<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ercan-Herbst E</submitter><funding>AbbVie Deutschland</funding><pagination>192</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6892178</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>7(1)</volume><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</pubmed_abstract><journal>Acta neuropathologica communications</journal><pubmed_title>A post-translational modification signature defines changes in soluble tau correlating with oligomerization in early stage Alzheimer's disease brain.</pubmed_title><pmcid>PMC6892178</pmcid><funding_grant_id>n.a.</funding_grant_id><pubmed_authors>Behrendt A</pubmed_authors><pubmed_authors>Prat Oriol N</pubmed_authors><pubmed_authors>Schondorf DC</pubmed_authors><pubmed_authors>Ercan-Herbst E</pubmed_authors><pubmed_authors>Ehrnhoefer DE</pubmed_authors><pubmed_authors>Weber C</pubmed_authors><pubmed_authors>Ehrig J</pubmed_authors><pubmed_authors>Klaus B</pubmed_authors><pubmed_authors>Gomez Ramos B</pubmed_authors></additional><is_claimable>false</is_claimable><name>A post-translational modification signature defines changes in soluble tau correlating with oligomerization in early stage Alzheimer's disease brain.</name><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</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Dec</publication><modification>2025-04-04T07:13:57.022Z</modification><creation>2020-05-21T21:44:19Z</creation></dates><accession>S-EPMC6892178</accession><cross_references><pubmed>31796124</pubmed><doi>10.1186/s40478-019-0823-2</doi></cross_references></HashMap>