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acetate-coa ligase - metabolism (378) 378
acetate-coa ligase - genetics (160) 160
animals (153) 153
index medicus (140) 140
biochemistry & molecular biology (125) 125
microbiology (98) 98
acetates - metabolism (97) 97
acetate-coa ligase - chemistry (85) 85
kinetics (80) 80
humans (76) 76
metabolism (69) 69
molecular sequence data (66) 66
enzymes (65) 65
escherichia-coli (62) 62
research (61) 61
amino acid sequence (59) 59
acetate (58) 58
ligases (58) 58
male (56) 56
acetyl coenzyme a - metabolism (55) 55
rats (52) 52
coenzyme a ligases - metabolism (50) 50
physiological aspects (49) 49
acetyl-coa synthetase (48) 48
acetylation (48) 48
bacteria (48) 48
mice (45) 45
escherichia coli - genetics (43) 43
proteins (41) 41
coenzyme-a synthetase (40) 40
expression (40) 40
mutation (40) 40
saccharomyces-cerevisiae (40) 40
substrate specificity (39) 39
acetates (38) 38
biotechnology & applied microbiology (38) 38
bacterial proteins - metabolism (36) 36
glucose - metabolism (36) 36
binding sites (35) 35
cell biology (35) 35
female (35) 35
gene expression (35) 35
genes (35) 35
aldehyde oxidoreductases - metabolism (34) 34
analysis (34) 34
research article (34) 34
carbon-monoxide dehydrogenase (32) 32
catalysis (32) 32
clostridium-thermoaceticum (32) 32
glucose (31) 31
article (29) 29
gene (29) 29
base sequence (28) 28
growth (28) 28
saccharomyces cerevisiae - enzymology (28) 28
yeast (28) 28
biosynthesis (27) 27
bacterial proteins - genetics (26) 26
gene expression regulation, bacterial (26) 26
cloning, molecular (25) 25
enzyme (25) 25
multidisciplinary sciences (25) 25
multienzyme complexes - metabolism (25) 25
acetate-coa ligase - isolation & purification (24) 24
adenosine triphosphate - metabolism (24) 24
escherichia coli - metabolism (24) 24
ethanol - metabolism (24) 24
nickel (24) 24
transcription, genetic (24) 24
acetate-coa ligase - biosynthesis (23) 23
acetic acid (23) 23
genetic aspects (23) 23
oxidation-reduction (23) 23
fatty acids (22) 22
liver - enzymology (22) 22
nickel - chemistry (22) 22
atp citrate-lyase - metabolism (21) 21
crystal-structure (21) 21
models, biological (21) 21
acetyl coenzyme a - biosynthesis (20) 20
bacteriology (20) 20
biochemistry (20) 20
fermentation (20) 20
lipid metabolism (20) 20
liver - metabolism (20) 20
purification (20) 20
activation (19) 19
escherichia coli (19) 19
escherichia coli - enzymology (19) 19
hydrogen-ion concentration (19) 19
identification (19) 19
saccharomyces cerevisiae - genetics (19) 19
acetate-coa ligase - antagonists & inhibitors (18) 18
biophysics (18) 18
coa synthetase (18) 18
coenzyme (18) 18
fatty acids - metabolism (18) 18
gene expression regulation, enzymologic (18) 18
iron-sulfur protein (18) 18
molecular weight (18) 18
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1. Full Text Acetate Dependence of Tumors
by Comerford, Sarah A and Huang, Zhiguang and Du, Xinlin and Wang, Yun and Cai, Ling and Witkiewicz, Agnes K and Walters, Holly and Tantawy, Mohammed N and Fu, Allie and Manning, H. Charles and Horton, Jay D and Hammer, Robert E and McKnight, Steven L and Tu, Benjamin P
Cell, ISSN 0092-8674, 12/2014, Volume 159, Issue 7, pp. 1591 - 1602
Acetyl-CoA represents a central node of carbon metabolism that plays a key role in bioenergetics, cell proliferation, and the regulation of gene expression.... 
COENZYME-A-SYNTHETASE | HEPATOCELLULAR-CARCINOMA | CANCER CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | ACETYL-COA SYNTHETASE | CELL-SURVIVAL | SACCHAROMYCES-CEREVISIAE | HISTONE ACETYLATION | REDUCTIVE CARBOXYLATION | GLUTAMINE-METABOLISM | CELL BIOLOGY | Immunohistochemistry | Neoplasms - metabolism | Acetates - metabolism | Humans | Positron-Emission Tomography | Acetyl Coenzyme A - metabolism | Acetate-CoA Ligase - analysis | Neoplasms - chemistry | Triple Negative Breast Neoplasms - chemistry | Animals | Acetate-CoA Ligase - genetics | Acetate-CoA Ligase - metabolism | Liver Neoplasms - metabolism | Triple Negative Breast Neoplasms - pathology | Mice | Neoplasms - pathology | Metabolites | Molecular genetics | Ligases | Physiological aspects | Histones | Lipids | Gene expression | Acetates | Tumors
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2. Full Text Acetate Is a Bioenergetic Substrate for Human Glioblastoma and Brain Metastases
by Mashimo, Tomoyuki and Pichumani, Kumar and Vemireddy, Vamsidhara and Hatanpaa, Kimmo J and Singh, Dinesh Kumar and Sirasanagandla, Shyam and Nannepaga, Suraj and Piccirillo, Sara G and Kovacs, Zoltan and Foong, Chan and Huang, Zhiguang and Barnett, Samuel and Mickey, Bruce E and DeBerardinis, Ralph J and Tu, Benjamin P and Maher, Elizabeth A and Bachoo, Robert M
Cell, ISSN 0092-8674, 12/2014, Volume 159, Issue 7, pp. 1603 - 1614
Glioblastomas and brain metastases are highly proliferative brain tumors with short survival times. Previously, using C-NMR analysis of brain tumors resected... 
MOUSE-BRAIN | OXIDATION | HEART | CITRIC-ACID CYCLE | METABOLISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | C-11-ACETATE PET | C-13 NMR-SPECTROSCOPY | CANCER | CARBON FLUX | CELL BIOLOGY | Acetates - metabolism | Humans | Brain Neoplasms - pathology | Brain Neoplasms - metabolism | Citric Acid Cycle | Brain Neoplasms - secondary | Animals | Acetate-CoA Ligase - genetics | Acetate-CoA Ligase - metabolism | Neoplasm Metastasis - pathology | Glioblastoma - pathology | Glioblastoma - metabolism | Glutamic Acid - metabolism | Mice | Disease Models, Animal | Glucose metabolism | Ligases | Metastasis | Glucose | Acetates | Dextrose | Citric acid | Glutamine
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3. Full Text ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation
by Kathryn E. Wellen and Georgia Hatzivassiliou and Uma M. Sachdeva and Thi V. Bui and Justin R. Cross and Craig B. Thompson
Science, ISSN 0036-8075, 5/2009, Volume 324, Issue 5930, pp. 1076 - 1080
Histone acetylation in single-cell eukaryotes relies on acetyl coenzyme A (acetyl-CoA) synthetase enzymes that use acetate to produce acetyl-CoA. Metazoans,... 
Cellular metabolism | HCT116 cells | Cell lines | Histones | Small interfering RNA | Reports | Gene expression regulation | Acetylation | Adipocytes | Acetates | Cellular differentiation | ACTIVATION | DEACETYLATION | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | COMPLEXES | DYNAMICS | SYNTHETASE | SIRTUINS | EXPRESSION | ACETYLTRANSFERASE | Cell Proliferation | Humans | Adipocytes - cytology | Cell Nucleus - enzymology | Intercellular Signaling Peptides and Proteins - metabolism | RNA Interference | Acetate-CoA Ligase - genetics | Transcription, Genetic | Cell Differentiation | ATP Citrate (pro-S)-Lyase - metabolism | Cell Line | Cytoplasm - enzymology | Interleukin-3 - metabolism | Gene Expression Regulation | ATP Citrate (pro-S)-Lyase - genetics | Histone Deacetylases - metabolism | Acetyl Coenzyme A - metabolism | Animals | Acetate-CoA Ligase - metabolism | Adipocytes - metabolism | Cell Line, Tumor | Glucose - metabolism | Glycolysis | Citric Acid - metabolism | Histone Deacetylase Inhibitors | Mice | Histones - metabolism | 3T3 Cells | Cell metabolism | Research | Properties | Adenosine triphosphate | Enzymes | Chromatin | Biochemistry | Glucose | Cellular biology | Metabolism
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4. Full Text Intracellular Crotonyl-CoA Stimulates Transcription through p300-Catalyzed Histone Crotonylation
by Sabari, Benjamin R and Tang, Zhanyun and Huang, He and Yong-Gonzalez, Vladimir and Molina, Henrik and Kong, Ha Eun and Dai, Lunzhi and Shimada, Miho and Cross, Justin R and Zhao, Yingming and Roeder, Robert G and Allis, C. David
Molecular Cell, ISSN 1097-2765, 04/2015, Volume 58, Issue 2, pp. 203 - 215
Acetylation of histones at DNA regulatory elements plays a critical role in transcriptional activation. Histones are also modified by other acyl moieties,... 
YEAST | ACTIVATION | METABOLISM | CHROMATIN | ACETYLATION | P300 | BIOCHEMISTRY & MOLECULAR BIOLOGY | PURIFICATION | IDENTIFICATION | P53 | CELL BIOLOGY | Cell Line | Humans | Transcriptional Activation | E1A-Associated p300 Protein - genetics | Molecular Sequence Data | Acyl Coenzyme A - genetics | E1A-Associated p300 Protein - metabolism | Macrophages - cytology | RNA, Messenger - metabolism | Cell-Free System | Acetate-CoA Ligase - genetics | Acetate-CoA Ligase - metabolism | HEK293 Cells | Lipopolysaccharides - pharmacology | Macrophages - drug effects | Acetylation | HeLa Cells | Histones - metabolism | Acyl Coenzyme A - metabolism | Macrophages - immunology | Epigenetic inheritance | Analysis | Histones | Genetic transcription | Molecular biology | Acetates | Acylation
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5. Full Text Acetyl-CoA Synthetase 2 Promotes Acetate Utilization and Maintains Cancer Cell Growth under Metabolic Stress
by Schug, Zachary T and Peck, Barrie and Jones, Dylan T and Zhang, Qifeng and Grosskurth, Shaun and Alam, Israt S and Goodwin, Louise M and Smethurst, Elizabeth and Mason, Susan and Blyth, Karen and McGarry, Lynn and James, Daniel and Shanks, Emma and Kalna, Gabriela and Saunders, Rebecca E and Jiang, Ming and Howell, Michael and Lassailly, Francois and Thin, May Zaw and Spencer-Dene, Bradley and Stamp, Gordon and van den Broek, Niels J.F and Mackay, Gillian and Bulusu, Vinay and Kamphorst, Jurre J and Tardito, Saverio and Strachan, David and Harris, Adrian L and Aboagye, Eric O and Critchlow, Susan E and Wakelam, Michael J.O and Schulze, Almut and Gottlieb, Eyal
Cancer Cell, ISSN 1535-6108, 01/2015, Volume 27, Issue 1, pp. 57 - 71
A functional genomics study revealed that the activity of acetyl-CoA synthetase 2 (ACSS2) contributes to cancer cell growth under low-oxygen and lipid-depleted... 
COENZYME-A-SYNTHETASE | BREAST-CANCER | HUMAN LIVER COMPLEX | ONCOLOGY | STEROL REGULATORY ELEMENT | PROSTATE-CANCER | TUMOR-CELLS | FATTY-ACID SYNTHASE | LIPOPROTEIN RECEPTOR PROMOTER | NUCLEAR-PROTEIN | SYNTHESIS PATHWAY | CELL BIOLOGY | Neoplasms - metabolism | Neoplasm Transplantation | Cell Proliferation | Humans | Gene Expression Regulation, Neoplastic | Stress, Physiological | Gene Dosage | Disease Progression | Animals | MCF-7 Cells | Neoplasms - genetics | Acetate-CoA Ligase - genetics | Acetate-CoA Ligase - metabolism | Mice, Nude | Cell Line, Tumor | Hypoxia | Mice | Neoplasms - pathology | Fatty Acids - metabolism | Growth | Ligases | Genomics | Development and progression | Stress (Physiology) | Fatty acids | Acetates | Cancer | Index Medicus
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6. Full Text Acetyl-CoA synthetase regulates histone acetylation and hippocampal memory
by Mews, Philipp and Donahue, Greg and Drake, Adam M and Luczak, Vincent and Abel, Ted and Berger, Shelley L
Nature, ISSN 0028-0836, 06/2017, Volume 546, Issue 7658, pp. 381 - 386
Metabolic production of acetyl coenzyme A (acetyl-CoA) is linked to histone acetylation and gene regulation, but the precise mechanisms of this process are... 
COENZYME | CONSOLIDATION | EPIGENETICS | ACTIVATION | METABOLISM | CHROMATIN | MULTIDISCIPLINARY SCIENCES | GENE-EXPRESSION | ACETATE | SYNAPTIC PLASTICITY | BRAIN | Chromatin - metabolism | Up-Regulation | Histones - chemistry | Transcriptional Activation | Neurons - cytology | Neuronal Plasticity - genetics | Cell Nucleus - metabolism | Neuronal Plasticity - physiology | Acetate-CoA Ligase - genetics | Hippocampus - enzymology | Cell Differentiation | Neurons - metabolism | Acetylation | Cells, Cultured | Acetyl Coenzyme A - metabolism | Acetate-CoA Ligase - deficiency | Memory Consolidation - physiology | Gene Expression Regulation, Enzymologic | Hippocampus - metabolism | Animals | Acetate-CoA Ligase - metabolism | Chromatin - enzymology | Mice | Histones - metabolism | Hippocampus - physiology | Chromatin - genetics | Memory - physiology | Histones | Hippocampus (Brain) | Health aspects | Memory | Cell culture | Chromatin | Ontology | Transcription | Genes | Gene regulation | Genomics | Spatial discrimination | Cognitive ability | Kinases | Plasticity (neural) | Proteins | Memory tasks | Metabolites | Rodents | Coenzyme A | Enzymes | Neurons | Spatial analysis | Metabolism | Mammals | Gene expression | Epigenetics | Nuclei (cytology) | Genetic engineering | Hippocampus | Spatial memory | Plastic foam
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7. Full Text Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase
by Can, Mehmet and Armstrong, Fraser A and Ragsdale, Stephen W
Chemical Reviews, ISSN 0009-2665, 04/2014, Volume 114, Issue 8, pp. 4149 - 4174
  A study investivated the structure, function and mechanism of the nickel metalloenzymes carbon monoxide (CO) dehydrogenase and acetyl coenzyme A synthase... 
CORRINOID ENZYME COMPLEX | WOOD-LJUNGDAHL PATHWAY | IRON-SULFUR PROTEIN | WATER-GAS SHIFT | CARBON-MONOXIDE DEHYDROGENASE | RAY-ABSORPTION-SPECTROSCOPY | RHODOSPIRILLUM-RUBRUM | COENZYME-A SYNTHASE | CHEMISTRY, MULTIDISCIPLINARY | N-BUTYL ISOCYANIDE | CLOSTRIDIUM-THERMOACETICUM | Acetate-CoA Ligase - chemistry | Humans | Multienzyme Complexes - metabolism | Multienzyme Complexes - antagonists & inhibitors | Aldehyde Oxidoreductases - metabolism | Multienzyme Complexes - chemistry | Metalloproteins - metabolism | Animals | Metalloproteins - chemistry | Acetate-CoA Ligase - metabolism | Aldehyde Oxidoreductases - chemistry | Aldehyde Oxidoreductases - antagonists & inhibitors | Nickel - metabolism | Acetyl coenzyme A synthetase | Chemical properties | Research | Chemical structure | Chemical bonds | Enzymes | Oxidation | Carbon monoxide | Carbon dioxide | Review
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8. Full Text Reversible Lysine Acetylation Controls the Activity of the Mitochondrial Enzyme Acetyl-CoA Synthetase 2
by Bjoern Schwer and Jakob Bunkenborg and Regis O. Verdin and Jens S. Andersen and Eric Verdin
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2006, Volume 103, Issue 27, pp. 10224 - 10229
We report that human acetyl-CoA synthetase 2 (AceCS2) is a mitochondrial matrix protein. AceCS2 is reversibly acetylated at Lys-642 in the active site of the... 
Proteins | Enzymes | Mitochondria | HEK293 cells | Antibodies | HeLa cells | Bacteria | Immunoblotting | Acetylation | Acetates | SIRT5 | sir2 | Sirtuin | SIRT3 | SIR2-LIKE PROTEINS | MULTIDISCIPLINARY SCIENCES | PROTEIN DEACETYLASES | TARGETING SEQUENCES | SACCHAROMYCES-CEREVISIAE | DEPENDENT DEACETYLASE | LIFE-SPAN EXTENSION | SALMONELLA-ENTERICA | sirtuin | ACETATE | CALORIE RESTRICTION | Amino Acid Sequence | Cell Line | Mitochondria - enzymology | Acetate-CoA Ligase - chemistry | Humans | Cercopithecus aethiops | Molecular Sequence Data | Mitochondrial Proteins - genetics | Lysine - genetics | Sequence Alignment | Animals | Sirtuin 3 | Acetate-CoA Ligase - genetics | Acetate-CoA Ligase - metabolism | Mitochondrial Proteins - metabolism | Conserved Sequence | Lysine - metabolism | Sirtuins - genetics | Binding Sites | Sirtuins - metabolism | Research | Amino acids | Metabolism | Mammals | Biological Sciences
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9. Full Text Sirtuins Deacetylate and Activate Mammalian Acetyl-CoA Synthetases
by William C. Hallows and Susan Lee and John M. Denu
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2006, Volume 103, Issue 27, pp. 10230 - 10235
Silent Information Regulator 2 (Sir2) enzymes (or sirtuins) are NAD⁺-dependent deacetylases that modulate gene silencing, aging and energy metabolism. Previous... 
COS cells | Enzymes | Mitochondria | Energy metabolism | Antibodies | Lipids | Gene expression regulation | Acetylation | Acetates | Fatty acids | Sir2 | Acetyltransferase | Acetate | Metabolism | Deacetylation | TRANSCRIPTION FACTORS | SIR2-LIKE PROTEINS | MULTIDISCIPLINARY SCIENCES | SIRT1 DEACETYLASE | PLASMA ACETATE | CELL-SURVIVAL | ELEMENT-BINDING PROTEINS | SACCHAROMYCES-CEREVISIAE | DEPENDENT DEACETYLASE | acetate | SALMONELLA-ENTERICA | deacetylation | metabolism | acetyltransferase | INCREASED DOSAGE | Acetyltransferases - metabolism | Humans | Cercopithecus aethiops | Animals | Acetate-CoA Ligase - genetics | Acetate-CoA Ligase - metabolism | Mice | Catalysis | Enzyme Activation | Sirtuins - genetics | COS Cells | Sirtuins - metabolism | Research | Proteins | Studies | Mammals | Biological Sciences
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10. Full Text Acetate Recapturing by Nuclear Acetyl-CoA Synthetase 2 Prevents Loss of Histone Acetylation during Oxygen and Serum Limitation
by Bulusu, Vinay and Tumanov, Sergey and Michalopoulou, Evdokia and van den Broek, Niels J and MacKay, Gillian and Nixon, Colin and Dhayade, Sandeep and Schug, Zachary T and Vande Voorde, Johan and Blyth, Karen and Gottlieb, Eyal and Vazquez, Alexei and Kamphorst, Jurre J
Cell Reports, ISSN 2211-1247, 01/2017, Volume 18, Issue 3, pp. 647 - 658
Acetyl-CoA is a key metabolic intermediate with an important role in transcriptional regulation. The nuclear-cytosolic acetyl-CoA synthetase 2 (ACSS2) was... 
acetate | cancer metabolism | hypoxia | acetyl-CoA synthetase 2 | histone deacetylation | lipogenesis | stable isotope tracing | enzyme localization | histone acetylation | metabolite compartmentalization | LC-MS | ISOTOPE TRACERS | ADAPTATION | FATTY-ACID-METABOLISM | DYNAMICS | MECHANISMS | CELL-GROWTH | HYPOXIA | CANCER | EXPRESSION | CELL BIOLOGY | Acetates - metabolism | Humans | Metabolome | Acetates - chemistry | Mitochondria - metabolism | Chromatography, High Pressure Liquid | Acetyl Coenzyme A - metabolism | Cell Nucleus - enzymology | Acetate-CoA Ligase - antagonists & inhibitors | Cell Hypoxia | RNA Interference | Acetate-CoA Ligase - genetics | Acetate-CoA Ligase - metabolism | Mass Spectrometry | Cell Line, Tumor | Acetylation | Histones - metabolism | Culture Media - chemistry | Carbon Isotopes - chemistry | Microscopy, Fluorescence | RNA, Small Interfering - metabolism | Serum - chemistry
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11. Full Text Nucleus-Translocated ACSS2 Promotes Gene Transcription for Lysosomal Biogenesis and Autophagy
by Li, Wei and Li, Xinjian and Yu, Willie and Qian, Xu and Qian, Chao-Nan and Xia, Yan and Zheng, Yanhua and Lee, Jong-Ho and Lyu, Jianxin and Rao, Ganesh and Zhang, Xiaochun and Rozen, Steven G and Jiang, Tao and Lu, Zhimin
Molecular Cell, ISSN 1097-2765, 06/2017, Volume 66, Issue 5, pp. 684 - 697.e9
Overcoming metabolic stress is a critical step in tumor growth. Acetyl coenzyme A (acetyl-CoA) generated from glucose and acetate uptake is important for... 
ACSS2 | lysosomal biogenesis | autophagy | TFEB | nucleus | AMPK | acetyl-CoA | tumor development | COENZYME-A-SYNTHETASE | ENERGY STRESS | HUMAN GENOME | PROTEIN-KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACETYL-COA SYNTHETASE | CELL-GROWTH | BETA-CATENIN | ACETATE | HISTONE ACETYLATION | METABOLIC STRESS | CELL BIOLOGY | alpha Karyopherins - metabolism | AMP-Activated Protein Kinases - metabolism | Glioblastoma - enzymology | Phosphorylation | Humans | Brain Neoplasms - pathology | Gene Expression Regulation, Neoplastic | Stress, Physiological | Male | Autophagy | Cell Nucleus - enzymology | Organelle Biogenesis | Lysosomes - metabolism | Transfection | Glioblastoma - genetics | RNA Interference | Acetate-CoA Ligase - genetics | Cell Nucleus - pathology | Transcription, Genetic | Acetylation | Active Transport, Cell Nucleus | Binding Sites | Promoter Regions, Genetic | Brain Neoplasms - enzymology | Cell Survival | Brain Neoplasms - genetics | Acetyl Coenzyme A - metabolism | Animals | Energy Metabolism | Acetate-CoA Ligase - metabolism | Mice, Nude | Glioblastoma - pathology | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - genetics | alpha Karyopherins - genetics | Cell Line, Tumor | Protein Binding | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - metabolism | Mice, Inbred BALB C | Protein Processing, Post-Translational | Histones - metabolism | Medical colleges | Thiols | Brain tumors | Genes | Genetic transcription | Glucose | Dextrose | Gliomas | Ligases | Stem cells | Medical genetics | Genetic aspects | Protein kinases | Resveratrol | Development and progression
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12. Full Text Conserved Metabolic Regulatory Functions of Sirtuins
by Schwer, Bjoern and Verdin, Eric
Cell Metabolism, ISSN 1550-4131, 2008, Volume 7, Issue 2, pp. 104 - 112
Silent information regulator 2 (Sir2) proteins, or sirtuins, are protein deacetylases/mono-ADP-ribosyltransferases found in organisms ranging from bacteria to... 
COENZYME-A SYNTHETASE | DEPENDENT PROTEIN DEACETYLASES | CEREVISIAE LIFE-SPAN | MITOCHONDRIAL-FUNCTION | INSULIN-SECRETION | ENDOCRINOLOGY & METABOLISM | PANCREATIC BETA-CELLS | ACETYL-COA SYNTHETASE | LYSINE ACETYLATION | SACCHAROMYCES-CEREVISIAE | CALORIE RESTRICTION | CELL BIOLOGY | Animals | Acetate-CoA Ligase - metabolism | Humans | Sirtuins - physiology | Bacteria | Metabolism | NAD - metabolism | Physiological aspects | Niacinamide | Purines | Ligases
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