Outeiro, Tiago Fleming

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Tenreiro, Sandra"],["dc.contributor.author","Reimao-Pinto, Madalena M."],["dc.contributor.author","Antas, Pedro"],["dc.contributor.author","Rino, Jose"],["dc.contributor.author","Waiss, Meytal"],["dc.contributor.author","Magalhaes, Filipa"],["dc.contributor.author","Wawrzycka, Donata"],["dc.contributor.author","Macedo, Diana"],["dc.contributor.author","Cunha, Monica E."],["dc.contributor.author","Kaganovich, Daniel"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2018-11-07T09:20:11Z"],["dc.date.available","2018-11-07T09:20:11Z"],["dc.date.issued","2013"],["dc.format.extent","79"],["dc.identifier.isi","000327927400108"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28826"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.eventlocation","Frankfurt Main, GERMANY"],["dc.relation.issn","1097-0061"],["dc.relation.issn","0749-503X"],["dc.title","Harnessing the power of yeast to decipher the role of alpha-synuclein phosphorylation in Parkinson's disease"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Brás, Inês Caldeira"],["dc.contributor.author","Khani, Mohammad Hossein"],["dc.contributor.author","Vasili, Eftychia"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Parfentev, Iwan"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","Fahlbusch, Christiane"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Gollisch, Tim"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2022-02-23T16:36:34Z"],["dc.date.available","2022-02-23T16:36:34Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1101/2021.07.18.452825"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100391"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/327"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/128"],["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.workinggroup","RG Gollisch (Sensory Processing in the Retina)"],["dc.relation.workinggroup","RG Möbius"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.title","Common molecular mechanisms underlie the transfer of alpha-synuclein, Tau and huntingtin and modulate spontaneous activity in neuronal cells"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1539"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Cellular and Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","1550"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Gustafsson, Gabriel"],["dc.contributor.author","Lööv, Camilla"],["dc.contributor.author","Persson, Emma"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Takeda, Shuko"],["dc.contributor.author","Bergström, Joakim"],["dc.contributor.author","Erlandsson, Anna"],["dc.contributor.author","Sehlin, Dag"],["dc.contributor.author","Balaj, Leonora"],["dc.contributor.author","György, Bence"],["dc.contributor.author","Hallbeck, Martin"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Breakefield, Xandra O."],["dc.contributor.author","Hyman, Bradley T."],["dc.contributor.author","Ingelsson, Martin"],["dc.date.accessioned","2020-12-10T14:11:26Z"],["dc.date.available","2020-12-10T14:11:26Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1007/s10571-018-0622-5"],["dc.identifier.eissn","1573-6830"],["dc.identifier.issn","0272-4340"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15557"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71076"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Secretion and Uptake of α-Synuclein Via Extracellular Vesicles in Cultured Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","E4971"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","E4977"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Turriani, Elisa"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Schön, Margarete"],["dc.contributor.author","Schön, Michael P."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.contributor.author","Becker, Dorothea"],["dc.date.accessioned","2018-04-23T11:47:36Z"],["dc.date.available","2018-04-23T11:47:36Z"],["dc.date.issued","2017"],["dc.description.abstract","Recent epidemiological and clinical studies have reported a significantly increased risk for melanoma in people with Parkinson’s disease. Because no evidence could be obtained that genetic factors are the reason for the association between these two diseases, we hypothesized that of the three major Parkinson’s disease-related proteins—α-synuclein, LRRK2, and Parkin—α-synuclein might be a major link. Our data, presented here, demonstrate that α-synuclein promotes the survival of primary and metastatic melanoma cells, which is the exact opposite of the effect that α-synuclein has on dopaminergic neurons, where its accumulation causes neuronal dysfunction and death. Because this detrimental effect of α-synuclein on neurons can be rescued by the small molecule anle138b, we explored its effect on melanoma cells. We found that treatment with anle138b leads to massive melanoma cell death due to a major dysregulation of autophagy, suggesting that α-synuclein is highly beneficial to advanced melanoma because it ensures that autophagy is maintained at a homeostatic level that promotes and ensures the cell’s survival."],["dc.identifier.doi","10.1073/pnas.1700200114"],["dc.identifier.gro","3142238"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13362"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0027-8424"],["dc.title","Treatment with diphenyl–pyrazole compound anle138b/c reveals that α-synuclein protects melanoma cells from autophagic cell death"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","693"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Molecular Medicine"],["dc.bibliographiccitation.lastpage","703"],["dc.bibliographiccitation.volume","91"],["dc.contributor.author","Eisbach, Sibylle E."],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2018-11-07T09:24:21Z"],["dc.date.available","2018-11-07T09:24:21Z"],["dc.date.issued","2013"],["dc.description.abstract","Parkinson's disease is characterized by intracellular proteinaceous depositions known as Lewy bodies. These largely consist of the protein alpha-synuclein, whose physiological function remains unclear, but mutations and overexpression of the protein have been shown to cause early onset cases of Parkinson's disease. Deregulation of alpha-synuclein biology causes neurodegeneration and impaired neuronal trafficking, hinting at a possible contribution to the pathological mechanism. Recent studies produced some evidence hinting at the involvement of several regulators of the transport machinery such as Rab GTPases and SNARE proteins, but also shown that alpha-synuclein can be propagated between cells. Here, we discuss the molecular interplay of alpha-synuclein with the intracellular transport machinery, its consequences, and the implications for disease mechanisms."],["dc.identifier.doi","10.1007/s00109-013-1038-9"],["dc.identifier.isi","000319297200006"],["dc.identifier.pmid","23616088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29803"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0946-2716"],["dc.title","alpha-Synuclein and intracellular trafficking: impact on the spreading of Parkinson's disease pathology"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","889"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","890"],["dc.bibliographiccitation.volume","157"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2021-04-14T08:28:16Z"],["dc.date.available","2021-04-14T08:28:16Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract image"],["dc.description.abstract","The process of a‐syn aggregation is thought to be central in synucleinopathies, but has been difficult to study in the laboratory. Different models attempt to recapitulate specific aspects of the aggregation process. The BiFC assay uses engineered fusion proteins in order to enable the detection of a‐syn dimers and oligomers in living cells. As any model, it has strengths and limitations and, therefore, should only be regarded as a model for the study of basic molecular mechanisms involved in PD and other synucleinopathies. image"],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.identifier.doi","10.1111/jnc.15264"],["dc.identifier.pmid","33300125"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82557"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/100"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1471-4159"],["dc.relation.issn","0022-3042"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes."],["dc.title","Alpha‐synuclein oligomerization and aggregation: A model will always be a model"],["dc.title.alternative","This is a response to “Monitoring alpha‐synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get”. Read the reply on “Alpha‐Synuclein oligomerization and aggregation: All models are useful but only if we know what they model”. The articles are accompanied by a Preface “How good are cellular models?”."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Pathology"],["dc.bibliographiccitation.lastpage","25"],["dc.bibliographiccitation.volume","221"],["dc.contributor.author","Miranda, Hugo Vicente"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2022-03-01T11:46:30Z"],["dc.date.available","2022-03-01T11:46:30Z"],["dc.date.issued","2009"],["dc.identifier.doi","10.1002/path.2682"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103693"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0022-3417"],["dc.title","The sour side of neurodegenerative disorders: the effects of protein glycation"],["dc.title.alternative","Effects of protein glycation in neurodegenerative disorders"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","1122.e23"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Neurobiology of Aging"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Kemppainen, Susanna"],["dc.contributor.author","Rantamaki, Tomi"],["dc.contributor.author","Jeronimo-Santos, Andre"],["dc.contributor.author","Lavasseur, Gregoire"],["dc.contributor.author","Autio, Henri"],["dc.contributor.author","Karpova, Nina"],["dc.contributor.author","Karkkainen, Elisa"],["dc.contributor.author","Staven, Saara"],["dc.contributor.author","Vicente Miranda, Hugo"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Diogenes, Maria Jose"],["dc.contributor.author","Laroche, Serge"],["dc.contributor.author","Davis, Sabrina"],["dc.contributor.author","Sebastiao, Ana Maria"],["dc.contributor.author","Castren, Eero"],["dc.contributor.author","Tanila, Heikki"],["dc.date.accessioned","2018-11-07T09:10:09Z"],["dc.date.available","2018-11-07T09:10:09Z"],["dc.date.issued","2012"],["dc.description.abstract","Brain-derived neurotrophic factor (BDNF) plays an important role in neuronal plasticity, learning, and memory. Levels of BDNF and its main receptor TrkB (TrkB.TK) have been reported to be decreased while the levels of the truncated TrkB (TrkB.T1) are increased in Alzheimer's disease. We show here that incubation with amyloid-beta increased TrkB.T1 receptor levels and decreased TrkB.TK levels in primary neurons. In vivo, APPswe/PS1dE9 transgenic mice (APdE9) showed an age-dependent relative increase in cortical but not hippocampal TrkB.T1 receptor levels compared with TrkB.TK. To investigate the role of TrkB isoforms in Alzheimer's disease, we crossed AP mice with mice overexpressing the truncated TrkB.T1 receptor (T1) or the full-length TrkB.TK isoform. Overexpression of TrkB.T1 in APdE9 mice exacerbated their spatial memory impairment while the overexpression of TrkB.TK alleviated it. These data suggest that amyloid-beta changes the ratio between TrkB isoforms in favor of the dominant-negative TrkB.T1 isoform both in vitro and in vivo and supports the role of BDNF signaling through TrkB in the pathophysiology and cognitive deficits of Alzheimer's disease. (C) 2012 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.neurobiolaging.2011.11.006"],["dc.identifier.isi","000303197100016"],["dc.identifier.pmid","22209410"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26426"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","1558-1497"],["dc.relation.issn","0197-4580"],["dc.title","Impaired TrkB receptor signaling contributes to memory impairment in APP/PS1 mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5724"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Morato Torres, C. Alejandra"],["dc.contributor.author","Wassouf, Zinah"],["dc.contributor.author","Zafar, Faria"],["dc.contributor.author","Sastre, Danuta"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Schüle, Birgitt"],["dc.date.accessioned","2021-04-14T08:23:46Z"],["dc.date.available","2021-04-14T08:23:46Z"],["dc.date.issued","2020"],["dc.description.abstract","Neurodevelopmental and late-onset neurodegenerative disorders present as separate entities that are clinically and neuropathologically quite distinct. However, recent evidence has highlighted surprising commonalities and converging features at the clinical, genomic, and molecular level between these two disease spectra. This is particularly striking in the context of autism spectrum disorder (ASD) and Parkinson’s disease (PD). Genetic causes and risk factors play a central role in disease pathophysiology and enable the identification of overlapping mechanisms and pathways. Here, we focus on clinico-genetic studies of causal variants and overlapping clinical and cellular features of ASD and PD. Several genes and genomic regions were selected for our review, including SNCA (alpha-synuclein), PARK2 (parkin RBR E3 ubiquitin protein ligase), chromosome 22q11 deletion/DiGeorge region, and FMR1 (fragile X mental retardation 1) repeat expansion, which influence the development of both ASD and PD, with converging features related to synaptic function and neurogenesis. Both PD and ASD display alterations and impairments at the synaptic level, representing early and key disease phenotypes, which support the hypothesis of converging mechanisms between the two types of diseases. Therefore, understanding the underlying molecular mechanisms might inform on common targets and therapeutic approaches. We propose to re-conceptualize how we understand these disorders and provide a new angle into disease targets and mechanisms linking neurodevelopmental disorders and neurodegeneration."],["dc.identifier.doi","10.3390/ijms21165724"],["dc.identifier.pmid","32785033"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81042"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/163"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/98"],["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","1422-0067"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","CC BY 4.0"],["dc.title","The Role of Alpha-Synuclein and Other Parkinson’s Genes in Neurodevelopmental and Neurodegenerative 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.firstpage","109"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Annals of Neurology"],["dc.bibliographiccitation.lastpage","118"],["dc.bibliographiccitation.volume","74"],["dc.contributor.author","Taschenberger, G."],["dc.contributor.author","Toloe, J."],["dc.contributor.author","Tereshchenko, J."],["dc.contributor.author","Akerboom, J."],["dc.contributor.author","Wales, P."],["dc.contributor.author","Benz, R."],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Outeiro, T. F."],["dc.contributor.author","Looger, L. L."],["dc.contributor.author","Bähr, M."],["dc.contributor.author","Zweckstetter, M."],["dc.contributor.author","Kügler, Sebastian"],["dc.date.accessioned","2017-09-07T11:47:39Z"],["dc.date.available","2017-09-07T11:47:39Z"],["dc.date.issued","2013"],["dc.description.abstract","ObjectiveWhereas the contribution of -synuclein to neurodegeneration in Parkinson disease is well accepted, the putative impact of its close homologue, -synuclein, is enigmatic. -Synuclein is widely expressed throughout the central nervous system, as is -synuclein, but the physiological functions of both proteins remain unknown. Recent findings have supported the view that -synuclein can act as an ameliorating regulator of -synuclein-induced neurotoxicity, having neuroprotective rather than neurodegenerative capabilities, and being nonaggregating due to the absence of most of the aggregation-promoting NAC domain. However, a mutation of -synuclein linked to dementia with Lewy bodies rendered the protein neurotoxic in transgenic mice, and fibrillation of -synuclein has been demonstrated in vitro. MethodsNeurotoxicity and aggregation properties of -, -, and -synuclein were comparatively elucidated in the rat nigro-striatal projection and in cultured neurons. ResultsSupporting the hypothesis that -synuclein can act as a neurodegeneration-inducing factor, we demonstrated that wild-type -synuclein is neurotoxic for cultured primary neurons. Furthermore, -synuclein formed proteinase K-resistant aggregates in dopaminergic neurons in vivo, leading to pronounced and progressive neurodegeneration in rats. Expression of -synuclein caused mitochondrial fragmentation, but this fragmentation did not render mitochondria nonfunctional in terms of ion handling and respiration even at late stages of neurodegeneration. A comparison of the neurodegenerative effects induced by -, -, and -synuclein revealed that -synuclein was eventually as neurotoxic as -synuclein for nigral dopaminergic neurons, whereas -synuclein proved to be nontoxic and had very low aggregation propensity. InterpretationOur results suggest that the role of -synuclein as a putative modulator of neuropathology in aggregopathies like Parkinson disease and dementia with Lewy bodies needs to be revisited. Ann Neurol 2013;74:109-118"],["dc.identifier.doi","10.1002/ana.23905"],["dc.identifier.gro","3142329"],["dc.identifier.isi","000329198600014"],["dc.identifier.pmid","23536356"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7075"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1531-8249"],["dc.relation.issn","0364-5134"],["dc.title","β-Synuclein Aggregates and Induces Neurodegeneration in Dopaminergic Neurons"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]