Sirtuins

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  Subject Areas on Research

  • Ablation of Sirtuin5 in the postnatal mouse heart results in protein succinylation and normal survival in response to chronic pressure overload. 
  • Acetate metabolism and aging: An emerging connection. 
  • Acetylation of mitochondrial proteins. 
  • Coming of age: molecular drivers of aging and therapeutic opportunities. 
  • Deglutarylation of glutaryl-CoA dehydrogenase by deacylating enzyme SIRT5 promotes lysine oxidation in mice. 
  • Disruption of the Ang II type 1 receptor promotes longevity in mice. 
  • Epidermal growth factor receptor mediated proliferation depends on increased lipid droplet density regulated via a negative regulatory loop with FOXO3/Sirtuin6. 
  • FOXO3 growth inhibition of colonic cells is dependent on intraepithelial lipid droplet density. 
  • Generating mammalian sirtuin tools for protein-interaction analysis. 
  • Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH. 
  • Loss of sirtuin 4 leads to elevated glucose- and leucine-stimulated insulin levels and accelerated age-induced insulin resistance in multiple murine genetic backgrounds. 
  • Low levels of DNA polymerase alpha induce mitotic and meiotic instability in the ribosomal DNA gene cluster of Saccharomyces cerevisiae. 
  • Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. 
  • Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. 
  • Mechanism-Based Inhibitors of the Human Sirtuin 5 Deacylase: Structure-Activity Relationship, Biostructural, and Kinetic Insight. 
  • Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation. 
  • Metabolic control by sirtuins and other enzymes that sense NAD+, NADH, or their ratio. 
  • Metabolomics-assisted proteomics identifies succinylation and SIRT5 as important regulators of cardiac function. 
  • Mitochondrial sirtuins. 
  • Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases. 
  • Oxygen flux analysis to understand the biological function of sirtuins. 
  • Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. 
  • Quantifying Competition among Mitochondrial Protein Acylation Events Induced by Ethanol Metabolism. 
  • Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications. 
  • Regulation of UCP1 and Mitochondrial Metabolism in Brown Adipose Tissue by Reversible Succinylation. 
  • Respiratory Phenomics across Multiple Models of Protein Hyperacylation in Cardiac Mitochondria Reveals a Marginal Impact on Bioenergetics. 
  • Role of NAD+ and mitochondrial sirtuins in cardiac and renal diseases. 
  • SIRT4 Is a Lysine Deacylase that Controls Leucine Metabolism and Insulin Secretion. 
  • SIRT4 coordinates the balance between lipid synthesis and catabolism by repressing malonyl CoA decarboxylase. 
  • SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks. 
  • SIRT6 Promotes Hepatic Beta-Oxidation via Activation of PPARα. 
  • SUCLA2 mutations cause global protein succinylation contributing to the pathomechanism of a hereditary mitochondrial disease. 
  • Sirtuin 5 Is Regulated by the SCFCyclin F Ubiquitin Ligase and Is Involved in Cell Cycle Control. 
  • Sirtuin 5 is required for mouse survival in response to cardiac pressure overload. 
  • Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling. 
  • SnapShot: Mammalian Sirtuins. 
  • The sirtuins, oxidative stress and aging: an emerging link. 
  • Upregulation of VEGF-C by androgen depletion: the involvement of IGF-IR-FOXO pathway. 
  • Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly. 
  • β-Cell-specific ablation of sirtuin 4 does not affect nutrient-stimulated insulin secretion in mice. 
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  Keywords of People

  • Hirschey, Matthew, Associate Professor of Medicine, Cell Biology