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Briefly, samples were shortly separated in polyacrylamide-gels, reduced with dithiothreitol, alkylated with iodoacetamide and digested with trypsin overnight."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Database searches and quantification was carried out within MaxQuant 2.0.3.0 based on 55341 mus musculus sequences (UP000000589 from the UniProt KB downloaded on 18th January 2022) as well as well as eight AD related sequence variants. The “match between runs” feature as well as label-free quantification within the different analyzed fractions was enabled."],"omics_type":["Proteomics"],"labhead":["Gereon Poschmann"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Proteome research Molecular Medicine Heinrich-Heine-University Düsseldorf 40225 Düsseldorf Germany"],"species":["Mus Musculus (mouse)"],"publication":["41532798 Kass B, Poschmann G, Demir F, Huesgen P, Stühler K, Kutzsche J, Willbold D. The Proteome of Human Amyloid Beta Oligomers. Biochemistry. 2026 65(3):339-353 10.1021/acs.biochem.5c00597"],"submitter_mail":["gereon.poschmann@hhu.de"],"submitter_affiliation":["Molecular Proteomics Laboratory"],"submitter_country":["Germany"],"pubmed_abstract":["Amyloid beta (Aβ) oligomers are thought to play an important role during development and progression of Alzheimer's disease (AD). Previously, we determined the Aβ oligomer concentrations in various AD mouse models and in human brain tissues of former AD patients. Here, we investigate which proteins are part of these Aβ oligomers, apart from Aβ itself. Because several oligomer-associated proteins have been implicated in mechanisms leading to AD pathology, identification of the Aβ oligomer proteome may provide insights into the formation of Aβ oligomers <i>in vivo</i> and may reveal novel targets for disease-modifying therapeutic approaches. Here, we separated different native Aβ assemblies in brain homogenates of transgenic (tg) AD mice and human AD <i>post mortem</i> samples by density gradient centrifugation, then isolated Aβ-containing assemblies by co-immunoprecipitation. Mass spectrometry of immunoprecipitated proteins with label-free quantification (LFQ) showed significant changes between the proteomes of Aβ oligomers from tg AD mice and wildtype (wt) mice, confirming some proteins that have been expected to bind Aβ species, like ApoE and Clusterin, but also indicating novel, so far unknown, protein content of Aβ oligomers, such as the RabGAP Tbc1d10b. Some of the hereby identified proteins, like, for example, Clusterin, were also found to be enriched in Aβ oligomers from human AD brain tissue derived homogenates as compared to brain tissue from non-demented controls (NC). Others, such as Netrin-1, were specifically enriched in Aβ oligomers in AD compared to NC samples, but not in mouse samples."],"pubmed_title":["The Proteome of Human Amyloid Beta Oligomers."],"pubmed_authors":["Kass Bettina B, Poschmann Gereon G, Demir Fatih F, Huesgen Pitter P, Stühler Kai K, Kutzsche Janine J, Willbold Dieter D"],"additional_accession":[]},"is_claimable":false,"name":"The proteome of APP/PS1 mouse amyloid beta oligomers","description":"Amyloid β (Aβ) oligomers are thought to play an important role in the onset and progression of Alzheimer’s disease (AD). Several oligomer-binding proteins have been implicated in mechanisms leading to AD pathology. Such proteins could provide insights into the pathways involved in the disease process of AD and might reveal novel targets for disease-modifying therapy approaches. Here, we separated different native Aβ assemblies in brain homogenates of transgenic AD mice samples by density gradient centrifugation, then isolated Aβ-containing complexes by co-immunoprecipitation. Mass spectrometry of immunoprecipitated proteins with label-free quantification (LFQ) showed numerous significant changes between transgenic AD mice and wildtype mice, confirming familiar binding proteins and also indicating putative new 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