Outeiro, Tiago Fleming

[["dc.bibliographiccitation.firstpage","120"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Brain Pathology"],["dc.bibliographiccitation.lastpage","132"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Koss, David J."],["dc.contributor.author","Bondarevaite, Odeta"],["dc.contributor.author","Adams, Sara"],["dc.contributor.author","Leite, Marta"],["dc.contributor.author","Giorgini, Flaviano"],["dc.contributor.author","Attems, Johannes"],["dc.contributor.author","Outeiro, Tiago F."],["dc.date.accessioned","2021-04-14T08:24:10Z"],["dc.date.available","2021-04-14T08:24:10Z"],["dc.date.issued","2020"],["dc.description.abstract","Loss of function mutations within the vesicular trafficking protein Ras analogy in brain 39B (RAB39B) are associated with rare X-linked Parkinson’s disease (PD). Physiologically, RAB39B is localized to Golgi vesicles and recycling endosomes and is required for glutamatergic receptor maturation but also for alpha-Synuclein (aSyn) homeostasis and the inhibition of its aggregation. Despite evidence linking RAB39B to neurodegeneration, the involvement of the protein in idiopathic neurodegenerative diseases remains undetermined. Here, analysis of the spatial distribution and expression of RAB39B was conducted in post-mortem human brain tissue from cases of dementia with Lewy bodies (DLB, n = 10), Alzheimer’s disease (AD, n = 12) and controls (n = 12). Assessment of cortical RAB39B immunoreactivity using tissue microarrays revealed an overall reduction in the area of RAB39B positive gray matter in DLB cases when compared to controls and AD cases. Strikingly, RAB39B co-localized with beta-amyloid (Aβ) plaques in all cases examined and was additionally present in a subpopulation of Lewy bodies (LBs) in DLB. Biochemical measures of total RAB39B levels within the temporal cortex were unchanged between DLB, AD and controls. However, upon subcellular fractionation, a reduction of RAB39B in the cytoplasmic pool was found in DLB cases, alongside an increase of phosphorylated aSyn and Aβ in whole tissue lysates. The reduction of cytoplasmic RAB39B is consistent with an impaired reserve capacity for RAB39B-associated functions, which in turn may facilitate LB aggregation and synaptic impairment. Collectively, our data support the involvement of RAB39B in the pathogenesis of DLB and the co-aggregation of RAB39B with Aβ in plaques suggests that age-associated cerebral Aβ pathology may be contributory to the loss of RAB39B. Thus RAB39B, its associated functional pathways and its entrapment in aggregates may be considered as future targets for therapeutic interventions to impede the overall pathological burden and cellular dysfunction in Lewy body diseases."],["dc.identifier.doi","10.1111/bpa.12890"],["dc.identifier.pmid","32762091"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81186"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/166"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/97"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B08: Definition von Kaskaden molekularer Veränderungen bei Synucleinopathien während der Neurodegeneration"],["dc.relation.eissn","1750-3639"],["dc.relation.issn","1015-6305"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","CC BY 4.0"],["dc.title","RAB39B is redistributed in dementia with Lewy bodies and is sequestered within aβ plaques and Lewy bodies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Koss, David J."],["dc.contributor.author","Erskine, Daniel"],["dc.contributor.author","Porter, Andrew"],["dc.contributor.author","Palmoski, Pawel"],["dc.contributor.author","Leite, Marta"],["dc.contributor.author","Attems, Johannes"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2022-08-24T06:03:57Z"],["dc.date.available","2022-08-24T06:03:57Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1101/2021.10.20.465125"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113158"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/486"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/165"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.title","Nuclear alpha-synuclein is present in the human brain and is modified in dementia with Lewy bodies"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","511"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Acta Neuropathologica"],["dc.bibliographiccitation.lastpage","526"],["dc.bibliographiccitation.volume","141"],["dc.contributor.author","Erskine, Daniel"],["dc.contributor.author","Koss, David"],["dc.contributor.author","Korolchuk, Viktor I."],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Attems, Johannes"],["dc.contributor.author","McKeith, Ian"],["dc.date.accessioned","2021-04-14T08:30:40Z"],["dc.date.available","2021-04-14T08:30:40Z"],["dc.date.issued","2021"],["dc.description.abstract","Accumulation of the protein α-synuclein into insoluble intracellular deposits termed Lewy bodies (LBs) is the characteristic neuropathological feature of LB diseases, such as Parkinson’s disease (PD), Parkinson’s disease dementia (PDD) and dementia with LB (DLB). α-Synuclein aggregation is thought to be a critical pathogenic event in the aetiology of LB disease, based on genetic analyses, fundamental studies using model systems, and the observation of LB pathology in post-mortem tissue. However, some monogenic disorders not traditionally characterised as synucleinopathies, such as lysosomal storage disorders, iron storage disorders and mitochondrial diseases, appear disproportionately vulnerable to the deposition of LBs, perhaps suggesting the process of LB formation may be a result of processes perturbed as a result of these conditions. The present review discusses biological pathways common to monogenic disorders associated with LB formation, identifying catabolic processes, particularly related to lipid homeostasis, autophagy and mitochondrial function, as processes that could contribute to LB formation. These findings are discussed in the context of known mediators of α-synuclein aggregation, highlighting the potential influence of impairments to these processes in the aetiology of LB formation."],["dc.identifier.doi","10.1007/s00401-021-02266-7"],["dc.identifier.pmid","33515275"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83330"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/215"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/96"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B06: Die Rolle von RNA in Synapsenphysiologie und Neurodegeneration"],["dc.relation","SFB 1286 | B08: Definition von Kaskaden molekularer Veränderungen bei Synucleinopathien während der Neurodegeneration"],["dc.relation.eissn","1432-0533"],["dc.relation.issn","0001-6322"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","CC BY 4.0"],["dc.title","Lipids, lysosomes and mitochondria: insights into Lewy body formation from rare monogenic disorders"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Acta Neuropathologica Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Koss, David J."],["dc.contributor.author","Erskine, Daniel"],["dc.contributor.author","Porter, Andrew"],["dc.contributor.author","Palmoski, Pawel"],["dc.contributor.author","Menon, Hariharan"],["dc.contributor.author","Todd, Olivia G. J."],["dc.contributor.author","Leite, Marta"],["dc.contributor.author","Attems, Johannes"],["dc.contributor.author","Outeiro, Tiago F."],["dc.date.accessioned","2022-09-01T09:50:57Z"],["dc.date.available","2022-09-01T09:50:57Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n \n Dementia with Lewy bodies (DLB) is pathologically defined by the cytoplasmic accumulation of alpha-synuclein (aSyn) within neurons in the brain. Predominately pre-synaptic, aSyn has been reported in various subcellular compartments in experimental models. Indeed, nuclear alpha-synuclein (aSyn\n Nuc\n ) is evident in many models, the dysregulation of which is associated with altered DNA integrity, transcription and nuclear homeostasis. However, the presence of aSyn\n Nuc\n in human brain cells remains controversial, yet the determination of human brain aSyn\n Nuc\n and its pathological modification is essential for understanding synucleinopathies. Here, using a multi-disciplinary approach employing immunohistochemistry, immunoblot, and mass-spectrometry (MS), we confirm aSyn\n Nuc\n in post-mortem brain tissue obtained from DLB and control cases. Highly dependent on antigen retrieval methods, in optimal conditions, intra-nuclear pan and phospho-S129 positive aSyn puncta were observed in cortical neurons and non-neuronal cells in fixed brain sections and in isolated nuclear preparations in all cases examined. Furthermore, an increase in nuclear phospho-S129 positive aSyn immunoreactivity was apparent in DLB cases compared to controls, in both neuronal and non-neuronal cell types. Our initial histological investigations identified that aSyn\n Nuc\n is affected by epitope unmasking methods but present under optimal conditions, and this presence was confirmed by isolation of nuclei and a combined approach of immunoblotting and mass spectrometry, where aSyn\n Nuc\n was approximately tenfold less abundant in the nucleus than cytoplasm. Notably, direct comparison of DLB cases to aged controls identified increased pS129 and higher molecular weight species in the nuclei of DLB cases, suggesting putative pathogenic modifications to aSyn\n Nuc\n in DLB. In summary, using multiple approaches we provide several lines of evidence supporting the presence of aSyn\n Nuc\n in autoptic human brain tissue and, notably, that it is subject to putative pathogenic modifications in DLB that may contribute to the disease phenotype."],["dc.description.sponsorship","The Lewy Body Society"],["dc.description.sponsorship","ARUK Northern network"],["dc.identifier.doi","10.1186/s40478-022-01403-x"],["dc.identifier.pii","1403"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113844"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","2051-5960"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Nuclear alpha-synuclein is present in the human brain and is modified in dementia with Lewy bodies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","65.e6"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","77.e6"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Szegő, Éva M."],["dc.contributor.author","Dominguez-Meijide, Antonio"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","König, Annekatrin"],["dc.contributor.author","Koss, David J."],["dc.contributor.author","Li, Wen"],["dc.contributor.author","Pinho, Raquel"],["dc.contributor.author","Fahlbusch, Christiane"],["dc.contributor.author","Johnson, Mary"],["dc.contributor.author","Santos, Patricia"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Thom, Tobias"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Li, Jiayi"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Attems, Johannes"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2021-04-26T14:09:42Z"],["dc.date.available","2021-04-26T14:09:42Z"],["dc.date.issued","2019"],["dc.description.abstract","Alpha-synuclein (aSyn) accumulates in intracellular inclusions in synucleinopathies, but the molecular mechanisms leading to disease are unclear. We identify the 10 kDa heat shock protein (HSP10) as a mediator of aSyn-induced mitochondrial impairments in striatal synaptosomes. We find an age-associated increase in the cytosolic levels of HSP10, and a concomitant decrease in the mitochondrial levels, in aSyn transgenic mice. The levels of superoxide dismutase 2, a client of the HSP10/HSP60 folding complex, and synaptosomal spare respiratory capacity are also reduced. Overexpression of HSP10 ameliorates aSyn-associated mitochondrial dysfunction and delays aSyn pathology in vitro and in vivo. Altogether, our data indicate that increased levels of aSyn induce mitochondrial deficits, at least partially, by sequestering HSP10 in the cytosol and preventing it from acting in mitochondria. Importantly, these alterations manifest first at presynaptic terminals. Our study not only provides mechanistic insight into synucleinopathies but opens new avenues for targeting underlying cellular pathologies."],["dc.identifier.doi","10.1016/j.celrep.2019.06.009"],["dc.identifier.pmid","31269451"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16257"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84389"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/6"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B08: Definition von Kaskaden molekularer Veränderungen bei Synucleinopathien während der Neurodegeneration"],["dc.relation.eissn","2211-1247"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Cytosolic Trapping of a Mitochondrial Heat Shock Protein Is an Early Pathological Event in Synucleinopathies"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Brain: A Journal of Neurology"],["dc.contributor.author","Hatton, Christopher"],["dc.contributor.author","Ghanem, Simona S."],["dc.contributor.author","Koss, David J."],["dc.contributor.author","Abdi, Ilham Y."],["dc.contributor.author","Gibbons, Elizabeth"],["dc.contributor.author","Guerreiro, Rita"],["dc.contributor.author","Bras, Jose"],["dc.contributor.author","Walker, Lauren"],["dc.contributor.author","Gelpi, Ellen"],["dc.contributor.author","Heywood, Wendy"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Attems, Johannes"],["dc.contributor.author","McFarland, Robert"],["dc.contributor.author","Forsyth, Rob"],["dc.contributor.author","El-Agnaf, Omar M."],["dc.contributor.author","Erskine, Daniel"],["dc.date.accessioned","2022-02-22T15:58:07Z"],["dc.date.available","2022-02-22T15:58:07Z"],["dc.date.issued","2022-01-06"],["dc.description.abstract","Krabbe disease is an infantile neurodegenerative disorder resulting from pathogenic variants in the GALC gene which causes accumulation of the toxic sphingolipid psychosine. GALC variants are also associated with Lewy body diseases, an umbrella term for age-associated neurodegenerative diseases in which the protein α-synuclein aggregates into Lewy bodies. To explore whether α-synuclein in Krabbe disease has pathological similarities to that in Lewy body disease, we performed an observational post-mortem study of Krabbe disease brain tissue (N = 4) compared to infant controls (N = 4) and identified widespread accumulations of α-synuclein. To determine whether α-synuclein in Krabbe disease brain displayed disease-associated pathogenic properties we evaluated its seeding capacity using the real-time quaking-induced conversion assay in two cases for which frozen tissue was available and strikingly identified aggregation into fibrils similar to those observed in Lewy body disease, confirming the prion-like capacity of Krabbe disease-derived α-synuclein. These observations constitute the first report of prion-like α-synuclein in the brain tissue of infants and challenge the putative view that α-synuclein pathology is merely an age-associated phenomenon, instead suggesting it results from alterations to biological pathways, such as sphingolipid metabolism. Our findings have important implications for understanding the mechanisms underlying Lewy body formation in Lewy body disease."],["dc.identifier.doi","10.1093/brain/awac002"],["dc.identifier.pmid","34999780"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100198"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/388"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/148"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation.eissn","1460-2156"],["dc.relation.issn","0006-8950"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","CC BY-NC 4.0"],["dc.title","Prion-like α-synuclein pathology in the brain of infants with Krabbe disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","unpublished"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","5"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Neurodegeneration"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Koss, David J."],["dc.contributor.author","Erskine, Daniel"],["dc.contributor.author","Walker, Lauren"],["dc.contributor.author","Kurzawa-Akanbi, Marzena"],["dc.contributor.author","Burn, David"],["dc.contributor.author","Donaghy, Paul"],["dc.contributor.author","Morris, Christopher"],["dc.contributor.author","Taylor, John-Paul"],["dc.contributor.author","Thomas, Alan"],["dc.contributor.author","Attems, Johannes"],["dc.contributor.author","McKeith, Ian"],["dc.date.accessioned","2019-07-09T11:51:10Z"],["dc.date.available","2019-07-09T11:51:10Z"],["dc.date.issued","2019"],["dc.description.abstract","Dementia with Lewy bodies (DLB) is an age-associated neurodegenerative disorder producing progressive cognitive decline that interferes with normal life and daily activities. Neuropathologically, DLB is characterised by the accumulation of aggregated α-synuclein protein in Lewy bodies and Lewy neurites, similar to Parkinson's disease (PD). Extrapyramidal motor features characteristic of PD, are common in DLB patients, but are not essential for the clinical diagnosis of DLB. Since many PD patients develop dementia as disease progresses, there has been controversy about the separation of DLB from PD dementia (PDD) and consensus reports have put forward guidelines to assist clinicians in the identification and management of both syndromes. Here, we present basic concepts and definitions, based on our current understanding, that should guide the community to address open questions that will, hopefully, lead us towards improved diagnosis and novel therapeutic strategies for DLB and other synucleinopathies."],["dc.identifier.doi","10.1186/s13024-019-0306-8"],["dc.identifier.pmid","30665447"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16061"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59887"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","006"],["dc.subject.ddc","573"],["dc.subject.ddc","612"],["dc.title","Dementia with Lewy bodies: an update and outlook"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","31"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Human Molecular Genetics"],["dc.bibliographiccitation.lastpage","50"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Pinho, Raquel"],["dc.contributor.author","Paiva, Isabel"],["dc.contributor.author","Jercic, Kristina Gotovac"],["dc.contributor.author","Fonseca-Ornelas, Luis"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","Fahlbusch, Christiane"],["dc.contributor.author","Garcia-Esparcia, Paula"],["dc.contributor.author","Kerimoglu, Cemil"],["dc.contributor.author","Pavlou, Maria A. S."],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Szego, Éva"],["dc.contributor.author","Lopes da Fonseca, Tomás"],["dc.contributor.author","Odoardi, Francesca"],["dc.contributor.author","Soeroes, Szabolcs"],["dc.contributor.author","Rego, Ana Cristina"],["dc.contributor.author","Fischle, Wolfgang"],["dc.contributor.author","Schwamborn, Jens C."],["dc.contributor.author","Meyer, Thomas"],["dc.contributor.author","Kügler, Sebastian"],["dc.contributor.author","Ferrer, Isidre"],["dc.contributor.author","Attems, Johannes"],["dc.contributor.author","Fischer, André"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Borovecki, Fran"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2020-07-06T13:57:16Z"],["dc.date.available","2020-07-06T13:57:16Z"],["dc.date.issued","2019"],["dc.description.abstract","Alpha-synuclein (aSyn) is a central player in Parkinson's 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."],["dc.identifier.doi","10.1093/hmg/ddy326"],["dc.identifier.pmid","30219847"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/66857"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/84"],["dc.language.iso","en"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B08: Definition von Kaskaden molekularer Veränderungen bei Synucleinopathien während der Neurodegeneration"],["dc.relation.eissn","1460-2083"],["dc.relation.issn","0964-6906"],["dc.relation.workinggroup","RG A. Fischer (Epigenetics and Systems Medicine in Neurodegenerative Diseases)"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.title","Nuclear localization and phosphorylation modulate pathological effects of alpha-synuclein"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]