Protective effects and mechanisms of sirtuins in the nervous system

MicroRNAs: Target Recognition and Regulatory Functions

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Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

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A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis

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Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

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Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

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Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

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Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1

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Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase

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hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

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The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

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Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

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Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

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Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ

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Sirtuin activators mimic caloric restriction and delay ageing in metazoans

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Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1

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The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress

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CBP/p300 in cell growth, transformation, and development

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Requirement of NAD and SIR2 for Life-Span Extension by Calorie Restriction in Saccharomyces cerevisiae

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Sirtuins in mammals: insights into their biological function

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SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation

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Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans

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A probability-based approach for high-throughput protein phosphorylation analysis and site localization

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The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase

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Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction

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Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey

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Large-scale characterization of HeLa cell nuclear phosphoproteins

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Mammalian SIRT1 Represses Forkhead Transcription Factors

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Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins

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miR-34a repression of SIRT1 regulates apoptosis

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Sir2 mediates longevity in the fly through a pathway related to calorie restriction

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Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation

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A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis

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Amyloid-β and tau--a toxic pas de deux in Alzheimer’s disease

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Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation

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Circadian Control of the NAD + Salvage Pathway by CLOCK-SIRT1

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The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor α in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes

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SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells

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Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction

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Circadian Clock Feedback Cycle Through NAMPT-Mediated NAD + Biosynthesis

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HuR and mRNA stability

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Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

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‘Ischemic tolerance’ phenomenon found in the brain

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Sirtuin 2 Inhibitors Rescue α-Synuclein-Mediated Toxicity in Models of Parkinson's Disease

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Nibrin, a Novel DNA Double-Strand Break Repair Protein, Is Mutated in Nijmegen Breakage Syndrome

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SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis

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Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration

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SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α

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Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice

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Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation

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Inhibition of Silencing and Accelerated Aging by Nicotinamide, a Putative Negative Regulator of Yeast Sir2 and Human SIRT1

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A novel pathway regulates memory and plasticity via SIRT1 and miR-134

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The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases

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Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival

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Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

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In vivo evidence that erythropoietin protects neurons from ischemic damage

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HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention

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Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

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SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1

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Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress

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SIRT1 Promotes Endothelium-Dependent Vascular Relaxation by Activating Endothelial Nitric Oxide Synthase

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SIRT6 Promotes DNA Repair Under Stress by Activating PARP1

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Glucose Restriction Inhibits Skeletal Myoblast Differentiation by Activating SIRT1 through AMPK-Mediated Regulation of Nampt

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SIRT1 Modulation of the Acetylation Status, Cytosolic Localization, and Activity of LKB1

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Axon degeneration mechanisms: Commonality amid diversity

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Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.Preprint

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SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle

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Nucleocytoplasmic Shuttling of the NAD+-dependent Histone Deacetylase SIRT1*

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The biochemistry of sirtuins

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Sirtuin 1 Modulates Cellular Responses to Hypoxia by Deacetylating Hypoxia-Inducible Factor 1α

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SIRT1 Protects against Microglia-dependent Amyloid-β Toxicity through Inhibiting NF-κB Signaling

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Resveratrol stimulates AMP kinase activity in neurons

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Enlarged Infarcts in Endothelial Nitric Oxide Synthase Knockout Mice are Attenuated by Nitro-L-Arginine

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A phylogenetically conserved NAD + -dependent protein deacetylase activity in the Sir2 protein family

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Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

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Mitochondrial calcium and the permeability transition in cell death

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Identification of the differential distribution patterns of mRNAs and consensus binding sequences for mouse DAF-16 homologues

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Nutrient Availability Regulates SIRT1 Through a Forkhead-Dependent Pathway

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Regulation of SIRT1 in cellular functions: Role of polyphenols

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Tumor Suppressor HIC1 Directly Regulates SIRT1 to Modulate p53-Dependent DNA-Damage Responses

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p300/CBP and cancer

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SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction

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FOXO transcription factors directly activate bim gene expression and promote apoptosis in sympathetic neurons

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SIRT1 Deacetylates and Positively Regulates the Nuclear Receptor LXR

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Calorie restriction enhances cell adaptation to hypoxia through Sirt1-dependent mitochondrial autophagy in mouse aged kidney

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Calorie restriction extends yeast life span by lowering the level of NADH

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Neuronal SIRT1 Activation as a Novel Mechanism Underlying the Prevention of Alzheimer Disease Amyloid Neuropathology by Calorie Restriction

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Wallerian degeneration of injured axons and synapses is delayed by a Ube4b/Nmnat chimeric gene

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Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase

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Quercetin increases brain and muscle mitochondrial biogenesis and exercise tolerance

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MicroRNA 217 Modulates Endothelial Cell Senescence via Silent Information Regulator 1

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Regulation of Succinate Dehydrogenase Activity by SIRT3 in Mammalian Mitochondria

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Regulation of Hypoxia-Inducible Factor 2α Signaling by the Stress-Responsive Deacetylase Sirtuin 1

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Sirtuin 1 Reduction Parallels the Accumulation of Tau in Alzheimer Disease

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Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage

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Sirt1 contributes critically to the redox-dependent fate of neural progenitors

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Can autophagy promote longevity?

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Regulation of Insulin Secretion by SIRT4, a Mitochondrial ADP-ribosyltransferase

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Atomic structure and chemistry of human serum albumin

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Mammalian Abasic Site Base Excision Repair

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Composition and dynamics of human mitochondrial nucleoids.

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Molecular Mechanisms of Prion Pathogenesis

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Mitochondrial and apoptotic neuronal death signaling pathways in cerebral ischemia

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Repeat motifs of tau bind to the insides of microtubules in the absence of taxol

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A local mechanism mediates NAD-dependent protection of axon degeneration

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Identification of a small molecule inhibitor of Sir2p

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SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

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Resveratrol as a Therapeutic Agent for Neurodegenerative Diseases

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SirT1 inhibition reduces IGF-I/IRS-2/Ras/ERK1/2 signaling and protects neurons

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MicroRNA-34a induces endothelial progenitor cell senescence and impedes its angiogenesis via suppressing silent information regulator 1

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Caloric restriction attenuates Aβ-deposition in Alzheimer transgenic models

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Optimal Depth and Duration of Mild Hypothermia in a Focal Model of Transient Cerebral Ischemia

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SIRT1-dependent regulation of chromatin and transcription: Linking NAD+ metabolism and signaling to the control of cellular functions

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Brain SIRT1: Anatomical Distribution and Regulation by Energy Availability

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SIRT1 Promotes Cell Survival under Stress by Deacetylation-Dependent Deactivation of Poly(ADP-Ribose) Polymerase 1

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DYRK2 Is Targeted to the Nucleus and Controls p53 via Ser46 Phosphorylation in the Apoptotic Response to DNA Damage

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SIRT1 Promotes Proliferation and Prevents Senescence Through Targeting LKB1 in Primary Porcine Aortic Endothelial Cells

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Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic Tau mutant

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Chemistry of Gene Silencing: The Mechanism of NAD+-Dependent Deacetylation Reactions

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SIRT1 is a redox‐sensitive deacetylase that is post‐translationally modified by oxidants and carbonyl stress

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PGC-1α and PGC-1Β Regulate Mitochondrial Density in Neurons

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Post-ischemic inflammation: molecular mechanisms and therapeutic implications

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Nicotinamide phosphoribosyltransferase protects against ischemic stroke through SIRT1‐dependent adenosine monophosphate–activated kinase pathway

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Phosphorylation Regulates SIRT1 Function

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Neuroprotection by Hypoxic Preconditioning Requires Sequential Activation of Vascular Endothelial Growth Factor Receptor and Akt

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Histone deacetylase SIRT1 modulates neuronal differentiation by its nuclear translocation

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PPAR: a new pharmacological target for neuroprotection in stroke and neurodegenerative diseases

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SIRT1 Regulates the Function of the Nijmegen Breakage Syndrome Protein

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Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington’s disease

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JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity

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NAD + as a metabolic link between DNA damage and cell death

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Sirtuin 2, a Mammalian Homolog of Yeast Silent Information Regulator-2 Longevity Regulator, Is an Oligodendroglial Protein That Decelerates Cell Differentiation through Deacetylating α-Tubulin

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The SIRT1 activator resveratrol protects SK‐N‐BE cells from oxidative stress and against toxicity caused by α‐synuclein or amyloid‐β (1‐42) peptide

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Nicotinamide Prevents NAD+ Depletion and Protects Neurons Against Excitotoxicity and Cerebral Ischemia: NAD+ Consumption by SIRT1 may Endanger Energetically Compromised Neurons

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Suppressing Cancer: The Importance of Being Senescent

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Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product

Tanny, J. C., & Moazed, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.415 · Cited by 253

DYRK1A and DYRK3 Promote Cell Survival through Phosphorylation and Activation of SIRT1

Guo, X., Williams, J. G., Schug, T. T., & Li, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102574 · Cited by 251

A Ufd2/D4Cole1e chimeric protein and overexpression of Rbp7 in the slow Wallerian degeneration ( Wld S ) mouse

Conforti, L., Tarlton, A., Mack, T. G. A., Mi, W., Buckmaster, E. A., Wagner, D., Perry, V. H., & Coleman, M. P. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.21.11377 · Cited by 251

Mechanism of Nicotinamide Inhibition and Transglycosidation by Sir2 Histone/Protein Deacetylases

Jackson, M. D., Schmidt, M. T., Oppenheimer, N. J., & Denu, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306552200 · Cited by 240

miRNAs regulate SIRT1 expression during mouse embryonic stem cell differentiation and in adult mouse tissues

Saunders, L. R., Sharma, A., Tawney, J., Nakagawa, M., Okita, K., Yamanaka, S., Willenbring, H., & Verdin, E. M. (2010) · Aging · doi:10.18632/aging.100176 · Cited by 240

Resveratrol Mimics Ischemic Preconditioning in the Brain

Raval, A. P., Dave, K. R., & Pérez‐Pinzón, M. A. (2006) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600262 · Cited by 239

SIRT1 promotes the central adaptive response to diet restriction through activation of the dorsomedial and lateral nuclei of the hypothalamus

Satoh, A., Brace, C. S., Ben-Josef, G., West, T., Wozniak, D. F., Holtzman, D. M., Herzog, E. D., & Imai, S.-I. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1385-10.2010 · Cited by 237

Enzymes in the NAD+ Salvage Pathway Regulate SIRT1 Activity at Target Gene Promoters

Zhang, T., Berrocal, J. G., Frizzell, K. M., Gamble, M. J., DuMond, M. E., Krishnakumar, R., Yang, T., Sauve, A. A., & Kraus, W. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016469 · Cited by 234

PCAF Modulates PTEN Activity

Okumura, K., Mendoza, M. C., Bachoo, R. M., DePinho, R. A., Cavenee, W. K., & Furnari, F. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605391200 · Cited by 232

MicroRNA 132 Regulates Nutritional Stress-Induced Chemokine Production through Repression of SirT1

Strum, J. C., Johnson, J. H., Ward, J. M., Xie, H., Feild, J. A., Hester, A. G., Alford, A., & Waters, K. M. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0117 · Cited by 229

Agrp Neurons Mediate Sirt1's Action on the Melanocortin System and Energy Balance: Roles for Sirt1 in Neuronal Firing and Synaptic Plasticity

Dietrich, M. O., Antunes, C., Geliang, G., Liu, Z.-W., Borók, E., Nie, Y., Xu, A. W., Souza, D. O., Gao, Q., Diano, S., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2234-10.2010 · Cited by 229

A tale of two mitochondrial channels, MAC and PTP, in apoptosis

Kinnally, K. W., & Antonsson, B. E. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0722-z · Cited by 227

SIRT1 Regulates UV-Induced DNA Repair through Deacetylating XPA

Fan, W., & Luo, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.006 · Cited by 223

FoxO1 Mediates an Autofeedback Loop Regulating SIRT1 Expression

Xiong, S., Salazar, G., Patrushev, N. A., & Alexander, R. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163667 · Cited by 221

Peroxisome Proliferator-Activated Receptor-α Activation as a Mechanism of Preventive Neuroprotection Induced by Chronic Fenofibrate Treatment

Deplanque, D., Gelé, P., Pétrault, O., Six, I., Furman, C., Bouly, M., Nion, S., Dupuis, B., Leys, D., Fruchart, J., et al. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-15-06264.2003 · Cited by 219

SIRT1 is regulated by a PPARγ–SIRT1 negative feedback loop associated with senescence

Han, L., Zhou, R., Niu, J., McNutt, M. A., Wang, P., & Tong, T. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq609 · Cited by 218

Neuroprotective Effects of Adenosine Monophosphate- Activated Protein Kinase Inhibition and Gene Deletion in Stroke

Li, J., Zeng, Z., Viollet, B., Ronnett, G. V., & McCullough, L. D. (2007) · Stroke · doi:10.1161/strokeaha.107.490904 · Cited by 216

SIRT1 Activation by Small Molecules

Dai, H., Kustigian, L. M., Carney, D. P., Case, A. W., Considine, T., Hubbard, B. P., Perni, R. B., Riera, T. V., Szczepankiewicz, B. G., Vlasuk, G. P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.133892 · Cited by 215

MNB/DYRK1A as a multiple regulator of neuronal development

Tejedor, F. J., & Hämmerle, B. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07954.x · Cited by 214

Sir2 Regulation by Nicotinamide Results from Switching between Base Exchange and Deacetylation Chemistry

Sauve, A. A., & Schramm, V. L. (2003) · Biochemistry · doi:10.1021/bi034959l · Cited by 213

Sirt1 and the Mitochondria

Luen Tang, B. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2318 · Cited by 740

SIRT1 and SIRT2: emerging targets in neurodegeneration

Dönmez, G., & Outeiro, T. F. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302451 · Cited by 419

Role of NAD+ in regulating cellular and metabolic signaling pathways

Amjad, S., Nisar, S., Bhat, A. A., Shah, A. R., Frenneaux, M. P., Fakhro, K. A., Haris, M., Reddy, R. D., Patay, Z. J., Baur, J. A., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101195 · Cited by 413

Mitochondrial function in hypoxic ischemic injury and influence of aging

Ham, P. B., & Raju, R. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.006 · Cited by 374

SIRT1 Deficiency in Microglia Contributes to Cognitive Decline in Aging and Neurodegeneration via Epigenetic Regulation of IL-1β

Cho, S.-H., Chen, J. A., Sayed, F., Ward, M. E., Gao, F., Nguyen, T. A., Krabbe, G., Sohn, P. D., Lo, I., Minami, S., et al. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.2939-14.2015 · Cited by 275

Sirtuins in neurodegenerative diseases

Sachan, N., Ali, Z., Fatma, N., & Chandra, P. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-45380-9.00002-x

Neuronal protection by sirtuins in Alzheimer's disease

Anekonda, T. S., & Reddy, P. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03492.x · Cited by 152

Targeting sirtuins in neurological disorders: A comprehensive review

Zhang, S.-Y., Yang, N., Hao, P.-H., Wen, R., & Zhang, T. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.139258 · Cited by 20

Sirtuins in Neuroendocrine Regulation and Neurological Diseases

Fujita, Y., & Yamashita, T. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00778 · Cited by 110

Sirtuins in neurodegenerative diseases: an update on potential mechanisms

Min, S., Sohn, P., Cho, S.-H., Swanson, R. A., & Gan, L. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00053 · Cited by 124