Schmitz, Matthias

[["dc.bibliographiccitation.firstpage","726"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Antioxidants"],["dc.bibliographiccitation.volume","11"],["dc.contributor.affiliation","Karagianni, Korina; 1Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; korinagk@bio.auth.gr (K.K.); spyrospg@bio.auth.gr (S.P.); lioulia@bio.auth.gr (E.L.)"],["dc.contributor.affiliation","Pettas, Spyros; 1Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; korinagk@bio.auth.gr (K.K.); spyrospg@bio.auth.gr (S.P.); lioulia@bio.auth.gr (E.L.)"],["dc.contributor.affiliation","Kanata, Eirini; 2Neurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; ekanata@bio.auth.gr (E.K.); xantho@pharm.auth.gr (K.X.); sklaviad@pharm.auth.gr (T.S.)"],["dc.contributor.affiliation","Lioulia, Elisavet; 1Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; korinagk@bio.auth.gr (K.K.); spyrospg@bio.auth.gr (S.P.); lioulia@bio.auth.gr (E.L.)"],["dc.contributor.affiliation","Thune, Katrin; 3Department of Neurology, German Center for Neurodegenerative Diseases (DZNE), University Medicine Goettingen, 37075 Goettingen, Germany; katrin.thuene@med.uni-goettingen.de (K.T.); matthias.schmitz@med.uni-goettingen.de (M.S.)"],["dc.contributor.affiliation","Schmitz, Matthias; 3Department of Neurology, German Center for Neurodegenerative Diseases (DZNE), University Medicine Goettingen, 37075 Goettingen, Germany; katrin.thuene@med.uni-goettingen.de (K.T.); matthias.schmitz@med.uni-goettingen.de (M.S.)"],["dc.contributor.affiliation","Tsamesidis, Ioannis; 4Department of Prosthodontics, School of Dentistry, Faculty of Health Sciences, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; itsamesidis@auth.gr"],["dc.contributor.affiliation","Lymperaki, Evgenia; 5Department of Biomedical Sciences, International Hellenic University, 570 01 Thessaloniki, Greece; evlimper@mls.teithe.gr"],["dc.contributor.affiliation","Xanthopoulos, Konstantinos; 2Neurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; ekanata@bio.auth.gr (E.K.); xantho@pharm.auth.gr (K.X.); sklaviad@pharm.auth.gr (T.S.)"],["dc.contributor.affiliation","Sklaviadis, Theodoros; 2Neurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; ekanata@bio.auth.gr (E.K.); xantho@pharm.auth.gr (K.X.); sklaviad@pharm.auth.gr (T.S.)"],["dc.contributor.affiliation","Dafou, Dimitra; 1Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; korinagk@bio.auth.gr (K.K.); spyrospg@bio.auth.gr (S.P.); lioulia@bio.auth.gr (E.L.)"],["dc.contributor.author","Karagianni, Korina"],["dc.contributor.author","Pettas, Spyros"],["dc.contributor.author","Kanata, Eirini"],["dc.contributor.author","Lioulia, Elisavet"],["dc.contributor.author","Thune, Katrin"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Tsamesidis, Ioannis"],["dc.contributor.author","Lymperaki, Evgenia"],["dc.contributor.author","Xanthopoulos, Konstantinos"],["dc.contributor.author","Sklaviadis, Theodoros"],["dc.contributor.author","Dafou, Dimitra"],["dc.date.accessioned","2022-05-02T08:09:33Z"],["dc.date.available","2022-05-02T08:09:33Z"],["dc.date.issued","2022"],["dc.date.updated","2022-05-05T13:21:13Z"],["dc.description.abstract","Prion diseases are transmissible encephalopathies associated with the conversion of the physiological form of the prion protein (PrPC) to the disease-associated (PrPSc). Despite intense research, no therapeutic or prophylactic agent is available. The catechol-type diterpene Carnosic acid (CA) and its metabolite Carnosol (CS) from Rosmarinus officinalis have well-documented anti-oxidative and neuroprotective effects. Since oxidative stress plays an important role in the pathogenesis of prion diseases, we investigated the potential beneficial role of CA and CS in a cellular model of prion diseases (N2a22L cells) and in a cell-free prion amplification assay (RT-QuIC). The antioxidant effects of the compounds were confirmed when N2a22L were incubated with CA or CS. Furthermore, CA and CS reduced the accumulation of the disease-associated form of PrP, detected by Western Blotting, in N2a22L cells. This effect was validated in RT-QuIC assays, indicating that it is not associated with the antioxidant effects of CA and CS. Importantly, cell-free assays revealed that these natural products not only prevent the formation of PrP aggregates but can also disrupt already formed aggregates. Our results indicate that CA and CS have pleiotropic effects against prion diseases and could evolve into useful prophylactic and/or therapeutic agents against prion and other neurodegenerative diseases."],["dc.description.abstract","Prion diseases are transmissible encephalopathies associated with the conversion of the physiological form of the prion protein (PrPC) to the disease-associated (PrPSc). Despite intense research, no therapeutic or prophylactic agent is available. The catechol-type diterpene Carnosic acid (CA) and its metabolite Carnosol (CS) from Rosmarinus officinalis have well-documented anti-oxidative and neuroprotective effects. Since oxidative stress plays an important role in the pathogenesis of prion diseases, we investigated the potential beneficial role of CA and CS in a cellular model of prion diseases (N2a22L cells) and in a cell-free prion amplification assay (RT-QuIC). The antioxidant effects of the compounds were confirmed when N2a22L were incubated with CA or CS. Furthermore, CA and CS reduced the accumulation of the disease-associated form of PrP, detected by Western Blotting, in N2a22L cells. This effect was validated in RT-QuIC assays, indicating that it is not associated with the antioxidant effects of CA and CS. Importantly, cell-free assays revealed that these natural products not only prevent the formation of PrP aggregates but can also disrupt already formed aggregates. Our results indicate that CA and CS have pleiotropic effects against prion diseases and could evolve into useful prophylactic and/or therapeutic agents against prion and other neurodegenerative diseases."],["dc.identifier.doi","10.3390/antiox11040726"],["dc.identifier.pii","antiox11040726"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/107408"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-561"],["dc.relation.eissn","2076-3921"],["dc.title","Carnosic Acid and Carnosol Display Antioxidant and Anti-Prion Properties in In Vitro and Cell-Free Models of Prion Diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1566"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["dc.contributor.affiliation","Ramljak, Sanja; \t\t \r\n\t\t Digital Diagnostics AG, 55129 Mainz, Germany, sr@digid.com"],["dc.contributor.affiliation","Schmitz, Matthias; \t\t \r\n\t\t Department of Neurology, University Medicine Goettingen and The German Center for Neurodegenerative Diseases (DZNE), 37075 Goettingen, Germany, matthias.schmitz@med.uni-goettingen.de"],["dc.contributor.affiliation","Repond, Cendrine; \t\t \r\n\t\t Département de Physiologie, Université de Lausanne, 1005 Lausanne, Switzerland, Cendrine.Repond@unil.ch"],["dc.contributor.affiliation","Zerr, Inga; \t\t \r\n\t\t Department of Neurology, University Medicine Goettingen and The German Center for Neurodegenerative Diseases (DZNE), 37075 Goettingen, Germany, ingazerr@med.uni-goettingen.de"],["dc.contributor.affiliation","Pellerin, Luc; \t\t \r\n\t\t Département de Physiologie, Université de Lausanne, 1005 Lausanne, Switzerland, luc.pellerin@univ-poitiers.fr\t\t \r\n\t\t Centre de Résonance Magnétique des Systèmes Biologiques, UMR5536 CNRS, LabEx TRAIL-IBIO, Université de Bordeaux, 33760 Bordeaux CEDEX, France, luc.pellerin@univ-poitiers.fr"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Repond, Cendrine"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Pellerin, Luc"],["dc.date.accessioned","2021-06-01T10:48:47Z"],["dc.date.available","2021-06-01T10:48:47Z"],["dc.date.issued","2021"],["dc.date.updated","2022-09-06T18:21:55Z"],["dc.description.abstract","The effect of a cellular prion protein (PrPc) deficiency on neuroenergetics was primarily analyzed via surveying the expression of genes specifically involved in lactate/pyruvate metabolism, such as monocarboxylate transporters (MCT1, MCT2, MCT4). The aim of the present study was to elucidate a potential involvement of PrPc in the regulation of energy metabolism in different brain regions. By using quantitative real-time polymerase chain reaction (qRT-PCR), we observed a marked reduction in MCT1 mRNA expression in the cortex of symptomatic Zürich I Prnp−/− mice, as compared to their wild-type (WT) counterparts. MCT1 downregulation in the cortex was accompanied with significantly decreased expression of the MCT1 functional interplayer, the Na+/K+ ATPase α2 subunit. Conversely, the MCT1 mRNA level was significantly raised in the cerebellum of Prnp−/− vs. WT control group, without a substantial change in the Na+/K+ ATPase α2 subunit expression. To validate the observed mRNA findings, we confirmed the observed change in MCT1 mRNA expression level in the cortex at the protein level. MCT4, highly expressed in tissues that rely on glycolysis as an energy source, exhibited a significant reduction in the hippocampus of Prnp−/− vs. WT mice. The present study demonstrates that a lack of PrPc leads to altered MCT1 and MCT4 mRNA/protein expression in different brain regions of Prnp−/− vs. WT mice. Our findings provide evidence that PrPc might affect the monocarboxylate intercellular transport, which needs to be confirmed in further studies."],["dc.description.sponsorship","IDEX"],["dc.identifier.doi","10.3390/ijms22041566"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86055"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1422-0067"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Altered mRNA and Protein Expression of Monocarboxylate Transporter MCT1 in the Cerebral Cortex and Cerebellum of Prion Protein Knockout Mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","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","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","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","165"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Prion"],["dc.bibliographiccitation.lastpage","181"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Requena, Jesus R."],["dc.contributor.author","Kristensson, Krister"],["dc.contributor.author","Korth, Carsten"],["dc.contributor.author","Zurzolo, Chiara"],["dc.contributor.author","Simmons, Marion"],["dc.contributor.author","Aguilar-Calvo, Patricia"],["dc.contributor.author","Aguzzi, Adriano"],["dc.contributor.author","Andreoletti, Olivier"],["dc.contributor.author","Benestad, Sylvie L."],["dc.contributor.author","Boehm, Reinhard"],["dc.contributor.author","Brown, Karen"],["dc.contributor.author","Calgua, Byron"],["dc.contributor.author","Antonio del Rio, Jose"],["dc.contributor.author","Carlos Espinosa, Juan"],["dc.contributor.author","Girones, Rosina"],["dc.contributor.author","Godsave, Sue"],["dc.contributor.author","Hoelzle, Ludwig E."],["dc.contributor.author","Knittler, Michael R."],["dc.contributor.author","Kuhn, Franziska"],["dc.contributor.author","Legname, Giuseppe"],["dc.contributor.author","Laeven, Paul"],["dc.contributor.author","Mabbott, Neil"],["dc.contributor.author","Mitrova, Eva"],["dc.contributor.author","Mueller-Schiffmann, Andreas"],["dc.contributor.author","Nuvolone, Mario"],["dc.contributor.author","Peters, Peter J."],["dc.contributor.author","Raeber, Alex"],["dc.contributor.author","Roth, Klaus"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Schroeder, Bjorn"],["dc.contributor.author","Sonati, Tiziana"],["dc.contributor.author","Stitz, Lothar"],["dc.contributor.author","Taraboulos, Albert"],["dc.contributor.author","Maria Torres, Juan"],["dc.contributor.author","Yan, Zheng-Xin"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T10:20:05Z"],["dc.date.available","2018-11-07T10:20:05Z"],["dc.date.issued","2016"],["dc.description.abstract","Bovine spongiform encephalopathy (BSE) created a global European crisis in the 1980s and 90s, with very serious health and economic implications. Classical BSE now appears to be under control, to a great extent as a result of a global research effort that identified the sources of prions in meat and bone meal (MBM) and developed new animal-testing tools that guided policy. Priority (www.prionpriority.eu) was a European Union (EU) Framework Program 7 (FP7)-funded project through which 21 European research institutions and small and medium enterprises (SMEs) joined efforts between 2009 and 2014, to conduct coordinated basic and applied research on prions and prion diseases. At the end of the project, the Priority consortium drafted a position paper (www.prionpriority.eu/Priority position paper) with its main conclusions. In the present opinion paper, we summarize these conclusions. With respect to the issue of re-introducing ruminant protein into the feed-chain, our opinion is that sus taining an absolute ban on feeding ruminant protein to ruminants is essential. In particular, the spread and impact of non-classical forms of scrapie and BSE in ruminants is not fully understood and the risks cannot be estimated. Atypical prion agents will probably continue to represent the dominant form of prion diseases in the near future in Europe. Atypical L-type BSE has clear zoonotic potential, as demonstrated in experimental models. Similarly, there are now data indicating that the atypical scrapie agent can cross various species barriers. More epidemiological data from large cohorts are nec essary to reach any conclusion on the impact of its transmissibility on public health. Re-evaluations of safety precautions may become necessary depending on the outcome of these studies. Intensified searching for molecular determinants of the species barrier is recommended, since this bar rier is key for important policy areas and risk assessment. Understanding the structural basis for strains and the basis for adaptation of a strain to a new host will require continued fundamental research, also needed to understand mechanisms of prion transmission, replication and how they cause nervous system dysfunction and death. Early detection of prion infection, ideally at a preclini cal stage, also remains crucial for development of effective treatment strategies."],["dc.identifier.doi","10.1080/19336896.2016.1175801"],["dc.identifier.isi","000383360900001"],["dc.identifier.pmid","27220820"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13748"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41805"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Taylor & Francis Inc"],["dc.relation.issn","1933-690X"],["dc.relation.issn","1933-6896"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","The Priority position paper: Protecting Europe's food chain from prions"],["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","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","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","e54915"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Sano, Kazunori"],["dc.contributor.author","Satoh, Katsuya"],["dc.contributor.author","Atarashi, Ryuichiro"],["dc.contributor.author","Takashima, Hiroshi"],["dc.contributor.author","Iwasaki, Yasushi"],["dc.contributor.author","Yoshida, Mari"],["dc.contributor.author","Sanjo, Nobuo"],["dc.contributor.author","Murai, Hiroyuki"],["dc.contributor.author","Mizusawa, Hidehiro"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Kim, Yong-Sun"],["dc.contributor.author","Nishida, Noriyuki"],["dc.date.accessioned","2018-11-07T09:29:01Z"],["dc.date.available","2018-11-07T09:29:01Z"],["dc.date.issued","2013"],["dc.description.abstract","Introduction: The definitive diagnosis of genetic prion diseases (gPrD) requires pathological confirmation. To date, diagnosis has relied upon the finding of the biomarkers 14-3-3 protein and total tau (t-tau) protein in the cerebrospinal fluid (CSF), but many researchers have reported that these markers are not sufficiently elevated in gPrD, especially in Gerstmann-Straussler-Scheinker syndrome (GSS). We recently developed a new in vitro amplification technology, designated \"real-time quaking-induced conversion (RT-QUIC)\", to detect the abnormal form of prion protein in CSF from sporadic Creutzfeldt-Jakob disease (sCJD) patients. In the present study, we aimed to investigate the presence of biomarkers and evaluate RT-QUIC assay in patients with gPrD, as the utility of RT-QUIC as a diagnostic tool in gPrD has yet to be determined. Method/Principal Findings: 56 CSF samples were obtained from gPrD patients, including 20 cases of GSS with P102L mutation, 12 cases of fatal familial insomnia (FFI; D178N), and 24 cases of genetic CJD (gCJD), comprising 22 cases with E200K mutation and 2 with V203I mutation. We subjected all CSF samples to RT-QUIC assay, analyzed 14-3-3 protein by Western blotting, and measured t-tau protein using an ELISA kit. The detection sensitivities of RT-QUIC were as follows: GSS (78%), FFI (100%), gCJD E200K (87%), and gCJD V203I (100%). On the other hand the detection sensitivities of biomarkers were considerably lower: GSS (11%), FFI (0%), gCJD E200K (73%), and gCJD V203I (67%). Thus, RT-QUIC had a much higher detection sensitivity compared with testing for biomarkers, especially in patients with GSS and FFI. Conclusion/Significance: RT-QUIC assay is more sensitive than testing for biomarkers in gPrD patients. RT-QUIC method would thus be useful as a diagnostic tool when the patient or the patient's family does not agree to genetic testing, or to confirm the diagnosis in the presence of a positive result for genetic testing."],["dc.identifier.doi","10.1371/journal.pone.0054915"],["dc.identifier.isi","000315210400040"],["dc.identifier.pmid","23372790"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8553"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30923"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Early Detection of Abnormal Prion Protein in Genetic Human Prion Diseases Now Possible Using Real-Time QUIC Assay"],["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","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"]]