Bayer, Thomas A.

[["dc.bibliographiccitation.journal","European Neuropsychopharmacology"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2018-11-07T11:24:51Z"],["dc.date.available","2018-11-07T11:24:51Z"],["dc.date.issued","2009"],["dc.format.extent","S211"],["dc.identifier.isi","000270312500101"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56500"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.publisher.place","Amsterdam"],["dc.relation.conference","22nd Congress of the European-College-of-Neuropsychopharmacology"],["dc.relation.eventlocation","Istanbul, TURKEY"],["dc.relation.issn","0924-977X"],["dc.title","Paradigm shift in Abeta toxicity"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","4S_Part_12"],["dc.bibliographiccitation.journal","Alzheimer's & Dementia"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Bouter, Yvonne"],["dc.contributor.author","Dietrich, Katharina"],["dc.contributor.author","Wittnam, Jessica"],["dc.contributor.author","Pillot, Thierry"],["dc.contributor.author","Papot‐Couturier, Sophie"],["dc.contributor.author","Lefebvre, Thomas"],["dc.contributor.author","Sprenger, Frederick"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Bayer, Thomas"],["dc.date.accessioned","2021-12-08T12:27:20Z"],["dc.date.available","2021-12-08T12:27:20Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1016/j.jalz.2013.05.1031"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/95321"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.eissn","1552-5279"],["dc.relation.issn","1552-5260"],["dc.rights.uri","http://onlinelibrary.wiley.com/termsAndConditions#vor"],["dc.title","P2–382: Tg4–42: A new mouse model of Alzheimer's disease—N‐truncated amyloid β (Aβ) 4–42 induces severe neuron loss and behavioral deficits"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","38"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","39"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Christensen, Ditte Zerlang"],["dc.contributor.author","Bayer, Thomas A."],["dc.date.accessioned","2018-11-07T08:28:16Z"],["dc.date.available","2018-11-07T08:28:16Z"],["dc.date.issued","2009"],["dc.identifier.isi","000266400900098"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16383"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.publisher.place","Malden"],["dc.relation.conference","4th European-Society-for-Neurochemistry Conference on Advances in Molecular Mechanisms of Neurological Disorders"],["dc.relation.eventlocation","Leipzig, GERMANY"],["dc.relation.issn","0022-3042"],["dc.title","Increasing Abeta peptide levels aggravate axonal degeneration in an Alzheimer mouse model"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","849"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","858"],["dc.bibliographiccitation.volume","67"],["dc.contributor.author","Hornung, Karen"],["dc.contributor.author","Zampar, Silvia"],["dc.contributor.author","Engel, Nadine"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2020-12-10T18:44:12Z"],["dc.date.available","2020-12-10T18:44:12Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3233/JAD-181134"],["dc.identifier.eissn","1875-8908"],["dc.identifier.issn","1387-2877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78365"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","N-Terminal Truncated Aβ4-42 Is a Substrate for Neprilysin Degradation in vitro and in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","101"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Alzheimer s Disease"],["dc.bibliographiccitation.lastpage","110"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Savastano, Adriana"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Haussman, Ute"],["dc.contributor.author","Oberstein, Timo Jan"],["dc.contributor.author","Mueller, Petr"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Bayer, Thomas A."],["dc.date.accessioned","2018-11-07T10:21:48Z"],["dc.date.available","2018-11-07T10:21:48Z"],["dc.date.issued","2016"],["dc.description.abstract","According to the modified amyloid hypothesis, the key event in the pathogenesis of Alzheimer's disease (AD) is the deposition of neurotoxic amyloid beta-peptides (A beta s) in plaques and cerebral blood vessels. Additionally to full-length peptides, a great diversity of N-truncated A beta variants is derived from the larger amyloid-beta protein precursor (A beta PP). Vast evidence suggests that A beta(x-42) isoforms play an important role in triggering neurodegeneration due to their high abundance, amyloidogenic propensity and toxicity. Although N-truncated Ap peptides and A beta(x-42) species appear to be the crucial players in AD etiology, the A beta(2-x) isoforms did not receive much attention yet. The present study is the first to show immunohistochemical evidence of A beta(2-x) in cases of AD and its distribution in Al3PP/PS 1KI and 5XFAD transgenic mouse models using a novel antibody pAB77 that has been developed using A132-14 as antigen. Positive plaques and congophilic amyloid angiopathy (CAA) were observed in AD cases and in both mouse models. While in AD cases, abundant CAA and less pronounced plaque pathology was evident, the two mouse models showed predominantly extracellular Ap deposits and minor CAA staining. Western blotting and a capillary isoelectric focusing immunoassay demonstrated the high specificity of the antibody pAb77 against A13-variants starting with the N-terminal Alanine-2."],["dc.identifier.doi","10.3233/JAD-150394"],["dc.identifier.isi","000364409100012"],["dc.identifier.pmid","26529393"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42160"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Ios Press"],["dc.relation.issn","1875-8908"],["dc.relation.issn","1387-2877"],["dc.title","N-Truncated A beta(2-X) Starting with Position Two in Sporadic Alzheimer's Disease Cases and Two Alzheimer Mouse Models"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10101"],["dc.bibliographiccitation.issue","31"],["dc.bibliographiccitation.journal","Chemistry - A European Journal"],["dc.bibliographiccitation.lastpage","10106"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Albers, Antonia"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Demeshko, Serhiy"],["dc.contributor.author","Dechert, Sebastian"],["dc.contributor.author","Meyer, Franc"],["dc.date.accessioned","2018-11-07T09:22:18Z"],["dc.date.available","2018-11-07T09:22:18Z"],["dc.date.issued","2013"],["dc.description.sponsorship","DFG [IGRK 1422]; Cusanuswerk"],["dc.identifier.doi","10.1002/chem.201301760"],["dc.identifier.isi","000321983700006"],["dc.identifier.pmid","23780647"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29311"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0947-6539"],["dc.title","A Functional Model for the Rieske Center: Full Characterization of a Biomimetic N-Ligated [2Fe-2S] Cluster in Different Protonation States"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","871"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Alzheimer s Disease"],["dc.bibliographiccitation.lastpage","881"],["dc.bibliographiccitation.volume","39"],["dc.contributor.author","Reinert, Jochim"],["dc.contributor.author","Martens, Henrik"],["dc.contributor.author","Huettenrauch, Melanie"],["dc.contributor.author","Kolbow, Tekla"],["dc.contributor.author","Lannfelt, Lars"],["dc.contributor.author","Ingelsson, Martin"],["dc.contributor.author","Paetau, Anders"],["dc.contributor.author","Verkkoniemi-Ahola, Auli"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2018-11-07T09:46:32Z"],["dc.date.available","2018-11-07T09:46:32Z"],["dc.date.issued","2014"],["dc.description.abstract","The pathogenesis of Alzheimer's disease (AD) is believed to be closely dependent on deposits of neurotoxic amyloid-beta peptides (A beta), which become abundantly present throughout the central nervous system in advanced stages of the disease. The different A beta peptides existing are generated by subsequent cleavage of the amyloid-beta protein precursor (A beta PP) and may vary in length and differ at their C-terminus. Despite extensive studies on the most prevalent species A beta(40) and A beta(42), A beta peptides with other C-termini such as A beta(38) have not received much attention. In the present study, we used a highly specific and sensitive antibody against A beta(38) to analyze the distribution of this A beta species in cases of sporadic and familial AD, as well as in the brains of a series of established transgenic AD mouse models. We found A beta(38) to be present as vascular deposits in the brains of the majority of sporadic AD cases, whereas it is largely absent in non-demented control cases. A beta(38)-positive extracellular plaques were virtually limited to familial cases. Interestingly we observed A beta(38)-positive plaques not only among familial cases due to A beta PP mutations, but also in cases of familial AD caused by presenilin (PSEN) mutations. Furthermore we demonstrate that A beta(38) deposits in the form of extracellular plaques are common in several AD transgenic mouse models carrying either only A beta PP, or combinations of A beta PP, PSEN1, and tau transgenes."],["dc.identifier.doi","10.3233/JAD-131373"],["dc.identifier.isi","000331842500017"],["dc.identifier.pmid","24305500"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34892"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Ios Press"],["dc.relation.issn","1875-8908"],["dc.relation.issn","1387-2877"],["dc.title","A beta(38) in the Brains of Patients with Sporadic and Familial Alzheimer's Disease and Transgenic Mouse Models"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e34095"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Grimm, Marc-Oliver"],["dc.contributor.author","Zinser, Eva G."],["dc.contributor.author","Groesgen, Sven"],["dc.contributor.author","Hundsdoerfer, Benjamin"],["dc.contributor.author","Rothhaar, Tatjana L."],["dc.contributor.author","Burg, Verena K."],["dc.contributor.author","Kaestner, Lars"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Lipp, Peter"],["dc.contributor.author","Mueller, Ulrike"],["dc.contributor.author","Grimm, Heike S."],["dc.contributor.author","Hartmann, Tobias"],["dc.date.accessioned","2018-11-07T09:12:08Z"],["dc.date.available","2018-11-07T09:12:08Z"],["dc.date.issued","2012"],["dc.description.abstract","Gangliosides are important players for controlling neuronal function and are directly involved in AD pathology. They are among the most potent stimulators of A beta production, are enriched in amyloid plaques and bind amyloid beta (A beta). However, the molecular mechanisms linking gangliosides with AD are unknown. Here we identified the previously unknown function of the amyloid precursor protein (APP), specifically its cleavage products A beta and the APP intracellular domain (AICD), of regulating GD3-synthase (GD3S). Since GD3S is the key enzyme converting a-to b-series gangliosides, it therefore plays a major role in controlling the levels of major brain gangliosides. This regulation occurs by two separate and additive mechanisms. The first mechanism directly targets the enzymatic activity of GD3S: Upon binding of A beta to the ganglioside GM3, the immediate substrate of the GD3S, enzymatic turnover of GM3 by GD3S was strongly reduced. The second mechanism targets GD3S expression. APP cleavage results, in addition to A beta release, in the release of AICD, a known candidate for gene transcriptional regulation. AICD strongly down regulated GD3S transcription and knock-in of an AICD deletion mutant of APP in vivo, or knock-down of Fe65 in neuroblastoma cells, was sufficient to abrogate normal GD3S functionality. Equally, knock-out of the presenilin genes, presenilin 1 and presenilin 2, essential for A beta and AICD production, or of APP itself, increased GD3S activity and expression and consequently resulted in a major shift of a- to b-series gangliosides. In addition to GD3S regulation by APP processing, gangliosides in turn altered APP cleavage. GM3 decreased, whereas the ganglioside GD3, the GD3S product, increased A beta production, resulting in a regulatory feedback cycle, directly linking ganglioside metabolism with APP processing and A beta generation. A central aspect of this homeostatic control is the reduction of GD3S activity via an A beta-GM3 complex and AICD-mediated repression of GD3S transcription."],["dc.identifier.doi","10.1371/journal.pone.0034095"],["dc.identifier.isi","000304489000064"],["dc.identifier.pmid","22470521"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7774"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26881"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Amyloid Precursor Protein (APP) Mediated Regulation of Ganglioside Homeostasis Linking Alzheimer's Disease Pathology with Ganglioside Metabolism"],["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","1153"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Neurobiology of Aging"],["dc.bibliographiccitation.lastpage","1163"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Christensen, Ditte Zerlang"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2018-11-07T08:41:56Z"],["dc.date.available","2018-11-07T08:41:56Z"],["dc.date.issued","2010"],["dc.description.abstract","Loss of cholinergic neurons in the Nucleus Basalis of Meynert in Alzheimer's disease (AD) patients was one of the first discoveries of neuron loss in AD. Despite an intense focus on the cholinergic system in AD, the reason for this cholinergic neuron loss is yet unknown. In the present study we examined A beta-induced pathology and neuron loss in the cholinergic system of the bigenic APP/PS1KI mouse model. Expression of the APP transgene was found in ChAT-positive neurons of motor nuclei accompanied by robust intracellular A beta accumulation, whereas no APP expressing neurons and thus no intracellular A beta accumulation were found in neither the forebrain or pons complexes, nor in the caudate putamen. This expression pattern was used as a model system to study the effect of intra- and extracellular A beta accumulation on neuron loss in the cholinergic system. Stereological quantification revealed a loss of ChAT-positive neurons in APP/PS1KI mice only in the motor nuclei Mo5 and 7N accumulating intracellular A beta. This study supports the hypothesis of intracellular A beta accumulation as an early pathological alteration contributing to cell death in AD. (C) 2008 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.neurobiolaging.2008.07.022"],["dc.identifier.isi","000278438300008"],["dc.identifier.pmid","18771817"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19581"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","0197-4580"],["dc.title","Intracellular A beta triggers neuron loss in the cholinergic system of the APP/PS1KI mouse model of Alzheimer's disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","26"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Neurodegeneration"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Ramos-Miguel, Alfredo"],["dc.contributor.author","García-Sevilla, Jesús A."],["dc.contributor.author","Barr, Alasdair M."],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Falkai, Peter"],["dc.contributor.author","Leurgans, Sue E."],["dc.contributor.author","Schneider, Julie A."],["dc.contributor.author","Bennett, David A."],["dc.contributor.author","Honer, William G."],["dc.contributor.author","García-Fuster, M. J."],["dc.date.accessioned","2019-07-09T11:43:17Z"],["dc.date.available","2019-07-09T11:43:17Z"],["dc.date.issued","2017"],["dc.description.abstract","Abstract Background FADD (Fas-associated death domain) adaptor is a crucial protein involved in the induction of cell death but also mediates non-apoptotic actions via a phosphorylated form (p-Ser194-FADD). This study investigated the possible association of FADD forms with age-related neuropathologies, cognitive function, and the odds of dementia in an elderly community sample. Methods FADD forms were quantified by western blot analysis in dorsolateral prefrontal cortex (DLPFC) samples from a large cohort of participants in a community-based aging study (Memory and Aging Project, MAP), experiencing no-(NCI, n = 51) or mild-(MCI, n = 42) cognitive impairment, or dementia (n = 57). Results Cortical FADD was lower in subjects with dementia and lower FADD was associated with a greater load of amyloid-β pathology, fewer presynaptic terminal markers, poorer cognitive function and increased odds of dementia. Together with the observations of FADD redistribution into tangles and dystrophic neurites within plaques in Alzheimer\\’s disease brains, and its reduction in APP23 mouse cortex, the results suggest this multifunctional protein might participate in the mechanisms linking amyloid and tau pathologies during the course of the illness. Conclusions The present data suggests FADD as a putative biomarker for pathological processes associated with the course of clinical dementia."],["dc.identifier.doi","10.1186/s13024-017-0168-x"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58852"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","BioMed Central"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Decreased cortical FADD protein is associated with clinical dementia and cognitive decline in an elderly community sample"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]