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","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","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","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"]]

[["dc.bibliographiccitation.firstpage","518"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","The Journal of Infectious Diseases"],["dc.bibliographiccitation.lastpage","520"],["dc.bibliographiccitation.volume","180"],["dc.contributor.author","Beekes, Michael"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Poser, Sigrid"],["dc.contributor.author","Baier, Michael"],["dc.date.accessioned","2017-09-07T11:44:34Z"],["dc.date.available","2017-09-07T11:44:34Z"],["dc.date.issued","1999"],["dc.description.abstract","Following recent reports of elevated serum S100 β protein (S100 β) levels in patients with genetic and sporadic Creutzfeldt-Jakob disease and in rodents parenterally infected with scrapie, the suitability of serum S100 β as a preclinical marker for transmissible spongiform encephalopathies was assessed in time-course studies. Syrian hamsters were orally and intra-peritoneally challenged with scrapie and assayed for serum S100 β levels at various times after infection. Although elevated serum S100 β levels were consistently observed in terminally ill animals for both routes of infection, the experiments failed to detect significantly increased S100 β serum concentrations prior to the manifestation of clinical symptoms. Thus, in this animal model, serum S100 β does not appear to be an appropriate marker for the preclinical detection of scrapie, but it may provide a convenient laboratory aid for the diagnosis of transmissible spongiform encephalopathy in naturally or accidentally infected animals and humans."],["dc.identifier.doi","10.1086/314907"],["dc.identifier.gro","3151706"],["dc.identifier.pmid","10395873"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8525"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0022-1899"],["dc.title","Late Increase of Serum S100 β Protein Levels in Hamsters after Oral or Intraperitoneal Infection with Scrapie"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","171"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neuroscience Letters"],["dc.bibliographiccitation.lastpage","173"],["dc.bibliographiccitation.volume","240"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Boekhoff, Immo"],["dc.contributor.author","Beuche, Wolfgang"],["dc.date.accessioned","2017-09-07T11:44:38Z"],["dc.date.available","2017-09-07T11:44:38Z"],["dc.date.issued","1998"],["dc.description.abstract","Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease of unknown origin characterized by loss of upper and lower motor neurons and concomitant astrogliosis. We have investigated the S100 beta protein levels in serum as a marker for astroglia of patients with ALS (n=41) in comparison to a control group (n=32). Additionally we have investigated 12 patients at different follow-up time points (minimum 6 months). We could not observe a significant difference of S100 beta protein in patients with ALS in comparison to our control group (P=0.11) but we could clearly see a decrease of S100 beta levels in the further course of the disease. As S100 beta is also seen as a protein with nerve growth factor activity we assume that the fall of serum levels may reflect the loss of nerve growth stimulation in patients with ALS and suppose that repetitive measurements of S100 beta in serum can be used as an objective marker for disease progression."],["dc.identifier.doi","10.1016/s0304-3940(97)00947-6"],["dc.identifier.gro","3151715"],["dc.identifier.pmid","9502231"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8535"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0304-3940"],["dc.title","Decrease of S100 beta protein in serum of patients with amyotrophic lateral sclerosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","551"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","International Journal of Sports Medicine"],["dc.bibliographiccitation.lastpage","555"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Otto, M."],["dc.contributor.author","Holthusen, S."],["dc.contributor.author","Bahn, E."],["dc.contributor.author","Söhnchen, N."],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Geese, R."],["dc.contributor.author","Fischer, A."],["dc.contributor.author","Reimers, C. D."],["dc.date.accessioned","2017-09-07T11:44:38Z"],["dc.date.available","2017-09-07T11:44:38Z"],["dc.date.issued","2002"],["dc.description.abstract","Permanent neurological dysfunction is the primary medical concern of boxing. Recently it was reported that patients presenting elevated levels of the glial protein S-100B in serum after minor head injuries are more prone to develop neuropsychological deficits than patients with lower levels of S-100B protein. We assessed this protein before and after amateur boxing competitions (n = 10) and sparring bouts (n = 15). In several control groups, we investigated S-100B levels of participants before and after a 25 km race (n = 11), jogging (10 km, n = 12), short-term running (n = 12), and heading footballs (n = 12). There was an increase in S-100B protein after boxing and the running disciplines but not after ergometer cycling or soft heading of footballs. The increase in S-100B protein concentrations due to competitive boxing and after the 25 km race was significantly higher than that after performing other disciplines (p < 0.001). There was no significant difference between the increases caused by sparring and the running disciplines (p = 0.21). The number and severity of the strikes to the head correlated significantly with the increase in the S-100B protein levels. Levels of S-100B protein known to be associated with neuropsychological deficits were not reached in our study. In professional boxing, much higher levels are to be expected and would be worthy of investigation."],["dc.identifier.doi","10.1055/s-2000-8480"],["dc.identifier.gro","3151716"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8536"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0172-4622"],["dc.title","Boxing and Running Lead to a Rise in Serum Levels of S-100B Protein"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","366"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Neurodegenerative Diseases"],["dc.bibliographiccitation.lastpage","375"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Bibl, Mirko"],["dc.contributor.author","Brechlin, Peter"],["dc.contributor.author","Schlossmacher, Michael G."],["dc.contributor.author","Locascio, Joseph J."],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Kretzschmar, Hans A."],["dc.contributor.author","Poser, Sigrid"],["dc.contributor.author","Trenkwalder, Claudia"],["dc.contributor.author","Otto, Markus"],["dc.date.accessioned","2018-11-07T11:07:10Z"],["dc.date.available","2018-11-07T11:07:10Z"],["dc.date.issued","2007"],["dc.description.abstract","Background: The measurement of biomarkers in cerebrospinal fluid (CSF) has gained increasing acceptance in establishing the diagnosis of some neurodegenerative diseases. Heart-type fatty acid-binding protein (H-FABP) was recently discovered in CSF and serum of patients with neurodegenerative diseases. Objective: We investigated H-FABP in CSF and serum alone and in combination with CSF tau protein to evaluate these as potential biomarkers for the differentiation between dementia with Lewy bodies (DLB) and Alzheimer's disease (AD). Methods: We established H-FABP and tau protein values in a set of 144 persons with DLB (n = 33), Parkinson disease with dementia (PDD; n = 25), AD (n = 35) and nonclemented neurological controls (NNC; n = 51). Additionally, serum H-FABP levels were analyzed in idiopathic Parkinson disease patients without evidence of cognitive decline (n = 45) using commercially available enzyme-linked immunosorbent assays. We calculated absolute values of HFABP and tau protein in CSF and serum and established relative ratios between the two to obtain the best possible match for the clinical working diagnosis. Results: Serum HFABP levels were elevated in DLB and PDD patients compared with NNC and AD subjects. To better discriminate between DLB and AD, we calculated the ratio of serum H-FABP to CSF tau protein levels. At the arbitrary chosen cutoff ratio >= 8 this quotient reached a sensitivity of 91% and a specificity of 66%. Conclusion: Our results suggest that the measurement of CSF tau protein, together with H-FABP quantification in serum and CSF, and the ratio of serum H-FABP to CSF tau protein represent marker candidates for the differentiation between AD and DLB. Copyright (c) 2007 S. Karger AG, Basel."],["dc.identifier.doi","10.1159/000105157"],["dc.identifier.isi","000248386400002"],["dc.identifier.pmid","17622779"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52491"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1660-2854"],["dc.title","Serum heart-type fatty acid-binding protein and cerebrospinal fluid tau: Marker candidates for dementia with Lewy bodies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","572"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Neurovirology"],["dc.bibliographiccitation.lastpage","573"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Beekes, Michael"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Bahn, Erik"],["dc.contributor.author","Poser, S."],["dc.contributor.author","Diringer, Heino"],["dc.date.accessioned","2017-09-07T11:44:40Z"],["dc.date.available","2017-09-07T11:44:40Z"],["dc.date.issued","2009"],["dc.description.abstract","Recently, immunoluminometric analysis revealed elevated levels of serum SlOO beta protein in sporadic and genetic cases of Creutzfeldt-Jakob disease (CJD) as compared to demented and non-demented control patients (Otto et al, 1998). SlOO beta protein is a well established marker for the activation of astrocytes and also shows enhanced histochemical presentation in Alzheimer's disease (Sheng et al, 1997). Thus, it will be necessary to precisely assess the specificity of the new test for human transmissible spongiform encephalopathies (TSE) in larger study populations."],["dc.identifier.doi","10.3109/13550289809113503"],["dc.identifier.gro","3151709"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8528"],["dc.language.iso","en"],["dc.notes.status","public"],["dc.notes.submitter","chake"],["dc.relation.issn","1355-0284"],["dc.title","Elevated levels of serum SlOO beta protein in scrapie hamsters"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]