Sirtuin 3

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  Subject Areas on Research

  • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. 
  • Circadian clock NAD+ cycle drives mitochondrial oxidative metabolism in mice. 
  • Disruption of Acetyl-Lysine Turnover in Muscle Mitochondria Promotes Insulin Resistance and Redox Stress without Overt Respiratory Dysfunction. 
  • Disruption of the Ang II type 1 receptor promotes longevity in mice. 
  • Ethanol metabolism modifies hepatic protein acylation in mice. 
  • Extreme Acetylation of the Cardiac Mitochondrial Proteome Does Not Promote Heart Failure. 
  • Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. 
  • Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice. 
  • Mitochondrial protein acetylation regulates metabolism. 
  • Mitochondrial sirtuins. 
  • Progressive mitochondrial protein lysine acetylation and heart failure in a model of Friedreich's ataxia cardiomyopathy. 
  • Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation. 
  • Quantifying Competition among Mitochondrial Protein Acylation Events Induced by Ethanol Metabolism. 
  • Remodeling of the Acetylproteome by SIRT3 Manipulation Fails to Affect Insulin Secretion or β Cell Metabolism in the Absence of Overnutrition. 
  • Respiratory Phenomics across Multiple Models of Protein Hyperacylation in Cardiac Mitochondria Reveals a Marginal Impact on Bioenergetics. 
  • Roles of Progesterone Receptor Membrane Component 1 in Oxidative Stress-Induced Aging in Chorion Cells. 
  • SIRT1 and SIRT3 deacetylate homologous substrates: AceCS1,2 and HMGCS1,2. 
  • SIRT3 Directs Carbon Traffic in Muscle to Promote Glucose Control. 
  • SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production. 
  • SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome. 
  • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. 
  • SIRT3 regulates mitochondrial protein acetylation and intermediary metabolism. 
  • SIRT3 regulates progression and development of diseases of aging. 
  • SIRT3 weighs heavily in the metabolic balance: a new role for SIRT3 in metabolic syndrome. 
  • Sirt3 regulates metabolic flexibility of skeletal muscle through reversible enzymatic deacetylation. 
  • Sirtuin 3 (SIRT3) protein regulates long-chain acyl-CoA dehydrogenase by deacetylating conserved lysines near the active site. 
  • Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production. 
  • Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly. 
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  Keywords of People

  • Hirschey, Matthew, Associate Professor of Medicine, Pharmacology & Cancer Biology