{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9"],"submitter":["Faris S"],"pubmed_abstract":["Tauopathies are neurodegenerative diseases characterized by intracellular abnormal tau deposits in the brain. Tau aggregates can propagate from one neuron to another in a prion-like manner, mediated by the interaction between tau and cell surface heparan sulfate proteoglycans. We developed an AlphaScreen assay, with His-tagged tau and biotinylated heparin, to represent the tau-HS interface to target the tau-glycan interface. Using our AlphaScreen assay, with a Z-factor of 0.65, we screened ∼300 compounds and discovered a small-molecule compound (herein referred to as A9), which can disrupt the tau-heparin interaction with micromolar efficacy. A9 also effectively inhibited heparin-induced tau aggregation in Thioflavin T fluorescence assays and attenuated tau internalization by H4 neurogliom"],"journal":["Frontiers in molecular biosciences"],"pagination":["1083225"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9798536"],"repository":["biostudies-literature"],"pubmed_title":["Small-molecule compound from AlphaScreen disrupts tau-glycan interface."],"pmcid":["PMC9798536"],"pubmed_authors":["Murray A","Zhang F","Jin W","Smith N","Faris S","Wang C","Gibson J","Linhardt R","He P"],"additional_accession":[]},"is_claimable":false,"name":"Small-molecule compound from AlphaScreen disrupts tau-glycan interface.","description":"Tauopathies are neurodegenerative diseases characterized by intracellular abnormal tau deposits in the brain. Tau aggregates can propagate from one neuron to another in a prion-like manner, mediated by the interaction between tau and cell surface heparan sulfate proteoglycans. We developed an AlphaScreen assay, with His-tagged tau and biotinylated heparin, to represent the tau-HS interface to target the tau-glycan interface. Using our AlphaScreen assay, with a Z-factor of 0.65, we screened ∼300 compounds and discovered a small-molecule compound (herein referred to as A9), which can disrupt the tau-heparin interaction with micromolar efficacy. A9 also effectively inhibited heparin-induced tau aggregation in Thioflavin T fluorescence assays and attenuated tau internalization by H4 neurogliom","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-18T22:24:09.297Z","creation":"2025-04-07T10:07:37.945Z"},"accession":"S-EPMC9798536","cross_references":{"pubmed":["36589242"],"doi":["10.3389/fmolb.2022.1083225"]}}