Villar-Piqué, Anna

[["dc.bibliographiccitation.firstpage","240"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","255"],["dc.bibliographiccitation.volume","139"],["dc.contributor.author","Villar-Pique, Anna"],["dc.contributor.author","da Fonseca, Tomas Lopes"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2018-11-07T10:07:22Z"],["dc.date.available","2018-11-07T10:07:22Z"],["dc.date.issued","2016"],["dc.description.abstract","Parkinson's disease belongs to a group of currently incurable neurodegenerative disorders characterized by the misfolding and accumulation of alpha-synuclein aggregates that are commonly known as synucleinopathies. Clinically, synucleinopathies are heterogeneous, reflecting the somewhat selective neuronal vulnerability characteristic of each disease. The precise molecular underpinnings of synucleinopathies remain unclear, but the process of aggregation of alpha-synuclein appears as a central event. However, there is still no consensus with respect to the toxic forms of alpha-synuclein, hampering our ability to use the protein as a target for therapeutic intervention. To decipher the molecular bases of synucleinopathies, it is essential to understand the complex triangle formed between the structure, function and toxicity of alpha-synuclein. Recently, important steps have been undertaken to elucidate the role of the protein in both physiological and pathological conditions. Here, we provide an overview of recent findings in the field of alpha-synuclein research, and put forward a new perspective over paradigms that persist in the field. Establishing whether alpha-synuclein has a causative role in all synucleinopathies will enable the identification of targets for the development of novel therapeutic strategies for this devastating group of disorders. Alpha-synuclein is the speculated cornerstone of several neurodegenerative disorders known as Synucleinopathies. Nevertheless, the mechanisms underlying the pathogenic effects of this protein remain unknown. Here, we review the recent findings in the three corners of alpha-synuclein biology - structure, function and toxicity - and discuss the enigmatic roads that have accompanied alpha-synuclein from the beginning. This article is part of a ."],["dc.identifier.doi","10.1111/jnc.13249"],["dc.identifier.isi","000385770500016"],["dc.identifier.pmid","26190401"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39265"],["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","Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1863"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","1874"],["dc.bibliographiccitation.volume","57"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Candelise, Niccolo"],["dc.contributor.author","Kanata, Eirini"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Thüne, Katrin"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","da Silva Correia, Susana Margarida"],["dc.contributor.author","Dafou, Dimitra"],["dc.contributor.author","Sklaviadis, Theodoros"],["dc.contributor.author","Appelhans, Dietmar"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T14:14:28Z"],["dc.date.available","2020-12-10T14:14:28Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/s12035-019-01837-w"],["dc.identifier.eissn","1559-1182"],["dc.identifier.issn","0893-7648"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71354"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Validation of Poly(Propylene Imine) Glycodendrimers Towards Their Anti-prion Conversion Efficiency"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","691"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Annals of Neurology"],["dc.bibliographiccitation.lastpage","703"],["dc.bibliographiccitation.volume","85"],["dc.contributor.author","Candelise, Niccolò"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Villar‐Piqué, Anna"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Thom, Tobias"],["dc.contributor.author","Silva Correia, Susana Margarida"],["dc.contributor.author","Cunha, José Eriton Gomes"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2021-06-01T10:49:23Z"],["dc.date.available","2021-06-01T10:49:23Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1002/ana.25446"],["dc.identifier.pmid","30805957"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86271"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/82"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B08: Definition von Kaskaden molekularer Veränderungen bei Synucleinopathien während der Neurodegeneration"],["dc.relation.eissn","1531-8249"],["dc.relation.issn","0364-5134"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.title","Seeding variability of different alpha synuclein strains in synucleinopathies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","461"],["dc.bibliographiccitation.journal","Alzheimer's & Dementia: Diagnosis, Assessment & Disease Monitoring"],["dc.bibliographiccitation.lastpage","470"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Kruse, Niels"],["dc.contributor.author","Heslegrave, Amanda"],["dc.contributor.author","Gupta, Vandana"],["dc.contributor.author","Foiani, Martha"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Lehmann, Sylvain"],["dc.contributor.author","Teunissen, Charlotte"],["dc.contributor.author","Blennow, Kaj"],["dc.contributor.author","Zetterberg, Henrik"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Llorens, Franc"],["dc.date.accessioned","2019-07-09T11:49:35Z"],["dc.date.available","2019-07-09T11:49:35Z"],["dc.date.issued","2018"],["dc.description.abstract","ntroduction: Cerebrospinal fluid α-synuclein level is increased in sporadic Creutzfeldt-Jakob disease cases. However, the clinical value of this biomarker remains to be established. In this study, we have addressed the clinical validation parameters and the interlaboratory reproducibility by using an electrochemiluminescent assay. Methods: Cerebrospinal fluid α-synuclein was quantified in a total of 188 sporadic Creutzfeldt-Jakob disease and non-Creutzfeldt-Jakob-disease cases to determine sensitivity and specificity values and lot-to-lot variability. Two round robin tests with 70 additional cases were performed in six independent laboratories. Results: A sensitivity of 93% and a specificity of 96% were achieved in discriminating sporadic Creutzfeldt-Jakob disease. No differences were detected between lots. The mean interlaboratory coefficient of variation was 23%, and the intralaboratory coefficient of variations ranged 2.70%-11.39%. Overall, 97% of samples were correctly diagnosed. Discussion: The herein validated α-synuclein assay is robust, accurate, and reproducible in identifying Creutzfeldt-Jakob disease cases. Thus, it is ready for implementation in the clinical practice to support the diagnosis of Creutzfeldt-Jakob disease."],["dc.identifier.doi","10.1016/j.dadm.2018.06.005"],["dc.identifier.pmid","30294658"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15718"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59586"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.subject.ddc","610"],["dc.title","Interlaboratory validation of cerebrospinal fluid α-synuclein quantification in the diagnosis of sporadic Creutzfeldt-Jakob disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","290"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biomolecules"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Hermann, Peter"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Calero, Olga"],["dc.contributor.author","Stehmann, Christiane"],["dc.contributor.author","Sarros, Shannon"],["dc.contributor.author","Moda, Fabio"],["dc.contributor.author","Ferrer, Isidre"],["dc.contributor.author","Poleggi, Anna"],["dc.contributor.author","Pocchiari, Maurizio"],["dc.contributor.author","Catania, Marcella"],["dc.contributor.author","Klotz, Sigrid"],["dc.contributor.author","O’Regan, Carl"],["dc.contributor.author","Brett, Francesca"],["dc.contributor.author","Heffernan, Josephine"],["dc.contributor.author","Ladogana, Anna"],["dc.contributor.author","Collins, Steven J."],["dc.contributor.author","Calero, Miguel"],["dc.contributor.author","Kovacs, Gabor G."],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T18:46:57Z"],["dc.date.available","2020-12-10T18:46:57Z"],["dc.date.issued","2020"],["dc.description.sponsorship","Instituto de Salud Carlos III"],["dc.identifier.doi","10.3390/biom10020290"],["dc.identifier.eissn","2218-273X"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17338"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78594"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","MDPI"],["dc.relation.eissn","2218-273X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Diagnostic Accuracy of Prion Disease Biomarkers in Iatrogenic Creutzfeldt-Jakob Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","UNSP 140221"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Open Biology"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","de Groot, Natalia Sanchez"],["dc.contributor.author","Gomes, Ricardo A."],["dc.contributor.author","Villar-Pique, Anna"],["dc.contributor.author","Babu, M. Madan"],["dc.contributor.author","Coelho, Ana Varela"],["dc.contributor.author","Ventura, Salvador"],["dc.date.accessioned","2018-11-07T10:01:15Z"],["dc.date.available","2018-11-07T10:01:15Z"],["dc.date.issued","2015"],["dc.description.abstract","Proteins adopt defined structures and are crucial to most cellular functions. Their misfolding and aggregation is associated with numerous degenerative human disorders such as type II diabetes, Huntington's or Alzheimer's diseases. Here, we aim to understand why cells promote the formation of protein foci. Comparison of two amyloid-b-peptide variants, mostly insoluble but differently recruited by the cell (inclusion body versus diffused), reveals small differences in cell fitness and proteome response. We suggest that the levels of oxidative stress act as a sensor to trigger protein recruitment into foci. Our data support a common cytoplasmic response being able to discern and react to the specific properties of polypeptides."],["dc.identifier.doi","10.1098/rsob.140221"],["dc.identifier.isi","000351921700005"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11768"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37976"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc"],["dc.relation.issn","2046-2441"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Proteome response at the edge of protein aggregation"],["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"]]

[["dc.bibliographiccitation.artnumber","86"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Alzheimer's Research & Therapy"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Hermann, Peter"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Varges, Daniela"],["dc.contributor.author","Ferrer, Isidre"],["dc.contributor.author","Riggert, Joachim"],["dc.contributor.author","Zetterberg, Henrik"],["dc.contributor.author","Blennow, Kaj"],["dc.contributor.author","Llorens, Franc"],["dc.date.accessioned","2021-06-01T09:42:16Z"],["dc.date.accessioned","2022-08-18T12:38:53Z"],["dc.date.available","2021-06-01T09:42:16Z"],["dc.date.available","2022-08-18T12:38:53Z"],["dc.date.issued","2021-04-21"],["dc.date.updated","2022-07-29T12:17:47Z"],["dc.description.abstract","Abstract\r\n \r\n Background\r\n Blood neurofilament light (Nfl) and total-tau (t-tau) have been described to be increased in several neurological conditions, including prion diseases and other neurodegenerative dementias. Here, we aim to determine the accuracy of plasma Nfl and t-tau in the differential diagnosis of neurodegenerative dementias and their potential value as prognostic markers of disease severity.\r\n \r\n \r\n Methods\r\n Plasma Nfl and t-tau were measured in healthy controls (HC, n = 70), non-neurodegenerative neurological disease with (NND-Dem, n = 17) and without dementia syndrome (NND, n = 26), Alzheimer’s disease (AD, n = 44), Creutzfeldt-Jakob disease (CJD, n = 83), dementia with Lewy bodies/Parkinson’s disease with dementia (DLB/PDD, n = 35), frontotemporal dementia (FTD, n = 12), and vascular dementia (VaD, n = 22). Biomarker diagnostic accuracies and cutoff points for the diagnosis of CJD were calculated, and associations between Nfl and t-tau concentrations with other fluid biomarkers, demographic, genetic, and clinical data in CJD cases were assessed. Additionally, the value of Nfl and t-tau predicting disease survival in CJD was evaluated.\r\n \r\n \r\n Results\r\n Among diagnostic groups, highest plasma Nfl and t-tau concentrations were detected in CJD (fold changes of 38 and 18, respectively, compared to HC). Elevated t-tau was able to differentiate CJD from all other groups, whereas elevated Nfl concentrations were also detected in NND-Dem, AD, DLB/PDD, FTD, and VaD compared to HC. Both biomarkers discriminated CJD from non-CJD dementias with an AUC of 0.93. In CJD, plasma t-tau, but not Nfl, was associated with PRNP codon 129 genotype and CJD subtype. Positive correlations were observed between plasma Nfl and t-tau concentrations, as well as between plasma and CSF concentrations of both biomarkers (p < 0.001). Nfl was increased in rapidly progressive AD (rpAD) compared to slow progressive AD (spAD) and associated to Mini-Mental State Examination results. However, Nfl displayed higher accuracy than t-tau discriminating CJD from rpAD and spAD. Finally, plasma t-tau, but not plasma Nfl, was significantly associated with disease duration, offering a moderate survival prediction capacity.\r\n \r\n \r\n Conclusions\r\n Plasma Nfl and t-tau are useful complementary biomarkers for the differential diagnosis of CJD. Additionally, plasma t-tau emerges as a potential prognostic marker of disease duration."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.citation","Alzheimer's Research & Therapy. 2021 Apr 21;13(1):86"],["dc.identifier.doi","10.1186/s13195-021-00815-6"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17765"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85196"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112965"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","BioMed Central"],["dc.relation.eissn","1758-9193"],["dc.rights","CC BY 4.0"],["dc.rights.holder","The Author(s)"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject","Dementia"],["dc.subject","Creutzfeldt-Jakob disease"],["dc.subject","Biomarkers"],["dc.subject","Plasma"],["dc.subject","Neurofilament light"],["dc.subject","Tau"],["dc.subject","Diagnosis"],["dc.subject","Disease progression"],["dc.title","Diagnostic and prognostic value of plasma neurofilament light and total-tau in sporadic Creutzfeldt-Jakob disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","841"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Acta Neuropathologica"],["dc.bibliographiccitation.lastpage","859"],["dc.bibliographiccitation.volume","141"],["dc.contributor.author","Diaz-Lucena, Daniela"],["dc.contributor.author","Kruse, Niels"],["dc.contributor.author","Thüne, Katrin"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","da Cunha, Jose Eriton Gomes"],["dc.contributor.author","Hermann, Peter"],["dc.contributor.author","López-Pérez, Óscar"],["dc.contributor.author","Andrés-Benito, Pol"],["dc.contributor.author","Llorens, Franc"],["dc.date.accessioned","2021-06-01T09:42:50Z"],["dc.date.available","2021-06-01T09:42:50Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Triggering receptor expressed on myeloid cells 2 (TREM2) is an innate immune cell surface receptor that regulates microglial function and is involved in the pathophysiology of several neurodegenerative diseases. Its soluble form (sTREM2) results from shedding of the TREM2 ectodomain. The role of TREM2 in prion diseases, a group of rapidly progressive dementias remains to be elucidated. In the present study, we analysed the expression of TREM2 and its main sheddase ADAM10 in the brain of sporadic Creutzfeldt-Jakob disease (sCJD) patients and evaluated the role of CSF and plasma sTREM2 as a potential diagnostic marker of prion disease. Our data indicate that, compared to controls, TREM2 is increased in sCJD patient brains at the mRNA and protein levels in a regional and subtype dependent fashion, and expressed in a subpopulation of microglia. In contrast, ADAM10 is increased at the protein, but not the mRNA level, with a restricted neuronal expression. Elevated CSF sTREM2 is found in sCJD, genetic CJD with mutations E200K and V210I in the prion protein gene ( PRNP ), and iatrogenic CJD, as compared to healthy controls (HC) (AUC = 0.78–0.90) and neurological controls (AUC = 0.73–0.85), while CSF sTREM2 is unchanged in fatal familial insomnia. sTREM2 in the CSF of cases with Alzheimer’s disease, and multiple sclerosis was not significantly altered in our series. CSF sTREM2 concentrations in sCJD are PRNP codon 129 and subtype-related, correlate with CSF 14-3-3 positivity, total-tau and YKL-40, and increase with disease progression. In plasma, sTREM2 is increased in sCJD compared with HC (AUC = 0.80), displaying positive correlations with plasma total-tau, neurofilament light, and YKL-40. We conclude that comparative study of TREM2 in brain and biological fluids of prion diseases reveals TREM2 to be altered in human prion diseases with a potential value in target engagement, patient stratification, and disease monitoring."],["dc.identifier.doi","10.1007/s00401-021-02296-1"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85371"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1432-0533"],["dc.relation.issn","0001-6322"],["dc.title","TREM2 expression in the brain and biological fluids in prion diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","79"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Acta Neuropathologica Communications"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Masaracchia, Caterina"],["dc.contributor.author","Hnida, Marilena"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","Lopes da Fonseca, Tomás"],["dc.contributor.author","Villar-Pique, Anna"],["dc.contributor.author","Branco, Tiago"],["dc.contributor.author","Stahlberg, Markus A."],["dc.contributor.author","Dean, Camin"],["dc.contributor.author","Fernández, Claudio O."],["dc.contributor.author","Milošević, Ira"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2019-07-09T11:45:45Z"],["dc.date.available","2019-07-09T11:45:45Z"],["dc.date.issued","2018"],["dc.description.abstract","Abstract Alpha-synuclein (aSyn) plays a crucial role in Parkinson\\’s disease (PD) and other synucleinopathies, since it misfolds and accumulates in typical proteinaceous inclusions. While the function of aSyn is thought to be related to vesicle binding and trafficking, the precise molecular mechanisms linking aSyn with synucleinopathies are still obscure. aSyn can spread in a prion-like manner between interconnected neurons, contributing to the propagation of the pathology and to the progressive nature of synucleinopathies. Here, we investigated the interaction of aSyn with membranes and trafficking machinery pathways using cellular models of PD that are amenable to detailed molecular analyses. We found that different species of aSyn can enter cells and form high molecular weight species, and that membrane binding properties are important for the internalization of aSyn. Once internalized, aSyn accumulates in intracellular inclusions. Interestingly, we found that internalization is blocked in the presence of dynamin inhibitors (blocked membrane scission), suggesting the involvement of the endocytic pathway in the internalization of aSyn. By screening a pool of small Rab-GTPase proteins (Rabs) which regulate membrane trafficking, we found that internalized aSyn partially colocalized with Rab5A and Rab7. Initially, aSyn accumulated in Rab4A-labelled vesicles and, at later stages, it reached the autophagy-lysosomal pathway (ALP) where it gets degraded. In total, our study emphasizes the importance of membrane binding, not only as part of the normal function but also as an important step in the internalization and subsequent accumulation of aSyn. Importantly, we identified a fundamental role for Rab proteins in the modulation of aSyn processing, clearance and spreading, suggesting that targeting Rab proteins may hold important therapeutic value in PD and other synucleinopathies."],["dc.identifier.doi","10.1186/s40478-018-0578-1"],["dc.identifier.pmid","30107856"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15309"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59304"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/98"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/36"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P02: Charakterisierung der ER-Mitochondrien-Kontakte und ihre Rolle in der Signalweiterleitung"],["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 Milosevic (Synaptic Vesicle Dynamics)"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Membrane binding, internalization, and sorting of alpha-synuclein in the cell"],["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","172"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Biotechnology Journal"],["dc.bibliographiccitation.lastpage","177"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Villar-Pique, Anna"],["dc.contributor.author","Espargaro, Alba"],["dc.contributor.author","Ventura, Salvador"],["dc.contributor.author","Sabate, Raimon"],["dc.date.accessioned","2018-11-07T10:21:03Z"],["dc.date.available","2018-11-07T10:21:03Z"],["dc.date.issued","2016"],["dc.description.abstract","Amyloid polymerization underlies an increasing number of human diseases. Despite it having been studied extensively in vitro, aggregation is a difficult process to track in vivo due to methodological limitations and the slow kinetics of aggregation reactions in cells and tissues. Herein we exploit the amyloid properties of the inclusions bodies (IBs) formed by amyloidogenic proteins in bacteria to address the kinetics of in vivo amyloid aggregation. To this aim we used time-lapse confocal microscopy and a fusion of the amyloid-beta peptide (A beta 42) with a fluorescent reporter. This strategy allowed us to follow the intracellular kinetics of amyloid-like aggregation in real-time and to discriminate between variants exhibiting different in vivo aggregation propensity. Overall, the approach opens the possibility to assess the impact of point mutations as well as potential anti-aggregation drugs in the process of amyloid formation in living cells."],["dc.identifier.doi","10.1002/biot.201500252"],["dc.identifier.isi","000370002300017"],["dc.identifier.pmid","26580000"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42010"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1860-7314"],["dc.relation.issn","1860-6768"],["dc.title","In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]