Wirths, Oliver

[["dc.bibliographiccitation.firstpage","6564"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","21"],["dc.contributor.affiliation","Klafki, Hans W.; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, hans.klafki@med.uni-goettingen.de"],["dc.contributor.affiliation","Rieper, Petra; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, petra.rieper@med.uni-goettingen.de"],["dc.contributor.affiliation","Matzen, Anja; \t\t \r\n\t\t IBL International GmbH, Tecan Group Company, D-22335 Hamburg, Germany, Anja.Matzen@tecan.com"],["dc.contributor.affiliation","Zampar, Silvia; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, silvia.zampar@med.uni-goettingen.de"],["dc.contributor.affiliation","Wirths, Oliver; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, oliver.wirths@medizin.uni-goettingen.de"],["dc.contributor.affiliation","Vogelgsang, Jonathan; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, jonathan.vogelgsang@med.uni-goettingen.de"],["dc.contributor.affiliation","Osterloh, Dirk; \t\t \r\n\t\t Roboscreen GmbH, D-04129 Leipzig, Germany, dirk.osterloh@roboscreen.com"],["dc.contributor.affiliation","Rohdenburg, Lara; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, lara.rohdenburg@stud.uni-goettingen.de"],["dc.contributor.affiliation","Oberstein, Timo J.; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, Friedrich-Alexander-University of Erlangen-Nuremberg, D-91054 Erlangen, Germany, Timo.Oberstein@uk-erlangen.de"],["dc.contributor.affiliation","Jahn, Olaf; \t\t \r\n\t\t Max-Planck-Institute of Experimental Medicine, Proteomics Group, D-37075 Göttingen, Germany, jahn@em.mpg.de"],["dc.contributor.affiliation","Beyer, Isaak; \t\t \r\n\t\t Faculty of Chemistry, Technische Universität Dresden, D-01069 Dresden, Germany, isaak.beyer@web.de"],["dc.contributor.affiliation","Lachmann, Ingolf; \t\t \r\n\t\t Roboscreen GmbH, D-04129 Leipzig, Germany, ingolf.lachmann@roboscreen.com"],["dc.contributor.affiliation","Knölker, Hans-Joachim; \t\t \r\n\t\t Faculty of Chemistry, Technische Universität Dresden, D-01069 Dresden, Germany, hans-joachim.knoelker@tu-dresden.de"],["dc.contributor.affiliation","Wiltfang, Jens; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, Jens.Wiltfang@med.uni-goettingen.de\t\t \r\n\t\t German Center for Neurodegenerative Diseases (DZNE), D-37075 Göttingen, Germany, Jens.Wiltfang@med.uni-goettingen.de\t\t \r\n\t\t Neurosciences and Signaling Group, Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, 3810-193 Aveiro, Portugal, Jens.Wiltfang@med.uni-goettingen.de"],["dc.contributor.author","Klafki, Hans W."],["dc.contributor.author","Rieper, Petra"],["dc.contributor.author","Matzen, Anja"],["dc.contributor.author","Zampar, Silvia"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Vogelgsang, Jonathan"],["dc.contributor.author","Osterloh, Dirk"],["dc.contributor.author","Rohdenburg, Lara"],["dc.contributor.author","Oberstein, Timo J."],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Beyer, Isaak"],["dc.contributor.author","Lachmann, Ingolf"],["dc.contributor.author","Knölker, Hans-Joachim"],["dc.contributor.author","Wiltfang, Jens"],["dc.date.accessioned","2021-04-14T08:32:33Z"],["dc.date.available","2021-04-14T08:32:33Z"],["dc.date.issued","2020"],["dc.date.updated","2022-09-06T16:24:24Z"],["dc.identifier.doi","10.3390/ijms21186564"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17555"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83948"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","1422-0067"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Development and Technical Validation of an Immunoassay for the Detection of APP669–711 (Aβ−3–40) in Biological Samples"],["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","175909141989269"],["dc.bibliographiccitation.journal","ASN Neuro"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Gerberding, Anna-Lina"],["dc.contributor.author","Zampar, Silvia"],["dc.contributor.author","Stazi, Martina"],["dc.contributor.author","Liebetanz, David"],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2020-12-10T18:38:38Z"],["dc.date.available","2020-12-10T18:38:38Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1177/1759091419892692"],["dc.identifier.eissn","1759-0914"],["dc.identifier.issn","1759-0914"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16938"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77392"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","Physical Activity Ameliorates Impaired Hippocampal Neurogenesis in the Tg4-42 Mouse Model of Alzheimer’s Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","555"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Acta Neuropathologica"],["dc.bibliographiccitation.lastpage","566"],["dc.bibliographiccitation.volume","119"],["dc.contributor.author","Christensen, Ditte Zerlang"],["dc.contributor.author","Schneider-Axmann, Thomas"],["dc.contributor.author","Lucassen, Paul J."],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2018-11-07T08:43:18Z"],["dc.date.available","2018-11-07T08:43:18Z"],["dc.date.issued","2010"],["dc.description.abstract","In contrast to extracellular plaque and intracellular tangle pathology, the presence and relevance of intraneuronal A beta in Alzheimer's disease (AD) is still a matter of debate. Human brain tissue offers technical challenges such as post-mortem delay and uneven or prolonged tissue fixation that might affect immunohistochemical staining. In addition, previous studies on intracellular A beta accumulation in human brain often used antibodies targeting the C-terminus of A beta and differed strongly in the pretreatments used. To overcome these inconsistencies, we performed extensive parametrical testing using a highly specific N-terminal A beta antibody detecting the aspartate at position 1, before developing an optimal staining protocol for intraneuronal A beta detection in paraffin-embedded sections from AD patients. To rule out that this antibody also detects the beta-cleaved APP C-terminal fragment (beta-CTF, C99) bearing the same epitope, paraffin-sections of transgenic mice overexpressing the C99-fragment were stained without any evidence for cross-reactivity in our staining protocol. The staining intensity of intraneuronal A beta in cortex and hippocampal tissue of 10 controls and 20 sporadic AD cases was then correlated to patient data including sex, Braak stage, plaque load, and apolipoprotein E (ApoE) genotype. In particular, the presence of one or two ApoE4 alleles strongly correlated with an increased accumulation of intraneuronal A beta peptides. Given that ApoE4 is a major genetic risk factor for AD and is involved in neuronal cholesterol transport, it is tempting to speculate that perturbed intracellular trafficking is involved in the increased intraneuronal A beta aggregation in AD."],["dc.identifier.doi","10.1007/s00401-010-0666-1"],["dc.identifier.isi","000276353400003"],["dc.identifier.pmid","20217101"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/4175"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19930"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0001-6322"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Accumulation of intraneuronal A beta correlates with ApoE4 genotype"],["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.issue","1"],["dc.bibliographiccitation.journal","Acta neuropathologica communications"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Kalimo, Hannu"],["dc.contributor.author","Lalowski, Maciej"],["dc.contributor.author","Bogdanovic, Nenad"],["dc.contributor.author","Philipson, Ola"],["dc.contributor.author","Bird, Thomas D."],["dc.contributor.author","Nochlin, David"],["dc.contributor.author","Schellenberg, Gerard D."],["dc.contributor.author","Brundin, Rosemarie"],["dc.contributor.author","Olofsson, Tommie"],["dc.contributor.author","Soliymani, Rabah"],["dc.contributor.author","Baumann, Marc"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Nilsson, Lars"],["dc.contributor.author","Basun, Hans"],["dc.contributor.author","Lannfelt, Lars"],["dc.contributor.author","Ingelsson, Martin"],["dc.date.accessioned","2019-07-09T11:42:19Z"],["dc.date.available","2019-07-09T11:42:19Z"],["dc.date.issued","2013"],["dc.description.abstract","BACKGROUND: The Arctic mutation (p.E693G/p.E22G)fs within the β-amyloid (Aβ) region of the β-amyloid precursor protein gene causes an autosomal dominant disease with clinical picture of typical Alzheimer's disease. Here we report the special character of Arctic AD neuropathology in four deceased patients. RESULTS: Aβ deposition in the brains was wide-spread (Thal phase 5) and profuse. Virtually all parenchymal deposits were composed of non-fibrillar, Congo red negative Aβ aggregates. Congo red only stained angiopathic vessels. Mass spectrometric analyses showed that Aβ deposits contained variably truncated and modified wild type and mutated Aβ species. In three of four Arctic AD brains, most cerebral cortical plaques appeared targetoid with centres containing C-terminally (beyond aa 40) and variably N-terminally truncated Aβ surrounded by coronas immunopositive for Aβx-42. In the fourth patient plaque centres contained almost no Aβ making the plaques ring-shaped. The architectural pattern of plaques also varied between different anatomic regions. Tau pathology corresponded to Braak stage VI, and appeared mainly as delicate neuropil threads (NT) enriched within Aβ plaques. Dystrophic neurites were scarce, while neurofibrillary tangles were relatively common. Neuronal perikarya within the Aβ plaques appeared relatively intact. CONCLUSIONS: In Arctic AD brain differentially truncated abundant Aβ is deposited in plaques of variable numbers and shapes in different regions of the brain (including exceptional targetoid plaques in neocortex). The extracellular non-fibrillar Aβ does not seem to cause overt damage to adjacent neurons or to induce formation of neurofibrillary tangles, supporting the view that intracellular Aβ oligomers are more neurotoxic than extracellular Aβ deposits. However, the enrichment of NTs within plaques suggests some degree of intra-plaque axonal damage including accumulation of hp-tau, which may impair axoplasmic transport, and thereby contribute to synaptic loss. Finally, similarly as the cotton wool plaques in AD resulting from exon 9 deletion in the presenilin-1 gene, the Arctic plaques induced only modest glial and inflammatory tissue reaction."],["dc.identifier.doi","10.1186/2051-5960-1-60"],["dc.identifier.fs","599195"],["dc.identifier.pmid","24252272"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58642"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2051-5960"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The Arctic AβPP mutation leads to Alzheimer's disease pathology with highly variable topographic deposition of differentially truncated Aβ."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8144"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","21"],["dc.contributor.affiliation","Wirths, Oliver; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D-37075 Göttingen, Germany, oliver.wirths@medizin.uni-goettingen.de"],["dc.contributor.affiliation","Zampar, Silvia; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D-37075 Göttingen, Germany, silvia.zampar@med.uni-goettingen.de"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Zampar, Silvia"],["dc.date.accessioned","2021-04-14T08:31:06Z"],["dc.date.available","2021-04-14T08:31:06Z"],["dc.date.issued","2020"],["dc.date.updated","2022-09-06T08:29:14Z"],["dc.identifier.doi","10.3390/ijms21218144"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17647"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83486"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","1422-0067"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Neuron Loss in Alzheimer’s Disease: Translation in Transgenic Mouse Models"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","24"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Acta Neuropathologica Communications"],["dc.bibliographiccitation.lastpage","12"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Reinert, Jochim"],["dc.contributor.author","Richard, Bernhard C."],["dc.contributor.author","Klafki, Hans W."],["dc.contributor.author","Friedrich, Beate"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Kovacs, Gabor G."],["dc.contributor.author","Ingelsson, Martin"],["dc.contributor.author","Lannfelt, Lars"],["dc.contributor.author","Paetau, Anders"],["dc.contributor.author","Bergquist, Jonas"],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2017-09-07T11:44:29Z"],["dc.date.available","2017-09-07T11:44:29Z"],["dc.date.issued","2016"],["dc.description.abstract","In Alzheimer’s disease (AD) a variety of amyloid β-peptides (Aβ) are deposited in the form of extracellular diffuse and neuritic plaques (NP), as well as within the vasculature. The generation of Aβ from its precursor, the amyloid precursor protein (APP), is a highly complex procedure that involves subsequent proteolysis of APP by β- and γ-secretases. Brain accumulation of Aβ due to impaired Aβ degradation and/or altered ratios between the different Aβ species produced is believed to play a pivotal role in AD pathogenesis. While the presence of Aβ40 and Aβ42 in vascular and parenchymal amyloid have been subject of extensive studies, the deposition of carboxyterminal truncated Aβ peptides in AD has not received comparable attention. In the current study, we for the first time demonstrate the immunohistochemical localization of Aβ37 and Aβ39 in human sporadic AD (SAD). Our study further included the analysis of familial AD (FAD) cases carrying the APP mutations KM670/671NL, E693G and I716F, as well as a case of the PSEN1 ΔExon9 mutation. Aβ37 and Aβ39 were found to be widely distributed within the vasculature in the brains of the majority of studied SAD and FAD cases, the latter also presenting considerable amounts of Aβ37 containing NPs. In addition, both peptides were found to be present in extracellular plaques but only scarce within the vasculature in brains of a variety of transgenic AD mouse models. Taken together, our study indicates the importance of C-terminally truncated Aβ in sporadic and familial AD and raises questions about how these species are generated and regulated."],["dc.identifier.doi","10.1186/s40478-016-0294-7"],["dc.identifier.gro","3151681"],["dc.identifier.pmid","26955942"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12971"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8499"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","public"],["dc.notes.submitter","chake"],["dc.relation.issn","2051-5960"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Deposition of C-terminally truncated Aβ species Aβ37 and Aβ39 in Alzheimer’s disease and transgenic mouse models"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","913"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Neural Transmission"],["dc.bibliographiccitation.lastpage","920"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Marcello, Andrea"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Schneider-Axmann, Thomas"],["dc.contributor.author","Degerman-Gunnarsson, Malin"],["dc.contributor.author","Lannfelt, Lars"],["dc.contributor.author","Bayer, Thomas"],["dc.date.accessioned","2019-07-09T11:52:23Z"],["dc.date.available","2019-07-09T11:52:23Z"],["dc.date.issued","2009"],["dc.description.abstract","It has previously been shown that immune complexes (IC) of a given biomarker with class M immunoglobulins (IgM) provide better performances compared to the unbound biomarker in a number of cancer entities. In the present work, we investigated IC of IgM-Aβ as a potential biomarker for Alzheimer’s disease (AD). Aβ–IgM concentration has been measured in 75 plasma samples from patients with AD, individuals with mild cognitive impairment (MCI), and healthy age- and sex-matched controls (HC). To characterize the fractions associated with Aβ, pooled plasma samples were subjected to gel-filtration analysis. Size-separated fractions were analyzed for the presence of Aβ using a sandwich ELIp. assay. A strong reactivity was observed in the high molecular weight IgM (>500 kDa) and 150 kDa (IgG) fractions indicating that blood Aβ is strongly associated with antibodies. Using an ELISA assay detecting Aβ–IgM complexes, we observed that high levels of Aβ–IgMs were detectable in HC and MCI patients; however, there was no significant difference to the AD group."],["dc.identifier.doi","10.1007/s00702-009-0224-y"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3557"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60171"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Springer"],["dc.publisher.place","Vienna"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Circulating immune complexes of Aβ and IgM in plasma of patients with Alzheimer’s disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","175909142092535"],["dc.bibliographiccitation.journal","ASN Neuro"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Giesers, Naomi K."],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2021-04-14T08:26:32Z"],["dc.date.available","2021-04-14T08:26:32Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1177/1759091420925356"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17410"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81984"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","1759-0914"],["dc.relation.issn","1759-0914"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Loss of Hippocampal Calretinin and Parvalbumin Interneurons in the 5XFAD Mouse Model of Alzheimer’s Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7"],["dc.bibliographiccitation.journal","Open Longevity Science"],["dc.bibliographiccitation.lastpage","12"],["dc.bibliographiccitation.volume","2"],["dc.contributor.author","Wirths, O."],["dc.contributor.author","Bayer, T. A."],["dc.date.accessioned","2011-09-28T16:39:26Z"],["dc.date.accessioned","2021-10-27T13:11:11Z"],["dc.date.available","2011-09-28T16:39:26Z"],["dc.date.available","2021-10-27T13:11:11Z"],["dc.date.issued","2008"],["dc.description.abstract","Whereas a plethora of studies focusses on extracellular plaque deposition, only a very limited amount of reports deal with intraneuronal accumulation of A􀀂 peptides in human AD. However, over the past years, accumulating evidence points to a significant role of intraneuronal A􀀂 triggering the pathological cascade leading to neurodegeneration in Alzheimer’s disease (AD). Much of the data originate from studies on transgenic mouse models of AD, where initial intraneuronal A􀀂 accumulation which predes extracellular plaque deposition, has been repeatedly reported. The current review discusses the impact of this finding on the future development of novel mouse models for preclinical research as a basis for therapeutic intervention."],["dc.identifier.doi","10.2174/1876326X00802010007"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6974"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91567"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.orgunit","Fakultät für Biologie und Psychologie"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","570"],["dc.title","Early Intraneuronal Beta-Amyloid Pathology: Do Transgenic Mice Represent Valid Model Systems?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","723782"],["dc.bibliographiccitation.journal","International journal of Alzheimer's disease"],["dc.bibliographiccitation.volume","2010"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Bayer, Thomas A."],["dc.date.accessioned","2019-07-09T11:53:08Z"],["dc.date.available","2019-07-09T11:53:08Z"],["dc.date.issued","2010"],["dc.description.abstract","Since their initial generation in the mid 1990s, transgenic mouse models of Alzheimers's disease (AD) have been proven to be valuable model systems which are indispensable for modern AD research. Whereas most of these models are characterized by extensive amyloid plaque pathology, inflammatory changes and often behavioral deficits, modeling of neuron loss was much less successful. The present paper discusses the current achievements of modeling neuron loss in transgenic mouse models based on APP/Aβ and Tau overexpression and provides an overview of currently available AD mouse models showing these pathological alterations."],["dc.identifier.doi","10.4061/2010/723782"],["dc.identifier.fs","575497"],["dc.identifier.pmid","20871861"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6917"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60349"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2090-0252"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Neuron loss in transgenic mouse models of Alzheimer's disease."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]