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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
Science, ISSN 0036-8075, 1/2003, Volume 299, Issue 5607, pp. 700 - 704
The structure of Escherichia coli succinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the... 
Enzymes | Reactive oxygen species | Dehydrogenases | Atoms | Ligands | Reports | Genetic mutation | Binding sites | Monomers | Electrons | P branes | REPLACEMENT | RESPIRATORY-CHAIN | COMPLEX-II | GENE | COLI FUMARATE REDUCTASE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | HEREDITARY PARAGANGLIOMA | 2FE-2S CLUSTER | MUTATIONS | QUINONE BINDING-SITES | Anaerobiosis | Oxidoreductases - antagonists & inhibitors | Electron Transport | Reactive Oxygen Species - metabolism | Multienzyme Complexes - metabolism | Ubiquinone - metabolism | Crystallography, X-Ray | Succinate Dehydrogenase - chemistry | Oxidoreductases - chemistry | Dinitrophenols - chemistry | Electron Transport Complex II | Flavin-Adenine Dinucleotide - metabolism | Heme - chemistry | Superoxides - metabolism | Binding Sites | Protein Structure, Tertiary | Aerobiosis | Escherichia coli - enzymology | Oxidation-Reduction | Oxidoreductases - metabolism | Protein Structure, Secondary | Oxidoreductases - genetics | Succinate Dehydrogenase - antagonists & inhibitors | Models, Molecular | Multienzyme Complexes - genetics | Multienzyme Complexes - antagonists & inhibitors | Multienzyme Complexes - chemistry | Dinitrophenols - pharmacology | Succinate Dehydrogenase - genetics | Succinic Acid - metabolism | Protein Conformation | Succinate Dehydrogenase - metabolism | Protein Subunits - chemistry | Mutation | Ubiquinone - chemistry | Escherichia coli | Oxidoreductases | Research | Bacteria | Oxygen
Journal Article
Journal Article
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 31, pp. 12744 - 12753
Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent... 
HSPA9 | iron-response element (IRE) | mitochondrial respiratory chain complex | RESPIRATORY-CHAIN | ELEMENT-BINDING-PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FE-S CLUSTERS | ESCHERICHIA-COLI | HSC20 | metalloenzyme | HEAVY-SUBUNIT | RESPONSIVE ELEMENT | CYSTEINE DESULFURASE | MESSENGER-RNA | iron-sulfur protein | iron-sulfur cluster biogenesis | SCAFFOLD PROTEIN | TARGETED DELETION | energy metabolism | ISCU | Iron Regulatory Protein 1 - physiology | Electron Transport | Humans | Protein Multimerization | Homeostasis | Succinate Dehydrogenase - biosynthesis | Iron-Binding Proteins - chemistry | Iron-Regulatory Proteins - biosynthesis | Succinate Dehydrogenase - chemistry | Iron-Sulfur Proteins - chemistry | Molecular Chaperones - chemistry | Apoenzymes - metabolism | Iron-Regulatory Proteins - physiology | Iron-Regulatory Proteins - chemistry | Iron-Sulfur Proteins - biosynthesis | Carbon-Sulfur Lyases - physiology | HSP70 Heat-Shock Proteins - chemistry | Protein Interaction Domains and Motifs | HSP70 Heat-Shock Proteins - biosynthesis | Molecular Chaperones - biosynthesis | Iron-Binding Proteins - physiology | Response Elements | Iron Regulatory Protein 1 - chemistry | Carbon-Sulfur Lyases - biosynthesis | Mitochondrial Proteins - physiology | Models, Molecular | Mitochondrial Proteins - biosynthesis | Molecular Chaperones - physiology | Iron-Binding Proteins - biosynthesis | Protein Folding | Iron-Sulfur Proteins - physiology | Gene Expression Regulation, Enzymologic | Animals | Iron - physiology | Mitochondrial Proteins - chemistry | Apoenzymes - chemistry | HSP70 Heat-Shock Proteins - physiology | Succinate Dehydrogenase - physiology | Carbon-Sulfur Lyases - chemistry | Iron Regulatory Protein 1 - biosynthesis | Minireviews
Journal Article
Pest Management Science, ISSN 1526-498X, 08/2017, Volume 73, Issue 8, pp. 1585 - 1592
BACKGROUNDSuccinate dehydrogenase (SDH) plays an important role in the Krebs cycle, which is considered as an attractive target for development of succinate... 
pyrazole | succinate dehydrogenase inhibitors | molecule docking | nicotinamide | SUCCINATE-DEHYDROGENASE | MITOCHONDRIAL RESPIRATION | FUMARATE REDUCTASE | COMPLEX | AGRONOMY | FUNGICIDES | ENTOMOLOGY | DISCOVERY | Antifungal Agents - pharmacology | Catalytic Domain | Chemistry Techniques, Synthetic | Enzyme Inhibitors - metabolism | Helminthosporium - drug effects | Niacinamide - metabolism | Succinate Dehydrogenase - antagonists & inhibitors | Enzyme Inhibitors - pharmacology | Niacinamide - chemical synthesis | Antifungal Agents - chemical synthesis | Antifungal Agents - chemistry | Succinate Dehydrogenase - chemistry | Enzyme Inhibitors - chemical synthesis | Pyrazoles - chemistry | Rhizoctonia - drug effects | Niacinamide - chemistry | Enzyme Inhibitors - chemistry | Antifungal Agents - metabolism | Drug Design | Succinate Dehydrogenase - metabolism | Molecular Docking Simulation | Niacinamide - pharmacology | Niacinamide | Chemical industry | Herbicides | Pesticides industry | Analysis | NADPH | Binding | Tricarboxylic acid cycle | Enzymes | Succinate dehydrogenase | Dehydrogenases | Fungicides | Computer simulation | Antifungal agents | Derivatives | Dehydrogenase | Krebs cycle | Pyrazole | Design optimization | Antifungal activity | Biological effects | Inhibitors | Simulation | Docking | Nicotinamide | Chemical synthesis
Journal Article