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","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.firstpage","23"],["dc.bibliographiccitation.lastpage","49"],["dc.contributor.author","Zampar, Silvia"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.editor","Huang, Xudong"],["dc.date.accessioned","2021-06-02T10:44:27Z"],["dc.date.available","2021-06-02T10:44:27Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.36255/exonpublications.alzheimersdisease.2020.ch2"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17719"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87044"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Exon Publications"],["dc.relation.doi","10.36255/exonpublications.alzheimersdisease.2020"],["dc.relation.isbn","9780645001709"],["dc.relation.ispartof","Alzheimer’s Disease: Drug Discovery"],["dc.rights","CC BY-NC-SD 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc-nd/4.0/"],["dc.subject.ddc","610"],["dc.title","Immunotherapy Targeting Amyloid-β Peptides in Alzheimer’s Disease"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5191"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["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.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.author","Zampar, Silvia"],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2021-07-05T15:00:45Z"],["dc.date.available","2021-07-05T15:00:45Z"],["dc.date.issued","2021"],["dc.date.updated","2022-09-05T10:37:20Z"],["dc.description.abstract","The relationship between the two most prominent neuropathological hallmarks of Alzheimer’s Disease (AD), extracellular amyloid-β (Aβ) deposits and intracellular accumulation of hyperphosphorylated tau in neurofibrillary tangles (NFT), remains at present not fully understood. A large body of evidence places Aβ upstream in the cascade of pathological events, triggering NFTs formation and the subsequent neuron loss. Extracellular Aβ deposits were indeed causative of an increased tau phosphorylation and accumulation in several transgenic models but the contribution of soluble Aβ peptides is still controversial. Among the different Aβ variants, the N-terminally truncated peptide Aβ4–42 is among the most abundant. To understand whether soluble Aβ4–42 peptides impact the onset or extent of tau pathology, we have crossed the homozygous Tg4–42 mouse model of AD, exclusively expressing Aβ4–42 peptides, with the PS19 (P301S) tau transgenic model. Behavioral assessment showed that the resulting double-transgenic line presented a partial worsening of motor performance and spatial memory deficits in the aged group. While an increased loss of distal CA1 pyramidal neurons was detected in young mice, no significant alterations in hippocampal tau phosphorylation were observed in immunohistochemical analyses."],["dc.description.abstract","The relationship between the two most prominent neuropathological hallmarks of Alzheimer’s Disease (AD), extracellular amyloid-β (Aβ) deposits and intracellular accumulation of hyperphosphorylated tau in neurofibrillary tangles (NFT), remains at present not fully understood. A large body of evidence places Aβ upstream in the cascade of pathological events, triggering NFTs formation and the subsequent neuron loss. Extracellular Aβ deposits were indeed causative of an increased tau phosphorylation and accumulation in several transgenic models but the contribution of soluble Aβ peptides is still controversial. Among the different Aβ variants, the N-terminally truncated peptide Aβ4–42 is among the most abundant. To understand whether soluble Aβ4–42 peptides impact the onset or extent of tau pathology, we have crossed the homozygous Tg4–42 mouse model of AD, exclusively expressing Aβ4–42 peptides, with the PS19 (P301S) tau transgenic model. Behavioral assessment showed that the resulting double-transgenic line presented a partial worsening of motor performance and spatial memory deficits in the aged group. While an increased loss of distal CA1 pyramidal neurons was detected in young mice, no significant alterations in hippocampal tau phosphorylation were observed in immunohistochemical analyses."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3390/ijms22105191"],["dc.identifier.pii","ijms22105191"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87896"],["dc.language.iso","en"],["dc.notes.intern","DOI Import DOI-Import GROB-441"],["dc.relation.eissn","1422-0067"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Characterization of a Mouse Model of Alzheimer’s Disease Expressing Aβ4-42 and Human Mutant Tau"],["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","107"],["dc.bibliographiccitation.lastpage","122"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Zampar, Silvia"],["dc.contributor.author","Weggen, Sascha"],["dc.date.accessioned","2019-12-11T10:39:58Z"],["dc.date.accessioned","2021-10-27T13:21:51Z"],["dc.date.available","2019-12-11T10:39:58Z"],["dc.date.available","2021-10-27T13:21:51Z"],["dc.date.issued","2019"],["dc.description.abstract","The accumulation and aggregation of amyloid-β (Aβ) peptides in the brain is believed to be the initial trigger in the molecular pathology of Alzheimer’s disease (AD). In addition to the widely studied full-length Aβ peptides (mainly Aβ1–40 and Aβ1–42), a variety of amino-terminally truncated (N-truncated) peptides, such as AβpE3-x and Aβ4-x, have been detected in high abundance in autopsy samples from sporadic and familial AD patients. N-truncated Aβ species adopt specific physicochemical properties resulting in a higher aggregation propensity and increased peptide stability, which likely account for their neurotoxic potential. The presence of N-truncated Aβ peptides in transgenic mouse models of AD and the selective overexpression of specific N-truncated variants in the murine brain have facilitated their investigation in relevant in vivo settings. In this chapter, we address the pathological relevance of N-truncated Aβ peptide species and summarize the current knowledge about the enzymatic activities that might be involved in their generation."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2019"],["dc.identifier.doi","10.15586/alzheimersdisease.2019.ch7"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16904"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92049"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.doi","10.15586/alzheimersdisease.2019"],["dc.relation.doi","10.15586/alzheimersdisease.2019"],["dc.relation.isbn","978-0-646-80968-7"],["dc.relation.ispartof","Alzheimer’s Disease"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.subject.ddc","610"],["dc.title","N-Terminally Truncated Aβ Peptide Variants in Alzheimer’s Disease"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]