Sirtuin 3 (SIRT3) protein regulates long-chain acyl-CoA dehydrogenase by deacetylating conserved lysines near the active site.
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Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondriaSIRT3 regulates progression and development of diseases of aging.Sirtuins, metabolism, and DNA repairNonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylasesCell Death and Heart Failure in Obesity: Role of Uncoupling ProteinsSIRT3 in Cardiac Physiology and DiseaseLong-chain acyl-CoA dehydrogenase deficiency as a cause of pulmonary surfactant dysfunctionGlobal analysis of lysine acetylation in strawberry leaves.High Sensitivity of SIRT3 Deficient Hearts to Ischemia-Reperfusion Is Associated with Mitochondrial Abnormalities.Prolonged fasting identifies heat shock protein 10 as a Sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function.SIRT3 and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase.Lysine Acetylation Activates Mitochondrial Aconitase in the HeartSIRT5 Regulates both Cytosolic and Mitochondrial Protein Malonylation with Glycolysis as a Major Target.Sirtuin regulation in aging and injuryProgressive mitochondrial protein lysine acetylation and heart failure in a model of Friedreich's ataxia cardiomyopathy.Acetyl-L-carnitine increases mitochondrial protein acetylation in the aged rat heart.The Acetyl Group Buffering Action of Carnitine Acetyltransferase Offsets Macronutrient-Induced Lysine Acetylation of Mitochondrial ProteinsMechanisms and Dynamics of Protein Acetylation in Mitochondria.New assays and approaches for discovery and design of Sirtuin modulators.An integrated perspective and functional impact of the mitochondrial acetylome.Roles of sirtuins in the regulation of antioxidant defense and bioenergetic function of mitochondria under oxidative stress.Role of CoA and acetyl-CoA in regulating cardiac fatty acid and glucose oxidation.Metabolic Catastrophe in Mice Lacking Transferrin Receptor in MuscleIntersections between mitochondrial sirtuin signaling and tumor cell metabolism.Acetylation of mitochondrial proteins by GCN5L1 promotes enhanced fatty acid oxidation in the heart.Acetylation and succinylation contribute to maturational alterations in energy metabolism in the newborn heart.Post-translational modifications in mitochondria: protein signaling in the powerhouse.Metabolic control of epigenetics in cancer.Aspirin increases mitochondrial fatty acid oxidation.Methylene blue decreases mitochondrial lysine acetylation in the diabetic heartSIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.Obesity-induced lysine acetylation increases cardiac fatty acid oxidation and impairs insulin signalling.Lysine desuccinylase SIRT5 binds to cardiolipin and regulates the electron transport chain.Advances in the Understanding and Treatment of Mitochondrial Fatty Acid Oxidation Disorders.Obesity and aging diminish sirtuin 1 (SIRT1)-mediated deacetylation of SIRT3, leading to hyperacetylation and decreased activity and stability of SIRT3.Characterizing Sirtuin 3 Deacetylase Affinity for Aldehyde Dehydrogenase 2.SIRT3 gene expression but not SIRT3 subcellular localization is altered in response to fasting and exercise in human skeletal muscle.Mitochondrial Sirtuin 4 Resolves Immune Tolerance in Monocytes by Rebalancing Glycolysis and Glucose Oxidation Homeostasis.Nutritional Ketosis and Mitohormesis: Potential Implications for Mitochondrial Function and Human Health.First comprehensive analysis of lysine acetylation in Alvinocaris longirostris from the deep-sea hydrothermal vents.
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Sirtuin 3 (SIRT3) protein regulates long-chain acyl-CoA dehydrogenase by deacetylating conserved lysines near the active site.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 11 October 2013
@en
vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Sirtuin 3 (SIRT3) protein regu ...... lysines near the active site.
@en
Sirtuin 3
@nl
type
label
Sirtuin 3 (SIRT3) protein regu ...... lysines near the active site.
@en
Sirtuin 3
@nl
prefLabel
Sirtuin 3 (SIRT3) protein regu ...... lysines near the active site.
@en
Sirtuin 3
@nl
P2093
P2860
P50
P356
P1476
Sirtuin 3 (SIRT3) protein regu ...... lysines near the active site.
@en
P2093
Bradford W Gibson
Emanuel Schreiber
Eric S Goetzman
Manimalha Balasubramani
Matthew J Rardin
Megan E Beck
Radha Uppala
Sivakama S Bharathi
Yuxun Zhang
P2860
P304
33837-33847
P356
10.1074/JBC.M113.510354
P407
P577
2013-10-11T00:00:00Z