Bahn, Erik

[["dc.bibliographiccitation.firstpage","2485"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","2490"],["dc.bibliographiccitation.volume","73"],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Otto, M."],["dc.contributor.author","Baxter, H. C."],["dc.contributor.author","Bodemer, M."],["dc.contributor.author","Steinacker, P."],["dc.contributor.author","Bahn, E."],["dc.contributor.author","Zerr, I."],["dc.contributor.author","Kornhuber, J."],["dc.contributor.author","Kretzschmar, H. A."],["dc.contributor.author","Poser, S."],["dc.contributor.author","Rüther, E."],["dc.contributor.author","Aitken, A."],["dc.date.accessioned","2017-09-07T11:44:33Z"],["dc.date.available","2017-09-07T11:44:33Z"],["dc.date.issued","1999"],["dc.description.abstract","Two-dimensional polyacrylamide gel electrophoresis of CSF has been used in the diagnosis of Creutzfeldt-Jakob disease (CJD). One of the two diagnostic protein spots was identified as isoform(s) of the 14-3-3 family of abundant brain proteins. This has led to the development of one-dimensional 14-3-3 sodium dodecyl sulfate polyacrylamide gel electrophoresis immunoblot, which is currently used to support the diagnosis of CJD. In the present study employing western blot analysis, we have identified the panel of 14-3-3 isoforms that appear in the CSF of 10 patients with CJD compared with 10 patients with other dementias. The results clearly show that the 14-3-3 isoforms β, γ, ε, and η are present in the CSF of patients with CJD and can be used to differentiate other dementias. 14-3-3η also gave a baseline signal in all patients with other dementias, including six patients with Alzheimer's disease. The presence of 14-3-3η in the CSF of a patient with herpes simplex encephalitis was particularly noteworthy. This study has determined that isoform-specific 14-3-3 antibodies against β, γ, and ε should be considered for the neurochemical differentiation of CJD from other neurodegenerative diseases."],["dc.identifier.doi","10.1046/j.1471-4159.1999.0732485.x"],["dc.identifier.gro","3151688"],["dc.identifier.pmid","10582609"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8506"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0022-3042"],["dc.title","Isoform Pattern of 14-3-3 Proteins in the Cerebrospinal Fluid of Patients with Creutzfeldt-Jakob Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","257"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Acta Neuropathologica"],["dc.bibliographiccitation.lastpage","259"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Neudecker, S."],["dc.contributor.author","Krasnianski, M."],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Zierz, S."],["dc.date.accessioned","2018-11-07T10:45:40Z"],["dc.date.available","2018-11-07T10:45:40Z"],["dc.date.issued","2004"],["dc.description.abstract","Rimmed vacuoles (RV) are a characteristic pathological feature in inclusion body myositis, but may also occur in other neuromuscular disorders, such as distal myopathies, oculopharyngeal myopathy, polymyositis, rigid spine syndrome, congenital myopathies, and some limb girdle muscular dystrophies, as well as in various neurogenic diseases. We describe a patient with RV in familial facioscapulohumeral muscular dystrophy (FSHD) associated with an FSHD-typical deletion on chromosome 4q35. Thus, FSHD should be included in the differential diagnosis of neuromuscular disorders with RV."],["dc.identifier.doi","10.1007/s00401-004-0894-3"],["dc.identifier.isi","000223123000012"],["dc.identifier.pmid","15221332"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/47556"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0001-6322"],["dc.title","Rimmed vacuoles in facioscapulohumeral muscular dystrophy: a unique ultrastructural feature"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","387"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biochemical Society Transactions"],["dc.bibliographiccitation.lastpage","391"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Baxter, H. C."],["dc.contributor.author","Fraser, J. R."],["dc.contributor.author","Liu, W.-G."],["dc.contributor.author","Forster, J. L."],["dc.contributor.author","Clokie, S."],["dc.contributor.author","Steinacker, P."],["dc.contributor.author","Otto, M."],["dc.contributor.author","Bahn, E."],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Aitken, A."],["dc.date.accessioned","2017-09-07T11:44:41Z"],["dc.date.available","2017-09-07T11:44:41Z"],["dc.date.issued","2002"],["dc.description.abstract","14-3-3 proteins are involved in signalling processes in neuronal cells. Using isoform-specific antibodies we have examined the variation in 14-3-3 isoform neurolocation in normal and scrapie-infected murine brain and show that in defined areas of the brain there are significant changes associated with the pathology of the disease process. The appearance of 14-3-3 proteins in the cerebrospinal fluid (CSF) is a consequence of neuronal disease and the detection of specific isoforms of the 14-3-3 proteins in the CSF is characteristic of some neurodegenerative diseases. In this study, monitoring specifically for theγ 14-3-3 isoform in the CSF by both Western-blot analysis and ELISA we can show a level of correlation between the assays."],["dc.identifier.doi","10.1042/bst0300387"],["dc.identifier.gro","3151722"],["dc.identifier.pmid","12196100"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8543"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0300-5127"],["dc.title","Specific 14-3-3 isoform detection and immunolocalization in prion diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","45"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Neurology"],["dc.bibliographiccitation.lastpage","51"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Bitsch, Annette"],["dc.contributor.author","Horn, C."],["dc.contributor.author","Kemmling, Y."],["dc.contributor.author","Seipelt, M."],["dc.contributor.author","Hellenbrand, U."],["dc.contributor.author","Stiefel, M."],["dc.contributor.author","Ciesielczyk, Barbara"],["dc.contributor.author","Cepek, L."],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Ratzka, P."],["dc.contributor.author","Prange, Hilmar"],["dc.contributor.author","Otto, Markus"],["dc.date.accessioned","2018-11-07T10:33:03Z"],["dc.date.available","2018-11-07T10:33:03Z"],["dc.date.issued","2002"],["dc.description.abstract","Biochemical markers of brain damage, e.g. ischemic stroke, should reflect the volume of irreversibly damaged brain parenchyma and the clinical outcome in a single patient in order to allow estimation of prognosis at an early stage. Tau protein, which derives predominantly from neurons and axons, is elevated in the cerebrospinal fluid of patients with neurodegenerative disease. This makes tau protein a potential marker of neuronal/axonal injury. In order to test this hypothesis, the current study aimed at showing that tau protein is measurable in the blood after acute ischemic stroke and that it correlates with clinical disability and stroke volume. In a longitudinal prospective study we measured tau protein serum levels with an ELISA in 30 patients longitudinally after ischemic stroke. Tau protein was detectable within 5 days after ischemia in the sera of 7/20 patients with MRI-proven infarction and in 2/10 patients with transitory ischemic attack; both of them had a small infarction visible on the MRI scan. Tau protein was measurable within 6 h after symptom onset, peaked after 3-5 days and correlated with infarct volume and disability after 3 months. In conclusion, serum tau protein is a candidate marker of axonal injury. In stroke, its clinical use is limited, because it is detectable only in a proportion of patients. Copyright (C) 2002 S. Karger AG, Basel."],["dc.identifier.doi","10.1159/000047946"],["dc.identifier.isi","000173547300008"],["dc.identifier.pmid","11803192"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44511"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","0014-3022"],["dc.title","Serum tau protein level as a marker of axonal damage in acute ischemic stroke"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1254"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Neurology Neurosurgery & Psychiatry"],["dc.bibliographiccitation.lastpage","1255"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Dibaj, Payam"],["dc.contributor.author","Herrendorf, Gregor"],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Obermann, Mark"],["dc.date.accessioned","2018-11-07T10:06:16Z"],["dc.date.available","2018-11-07T10:06:16Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1136/jnnp-2016-313091"],["dc.identifier.isi","000389151200017"],["dc.identifier.pmid","27071645"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39056"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Bmj Publishing Group"],["dc.relation.issn","1468-330X"],["dc.relation.issn","0022-3050"],["dc.title","Late progression of neurological symptoms and MRI T2 hyperintensities in Parry-Romberg syndrome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","239"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Metabolic Brain Disease"],["dc.bibliographiccitation.lastpage","251"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Nolte, Wilhelm"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Wildberg, Jens"],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Figulla, Hans Reiner"],["dc.contributor.author","Pralle, Lars"],["dc.contributor.author","Hartmann, Heinz"],["dc.contributor.author","Rüther, Eckhard"],["dc.contributor.author","Ramadori, Giuliano"],["dc.date.accessioned","2017-09-07T11:44:42Z"],["dc.date.available","2017-09-07T11:44:42Z"],["dc.date.issued","1999"],["dc.description.abstract","Portal-systemic encephalopathy is the prototype among the neuropsychiatric disorders that fall under the term Hepatic Encephalopathies. Ammonia toxicity is central to the pathophysiology of Portal-systemic encephalopathy, and neuronal ammonia toxicity is modulated by activated astrocytes. The calcium-binding astroglial key protein S100β is released in response to glial activation, and its measurement in serum only recently became possible. Serum S100β was determined by an ultrasensitive ELISA in patients (n=36) with liver cirrhosis and transjugular intrahepatic portosystemic stent-shunt. Subclinical portal-systemic encephalopathy and overt portal-systemic encephalopathy were determined by age-adjusted psychometric tests and clinical staging, respectively. Serum S100β was specifically elevated in the presence of subclinical or early portal-systemic encephalopathy, but not arterial ammonia. S100β levels elevated above a reference value (S100β ≤ 110pg/ml) or the cut off value determined in our group of patients (112pg/ml) predicted subclinical portal-systemic encephalopathy with a specificity and sensitivity of 100 and 56.5%, respectively. Serum S100β was significantly dependent on liver dysfunction (Child-Pugh score), but was more closely related to cognitive impairments than the score. Serum S100β seems to be a promising biochemical surrogate marker for mild cognitive impairments due to portal-systemic encephalopathy."],["dc.identifier.doi","10.1023/a:1020785009005"],["dc.identifier.gro","3151726"],["dc.identifier.pmid","10850551"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8547"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0885-7490"],["dc.title","Elevated Serum Levels of Astroglial S100β in Patients with Liver Cirrhosis Indicate Early and Subclinical Portal-Systemic Encephalopathy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","848"],["dc.bibliographiccitation.journal","Multiple Sclerosis Journal"],["dc.bibliographiccitation.lastpage","849"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Paap, Franziska"],["dc.contributor.author","Mueller, F."],["dc.contributor.author","Barrantes-Freer, Alonso"],["dc.contributor.author","Brueck, Wolfgang"],["dc.contributor.author","Nessler, S."],["dc.contributor.author","Stadelmann, Christine"],["dc.date.accessioned","2018-11-07T10:08:50Z"],["dc.date.available","2018-11-07T10:08:50Z"],["dc.date.issued","2016"],["dc.identifier.isi","000383267203281"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39546"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Sage Publications Ltd"],["dc.publisher.place","London"],["dc.relation.eventlocation","London, ENGLAND"],["dc.relation.issn","1477-0970"],["dc.relation.issn","1352-4585"],["dc.title","Histopathological characteristics of cavitary multiple sclerosis"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","112"],["dc.bibliographiccitation.journal","Brain Research"],["dc.bibliographiccitation.lastpage","119"],["dc.bibliographiccitation.volume","1116"],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Siegert, S."],["dc.contributor.author","Pfander, Tatjana"],["dc.contributor.author","Kramer, Michael L."],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Hewett, J. W."],["dc.contributor.author","Breakefield, X. O."],["dc.contributor.author","Hedreen, J. C."],["dc.contributor.author","Rostasy, Kevin"],["dc.date.accessioned","2018-11-07T09:06:00Z"],["dc.date.available","2018-11-07T09:06:00Z"],["dc.date.issued","2006"],["dc.description.abstract","Familial, early onset, generalized torsion dystonia is the most common and severe primary dystonia. The majority of cases are caused by a 3-bp deletion (GAG) in the coding region of the DYT1 (TOR1A) gene. The cellular and regional distribution of torsinA protein, which is restricted to neuronal cells and present in all brain regions by the age of 2 months has been described recently in human developing brain. TorsinB is a member of the same family of proteins and is highly homologous with its gene adjacent to that for torsinA on chromosome 9q34. TorsinA and torsinB share several remarkable features suggesting that they may interact in vivo. This study examined the expression of torsinB in the human brain of fetuses, infants and children up to 7 years of age. Our results indicate that torsinB protein expression is temporarily and spatially regulated in a similar fashion as torsinA. Expression of torsinB protein was detectable beginning at four to 8 weeks of age in the cerebellum (Purkinje cells), substantia nigra (dopaminergic neurons), hippocampus and basal ganglia and was predominantly restricted to neuronal cells. In contrast to torsinA, torsinB immunoreactivity was found more readily in the nuclear envelope. High levels of torsinB protein were maintained throughout infancy, childhood and adulthood suggesting that torsinB is also needed for developmental events occurring in the early postnatal phase and is necessary for functional activity throughout life. (c) 2006 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.brainres.2006.07.102"],["dc.identifier.isi","000241793900013"],["dc.identifier.pmid","16938275"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25457"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0006-8993"],["dc.title","TorsinB expression in the developing human brain"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","S297"],["dc.bibliographiccitation.journal","Multiple Sclerosis Journal"],["dc.bibliographiccitation.lastpage","S298"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Daumer, M."],["dc.contributor.author","Lederer, C."],["dc.contributor.author","Neuhaus, A."],["dc.contributor.author","Muraro, I. Galea P."],["dc.contributor.author","Scalfari, A. S."],["dc.contributor.author","Koch-Henriksen, Nils"],["dc.contributor.author","Heesen, Christoph"],["dc.contributor.author","Koepke, S."],["dc.contributor.author","Schaeffler, N."],["dc.contributor.author","Stellmann, J.-P."],["dc.contributor.author","Albrecht, H."],["dc.contributor.author","Winkelmann, Alexander"],["dc.contributor.author","Weber, F."],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Hauser, Michael"],["dc.contributor.author","Skoda, M."],["dc.contributor.author","Edan, G."],["dc.contributor.author","Ebers, G."],["dc.date.accessioned","2018-11-07T08:51:27Z"],["dc.date.available","2018-11-07T08:51:27Z"],["dc.date.issued","2011"],["dc.identifier.isi","000209137301045"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21937"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Sage Publications Ltd"],["dc.publisher.place","London"],["dc.relation.issn","1477-0970"],["dc.relation.issn","1352-4585"],["dc.title","Validation of a decision support system for the individual long-term prognosis of MS disease course: interim results from a web-based survey"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1339"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","1346"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Schwarz, P."],["dc.contributor.author","Reim, K."],["dc.contributor.author","Brechlin, P."],["dc.contributor.author","Jahn, O."],["dc.contributor.author","Kratzin, H."],["dc.contributor.author","Aitken, A."],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Aguzzi, A."],["dc.contributor.author","Bahn, E."],["dc.contributor.author","Baxter, Helen C."],["dc.contributor.author","Brose, N."],["dc.contributor.author","Otto, M."],["dc.date.accessioned","2017-09-07T11:43:02Z"],["dc.date.available","2017-09-07T11:43:02Z"],["dc.date.issued","2005"],["dc.description.abstract","The diagnosis of sporadic Creutzfeldt-Jakob disease (CJD) is based on typical clinical findings and is supported by a positive 14-3-3 Western blot of cerebrospinal fluid. However, it is not clear whether 14-3-3 indicates general neuronal damage or is of pathophysiological relevance in CJD. The fact that the 14-3-3 isoform spectrum in cerebrospinal fluid does not correspond to that found in the brain points to a regulated process. To investigate a possible role of 14-3-3 proteins in transmissible spongiform diseases, we generated a 14-3-3gamma-deficient mutant mouse line by using a classical knockout strategy. The anatomy and cage behavior of the mutant mice were normal. Western blot analyses of brain homogenates revealed no changes in the protein expression of other 14-3-3 isoforms (epsilon, beta, zeta, and eta). Proteomic analyses of mouse brains by two-dimensional differential gel electrophoresis showed that several proteins, including growth hormone, 1-Cys peroxiredoxin, CCT-zeta, glucose-6-phosphate isomerase, GRP170 precursor, and et-SNAP, were differentially expressed. Mutant and wild-type mice were inoculated either intracerebrally or intraperitoneally with the Rocky Mountain Laboratory strain of scrapie, but no differences were detected in the postinoculation survival rates. These results indicate that 14-3-3gamma is unlikely to play a causal role in CJD and related diseases."],["dc.identifier.doi","10.1128/MCB.25.4.1339-1346.2005"],["dc.identifier.gro","3143900"],["dc.identifier.isi","000226908000010"],["dc.identifier.pmid","15684385"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1465"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","Unchanged survival rates of 14-3-3 gamma knockout mice after inoculation with pathological prion protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]