Fernandes Lázaro, Diana

[["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.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.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Wang, Dan"],["dc.contributor.author","Rajavel, Abirami"],["dc.contributor.author","Dhamotharan, Karthikeyan"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Hoppert, Michael"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2021-06-01T09:42:26Z"],["dc.date.available","2021-06-01T09:42:26Z"],["dc.date.issued","2021"],["dc.description.abstract","Aggregation of α-synuclein (αSyn) into proteinaceous deposits is a pathological hallmark of a range of neurodegenerative diseases including Parkinson’s disease (PD). Numerous lines of evidence indicate that the accumulation of toxic oligomeric and prefibrillar αSyn species may underpin the cellular toxicity and spread of pathology between cells. Therefore, aggregation of αSyn is considered a priority target for drug development, as aggregation inhibitors are expected to reduce αSyn toxicity and serve as therapeutic agents. Here, we used the budding yeast S. cerevisiae as a platform for the identification of short peptides that inhibit αSyn aggregation and toxicity. A library consisting of approximately one million peptide variants was utilized in two high-throughput screening approaches for isolation of library representatives that reduce αSyn-associated toxicity and aggregation. Seven peptides were isolated that were able to suppress specifically αSyn toxicity and aggregation in living cells. Expression of the peptides in yeast reduced the accumulation of αSyn-induced reactive oxygen species and increased cell viability. Next, the peptides were chemically synthesized and probed for their ability to modulate αSyn aggregation in vitro . Two synthetic peptides, K84s and K102s, of 25 and 19 amino acids, respectively, significantly inhibited αSyn oligomerization and aggregation at sub-stoichiometric molar ratios. Importantly, K84s reduced αSyn aggregation in human cells. These peptides represent promising αSyn aggregation antagonists for the development of future therapeutic interventions."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3389/fnmol.2021.659926"],["dc.identifier.pmid","33912013"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17845"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85254"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/420"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1662-5099"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1006098"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLOS Genetics"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Kleinknecht, Alexandra"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Pinho, Raquel"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.editor","Lu, Bingwei"],["dc.date.accessioned","2018-09-28T07:41:43Z"],["dc.date.available","2018-09-28T07:41:43Z"],["dc.date.issued","2016"],["dc.description.abstract","Parkinson´s disease (PD) is characterized by the presence of proteinaceous inclusions called Lewy bodies that are mainly composed of α-synuclein (αSyn). Elevated levels of oxidative or nitrative stresses have been implicated in αSyn related toxicity. Phosphorylation of αSyn on serine 129 (S129) modulates autophagic clearance of inclusions and is prominently found in Lewy bodies. The neighboring tyrosine residues Y125, Y133 and Y136 are phosphorylation and nitration sites. Using a yeast model of PD, we found that Y133 is required for protective S129 phosphorylation and for S129-independent proteasome clearance. αSyn can be nitrated and form stable covalent dimers originating from covalent crosslinking of two tyrosine residues. Nitrated tyrosine residues, but not di-tyrosine-crosslinked dimers, contributed to αSyn cytotoxicity and aggregation. Analysis of tyrosine residues involved in nitration and crosslinking revealed that the C-terminus, rather than the N-terminus of αSyn, is modified by nitration and di-tyrosine formation. The nitration level of wild-type αSyn was higher compared to that of A30P mutant that is non-toxic in yeast. A30P formed more dimers than wild-type αSyn, suggesting that dimer formation represents a cellular detoxification pathway in yeast. Deletion of the yeast flavohemoglobin gene YHB1 resulted in an increase of cellular nitrative stress and cytotoxicity leading to enhanced aggregation of A30P αSyn. Yhb1 protected yeast from A30P-induced mitochondrial fragmentation and peroxynitrite-induced nitrative stress. Strikingly, overexpression of neuroglobin, the human homolog of YHB1, protected against αSyn inclusion formation in mammalian cells. In total, our data suggest that C-terminal Y133 plays a major role in αSyn aggregate clearance by supporting the protective S129 phosphorylation for autophagy and by promoting proteasome clearance. C-terminal tyrosine nitration increases pathogenicity and can only be partially detoxified by αSyn di-tyrosine dimers. Our findings uncover a complex interplay between S129 phosphorylation and C-terminal tyrosine modifications of αSyn that likely participates in PD pathology."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1371/journal.pgen.1006098"],["dc.identifier.pmid","27341336"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13384"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15831"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","1553-7404"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","C-Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α-Synuclein in a Yeast Model of Parkinson's Disease"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","105256"],["dc.bibliographiccitation.journal","Neurobiology of Disease"],["dc.bibliographiccitation.volume","151"],["dc.contributor.author","Dominguez-Meijide, Antonio"],["dc.contributor.author","Parrales, Valeria"],["dc.contributor.author","Vasili, Eftychia"],["dc.contributor.author","González-Lizárraga, Florencia"],["dc.contributor.author","König, Annekatrin"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Lannuzel, Annie"],["dc.contributor.author","Haik, Stéphane"],["dc.contributor.author","Del Bel, Elaine"],["dc.contributor.author","Chehín, Rosana"],["dc.contributor.author","Raisman-Vozari, Rita"],["dc.contributor.author","Michel, Patrick P."],["dc.contributor.author","Bizat, Nicolas"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2021-04-14T08:28:53Z"],["dc.date.available","2021-04-14T08:28:53Z"],["dc.date.issued","2021"],["dc.description.abstract","Parkinson's disease (PD) and dementia with Lewy bodies (DLB) are neurodegenerative disorders characterized by the misfolding and aggregation of alpha-synuclein (aSyn). Doxycycline, a tetracyclic antibiotic shows neuroprotective effects, initially proposed to be due to its anti-inflammatory properties. More recently, an additional mechanism by which doxycycline may exert its neuroprotective effects has been proposed as it has been shown that it inhibits amyloid aggregation. Here, we studied the effects of doxycycline on aSyn aggregation in vivo, in vitro and in a cell free system using real-time quaking induced conversion (RT-QuiC). Using H4, SH-SY5Y and HEK293 cells, we found that doxycycline decreases the number and size of aSyn aggregates in cells. In addition, doxycycline inhibits the aggregation and seeding of recombinant aSyn, and attenuates the production of mitochondrial-derived reactive oxygen species. Finally, we found that doxycycline induces a cellular redistribution of aggregates in a C.elegans animal model of PD, an effect that is associated with a recovery of dopaminergic function. In summary, we provide strong evidence that doxycycline treatment may be an effective strategy against synucleinopathies."],["dc.identifier.doi","10.1016/j.nbd.2021.105256"],["dc.identifier.pmid","33429042"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82728"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/223"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/105"],["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.issn","0969-9961"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Doxycycline inhibits α-synuclein-associated pathologies in vitro and in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1009407"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Wang, Dan"],["dc.contributor.author","Pätz, Christina"],["dc.contributor.author","Akkermann, Dagmar"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Galka, Dajana"],["dc.contributor.author","Kolog Gulko, Miriam"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2021-04-14T08:28:05Z"],["dc.date.available","2021-04-14T08:28:05Z"],["dc.date.issued","2021"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1371/journal.pgen.1009407"],["dc.identifier.pmid","33657088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82500"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/140"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.eissn","1553-7404"],["dc.relation.orgunit","Abteilung Molekulare Mikrobiologie & Genetik"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.rights","CC BY 4.0"],["dc.title","DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["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.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.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"]]