Villar-Piqué, Anna

[["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.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.journal","Frontiers in Bioengineering and Biotechnology"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","da Silva Correia, Susana Margarida"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Schmitz, Matthias"],["dc.date.accessioned","2021-04-14T08:31:15Z"],["dc.date.available","2021-04-14T08:31:15Z"],["dc.date.issued","2020"],["dc.description.abstract","The real-time quaking-induced conversion (RT-QuIC) assay is a highly reproducible and robust methodology exhibiting an excellent pre-mortem diagnostic accuracy for prion diseases. However, the protocols might be time-consuming and improvement of the detection technology is needed. In the present study, we investigated the influence of a pre-analytical cerebrospinal fluid (CSF) treatment with proteinase K (PK) on the kinetic of the RT-QuIC signal response. For this purpose, we added PK at different concentrations in RT-QuIC reactions seeded with Creutzfeldt–Jakob disease (sCJD) CSF. We observed that a mild pre-analytical PK treatment of CSF samples resulted in an increased seeding efficiency of the RT-QuIC reaction. Quantitative seeding parameters, such as a higher area under the curve (AUC) value or a shorter lag phase indicated a higher conversion efficiency after treatment. The diagnostic accuracy resulting from 2 μg/ml PK treatment was analyzed in a retrospective study, where we obtained a sensitivity of 89%. Additionally, we analyzed the agreement with the previously established standard RT-QuIC protocol without PK treatment in a prospective study. Here, we found an overall agreement of 94% to 96%. A Cohen’s kappa of 0.9036 (95% CI: 0.8114–0.9958) indicates an almost perfect agreement between both protocols. In conclusion, the outcome of our study can be used for a further optimization of the RT-QuIC assay in particular for a reduction of the testing time."],["dc.identifier.doi","10.3389/fbioe.2020.586890"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17661"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83533"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","2296-4185"],["dc.rights","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Optimization of the Real-Time Quaking-Induced Conversion Assay for Prion Disease Diagnosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Translational Neurodegeneration"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Candelise, Niccolo"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Thüne, Katrin"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Rabano, Alberto"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Stoops, Erik"],["dc.contributor.author","Vanderstichele, Hugo"],["dc.contributor.author","Villar-Pique, Anna"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T18:41:21Z"],["dc.date.available","2020-12-10T18:41:21Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1186/s40035-019-0181-9"],["dc.identifier.eissn","2047-9158"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17126"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77561"],["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","Effect of the micro-environment on α-synuclein conversion and implication in seeded conversion assays"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","800"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Biomolecules"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Schmitz, Vanda Edit"],["dc.contributor.author","Poleggi, Anna"],["dc.contributor.author","Pocchiari, Maurizio"],["dc.contributor.author","Sánchez-Valle, Raquel"],["dc.contributor.author","Calero, Miguel"],["dc.contributor.author","Calero, Olga"],["dc.contributor.author","Baldeiras, Inês"],["dc.contributor.author","Santana, Isabel"],["dc.contributor.author","Kovacs, Gabor G."],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Schmitz, Matthias"],["dc.date.accessioned","2020-12-10T18:46:57Z"],["dc.date.available","2020-12-10T18:46:57Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3390/biom9120800"],["dc.identifier.eissn","2218-273X"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16939"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78595"],["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","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Evaluation of Human Cerebrospinal Fluid Malate Dehydrogenase 1 as a Marker in Genetic Prion Disease Patients"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Hermann, Peter"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","Diaz-Lucena, Daniela"],["dc.contributor.author","Nägga, Katarina"],["dc.contributor.author","Hansson, Oskar"],["dc.contributor.author","Santana, Isabel"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Schmidt, Christian"],["dc.contributor.author","Varges, Daniela"],["dc.contributor.author","Goebel, Stefan"],["dc.contributor.author","Dumurgier, Julien"],["dc.contributor.author","Zetterberg, Henrik"],["dc.contributor.author","Blennow, Kaj"],["dc.contributor.author","Paquet, Claire"],["dc.contributor.author","Baldeiras, Inês"],["dc.contributor.author","Ferrer, Isidro"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2021-04-14T08:27:37Z"],["dc.date.available","2021-04-14T08:27:37Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41467-020-14373-2"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17201"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82349"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Cerebrospinal fluid lipocalin 2 as a novel biomarker for the differential diagnosis of vascular dementia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1841"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","European Journal of Neurology"],["dc.bibliographiccitation.lastpage","1846"],["dc.bibliographiccitation.volume","29"],["dc.contributor.affiliation","Canaslan, Sezgi; 1\r\nDepartment of Neurology\r\nNational Reference Center for CJD Surveillance\r\nGöttingen University Medical Center\r\nGöttingen Germany"],["dc.contributor.affiliation","Villar‐Piqué, Anna; 2\r\nBellvitge Biomedical Research Institute\r\nHospitalet de Llobregat Spain"],["dc.contributor.affiliation","Bunck, Timothy; 1\r\nDepartment of Neurology\r\nNational Reference Center for CJD Surveillance\r\nGöttingen University Medical Center\r\nGöttingen Germany"],["dc.contributor.affiliation","Goebel, Stefan; 1\r\nDepartment of Neurology\r\nNational Reference Center for CJD Surveillance\r\nGöttingen University Medical Center\r\nGöttingen Germany"],["dc.contributor.affiliation","Llorens, Franc; 1\r\nDepartment of Neurology\r\nNational Reference Center for CJD Surveillance\r\nGöttingen University Medical Center\r\nGöttingen Germany"],["dc.contributor.affiliation","Schmitz, Matthias; 1\r\nDepartment of Neurology\r\nNational Reference Center for CJD Surveillance\r\nGöttingen University Medical Center\r\nGöttingen Germany"],["dc.contributor.affiliation","Zerr, Inga; 1\r\nDepartment of Neurology\r\nNational Reference Center for CJD Surveillance\r\nGöttingen University Medical Center\r\nGöttingen Germany"],["dc.contributor.author","Hermann, Peter"],["dc.contributor.author","Canaslan, Sezgi"],["dc.contributor.author","Villar‐Piqué, Anna"],["dc.contributor.author","Bunck, Timothy"],["dc.contributor.author","Goebel, Stefan"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2022-04-01T10:03:27Z"],["dc.date.available","2022-04-01T10:03:27Z"],["dc.date.issued","2022"],["dc.date.updated","2022-06-14T22:22:24Z"],["dc.description.abstract","Abstract Background and purpose Fatal familial insomnia is a rare hereditary prion disease associated with the D178N‐129M PRNP mutation. Early diagnosis is difficult, because the clinical syndrome may overlap with affective disorders. In addition, most known cerebrospinal fluid biomarkers for prion diseases and magnetic resonance imaging do not show a good diagnostic accuracy for fatal familial insomnia. In this context, data on plasma biomarkers are scarce. Methods We analyzed levels of neurofilament light chain, glial fibrillary acidic protein, chitinase‐3‐like protein 1, calcium‐binding protein B, and total tau protein in six serial plasma samples from a patient with fatal familial insomnia. Subsequently, plasma neurofilament light chain was analyzed in n = 25 patients and n = 19 controls. The diagnostic accuracy and associations with disease stage and duration were explored. Results Among all biomarker candidates in the case study, only neurofilament light chain levels showed a constant evolution and increased over time. They discriminated fatal familial insomnia from controls with an area under the curve of 0.992 (95% confidence interval [CI] = 0.974–1) in the case–control study. Higher concentrations were associated with methionine homozygosity at codon 129 PRNP (p = 0.006), shorter total disease duration (rho = −0.467, p = 0.019, 95% CI = −0.790 to −0.015), and shorter time from sampling to death (rho = −0.467, p = 0.019, 95% CI = −0.773 to −0.019). Conclusions Plasma neurofilament light chain may be a valuable minimally invasive diagnostic biomarker for fatal familial insomnia after clinical onset. Most important, stage‐related increase and association with disease duration indicate potential as a prognostic marker and as a surrogate marker in clinical trials."],["dc.description.abstract","We investigated plasma biomarkers during preclinical and clinical phase in a patient with fatal familial insomnia (FFI) and identified a stage‐related increase of neurofilament light chain (NfL) from disease onset to late clinical stage. In a retrospective analysis, we observed high discriminatory value of plasma NfL in 25 FFI patients versus 19 control patients (area under the curve = 0.992). In FFI, higher NfL concentrations were significantly associated with shorter overall disease duration and shorter time from sampling to death. image"],["dc.description.sponsorship","CJD Foundation"],["dc.description.sponsorship","Alzheimer Forschung Initiative http://dx.doi.org/10.13039/100010146"],["dc.description.sponsorship","Robert‐Koch‐Institute"],["dc.identifier.doi","10.1111/ene.15302"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/106170"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.eissn","1468-1331"],["dc.relation.issn","1351-5101"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes."],["dc.title","Plasma neurofilament light chain as a biomarker for fatal familial insomnia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]