Llorens, Franc

[["dc.bibliographiccitation.firstpage","115"],["dc.bibliographiccitation.lastpage","124"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Llorens, Franc"],["dc.date.accessioned","2021-06-02T10:44:30Z"],["dc.date.available","2021-06-02T10:44:30Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/B978-0-12-804279-3.00008-3"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87066"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Elsevier"],["dc.relation.isbn","978-0-12-804279-3"],["dc.relation.ispartof","Cerebrospinal Fluid in Neurologic Disorders"],["dc.title","Cerebrospinal fluid in Creutzfeldt–Jakob disease"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","95"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Prion"],["dc.bibliographiccitation.lastpage","108"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Arora, Amandeep Singh"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Latif, Umair"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Mihm, Sabine"],["dc.contributor.author","Kumar, Prateek"],["dc.contributor.author","Tahir, Waqas"],["dc.contributor.author","Thüne, Katrin"],["dc.contributor.author","Shafiq, Mohsin"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T18:15:28Z"],["dc.date.available","2020-12-10T18:15:28Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1080/19336896.2020.1729074"],["dc.identifier.eissn","1933-690X"],["dc.identifier.issn","1933-6896"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17401"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74854"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The role of cellular prion protein in lipid metabolism in the liver"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["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","329"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Molecular Neuroscience"],["dc.bibliographiccitation.lastpage","348"],["dc.bibliographiccitation.volume","56"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Younus, Neelam"],["dc.contributor.author","Tahir, Waqas"],["dc.contributor.author","Shafiq, Mohsin"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Ferrer, Isidre"],["dc.contributor.author","Andeoletti, Olivier"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:56:36Z"],["dc.date.available","2018-11-07T09:56:36Z"],["dc.date.issued","2015"],["dc.description.abstract","Small GTPases of the Arf family mainly activate the formation of coated carrier vesicles. We showed that classI Arf1 interacts specifically with full length GPI-anchored cellular prion protein (PrPC). Several recent reports have also demonstrated a missing link between the endoplasmic reticulum and the Golgi-complex role for proper folding, but the exact molecular mechanism is not yet fully understood. In the present study, we identified and characterized the interactive role of Arf1 during PrPC intracellular distribution under pathophysiological conditions. PrPC interaction with Arf1 was investigated in cortical primary neuronal cultures of PrPC wild type and knockout mice (PrP-/-). Arf1 and PrPC co-binding affinity was confirmed using reverse co-immunoprecipitation, co-localization affinity using confocal laser-scanning microscopy. Treatment with brefeldin-A modulated Arf1 expression and resulted in down-regulation and redistribution of PrPC into cytosolic region. In the pre-symptomatic stage of the disease, Arf1 expression was significantly downregulated in the frontal cortex in tg340 mice expressing about fourfold of human PrP-M129 with PrP null background that had been inoculated with human sCJD MM1 brain tissue homogenates (sCJD MM1 mice). In addition, the frontal cortex of CJD human brain demonstrated significant binding capacity of Arf1 protein using co-immunoprecipitation analysis. We also examined Arf1 expression in the brain of CJD patients with the subtypesMM1 and VV2 and found that it was regulated in a region-specific manner. In the frontal cortex, Arf1 expression was not significantly changed in either MM1 or VV2 subtype. Interestingly, Arf1 expression was significantly reduced in the cerebellum in both subtypes as compared to controls. Furthermore, we observed altered RhoA activity, which in turn affects myosin light-chain (MLC) phosphorylation and Arf1-dependent PI3K pathway. Together, our findings underscore a key early symptomatic role of Arf1 in neurodegeneration. Targeting the Arf/Rho/MLC signaling axis might be a promising strategy to uncover the missing link which probably influences disease progression and internal homeostasis of misfolded proteins."],["dc.identifier.doi","10.1007/s12031-015-0544-3"],["dc.identifier.isi","000355753800010"],["dc.identifier.pmid","25896910"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36992"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Humana Press Inc"],["dc.relation.issn","1559-1166"],["dc.relation.issn","0895-8696"],["dc.title","Creutzfeldt-Jakob Disease Subtype-Specific Regional and Temporal Regulation of ADP Ribosylation Factor-1-Dependent Rho/MLC Pathway at Pre-Clinical Stage"],["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.firstpage","1"],["dc.bibliographiccitation.issue","35"],["dc.bibliographiccitation.journal","Acta Neuropathologica Communication"],["dc.bibliographiccitation.lastpage","20"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Fischer, Andre"],["dc.contributor.author","Thüne, Katrin"],["dc.contributor.author","Sikorska, Beata"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Tahir, Waqas"],["dc.contributor.author","Fernández-Borges, Natalia"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Gotzmann, Nadine"],["dc.contributor.author","Carmona, Margarita"],["dc.contributor.author","Streichenberger, Nathalie"],["dc.contributor.author","Michel, Uwe"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Schuetz, Anna-Lena"],["dc.contributor.author","Rajput, Ashish"],["dc.contributor.author","Andréoletti, Olivier"],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Liberski, Pawel P."],["dc.contributor.author","Torres, Juan Maria"],["dc.contributor.author","Ferrer, Isidre"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-01-09T14:57:08Z"],["dc.date.available","2018-01-09T14:57:08Z"],["dc.date.issued","2017-04-27"],["dc.description.abstract","Sporadic Creutzfeldt-Jakob disease (sCJD) is the most prevalent form of human prion disease and it is characterized by the presence of neuronal loss, spongiform degeneration, chronic inflammation and the accumulation of misfolded and pathogenic prion protein (PrPSc). The molecular mechanisms underlying these alterations are largely unknown, but the presence of intracellular neuronal calcium (Ca2+) overload, a general feature in models of prion diseases, is suggested to play a key role in prion pathogenesis.Here we describe the presence of massive regulation of Ca2+ responsive genes in sCJD brain tissue, accompanied by two Ca2+-dependent processes: endoplasmic reticulum stress and the activation of the cysteine proteases Calpains 1/2. Pathogenic Calpain proteins activation in sCJD is linked to the cleavage of their cellular substrates, impaired autophagy and lysosomal damage, which is partially reversed by Calpain inhibition in a cellular prion model. Additionally, Calpain 1 treatment enhances seeding activity of PrPSc in a prion conversion assay. Neuronal lysosomal impairment caused by Calpain over activation leads to the release of the lysosomal protease Cathepsin S that in sCJD mainly localises in axons, although massive Cathepsin S overexpression is detected in microglial cells. Alterations in Ca2+ homeostasis and activation of Calpain-Cathepsin axis already occur at pre-clinical stages of the disease as detected in a humanized sCJD mouse model.Altogether our work indicates that unbalanced Calpain-Cathepsin activation is a relevant contributor to the pathogenesis of sCJD at multiple molecular levels and a potential target for therapeutic intervention."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2017"],["dc.identifier.doi","10.1186/s40478-017-0431-y"],["dc.identifier.pmid","28449707"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14726"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11612"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","2051-5960"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Altered Ca2+ homeostasis induces Calpain-Cathepsin axis activation in sporadic Creutzfeldt-Jakob disease"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2305"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Neurology"],["dc.bibliographiccitation.lastpage","2311"],["dc.bibliographiccitation.volume","262"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Kruse, Niels"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Shafiq, Mohsin"],["dc.contributor.author","Gomes da Cunha, Jose Eriton"],["dc.contributor.author","Gotzman, Nadine"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Thune, Katrin"],["dc.contributor.author","Mendes de Oliveira, Joao Ricardo"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:50:51Z"],["dc.date.available","2018-11-07T09:50:51Z"],["dc.date.issued","2015"],["dc.description.abstract","The identification of reliable diagnostic tools for the differential diagnosis between sporadic Creutzfeldt-Jakob Disease (sCJD) and Alzheimer's disease (AD) remains impeded by the existing clinical, neuropathological and molecular overlap between both diseases. The development of new tools for the quantitative measurement of biomarkers is gaining experimental momentum due to recent advances in high-throughput screening analysis and with the optimization of assays for their quantification in biological fluids, including cerebrospinal fluid (CSF). Electrochemiluminescence (ECL)-based immunoassays have demonstrated to achieve clinical quality performance in a variety of sample types due to its high sensitivity and dynamic range. Here, we quantified the CSF levels of Tau-protein, beta-amyloid 1-42 (A beta 42) and alpha-synuclein, as important biomarkers in CSF used in the differential diagnosis of neurodegenerative disorders in 12 AD, 12 sCJD and 12 control cases by singleplex ECL-based technology. Its performance has been compared to classical enzyme-linked immunosorbent assays (ELISA) to confront their clinical accuracy. ECL-based technology validates previous data obtained with ELISA and presents a higher performance in the discrimination of three analysed groups as determined by increased area under the curve (AUC) values for the three biomarkers. Importantly, alpha-synuclein levels detected by ECL allow an excellent discrimination between sCJD cases and AD and control cases, unveiling a new clinical approach for the differential diagnosis of sCJD."],["dc.identifier.doi","10.1007/s00415-015-7837-x"],["dc.identifier.isi","000363035800012"],["dc.identifier.pmid","26162713"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35791"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Heidelberg"],["dc.relation.issn","1432-1459"],["dc.relation.issn","0340-5354"],["dc.title","Quantification of CSF biomarkers using an electrochemiluminescence-based detection system in the differential diagnosis of AD and sCJD"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Prion"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Llorens, Franc"],["dc.date.accessioned","2018-11-07T10:20:27Z"],["dc.date.available","2018-11-07T10:20:27Z"],["dc.date.issued","2016"],["dc.format.extent","S9"],["dc.identifier.isi","000374656300011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41894"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Taylor & Francis Inc"],["dc.publisher.place","Philadelphia"],["dc.relation.issn","1933-690X"],["dc.relation.issn","1933-6896"],["dc.title","Genetic prion diseases"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","383"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Prion"],["dc.bibliographiccitation.lastpage","393"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Ansoleaga, Belen"],["dc.contributor.author","Garcia-Esparcia, Paula"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Grau-Rivera, Oriol"],["dc.contributor.author","Lopez-Gonzalez, Irene"],["dc.contributor.author","Blanco, Rosi"],["dc.contributor.author","Carmona, Margarita"],["dc.contributor.author","Yaguee, Jordi"],["dc.contributor.author","Nos, Carlos"],["dc.contributor.author","Antonio del Rio, Jose"],["dc.contributor.author","Gelpi, Ellen"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Ferrer, Isidre"],["dc.date.accessioned","2018-11-07T09:20:16Z"],["dc.date.available","2018-11-07T09:20:16Z"],["dc.date.issued","2013"],["dc.description.abstract","Creutzfeldt-Jakob disease (CJD) is a heterogenic neurodegenerative disorder associated with abnormal post-translational processing of cellular prion protein (PrPc). CJD displays distinctive clinical and pathological features which correlate with the genotype at the codon 129 (methionine or valine: M or V respectively) in the prion protein gene and with size of the protease-resistant core of the abnormal prion protein PrPsc (type 1: 20/21 kDa and type 2: 19 kDa). MM1 and VV2 are the most common sporadic CJD (sCJD) subtypes. PrP mRNA expression levels in the frontal cortex and cerebellum are reduced in sCJD in a form subtype-dependent. Total PrP protein levels and PrPsc levels in the frontal cortex and cerebellum accumulate differentially in sCJD MM1 and sCJD VV2 with no relation between PrPsc deposition and spongiform degeneration and neuron loss, but with microgliosis, and IL6 and TNF- response. In the CSF, reduced PrPc, the only form present in this compartment, occurs in sCJD MM1 and VV2. PrP mRNA expression is also reduced in the frontal cortex in advanced stages of Alzheimer disease, Lewy body disease, progressive supranuclear palsy, and frontotemporal lobe degeneration, but PrPc levels in brain varies from one disease to another. Reduced PrPc levels in CSF correlate with PrP mRNA expression in brain, which in turn reflects severity of degeneration in sCJD."],["dc.identifier.doi","10.4161/pri.26416"],["dc.identifier.isi","000327383600005"],["dc.identifier.pmid","24047819"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28844"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.relation.issn","1933-690X"],["dc.relation.issn","1933-6896"],["dc.title","PrP mRNA and protein expression in brain and PrPc in CSF in Creutzfeldt-Jakob disease MM1 and VV2"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]