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

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

Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290

Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1

Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139

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

Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057

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

Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864

Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796

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

Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510

A central role for JNK in obesity and insulin resistance

Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359

Activation of β2 adrenergic receptor signaling modulates inflammation: a target limiting the progression of kidney diseases

Dorotea, D., & Ha, H. (2020) · Archives of Pharmacal Research · doi:10.1007/s12272-020-01280-9 · Cited by 27

Integrative metabolomics as emerging tool to study autophagy regulation

Stryeck, S., Birner‐Gruenberger, R., & Madl, T. (2017) · Microbial Cell · doi:10.15698/mic2017.08.584 · Cited by 28

Dual-edged role of SIRT1 in energy metabolism and cardiovascular disease

Zhou, R., Barnes, K., Gibson, S., & Fillmore, N. (2024) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00001.2024 · Cited by 29

Hyperglycemia-Induced Endothelial Dysfunction

Gerő, D. (2018) · InTech eBooks · doi:10.5772/intechopen.71433 · Cited by 33

The Effect of Alcohol on Sirt1 Expression and Function in Animal and Human Models of Hepatocellular Carcinoma (HCC)

Thompson, K. J., Humphries, J. R., Niemeyer, D. J., Sindram, D., & McKillop, I. H. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-09614-8_21 · Cited by 26

Sirtuin dysregulation in Parkinson's disease: Implications of acetylation and deacetylation processes

Dhiman, S., Mannan, A., Taneja, A., Mohan, M., & Singh, T. G. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122537 · Cited by 25

Cyanidin-3-glucoside enhances mitochondrial function and biogenesis in a human hepatocyte cell line

Mogalli, R., Matsukawa, T., Shimomura, O., Isoda, H., & Ohkohchi, N. (2018) · Cytotechnology · doi:10.1007/s10616-018-0242-4 · Cited by 24

Sirt1: An Increasingly Interesting Molecule with a Potential Role in Bone Metabolism and Osteoporosis

Chen, Y., Xiao, H., Liu, Z., Teng, F., Yang, A., Geng, B., Sheng, X., & Xia, Y. (2024) · Biomolecules · doi:10.3390/biom14080970 · Cited by 29

FK866 compromises mitochondrial metabolism and adaptive stress responses in cultured cardiomyocytes

Oyarzún, A. P., Westermeier, F., Pennanen, C., López‐Crisosto, C., Parra, V., Sotomayor-Flores, C., Sánchez, G., Pedrozo, Z., Troncoso, R., & Lavandero, S. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.08.097 · Cited by 24

Nicotinamide ameliorates energy deficiency and improves retinal function in Cav‐1‐/‐ mice

Tang, Y., Fang, W., Xiao, Z., Song, M., Zhuang, D., Han, B., Wu, J., & Sun, X. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15266 · Cited by 24

Emerging Role of Nicotinamide Riboside in Health and Diseases

Sharma, C., Donu, D., & Cen, Y. (2022) · Nutrients · doi:10.3390/nu14193889 · Cited by 24

SIRT1: An Intermediator of Key Pathways Regulating Pulmonary Diseases

Jiang, Y.-Z., Huang, X.-R., Chang, J., Zhou, Y., & Huang, X.-T. (2024) · Laboratory Investigation · doi:10.1016/j.labinv.2024.102044 · Cited by 24

Silent information regulator 1 modulator resveratrol increases brain lactate production and inhibits mitochondrial metabolism, whereas SRT1720 increases oxidative metabolism

Rowlands, B. D., Lau, C. L., Ryall, J. G., Thomas, D. S., Klugmann, M., Beart, P. M., & Rae, C. D. (2015) · Journal of Neuroscience Research · doi:10.1002/jnr.23570 · Cited by 24

The effects of nicotinamide adenine dinucleotide in cardiovascular diseases: Molecular mechanisms, roles and therapeutic potential

Zhang, X., Zhang, Y., Sun, A., & Ge, J. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.04.001 · Cited by 24

An acetylation rheostat for the control of muscle energy homeostasis

Menzies, K. J., & Auwerx, J. H. (2013) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0140 · Cited by 23

NAMPT-Mediated NAD Biosynthesis as the Internal Timing Mechanism: In NAD+ World, Time Is Running in Its Own Way

Poljšak, B. (2017) · Rejuvenation Research · doi:10.1089/rej.2017.1975 · Cited by 24

Development of Aldose Reductase Inhibitors for the Treatment of Inflammatory Disorders and Cancer: Current Drug Design Strategies and Future Directions

Sonowal, H., & Ramana, K. V. (2020) · Current Medicinal Chemistry · doi:10.2174/0929867327666201027152737 · Cited by 23

Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation

Bi, X., Ye, Q., Li, D., Peng, Q., Wang, Z., Wu, X. B., Zhang, Y., Zhang, Q., & Jiang, F. (2019) · Aging Cell · doi:10.1111/acel.12900 · Cited by 23

Mitochondrial NAD(P)H In vivo: Identifying Natural Indicators of Oxidative Phosphorylation in the 31P Magnetic Resonance Spectrum

Conley, K. E., Ali, A. S., Flores, B., Jubrias, S. A., & Shankland, E. G. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00045 · Cited by 22

Repeated resveratrol treatment attenuates methamphetamine-induced hyperactivity and [3H]dopamine overflow in rodents

Miller, D. K., Oelrichs, C. E., Sage, A. S., Sun, G. Y., & Simonyi, Á. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.08.051 · Cited by 22

Acute effects of resveratrol to enhance cocaine-induced dopamine neurotransmission in the striatum

Shuto, T., Kuroiwa, M., Koga, Y., Kawahara, Y., Sotogaku, N., Toyomasu, K., & Nishi, A. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.02.050 · Cited by 22

Temporal overexpression of SIRT1 in skeletal muscle of adult mice does not improve insulin sensitivity or markers of mitochondrial biogenesis

Svensson, K., LaBarge, S. A., Martins, V. F., & Schenk, S. (2017) · Acta Physiologica · doi:10.1111/apha.12897 · Cited by 22

Metabolic responses induced by DNA damage and poly (ADP-ribose) polymerase (PARP) inhibition in MCF-7 cells

Bhute, V. J., & Palecek, S. P. (2015) · Metabolomics · doi:10.1007/s11306-015-0831-6 · Cited by 21

LPG 18:0 is a general biomarker of asthma and inhibits the differentiation and function of regulatory T-cells

Aili, A., Wang, Y., Shang, Y., Zhang, L., Liu, H., Li, Z., Xue, L., Chen, Y., Sun, Y., Zhang, X., et al. (2024) · European Respiratory Journal · doi:10.1183/13993003.01752-2023 · Cited by 20

Resveratrol and its oligomers: modulation of sphingolipid metabolism and signaling in disease

Lim, K. G., Gray, A. I., Anthony, N. G., Mackay, S. P., Pyne, S., & Pyne, N. J. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1386-4 · Cited by 20

A novel role of SIRT1 in gammaherpesvirus latency and replication

He, M., & Gao, S. (2014) · Cell Cycle · doi:10.4161/15384101.2014.968431 · Cited by 19

Biochemical and Mutational Analysis of a Novel Nicotinamidase from Oceanobacillus iheyensis HTE831

Sánchez-Carrón, G., García-García, M. I., Perez, R. Z., Takami, H., García‐Carmona, F., & Sánchez‐Ferrer, Á. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056727 · Cited by 19

Role of alcohol in the development and progression of hepatocellular carcinoma

McKillop, I. H., Schrum, L. W., & Thompson, K. J. (2015) · Hepatic Oncology · doi:10.2217/hep.15.40 · Cited by 18

Sirtuins-Mediators of Maternal Obesity-Induced Complications in Offspring?

Nguyen, L. T., Chen, H., Pollock, C. A., & Saad, S. (2016) · The FASEB Journal · doi:10.1096/fj.15-280743 · Cited by 19

Intrathecal Injection of SIRT1-modified Human Mesenchymal Stem Cells Alleviates Neuropathic Pain in Rat

Tian, J., Song, T., Wang, H., Wang, W., Zhang, Z., Yan, R., Ma, X., & Hu, Y. H. (2020) · Journal of Molecular Neuroscience · doi:10.1007/s12031-020-01717-2 · Cited by 18

Contemporary perspective and management of testosterone deficiency: Modifiable factors and variable management

Hisasue, S. (2015) · International Journal of Urology · doi:10.1111/iju.12880 · Cited by 18

Chronic-Leptin Attenuates Cisplatin Cytotoxicity in MCF-7 Breast Cancer Cell Line

Nadal‐Serrano, M., Sastre‐Serra, J., Valle, A., Roca, P., & Oliver, J. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000374066 · Cited by 18

The Effects of Graded Levels of Calorie Restriction: XIV. Global Metabolomics Screen Reveals Brown Adipose Tissue Changes in Amino Acids, Catecholamines, and Antioxidants After Short-Term Restriction in C57BL/6 Mice

Green, C. L., Mitchell, S. E., Derous, D., Wang, Y., Chen, L., Han, J. J., Promislow, D., Lusseau, D., Douglas, A., & Speakman, J. R. (2019) · The Journals of Gerontology Series A · doi:10.1093/gerona/glz023 · Cited by 18

Development of a dietary‐induced metabolic syndrome model using miniature pigs involvement of AMPK and SIRT 1

Li, S., Liu, C., Chang, C., Chu, H., Chen, K., Mersmann, H. J., Ding, S., Chu, C., & Chen, C. (2014) · European Journal of Clinical Investigation · doi:10.1111/eci.12370 · Cited by 18

The Treatment of Rhodiola Mimics Exercise to Resist High-Fat Diet-Induced Muscle Dysfunction via Sirtuin1-Dependent Mechanisms

You, B., Dun, Y., Fu, S., Qi, D., Zhang, W., Liu, Y., Qiu, L., Xie, M., & Liu, S. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.646489 · Cited by 17

The role of polydatin in inhibiting oxidative stress through SIRT1 activation: A comprehensive review of molecular targets

Liu, K., Liu, J., Xu, A., & Ding, J. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118322 · Cited by 17

A Novel Role for SIRT3 in Regulating Mediators Involved in the Terminal Pathways of Human Labor and Delivery

Lim, R., Barker, G., Menon, R., & Lappas, M. (2016) · Biology of Reproduction · doi:10.1095/biolreprod.116.142372 · Cited by 17

Hsp90 Stabilizes SIRT1 Orthologs in Mammalian Cells and C. elegans

Nguyễn, M. T., Somogyvári, M., & Sőti, C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113661 · Cited by 17

Role of histone deacetylases in bone development and skeletal disorders

Wang, J. S., Yoon, S.-H., & Wein, M. N. (2020) · Bone · doi:10.1016/j.bone.2020.115606 · Cited by 19

Sirt1 promotes tissue regeneration in zebrafish through regulating the mitochondrial unfolded protein response

Lin, Y., Sam, J., & Evans, T. (2021) · iScience · doi:10.1016/j.isci.2021.103118 · Cited by 17

Primary Stress Response Pathways for Preconditioning and Physiological Hormesis

Bhattacharya, S., & Rattan, S. I. S. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-814253-0.00003-6 · Cited by 16

Anergy into T regulatory cells: an integration of metabolic cues and epigenetic changes at the Foxp3 conserved non-coding sequence 2

Morales, M. S., & Mueller, D. L. (2018) · F1000Research · doi:10.12688/f1000research.16551.1 · Cited by 17

Circadian transcription factor NPAS2 and the NAD + ‐dependent deacetylase SIRT1 interact in the mouse nucleus accumbens and regulate reward

Becker‐Krail, D. D., Parekh, P. K., Ketchesin, K. D., Yamaguchi, S., Yoshino, J., Hildebrand, M. A., Dunham, B., Ganapathiraju, M. K., Logan, R. W., & McClung, C. A. (2022) · European Journal of Neuroscience · doi:10.1111/ejn.15596 · Cited by 15

Nutritional Energy Stimulates NAD+ Production to Promote Tankyrase-Mediated PARsylation in Insulinoma Cells

Zhong, L., Yeh, T.-Y. J., Hao, J., Pourtabatabaei, N., Mahata, S. K., Shao, J., Chessler, S. D., & Chi, N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122948 · Cited by 15

NMR Spectroscopy-based Metabolomics of Drosophila Model of Huntington’s Disease Suggests Altered Cell Energetics

Singh, V. P., Sharma, R. K., Athilingam, T., Sinha, P., Sinha, N., & Thakur, A. K. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00491 · Cited by 15

Chemo-enzymatic synthesis of isotopically labeled nicotinamide riboside

Tran, A., Yokose, R., & Cen, Y. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob00552d · Cited by 14

Dietary Restrictions and Cancer Prevention: State of the Art

Caprara, G., Pallavi, R., Sanyal, S., & Pelicci, P. G. (2025) · Nutrients · doi:10.3390/nu17030503 · Cited by 18

A new facet of ADP-ribosylation reactions SIRTs and PARPs interplay

Mennella, M. R. F. (2015) · Frontiers in bioscience · doi:10.2741/4319 · Cited by 14

Shrimp SIRT1 activates of the WSSV IE1 promoter independently of the NF-κB binding site

Kao, Z.-N., Liu, C., Liu, W.-J., Kumar, R., Leu, J., & Wang, H. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.08.034 · Cited by 14

Nicotinamide Riboside for the Prevention and Treatment of Doxorubicin Cardiomyopathy. Opportunities and Prospects

Podyacheva, E., & Toropova, Y. G. (2021) · Nutrients · doi:10.3390/nu13103435 · Cited by 15

(Healthy) Ageing: Focus on Iodothyronines

de Lange, P., Cioffi, F., Silvestri, E., Moreno, M., Goglia, F., & Lanni, A. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140713873 · Cited by 14

Increased serum levels of advanced glycation end products due to induced molting in hen layers trigger a proinflammatory response by peripheral blood leukocytes

Wein, Y., Shira, E. B., & Friedman, A. (2020) · Poultry Science · doi:10.1016/j.psj.2020.04.009 · Cited by 17

Secoiridoid-enriched extra virgin olive oil extracts enhance mitochondrial activity and antioxidant response in colorectal cancer cells: The role of Oleacein and Oleocanthal in PPARγ interaction

Leo, M., Mancini, C., Lori, G., Delre, P., Ferraris, I., Lucchini, F., Molinario, A., Leri, M., Castellaneta, A., Losito, I., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.04.031 · Cited by 13

Overexpression of nicotinamide mononucleotide adenylyltransferase (nmnat) increases the growth rate, Ca2+ concentration and cellulase production in Ganoderma lucidum

Wang, S., Han, J. D. J., Xia, J., Hu, Y., Shi, L., Ren, A., Zhu, J. K., & Zhao, M. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10763-0 · Cited by 13

SIRT1 Regulation—It Ain't All NAD

Chao, L. C., & Tontonoz, P. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.12.017 · Cited by 13

The transcription cofactor CRTC1 protects from aberrant hepatic lipid accumulation

Kim, H. (2016) · Scientific Reports · doi:10.1038/srep37280 · Cited by 13

Sirt7 inhibits Sirt1-mediated activation of Suv39h1

Kumari, P., Popescu, D., Yue, S., Bober, E., Ianni, A., & Braun, T. W. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1486166 · Cited by 13

Advances in mitochondria–nucleus crosstalk in septic cardiomyopathy

Chen, W., Zhao, Z., Geng, Z., Zhang, H., & Fu, X. (2025) · Cell Biology and Toxicology · doi:10.1007/s10565-025-10090-y · Cited by 12

Potential role of sirtuins in livestock production

Ghinis-Hozumi, Y., Antaramián, A., Villarroya, F., Piña, E., & Mora, O. (2012) · animal · doi:10.1017/s1751731112001115 · Cited by 12

Therapeutic potential of nicotinamide adenine dinucleotide for nonalcoholic fatty liver disease

Gual, P., & Postic, C. (2015) · Hepatology · doi:10.1002/hep.28383 · Cited by 12

Effect of nicotinamide supplementation in in vitro fertilization medium on bovine embryo development

Yuan, Y., Mesalam, A., Song, S., Lee, K., Xu, L., Joo, M., & Kong, I. (2020) · Molecular Reproduction and Development · doi:10.1002/mrd.23417 · Cited by 11

Hepatic COX-2 expression protects mice from an alcohol-high fat diet-induced metabolic disorder by involving protein acetylation related energy metabolism

Chen, M., Sun, X., Wei, W., Cucarella, C., Martín‐Sanz, P., Casado, M., Pi, L., Ren, B., & Cao, Q. (2021) · Alcohol · doi:10.1016/j.alcohol.2020.08.007 · Cited by 11

Promising drug discovery strategies for sirtuin modulators: what lessons have we learnt?

Garg, G., Singh, A. K., Singh, S., & Rizvi, S. I. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1915980 · Cited by 11

NMNAT1 Is a Survival Factor in Actinomycin D-Induced Osteosarcoma Cell Death

Kiss, A., Csikos, C., Regdon, Z., Polgár, Z., Virág, L., & Hegedűs, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168869 · Cited by 11

Decreased levels and activity of Sirt1 are modulated by increased miR-34a expression in adipose tissue mononuclear cells from subjects with overweight and obesity: A pilot study

Briones-Espinoza, M., Cortés-García, J. D., Vega‐Cárdenas, M., Uresti‐Rivera, E. E., Gómez-Otero, A., López‐López, N., Mejía-Torres, M., & Portales‐Pérez, D. P. (2020) · Diabetes & Metabolic Syndrome Clinical Research & Reviews · doi:10.1016/j.dsx.2020.07.014 · Cited by 11

Vascular Calcification: Mechanisms, Models, and Therapies

Zhu, W., Yang, S., Chen, Z., Yang, X., Liang, Z., & Chen, Y. (2026) · iNew Medicine · doi:10.1002/inm3.70035 · Cited by 10

Harnessing conserved signaling and metabolic pathways to enhance the maturation of functional engineered tissues

Callaghan, N. I., Durland, L. J., Ireland, R. G., Santerre, J. P., Simmons, C. A., & Huyer, L. D. (2022) · npj Regenerative Medicine · doi:10.1038/s41536-022-00246-3 · Cited by 10

Similarities and Differences of Vascular Calcification in Diabetes and Chronic Kidney Disease

Wang, X., Wang, Z., & He, J. (2024) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s438618 · Cited by 12

Role of SIRT1 in Potentially Toxic Trace Elements (Lead, Fluoride, Aluminum and Cadmium) Associated Neurodevelopmental Toxicity

Fathima, A., Bagang, N., Kumar, N., Dastidar, S. G., & Shenoy, S. (2024) · Biological Trace Element Research · doi:10.1007/s12011-024-04116-5 · Cited by 12

Unlocking the Potential: Caloric Restriction, Caloric Restriction Mimetics, and Their Impact on Cancer Prevention and Treatment

De-Leon-Covarrubias, U. E., Perez‐Trujillo, J. J., Villa‐Cedillo, S. A., Martínez-Pérez, A. G., Montes-de-Oca-Saucedo, C. R., Loera‐Arias, M. D. J., García‐García, A., Cárdenas, O. S., & Montes‐de‐Oca‐Luna, R. (2024) · Metabolites · doi:10.3390/metabo14080418 · Cited by 10

A multifactorial lens on risk factors promoting the progression of Alzheimer’s disease

Parker, J., Moris, J. M., Goodman, L. C., Paidisetty, V. K., Vanegas, V., Turner, H. A., Melgar, D., & Koh, Y. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149262 · Cited by 12

SIRT1 and exercise-induced bone metabolism: a regulatory nexus

Liu, L., Zhang, J., Cui, R., Wang, N., Zhang, Y., Liu, L., Zhang, X., & Liu, Q. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1522821 · Cited by 11

Transient decrease of hepatic NAD+ and amino acid alterations during treatment with valproate: new insights on drug-induced effects in vivo using targeted MS-based metabolomics

Moedas, M. F., van Cruchten, A. G., IJlst, L., Kulik, W., de Almeida, I. T., Diogo, L. M., Wanders, R. J. A., & Silva, M. F. B. (2016) · Metabolomics · doi:10.1007/s11306-016-1091-9 · Cited by 10

Innovations and Emerging Therapies to Combat Renal Cell Damage: NAD + As a Drug Target

Manrique‐Caballero, C. L., Kellum, J. A., Gómez, H., Franco, F., Giacchè, N., & Pellicciari, R. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8066 · Cited by 10

Inherited myogenic abilities in muscle precursor cells defined by the mitochondrial complex I-encoding protein

Motohashi, N., Minegishi, K., & Aoki, Y. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06192-2 · Cited by 10

Melatonin attenuates liver injury in arsenic‐treated rats: The potential role of the Nrf2/HO‐1, apoptosis, and miR‐34a/Sirt1/autophagy pathways

Barangi, S., Mehri, S., Moosavi, Z. B., Yarmohammadi, F., Hayes, A. W., & Karimi, G. (2024) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23635 · Cited by 9

Sirt1 Mitigates Hepatic Lipotoxic Injury Induced by High-Fat-Diet in Fish Through Ire1α Deacetylation

Jin, M., Shen, Y., Monroig, Ó., Zhao, W., Bao, Y., Zhu, T., Tocher, D. R., & Zhou, Q. (2024) · Journal of Nutrition · doi:10.1016/j.tjnut.2024.09.013 · Cited by 9

Activation of nicotinamide phosphoribosyltransferase protects against unilateral renal ischemia-reperfusion injury via the NAD+/SIRT1/PGC-1α signaling pathway and modulation of NFκB/TNF-α/IL-6

Elmorsy, E. A., Khodeir, M. M., Kamal, M. M., El-Sayed, M., Alharbi, M. S., Alsaykhan, H., Hamad, R. S., Abdel‐Reheim, M. A., Eissa, H., Gabr, A. M., et al. (2025) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2025.107302 · Cited by 9

Endothelial LRRC8A delays vascular ageing in natural and accelerated ageing mouse models

Pang, J., Pan, L., Shen, W., Yi, G.-S., Kong, X., Zhang, H., Feng, B., Sun, H., Chen, L., Li, G., et al. (2025) · Cardiovascular Research · doi:10.1093/cvr/cvaf212 · Cited by 9

Untargeted Metabolomics Studies of H9c2 Cardiac Cells Submitted to Oxidative Stress, β-Adrenergic Stimulation and Doxorubicin Treatment: Investigation of Cardiac Biomarkers

Lima, M. F., Amaral, A. G., Moretto, I. A., Paiva-Silva, F. J. T. N., Pereira, F. O. B., Barbas, C., dos Santos, A. M., Simionato, A. V. C., & Rupérez, F. J. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.898742 · Cited by 9

1,2,3-Triazole-Dithiocarbamate Hybrids, a Group of Novel Cell Active SIRT1 Inhibitors

Zheng, Y., Wang, L.-Z., Zhao, L.-J., Zhao, L., Zhan, Q.-N., Ma, J., Zhang, B., Wang, M.-M., Wang, Z.-R., Li, J., et al. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000438620 · Cited by 9

Dihydrocapsiate improved age-associated impairments in mice by increasing energy expenditure

Ohyama, K., & Suzuki, K. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00132.2017 · Cited by 9

Metabolic energy sensors as targets for designing host-directed therapies for tuberculosis

Cheng, C. Y., Böhme, J., & Singhal, A. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.4mr0617-226r · Cited by 9

Role of APD-Ribosylation in Bone Health and Disease

Wang, C., & Mbalaviele, G. (2019) · Cells · doi:10.3390/cells8101201 · Cited by 9

Domesticated and optimized mitochondria: Mitochondrial modifications based on energetic status and cellular stress

Zeng, M., He, Y. T., Zhou, H., Du, H., Shao, C., Yang, J., & Wan, H. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118766 · Cited by 9

Combined Salt and Caloric Restrictions: Potential Adverse Outcomes

Homma, T., Homma, M., Huang, Y., Mayurasakorn, K., Rodi, N. M., Hamid, A. A. A., Hurwitz, S., Yao, T. M., Adler, G. K., Pojoga, L. H., et al. (2017) · Journal of the American Heart Association · doi:10.1161/jaha.116.005374 · Cited by 9

Tobacco SABP2-interacting protein SIP428 is a SIR2 type deacetylase

Haq, M. I., Thakuri, B. K. C., Hobbs, T., Davenport, M. L., & Kumar, D. (2020) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2020.04.034 · Cited by 8

Circular and linear: a tale of aptamer selection for the activation of SIRT1 to induce death in cancer cells

Al-Sudani, B. T., Ragazzon-Smith, A., Aziz, A., Alansari, R., Ferry, N., Krstic–Demonacos, M., & Ragazzon, P. A. (2020) · RSC Advances · doi:10.1039/d0ra07857c · Cited by 9

NAD+-dependent Glsirt1 has a key role on secondary metabolism in Ganoderma lucidum

Han, J. D. J., Wang, S., Chen, X., Liu, R., Zhu, J. K., Shi, L., Ren, A., & Zhao, M. (2022) · Microbiological Research · doi:10.1016/j.micres.2022.126992 · Cited by 8

Sexual Dimorphism in Brain Sirtuin-1 and m6A Methylated Sirtuin-1 mRNA, and in Protection with Post-Injury Anti-miR-200c treatment, after Experimental Stroke in Aged Mice

Xu, L. (2023) · Aging and Disease · doi:10.14336/ad.2022.1225 · Cited by 8

Oxytocin, a main breastfeeding hormone, prevents hypertension acquired in utero: A therapeutics preview

Vargas-Martínez, F., Schanler, R. J., Abrams, S. A., Hawthorne, K. M., Landers, S., Guzmán-Bárcenas, J., Muñoz, O., Henriksen, T., Petersson, M., Uvnäs‐Moberg, K., et al. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.09.020 · Cited by 9

Oral niacin mitigates heat-induced reproductive impairments in male mice

Zahra, M., Divar, M. R., Jelodar, G., Reza, M. H., Sanaz, A. J., Amir, M. A., & Eshghi, D. (2025) · Scientific Reports · doi:10.1038/s41598-025-22341-3 · Cited by 7

Sex-Dependent Metabolic Effects in Diet-Induced Obese Rats following Intermittent Fasting Compared with Continuous Food Restriction

de Basea, L. B., Boguñà, M., Sánchez, A., Esteve, M., Grasa, M., & Romero, M. D. M. (2024) · Nutrients · doi:10.3390/nu16071009 · Cited by 7

Flavonostilbenes Isolated from the Stems of Rhamnoneuron balansae as Potential SIRT1 Activators

Cho, H. M., Zhang, M., Park, E. J., Lee, B.-W., Park, Y.-J., Kim, H. W., Pham, H. T. T., Chin, Y., & Oh, W. K. (2022) · Journal of Natural Products · doi:10.1021/acs.jnatprod.1c00689 · Cited by 8

Ageing, Metabolic Dysfunction, and the Therapeutic Role of Antioxidants

Santos, A. L., & Sinha, S. (2023) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-26576-1_15 · Cited by 8

The AMPK-SIRT1 Axis: Redefining type 2 diabetes mellitus management

Kemelo, M. K., & Moseki, P. (2025) · Results in Chemistry · doi:10.1016/j.rechem.2025.102139 · Cited by 6

Nicotinamide N-methyltransferase upregulation contributes to palmitate-elicited peroxisome proliferator-activated receptor transactivation in hepatocytes

Song, Q., Wang, J., Griffiths, A., Lee, S. M., Iyamu, I. D., Huang, R., Córdoba‐Chacón, J., & Song, Z. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00010.2023 · Cited by 6

Grape Seed Proanthocyanidin Extract Attenuates Cafeteria-Diet-Induced Liver Metabolic Disturbances in Rats: Influence of Photoperiod

Rodríguez, R. M., Colom‐Pellicer, M., Hernández-Baixauli, J., Calvo, E., Suárez, M., Arola‐Arnal, A., Torres‐Fuentes, C., Aragonès, G., & Mulero, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147713 · Cited by 7

SIRT1 in Metabolic Health and Disease

Boutant, M., & Cantó, C. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_4 · Cited by 3

Spatial Dynamics of SIRT1 Dictate Metabolic Transitions in the Cell Nucleus

Ranjit, S., Aguilar‐Arnal, L., Stringari, C., Sassone‐Corsi, P., & Gratton, E. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.11.1309

Sirtuin 1 and Sirtuin 3: Physiological Modulators of Metabolism

Nogueiras, R., Habegger, K. M., Chaudhary, N., Finan, B., Banks, A. S., Dietrich, M. O., Horváth, T. L., Sinclair, D. A., Pfluger, P. T., & Tschöp, M. H. (2012) · Physiological Reviews · doi:10.1152/physrev.00022.2011 · Cited by 724

SIRT1 and other sirtuins in metabolism

Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,157

NAD+ as a Pharmacological Tool to Boost Sirtuin Activity

Houtkooper, R. H. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_2