Reference health

Sirtuins as regulators of metabolism and healthspan

1 of 158 checkable references need attention · checked 2026-09-03

At the dated check, the references listed below either did not resolve in Crossref or DataCite, or carried a retraction notice. Each one is shown with the registry record that put it there.

References needing attention

marked retracted — notice via Crossref, record curated by Retraction Watch10.1073/pnas.0610590104

RETRACTED: Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex

The 157 checked references that resolve

resolves10.1038/nrm3025

mTOR: from growth signal integration to cancer, diabetes and ageing

resolves10.1007/s00018-010-0454-z

AMP-activated protein kinase and its downstream transcriptional pathways

resolves10.1016/j.cell.2010.06.029

Metabolic Networks of Longevity

resolves10.1126/science.1172539

Extending Healthy Life Span—From Yeast to Humans

resolves10.1146/annurev.pathol.4.110807.092250

Mammalian Sirtuins: Biological Insights and Disease Relevance

resolves10.1056/NEJMra1100831

Sirtuins, Aging, and Medicine

resolves10.1101/gad.13.19.2570

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

resolves10.1038/35001622

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

resolves10.1038/nature01960

Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

resolves10.1006/bbrc.2000.3000

Phylogenetic Classification of Prokaryotic and Eukaryotic Sir2-like Proteins

resolves10.1074/jbc.M609554200

Nucleocytoplasmic Shuttling of the NAD+-dependent Histone Deacetylase SIRT1

resolves10.1101/gad.1412706

SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis

resolves10.1016/j.bbapap.2009.12.021

Mitochondrial sirtuins

resolves10.1016/j.cell.2005.11.044

Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6

resolves10.1101/gad.1399706

Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription

resolves10.1128/MCB.16.8.4349

Efficient Transcriptional Silencing in <i>Saccharomyces cerevisiae</i> Requires a Heterochromatin Histone Acetylation Pattern

resolves10.1016/j.cell.2006.06.057

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

resolves10.1074/jbc.M413296200

Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase

resolves10.1038/nature06736

SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin

resolves10.1016/j.cell.2009.12.041

The Histone Deacetylase Sirt6 Regulates Glucose Homeostasis via Hif1α

resolves10.1016/j.cell.2009.02.026

SIRT5 Deacetylates Carbamoyl Phosphate Synthetase 1 and Regulates the Urea Cycle

resolves10.1074/mcp.M111.012658

The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme

resolves10.1126/science.1207861

Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

resolves10.1210/er.2009-0026

The Secret Life of NAD+: An Old Metabolite Controlling New Metabolic Signaling Pathways

resolves10.1074/jbc.M205670200

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

resolves10.1038/nature01578

Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae

resolves10.1038/nsmb956

Splicing regulates NAD metabolite binding to histone macroH2A

resolves10.1016/j.cell.2005.03.035

Assembly of the SIR Complex and Its Regulation by O-Acetyl-ADP-Ribose, a Product of NAD-Dependent Histone Deacetylation

resolves10.1016/j.bbapap.2010.02.007

Function and metabolism of sirtuin metabolite O-acetyl-ADP-ribose

resolves10.1016/j.ceb.2008.03.012

Transcriptional targets of sirtuins in the coordination of mammalian physiology

resolves10.1124/pr.110.003905

Targeting Sirtuin 1 to Improve Metabolism: All You Need Is NAD+?

resolves10.1016/S0092-8674(01)00527-X

hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

resolves10.1016/S0092-8674(01)00524-4

Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

resolves10.1038/nrc2962

SIRT1: recent lessons from mouse models

resolves10.1016/j.cmet.2006.04.013

GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1α

resolves10.1038/nature03354

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

resolves10.1038/srep00070

SRT1720 improves survival and healthspan of obese mice

resolves10.1016/j.cmet.2010.02.006

Interdependence of AMPK and SIRT1 for Metabolic Adaptation to Fasting and Exercise in Skeletal Muscle

resolves10.1038/nature07813

AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

resolves10.1016/j.cmet.2008.08.017

Specific SIRT1 Activation Mimics Low Energy Levels and Protects against Diet-Induced Metabolic Disorders by Enhancing Fat Oxidation

resolves10.1016/j.cell.2006.11.013

Resveratrol Improves Mitochondrial Function and Protects against Metabolic Disease by Activating SIRT1 and PGC-1α

resolves10.1038/nature05354

Resveratrol improves health and survival of mice on a high-calorie diet

resolves10.1126/science.1094637

Stress-Dependent Regulation of FOXO Transcription Factors by the SIRT1 Deacetylase

resolves10.1016/S0092-8674(04)00126-6

Mammalian SIRT1 Represses Forkhead Transcription Factors

resolves10.1074/jbc.M401138200

FOXO4 Is Acetylated upon Peroxide Stress and Deacetylated by the Longevity Protein hSir2

resolves10.1016/j.cmet.2011.05.004

Fine Tuning Our Cellular Factories: Sirtuins in Mitochondrial Biology

resolves10.1016/j.tibs.2010.07.003

Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling

resolves10.1128/MCB.01636-07

Mammalian Sir2 Homolog SIRT3 Regulates Global Mitochondrial Lysine Acetylation

resolves10.1038/nature08778

SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation

resolves10.1016/j.molcel.2011.07.019

SIRT3 Deficiency and Mitochondrial Protein Hyperacetylation Accelerate the Development of the Metabolic Syndrome

resolves10.1016/j.cmet.2010.11.003

SIRT3 Deacetylates Mitochondrial 3-Hydroxy-3-Methylglutaryl CoA Synthase 2 and Regulates Ketone Body Production

resolves10.1016/j.cell.2010.10.002

Sirt3 Mediates Reduction of Oxidative Damage and Prevention of Age-Related Hearing Loss under Caloric Restriction

resolves10.1073/pnas.0803790105

A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis

resolves10.1371/journal.pone.0023295

Succinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity

resolves10.1073/pnas.1111308108

Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production

resolves10.1016/j.cmet.2010.11.015

Calorie Restriction Reduces Oxidative Stress by SIRT3-Mediated SOD2 Activation

resolves10.1016/j.jmb.2008.07.048

Substrates and Regulation Mechanisms for the Human Mitochondrial Sirtuins Sirt3 and Sirt5

resolves10.1016/S1097-2765(03)00038-8

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

resolves10.1073/pnas.1104969108

Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling

resolves10.1016/j.molcel.2011.04.028

Acetylation Regulates Gluconeogenesis by Promoting PEPCK1 Degradation via Recruiting the UBR5 Ubiquitin Ligase

resolves10.1016/j.cmet.2007.07.003

SIRT2 Regulates Adipocyte Differentiation through FoxO1 Acetylation/Deacetylation

resolves10.1074/jbc.M110.124164

SIRT4 Regulates Fatty Acid Oxidation and Mitochondrial Gene Expression in Liver and Muscle Cells

resolves10.1073/pnas.1016306107

Neural sirtuin 6 (Sirt6) ablation attenuates somatic growth and causes obesity

resolves10.1161/CIRCRESAHA.107.164558

Sirt7 Increases Stress Resistance of Cardiomyocytes and Prevents Apoptosis and Inflammatory Cardiomyopathy in Mice

resolves10.1126/science.1101731

Nutrient Availability Regulates SIRT1 Through a Forkhead-Dependent Pathway

resolves10.1073/pnas.0808207105

The genetic ablation of SRC-3 protects against obesity and improves insulin sensitivity by reducing the acetylation of PGC-1α

resolves10.1038/embor.2011.151

CREB and ChREBP oppositely regulate SIRT1 expression in response to energy availability

resolves10.1007/s11010-010-0391-z

Fasting promotes the expression of SIRT1, an NAD+-dependent protein deacetylase, via activation of PPARα in mice

resolves10.1093/nar/gkq609

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

resolves10.1507/endocrj.K10E-004

PPAR.BETA./.DELTA. regulates the human SIRT1 gene transcription via Sp1

resolves10.1016/j.cell.2005.08.011

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

resolves10.1016/j.cmet.2011.03.013

PARP-2 Regulates SIRT1 Expression and Whole-Body Energy Expenditure

resolves10.1073/pnas.0801613105

miR-34a repression of SIRT1 regulates apoptosis

resolves10.1074/jbc.M109.094524

A Pathway Involving Farnesoid X Receptor and Small Heterodimer Partner Positively Regulates Hepatic Sirtuin 1 Levels via MicroRNA-34a Inhibition

resolves10.1161/CIRCRESAHA.108.193102

Downregulation of MiR-199a Derepresses Hypoxia-Inducible Factor-1α and Sirtuin 1 and Recapitulates Hypoxia Preconditioning in Cardiac Myocytes

resolves10.1074/jbc.M110.202390

Peroxisome Proliferator-activated Receptor-γ Coactivator-1α Controls Transcription of the Sirt3 Gene, an Essential Component of the Thermogenic Brown Adipocyte Phenotype

resolves10.1371/journal.pone.0004020

Phosphorylation Regulates SIRT1 Function

resolves10.1371/journal.pone.0008414

JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity

resolves10.1074/jbc.M110.102574

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

resolves10.1038/ncb1645

SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress

resolves10.1016/j.cmet.2011.03.004

PARP-1 Inhibition Increases Mitochondrial Metabolism through SIRT1 Activation

resolves10.1016/j.molcel.2007.08.030

Active Regulator of SIRT1 Cooperates with SIRT1 and Facilitates Suppression of p53 Activity

resolves10.1038/nature02583

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

resolves10.1038/nature06500

DBC1 is a negative regulator of SIRT1

resolves10.1038/nature06515

Negative regulation of the deacetylase SIRT1 by DBC1

resolves10.1172/JCI39319

Deleted in breast cancer–1 regulates SIRT1 activity and contributes to high-fat diet–induced liver steatosis in mice

resolves10.1016/j.molcel.2011.04.020

A SIRT1-LSD1 Corepressor Complex Regulates Notch Target Gene Expression and Development

resolves10.1101/gad.1650608

Tissue-specific regulation of SIRT1 by calorie restriction

resolves10.1021/pr100892r

Metabolomic Analysis of Livers and Serum from High-Fat Diet Induced Obese Mice

resolves10.1016/S0021-9258(19)45675-5

The Management of Nicotinamide and Nicotinic Acid in the Mouse

resolves10.1016/S0092-8674(04)00416-7

Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans

resolves10.1016/j.cmet.2011.08.014

Nicotinamide Mononucleotide, a Key NAD+ Intermediate, Treats the Pathophysiology of Diet- and Age-Induced Diabetes in Mice

resolves10.1038/nrm1963

Poly(ADP-ribose): novel functions for an old molecule

resolves10.1016/j.molcel.2010.06.017

The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets

resolves10.1096/fj.07-8290com

The enzyme CD38 (a NAD glycohydrolase, EC 3.2.2.5) is necessary for the development of diet‐induced obesity

resolves10.1039/c0ob00768d

Design, synthesis and biological characterization of novel inhibitors of CD38

resolves10.1038/nrd2665

Sirtuins — novel therapeutic targets to treat age-associated diseases

resolves10.1016/j.cmet.2008.06.011

Resveratrol Delays Age-Related Deterioration and Mimics Transcriptional Aspects of Dietary Restriction without Extending Life Span

resolves10.1016/j.cmet.2011.10.002

Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans

resolves10.1038/nature06261

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

resolves10.1074/jbc.M109.088682

SRT1720, SRT2183, SRT1460, and Resveratrol Are Not Direct Activators of SIRT1

resolves10.1111/j.1747-0285.2009.00901.x

Resveratrol is Not a Direct Activator of SIRT1 Enzyme Activity

resolves10.2337/db09-0482

AMP-Activated Protein Kinase–Deficient Mice Are Resistant to the Metabolic Effects of Resveratrol

resolves10.1016/j.cmet.2010.04.001

Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation

resolves10.1038/sj.bjp.0703397

Inhibition of mitochondrial proton F0F1‐ATPase/ATP synthase by polyphenolic phytochemicals

resolves10.1210/er.2003-0026

The Cellular Fate of Glucose and Its Relevance in Type 2 Diabetes

resolves10.1038/nature07349

A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange

resolves10.1074/jbc.M412357200

Nuclear Trapping of the Forkhead Transcription Factor FoxO1 via Sirt-dependent Deacetylation Promotes Expression of Glucogenetic Genes

resolves10.1210/me.2003-0384

Peroxisome Proliferator-Activated Receptor γ Coactivator-1α, as a Transcription Amplifier, Is Not Essential for Basal and Hormone-Induced Phosphoenolpyruvate Carboxykinase Gene Expression

resolves10.1111/j.1474-9726.2007.00335.x

SIRT1 transgenic mice show phenotypes resembling calorie restriction

resolves10.2337/db09-1191

SIRT1 mRNA Expression May Be Associated With Energy Expenditure and Insulin Sensitivity

resolves10.1172/JCI46243

Hepatic Sirt1 deficiency in mice impairs mTorc2/Akt signaling and results in hyperglycemia, oxidative damage, and insulin resistance

resolves10.1016/j.cmet.2009.02.006

Hepatocyte-Specific Deletion of SIRT1 Alters Fatty Acid Metabolism and Results in Hepatic Steatosis and Inflammation

resolves10.1073/pnas.0702509104

Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1

resolves10.1016/j.cmet.2006.02.002

HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia

resolves10.1016/j.molcel.2010.05.023

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

resolves10.1016/j.ccr.2011.02.014

SIRT3 Opposes Reprogramming of Cancer Cell Metabolism through HIF1α Destabilization

resolves10.1038/nrm2327

Molecular and metabolic mechanisms of insulin resistance and β-cell failure in type 2 diabetes

resolves10.1016/j.cmet.2005.07.001

Increased dosage of mammalian Sir2 in pancreatic β cells enhances glucose-stimulated insulin secretion in mice

resolves10.1371/journal.pbio.0040031

Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells

resolves10.1074/jbc.M705488200

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

resolves10.3109/07853890.2010.547211

Sirtuin 1 in lipid metabolism and obesity

resolves10.3109/10409231003667500

Genetic control of <i>de novo</i> lipogenesis: role in diet-induced obesity

resolves10.1172/JCI0215593

SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver

resolves10.1016/j.molcel.2007.07.032

SIRT1 Deacetylates and Positively Regulates the Nuclear Receptor LXR

resolves10.1074/jbc.M110.122978

SIRT1 Deacetylates and Inhibits SREBP-1C Activity in Regulation of Hepatic Lipid Metabolism*

resolves10.1101/gad.1901210

Conserved role of SIRT1 orthologs in fasting-dependent inhibition of the lipid/cholesterol regulator SREBP

resolves10.1073/pnas.0802917105

Sirt1 protects against high-fat diet-induced metabolic damage

resolves10.7150/ijbs.6.682

Liver Steatosis and Increased ChREBP Expression in Mice Carrying a Liver Specific SIRT1 Null Mutation under a Normal Feeding Condition

resolves10.1016/j.cmet.2010.06.009

Hepatic-Specific Disruption of SIRT6 in Mice Results in Fatty Liver Formation Due to Enhanced Glycolysis and Triglyceride Synthesis

resolves10.1002/jcp.21386

The secretory function of adipocytes in the physiology of white adipose tissue

resolves10.1016/j.bbalip.2007.03.006

PPARγ in human and mouse physiology

resolves10.1091/mbc.e08-06-0647

SIRT2 Suppresses Adipocyte Differentiation by Deacetylating FOXO1 and Enhancing FOXO1's Repressive Interaction with PPARγ

resolves10.1111/j.1467-789X.2009.00642.x

Regulatory enzymes of mitochondrial β‐oxidation as targets for treatment of the metabolic syndrome

resolves10.1210/en.2009-1013

Lack of SIRT1 (Mammalian Sirtuin 1) Activity Leads to Liver Steatosis in the SIRT1+/− Mice: A Role of Lipid Mobilization and Inflammation

resolves10.1096/fj.10-173492

Hepatic overexpression of SIRT1 in mice attenuates endoplasmic reticulum stress and insulin resistance in the liver

resolves10.1152/ajpgi.90358.2008

Resveratrol alleviates alcoholic fatty liver in mice

resolves10.1152/ajpendo.90997.2008

Treatment with SRT1720, a SIRT1 activator, ameliorates fatty liver with reduced expression of lipogenic enzymes in MSG mice

resolves10.1016/j.cell.2011.10.017

NCoR1 Is a Conserved Physiological Modulator of Muscle Mass and Oxidative Function

resolves10.1210/er.2006-0037

Peroxisome Proliferator-Activated Receptor γ Coactivator 1 Coactivators, Energy Homeostasis, and Metabolism

resolves10.3945/ajcn.110.001917

Regulation of PGC-1α, a nodal regulator of mitochondrial biogenesis

resolves10.1073/pnas.0705070104

AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α

resolves10.1152/ajpregu.00409.2004

Effects of aging on cardiac and skeletal muscle AMPK activity: basal activity, allosteric activation, and response to in vivo hypoxemia in mice

resolves10.1172/JCI58554

Sirt1 enhances skeletal muscle insulin sensitivity in mice during caloric restriction

resolves10.18632/aging.100075

Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle

resolves10.1074/jbc.M111.261685

Sirtuin 1 (SIRT1) Deacetylase Activity Is Not Required for Mitochondrial Biogenesis or Peroxisome Proliferator-activated Receptor-γ Coactivator-1α (PGC-1α) Deacetylation following Endurance Exercise

resolves10.1097/MOL.0b013e328328d0a4

PGC-1α, SIRT1 and AMPK, an energy sensing network that controls energy expenditure

resolves10.1038/35065638

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

resolves10.1073/pnas.0404184101

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

resolves10.1016/j.mad.2007.07.007

Effects of resveratrol on lifespan in Drosophila melanogaster and Caenorhabditis elegans

resolves10.1016/j.arr.2007.04.001

Sir2 and calorie restriction in yeast: A skeptical perspective

resolves10.1038/nature10296

Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila

resolves10.1038/nature10440

Regulation of Caenorhabditis elegans lifespan by sir-2.1 transgenes

resolves10.1016/j.cmet.2008.05.004

SirT1 Inhibition Reduces IGF-I/IRS-2/Ras/ERK1/2 Signaling and Protects Neurons

resolves10.1038/ncomms1001

Sirt1 improves healthy ageing and protects from metabolic syndrome-associated cancer

resolves10.1016/j.exger.2005.09.008

Sirtuin 1 (SIRT1) sequence variation is not associated with exceptional human longevity

resolves10.1093/hmg/ddr089

Exposure to resveratrol triggers pharmacological correction of fatty acid utilization in human fatty acid oxidation-deficient fibroblasts

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