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

Oxidants, oxidative stress and the biology of ageing

Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413

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

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

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

Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239

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

Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750

hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690

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

Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253

Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081

Peroxisome Proliferator-Activated Receptor-γ Coactivator 1α (PGC-1α): Transcriptional Coactivator and Metabolic Regulator

Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076

Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase

Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924

Mitochondrial quality control in amyotrophic lateral sclerosis: towards a common pathway?

Khalil, B., & Liévens, J.-C. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.211179 · Cited by 51

A specific amino acid formula prevents alcoholic liver disease in rodents

Tedesco, L., Corsetti, G., Ruocco, C., Ragni, M., Rossi, F., Carruba, M. O., Valerio, A., & Nisoli, E. (2018) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00231.2017 · Cited by 51

A review on the cardioprotective mechanisms of metformin against doxorubicin

Ajzashokouhi, A. H., Bostan, H. B., Jomezadeh, V., Hayes, A. W., & Karimi, G. (2019) · Human & Experimental Toxicology · doi:10.1177/0960327119888277 · Cited by 50

Adipose Tissue SIRT1 Regulates Insulin Sensitizing and Anti-Inflammatory Effects of Berberine

Shan, Y., Zhang, S., Gao, B., Liang, S., Zhang, H., Yu, X., Zhao, J., Ye, L., Yang, Q., & Shang, W. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.591227 · Cited by 49

Diabetic retinopathy, oxidative stress, and sirtuins: an in depth look in enzymatic patterns and new therapeutic horizons

Nebbioso, M., Lambìase, A., Armentano, M., Tucciarone, G., Sacchetti, M., Greco, A., & Alisi, L. (2021) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2021.04.003 · Cited by 53

Catalase expression in MCF-7 breast cancer cells is mainly controlled by PI3K/Akt/mTor signaling pathway

Glorieux, C., Auquier, J., Dejeans, N., Sid, B., Demoulin, J., Bertrand, L., Verrax, J., & Calderón, P. B. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.02.025 · Cited by 49

Dysregulation of hepatic cAMP levels via altered Pde4b expression plays a critical role in alcohol‐induced steatosis

Avila, D. V., Barker, D. F., Zhang, J., McClain, C. J., Barve, S. S., & Gobejishvili, L. (2016) · The Journal of Pathology · doi:10.1002/path.4760 · Cited by 49

Histone Demethylase LSD1 Promotes Adipocyte Differentiation through Repressing Wnt Signaling

Chen, Y., Kim, J., Zhang, R., Yang, X., Zhang, Y., Fang, J., Chen, Z., Teng, L., Chen, X., Ge, H., et al. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.08.010 · Cited by 49

Small molecule PGC-1α1 protein stabilizers induce adipocyte Ucp1 expression and uncoupled mitochondrial respiration

Pettersson-Klein, A. T., Izadi, M., Ferreira, D. M. S., Červenka, I., Correia, J. C., Martínez-Redondo, V., Southern, M. R., Cameron, M. D., Kamenecka, T. M., Agudelo, L. Z., et al. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2018.01.017 · Cited by 51

Sirt1 is involved in energy metabolism: The role of chronic ethanol feeding and resveratrol

Oliva, J., French, B. A., Li, J., Bardag‐Gorce, F., Fu, P. C., & French, S. W. (2008) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2008.08.002 · Cited by 49

The Protective Mechanism of SIRT1 in the Regulation of Mitochondrial Biogenesis and Mitochondrial Autophagy in Alzheimer’s Disease

Ye, F., & Wu, A. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210132 · Cited by 50

Recharge of chondrocyte mitochondria by sustained release of melatonin protects cartilage matrix homeostasis in osteoarthritis

Zhang, Y., Hou, M., Liu, Y., Liu, T., Chen, X., Shi, Q., Geng, D., Yang, H., He, F., & Zhu, X. (2022) · Journal of Pineal Research · doi:10.1111/jpi.12815 · Cited by 48

The Role of Sirtuin 1 (SIRT1) in Neurodegeneration

Razick, D., Akhtar, M., Wen, J., Alam, M., Dean, N., Karabala, M., Ansari, U., Ansari, Z., Tabaie, E. A., & Siddiqui, S. (2023) · Cureus · doi:10.7759/cureus.40463 · Cited by 48

Redox signaling and skeletal muscle adaptation during aerobic exercise

Zhou, Y., Zhang, X., Baker, J. S., Davison, G. W., & Yan, X. (2024) · iScience · doi:10.1016/j.isci.2024.109643 · Cited by 52

Targeting PGC-1α to control energy homeostasis

Wu, Z., & Boss, O. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.10.1329 · Cited by 50

The role of SirT1 in muscle mitochondrial turnover

Menzies, K. J., & Hood, D. A. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.03.001 · Cited by 49

Protein kinase Cβ deficiency attenuates obesity syndrome of ob/ob mice by promoting white adipose tissue remodeling

Huang, W., Bansode, R. R., Bal, N. C., Mehta, M., & Mehta, K. D. (2011) · Journal of Lipid Research · doi:10.1194/jlr.m019687 · Cited by 47

Sirt 1 activator inhibits the AGE-induced apoptosis and p53 acetylation in human vascular endothelial cells

Li, P., Zhang, L., Zhou, C., Lin, N., & Liu, A. (2015) · The Journal of Toxicological Sciences · doi:10.2131/jts.40.615 · Cited by 48

A p300 and SIRT1 Regulated Acetylation Switch of C/EBPα Controls Mitochondrial Function

Zaini, M. A., Müller, C., de Jong, T. V., Ackermann, T., Hartleben, G., Kortman, G., Gührs, K., Fusetti, F., Krämer, O. H., Guryev, V., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.061 · Cited by 49

Developmental Programming of NAFLD by Parental Obesity

Thompson, M. D. (2020) · Hepatology Communications · doi:10.1002/hep4.1578 · Cited by 47

The role of adiponectin signaling in metabolic syndrome and cancer

Scheid, M. P., & Sweeney, G. (2013) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-013-9265-5 · Cited by 47

Mechanism of Action of Ketogenic Diet Treatment: Impact of Decanoic Acid and Beta—Hydroxybutyrate on Sirtuins and Energy Metabolism in Hippocampal Murine Neurons

Dabke, P., & Das, A. M. (2020) · Nutrients · doi:10.3390/nu12082379 · Cited by 47

SIRT1/PGC-1α/PPAR-γ Correlate With Hypoxia-Induced Chemoresistance in Non-Small Cell Lung Cancer

Xu, R., Luo, X., Ye, X., Li, H., Liu, H., Du, Q., & Zhai, Q. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.682762 · Cited by 44

Heme-oxygenase and lipid mediators in obesity and associated cardiometabolic diseases: Therapeutic implications

McClung, J. A., Levy, L., Garcia, V. G., Stec, D. E., Peterson, S. J., & Abraham, N. G. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107975 · Cited by 48

Free [NADH]/[NAD+] regulates sirtuin expression

Gambini, J., Gómez‐Cabrera, M. C., Borrás, C., Vallés, S. L., López-Grueso, R., Martinez-Bello, V. E., Herranz, D., Pallardó, F. V., Tresguerres, J. A. F., Serrano, M., et al. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.04.020 · Cited by 47

Extremely low-volume, high-intensity interval training improves exercise capacity and increases mitochondrial protein content in human skeletal muscle

K. Ma, J., D. Scribbans, T., A. Edgett, B., Colin Boyd, J., A. Simpson, C., P. Little, J., & J. Gurd, B. (2013) · Open Journal of Molecular and Integrative Physiology · doi:10.4236/ojmip.2013.34027 · Cited by 47

Energy sensing factors PGC-1α and SIRT1 modulate PXR expression and function

Buler, M., Aatsinki, S., Skoumal, R., & Hakkola, J. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.09.006 · Cited by 46

Sirt1's systemic protective roles and its promise as a target in antiaging medicine

Tang, B. L. (2010) · Translational research · doi:10.1016/j.trsl.2010.11.006 · Cited by 45

Specific Sirt1 Activator-mediated Improvement in Glucose Homeostasis Requires Sirt1-Independent Activation of AMPK

Park, S. J., Ahmad, F., Um, J.-H., Brown, A. L., Xu, X., Kang, H., Ke, H., Feng, X., Ryall, J. G., Philp, A., et al. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.03.019 · Cited by 46

Perivascular Adipose Tissue as a Target for Antioxidant Therapy for Cardiovascular Complications

Man, A. W. C., Zhou, Y., Xia, N., & Li, H. (2020) · Antioxidants · doi:10.3390/antiox9070574 · Cited by 45

Moringa oleifera Leaf Extract Upregulates Nrf2/HO-1 Expression and Ameliorates Redox Status in C2C12 Skeletal Muscle Cells

Duranti, G., Maldini, M., Crognale, D., Horner, K. M., Dimauro, I., Sabatini, S., & Ceci, R. (2021) · Molecules · doi:10.3390/molecules26165041 · Cited by 45

NAD+ Metabolism and Immune Regulation: New Approaches to Inflammatory Bowel Disease Therapies

Chen, C., Yan, W., Tao, M., & Fu, Y. (2023) · Antioxidants · doi:10.3390/antiox12061230 · Cited by 44

DJ-1 activates SIRT1 through its direct binding to SIRT1

Takahashi-Niki, K., Ganaha, Y., Niki, T., Nakagawa, S., Kato-Ose, I., Iguchi‐Ariga, S. M. M., & Ariga, H. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.084 · Cited by 46

Sirtuins and their interactions with transcription factors and poly(ADP-ribose) polymerases

Jęśko, H. M., & Strosznajder, R. P. (2016) · Folia Neuropathologica · doi:10.5114/fn.2016.62531 · Cited by 44

TIGAR regulates mitochondrial functions through SIRT1‐PGC1α pathway and translocation of TIGAR into mitochondria in skeletal muscle

Geng, J., Wei, M., Yuan, X. N., Liu, Z., Wang, X., Zhang, D., Luo, L., Wu, J., Guo, W., & Qin, Z. (2019) · The FASEB Journal · doi:10.1096/fj.201802209r · Cited by 43

Role of Sirtuins in Tumor Angiogenesis

Edatt, L., Poyyakkara, A., Raji, G. R., Ramachandran, V., Shankar, S. S., & Kumar, V. B. S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2019.01516 · Cited by 43

Aβ25–35 Suppresses Mitochondrial Biogenesis in Primary Hippocampal Neurons

Dong, W., Wang, F., Guo, W.-Q., Zheng, X., Chen, Y., Zhang, W., & Shi, H. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0222-6 · Cited by 46

Novel acridinedione derivatives: Design, synthesis, SIRT1 enzyme and tumor cell growth inhibition studies

Alvala, M., Bhatnagar, S., Alvala, R., Jeankumar, V. U., Manjashetty, T. H., Yogeeswari, P., & Sriram, D. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.03.030 · Cited by 44

Hypoxia: Role of SIRT1 and the protective effect of resveratrol in ovarian function

Nishigaki, A., Tsubokura, H., Tsuzuki‐Nakao, T., & Okada, H. (2021) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12428 · Cited by 42

Deterioration of plasticity and metabolic homeostasis in the brain of the UCD-T2DM rat model of naturally occurring type-2 diabetes

Agrawal, R., Zhuang, Y., Cummings, B. P., Stanhope, K. L., Graham, J. L., Havel, P. J., & Gómez‐Pinilla, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.05.007 · Cited by 44

High-fat and obesogenic diets: current and future strategies to fight obesity and diabetes

Teodoro, J. S., Varela, A. T. I. F., Rolo, A. P., & Palmeira, C. M. (2014) · Genes & Nutrition · doi:10.1007/s12263-014-0406-6 · Cited by 45

Energy sensing pathways: Bridging type 2 diabetes and colorectal cancer?

Yang, J., Nishihara, R., Zhang, X., Ogino, S., & Qian, Z. R. (2017) · Journal of Diabetes and its Complications · doi:10.1016/j.jdiacomp.2017.04.012 · Cited by 42

Perturbations of NAD+salvage systems impact mitochondrial function and energy homeostasis in mouse myoblasts and intact skeletal muscle

Agerholm, M., Dall, M., Jensen, B. A. H., Prats, C., Madsen, S., Basse, A. L., Graae, A.-S., Risis, S., Goldenbaum, J., Quistorff, B., et al. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00213.2017 · Cited by 42

Thyroid hormone regulation of Sirtuin 1 expression and implications to integrated responses in fasted mice

Cordeiro, A., Souza, L. L., Oliveira, L. S. D., Faustino, L. C., Santiago, L. A., Bloise, F. F., Ortiga-Carvalho, T. M., Almeida, N. A. D. S., & Pazos-Moura, C. C. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0420 · Cited by 46

Facts and controversies in our understanding of how caloric restriction impacts the mitochondrion

Gouspillou, G., & Hepple, R. T. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.03.004 · Cited by 42

Sirtuins and cognition: implications for learning and memory in neurological disorders

Fagerli, E. A., Escobar, I., Ferrier, F. J., Jackson, C. W., Lao, E. J. P., & Pérez‐Pinzón, M. A. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.908689 · Cited by 43

Sirtuin1-p53: A potential axis for cancer therapy

Yin, J., Lu, X.-T., Hou, M.-L., Cao, T., & Tian, Z. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115543 · Cited by 44

The potential of herbal drugs to treat heart failure: The roles of Sirt1/AMPK

Zhang, T., Xu, L., Guo, X., Tao, H., Liu, Y., Liu, X., Zhang, Y., & Meng, X. (2023) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2023.09.001 · Cited by 45

Polydatin Alleviates Small Intestine Injury during Hemorrhagic Shock as a SIRT1 Activator

Zeng, Z., Chen, Z., Xu, S., Song, R., Yang, H. S., & Zhao, K. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/965961 · Cited by 42

G Protein-coupled Receptor 40 (GPR40) and Peroxisome Proliferator-activated Receptor γ (PPARγ)

Wang, S., Awad, K. S., Elinoff, J. M., Dougherty, E. J., Ferreyra, G. A., Wang, J. Y., Cai, R., Sun, J., Ptasinska, A., & Danner, R. L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.638924 · Cited by 44

HDAC 4 stabilizes SIRT 1 via sumoylation SIRT 1 to delay cellular senescence

Han, X., Niu, J., Zhao, Y., Kong, Q., Tong, T., & Han, L. (2015) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.12496 · Cited by 42

Amelioration of Huntington's disease phenotypes by Beta-Lapachone is associated with increases in Sirt1 expression, CREB phosphorylation and PGC-1α deacetylation

Lee, M., Ban, J.-J., Chung, J. Y., Im, W., & Kim, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0195968 · Cited by 42

JAK1-mediated Sirt1 phosphorylation functions as a negative feedback of the JAK1-STAT3 pathway

Wang, W., Li, F. R., Xu, Y., Wei, J., Zhang, Y., Yang, H., Gao, B., Yu, G., & Fang, D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001387 · Cited by 43

Reduced sirtuin 1/adenosine monophosphate‐activated protein kinase in amyotrophic lateral sclerosis patient‐derived mesenchymal stem cells can be restored by resveratrol

Yun, Y. C., Jeong, S., Kim, S. H., & Cho, G. (2018) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.2776 · Cited by 42

Metabolic Relationship Between Cancer-Associated Fibroblasts and Cancer Cells

Sazeides, C., & Le, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-65768-0_14 · Cited by 41

The Complex Interplay between Imbalanced Mitochondrial Dynamics and Metabolic Disorders in Type 2 Diabetes

Huynh, T. V., Rethi, L., Rethi, L., Chen, C., Chen, Y., & Kao, Y. (2023) · Cells · doi:10.3390/cells12091223 · Cited by 42

Epsilon PKC Increases Brain Mitochondrial SIRT1 Protein Levels via Heat Shock Protein 90 following Ischemic Preconditioning in Rats

Thompson, J. W., Dave, K. R., Saul, I., Narayanan, S., & Pérez‐Pinzón, M. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075753 · Cited by 41

Effect of near-infrared light exposure on mitochondrial signaling in C2C12 muscle cells

Nguyen, L. M. ‐., Malamo, A. G., Larkin-Kaiser, K. A., Borsa, P. A., & Adhihetty, P. J. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.11.001 · Cited by 41

The role of sirtuin proteins in obesity

Metoyer, C. F., & Pruitt, K. (2008) · Pathophysiology · doi:10.1016/j.pathophys.2008.04.002 · Cited by 40

IHG-1 Promotes Mitochondrial Biogenesis by Stabilizing PGC-1α

Hickey, F. B., Corcoran, J. B., Docherty, N. G., Griffin, B., Bhreathnach, Ú., Furlong, F. M., Martin, F., Godson, C., & Murphy, M. (2011) · Journal of the American Society of Nephrology · doi:10.1681/asn.2010111154 · Cited by 41

Electroacupuncture Upregulates SIRT1-Dependent PGC-1α Expression in SAMP8 Mice

Dong, W., Quo, W., Wang, F., Li, C., Xie, Y., Zheng, X., & Shi, H. (2015) · Medical Science Monitor · doi:10.12659/msm.894864 · Cited by 40

Short-term ursolic acid promotes skeletal muscle rejuvenation through enhancing of SIRT1 expression and satellite cells proliferation

Bakhtiari, N., Hosseinkhani, S., Soleimani, M., Hemmati, R., Noori-Zadeh, A., Javan, M., & Tashakor, A. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.01.010 · Cited by 40

Sirtuins as modifiers of Parkinson's disease pathology

Tang, B. L. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23806 · Cited by 41

SIRT1 interacts with metabolic transcriptional factors in the pancreas of insulin-resistant and calorie-restricted rats

Chen, Y.-R., Lai, Y.-L., Lin, S., Li, X.-T., Fu, Y., & Xu, W. (2013) · Molecular Biology Reports · doi:10.1007/s11033-012-2412-3 · Cited by 41

Unraveling the Complexities of SIRT1-Mediated Mitochondrial Regulation in Skeletal Muscle

Philp, A., & Schenk, S. (2013) · Exercise and Sport Sciences Reviews · doi:10.1097/jes.0b013e3182956803 · Cited by 39

Recreational scuba diving: negative or positive effects of oxidative and cardiovascular stress?

Perović, A., Unić, A., & Dumić, J. (2014) · Biochemia Medica · doi:10.11613/bm.2014.026 · Cited by 42

SIRT1 and NAD + precursors: Therapeutic targets in multiple sclerosis a review

Nimmagadda, V. K. C., Makar, T. K., Chandrasekaran, K., Sagi, A. R., Ray, J., Russell, J. W., & Bever, C. T. (2016) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2016.07.007 · Cited by 39

Systems approach to characterize the metabolism of liver cancer stem cells expressing CD133

Hur, W., Ryu, J. Y., Kim, H. U., Hong, S. W., Lee, E. B., Lee, S. Y., & Yoon, S. K. (2017) · Scientific Reports · doi:10.1038/srep45557 · Cited by 39

Ghrelin mediated neuroprotection - A possible therapy for Parkinson's disease?

Morgan, A. H., Rees, D. J., Andrews, Z. B., & Davies, J. S. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.12.027 · Cited by 40

Altered Redox Homeostasis in Branched‐Chain Amino Acid Disorders, Organic Acidurias, and Homocystinuria

Richard, E., Gallego‐Villar, L., Rivera‐Barahona, A., Oyarzábal, A., Pérez, B., Rodríguez‐Pombo, P., & Desviat, L. R. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1246069 · Cited by 39

Ginsenoside Rg3 Attenuates TNF-α-Induced Damage in Chondrocytes through Regulating SIRT1-Mediated Anti-Apoptotic and Anti-Inflammatory Mechanisms

Ma, C.-H., Chou, W.-C., Wu, C.-H., Jou, I., Tu, Y., Hsieh, P., & Tsai, K. (2021) · Antioxidants · doi:10.3390/antiox10121972 · Cited by 40

Peripheral Circadian Oscillators

Buijs, R. M., Salgado, R., Sabath, E., & Escobar, C. (2013) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396971-2.00004-x · Cited by 43

Acetylation in Nuclear Receptor Signaling and the Role of Sirtuins

Wang, C., Powell, M. J., Popov, V. M., & Pestell, R. G. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0379 · Cited by 39

The neuroprotective effects of icariin on ageing, various neurological, neuropsychiatric disorders, and brain injury induced by radiation exposure

Li, L. R., Sethi, G., Zhang, X., Liu, C. L., Yan, H., Liu, Q., Ren, B. X., & Tang, F. R. (2022) · Aging · doi:10.18632/aging.203893 · Cited by 41

Myostatin Knockout Affects Mitochondrial Function by Inhibiting the AMPK/SIRT1/PGC1α Pathway in Skeletal Muscle

Gu, M., Wei, Z., Wang, X., Gao, Y., Wang, D., Liu, X., Bai, C., Su, G., Yang, L., & Li, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213703 · Cited by 38

Sirtuin 1 and 7 mediate resveratrol-induced recovery from hyper-anxiety in high-fructose-fed prediabetic rats

Reddy, B. R., Maitra, S., Jhelum, P., Kumar, K. P., Bagul, P. K., Kaur, G., Banerjee, S., Kumar, A., & Chakravarty, S. (2016) · Journal of Biosciences · doi:10.1007/s12038-016-9627-8 · Cited by 40

Sirtuins in metabolism, stemness and differentiation

Correia, M., Perestrelo, T., Rodrigues, A. S., Ribeiro, M. F., Pereira, S. L., Sousa, M. I., & Ramalho‐Santos, J. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.09.008 · Cited by 40

Ribosomal transcription is regulated by PGC-1alpha and disturbed in Huntington’s disease

Jesse, S., Bayer, H., Alupei, M. C., Zügel, M., Mulaw, M. A., Tuorto, F., Malmsheimer, S., Singh, K., Steinacker, J. M., Schümann, U., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-09148-7 · Cited by 40

Aralia taibaiensis Protects against I/R-Induced Brain Cell Injury through the Akt/SIRT1/FOXO3a Pathway

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Systems Level Understanding of Circadian Integration with Cell Physiology

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Endothelial Nitric Oxide Synthase in the Perivascular Adipose Tissue

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Control of NAD+ homeostasis by autophagic flux modulates mitochondrial and cardiac function

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Carbonic anhydrases are involved in mitochondrial biogenesis and control the production of lactate by human Sertoli cells

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Sirtuins in Neurodegenerative Diseases: A Biological-Chemical Perspective

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Preventive effects of dietary walnuts on high-fat-induced hepatic fat accumulation, oxidative stress and apoptosis in mice

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Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins

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SIRT1 is a transcriptional enhancer of the glucocorticoid receptor acting independently to its deacetylase activity

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MeCP2-mediated epigenetic regulation in senescent endothelial progenitor cells

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Sirt1 and the Mitochondria

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The deacetylase enzyme SIRT1 is not associated with oxidative capacity in rat heart and skeletal muscle and its overexpression reduces mitochondrial biogenesis

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Identification of cofactor network, including SIRT1 and SRC-3, which converges on energy expenditure through PGC-1α

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Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC‐1α

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