Gawinecka, Joanna

[["dc.bibliographiccitation.firstpage","1620"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Neurology"],["dc.bibliographiccitation.lastpage","1628"],["dc.bibliographiccitation.volume","256"],["dc.contributor.author","Ladogana, Anna"],["dc.contributor.author","Sanchez-Juan, Pascual"],["dc.contributor.author","Mitrova, Eva"],["dc.contributor.author","Green, Alison"],["dc.contributor.author","Cuadrado-Corrales, Natividad"],["dc.contributor.author","Sanchez-Valle, Raquel"],["dc.contributor.author","Koscova, Silvia"],["dc.contributor.author","Aguzzi, Adriano"],["dc.contributor.author","Sklaviadis, Theodoros"],["dc.contributor.author","Kulczycki, Jerzy"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Saiz, Albert"],["dc.contributor.author","Calero, Miguel"],["dc.contributor.author","van Duijn, Cornelia M."],["dc.contributor.author","Pocchiari, Maurizio"],["dc.contributor.author","Knight, Richard"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T11:23:52Z"],["dc.date.available","2018-11-07T11:23:52Z"],["dc.date.issued","2009"],["dc.description.abstract","The 14-3-3 protein test has been shown to support the clinical diagnosis of sporadic Creutzfeldt-Jakob disease (CJD) when associated with an adequate clinical context, and a high differential potential for the diagnosis of sporadic CJD has been attributed to other cerebrospinal fluid (CSF) proteins such as tau protein, S100b and neuron specific enolase (NSE). So far there has been only limited information available about biochemical markers in genetic transmissible spongiform encephalopathies (gTSE), although they represent 10-15% of human TSEs. In this study, we analyzed CSF of 174 patients with gTSEs for 14-3-3 (n = 166), tau protein (n = 78), S100b (n = 46) and NSE (n = 50). Levels of brain-derived proteins in CSF varied in different forms of gTSE. Biomarkers were found positive in the majority of gCJD (81%) and insert gTSE (69%), while they were negative in most cases of fatal familial insomnia (13%) and Gerstmann-Straussler-Scheinker syndrome (10%). Disease duration and codon 129 genotype influence the findings in a different way than in sporadic CJD."],["dc.identifier.doi","10.1007/s00415-009-5163-x"],["dc.identifier.isi","000270385400003"],["dc.identifier.pmid","19444528"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6745"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56280"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Dr Dietrich Steinkopff Verlag"],["dc.relation.issn","0340-5354"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Cerebrospinal fluid biomarkers in human genetic transmissible spongiform encephalopathies"],["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","3051"],["dc.bibliographiccitation.journal","Brain"],["dc.bibliographiccitation.lastpage","3061"],["dc.bibliographiccitation.volume","135"],["dc.contributor.author","Stoeck, Katharina"],["dc.contributor.author","Sanchez-Juan, Pascual"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Green, Alison"],["dc.contributor.author","Ladogana, Anna"],["dc.contributor.author","Pocchiari, Maurizio"],["dc.contributor.author","Sanchez-Valle, Raquel"],["dc.contributor.author","Mitrova, Eva"],["dc.contributor.author","Sklaviadis, Theodor"],["dc.contributor.author","Kulczycki, Jerzy"],["dc.contributor.author","Slivarichova, Dana"],["dc.contributor.author","Saiz, Albert"],["dc.contributor.author","Calero, Miguel"],["dc.contributor.author","Knight, Richard"],["dc.contributor.author","Aguzzi, Adriano"],["dc.contributor.author","Laplanche, Jean-Louis"],["dc.contributor.author","Peoc'h, Katell"],["dc.contributor.author","Schelzke, Gabi"],["dc.contributor.author","Karch, Andre"],["dc.contributor.author","van Duijn, Cornelia M."],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:04:59Z"],["dc.date.available","2018-11-07T09:04:59Z"],["dc.date.issued","2012"],["dc.description.abstract","To date, cerebrospinal fluid analysis, particularly protein 14-3-3 testing, presents an important approach in the identification of Creutzfeldt-Jakob disease cases. However, one special point of criticism of 14-3-3 testing is the specificity in the differential diagnosis of rapid dementia. The constant observation of increased cerebrospinal fluid referrals in the national surveillance centres over the last years raises the concern of declining specificity due to higher number of cerebrospinal fluid tests performed in various neurological conditions. Within the framework of a European Community supported longitudinal multicentre study ('cerebrospinal fluid markers') we analysed the spectrum of rapid progressive dementia diagnoses, their potential influence on 14-3-3 specificity as well as results of other dementia markers (tau, phosphorylated tau and amyloid-beta(1-42)) and evaluated the specificity of 14-3-3 in Creutzfeldt-Jakob disease diagnosis for the years 1998-2008. A total of 29 022 cerebrospinal fluid samples were analysed for 14-3-3 protein and other cerebrospinal fluid dementia markers in patients with rapid dementia and suspected Creutzfeldt-Jakob disease in the participating centres. In 10 731 patients a definite diagnosis could be obtained. Protein 14-3-3 specificity was analysed for Creutzfeldt-Jakob disease with respect to increasing cerebrospinal fluid tests per year and spectrum of differential diagnosis. Ring trials were performed to ensure the comparability between centres during the reported time period. Protein 14-3-3 test specificity remained high and stable in the diagnosis of Creutzfeldt-Jakob disease during the observed time period across centres (total specificity 92%; when compared with patients with definite diagnoses only: specificity 90%). However, test specificity varied with respect to differential diagnosis. A high 14-3-3 specificity was obtained in differentiation to other neurodegenerative diseases (95-97%) and non-neurological conditions (91-97%). We observed lower specificity in the differential diagnoses of acute neurological diseases (82-87%). A marked and constant increase in cerebrospinal fluid test referrals per year in all centres did not influence 14-3-3 test specificity and no change in spectrum of differential diagnosis was observed. Cerebrospinal fluid protein 14-3-3 detection remains an important test in the diagnosis of Creutzfeldt-Jakob disease. Due to a loss in specificity in acute neurological events, the interpretation of positive 14-3-3 results needs to be performed in the clinical context. The spectrum of differential diagnosis of rapid progressive dementia varied from neurodegenerative dementias to dementia due to acute neurological conditions such as inflammatory diseases and non-neurological origin."],["dc.description.sponsorship","European Commission [QLG3-CT-2002-81606, 222887, 01ED1201A]"],["dc.identifier.doi","10.1093/brain/aws238"],["dc.identifier.isi","000310156700015"],["dc.identifier.pmid","23012332"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25223"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0006-8950"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Cerebrospinal fluid biomarker supported diagnosis of Creutzfeldt-Jakob disease and rapid dementias: a longitudinal multicentre study over 10 years"],["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","758"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Journal of neuropathology and experimental neurology"],["dc.bibliographiccitation.lastpage","767"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Wemheuer, Wiebke M."],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.date.accessioned","2015-11-18T10:28:52Z"],["dc.date.accessioned","2021-10-27T13:20:22Z"],["dc.date.available","2015-11-18T10:28:52Z"],["dc.date.available","2021-10-27T13:20:22Z"],["dc.date.issued","2013-08-01"],["dc.description.abstract","In brain biopsies taken from patients with rapidly progressive dementia, the first differential diagnoses to be ruled out are prion diseases. For safe diagnostic processing of tissue and instruments, a rapid, highly sensitive, and specific analysis for prion aggregates is necessary. Here, we examined 16 brain biopsies and brain samples (frontal cortex and cerebellum) from 65 autopsies by Western blot, paraffin-embedded tissue (PET) blot, immunohistochemistry, and the recently described membrane adsorption assay (MAA) for their suitability to detect pathologic prion protein. In our hands, the PET blot method provided the highest sensitivity in prion detection (biopsies, 100%; all autopsy sections, 96.3%), closely followed by the MAA (biopsies, 100%; all autopsy samples, 96%) and Western blot analysis (biopsies, 100%; all autopsy samples, 92%). Conventional immunohistochemistry is the least sensitive method (biopsies, 50%; all autopsy sections, 80%) and also gave 1 false-positive biopsy result. Consequently, our standard diagnostic protocol is to use the MAA as a first step for detecting or excluding a prion disease, followed by the PET blot for the prion deposition pattern, Western blotting for prion typing, and immunohistochemistry for differential diagnoses. With this standard and the availability of unfixed tissue, a diagnosis was possible in all 16 biopsies examined."],["dc.description.sponsorship","VolkswagenStiftung [VWZ2168]; Prionscreen [FP6-2005-SSP-5A]"],["dc.format.extent","19"],["dc.identifier.doi","10.1097/NEN.0b013e31829d2799"],["dc.identifier.isi","000330383600005"],["dc.identifier.pmid","23860029"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12445"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91960"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.issn","1554-6578"],["dc.relation.issn","0022-3069"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.mesh","Alzheimer Disease"],["dc.subject.mesh","Biopsy"],["dc.subject.mesh","Brain"],["dc.subject.mesh","Cell Membrane"],["dc.subject.mesh","Dementia"],["dc.subject.mesh","Female"],["dc.subject.mesh","Filtration"],["dc.subject.mesh","Frontotemporal Lobar Degeneration"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Male"],["dc.subject.mesh","Parkinson Disease"],["dc.subject.mesh","Positron-Emission Tomography"],["dc.subject.mesh","PrPSc Proteins"],["dc.subject.mesh","Prion Diseases"],["dc.subject.mesh","Prions"],["dc.subject.mesh","Sensitivity and Specificity"],["dc.title","Filtration of protein aggregates increases the accuracy for diagnosing prion diseases in brain biopsies."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","139"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neurodegenerative Diseases"],["dc.bibliographiccitation.lastpage","144"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Ciesielczyk, Barbara"],["dc.contributor.author","Sanchez-Juan, Pascual"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Heinemann, Uta"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:15:34Z"],["dc.date.available","2018-11-07T09:15:34Z"],["dc.date.issued","2012"],["dc.description.abstract","Background:The detection of a 14-3-3 elevated level in cerebrospinal fluid (CSF) is a part of the diagnostic criteria for probable sporadic Creutzfeldt-Jakob disease (sCJD), as defined by the WHO. However, some pathological conditions associated with acute neuronal damage may result in a positive 14-3-3 test and thereby reduce test specificity in sCJD. Objective: Desmoplakin has been previously identified as up-regulated CSF protein in sCJD and these studies aimed to investigate its diagnostic utility and compare it with two known CSF markers, 14-3-3 and tau. Methods and Results: We tested CSF levels of 14-3-3, tau and desmoplakin in 58 sCJD patients and 81 control patients including 45 cases with an elevated 14-3-3 level due to other disease than sCJD. We detected an elevated CSF level of desmoplakin in 78% of the sCJD patients, while 14-3-3 (88%) and tau (91%) showed a higher positive rate. However, the false positive rate of newly tested desmoplakin was significantly lower in comparison to 14-3-3 and tau, and it accounted for only 11% versus 56% and 35%, respectively. Further reduction of false positive rates was achieved by combination of elevated tau level with a positive desmoplakin test. Moreover, in the non-sCJD group, desmoplakin level did not correlate with the level of both above-mentioned CSF markers, whereas a clear correlation was observed in the sCJD group. Conclusion: Desmoplakin showed a low positive rate accompanied by a very low false positive rate. Thus, we conclude that desmoplakin is a promising candidate for supportive CSF marker to rule out 14-3-3 false positive cases in sCJD differential diagnosis. Copyright (C) 2011 S. Karger AG, Basel"],["dc.description.sponsorship","European Commission [KBBE-2007-2-4-06]"],["dc.identifier.doi","10.1159/000334499"],["dc.identifier.isi","000301700600004"],["dc.identifier.pmid","22213780"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9091"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27723"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","S. Karger AG"],["dc.relation.eissn","1660-2862"],["dc.relation.issn","1660-2854"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Desmoplakin as a Potential Candidate for Cerebrospinal Fluid Marker to Rule Out 14-3-3 False Positive Rates in Sporadic Creutzfeldt-Jakob Disease Differential Diagnosis"],["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","2566"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","American Journal Of Pathology"],["dc.bibliographiccitation.lastpage","2573"],["dc.bibliographiccitation.volume","175"],["dc.contributor.author","Wemheuer, Wiebke M."],["dc.contributor.author","Benestad, Sylvie L."],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Schulze-Sturm, Ulf"],["dc.contributor.author","Wemheuer, Wilhelm E."],["dc.contributor.author","Hahmann, Uwe"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Schuetz, Ekkehard"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Brenig, Bertram"],["dc.contributor.author","Bratberg, Bjorn"],["dc.contributor.author","Andreoletti, Olivier"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.date.accessioned","2018-11-07T11:21:14Z"],["dc.date.available","2018-11-07T11:21:14Z"],["dc.date.issued","2009"],["dc.description.abstract","Transmissible spongiform encephalopathies such as scrapie in sheep, Creutzfeldt-Jakob disease (CJD) in humans, and bovine sporadic encephalopathy in cattle are characterized by the accumulation of a mis-folded protein: the pathological prion protein. Ever since bovine sporadic encephalopathy was discovered as the likely cause of the new variant of CJD in humans, parallels between human and animal transmissible spongiform encephalopathies must be viewed under the aspect of a disease risk for humans. In our study we have compared prion characteristics of different forms of sheep scrapie with those of different phenotypes of sporadic CJD. The disease characteristics of sporadic CJD depend considerably on the prion type 1 or 2. Our results show that there are obvious parallels between sporadic CJD type 1 and the so-called atypical/Nor98 scrapie. These parelleles apply to the deposition form of pathological prion protein in the brain, detected by the paraffm-embedded-tissue blot and the prion aggregate stability with regard to denaturation by the chaotropic salt guanidine hydrochloride. The same applies to sporadic CJD type 2 and classical scrapie. The observed parallels between types of sporadic CJD and types of sheep scrapie demonstrate that distinct groups of prion disease exist in different species. This should be taken into consideration when discussing interspecies transmission. (Am J Pathol 2009, 175:2566-2573 DOI: 10.2353/ajpath.2009.090623"],["dc.description.sponsorship","VolkswagenStiftung [ZN 1294, ZN2168]"],["dc.identifier.doi","10.2353/ajpath.2009.090623"],["dc.identifier.isi","000272600600031"],["dc.identifier.pmid","19850886"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10435"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55724"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","1525-2191"],["dc.relation.issn","0002-9440"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Similarities between Forms of Sheep Scrapie and Creutzfeldt-Jakob Disease Are Encoded by Distinct Prion Types"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","263"],["dc.bibliographiccitation.issue","5-6"],["dc.bibliographiccitation.journal","Neurodegenerative Diseases"],["dc.bibliographiccitation.lastpage","269"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Gmitterova, Karin"],["dc.contributor.author","Heinemann, U."],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Varges, Daniel. A."],["dc.contributor.author","Ciesielczyk, Barbara"],["dc.contributor.author","Valkovic, P."],["dc.contributor.author","Benetin, J."],["dc.contributor.author","Zerr, I."],["dc.date.accessioned","2018-11-07T08:35:12Z"],["dc.date.available","2018-11-07T08:35:12Z"],["dc.date.issued","2009"],["dc.description.abstract","Background: The 8-hydroxy-2 deoxyguanosine (8-OHdG) is a product of nucleoside oxidation of DNA and a reliable marker of oxidative stress markers. Increased levels of oxidative stress have been reported in the cerebrospinal fluid (CSF) of patients with various neurodegenerative disorders. Objective: In search of a biochemical indicator of Parkinson's disease (PD), we analyzed the levels 8-OHdG in the CSF of 99 patients, using ELISA to assess the differences between various neurodegenerative disorders. Results: Statistically significant higher CSF levels (p = 0.022) of 8-OHdG in non-demented PD patients as compared to the control group were observed. No differences between CSF 8-OHdG levels and age at the time of lumbar puncture, presence or severity of dementia, or gender were found. Conclusions: 8-OHdG levels could be potentially useful in the neurochemically supported diagnosis of PD. Copyright (C) 2009 S. Karger AG, Basel"],["dc.description.sponsorship","European Commission [SP5A-CT-2007-044438]"],["dc.identifier.doi","10.1159/000237221"],["dc.identifier.isi","000274466900008"],["dc.identifier.pmid","19955696"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9327"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18007"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1660-2854"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","8-OHdG in Cerebrospinal Fluid as a Marker of Oxidative Stress in Various Neurodegenerative 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","3610"],["dc.bibliographiccitation.issue","23-24"],["dc.bibliographiccitation.journal","PROTEOMICS"],["dc.bibliographiccitation.lastpage","3620"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Gawinecka, Joanna"],["dc.contributor.author","Cardone, Franco"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","De Pascalis, Angela"],["dc.contributor.author","Wemheuer, Wiebke M."],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Pocchiari, Maurizio"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:02:39Z"],["dc.date.available","2018-11-07T09:02:39Z"],["dc.date.issued","2012"],["dc.description.abstract","Sporadic CreutzfeldtJakob disease (sCJD) is characterized by wide clinical and pathological variability, which is mainly influenced by the conformation of the misfolded prion protein, and by the methionine and valine polymorphism at codon 129 of the prion protein gene. This heterogeneity likely implies differences in the molecular cascade that leads to the development of certain disease phenotypes. In this study, we investigated the proteome of the frontal cortex of patients with the two most common sCJD subtypes (MM1 and VV2) using 2D-DIGE and MS. Analysis of 2D maps revealed that 46 proteins are differentially expressed in the sCJD. Common differential expression was detected for seven proteins, four showed opposite direction of differential expression, and the remaining ones displayed subtype-specific alteration. The highest number of differentially expressed proteins was associated with signal transduction and neuronal activity. Moreover, functional groups of proteins involved in cell cycle and death, as well as in structure and motility included subtype-specific expressed proteins exclusively. The expression of Rab GDP dissociation inhibitor alpha, which regulates Rab3a-mediated neurotransmitter release, was affected in both sCJD subtypes that were analyzed. Therefore, we also investigated as to whether Rab3a recycling is altered. Indeed, we found an accumulation of the membrane-associated form, thus the active one, which suggests that dysfunction of the Rab3a-mediated exocytosis might be implicated in sCJD pathology."],["dc.description.sponsorship","European Commission [222887, NeuroPrion FOOD-CT-2004-506579]"],["dc.identifier.doi","10.1002/pmic.201200201"],["dc.identifier.isi","000312650100016"],["dc.identifier.pmid","23070823"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9494"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24734"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1615-9853"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Sporadic Creutzfeldt-Jakob disease subtype-specific alterations of the brain proteome: Impact on Rab3a recycling"],["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"]]