<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Sreedevi K</submitter><funding>NHLBI NIH HHS</funding><pagination>1-12</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12646366</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>198</volume><pubmed_abstract>PERM1 was initially identified as a new downstream target of PGC-1α and ERRs that regulates mitochondrial bioenergetics in skeletal muscle. Subsequently, we and other groups demonstrated that PERM1 is also a positive regulator of mitochondrial bioenergetics in the heart. However, the exact mechanisms of regulatory functions of PERM1 remain poorly understood. O-GlcNAcylation is a post-translational modification of proteins that are regulated by two enzymes: O-GlcNAc transferase (OGT) that adds O-GlcNAc to proteins; O-GlcNAcase (OGA) that removes O-GlcNAc from proteins. O-GlcNAcylation is a powerful signaling mechanism mediating cellular responses to stressors and nutrient availability, which, among other targets, may influence cardiac metabolism. We hypothesized that PERM1 regulates mitocho</pubmed_abstract><journal>Journal of molecular and cellular cardiology</journal><pubmed_title>PERM1 regulates mitochondrial energetics through O-GlcNAcylation in the heart.</pubmed_title><pmcid>PMC12646366</pmcid><funding_grant_id>R01 HL156667</funding_grant_id><pubmed_authors>Wende AR</pubmed_authors><pubmed_authors>Warren JS</pubmed_authors><pubmed_authors>Zaitsev AV</pubmed_authors><pubmed_authors>James A</pubmed_authors><pubmed_authors>Yedla S</pubmed_authors><pubmed_authors>Arowa S</pubmed_authors><pubmed_authors>Sreedevi K</pubmed_authors><pubmed_authors>Do S</pubmed_authors><pubmed_authors>Oka SI</pubmed_authors></additional><is_claimable>false</is_claimable><name>PERM1 regulates mitochondrial energetics through O-GlcNAcylation in the heart.</name><description>PERM1 was initially identified as a new downstream target of PGC-1α and ERRs that regulates mitochondrial bioenergetics in skeletal muscle. Subsequently, we and other groups demonstrated that PERM1 is also a positive regulator of mitochondrial bioenergetics in the heart. However, the exact mechanisms of regulatory functions of PERM1 remain poorly understood. O-GlcNAcylation is a post-translational modification of proteins that are regulated by two enzymes: O-GlcNAc transferase (OGT) that adds O-GlcNAc to proteins; O-GlcNAcase (OGA) that removes O-GlcNAc from proteins. O-GlcNAcylation is a powerful signaling mechanism mediating cellular responses to stressors and nutrient availability, which, among other targets, may influence cardiac metabolism. We hypothesized that PERM1 regulates mitocho</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Jan</publication><modification>2026-06-06T08:57:12.519Z</modification><creation>2026-05-28T03:11:32.092Z</creation></dates><accession>S-EPMC12646366</accession><cross_references><pubmed>39581161</pubmed><doi>10.1016/j.yjmcc.2024.11.002</doi></cross_references></HashMap>