<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Isei MO</submitter><funding>NIA NIH HHS</funding><pubmed_abstract>Phosphorylation of tau at sites associated with Alzheimer's disease (AD) likely plays a role in the disease progression. Mitochondrial impairment, correlating with increased presence of phosphorylated tau, has been identified as a contributing factor to neurodegenerative processes in AD. However, how tau phosphorylated at specific sites impacts mitochondrial function has not been fully defined. We examined how AD-relevant phosphomimetics of tau impact selected aspects of mitochondrial biology. To mimic phosphorylation at AD-associated sites, the Ser/Thr sites in wild-type GFP tagged-tau (T4) were converted to glutamic acid (E) to make pseudophosphorylated GFP tagged-Ser-396/404 (2EC) and GFP tagged-Thr-231/Ser-235 (2EM) constructs. These constructs were expressed in neuronal HT22 cells and</pubmed_abstract><journal>bioRxiv : the preprint server for biology</journal><pagination>2023.02.19.529131</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9949115</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Site-specific phosphorylation of tau impacts mitochondrial biology and response to stressors.</pubmed_title><pmcid>PMC9949115</pmcid><funding_grant_id>R01 AG067617</funding_grant_id><pubmed_authors>Johnson GV</pubmed_authors><pubmed_authors>Rodwell-Bullock J</pubmed_authors><pubmed_authors>Isei MO</pubmed_authors><pubmed_authors>Girardi PA</pubmed_authors><pubmed_authors>Nehrke K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Site-specific phosphorylation of tau impacts mitochondrial biology and response to stressors.</name><description>Phosphorylation of tau at sites associated with Alzheimer's disease (AD) likely plays a role in the disease progression. Mitochondrial impairment, correlating with increased presence of phosphorylated tau, has been identified as a contributing factor to neurodegenerative processes in AD. However, how tau phosphorylated at specific sites impacts mitochondrial function has not been fully defined. We examined how AD-relevant phosphomimetics of tau impact selected aspects of mitochondrial biology. To mimic phosphorylation at AD-associated sites, the Ser/Thr sites in wild-type GFP tagged-tau (T4) were converted to glutamic acid (E) to make pseudophosphorylated GFP tagged-Ser-396/404 (2EC) and GFP tagged-Thr-231/Ser-235 (2EM) constructs. These constructs were expressed in neuronal HT22 cells and</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Feb</publication><modification>2025-04-18T12:50:11.094Z</modification><creation>2025-02-19T04:54:55.188Z</creation></dates><accession>S-EPMC9949115</accession><cross_references><pubmed>36824940</pubmed><doi>10.1101/2023.02.19.529131</doi></cross_references></HashMap>