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1. Full Text Sirtuin 1 and sirtuin 3: Physiological modulators of metabolism
by Nogueiras, Ruben and Habegger, Kirk M and Chaudhary, Nilika and Finan, Brian and Banks, Alexander S and Dietrich, Marcelo O and Horvath, Tamas L and Sinclair, David A and Pfluger, Paul T and Tschöp, Matthias H
Physiological Reviews, ISSN 0031-9333, 07/2012, Volume 92, Issue 3, pp. 1479 - 1514
Nogueiras R, Habegger KM, Chaudhary N, Finan B, Banks AS, Dietrich MO, Horvath TL, Sinclair DA, Pfluger PT, Tschop MH. Sirtuin 1 and Sirtuin 3: Physiological... 
LIFE-SPAN EXTENSION | PHYSIOLOGY | ACTIVATED PROTEIN-KINASE | STIMULATED INSULIN-SECRETION | FATTY-ACID OXIDATION | DNA-DAMAGE RESPONSE | PANCREATIC BETA-CELLS | FOXO TRANSCRIPTION FACTORS | SUPRACHIASMATIC NUCLEUS LESIONS | SMALL-MOLECULE ACTIVATORS | DEPENDENT HISTONE DEACETYLASE | Enzyme Activators - pharmacology | Sirtuin 1 - metabolism | Genetic Predisposition to Disease | Sirtuin 3 - genetics | Sirtuin 3 - metabolism | Humans | Homeostasis | Models, Molecular | Metabolic Diseases - drug therapy | Signal Transduction - genetics | Structure-Activity Relationship | Circadian Rhythm | Sirtuin 1 - genetics | Polymorphism, Genetic | Phenotype | Animals | Metabolic Diseases - metabolism | Signal Transduction - drug effects | Metabolic Diseases - genetics | Protein Conformation | Enzyme Activation | Energy Metabolism - genetics | Energy Metabolism - drug effects | Enzymes | Cell metabolism | Causes of | Metabolic diseases | NAD (Coenzyme) | Regulation | Research | Health aspects
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2. Full Text Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by Mammalian Sirtuins
by Feldman, Jessica L and Baeza, Josue and Denu, John M
Journal of Biological Chemistry, ISSN 0021-9258, 10/2013, Volume 288, Issue 43, pp. 31350 - 31356
Mammalian sirtuins (SIRT1 through SIRT7) are members of a highly conserved family of NAD(+)-dependent protein deacetylases that function in metabolism, genome... 
GENE-EXPRESSION | ASSAYS | METABOLISM | ACYLATION | GLUCOSE | BIOCHEMISTRY & MOLECULAR BIOLOGY | Sirtuin 1 - metabolism | Lipoylation - physiology | Sirtuin 3 - genetics | Sirtuin 3 - metabolism | Humans | Sirtuin 1 - genetics | Sirtuin 2 - metabolism | Hydrolysis | Sirtuin 2 - genetics | Histones - genetics | Acylation - physiology | Histones - metabolism | Sirtuins - genetics | Enzyme Activation - physiology | Fatty Acids - metabolism | Sirtuins - metabolism | Gene Regulation | Sirtuins | Fatty Acids | coA | Post-translational Modification | Reports | Metabolism | Polyunsaturated Fatty Acids | Enzymology | Histone Deacetylase
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3. Full Text Apelin gene therapy increases myocardial vascular density and ameliorates diabetic cardiomyopathy via upregulation of sirtuin 3
by Zeng, Heng and He, Xiaochen and Hou, Xuwei and Li, Lanfang and Chen, Jian-Xiong
American Journal of Physiology - Heart and Circulatory Physiology, ISSN 0363-6135, 02/2014, Volume 306, Issue 4, pp. H585 - H597
Microvascular insufficiency contributes to cardiac hypertrophy and worsens heart dysfunction in diabetic cardiomyopathy. Our recent study shows that apelin may... 
VEGF/VEGFR2 | Diabetic cardiomyopathy | Angiogenesis | Sirtuin 3 | Ang-1/Tie-2 | Apelin | NADPH OXIDASE | METABOLIC SYNDROME | CARDIAC & CARDIOVASCULAR SYSTEMS | PHYSIOLOGY | apelin | sirtuin 3 | angiogenesis | HEART-FAILURE | diabetic cardiomyopathy | TUMOR ANGIOGENESIS | PEPTIDE APELIN | IMPAIRED ANGIOGENESIS | CARDIAC-HYPERTROPHY | PERIPHERAL VASCULAR DISEASE | ORPHAN RECEPTOR APJ | EXPRESSION | ENDOTHELIAL GROWTH-FACTOR | Diabetic Cardiomyopathies - metabolism | Reactive Oxygen Species - metabolism | Sirtuin 3 - metabolism | Male | Vascular Endothelial Growth Factor A - metabolism | Angiopoietin-1 - metabolism | Vascular Endothelial Growth Factor A - genetics | Angiopoietin-2 - metabolism | Diabetic Cardiomyopathies - physiopathology | Receptors, Vascular Endothelial Growth Factor - metabolism | Myocardium - metabolism | Neovascularization, Pathologic - physiopathology | Receptor, TIE-2 - metabolism | Diabetic Cardiomyopathies - therapy | Receptors, Vascular Endothelial Growth Factor - genetics | Neovascularization, Pathologic - therapy | Heart - physiopathology | Sirtuin 3 - genetics | Endothelium, Vascular - physiopathology | Intercellular Signaling Peptides and Proteins - genetics | Up-Regulation - genetics | Adipokines | Receptor, TIE-2 - genetics | Diabetic Cardiomyopathies - genetics | Angiopoietin-1 - genetics | Animals | Endothelium, Vascular - metabolism | Neovascularization, Pathologic - genetics | Mice | Neovascularization, Pathologic - metabolism | Apoptosis - physiology | Prevention | Cardiomyopathy | Physiological aspects | Genetic research | Genetic aspects | Research | Diabetes | Gene therapy | Heart diseases | VEGFR2 | Tie-2 | VEGF | Ang-1 | Integrative Cardiovascular Physiology and Pathophysiology
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4. Full Text SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production
by Bell, E.L and Emerling, B.M and Ricoult, S.J.H and Guarente, L
Oncogene, ISSN 0950-9232, 06/2011, Volume 30, Issue 26, pp. 2986 - 2996
It has become increasing clear that alterations in cellular metabolism have a key role in the generation and maintenance of cancer. Some of the metabolic... 
SirT3 | hypoxia | HIF | mitochondria | ROS | OXIDATIVE STRESS | PROTEIN | PROLYL HYDROXYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | REPLICATIVE LIFE-SPAN | CANCER | CELL BIOLOGY | COMPLEX-III | METABOLISM | ONCOLOGY | GENETICS & HEREDITY | HIF-ALPHA | TUMORIGENESIS | CALORIE RESTRICTION | Neoplasms - metabolism | Sirtuin 3 - genetics | Reactive Oxygen Species - metabolism | Sirtuin 3 - metabolism | Embryo, Mammalian | Hypoxia-Inducible Factor 1, alpha Subunit - genetics | HCT116 Cells | Humans | RNA, Small Interfering - pharmacology | Cells, Cultured | Gene Expression Regulation, Neoplastic | Mitochondria - metabolism | Sirtuin 3 - antagonists & inhibitors | Mitochondria - drug effects | Down-Regulation - genetics | Xenograft Model Antitumor Assays | Animals | Neoplasms - genetics | Hypoxia-Inducible Factor 1, alpha Subunit - metabolism | Mice, Nude | Cell Proliferation - drug effects | Mice | Neoplasms - pathology | Sirtuin 3 - physiology | Original
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5. Full Text Sirtuin 3-dependent mitochondrial dynamic improvements protect against acute kidney injury
by Morigi, Marina and Perico, Luca and Rota, Cinzia and Longaretti, Lorena and Conti, Sara and Rottoli, Daniela and Novelli, Rubina and Remuzzi, Giuseppe and Benigni, Ariela
Journal of Clinical Investigation, ISSN 0021-9738, 02/2015, Volume 125, Issue 2, pp. 715 - 726
Acute kidney injury (AKI) is a public health concern with an annual mortality rate that exceeds those of breast and prostate cancer, heart failure, and... 
MEDICINE, RESEARCH & EXPERIMENTAL | SKELETAL-MUSCLE | CELLS | OXIDATIVE STRESS | L-CARNITINE | NAMPT | ACUTE-RENAL-FAILURE | MECHANISMS | MICE | CISPLATIN NEPHROTOXICITY | PATHOPHYSIOLOGY | Mitochondrial Dynamics | Cell Line | Kidney Tubules, Proximal - pathology | Sirtuin 3 - genetics | Sirtuin 3 - metabolism | Acetylcarnitine - pharmacology | Cisplatin - pharmacokinetics | Acute Kidney Injury - pathology | Humans | Oxidative Stress - genetics | Acute Kidney Injury - genetics | Mitochondria - metabolism | Antioxidants - pharmacology | Mitochondria - pathology | Acute Kidney Injury - enzymology | Vitamin B Complex - pharmacology | Mice, Knockout | Animals | Mitochondria - genetics | Antineoplastic Agents - pharmacology | Mice | Kidney Tubules, Proximal - enzymology | Oxidative Stress - drug effects | Enzymes | Mitochondria | Kidneys | Hydrolases | Genetic aspects | Regulation | Health aspects | Injuries | Membranes | Mortality | Kinases | Gene expression | Proteins | Studies | Rodents | Protein expression | Software | Laboratory animals | Apoptosis | Index Medicus | Abridged Index Medicus
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6. Full Text SIRT3 Deacetylates and Activates OPA1 To Regulate Mitochondrial Dynamics during Stress
by Sadhana A. Samant and Hannah J. Zhang and Zhigang Hong and Vinodkumar B. Pillai and Nagalingam R. Sundaresan and Donald Wolfgeher and Stephen L. Archer and David C. Chan and Mahesh P. Gupta
Molecular and Cellular Biology, ISSN 0270-7306, 03/2014, Volume 34, Issue 5, pp. 807 - 819
Classifications Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit... 
GTPASE OPA1 | SKELETAL-MUSCLE | DOMINANT OPTIC ATROPHY | PROTEIN | FUSION | INCREASED EXPRESSION | GENE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FISSION | CYTOCHROME-C RELEASE | MORPHOLOGY | CELL BIOLOGY | Sirtuin 3 - metabolism | Mitochondrial Dynamics - genetics | Fibroblasts - physiology | Heart - physiology | Humans | Protein Processing, Post-Translational - genetics | Mitochondrial Proteins - genetics | Mitochondrial Dynamics - physiology | Cell Death - genetics | Mitochondria - genetics | Mitochondrial Proteins - metabolism | Acetylation | Fibroblasts - metabolism | Sirtuin 3 - genetics | Cells, Cultured | Mice, Transgenic | Mitochondria - metabolism | Protein Processing, Post-Translational - physiology | Animals | GTP Phosphohydrolases - metabolism | Cell Death - physiology | GTP Phosphohydrolases - genetics | Myocytes, Cardiac - physiology | Cell Line, Tumor | Myocytes, Cardiac - metabolism | Mice | HeLa Cells | Mitochondria - physiology | Index Medicus
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7. Full Text Sirtuin 3 Deficiency Is Associated with Inhibited Mitochondrial Function and Pulmonary Arterial Hypertension in Rodents and Humans
by Paulin, Roxane and Dromparis, Peter and Sutendra, Gopinath and Gurtu, Vikram and Zervopoulos, Sotirios and Bowers, Lyndsay and Haromy, Alois and Webster, Linda and Provencher, Steeve and Bonnet, Sebastien and Michelakis, Evangelos D
Cell Metabolism, ISSN 1550-4131, 11/2014, Volume 20, Issue 5, pp. 827 - 839
Suppression of mitochondrial function promoting proliferation and apoptosis suppression has been described in the pulmonary arteries and extrapulmonary tissues... 
SKELETAL-MUSCLE | METABOLIC SYNDROME | CHANNEL | INSULIN-RESISTANCE | ENDOCRINOLOGY & METABOLISM | DEOXYCORTICOSTERONE ACETATE | SMOOTH-MUSCLE-CELLS | MICE | LYSINE ACETYLATION | HYPOXIA | STRESS | CELL BIOLOGY | Genetic Therapy | Humans | Middle Aged | Familial Primary Pulmonary Hypertension - therapy | Hypertension, Pulmonary - therapy | Pulmonary Artery - metabolism | Adult | Female | Lung - metabolism | Familial Primary Pulmonary Hypertension - pathology | Lung - pathology | Sirtuin 3 - genetics | Down-Regulation | Cells, Cultured | Rats | Familial Primary Pulmonary Hypertension - genetics | Hypertension, Pulmonary - genetics | Mitochondria - metabolism | Mitochondria - pathology | Rats, Sprague-Dawley | Mice, Knockout | Polymorphism, Genetic | Animals | Mice | Lung - blood supply | Hypertension, Pulmonary - pathology | Pulmonary Artery - pathology | Enzymes | Genetic polymorphisms | Pulmonary hypertension | Medical research | Analysis | Genes | Medicine, Experimental
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8. Full Text Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase activity
by Finley, Lydia W. S and Haas, Wilhelm and Desquiret-Dumas, Valérie and Wallace, Douglas C and Procaccio, Vincent and Gygi, Steven P and Haigis, Marcia C
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
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9. Full Text Reciprocal metabolic reprogramming through lactate shuttle coordinately influences tumor-stroma interplay
by Fiaschi, Tania and Marini, Alberto and Giannoni, Elisa and Taddei, Maria Letizia and Gandellini, Paolo and De Donatis, Alina and Lanciotti, Michele and Serni, Sergio and Cirri, Paolo and Chiarugi, Paola
Cancer Research, ISSN 0008-5472, 10/2012, Volume 72, Issue 19, pp. 5130 - 5140
Cancer-associated fibroblasts (CAF) engage in tumor progression by promoting the ability of cancer cells to undergo epithelial-mesenchymal transition (EMT),... 
CELLS | OXIDATIVE STRESS | METASTASIS | CANCER-ASSOCIATED FIBROBLASTS | PYRUVATE-KINASE | ONCOLOGY | INFLAMMATION | GROWTH | WARBURG | HYPOXIA | SIRT3 | Prostatic Neoplasms - metabolism | Sirtuin 3 - metabolism | Oxidative Stress | Humans | Gene Expression Regulation, Neoplastic | Glucose Transporter Type 1 - metabolism | Male | Transplantation, Heterologous | Hypoxia-Inducible Factor 1 - metabolism | Hypoxia-Inducible Factor 1 - genetics | Neoplasms, Experimental - pathology | Monocarboxylic Acid Transporters - metabolism | Prostatic Neoplasms - genetics | RNA Interference | Muscle Proteins - metabolism | Neoplasms, Experimental - genetics | Fibroblasts - metabolism | Prostatic Neoplasms - pathology | Sirtuin 3 - genetics | Lactic Acid - metabolism | Cells, Cultured | Mitochondria - metabolism | Fibroblasts - pathology | Mice, SCID | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Muscle Proteins - genetics | Animals | Glucose Transporter Type 1 - genetics | Models, Biological | Cell Line, Tumor | Glucose - metabolism | Glycolysis | Mice | Monocarboxylic Acid Transporters - genetics | Neoplasms, Experimental - metabolism
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10. Full Text Sirtuin 3 (SIRT3) protein regulates long-chain acyl-CoA dehydrogenase by deacetylating conserved lysines near the active site
by Bharathi, Sivakama S and Zhang, Yuxun and Mohsen, Al-Walid and Uppala, Radha and Balasubramani, Manimalha and Schreiber, Emanuel and Uechi, Guy and Beck, Megan E and Vockley, Jerry and Rardin, Matthew J and Verdin, Eric and Gibson, Bradford W and Hirschey, Matthew D and Goetzman, Eric S
Journal of Biological Chemistry, ISSN 0021-9258, 11/2013, Volume 288, Issue 47, pp. 33837 - 33847
Long-chain acyl-CoA dehydrogenase (LCAD) is a key mitochondrial fatty acid oxidation enzyme. We previously demonstrated increased LCAD lysine acetylation in... 
Sirtuins | OXIDATION | MECHANISM | ACETYLATION | ACYLATION | Enzyme Catalysis | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAD | Acyl-CoA Dehydrogenase | Mitochondria | METABOLISM | Electron Transfer | PLAYS | ENZYMES | Lysine Acetylation | Fatty Acid Oxidation | Posttranslational Modification | ACETYLOME | CALORIE RESTRICTION | PROTEOMICS | Flavin-Adenine Dinucleotide - chemistry | Mitochondria, Liver - genetics | Recombinant Proteins - metabolism | Sirtuin 3 - genetics | Fatty Acids - chemistry | Sirtuin 3 - metabolism | Oxidation-Reduction | Humans | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Catalytic Domain - physiology | Mitochondria, Liver - enzymology | Mice, Knockout | Flavin-Adenine Dinucleotide - metabolism | Animals | Fatty Acids - genetics | Acyl-CoA Dehydrogenase, Long-Chain | Sirtuin 3 - chemistry | Mice | Acetylation | Flavin-Adenine Dinucleotide - genetics | Fatty Acids - metabolism | Metabolism
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11. Full Text Honokiol blocks and reverses cardiac hypertrophy in mice by activating mitochondrial Sirt3
by Pillai, Vinodkumar B and Samant, Sadhana and Sundaresan, Nagalingam R and Raghuraman, Hariharasundaram and Kim, Gene and Bonner, Michael Y and Arbiser, Jack L and Walker, Douglas I and Jones, Dean P and Gius, David and Gupta, Mahesh P
Nature Communications, ISSN 2041-1723, 04/2015, Volume 6, Issue 1, p. 6656
Honokiol (HKL) is a natural biphenolic compound derived from the bark of magnolia trees with anti-inflammatory, anti-oxidative, anti-tumour and neuroprotective... 
METABOLISM | GENE | SIRT3-MEDIATED DEACETYLATION | PATHWAY | PROTEIN-KINASE | MULTIDISCIPLINARY SCIENCES | HOMOLOG | AKT | SIRTUINS | CALORIE RESTRICTION | CELL-DEATH | Mitochondria - enzymology | Fibroblasts - enzymology | Superoxide Dismutase - genetics | Reactive Oxygen Species - metabolism | Sirtuin 3 - metabolism | Myofibroblasts - enzymology | Superoxide Dismutase - antagonists & inhibitors | Cardiomegaly - pathology | Isoproterenol | Lignans - pharmacology | Myocytes, Cardiac - enzymology | Phenylephrine - pharmacology | Biphenyl Compounds - pharmacology | Membrane Proteins - metabolism | Superoxide Dismutase - metabolism | Myofibroblasts - pathology | Sirtuin 3 - genetics | Signal Transduction | Membrane Proteins - genetics | Carrier Proteins - antagonists & inhibitors | Gene Expression Regulation | Adenosine Triphosphatases - metabolism | Myocardium - pathology | Cardiotonic Agents - pharmacology | Mitochondria - drug effects | Mitochondria - pathology | Fibroblasts - pathology | Myofibroblasts - drug effects | Adenosine Triphosphatases - antagonists & inhibitors | Carrier Proteins - genetics | Myocytes, Cardiac - pathology | Acetylation - drug effects | Myocardium - enzymology | Reactive Oxygen Species - antagonists & inhibitors | Animals | Cardiomegaly - prevention & control | Carrier Proteins - metabolism | Myocytes, Cardiac - drug effects | Membrane Proteins - antagonists & inhibitors | Cell Differentiation - drug effects | Fibroblasts - drug effects | Cardiomegaly - chemically induced | Adenosine Triphosphatases - genetics | Cell Proliferation - drug effects | Mice | Enzyme Activation | Primary Cell Culture | Cardiomegaly - genetics
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