Paul, Shanty

[["dc.bibliographiccitation.firstpage","263"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Annals of Neurology"],["dc.bibliographiccitation.lastpage","267"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Esselmann, Herrmann"],["dc.contributor.author","Smirnov, Alexey"],["dc.contributor.author","Bibl, Mirko"],["dc.contributor.author","Cepek, L."],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Buerger, Katharina"],["dc.contributor.author","Hampel, Harald"],["dc.contributor.author","Paul, S."],["dc.contributor.author","Neumann, M."],["dc.contributor.author","Maler, M."],["dc.contributor.author","Zerr, I."],["dc.contributor.author","Kornhuber, Johannes"],["dc.contributor.author","Kretzschmar, Hans A."],["dc.contributor.author","Poser, Sigrid"],["dc.contributor.author","Otto, Markus"],["dc.date.accessioned","2018-11-07T10:37:04Z"],["dc.date.available","2018-11-07T10:37:04Z"],["dc.date.issued","2003"],["dc.description.abstract","Decreased levels of beta-amyloid peptide 1-42 (Abeta1-42) in cerebrospinal fluid (CSF) are a characteristic feature of Alzheimer's disease (AD) but recently were also observed in Creutzfeldt-Jakob disease (CJD). We analyzed the CSF of patients with CJD, and AD and nondemented controls using a quantitative urea-based Abeta sodium dodecyl sulfate polyacrylamide gel electrophoresis immunoblot. Like in AD and nondemented controls, we found a highly conserved pattern of carboxyterminally truncated Abeta1-37/38/39 in addition to Abeta1-40/42 also in CJD patients. By the introduction of the ratio Abeta1-39 to Abeta1-42, CJD and AD can effectively be differentiated. We conclude that the immunoblot shows disease-specific CSF Abeta peptide patterns in CJD and AD and suppose that measurement of the Abeta peptide pattern seems to be a promising diagnostic tool in the differential diagnosis of dementias."],["dc.identifier.doi","10.1002/ana.10661"],["dc.identifier.isi","000184352700021"],["dc.identifier.pmid","12891683"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45476"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.relation.issn","0364-5134"],["dc.title","beta-Amyloid peptides in cerebrospinal fluid of patients with 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.issue","1"],["dc.bibliographiccitation.journal","Neurobiology of Aging"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Esselmann, Herrmann"],["dc.contributor.author","Kunz, N."],["dc.contributor.author","Smirnov, Alexey"],["dc.contributor.author","Paul, S."],["dc.contributor.author","Dombek, M."],["dc.contributor.author","Ruether, Eckhart"],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Maler, M."],["dc.contributor.author","Kornhuber, Johannes"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Hampel, Harald"],["dc.contributor.author","Buerger, Katharina"],["dc.date.accessioned","2018-11-07T10:23:03Z"],["dc.date.available","2018-11-07T10:23:03Z"],["dc.date.issued","2002"],["dc.format.extent","S17"],["dc.identifier.isi","000177465300067"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42384"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.publisher.place","New york"],["dc.relation.issn","0197-4580"],["dc.title","Primary cell culture of chicken telencephalon: A model to study the catabolic processing of endogenous amyloid precursor protein and abeta peptides"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Pharmacopsychiatry"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Maler, Juan Manuel"],["dc.contributor.author","Esselmann, Herrmann"],["dc.contributor.author","Dyrks, T."],["dc.contributor.author","Klafki, H."],["dc.contributor.author","Fiszer, M."],["dc.contributor.author","Paul, S."],["dc.contributor.author","Reulbach, Udo"],["dc.contributor.author","Lewczuk, Piotr"],["dc.contributor.author","Ruther, Eckart"],["dc.contributor.author","Kornhuber, Johannes"],["dc.contributor.author","Wiltfang, J."],["dc.date.accessioned","2018-11-07T10:56:36Z"],["dc.date.available","2018-11-07T10:56:36Z"],["dc.date.issued","2005"],["dc.format.extent","262"],["dc.identifier.isi","000232591900164"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50051"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Georg Thieme Verlag Kg"],["dc.publisher.place","Stuttgart"],["dc.relation.conference","24th Symposium of the Arbeitsgemeinschaft-fur-Neuropsychopharmakologie-und-Pharmakopsychiatrie (AGNP)"],["dc.relation.eventlocation","Munich, GERMANY"],["dc.relation.issn","0176-3679"],["dc.title","Specific inhibition of beta-amyloid peptide secretion by ZK808762 mimicks the effect of non-steroidal antiinflammatory drugs"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Neurobiology of Aging"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Wiltfang, J."],["dc.contributor.author","Esselmann, Herrmann"],["dc.contributor.author","Bibl, Mirko"],["dc.contributor.author","Smirnov, Alexey"],["dc.contributor.author","Paul, S."],["dc.contributor.author","Ruether, Eckhart"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Schmidt, B."],["dc.contributor.author","Klafki, H. W."],["dc.contributor.author","Maler, M."],["dc.contributor.author","Kornhuber, Johannes"],["dc.contributor.author","Dyrks, T."],["dc.contributor.author","Bienert, M."],["dc.contributor.author","Beyermann, M."],["dc.date.accessioned","2018-11-07T10:23:20Z"],["dc.date.available","2018-11-07T10:23:20Z"],["dc.date.issued","2002"],["dc.format.extent","S275"],["dc.identifier.isi","000177465301009"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42438"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.publisher.place","New york"],["dc.relation.issn","0197-4580"],["dc.title","Highly conserved and disease-specific patterns of carboxyterminally truncated abeta peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","236"],["dc.bibliographiccitation.issue","4-5"],["dc.bibliographiccitation.journal","Neurodegenerative Diseases"],["dc.bibliographiccitation.lastpage","241"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Esselmann, Hermann"],["dc.contributor.author","Maler, J. M."],["dc.contributor.author","Kunz, N."],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Paul, S."],["dc.contributor.author","Lewczuk, Piotr"],["dc.contributor.author","Rüther, Eckart"],["dc.contributor.author","Kornhuber, Johannes"],["dc.contributor.author","Wiltfang, Jens"],["dc.date.accessioned","2017-09-07T11:44:27Z"],["dc.date.available","2017-09-07T11:44:27Z"],["dc.date.issued","2004"],["dc.description.abstract","We studied endogenous amyloid precursor protein (APP) processing and amyloid beta (Aβ) peptide formation in primary chicken telencephalic neurons, because their Aβ peptide sequence is identical to humans. As detected by quantitative Aβ-SDS-PAGE/immunoblot, Aβ peptides 1–40/42 and three additional C-truncated species, namely Aβ1–37/38/39 were regularly released into the supernatant. The highly conserved Aβ quintet strongly resembles the pattern of Aβ peptides found in human cerebrospinal fluid. Furthermore, the C-terminally shorter Aβ peptides 1–33/34 could be readily detected. Recent evidence indicates that lithium specifically inhibits secretion of the amyloidogenic Aβ1–42 peptide in cultured permanent cells transfected with human APP. We therefore investigated the effect of lithium on Aβ peptide secretion as well as intracellular Aβ peptides in our untransfected primary cell culture system. Our data shows that lithium leads to a dose-dependent reduction of Aβ1–37/38/39/40/42 secretion. Surprisingly, intracellular analysis revealed that lithium specifically increases a band comigrating with synthetic Aβ1–38 while Aβ1–40 and Aβ1–42 remained almost unaffected. These results demonstrate for the first time that lithium treatment decreases Aβ peptide secretion in primary chicken neuronal cells but specifically elevates intracellular Aβ1–38. Therefore, we conclude that there are two independent mechanisms of lithium in intra- and extracellular Aβ peptide production."],["dc.identifier.doi","10.1159/000080992"],["dc.identifier.gro","3151670"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8488"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","chake"],["dc.relation.issn","1660-2854"],["dc.title","Lithium Decreases Secretion of Aβ1–42 and C-Truncated Species Aβ1–37/38/39/40 in Chicken Telencephalic Cultures but Specifically Increases Intracellular Aβ1–38"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","481"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","496"],["dc.bibliographiccitation.volume","81"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Esselmann, Hermann"],["dc.contributor.author","Bibl, M."],["dc.contributor.author","Smirnov, A."],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Paul, S."],["dc.contributor.author","Schmidt, B."],["dc.contributor.author","Klafki, Hans-Wolfgang"],["dc.contributor.author","Maler, Manuel"],["dc.contributor.author","Dyrks, T."],["dc.contributor.author","Bienert, M."],["dc.contributor.author","Beyermann, Michael"],["dc.contributor.author","Rüther, Eckart"],["dc.contributor.author","Kornhuber, Johannes"],["dc.date.accessioned","2017-09-07T11:44:26Z"],["dc.date.available","2017-09-07T11:44:26Z"],["dc.date.issued","2003"],["dc.description.abstract","Human lumbar CSF patterns of Aβ peptides were analysed by urea-based β-amyloid sodium dodecyl sulphate polyacrylamide gel electrophoresis with western immunoblot (Aβ-SDS–PAGE/immunoblot). A highly conserved pattern of carboxyterminally truncated Aβ1–37/38/39 was found in addition to Aβ1–40 and Aβ1–42. Remarkably, Aβ1–38 was present at a higher concentration than Aβ1–42, being the second prominent Aβ peptide species in CSF. Patients with Alzheimer's disease (AD, n = 12) and patients with chronic inflammatory CNS disease (CID, n = 10) were differentiated by unique CSF Aβ peptide patterns from patients with other neuropsychiatric diseases (OND, n = 37). This became evident only when we investigated the amount of Aβ peptides relative to their total Aβ peptide concentration (Aβ1–x%, fractional Aβ peptide pattern), which may reflect disease-specific γ-secretase activities. Remarkably, patients with AD and CID shared elevated Aβ1–38% values, whereas otherwise the patterns were distinct, allowing separation of AD from CID or OND patients without overlap. The presence of one or two ApoE ε4 alleles resulted in an overall reduction of CSF Aβ peptides, which was pronounced for Aβ1–42. The severity of dementia was significantly correlated to the fractional Aβ peptide pattern but not to the absolute Aβ peptide concentrations."],["dc.identifier.doi","10.1046/j.1471-4159.2002.00818.x"],["dc.identifier.gro","3151651"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8468"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","chake"],["dc.relation.issn","0022-3042"],["dc.title","Highly conserved and disease-specific patterns of carboxyterminally truncated Aβ peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]