Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix.
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Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondriaLysine glutarylation is a protein posttranslational modification regulated by SIRT5Protein Modifications as Manifestations of Hyperglycemic Glucotoxicity in Diabetes and Its ComplicationsInhibition of histone deacetylases in cancer therapy: lessons from leukaemiaHyperglycemic Stress and Carbon Stress in Diabetic GlucotoxicityThe Impact of Non-Enzymatic Reactions and Enzyme Promiscuity on Cellular Metabolism during (Oxidative) Stress ConditionsNonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylasesActivation of SIRT3 by the NAD⁺ precursor nicotinamide riboside protects from noise-induced hearing lossStructural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylationChemical probing of the human sirtuin 5 active site reveals its substrate acyl specificity and peptide-based inhibitorsDefining the orphan functions of lysine acetyltransferasesMitochondrial protein acetylation is driven by acetyl-CoA from fatty acid oxidationInterplay between oxidant species and energy metabolismIntrinsic Tau Acetylation Is Coupled to Auto-Proteolytic Tau FragmentationNutritional stress exacerbates hepatic steatosis induced by deletion of the histidine nucleotide-binding (Hint2) mitochondrial proteinSIRT5 regulates the mitochondrial lysine succinylome and metabolic networksA Proteomic Approach to Analyze the Aspirin-mediated Lysine AcetylomeAvoiding abundance bias in the functional annotation of posttranslationally modified proteinsA continuous sirtuin activity assay without any coupling to enzymatic or chemical reactions.Quantitative proteomic analysis of histone modificationsQuantification of Lysine Acetylation and Succinylation Stoichiometry in Proteins Using Mass Spectrometric Data-Independent Acquisitions (SWATH)Stoichiometry of site-specific lysine acetylation in an entire proteome.In silico analysis of protein Lys-N(𝜀)-acetylation in plants.Interplay of mitochondrial metabolism and microRNAs.Overexpression of mitochondrial sirtuins alters glycolysis and mitochondrial function in HEK293 cells.Understanding the acetylome: translating targeted proteomics into meaningful physiologyProtein acetylation and acetyl coenzyme a metabolism in budding yeastLysine malonylation is elevated in type 2 diabetic mouse models and enriched in metabolic associated proteins.The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sitesMaximal oxidative capacity during exercise is associated with skeletal muscle fuel selection and dynamic changes in mitochondrial protein acetylationMitochondrial 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.Alpha-ketoglutarate dehydrogenase complex-dependent succinylation of proteins in neurons and neuronal cell lines.The ɛ-Amino Group of Protein Lysine Residues Is Highly Susceptible to Nonenzymatic Acylation by Several Physiological Acyl-CoA Thioesters.Lysine Acetylation Activates Mitochondrial Aconitase in the HeartUsing 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.Ketogenic diets, mitochondria, and neurological diseases.
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Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 13 August 2013
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Widespread and enzyme-independ ...... s of the mitochondrial matrix.
@en
Widespread and enzyme-independ ...... s of the mitochondrial matrix.
@nl
type
label
Widespread and enzyme-independ ...... s of the mitochondrial matrix.
@en
Widespread and enzyme-independ ...... s of the mitochondrial matrix.
@nl
prefLabel
Widespread and enzyme-independ ...... s of the mitochondrial matrix.
@en
Widespread and enzyme-independ ...... s of the mitochondrial matrix.
@nl
P2860
P356
P1476
Widespread and enzyme-independ ...... s of the mitochondrial matrix.
@en
P2093
Gregory R Wagner
R Mark Payne
P2860
P304
29036-29045
P356
10.1074/JBC.M113.486753
P407
P577
2013-08-13T00:00:00Z