Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases - Wikidata - awgldk - TriplyDB

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

http://www.wikidata.org/entity/Q24548362

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Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria p53-induced growth arrest is regulated by the mitochondrial SirT3 deacetylase Acetylation negatively regulates glycogen phosphorylase by recruiting protein phosphatase 1 Metabolism, cytoskeleton and cellular signalling in the grip of protein Nepsilon - and O-acetylation Acetylation of conserved lysines in the catalytic core of cyclin-dependent kinase 9 inhibits kinase activity and regulates transcription Crystal structures of human SIRT3 displaying substrate-induced conformational changes Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome Metabolic acetate therapy improves phenotype in the tremor rat model of Canavan disease SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival Gatekeepers of chromatin: Small metabolites elicit big changes in gene expression Metaboloepigenetics: interrelationships between energy metabolism and epigenetic control of gene expression SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1 Lysine acetylation: codified crosstalk with other posttranslational modifications SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70 Calorie restriction and the exercise of chromatin Catalysis and substrate selection by histone/protein lysine acetyltransferases SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation Post-Translational Modifications of Cardiac Mitochondrial Proteins in Cardiovascular Disease: Not Lost in Translation Potential Modulation of Sirtuins by Oxidative Stress Sirt1 and the Mitochondria Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration Protective effects and mechanisms of sirtuins in the nervous system Sirtuin 1 and sirtuin 3: physiological modulators of metabolism Targeting sirtuin 1 to improve metabolism: all you need is NAD(+)?Metabolism, longevity and epigenetics Structure and mechanism of non-histone protein acetyltransferase enzymes The potential of ¹¹C-acetate PET for monitoring the Fatty acid synthesis pathway in Tumors Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases Sirtuins in epigenetic regulation Protein lysine acylation and cysteine succination by intermediates of energy metabolism Flavonoid derivative 7,8-DHF attenuates TBI pathology via TrkB activation.Biochemical and Crystallographic Analysis of Substrate Binding and Conformational Changes in Acetyl-CoA Synthetase † , ‡Mitochondrial protein acetylation as a cell-intrinsic, evolutionary driver of fat storage: chemical and metabolic logic of acetyl-lysine modifications Hydrolase regulates NAD+ metabolites and modulates cellular redox.Acetyl-coenzyme A synthetase 2 is a nuclear protein required for replicative longevity in Saccharomyces cerevisiae Function of the SIRT3 mitochondrial deacetylase in cellular physiology, cancer, and neurodegenerative disease SIRT3 in Cardiac Physiology and Disease

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P2860

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

http://www.wikidata.org/entity/Q24548362

description

2006 nî lūn-bûn

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2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2006 թվականի հուլիսին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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prefLabel

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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PNAS.0604392103

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

@en

P2093

John M Denu

http://www.w3.org/2001/XMLSchema#string

Susan Lee

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William C Hallows

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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

Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins

Negative control of p53 by Sir2alpha promotes cell survival under stress

hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase

Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase.

The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase

Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.

Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity

Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle

Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

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10.1073/PNAS.0604392103

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27

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103

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2006-07-05T00:00:00Z

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6992993

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16790548

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Acyl-CoA synthetase short-chain family member 1

Acyl-CoA synthetase short-chain family member 2

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1480596

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