"Miller","year":"2007","journal-title":"Exp. Neurol."},{"key":"2019102302291620500_ref6","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1007\/s00702-004-0212-1","article-title":"Gene expression profiling of parkinsonian substantia nigra pars compacta; alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion\/cellular matrix and vesicle trafficking genes","volume":"111","author":"Grunblatt","year":"2004","journal-title":"J. Neural Transm."},{"key":"2019102302291620500_ref7","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0157852","article-title":"Gene expression differences in peripheral blood of Parkinson's disease patients with distinct progression profiles","volume":"11","author":"Pinho","year":"2016","journal-title":"PLoS One"},{"key":"2019102302291620500_ref8","doi-asserted-by":"crossref","first-page":"1018","DOI":"10.1016\/j.nbd.2011.12.021","article-title":"Meta-analysis of genetic and environmental Parkinson's disease models reveals a common role of mitochondrial protection pathways","volume":"45","author":"Soreq","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"2019102302291620500_ref9","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.neuroscience.2011.10.016","article-title":"Determining nuclear localization of alpha-synuclein in mouse brains","volume":"199","author":"Huang","year":"2011","journal-title":"Neuroscience"},{"key":"2019102302291620500_ref10","doi-asserted-by":"crossref","first-page":"415","DOI":"10.3233\/JPD-130216","article-title":"Limelight on alpha-synuclein: pathological and mechanistic implications in neurodegeneration","volume":"3","author":"Wales","year":"2013","journal-title":"J. Parkinsons Dis."},{"key":"2019102302291620500_ref11","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1016\/j.freeradbiomed.2012.05.024","article-title":"Selective binding of nuclear alpha-synuclein to the PGC1alpha promoter under conditions of oxidative stress may contribute to losses in mitochondrial function: implications for Parkinson's disease","volume":"53","author":"Siddiqui","year":"2012","journal-title":"Free Radic. Biol. Med."},{"key":"2019102302291620500_ref12","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1186\/s40478-015-0257-4","article-title":"Altered machinery of protein synthesis is region- and stage-dependent and is associated with alpha-synuclein oligomers in Parkinson's disease","volume":"3","author":"Garcia-Esparcia","year":"2015","journal-title":"Acta Neuropathol. Commun."},{"key":"2019102302291620500_ref13","doi-asserted-by":"crossref","first-page":"2804","DOI":"10.1523\/JNEUROSCI.08-08-02804.1988","article-title":"Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal","volume":"8","author":"Maroteaux","year":"1988","journal-title":"J. Neurosci."},{"key":"2019102302291620500_ref14","doi-asserted-by":"crossref","first-page":"3012","DOI":"10.1093\/hmg\/ddl243","article-title":"Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity","volume":"15","author":"Kontopoulos","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"2019102302291620500_ref15","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/9282f173-df82-4b70-9120-b4e62b3dacb1","article-title":"Formation of toxic oligomeric alpha-synuclein species in living cells","volume":"3","author":"Outeiro","year":"2008","journal-title":"PLoS One"},{"key":"2019102302291620500_ref16","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1007\/s10571-009-9473-4","article-title":"Expression and subcellular location of alpha-synuclein during mouse-embryonic development","volume":"30","author":"Zhong","year":"2010","journal-title":"Cell. Mol. Neurobiol."},{"key":"2019102302291620500_ref17","doi-asserted-by":"crossref","first-page":"8465","DOI":"10.1021\/bi0341152","article-title":"Nuclear localization of alpha-synuclein and its interaction with histones","volume":"42","author":"Goers","year":"2003","journal-title":"Biochemistry"},{"key":"2019102302291620500_ref18","doi-asserted-by":"crossref","first-page":"3401","DOI":"10.1093\/hmg\/ddr246","article-title":"Alpha-synuclein functions in the nucleus to protect against hydroxyurea-induced replication stress in yeast","volume":"20","author":"Liu","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"2019102302291620500_ref19","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.neuropharm.2013.07.035","article-title":"The nuclear accumulation of alpha-synuclein is mediated by importin alpha and promotes neurotoxicity by accelerating the cell cycle","volume":"82","author":"Ma","year":"2014","journal-title":"Neuropharmacology"},{"key":"2019102302291620500_ref20","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":"2019102302291620500_ref21","doi-asserted-by":"crossref","first-page":"E6506","DOI":"10.1073\/pnas.1606791113","article-title":"Environmental and genetic factors support the dissociation between alpha-synuclein aggregation and toxicity","volume":"113","author":"Villar-Pique","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2019102302291620500_ref22","doi-asserted-by":"crossref","first-page":"1819","DOI":"10.1002\/jnr.21310","article-title":"Accumulation of phosphorylated alpha-synuclein in dopaminergic neurons of transgenic mice that express human alpha-synuclein","volume":"85","author":"Wakamatsu","year":"2007","journal-title":"J. Neurosci. Res."},{"key":"2019102302291620500_ref23","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1007\/s12035-013-8406-x","article-title":"Assessing the subcellular dynamics of alpha-synuclein using photoactivation microscopy","volume":"47","author":"Goncalves","year":"2013","journal-title":"Mol. Neurobiol."},{"key":"2019102302291620500_ref24","first-page":"872","article-title":"Phosphorylation does not prompt, nor prevent, the formation of alpha-synuclein toxic species in a rat model of Parkinson's disease","volume":"18","author":"Azeredo da Silveira","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"2019102302291620500_ref25","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0025443","article-title":"Convergence of miRNA expression profiling, alpha-synuclein interacton and GWAS in Parkinson's disease","volume":"6","author":"Martins","year":"2011","journal-title":"PLoS One"},{"key":"2019102302291620500_ref26","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1016\/j.jmb.2004.09.096","article-title":"Double-stranded DNA stimulates the fibrillation of alpha-synuclein in vitro and is associated with the mature fibrils: an electron microscopy study","volume":"344","author":"Cherny","year":"2004","journal-title":"J. Mol. Biol."},{"key":"2019102302291620500_ref27","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/s00401-016-1542-4","article-title":"Proaggregant nuclear factor(s) trigger rapid formation of alpha-synuclein aggregates in apoptotic neurons","volume":"132","author":"Jiang","year":"2016","journal-title":"Acta Neuropathol."},{"key":"2019102302291620500_ref28","doi-asserted-by":"crossref","first-page":"39","DOI":"10.3233\/JPD-160779","article-title":"Implication of alpha-synuclein phosphorylation at S129 in synucleinopathies: what have we learned in the last decade?","volume":"6","author":"Oueslati","year":"2016","journal-title":"J. Parkinsons Dis."},{"key":"2019102302291620500_ref29","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1007\/s12035-013-8473-z","article-title":"PLK2 modulates alpha-synuclein aggregation in yeast and mammalian cells","volume":"48","author":"Basso","year":"2013","journal-title":"Mol. Neurobiol."},{"key":"2019102302291620500_ref30","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1004302","article-title":"Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease","volume":"10","author":"Tenreiro","year":"2014","journal-title":"PLoS Genet."},{"key":"2019102302291620500_ref31","doi-asserted-by":"crossref","first-page":"42","DOI":"10.3389\/fnmol.2014.00042","article-title":"Protein phosphorylation in neurodegeneration: friend or foe?","volume":"7","author":"Tenreiro","year":"2014","journal-title":"Front. Mol. Neurosci."},{"key":"2019102302291620500_ref32","doi-asserted-by":"crossref","first-page":"2231","DOI":"10.1093\/hmg\/ddx114","article-title":"Sodium butyrate rescues dopaminergic cells from alpha-synuclein-induced transcriptional deregulation and DNA damage","volume":"26","author":"Paiva","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"2019102302291620500_ref33","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.nbd.2018.08.001","article-title":"Alpha-synuclein deregulates the expression of COL4A2 and impairs ER-Golgi function","volume":"119","author":"Paiva","year":"2018","journal-title":"Neurobiol. Dis."},{"key":"2019102302291620500_ref34","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/nmeth.1432","article-title":"Exploring the sequence determinants of amyloid structure using position-specific scoring matrices","volume":"7","author":"Maurer-Stroh","year":"2010","journal-title":"Nat. Methods"},{"key":"2019102302291620500_ref35","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1021\/cn5002254","article-title":"Efficient modification of alpha-synuclein serine 129 by protein kinase CK1 requires phosphorylation of tyrosine 125 as a priming event","volume":"5","author":"Kosten","year":"2014","journal-title":"ACS Chem. Nerosci."},{"key":"2019102302291620500_ref36","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1111\/j.1600-0854.2007.00542.x","article-title":"Fragmentation of the Golgi apparatus: an early apoptotic event independent of the cytoskeleton","volume":"8","author":"Mukherjee","year":"2007","journal-title":"Traffic"},{"key":"2019102302291620500_ref37","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1002\/ana.23905","article-title":"Beta-synuclein aggregates and induces neurodegeneration in dopaminergic neurons","volume":"74","author":"Taschenberger","year":"2013","journal-title":"Ann. Neurol."},{"key":"2019102302291620500_ref38","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1089\/dna.2006.25.406","article-title":"DNA damage-dependent cell cycle checkpoints and genomic stability","volume":"25","author":"Ishikawa","year":"2006","journal-title":"DNA Cell Biol."},{"key":"2019102302291620500_ref39","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1111\/j.1365-2990.2010.01064.x","article-title":"Review: cell cycle aberrations and neurodegeneration","volume":"36","author":"Bonda","year":"2010","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"2019102302291620500_ref40","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/S0197-4580(00)00221-9","article-title":"Mitotic activation: a convergent mechanism for a cohort of neurodegenerative diseases","volume":"21","author":"Husseman","year":"2000","journal-title":"Neurobiol. Aging"},{"key":"2019102302291620500_ref41","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.jchemneu.2010.12.003","article-title":"Different sub-cellular localization of alpha-synuclein in the C57BL\\6J mouse's central nervous system by two novel monoclonal antibodies","volume":"41","author":"Vivacqua","year":"2011","journal-title":"J. Chem. Neuroanat."},{"key":"2019102302291620500_ref42","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1111\/j.1440-1789.2007.00841.x","article-title":"Multiple system atrophy: alpha-synuclein and neuronal degeneration","volume":"27","author":"Yoshida","year":"2007","journal-title":"Neuropathology"},{"key":"2019102302291620500_ref43","doi-asserted-by":"crossref","first-page":"7055","DOI":"10.1523\/JNEUROSCI.1241-16.2016","article-title":"Poststroke induction of alpha-synuclein mediates ischemic brain damage","volume":"36","author":"Kim","year":"2016","journal-title":"J. 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