Mollenhauer, Brit

[["dc.bibliographiccitation.firstpage","275"],["dc.bibliographiccitation.journal","International Review of Neurobiology"],["dc.bibliographiccitation.lastpage","294"],["dc.bibliographiccitation.volume","132"],["dc.contributor.author","Johar, Iskandar"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Aarsland, Dag"],["dc.date.accessioned","2018-10-09T07:05:24Z"],["dc.date.available","2018-10-09T07:05:24Z"],["dc.date.issued","2017"],["dc.description.abstract","Among the nonmotor symptoms in Parkinson's disease (PD), cognitive impairment is one of the most common and devastating. Over recent years, mild cognitive impairment (MCI) has become a recognized feature of PD (PD-MCI). The underlying mechanisms which influence onset, rate of decline, and conversion to dementia (PDD) are largely unknown. Adding to this uncertainty is the heterogeneity of cognitive domains affected. Currently there are no disease-modifying treatments that can slow or reverse this process. Identification of biomarkers that can predict rate and risk of cognitive decline is therefore an unmet need. Cerebrospinal fluid (CSF) is an ideal biomarker candidate as its constituents reflect the metabolic processes underlying the functioning of brain parenchyma. The pathological hallmark of PD is the presence of aggregated α-synuclein (α-Syn) in intracellular Lewy inclusions. In addition, there is concomitant Alzheimer's disease (AD) pathology. In AD, decreased CSF β-amyloid 1-42 (Aβ42) and increased CSF tau levels are predictive of future cognitive decline, setting a precedent for such studies to be carried out in PD. CSF studies in PD have focused on the classical AD biomarkers and α-Syn. Longitudinal studies indicate that low levels of CSF Aβ42 are predictive of cognitive decline; however, results for tau and α-Syn were not consistent. This chapter summarizes recent findings of CSF biomarker studies and cognitive dysfunction in PD."],["dc.fs.pkfprnr","51026"],["dc.identifier.doi","10.1016/bs.irn.2016.12.001"],["dc.identifier.fs","634518"],["dc.identifier.pmid","28554411"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15890"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","2162-5514"],["dc.relation.isbn","978-0-12-809714-4"],["dc.title","Cerebrospinal Fluid Biomarkers of Cognitive Decline in Parkinson's Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","739"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Neural Transmission"],["dc.bibliographiccitation.lastpage","746"],["dc.bibliographiccitation.volume","119"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Trautmann, Ellen"],["dc.contributor.author","Otte, Birgit"],["dc.contributor.author","Ng, Juliana"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Lange, Peter"],["dc.contributor.author","Sixel-Doering, Friederike"],["dc.contributor.author","Hakimi, Mansoureh"],["dc.contributor.author","VonSattel, Jean-Paul"],["dc.contributor.author","Nussbaum, Robert"],["dc.contributor.author","Trenkwalder, Claudia"],["dc.contributor.author","Schlossmacher, Michael G."],["dc.date.accessioned","2018-11-07T09:08:50Z"],["dc.date.available","2018-11-07T09:08:50Z"],["dc.date.issued","2012"],["dc.description.abstract","The source of Parkinson disease-linked alpha-synuclein (aSyn) in human cerebrospinal fluid (CSF) remains unknown. We decided to measure the concentration of aSyn and its gradient in human CSF specimens and compared it with serum to explore its origin. We correlated aSyn concentrations in CSF versus serum (Q(aSyn)) to the albumin quotient (Q(albumin)) to evaluate its relation to blood-CSF barrier function. We also compared aSyn with several other CSF constituents of either central or peripheral sources (or both) including albumin, neuron-specific enolase, beta-trace protein and total protein content. Finally, we examined whether aSyn is present within the structures of the choroid plexus (CP). We observed that Q(aSyn) did not rise or fall with Q(albumin) values, a relative measure of blood-CSF barrier integrity. In our CSF gradient analyses, aSyn levels decreased slightly from rostral to caudal fractions, in parallel to the recorded changes for neuron-specific enolase; the opposite trend was recorded for total protein, albumin and beta-trace protein. The latter showed higher concentrations in caudal CSF fractions due to the diffusion-mediated transfer of proteins from blood and leptomeninges into CSF in the lower regions of the spine. In postmortem sections of human brain, we detected highly variable aSyn reactivity within the epithelial cell layer of CP in patients diagnosed with a range of neurological diseases; however, in sections of mice that express only human SNCA alleles (and in those without any Snca gene expression), we detected no aSyn signal in the epithelial cells of the CP. We conclude from these complementary results that despite its higher levels in peripheral blood products, neurons of the brain and spinal cord represent the principal source of aSyn in human CSF."],["dc.identifier.doi","10.1007/s00702-012-0784-0"],["dc.identifier.isi","000305525800002"],["dc.identifier.pmid","22426833"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8104"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26122"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.relation.issn","0300-9564"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","alpha-Synuclein in human cerebrospinal fluid is principally derived from neurons of the central nervous system"],["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","919"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Neural Transmission"],["dc.bibliographiccitation.lastpage","927"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Bibl, Mirko"],["dc.contributor.author","Esselmann, Herrmann"],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Trenkwalder, Claudia"],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Otto, Markus"],["dc.date.accessioned","2018-11-07T11:06:56Z"],["dc.date.available","2018-11-07T11:06:56Z"],["dc.date.issued","2007"],["dc.description.abstract","To evaluate variations in amyloid beta (A beta) peptide pattern in cerebrospinal fluid (CSF) in neurodegenerative disorders. A recently estabfished quantitative urea-based A beta-sodium-dodecylsulfate-polyacrylamide-gel-electrophoresis with western immunoblot (AP-SDS-PAGE/immunoblot) revealed a highly conserved A beta peptide (A beta 1-37, 1-38, 1-39, 1-40, 1-42) pattern in CSF. We asked whether the variation might be useful to further elucidate the overlap between or distinctions among neurodegenerative diseases in A beta-processing. We used the A beta-SDS-PAGE/immunoblot to investigate CSF for diseasespecific A beta peptide patterns. CSF samples from 96 patients with mainly clinically diagnosed Alzheimer's disease (n = 15), progressive supranuclear palsy (n = 20), corticobasal degeneration (n =: 12), Parkinson's disease (n = 11), multiple systems atrophy (n = 18), and dementia with Lewy-bodies (n = 20) were analysed as well a comparison group (n = 19). The A beta peptide patterns varied between tauopathies and synucleinopathies and between all diseases and the comparison group, possibly due to the influence of tau and a-synuctein on Ap-processing."],["dc.identifier.doi","10.1007/s00702-007-0629-4"],["dc.identifier.isi","000248001800007"],["dc.identifier.pmid","17318305"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52433"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.relation.issn","0300-9564"],["dc.title","Tauopathies and synucleinopathies: Do cerebrospinal fluid beta-amyloid peptides reflect disease-specific pathogenesis?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","396"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","405"],["dc.bibliographiccitation.volume","123"],["dc.contributor.author","Luk, Connie"],["dc.contributor.author","Compta, Yaroslau"],["dc.contributor.author","Magdalinou, Nadia"],["dc.contributor.author","Jose Marti, Maria"],["dc.contributor.author","Hondhamuni, Geshanthi"],["dc.contributor.author","Zetterberg, Henrik"],["dc.contributor.author","Blennow, Kaj"],["dc.contributor.author","Constantinescu, Radu"],["dc.contributor.author","Pijnenburg, Yolande"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Trenkwalder, Claudia"],["dc.contributor.author","van Swieten, John"],["dc.contributor.author","Chiu, Wan Zheng"],["dc.contributor.author","Borroni, Barbara"],["dc.contributor.author","Camara, Ana"],["dc.contributor.author","Cheshire, Perdita"],["dc.contributor.author","Williams, David R."],["dc.contributor.author","Lees, Andrew J."],["dc.contributor.author","de Silva, Rohan"],["dc.date.accessioned","2018-11-07T09:04:11Z"],["dc.date.available","2018-11-07T09:04:11Z"],["dc.date.issued","2012"],["dc.description.abstract","Characteristic tau isoform composition of the insoluble fibrillar tau inclusions define tauopathies, including Alzheimer's disease (AD), progressive supranuclear palsy (PSP) and frontotemporal dementia with parkinsonism linked to chromosome 17/frontotemporal lobar degeneration-tau (FTDP-17/FTLD-tau). Exon 10 splicing mutations in the tau gene, MAPT, in familial FTDP-17 cause elevation of tau isoforms with four microtubule-binding repeat domains (4R-tau) compared to those with three repeats (3R-tau). On the basis of two well-characterised monoclonal antibodies against 3R- and 4R-tau, we developed novel, sensitive immuno-PCR assays for measuring the trace amounts of these isoforms in CSF. This was with the aim of assessing if CSF tau isoform changes reflect the pathological changes in tau isoform homeostasis in the degenerative brain and if these would be relevant for differential clinical diagnosis. Initial analysis of clinical CSF samples of PSP (n = 46), corticobasal syndrome (CBS; n = 22), AD (n = 11), Parkinson's disease with dementia (PDD; n = 16) and 35 controls revealed selective decreases of immunoreactive 4R-tau in CSF of PSP and AD patients compared with controls, and lower 4R-tau levels in AD compared with PDD. These decreases could be related to the disease-specific conformational masking of the RD4-binding epitope because of abnormal folding and/or aggregation of the 4R-tau isoforms in tauopathies or increased sequestration of the 4R-tau isoforms in brain tau pathology."],["dc.identifier.doi","10.1111/j.1471-4159.2012.07911.x"],["dc.identifier.isi","000309743600008"],["dc.identifier.pmid","22862741"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25061"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0022-3042"],["dc.title","Development and assessment of sensitive immuno-PCR assays for the quantification of cerebrospinal fluid three- and four-repeat tau isoforms in tauopathies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","856"],["dc.bibliographiccitation.issue","6518"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","860"],["dc.bibliographiccitation.volume","370"],["dc.contributor.author","Cantuti-Castelvetri, Ludovico"],["dc.contributor.author","Ojha, Ravi"],["dc.contributor.author","Pedro, Liliana D."],["dc.contributor.author","Djannatian, Minou"],["dc.contributor.author","Franz, Jonas"],["dc.contributor.author","Kuivanen, Suvi"],["dc.contributor.author","van der Meer, Franziska"],["dc.contributor.author","Kallio, Katri"],["dc.contributor.author","Kaya, Tuğberk"],["dc.contributor.author","Anastasina, Maria"],["dc.contributor.author","Smura, Teemu"],["dc.contributor.author","Levanov, Lev"],["dc.contributor.author","Szirovicza, Leonora"],["dc.contributor.author","Tobi, Allan"],["dc.contributor.author","Kallio-Kokko, Hannimari"],["dc.contributor.author","Österlund, Pamela"],["dc.contributor.author","Joensuu, Merja"],["dc.contributor.author","Meunier, Frédéric A."],["dc.contributor.author","Butcher, Sarah J."],["dc.contributor.author","Winkler, Martin Sebastian"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Helenius, Ari"],["dc.contributor.author","Gokce, Ozgun"],["dc.contributor.author","Teesalu, Tambet"],["dc.contributor.author","Hepojoki, Jussi"],["dc.contributor.author","Vapalahti, Olli"],["dc.contributor.author","Stadelmann, Christine"],["dc.contributor.author","Balistreri, Giuseppe"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2021-04-14T08:31:26Z"],["dc.date.available","2021-04-14T08:31:26Z"],["dc.date.issued","2020"],["dc.description.abstract","The causative agent of coronavirus disease 2019 (COVID-19) is the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). For many viruses, tissue tropism is determined by the availability of virus receptors and entry cofactors on the surface of host cells. In this study, we found that neuropilin-1 (NRP1), known to bind furin-cleaved substrates, significantly potentiates SARS-CoV-2 infectivity, an effect blocked by a monoclonal blocking antibody against NRP1. A SARS-CoV-2 mutant with an altered furin cleavage site did not depend on NRP1 for infectivity. Pathological analysis of olfactory epithelium obtained from human COVID-19 autopsies revealed that SARS-CoV-2 infected NRP1-positive cells facing the nasal cavity. Our data provide insight into SARS-CoV-2 cell infectivity and define a potential target for antiviral intervention."],["dc.identifier.doi","10.1126/science.abd2985"],["dc.identifier.pmid","33082293"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83594"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/73"],["dc.identifier.url","https://rdp.sfb274.de/literature/publications/8"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","TRR 274: Checkpoints of Central Nervous System Recovery"],["dc.relation","TRR 274 | A06: The role of lipid-sensing nuclear receptors as checkpoints in regulating phagocyte function during recovery from demyelinating injury"],["dc.relation.eissn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.relation.workinggroup","RG Stadelmann-Nessler"],["dc.relation.workinggroup","RG Cantuti"],["dc.relation.workinggroup","RG Gokce (Systems Neuroscience – Cell Diversity)"],["dc.relation.workinggroup","RG Simons (The Biology of Glia in Development and Disease)"],["dc.rights","CC BY 4.0"],["dc.title","Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity"],["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","200"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Dementia and Geriatric Cognitive Disorders"],["dc.bibliographiccitation.lastpage","208"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Trenkwalder, Claudia"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Bibl, Mirko"],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Brechlin, Peter"],["dc.contributor.author","Schindehuette, Jan"],["dc.contributor.author","Poser, Sigrid"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Otto, Markus"],["dc.date.accessioned","2018-11-07T10:33:04Z"],["dc.date.available","2018-11-07T10:33:04Z"],["dc.date.issued","2006"],["dc.description.abstract","Measurement of tau-protein and beta-amyloid(1-42) (A beta 42) in cerebrospinal fluid (CSF) has gained increasing acceptance in the differential diagnosis of Alzheimer's disease. We investigated CSF tau-protein and A beta 42 concentrations in 73 patients with advanced idiopathic Parkinson's disease with dementia (PDD) and 23 patients with idiopathic Parkinson's disease without dementia (PD) and in a comparison group of 41 non-demented neurological patients (CG) using commercially available enzyme-linked-immunoabsorbant- assay ( ELISA). tau-Protein levels were statistically significantly higher and A beta 42 lower in the PDD patients compared to PD patients and the CG. This observation was most marked ( p < 0.05) in a subgroup of patients with PDD carrying the apolipoprotein genotype epsilon 3/epsilon 3. The distribution of the apolipoprotein genotypes in PDD and PD patients was similar to that of the CG. Although a significant difference in tau-protein values was observed between PDD and CG, no diagnostic cut-off value was established. These findings suggest that such protein CSF changes may help to support the clinical diagnosis of cognitive decline in PD and that there may be apolipoprotein-E-isoform- specific differences in CSF protein regulation in advanced PDD. Copyright (C) 2006 S. Karger AG, Basel."],["dc.identifier.doi","10.1159/000094871"],["dc.identifier.isi","000242167100003"],["dc.identifier.pmid","16899997"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44513"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1420-8008"],["dc.title","Beta-amlyoid 1-42 and tau-protein in cerebrospinal fluid of patients with Parkinson's disease dementia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1401"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Movement Disorders"],["dc.bibliographiccitation.lastpage","1408"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Trezzi, Jean-Pierre"],["dc.contributor.author","Galozzi, Sara"],["dc.contributor.author","Jaeger, Christian"],["dc.contributor.author","Barkovits, Katalin"],["dc.contributor.author","Brockmann, Kathrin"],["dc.contributor.author","Maetzler, Walter"],["dc.contributor.author","Berg, Daniela"],["dc.contributor.author","Marcus, Katrin"],["dc.contributor.author","Betsou, Fay"],["dc.contributor.author","Hiller, Karsten"],["dc.contributor.author","Mollenhauer, Brit"],["dc.date.accessioned","2020-12-10T14:06:56Z"],["dc.date.available","2020-12-10T14:06:56Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1002/mds.27132"],["dc.identifier.issn","0885-3185"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70079"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Distinct metabolomic signature in cerebrospinal fluid in early parkinson's disease"],["dc.title.alternative","Early Parkinson'S CSF Metabolic Signature"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","70"],["dc.bibliographiccitation.journal","Journal of Immunological Methods"],["dc.bibliographiccitation.lastpage","75"],["dc.bibliographiccitation.volume","426"],["dc.contributor.author","Kruse, Niels"],["dc.contributor.author","Mollenhauer, Brit"],["dc.date.accessioned","2018-11-07T09:49:17Z"],["dc.date.available","2018-11-07T09:49:17Z"],["dc.date.issued","2015"],["dc.description.abstract","The quantification of a-Synuclein in cerebrospinal fluid (CSF) as a biornarker has gained tremendous interest in the last years. Several commercially available immunoassays are emerging. We here describe the full validation of one commercially available ELISA assay for the quantification of a-Synuclein in human CSF (Covance alpha-Synuclein ELISA kit). The study was conducted within the BIOMARKAPD project in the European initiative Joint Program for Neurodegenerative Diseases (JPND). We investigated the effect of several pre-analytical and analytical confounders: i.e. (1) need for centrifugation of freshly drawn CSF, (2) sample stability, (3) delay of freezing, (4) volume of storage aliquots, (5) freeze/thaw cycles, (6) thawing conditions, (7) dilution linearity, (8) parallelism, (9) spike recovery, and (10) precision. None of these confounders influenced the levels of alpha-Synuclein in CSF significantly. We found a very high intra-assay precision. The inter-assay precision was lower than expected due to different performances of kit lots used. Overall the validated immunoassay is useful for the quantification of alpha-Synuclein in human CSF. (C) 2015 Elsevier B.V. All rights reserved."],["dc.description.sponsorship","JPND"],["dc.identifier.doi","10.1016/j.jim.2015.08.003"],["dc.identifier.isi","000366079800010"],["dc.identifier.pmid","26271436"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35478"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1872-7905"],["dc.relation.issn","0022-1759"],["dc.title","Validation of a commercially available enzyme-linked immunoabsorbent assay for the quantification of human alpha-Synuclein in cerebrospinal fluid"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","312"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","DMW - Deutsche Medizinische Wochenschrift"],["dc.bibliographiccitation.lastpage","317"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Zerr, I."],["dc.contributor.author","Ruge, D."],["dc.contributor.author","Krause, G."],["dc.contributor.author","Mehnert, W. H."],["dc.contributor.author","Kretzschmar, Hans A."],["dc.contributor.author","Poser, Sigrid"],["dc.date.accessioned","2018-11-07T10:31:53Z"],["dc.date.available","2018-11-07T10:31:53Z"],["dc.date.issued","2002"],["dc.description.abstract","Objective: Analogous to prospective studies in other countries, prevalance and symptoms of sporadic Creutzfeldt-Jakob disease (CJD) were recorded in order to assess irregularities in the incidence of the disease in Germany since the onset of bovine spongioform encephalopathy (BSE). Patients and methods: Since 1993 all suspected case of CJD reported in the Federal Republic of Germany have been analysed by a unified schema and classified by standardised criteria. In addition to voluntary reporting two other systems were accessed: (1) compulsory reporting to the Robert Koch Institute via the appropriate Health Department and (2) cause of death statistics of the Federal Office of Statistics. Results: Between June 1993 and May 2001, a total of 1247 patients with suspected CJD, obtained by the >>Study of the epidemiology and early diagnosis of human spongioform encephalopathies<< at Gottingen University, were examined. The suspected disease was confirmed by autopsy in 404 cases, the diagnosis of probable CJD was made in 369 cases on the basis of clinical data and additional investigation. At the beginning of the Gottingen Study in 1993 the incidence in Germany was 0.7 per mill. population, while in the year 2000 it had risen to 1.3 per mill. population. Corresponding increases in the number of cases since 1993 have been noted also by the Robert Koch Institute and the Federal Office of Statistics. Conclusions: The increased incidence can be explained primarily by a decrease in previously unknown cases. Concerted action as part of the Gottingen Study has increased the cooperation of associated clinics. In addition to sporadic cases of CJD, genetic and, more rarely, iatrogenic forms have been seen in Germany. But no cases of new variant CJD have been reported so far."],["dc.identifier.doi","10.1055/s-2002-20150"],["dc.identifier.isi","000173968100002"],["dc.identifier.pmid","11845386"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44217"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Georg Thieme Verlag Kg"],["dc.relation.issn","0012-0472"],["dc.title","Epidemiology and clinical symptomatology of Creutzfeldt-Jakob disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","126"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","138"],["dc.bibliographiccitation.volume","149"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Bowman, Frederick DuBois"],["dc.contributor.author","Drake, Daniel"],["dc.contributor.author","Duong, Jimmy"],["dc.contributor.author","Blennow, Kaj"],["dc.contributor.author","El‐Agnaf, Omar"],["dc.contributor.author","Shaw, Leslie M."],["dc.contributor.author","Masucci, Jennifer"],["dc.contributor.author","Taylor, Peggy"],["dc.contributor.author","Umek, Robert M."],["dc.contributor.author","Dunty, Jill M."],["dc.contributor.author","Smith, Chris L."],["dc.contributor.author","Stoops, Erik"],["dc.contributor.author","Vanderstichele, Hugo"],["dc.contributor.author","Schmid, Adrian W."],["dc.contributor.author","Moniatte, Marc"],["dc.contributor.author","Zhang, Jing"],["dc.contributor.author","Kruse, Niels"],["dc.contributor.author","Lashuel, Hilal A."],["dc.contributor.author","Teunissen, Charlotte"],["dc.contributor.author","Schubert, Tanja"],["dc.contributor.author","Dave, Kuldip D."],["dc.contributor.author","Hutten, Samantha J."],["dc.contributor.author","Zetterberg, Henrik"],["dc.date.accessioned","2019-07-09T11:50:53Z"],["dc.date.available","2019-07-09T11:50:53Z"],["dc.date.issued","2019"],["dc.description.abstract","α-Synuclein is the major component of Lewy bodies and a candidate biomarker for neurodegenerative diseases in which Lewy bodies are common, including Parkinson's disease and dementia with Lewy bodies. A large body of literature suggests that these disorders are characterized by reduced concentrations of α-synuclein in cerebrospinal fluid (CSF), with overlapping concentrations compared to healthy controls and variability across studies. Several reasons can account for this variability, including technical ones, such as inter-assay and inter-laboratory variation (reproducibility). We compared four immunochemical methods for the quantification of α-synuclein concentration in 50 unique CSF samples. All methods were designed to capture most of the existing α-synuclein forms in CSF ('total' α-synuclein). Each of the four methods showed high analytical precision, excellent correlation between laboratories (R2 0.83-0.99), and good correlation with each other (R2 0.64-0.93), although the slopes of the regression lines were different between the four immunoassays. The use of common reference CSF samples decreased the differences in α-synuclein concentration between detection methods and technologies. Pilot data on an immunoprecipitation mass spectrometry (IP-MS) method is also presented. Our results suggest that the four immunochemical methods and the IP-MS method measure similar forms of α-synuclein and that a common reference material would allow harmonization of results between immunoassays."],["dc.identifier.doi","10.1111/jnc.14569"],["dc.identifier.pmid","30125936"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16020"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59849"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Antibody‐based methods for the measurement of α‐synuclein concentration in human cerebrospinal fluid – method comparison and round robin study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]