Cramm, Maria

[["dc.bibliographiccitation.firstpage","396"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","405"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Karch, Andre"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Varges, Daniel. A."],["dc.contributor.author","Mitrova, Eva"],["dc.contributor.author","Schroeder, Bjoern"],["dc.contributor.author","Raeber, Alex"],["dc.contributor.author","Kuhn, Franziska"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T10:01:38Z"],["dc.date.available","2018-11-07T10:01:38Z"],["dc.date.issued","2015"],["dc.description.abstract","The development of in vitro amplification systems allows detecting femtomolar amounts of prion protein scrapie (PrPSc) in human cerebrospinal fluid (CSF). We performed a CSF study to determine the effects of prion disease type, codon 129 genotype, PrPSc type, and other disease-related factors on the real-time quaking-induced conversion (RT-QuIC) response. We analyzed times to 10,000 relative fluorescence units, areas under the curve and the signal maximum of RT-QuIC response as seeding parameters of interest. Interestingly, type of prion disease (sporadic vs. genetic) and the PRNP mutation (E200K vs. V210I and FFI), codon 129 genotype, and PrPSc type affected RT-QuIC response. In genetic forms, type of mutation showed the strongest effect on the observed outcome variables. In sporadic CJD, MM1 patients displayed a higher RT-QuIC signal maximum compared to MV1 and VV1. Age and gender were not associated with RT-QuIC signal, but patients with a short disease course showed a higher seeding efficiency of the RT-QuIC response. This study demonstrated that PrPSc characteristics in the CSF of human prion disease patients are associated with disease subtypes and rate of decline as defined by disease duration."],["dc.identifier.doi","10.1007/s12035-014-8709-6"],["dc.identifier.isi","000349006200031"],["dc.identifier.pmid","24809690"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10255"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38062"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Humana Press Inc"],["dc.relation.issn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Characteristic CSF Prion Seeding Efficiency in Humans with Prion Diseases"],["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.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","2233"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nature Protocols"],["dc.bibliographiccitation.lastpage","2242"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Müller-Cramm, Dominik"],["dc.contributor.author","Collins, Steven"],["dc.contributor.author","Atarashi, Ryuichiro"],["dc.contributor.author","Satoh, Katsuya"],["dc.contributor.author","Orrù, Christina D"],["dc.contributor.author","Groveman, Bradley R"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Schulz-Schaeffer, Walter J"],["dc.contributor.author","Caughey, Byron"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T18:09:33Z"],["dc.date.available","2020-12-10T18:09:33Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1038/nprot.2016.120"],["dc.identifier.eissn","1750-2799"],["dc.identifier.issn","1754-2189"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73688"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The real-time quaking-induced conversion assay for detection of human prion disease and study of other protein misfolding diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","710"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Alzheimer's & Dementia: The Journal of the Alzheimer's Association"],["dc.bibliographiccitation.lastpage","719"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Kruse, Niels"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Gotzmann, Nadine"],["dc.contributor.author","Golanska, Ewa"],["dc.contributor.author","Thüne, Katrin"],["dc.contributor.author","Zejneli, Orgeta"],["dc.contributor.author","Kanata, Eirini"],["dc.contributor.author","Knipper, Tobias"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Lange, Peter"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Sikorska, Beata"],["dc.contributor.author","Liberski, Pawel P."],["dc.contributor.author","Mitrova, Eva"],["dc.contributor.author","Varges, Daniela"],["dc.contributor.author","Schmidt, Christian"],["dc.contributor.author","Sklaviadis, Theodoros"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-10-08T13:38:00Z"],["dc.date.available","2018-10-08T13:38:00Z"],["dc.date.issued","2017-06"],["dc.description.abstract","Accurate diagnosis of prion diseases and discrimination from alternative dementias gain importance in the clinical routine, but partial overlap in cerebrospinal fluid (CSF) biomarkers impedes absolute discrimination in the differential diagnostic context. We established the clinical parameters for prion disease diagnosis for the quantification of CSF α-synuclein in patients with sporadic (n = 234) and genetic (n = 56) prion diseases, in cases with cognitive impairment/dementia or neurodegenerative disease (n = 278), and in the neurologic control group (n = 111). An optimal cutoff value of 680 pg/mL α-synuclein results in 94% sensitivity and 96% specificity when diagnosing sporadic Creutzfeldt-Jakob disease (CJD). Genetic CJD cases showed increased CSF α-synuclein values. No increased α-synuclein levels were detected in non-CJD cases with rapid progression course. Detection of α-synuclein in the CSF of patients with suspected CJD is a valuable diagnostic test reaching almost full discrimination from non-prion disease cases. These data highlight the utility of CSF α-synuclein quantification in front of classical CSF biomarkers in clinical routine."],["dc.fs.pkfprnr","61006"],["dc.identifier.doi","10.1016/j.jalz.2016.09.013"],["dc.identifier.fs","631450"],["dc.identifier.pmid","27870938"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15884"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1552-5279"],["dc.title","Evaluation of α-synuclein as a novel cerebrospinal fluid biomarker in different forms of prion diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1896"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","1904"],["dc.bibliographiccitation.volume","53"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Karch, Andre"],["dc.contributor.author","Mitrova, Eva"],["dc.contributor.author","Kuhn, Franziska"],["dc.contributor.author","Schroeder, Bjoern"],["dc.contributor.author","Raeber, Alex"],["dc.contributor.author","Varges, Daniel. A."],["dc.contributor.author","Kim, Yong-Sun"],["dc.contributor.author","Satoh, Katsuya"],["dc.contributor.author","Collins, Steven J."],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T10:16:36Z"],["dc.date.available","2018-11-07T10:16:36Z"],["dc.date.issued","2016"],["dc.description.abstract","Real-time quaking-induced conversion (RT-QuIC) allows the amplification of miniscule amounts of scrapie prion protein (PrPSc). Recent studies applied the RT-QuIC methodology to cerebrospinal fluid (CSF) for diagnosing human prion diseases. However, to date, there has not been a formal multi-centre assessment of the reproducibility, validity and stability of RT-QuIC in this context, an indispensable step for establishment as a diagnostic test in clinical practice. In the present study, we analysed CSF from 110 prion disease patients and 400 control patients using the RT-QuIC method under various conditions. In addition, \"blinded\" ring trials between different participating sites were performed to estimate reproducibility. Using the previously established cut-off of 10,000 relative fluorescence units (rfu), we obtained a sensitivity of 85 % and a specificity of 99 %. The multi-centre inter-laboratory reproducibility of RT-QuIC revealed a Fleiss' kappa value of 0.83 (95 % CI: 0.40-1.00) indicating an almost perfect agreement. Moreover, we investigated the impact of short-term CSF storage at different temperatures, long-term storage, repeated freezing and thawing cycles and the contamination of CSF with blood on the RT-QuIC seeding response. Our data indicated that the PrPSc seed in CSF is stable to any type of storage condition but sensitive to contaminations with blood (> 1250 erythrocytes/mu L), which results in a false negative RT-QuIC response. Fresh blood-contaminated samples (3 days) can be rescued by removal of erythrocytes. The present study underlines the reproducibility and high stability of RT-QuIC across various CSF storage conditions with a remarkable sensitivity and specificity, suggesting RT-QuIC as an innovative and robust diagnostic method."],["dc.identifier.doi","10.1007/s12035-015-9133-2"],["dc.identifier.isi","000372263600045"],["dc.identifier.pmid","25823511"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11732"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41064"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Humana Press Inc"],["dc.relation.issn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Stability and Reproducibility Underscore Utility of RT-QuIC for Diagnosis of Creutzfeldt-Jakob Disease"],["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.firstpage","1871"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Neurology"],["dc.bibliographiccitation.lastpage","1879"],["dc.bibliographiccitation.volume","260"],["dc.contributor.author","Varges, Daniel. A."],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Wemheuer, Wiebke M."],["dc.contributor.author","Damman, Insa"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Kallenberg, Kai"],["dc.contributor.author","Shirneshan, Katayoon"],["dc.contributor.author","Elkenani, Manar"],["dc.contributor.author","Markwort, Susanne"],["dc.contributor.author","Faist, Michael"],["dc.contributor.author","Kohlhase, Juergen"],["dc.contributor.author","Windl, Otto"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:23:06Z"],["dc.date.available","2018-11-07T09:23:06Z"],["dc.date.issued","2013"],["dc.description.abstract","We discuss relevant aspects in two siblings with a neurodegenerative process of unclear aetiology who developed progressive dementia with global aphasia and hyperoral behaviour at the ages of 39 and 46 years and who died 6 and 5 years after disease onset. The cases were reported to the National Reference Center for TSE Surveillance in Gottingen, Germany. Detailed clinical examinations, CSF, blood samples, and copies of the important diagnostic tests (magnetic resonance imaging, electroencephalogram, laboratory tests) were obtained. Further neuropathological and genetic analyses were performed. Cerebral magnetic resonance imaging of both siblings showed prominent changes in signal intensity, especially in the left medial temporal cortex, but also the hippocampal formation. Neuropathological examination revealed spongiform changes, neuronal loss, and astrocytic gliosis, which are typical in Creutzfeldt-Jakob disease. However, no prion protein deposits were detectable by immunohistochemical analysis, Western blot, or PET blot, though abundant tau protein deposits were observed. A mutation in the coding region of the prion protein genes of both siblings was excluded. A detailed search of the literature revealed no other cases with a similar clinical and neuropathological appearance. While the disease aetiology remains unclear, the findings point to a neurodegenerative process and most likely a genetic disease."],["dc.identifier.doi","10.1007/s00415-013-6897-z"],["dc.identifier.isi","000321610500025"],["dc.identifier.pmid","23546304"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29501"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Heidelberg"],["dc.relation.issn","0340-5354"],["dc.title","Spongiform encephalopathy in siblings with no evidence of protease-resistant prion protein or a mutation in the prion protein gene"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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.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","577"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Alzheimer s & Dementia"],["dc.bibliographiccitation.lastpage","589"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Karch, Andre"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Lange, Peter"],["dc.contributor.author","Gherib, Kerim"],["dc.contributor.author","Varges, Daniel. A."],["dc.contributor.author","Schmidt, Christian D."],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Stoeck, Katharina"],["dc.date.accessioned","2018-11-07T10:14:52Z"],["dc.date.available","2018-11-07T10:14:52Z"],["dc.date.issued","2016"],["dc.description.abstract","Introduction: The analysis of cerebrospinal fluid biomarkers gains importance in clinical routine and is effective in substantiating dementia diagnosis in the differential diagnostic context. Methods: We evaluated the levels of beta-amyloid (A beta) 42, A beta 40, tau, and P-tau in a large patient population subdivided into prion diseases, tauopathies, synucleinopathies, and controls. Diagnostic test evaluation was assessed by ROC area under the curve analysis. Results: High tau levels were detected in sporadic Creutzfeldt-Jakob disease (sCJD) and high P-tau levels in Alzheimer's disease (AD) and sCJD. A beta 40 was lower exclusively in prionopathies, but low A beta 42 was detected in AD, sCJD, and Lewy body dementia. When disease groups were stratified according to the underlying proteinopathy, we detected disease-type specificities for all biomarkers. P-tau/tau, A beta 42/40, A beta 42/tau, and A beta 40/tau ratios proved valuable in discriminating disease groups and controls, especially P-tau/tau ratio in the identification of sCJD cases. Discussion: Combining the biomarker panel allows differentiating between various types of neuro-degenerative dementias and contributes to a better understanding of their pathophysiological processes. (C) 2015 Alzheimer's Association. Published by Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.jalz.2015.10.009"],["dc.identifier.isi","000376054200007"],["dc.identifier.pmid","26718584"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40704"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","1552-5279"],["dc.relation.issn","1552-5260"],["dc.title","Comparative analysis of cerebrospinal fluid biomarkers in the differential diagnosis of neurodegenerative dementia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","93"],["dc.bibliographiccitation.journal","Prion"],["dc.bibliographiccitation.lastpage","94"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:11:22Z"],["dc.date.available","2018-11-07T09:11:22Z"],["dc.date.issued","2012"],["dc.identifier.isi","000304234300193"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26705"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.publisher.place","Austin"],["dc.relation.issn","1933-6896"],["dc.title","Comparison of two diagnostic approaches-Detection of PrPSc via quaking-induced conversion and 14-3-3 in cerebrospinal fluid of Creutzfeldt-Jakob disease patients"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]