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Journal Article
International Journal of Oncology, ISSN 1019-6439, 12/2016, Volume 49, Issue 6, pp. 2227 - 2235
Journal Article
Journal Article
Journal Article
Journal of Cerebral Blood Flow & Metabolism, ISSN 0271-678X, 11/2015, Volume 35, Issue 11, pp. 1783 - 1789
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 8, p. e23295
Background: Sirtuins (SIRT1-7) are a family of NAD-dependent deacetylases and/or ADP-ribosyltransferases that are involved in metabolism, stress responses and... 
RESPIRATORY-CHAIN | COMPLEX-II | METABOLISM | FATTY-ACID OXIDATION | SIRT3-MEDIATED DEACETYLATION | MITOCHONDRIA | BIOLOGY | LYSINE ACETYLATION | STRESS | CALORIE RESTRICTION | PROTEOMICS | Immunoprecipitation | Sirtuin 3 - metabolism | Humans | Substrate Specificity | Immunoblotting | Male | Mitochondrial Proteins - genetics | Succinate Dehydrogenase - chemistry | Mice, 129 Strain | Protein Subunits - metabolism | Mitochondrial Proteins - metabolism | HEK293 Cells | Female | Acetylation | Fibroblasts - metabolism | Protein Subunits - genetics | Protein Structure, Tertiary | Sirtuin 3 - genetics | Mice, Inbred C57BL | Cells, Cultured | Models, Molecular | Binding Sites - genetics | Mice, Knockout | Succinate Dehydrogenase - genetics | Animals | Embryo, Mammalian - cytology | Mitochondrial Proteins - chemistry | Protein Binding | Succinate Dehydrogenase - metabolism | Adipose Tissue, Brown - metabolism | Mice | Protein Subunits - chemistry | Physiological aspects | Enzymes | Electron transport | Mass spectrometry | Sirtuins | Succinate dehydrogenase | Phosphorylation | Dehydrogenases | Adipose tissue | Enzyme activity | Biochemistry | Biology | Dehydrogenase | ADP | Medical schools | Proteins | Electron transport chain | Mitochondria | Enzymatic activity | Aging | Oxidation | Adipose tissue (brown) | Mass spectroscopy | Metabolism | Mammals | SIRT1 protein | Substrates | NAD | Proteomics | Ligands | Scientific imaging
Journal Article
Journal of the American Heart Association, ISSN 2047-9980, 09/2017, Volume 6, Issue 9, p. n/a
Background Trimethylamine‐N‐oxide (TMAO) has recently been identified as a novel and independent risk factor for promoting atherosclerosis through inducing... 
atherosclerosis | trimethylamine‐N‐oxide | vascular inflammation | NOD‐like receptor family pyrin domain containing 3 inflammasome | sirtuin 3 | Sirtuin 3 | Vascular inflammation | NOD-like receptor family pyrin domain containing 3 inflammasome | Atherosclerosis | Trimethylamine-Noxide | ATHEROSCLEROTIC LESIONS | OXIDATIVE STRESS | CARDIAC & CARDIOVASCULAR SYSTEMS | MICROBIOTA METABOLISM | SIRT3 | trimethylamine-N-oxide | CHOLESTEROL CRYSTALS | TRANSPORT | ENDOTHELIAL-CELLS | CARDIOVASCULAR-DISEASE | DYSFUNCTION | PHOSPHATIDYLCHOLINE | Inflammasomes - metabolism | Reactive Oxygen Species - metabolism | Sirtuin 3 - metabolism | Atherosclerosis - genetics | Humans | Sirtuin 3 - deficiency | Mice, 129 Strain | Dose-Response Relationship, Drug | NLR Family, Pyrin Domain-Containing 3 Protein - genetics | Atherosclerosis - enzymology | Vasculitis - genetics | Transfection | RNA Interference | Time Factors | Inflammation Mediators - metabolism | Female | Vasculitis - chemically induced | Superoxide Dismutase - metabolism | Disease Models, Animal | Genetic Predisposition to Disease | Sirtuin 3 - genetics | Human Umbilical Vein Endothelial Cells - drug effects | NLR Family, Pyrin Domain-Containing 3 Protein - metabolism | Atherosclerosis - chemically induced | Inflammasomes - agonists | Cells, Cultured | Mitochondria - metabolism | Antioxidants - pharmacology | Mice, Knockout, ApoE | Mitochondria - drug effects | Inflammasomes - genetics | Apoptosis Regulatory Proteins - metabolism | NLR Family, Pyrin Domain-Containing 3 Protein - agonists | Phenotype | Animals | Human Umbilical Vein Endothelial Cells - enzymology | Signal Transduction - drug effects | Vasculitis - enzymology | Methylamines - toxicity
Journal Article