{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ercan-Herbst E"],"funding":["AbbVie Deutschland"],"pagination":["192"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6892178"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(1)"],"pubmed_abstract":["Tau is a microtubule-binding protein that can receive various post-translational modifications (PTMs) including phosphorylation, methylation, acetylation, glycosylation, nitration, sumoylation and truncation. Hyperphosphorylation of tau is linked to its aggregation and the formation of neurofibrillary tangles (NFTs), which are a hallmark of Alzheimer's disease (AD). While more than 70 phosphorylation sites have been detected previously on NFT tau, studies of oligomeric and detergent-soluble tau in human brains during the early stages of AD are lacking. Here we apply a comprehensive electrochemiluminescence ELISA assay to analyze twenty-five different PTM sites as well as tau oligomerization in control and sporadic AD brain. The samples were classified as Braak stages 0-I, II or III-IV, cor"],"journal":["Acta neuropathologica communications"],"pubmed_title":["A post-translational modification signature defines changes in soluble tau correlating with oligomerization in early stage Alzheimer's disease brain."],"pmcid":["PMC6892178"],"funding_grant_id":["n.a."],"pubmed_authors":["Behrendt A","Prat Oriol N","Schondorf DC","Ercan-Herbst E","Ehrnhoefer DE","Weber C","Ehrig J","Klaus B","Gomez Ramos B"],"additional_accession":[]},"is_claimable":false,"name":"A post-translational modification signature defines changes in soluble tau correlating with oligomerization in early stage Alzheimer's disease brain.","description":"Tau is a microtubule-binding protein that can receive various post-translational modifications (PTMs) including phosphorylation, methylation, acetylation, glycosylation, nitration, sumoylation and truncation. Hyperphosphorylation of tau is linked to its aggregation and the formation of neurofibrillary tangles (NFTs), which are a hallmark of Alzheimer's disease (AD). While more than 70 phosphorylation sites have been detected previously on NFT tau, studies of oligomeric and detergent-soluble tau in human brains during the early stages of AD are lacking. Here we apply a comprehensive electrochemiluminescence ELISA assay to analyze twenty-five different PTM sites as well as tau oligomerization in control and sporadic AD brain. The samples were classified as Braak stages 0-I, II or III-IV, cor","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Dec","modification":"2025-04-04T07:13:57.022Z","creation":"2020-05-21T21:44:19Z"},"accession":"S-EPMC6892178","cross_references":{"pubmed":["31796124"],"doi":["10.1186/s40478-019-0823-2"]}}