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.bibliographiccitation.firstpage","438"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","452"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Tenreiro, Sandra"],["dc.contributor.author","Munder, Matthias C."],["dc.contributor.author","Alberti, Simon"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2018-11-07T09:18:09Z"],["dc.date.available","2018-11-07T09:18:09Z"],["dc.date.issued","2013"],["dc.description.abstract","Several neurodegenerative diseases, such as Parkinson's disease (PD), Alzheimer's disease (AD), Huntington's disease (HD), amyotrophic lateral sclerosis (ALS), or prion diseases, are known for their intimate association with protein misfolding and aggregation. These disorders are characterized by the loss of specific neuronal populations in the brain and are highly associated with aging, suggesting a decline in proteostasis capacity may contribute to pathogenesis. Nevertheless, the precise molecular mechanisms that lead to the selective demise of neurons remain poorly understood. As a consequence, appropriate therapeutic approaches and effective treatments are largely lacking. The development of cellular and animal models that faithfully reproduce central aspects of neurodegeneration has been crucial for advancing our understanding of these diseases. Approaches involving the sequential use of different model systems, starting with simpler cellular models and ending with validation in more complex animal models, resulted in the discovery of promising therapeutic targets and small molecules with therapeutic potential. Within this framework, the simple and well-characterized eukaryote Saccharomyces cerevisiae, also known as budding yeast, is being increasingly used to study the molecular basis of several neurodegenerative disorders. Yeast provides an unprecedented toolbox for the dissection of complex biological processes and pathways. Here, we summarize how yeast models are adding to our current understanding of several neurodegenerative disorders."],["dc.identifier.doi","10.1111/jnc.12271"],["dc.identifier.isi","000326467000004"],["dc.identifier.pmid","23600759"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28340"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1471-4159"],["dc.relation.issn","0022-3042"],["dc.title","Harnessing the power of yeast to unravel the molecular basis of neurodegeneration"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","FEMS Yeast Research"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Ferreira, Carla"],["dc.contributor.author","Couceiro, Joana"],["dc.contributor.author","Família, Carlos"],["dc.contributor.author","Jardim, Carolina"],["dc.contributor.author","Antas, Pedro"],["dc.contributor.author","Santos, Cláudia N"],["dc.contributor.author","Outeiro, Tiago F"],["dc.contributor.author","Tenreiro, Sandra"],["dc.contributor.author","Quintas, Alexandre"],["dc.date.accessioned","2020-12-10T18:19:12Z"],["dc.date.available","2020-12-10T18:19:12Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1093/femsyr/foz042"],["dc.identifier.eissn","1567-1364"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75158"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The synthetic cannabinoid JWH-018 modulates Saccharomyces cerevisiae energetic metabolism"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4065"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - General Subjects"],["dc.bibliographiccitation.lastpage","4072"],["dc.bibliographiccitation.volume","1830"],["dc.contributor.author","Faria, Cristiana"],["dc.contributor.author","Jorge, Carla D."],["dc.contributor.author","Borges, Nuno"],["dc.contributor.author","Tenreiro, Sandra"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Santos, Helena"],["dc.date.accessioned","2018-11-07T09:22:04Z"],["dc.date.available","2018-11-07T09:22:04Z"],["dc.date.issued","2013"],["dc.description.abstract","Background: Protein aggregation in the brain is a central hallmark in many neurodegenerative diseases. In Parkinson's disease, alpha-synuclein (alpha-Syn) is the major component of the intraneuronal inclusions found in the brains of patients. Current therapeutics is merely symptomatic, and there is a pressing need for developing novel therapies. Previously we showed that mannosylglycerate (MG), a compatible solute typical of marine microorganisms thriving in hot environments, is highly effective in protecting a variety of model proteins against thermal denaturation and aggregation in vitro. Methods: Saccharomyces cerevisiae cells expressing eGFP-tagged alpha-Syn, were further engineered to synthesize MG. The number of cells with fluorescent foci was assessed by fluorescence microscopy. Fluorescence spectroscopy and transmission electron microscopy were used to monitor fibril formation in vitro. Results: We observed a 3.3-fold reduction in the number of cells with alpha-Syn foci and mild attenuation of alpha-Syn-induced toxicity. Accordingly, sucrose gradient analysis confirmed a clear reduction in the size-range of alpha-Syn species in the cells. MG did not affect the expression levels of alpha-Syn or its degradation rate. Moreover, MG did not induce molecular chaperones (Hsp104, Hsp70 and Hsp40), suggesting the implication of other mechanisms for alpha-Syn stabilization. MG also inhibited alpha-Syn fibrillation in vitro. Conclusions: MG acts as a chemical chaperone and the stabilization mechanism involves direct solute/protein interactions. General significance: This is the first demonstration of the anti-aggregating ability of MG in the intracellular milieu. The work shows that MG is a good candidate to inspire the development of new drugs for protein-misfolding diseases. (c) 2013 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbagen.2013.04.015"],["dc.identifier.isi","000320896100007"],["dc.identifier.pmid","23608058"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29254"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0304-4165"],["dc.title","Inhibition of formation of alpha-synuclein inclusions by mannosylglycerate in a yeast model of Parkinson's disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","970"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","FEMS Yeast Research"],["dc.bibliographiccitation.lastpage","979"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Tenreiro, Sandra"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2022-03-01T11:47:09Z"],["dc.date.available","2022-03-01T11:47:09Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1111/j.1567-1364.2010.00649.x"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103931"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","1567-1356"],["dc.title","Simple is good: yeast models of neurodegeneration"],["dc.title.alternative","Yeast as a model for neurodegeneration"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","128"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Acta Neuropathologica Communications"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Dias, Mariana C."],["dc.contributor.author","Carija, Anita"],["dc.contributor.author","Navarro, Susanna"],["dc.contributor.author","Madaleno, Carolina S."],["dc.contributor.author","Tenreiro, Sandra"],["dc.contributor.author","Ventura, Salvador"],["dc.contributor.author","Outeiro, Tiago F."],["dc.date.accessioned","2019-07-09T11:42:53Z"],["dc.date.available","2019-07-09T11:42:53Z"],["dc.date.issued","2016"],["dc.description.abstract","Abstract α-synuclein (aSyn) is associated with both sporadic and familial forms of Parkinson’s disease (PD), the second most common neurodegenerative disorder after Alzheimer’s disease. In particular, multiplications and point mutations in the gene encoding for aSyn cause familial forms of PD. Moreover, the accumulation of aSyn in Lewy Bodies and Lewy neurites in disorders such as PD, dementia with Lewy bodies, or multiple system atrophy, suggests aSyn misfolding and aggregation plays an important role in these disorders, collectively known as synucleinopathies. The exact function of aSyn remains unclear, but it is known to be associated with vesicles and membranes, and to have an impact on important cellular functions such as intracellular trafficking and protein degradation systems, leading to cellular pathologies that can be readily studied in cell-based models. Thus, understanding the molecular effects of aSyn point mutations may provide important insight into the molecular mechanisms underlying disease onset. We investigated the effect of the recently identified A53E aSyn mutation. Combining in vitro studies with studies in cell models, we found that this mutation reduces aSyn aggregation and increases proteasome activity, altering normal proteostasis. We observed that, in our experimental paradigms, the A53E mutation affects specific steps of the aggregation process of aSyn and different cellular processes, providing novel ideas about the molecular mechanisms involved in synucleinopathies."],["dc.identifier.doi","10.1186/s40478-016-0402-8"],["dc.identifier.pmid","27938414"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13938"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58777"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","BioMed Central"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Macedo, Diana"],["dc.contributor.author","Tavares, Lucelia"],["dc.contributor.author","McDougall, Gordon J."],["dc.contributor.author","Stewart, Derek"],["dc.contributor.author","Ferreira, Ricardo B."],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Santos, Claudia N."],["dc.contributor.author","Tenreiro, Sandra"],["dc.date.accessioned","2018-11-07T09:20:14Z"],["dc.date.available","2018-11-07T09:20:14Z"],["dc.date.issued","2013"],["dc.format.extent","204"],["dc.identifier.isi","000327927400444"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28837"],["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","Polyphenols protect from alpha-synuclein toxicity by increasing autophagy and reducing reactive oxygen species in a yeast model of Parkinson's disease"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","FEMS Yeast Research"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Brás, Inês Caldeira"],["dc.contributor.author","Tenreiro, Sandra"],["dc.contributor.author","Silva, Andreia M"],["dc.contributor.author","Outeiro, Tiago F"],["dc.date.accessioned","2020-12-10T18:19:12Z"],["dc.date.available","2020-12-10T18:19:12Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1093/femsyr/foy108"],["dc.identifier.eissn","1567-1364"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75157"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Identification of novel protein phosphatases as modifiers of alpha-synuclein aggregation in yeast"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1717"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Human Molecular Genetics"],["dc.bibliographiccitation.lastpage","1732"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Macedo, Diana"],["dc.contributor.author","Tavares, Lucelia"],["dc.contributor.author","McDougall, Gordon J."],["dc.contributor.author","Vicente Miranda, Hugo"],["dc.contributor.author","Stewart, Derek"],["dc.contributor.author","Ferreira, Ricardo B."],["dc.contributor.author","Tenreiro, Sandra"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Santos, Claudia N."],["dc.date.accessioned","2018-11-07T09:59:39Z"],["dc.date.available","2018-11-07T09:59:39Z"],["dc.date.issued","2015"],["dc.description.abstract","Parkinson's disease (PD) is the most common movement neurodegenerative disorder and is associated with the aggregation of alpha-synuclein (alpha Syn) and oxidative stress, hallmarks of the disease. Although the precise molecular events underlying alpha Syn aggregation are still unclear, oxidative stress is known to contribute to this process. Therefore, agents that either prevent oxidative stress or inhibit alpha Syn toxicity are expected to constitute potential drug leads for PD. Both pre-clinical and clinical studies provided evidence that (poly) phenols, pure or in extracts, might protect against neurodegenerative disorders associated with oxidative stress in the brain. In this study, we analyzed, for the first time, a (poly) phenol-enriched fraction (PEF) from leaves of Corema album, and used in vitro and cellular models to evaluate its effects on alpha Syn toxicity and aggregation. Interestingly, the PEF promoted the formation of non-toxic alpha Syn species in vitro, and inhibited its toxicity and aggregation in cells, by promoting the autophagic flux and reducing oxidative stress. Thus, C. album (poly) phenols appear as promising cytoprotective compounds, modulating central events in the pathogenesis of PD, such as alpha Syn aggregation and the impairment of autophagy. Ultimately, the understanding of the molecular effects of (poly) phenols will open novel opportunities for the exploitation of their beneficial effects and for drug development."],["dc.identifier.doi","10.1093/hmg/ddu585"],["dc.identifier.isi","000350144200017"],["dc.identifier.pmid","25432533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37641"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1460-2083"],["dc.relation.issn","0964-6906"],["dc.title","(Poly)phenols protect from alpha-synuclein toxicity by reducing oxidative stress and promoting autophagy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3949"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Lab on a Chip"],["dc.bibliographiccitation.lastpage","3957"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Fernandes, Joao Tiago S."],["dc.contributor.author","Tenreiro, Sandra"],["dc.contributor.author","Gameiro, Andreia"],["dc.contributor.author","Chu, Virginia"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Conde, Joao P."],["dc.date.accessioned","2018-11-07T09:33:29Z"],["dc.date.available","2018-11-07T09:33:29Z"],["dc.date.issued","2014"],["dc.description.abstract","Parkinson's disease (PD) is a common age-associated neurodegenerative disorder. The protein a-synuclein (aSyn) is a key factor in PD both due to its association with familial and sporadic cases and because it is the main component of the pathological protein aggregates known as Lewy bodies. However, the precise cellular effects of aSyn aggregation are still elusive. Here, we developed an elastomeric microftuldic device equipped with a chemical gradient generator and 9 chambers containing cell traps to study aSyn production and aggregation in Saccharomyces cerevisiae. This study involved capturing single cells, exposing them to specific chemical environments and imaging the expression of aSyn by means of a GFP fusion (aSyn-GFP). Using a galactose (GAL) gradient we modulated aSyn expression and, surprisingly, by tracking the behavior of single cells, we found that the response of individual cells in a population to a given stimulus can differ widely. To study the combined effect of environmental factors and aSyn expression levels, we exposed cells to a gradient of FeCl3. We found a dramatic increase in the percentage of cells displaying aSyn inclusions from 27% to 96%. Finally, we studied the effects of ascorbic acid, an antioxidant, on aSyn aggregation and found a significant reduction in the percentage of cells bearing aSyn inclusions from 87% to 37%. In summary, the device developed here offers a powerful way of studying aSyn biology with single-cell resolution and high throughput using genetically modified yeast cells."],["dc.identifier.doi","10.1039/c4lc00756e"],["dc.identifier.isi","000342866400006"],["dc.identifier.pmid","25167219"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11724"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31972"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc Chemistry"],["dc.relation.issn","1473-0189"],["dc.relation.issn","1473-0197"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Modulation of alpha-synuclein toxicity in yeast using a novel microfluidic-based gradient generator"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]