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Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease.

Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease.

http://www.wikidata.org/entity/Q36466568

about

Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity Sirtuins Link Inflammation and Metabolism Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases Succinylome analysis reveals the involvement of lysine succinylation in metabolism in pathogenic Mycobacterium tuberculosis Mitochondrial protein acetylation as a cell-intrinsic, evolutionary driver of fat storage: chemical and metabolic logic of acetyl-lysine modifications Myocardial energetics and the role of micronutrients in heart failure: a critical review Interplay between oxidant species and energy metabolism Computational studies on sirtuins from Trypanosoma cruzi: structures, conformations and interactions with phytochemicals Differential effects of binge methamphetamine injections on the mRNA expression of histone deacetylases (HDACs) in the rat striatum SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks Functional decorations: post-translational modifications and heart disease delineated by targeted proteomics.Small-molecule allosteric activators of sirtuins.Quantitative Succinyl-Proteome Profiling of Camellia sinensis cv. 'Anji Baicha' During Periodic Albinism.Metabolic changes associated with the long winter fast dominate the liver proteome in 13-lined ground squirrels Differential expression and role of hyperglycemia induced oxidative stress in epigenetic regulation of β1, β2 and β3-adrenergic receptors in retinal endothelial cells Drosophila Sirt2/mammalian SIRT3 deacetylates ATP synthase β and regulates complex V activity.A method to determine lysine acetylation stoichiometries.Overexpression of mitochondrial sirtuins alters glycolysis and mitochondrial function in HEK293 cells.Inhibition of neuronal cell mitochondrial complex I with rotenone increases lipid β-oxidation, supporting acetyl-coenzyme A levels.Cyclophilin D modulates mitochondrial acetylome The nexus of chromatin regulation and intermediary metabolism.Targeted, LCMS-based Metabolomics for Quantitative Measurement of NAD(+) Metabolites.Energy metabolic reprogramming in the hypertrophied and early stage failing heart: a multisystems approach.Protein acetylation and acetyl coenzyme a metabolism in budding yeast Sorting out functions of sirtuins in cancer Fatty acids from membrane lipids become incorporated into lipid bodies during Myxococcus xanthus differentiation.SIRT3 mediates multi-tissue coupling for metabolic fuel switching Practicality of intermittent fasting in humans and its effect on oxidative stress and genes related to aging and metabolism Acetate supplementation as a means of inducing glioblastoma stem-like cell growth arrest Honokiol blocks and reverses cardiac hypertrophy in mice by activating mitochondrial Sirt3 The ɛ-Amino Group of Protein Lysine Residues Is Highly Susceptible to Nonenzymatic Acylation by Several Physiological Acyl-CoA Thioesters.Targeting Histone Deacetylases in Diseases: Where Are We?Characterization of Trypanosoma cruzi Sirtuins as Possible Drug Targets for Chagas Disease.Lysine Acetylation Activates Mitochondrial Aconitase in the Heart Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions.The Combination of Resveratrol and Quercetin Attenuates Metabolic Syndrome in Rats by Modifying the Serum Fatty Acid Composition and by Upregulating SIRT 1 and SIRT 2 Expression in White Adipose Tissue.Oroxylin A inhibits glycolysis-dependent proliferation of human breast cancer via promoting SIRT3-mediated SOD2 transcription and HIF1α destabilization The Acetyl Group Buffering Action of Carnitine Acetyltransferase Offsets Macronutrient-Induced Lysine Acetylation of Mitochondrial Proteins Metabolic inflexibility: when mitochondrial indecision leads to metabolic gridlock.

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Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease.

http://www.wikidata.org/entity/Q36466568

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2012 nî lūn-bûn

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Journal of Biological Chemistry

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Eric Verdin

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John C Newman

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Wenjuan He

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P2860

Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity

Positional cloning of the mouse obese gene and its human homologue

Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase

SIRT1 deacetylates and positively regulates the nuclear receptor LXR

Regulation of cellular metabolism by protein lysine acetylation

SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells

Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5

The first identification of lysine malonylation substrates and its regulatory enzyme

Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase

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42436-42443

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