Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
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Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondriaSirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activitySirtuin functions and modulation: from chemistry to the clinicPotential Modulation of Sirtuins by Oxidative StressBiochemical Genetic Pathways that Modulate Aging in Multiple SpeciesInterplay between sirtuins, MYC and hypoxia-inducible factor in cancer-associated metabolic reprogrammingNonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylasesSirtuins in epigenetic regulationStructure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesisMultiple Forms of Glutamate Dehydrogenase in Animals: Structural Determinants and Physiological ImplicationsMetabolic reprogramming in macrophages and dendritic cells in innate immunityDefining the orphan functions of lysine acetyltransferasesA continuous sirtuin activity assay without any coupling to enzymatic or chemical reactions.Quantitative proteomic analysis of histone modificationsRole of the Substrate Specificity-Defining Residues of Human SIRT5 in Modulating the Structural Stability and Inhibitory Features of the Enzyme.Sirtuins: guardians of mammalian healthspan.Role of NAD+ and mitochondrial sirtuins in cardiac and renal diseasesOverexpression of mitochondrial sirtuins alters glycolysis and mitochondrial function in HEK293 cells.Epigenetic control of gene function in schistosomes: a source of therapeutic targets?Lysine malonylation is elevated in type 2 diabetic mouse models and enriched in metabolic associated proteins.Mitochondrial sirtuins and their relationships with metabolic disease and cancer.Histone Acylation beyond Acetylation: Terra Incognita in Chromatin Biology.Changes in the Acetylome and Succinylome of Bacillus subtilis in Response to Carbon Source.High-Resolution Metabolomics with Acyl-CoA Profiling Reveals Widespread Remodeling in Response to Diet.The ɛ-Amino Group of Protein Lysine Residues Is Highly Susceptible to Nonenzymatic Acylation by Several Physiological Acyl-CoA Thioesters.Novel sirtuin inhibitory warheads derived from the N(ε)-acetyl-lysine analog L-2-amino-7-carboxamidoheptanoic acid.NAD(+) Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the NucleusSIRT5 regulation of ammonia-induced autophagy and mitophagy.Characterization of Trypanosoma cruzi Sirtuins as Possible Drug Targets for Chagas Disease.Using mitochondrial sirtuins as drug targets: disease implications and available compounds.Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation.SIRT5 Regulates both Cytosolic and Mitochondrial Protein Malonylation with Glycolysis as a Major Target.Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation.Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions.Sirtuin regulation in aging and injuryIdentification of sirtuin 5 inhibitors by ultrafast microchip electrophoresis using nanoliter volume samplesDeposition of 5-Methylcytosine on Enhancer RNAs Enables the Coactivator Function of PGC-1α.Altered acetylation and succinylation profiles in Corynebacterium glutamicum in response to conditions inducing glutamate overproductionCharacterization of the cardiac succinylome and its role in ischemia-reperfusion injury.Autophagy in Ischemic Livers: A Critical Role of Sirtuin 1/Mitofusin 2 Axis in Autophagy Induction.
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P2860
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
description
2014 nî lūn-bûn
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2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2014 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
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name
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@ast
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@en
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@nl
type
label
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@ast
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@en
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@nl
prefLabel
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@ast
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@en
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@nl
P2093
P2860
P50
P921
P3181
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P1476
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
@en
P2093
Brett S Peterson
Gregory R Wagner
Guofeng Xu
Jeongsoon Park
Jessica Schmiesing
Kristin A Anderson
Michael J Muehlbauer
Michelle F Green
P2860
P304
P3181
P356
10.1016/J.CMET.2014.03.014
P407
P50
P577
2014-04-01T00:00:00Z