Fernandes Lázaro, Diana

[["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.artnumber","ddac104"],["dc.bibliographiccitation.journal","Human Molecular Genetics"],["dc.contributor.author","Schaffner, Samantha L"],["dc.contributor.author","Wassouf, Zinah"],["dc.contributor.author","Lazaro, Diana F"],["dc.contributor.author","Xylaki, Mary"],["dc.contributor.author","Gladish, Nicole"],["dc.contributor.author","Lin, David T S"],["dc.contributor.author","MacIsaac, Julia"],["dc.contributor.author","Ramadori, Katia"],["dc.contributor.author","Hentrich, Thomas"],["dc.contributor.author","Schulze-Hentrich, Julia M"],["dc.contributor.author","Kobor, Michael S"],["dc.date.accessioned","2022-06-01T09:39:21Z"],["dc.date.available","2022-06-01T09:39:21Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract Parkinson’s disease (PD) is a neurological disorder with complex interindividual etiology that is becoming increasingly prevalent worldwide. Elevated alpha-synuclein levels can increase risk of PD and may influence epigenetic regulation of PD pathways. Here, we report genome-wide DNA methylation and hydroxymethylation alterations associated with overexpression of two PD-linked alpha-synuclein variants (wild-type and A30P) in LUHMES cells differentiated to dopaminergic neurons. Alpha-synuclein altered DNA methylation at thousands of CpGs and DNA hydroxymethylation at hundreds of CpGs in both genotypes, primarily in locomotor behavior and glutamate signaling pathway genes. In some cases, epigenetic changes were associated with transcription. SMITE network analysis incorporating H3K4me1 ChIP-seq to score DNA methylation and hydroxymethylation changes across promoters, enhancers, and gene bodies confirmed epigenetic and transcriptional deregulation of glutamate signaling modules in both genotypes. Our results identify distinct and shared impacts of alpha-synuclein variants on the epigenome, and associate alpha-synuclein with the epigenetic etiology of PD."],["dc.identifier.doi","10.1093/hmg/ddac104"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108451"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation.eissn","1460-2083"],["dc.relation.issn","0964-6906"],["dc.title","Alpha-synuclein overexpression induces epigenomic dysregulation of glutamate signaling and locomotor pathways"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","16252"],["dc.bibliographiccitation.issue","45"],["dc.bibliographiccitation.journal","Dalton Transactions"],["dc.bibliographiccitation.lastpage","16267"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Cukierman, Daphne S."],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Sacco, Pamela"],["dc.contributor.author","Ferreira, Patrícia R."],["dc.contributor.author","Diniz, Renata"],["dc.contributor.author","Fernández, Claudio O."],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Rey, Nicolás A."],["dc.date.accessioned","2021-04-14T08:26:32Z"],["dc.date.available","2021-04-14T08:26:32Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1039/d0dt01138j"],["dc.identifier.pmid","32391542"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81982"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/53"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B08: Definition von Kaskaden molekularer Veränderungen bei Synucleinopathien während der Neurodegeneration"],["dc.relation.eissn","1477-9234"],["dc.relation.issn","1477-9226"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.title","X1INH, an improved next-generation affinity-optimized hydrazonic ligand, attenuates abnormal copper( i )/copper( ii )-α-Syn interactions and affects protein aggregation in a cellular model of synucleinopathy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","415"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Parkinson s Disease"],["dc.bibliographiccitation.lastpage","459"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Wales, Pauline"],["dc.contributor.author","Pinho, Raquel"],["dc.contributor.author","Lazaro, Diana F."],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2018-11-07T09:29:27Z"],["dc.date.available","2018-11-07T09:29:27Z"],["dc.date.issued","2013"],["dc.description.abstract","The pathogenesis of many neurodegenerative disorders arises in association with the misfolding and accumulation of a wide variety of proteins. Much emphasis has been placed on understanding the nature of these protein accumulations, including their composition, the process by which they are formed and the physiological impact they impose at cellular and, ultimately, organismal levels. Alpha-synuclein (ASYN) is the major component of protein inclusions known as Lewy bodies and Lewy neurites, which are the typical pathological hallmarks in disorders referred to as synucleinopathies. In addition, mutations or multiplications in the gene encoding for ASYN have also been shown to cause familial cases of PD, the most common synucleinopathy. Although the precise function of ASYN remains unclear, it appears to be involved in a vast array of cellular processes. Here, we review, in depth, a spectrum of cellular and molecular mechanisms that have been implicated in synucleinopathies. Importantly, detailed understanding of the biology/pathobiology of ASYN may enable the development of novel avenues for diagnosis and/or therapeutic intervention in synucleinopathies."],["dc.identifier.doi","10.3233/JPD-130216"],["dc.identifier.isi","000328332100001"],["dc.identifier.pmid","24270242"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31034"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Ios Press"],["dc.relation.issn","1877-718X"],["dc.relation.issn","1877-7171"],["dc.title","Limelight on Alpha-Synuclein: Pathological and Mechanistic Implications in Neurodegeneration"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1252"],["dc.bibliographiccitation.issue","11-12"],["dc.bibliographiccitation.journal","Israel Journal of Chemistry"],["dc.bibliographiccitation.lastpage","1259"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","Amen, Triana"],["dc.contributor.author","Lazaro, Diana F."],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Kaganovich, Daniel"],["dc.date.accessioned","2018-11-07T09:49:15Z"],["dc.date.available","2018-11-07T09:49:15Z"],["dc.date.issued","2015"],["dc.description.abstract","The budding yeast Saccharomyces cerevisiae has been extensively studied as a model organism for biochemical and genetic research for almost a century. In recent years, yeast has been successfully used to model many aspects of human diseases. These \"humanized\" yeast models have had a profound influence on our understanding of the molecular events underlying neurodegenerative disorders. Yeast models can recapitulate important molecular events that occur in neurodegeneration, and provide clues about the underpinnings of toxicity in animal models of disease. Moreover, yeast models have also served as a powerful tool for drug discovery. In this mini-review, we describe yeast models that have been used to study the molecular aspects of Parkinson's disease pathology and recent advances in the field based on these models."],["dc.identifier.doi","10.1002/ijch.201500071"],["dc.identifier.isi","000367077400011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35472"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1869-5868"],["dc.relation.issn","0021-2148"],["dc.title","Modeling Neuronal Pathology in Yeast: Insights into the Molecular Basis of Parkinson's Disease"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10481"],["dc.bibliographiccitation.issue","41"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","10486"],["dc.bibliographiccitation.volume","115"],["dc.contributor.author","Pujols, Jordi"],["dc.contributor.author","Peña-Díaz, Samuel"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Peccati, Francesca"],["dc.contributor.author","Pinheiro, Francisca"],["dc.contributor.author","González, Danilo"],["dc.contributor.author","Carija, Anita"],["dc.contributor.author","Navarro, Susanna"],["dc.contributor.author","Conde-Giménez, María"],["dc.contributor.author","García, Jesús"],["dc.contributor.author","Guardiola, Salvador"],["dc.contributor.author","Giralt, Ernest"],["dc.contributor.author","Salvatella, Xavier"],["dc.contributor.author","Sancho, Javier"],["dc.contributor.author","Sodupe, Mariona"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Dalfó, Esther"],["dc.contributor.author","Ventura, Salvador"],["dc.date.accessioned","2020-12-10T18:12:49Z"],["dc.date.available","2020-12-10T18:12:49Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1073/pnas.1804198115"],["dc.identifier.pmid","30249646"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74508"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/85"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["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 Outeiro (Experimental Neurodegeneration)"],["dc.title","Small molecule inhibits α-synuclein aggregation, disrupts amyloid fibrils, and prevents degeneration of dopaminergic neurons"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1769"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","ACS Chemical Neuroscience"],["dc.bibliographiccitation.lastpage","1779"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Dučić, Tanja"],["dc.contributor.author","Carboni, Eleonora"],["dc.contributor.author","Lai, Barry"],["dc.contributor.author","Chen, Si"],["dc.contributor.author","Michalke, Bernhard"],["dc.contributor.author","Lazaro, Diana F."],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Bähr, Mathias"],["dc.contributor.author","Barski, Elisabeth"],["dc.contributor.author","Lingor, Paul"],["dc.date.accessioned","2017-09-07T11:43:30Z"],["dc.date.available","2017-09-07T11:43:30Z"],["dc.date.issued","2015"],["dc.description.abstract","Manganese (Mn) may foster aggregation of alpha-synuclein (alpha Syn) contributing to the pathogenesis of PD. Here, we examined the influence of aSyn overexpression on distribution and oxidation states of Mn in frozen-hydrated primary midbrain neurons (PMNs) by synchrotron-based Xray fluorescence (XRF) and X-ray absorption near edge structure spectroscopy (XANES). Overexpression of aSyn increased intracellular Mn levels, whereas levels of Ca, Zn, K, P, and S were significantly decreased. Mn oxidation states were not altered. A strong correlation between Cu-/Mn-levels as well as Fe-/Mn-levels was observed in alpha Syn-overexpressing cells. Subcellular resolution revealed a punctate or filament-like perinuclear and neuritic distribution of Mn, which resembled the expression of DMT1 and MnSOD. While overexpression of aSyn did not significantly alter the expression patterns of the most-expressed Mn transport proteins (DMT1, VGCC, Fpn1), it attenuated the Mn release from Mn-treated neurons. Thus, these data suggest that aSyn may act as an intracellular Mn store. In total, neurotoxicity in PD could be mediated via regulation of transition metal levels and the metal-binding capacity of aSyn, which could represent a promising therapeutic target for this neurodegenerative disorder."],["dc.identifier.doi","10.1021/acschemneuro.5b00093"],["dc.identifier.gro","3141816"],["dc.identifier.isi","000363435300012"],["dc.identifier.pmid","26284970"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1390"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1948-7193"],["dc.title","Alpha-Synuclein Regulates Neuronal Levels of Manganese and Calcium"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1002601"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","PLOS Biology"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","de Oliveira, Rita Machado"],["dc.contributor.author","Vicente Miranda, Hugo"],["dc.contributor.author","Francelle, Laetitia"],["dc.contributor.author","Pinho, Raquel"],["dc.contributor.author","Szegö, Éva M."],["dc.contributor.author","Martinho, Renato"],["dc.contributor.author","Munari, Francesca"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Moniot, Sébastien"],["dc.contributor.author","Guerreiro, Patrícia"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2022-03-01T11:44:08Z"],["dc.date.available","2022-03-01T11:44:08Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1371/journal.pbio.1002601"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/102935"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1545-7885"],["dc.relation.iserratumof","/handle/2/43121"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Correction: The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","erratum_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","S1570963921000996"],["dc.bibliographiccitation.firstpage","140693"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta. Proteins and Proteomics"],["dc.bibliographiccitation.volume","1869"],["dc.contributor.author","Flores-León, Manuel"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Shvachiy, Liana"],["dc.contributor.author","Krisko, Anita"],["dc.contributor.author","Outeiro, Tiago F."],["dc.date.accessioned","2021-08-12T07:46:16Z"],["dc.date.available","2021-08-12T07:46:16Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.bbapap.2021.140693"],["dc.identifier.pii","S1570963921000996"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/88663"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-448"],["dc.relation.issn","1570-9639"],["dc.title","In silico analysis of the aggregation propensity of the SARS-CoV-2 proteome: Insight into possible cellular pathologies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","162"],["dc.bibliographiccitation.journal","Experimental Neurology"],["dc.bibliographiccitation.lastpage","171"],["dc.bibliographiccitation.volume","298"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Pavlou, Maria Angeliki S."],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2020-12-10T14:24:00Z"],["dc.date.available","2020-12-10T14:24:00Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1016/j.expneurol.2017.05.007"],["dc.identifier.issn","0014-4886"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72103"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Cellular models as tools for the study of the role of alpha-synuclein in Parkinson's disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]