{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Hu Z"],"funding":["American Cancer Society","National Cancer Institute","NCI NIH HHS"],"pubmed_abstract":["Microtubule-associated protein tau is essential for microtubule assembly and stabilization. Hyperphosphorylation of the microtubule-associated protein tau plays an important pathological role in the development of Alzheimer's disease and other tauopathies. <i>In vivo</i> studies using kinase inhibitors suggest that reducing tau phosphorylation levels has therapeutic potential; however, such approaches showed limited benefits. We sought to further develop our phosphorylation targeting chimera (PhosTAC) technology to specifically induce tau dephosphorylation. Herein, we use small molecule-based PhosTACs to recruit tau to PP2A, a native tau phosphatase. PhosTACs induced the formation of a stable ternary complex, leading to rapid, efficient, and sustained tau dephosphorylation, which also corr"],"journal":["Journal of the American Chemical Society"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11670127"],"repository":["biostudies-literature"],"pubmed_title":["Targeted Dephosphorylation of Tau by Phosphorylation Targeting Chimeras (PhosTACs) as a Therapeutic Modality."],"pmcid":["PMC11670127"],"funding_grant_id":["R35 CA197589"],"pubmed_authors":["Li W","Chen PH","Liu Y","Hu Z","Crews CM","Douglas T","Hines J"],"additional_accession":[]},"is_claimable":false,"name":"Targeted Dephosphorylation of Tau by Phosphorylation Targeting Chimeras (PhosTACs) as a Therapeutic Modality.","description":"Microtubule-associated protein tau is essential for microtubule assembly and stabilization. Hyperphosphorylation of the microtubule-associated protein tau plays an important pathological role in the development of Alzheimer's disease and other tauopathies. <i>In vivo</i> studies using kinase inhibitors suggest that reducing tau phosphorylation levels has therapeutic potential; however, such approaches showed limited benefits. We sought to further develop our phosphorylation targeting chimera (PhosTAC) technology to specifically induce tau dephosphorylation. Herein, we use small molecule-based PhosTACs to recruit tau to PP2A, a native tau phosphatase. PhosTACs induced the formation of a stable ternary complex, leading to rapid, efficient, and sustained tau dephosphorylation, which also corr","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2025-04-18T22:01:33.474Z","creation":"2025-04-07T09:57:25.172Z"},"accession":"S-EPMC11670127","cross_references":{"pubmed":["36753634"],"doi":["10.1021/jacs.2c11706"]}}