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","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.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"]]

[["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Canaslan, Sezgi"],["dc.contributor.author","Espinosa, Juan Carlos"],["dc.contributor.author","Fernández-Borges, Natalia"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Varges, Daniela"],["dc.contributor.author","Maass, Fabian"],["dc.contributor.author","Torres, Juan Maria"],["dc.contributor.author","Hermann, Peter"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2022-07-01T07:35:38Z"],["dc.date.available","2022-07-01T07:35:38Z"],["dc.date.issued","2022"],["dc.description.sponsorship"," Fundació La Marató de TV3 http://dx.doi.org/10.13039/100008666"],["dc.description.sponsorship"," Alzheimer Forschung Initiative http://dx.doi.org/10.13039/100010146"],["dc.description.sponsorship","Robert Koch-Institute through funds of the Federal Ministry of Health"],["dc.description.sponsorship","CJD Foundation"],["dc.identifier.doi","10.1007/s12035-022-02891-7"],["dc.identifier.pii","2891"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112222"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.eissn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.rights.uri","https://www.springer.com/tdm"],["dc.title","Validation of Plasma and CSF Neurofilament Light Chain as an Early Marker for Sporadic Creutzfeldt-Jakob Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","E6506"],["dc.bibliographiccitation.issue","42"],["dc.bibliographiccitation.journal","PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA"],["dc.bibliographiccitation.lastpage","E6515"],["dc.bibliographiccitation.volume","113"],["dc.contributor.author","Villar-Pique, Anna"],["dc.contributor.author","da Fonseca, Tomas Lopes"],["dc.contributor.author","Sant'Anna, Ricardo"],["dc.contributor.author","Szegoe, Eva Monika"],["dc.contributor.author","Fonseca-Ornelas, Luis"],["dc.contributor.author","Pinho, Raquel"],["dc.contributor.author","Carija, Anita"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","Masaracchia, Caterina"],["dc.contributor.author","Gonzalez, Enrique Abad"],["dc.contributor.author","Rossetti, Giulia"],["dc.contributor.author","Carloni, Paolo"],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Foguel, Debora"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Ventura, Salvador"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2018-11-07T10:06:57Z"],["dc.date.available","2018-11-07T10:06:57Z"],["dc.date.issued","2016"],["dc.description.abstract","Synucleinopathies are a group of progressive disorders characterized by the abnormal aggregation and accumulation of alpha-synuclein (aSyn), an abundant neuronal protein that can adopt different conformations and biological properties. Recently, aSyn pathology was shown to spread between neurons in a prion-like manner. Proteins like aSyn that exhibit self-propagating capacity appear to be able to adopt different stable conformational states, known as protein strains, which can be modulated both by environmental and by protein-intrinsic factors. Here, we analyzed these factors and found that the unique combination of the neurodegeneration-related metal copper and the pathological H50Q aSyn mutation induces a significant alteration in the aggregation properties of aSyn. We compared the aggregation of WT and H50Q aSyn with and without copper, and assessed the effects of the resultant protein species when applied to primary neuronal cultures. The presence of copper induces the formation of structurally different and less-damaging aSyn aggregates. Interestingly, these aggregates exhibit a stronger capacity to induce aSyn inclusion formation in recipient cells, which demonstrates that the structural features of aSyn species determine their effect in neuronal cells and supports a lack of correlation between toxicity and inclusion formation. In total, our study provides strong support in favor of the hypothesis that protein aggregation is not a primary cause of cytotoxicity."],["dc.identifier.doi","10.1073/pnas.1606791113"],["dc.identifier.isi","000385610400024"],["dc.identifier.pmid","27708160"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39195"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Environmental and genetic factors support the dissociation between alpha-synuclein aggregation and toxicity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Brain"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Hermann, Peter"],["dc.contributor.author","Escaramís, Geòrgia"],["dc.contributor.author","Calero, Miguel"],["dc.contributor.author","Chen, Cao"],["dc.contributor.author","Kruse, Niels"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Golanska, Ewa"],["dc.contributor.author","Sikorska, Beata"],["dc.contributor.author","Llorens, Franc"],["dc.date.accessioned","2022-04-01T10:00:37Z"],["dc.date.available","2022-04-01T10:00:37Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract Genetic prion diseases are a rare and diverse group of fatal neurodegenerative disorders caused by pathogenic sequence variations in the prion protein gene, PRNP. Data on CSF biomarkers in patients with genetic prion diseases are limited and conflicting results have been reported for unclear reasons. Here, we aimed to analyse the diagnostic accuracy of CSF biomarkers currently used in prion clinical diagnosis in 302 symptomatic genetic prion disease cases from 11 prion diagnostic centres, encompassing a total of 36 different pathogenic sequence variations within the open reading frame of PRNP. CSF samples were assessed for the surrogate markers of neurodegeneration, 14-3-3 protein (14-3-3), total-tau protein (t-tau) and α-synuclein and for prion seeding activity through the real-time quaking-induced conversion assay. Biomarker results were compared with those obtained in healthy and neurological controls. For the most prevalent PRNP pathogenic sequence variations, biomarker accuracy and associations between biomarkers, demographic and genetic determinants were assessed. Additionally, the prognostic value of biomarkers for predicting total disease duration from symptom onset to death was investigated. High sensitivity of the four biomarkers was detected for genetic Creutzfeldt–Jakob disease associated with the E200K and V210I mutations, but low sensitivity was observed for mutations associated with Gerstmann–Sträussler–Scheinker syndrome and fatal familial insomnia. All biomarkers showed good to excellent specificity using the standard cut-offs often used for sporadic Creutzfeldt–Jakob disease. In genetic prion diseases related to octapeptide repeat insertions, the biomarker sensitivity correlated with the number of repeats. New genetic prion disease-specific cut-offs for 14-3-3, t-tau and α-synuclein were calculated. Disease duration in genetic Creutzfeldt–Jakob disease-E200K, Gerstmann–Sträussler–Scheinker-P102L and fatal familial insomnia was highly dependent on PRNP codon 129 MV polymorphism and was significantly associated with biomarker levels. In a large cohort of genetic prion diseases, the simultaneous analysis of CSF prion disease biomarkers allowed the determination of new mutation-specific cut-offs improving the discrimination of genetic prion disease cases and unveiled genetic prion disease-specific associations with disease duration."],["dc.identifier.doi","10.1093/brain/awab350"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/105472"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.eissn","1460-2156"],["dc.relation.issn","0006-8950"],["dc.title","Diagnostic accuracy of cerebrospinal fluid biomarkers in genetic prion diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2811"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","2821"],["dc.bibliographiccitation.volume","56"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Lachmann, Ingolf"],["dc.contributor.author","Karch, André"],["dc.contributor.author","Calero, Olga"],["dc.contributor.author","Stehmann, Christiane"],["dc.contributor.author","Sarros, Shannon"],["dc.contributor.author","Ladogana, Anna"],["dc.contributor.author","Poleggi, Anna"],["dc.contributor.author","Llorens, Franc"],["dc.date.accessioned","2021-06-01T10:49:20Z"],["dc.date.available","2021-06-01T10:49:20Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1007/s12035-018-1251-1"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86253"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.title","Cerebrospinal Fluid Total Prion Protein in the Spectrum of Prion Diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3476"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","3483"],["dc.bibliographiccitation.volume","56"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Gmitterová, Karin"],["dc.contributor.author","Hermann, Peter"],["dc.contributor.author","Varges, Daniela"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Lingor, Paul"],["dc.contributor.author","Vanderstichele, Hugo"],["dc.contributor.author","Demeyer, Leentje"],["dc.contributor.author","Stoops, Erik"],["dc.contributor.author","Trojanowski, John Q"],["dc.contributor.author","Lee, Virginia M-Y"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T14:14:28Z"],["dc.date.available","2020-12-10T14:14:28Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1007/s12035-018-1313-4"],["dc.identifier.eissn","1559-1182"],["dc.identifier.issn","0893-7648"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71351"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Cerebrospinal Fluid Total and Phosphorylated α-Synuclein in Patients with Creutzfeldt–Jakob Disease and Synucleinopathy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]