Sirt1 and the Mitochondria

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

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

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

Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300

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

Multiple Wearable Sensors in Parkinson and Huntington Disease Individuals: A Pilot Study in Clinic and at Home

Adams, J., Dinesh, K., Xiong, M., Tarolli, C. G., Sharma, S., Sheth, N., Aranyosi, A. J., Zhu, W. Y., Goldenthal, S. B., Biglan, K., et al. (2017) · Digital Biomarkers · doi:10.1159/000479018 · Cited by 3,190

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

Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160

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

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

Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491

Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease

Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654

PGC-1 α , Inflammation, and Oxidative Stress: An Integrative View in Metabolism

Rius‐Pérez, S., Torres-Cuevas, I., Millán, I., Ortega, Á., & Pérez, S. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1452696 · Cited by 671

Biological Activities of Stilbenoids

Akinwumi, B. C., Bordun, K.-A., & Anderson, H. D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030792 · Cited by 392

NAD+ improves cognitive function and reduces neuroinflammation by ameliorating mitochondrial damage and decreasing ROS production in chronic cerebral hypoperfusion models through Sirt1/PGC-1α pathway

Zhao, Y., Zhang, J., Zheng, Y., Zhang, Y., Zhang, X. J., Wang, H., Du, Y., Guan, J., Wang, X., & Fu, J. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02250-8 · Cited by 362

The Role of Autophagy and Mitophagy in Bone Metabolic Disorders

Wang, S., Deng, Z., Ma, Y., Jin, J., Qi, F., Li, S., Liu, C., Lyu, F., & Zheng, Q. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.46627 · Cited by 333

Mitochondrial dysfunction in neurodegenerative diseases and the potential countermeasure

Wang, Y., Xu, E., Musich, P. R., & Lin, F. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13116 · Cited by 298

Sirtuins and Their Roles in Brain Aging and Neurodegenerative Disorders

Jęśko, H. M., Wencel, P. L., Strosznajder, R. P., & Strosznajder, J. B. (2016) · Neurochemical Research · doi:10.1007/s11064-016-2110-y · Cited by 264

Mechanisms Leading to Differential Hypoxia-Inducible Factor Signaling in the Diabetic Kidney: Modulation by SGLT2 Inhibitors and Hypoxia Mimetics

Packer, M. (2020) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2020.04.016 · Cited by 218

The pleiotropic neuroprotective effects of resveratrol in cognitive decline and Alzheimer’s disease pathology: From antioxidant to epigenetic therapy

Griñán-Ferré, C., Bellver-Sanchis, A., Izquierdo, V., Corpas, R., Roig-Soriano, J., Chillón, M., Andres-Lacueva, C., Somogyvári, M., Sőti, C., Sanfeliu, C., et al. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101271 · Cited by 208

Mesenchymal stem cell secretome for regenerative medicine: Where do we stand?

Trigo, C. M., Rodrigues, J. S., Camões, S. P., Solá, S., & Miranda, J. P. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2024.05.004 · Cited by 252

Mitochondria as an important target of metformin: The mechanism of action, toxic and side effects, and new therapeutic applications

Feng, J., Wang, X., Ye, X., Arés, I., López-Torres, B., Martínez, M., Martínez‐Larrañaga, M., Wang, X., Anadón, A., & Martínez, M. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106114 · Cited by 201

SIRT1 and SIRT2 Activity Control in Neurodegenerative Diseases

Manjula, R., Anuja, K., & Alcain, F. J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.585821 · Cited by 197

Hepatic stellate cell senescence in liver fibrosis: Characteristics, mechanisms and perspectives

Zhang, M., Salas, S. S., Damba, T., Borghesan, M., Demaria, M., & Moshage, H. J. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111572 · Cited by 192

PGC-1α-Mediated Mitochondrial Quality Control: Molecular Mechanisms and Implications for Heart Failure

Chen, L., Qin, Y. H., Liu, B., Gao, M. Q., Li, A., Li, X., & Gong, G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.871357 · Cited by 186

Energy Metabolism Decline in the Aging Brain—Pathogenesis of Neurodegenerative Disorders

Błaszczyk, J. W. (2020) · Metabolites · doi:10.3390/metabo10110450 · Cited by 166

Deregulated mitochondrial microRNAs in Alzheimer's disease: Focus on synapse and mitochondria

Gowda, P., Reddy, P. H., & Kumar, S. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101529 · Cited by 170

Brain SIRT1 Mediates Metabolic Homeostasis and Neuroprotection

Xu, J., Jackson, C. W., Khoury, N., Escobar, I., & Pérez‐Pinzón, M. A. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00702 · Cited by 158

Resveratrol Induces Brain Resilience Against Alzheimer Neurodegeneration Through Proteostasis Enhancement

Corpas, R., Griñán‐Ferré, C., Rodrı́guez-Farré, E., Pallàs, M., & Sanfeliu, C. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1157-y · Cited by 164

Unraveling the AMPK-SIRT1-FOXO Pathway: The In-Depth Analysis and Breakthrough Prospects of Oxidative Stress-Induced Diseases

Guan, G., Chen, Y., & Dong, Y. (2025) · Antioxidants · doi:10.3390/antiox14010070 · Cited by 175

Idiopathic Pulmonary Fibrosis: Aging, Mitochondrial Dysfunction, and Cellular Bioenergetics

Zank, D. C., Bueno, M., Mora, A. L., & Rojas, M. M. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2018.00010 · Cited by 152

Nobiletin ameliorates hepatic ischemia and reperfusion injury through the activation of SIRT-1/FOXO3a-mediated autophagy and mitochondrial biogenesis

Dusabimana, T., Kim, S. R., Kim, H. J., Park, S. W., & Kim, H. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0245-z · Cited by 151

Protective Effects of Curcumin in Cardiovascular Diseases—Impact on Oxidative Stress and Mitochondria

Cox, F. F., Misiou, A., Vierkant, A., Ale‐Agha, N., Grandoch, M., Haendeler, J., & Altschmied, J. (2022) · Cells · doi:10.3390/cells11030342 · Cited by 154

Sirt1: A Guardian of the Development of Diabetic Retinopathy

Mishra, M., Duraisamy, A. J., & Kowluru, R. A. (2018) · Diabetes · doi:10.2337/db17-0996 · Cited by 132

SIRT1 in forebrain excitatory neurons produces sexually dimorphic effects on depression-related behaviors and modulates neuronal excitability and synaptic transmission in the medial prefrontal cortex

Lei, Y., Wang, J., Wang, D., Li, C., Liu, B., Fang, X., You, J., Guo, M., & Lu, X.-Y. (2020) · Molecular Psychiatry · doi:10.1038/s41380-019-0352-1 · Cited by 131

Oxidative Stress, Neuroinflammation and Mitochondria in the Pathophysiology of Amyotrophic Lateral Sclerosis

Obrador, E., Palmer, R. S., López‐Blanch, R., Jihad-Jebbar, A., Vallés, S. L., & Estrela, J. M. (2020) · Antioxidants · doi:10.3390/antiox9090901 · Cited by 132

Sepsis is associated with mitochondrial DNA damage and a reduced mitochondrial mass in the kidney of patients with sepsis-AKI

van der Slikke, E. C., Star, B. S., van Meurs, M., Henning, R., Moser, J., & Bouma, H. (2021) · Critical Care · doi:10.1186/s13054-020-03424-1 · Cited by 117

PGC-1α affects skeletal muscle and adipose tissue development by regulating mitochondrial biogenesis

Kong, S., Cai, B., & Nie, Q. (2022) · Molecular Genetics and Genomics · doi:10.1007/s00438-022-01878-2 · Cited by 132

Pharmacological advances in mitochondrial therapy

Singh, A., Faccenda, D., & Campanella, M. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103244 · Cited by 128

Ameliorating Mitochondrial Dysfunction of Neurons by Biomimetic Targeting Nanoparticles Mediated Mitochondrial Biogenesis to Boost the Therapy of Parkinson's Disease

Zheng, Q. Y., Liu, H., Zhang, H., Han, Y., Yuan, J., Wang, T., Gao, Y., & Li, Z. (2023) · Advanced Science · doi:10.1002/advs.202300758 · Cited by 117

Modulation of miR-34a/SIRT1 signaling protects cochlear hair cells against oxidative stress and delays age-related hearing loss through coordinated regulation of mitophagy and mitochondrial biogenesis

Xiong, H., Chen, S., Lai, L., Yang, H., Xu, Y., Pang, J., Su, Z., Lin, H., & Zheng, Y. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.03.013 · Cited by 117

MicroRNAs: pioneering regulators in Alzheimer’s disease pathogenesis, diagnosis, and therapy

Li, Y.-B., Fu, Q., Guo, M., Du, Y., Chen, Y., & Cheng, Y. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-03075-8 · Cited by 134

Pyrroloquinoline quinone promotes mitochondrial biogenesis in rotenone-induced Parkinson’s disease model via AMPK activation

Cheng, Q., Chen, J., Guo, H. M., Lu, J., Zhou, J., Guo, X., Shi, Y., Zhang, Y., Yu, S., Zhang, Q., et al. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0487-2 · Cited by 112

Phosphodiesterase Inhibitors for Alzheimer’s Disease: A Systematic Review of Clinical Trials and Epidemiology with a Mechanistic Rationale

Sanders, O. D., & Rajagopal, L. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200191 · Cited by 117

Mitochondria, Telomeres and Telomerase Subunits

Zheng, Q., Huang, J., & Wang, G. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00274 · Cited by 118

Ramadan diurnal intermittent fasting modulates SOD2, TFAM, Nrf2, and sirtuins (SIRT1, SIRT3) gene expressions in subjects with overweight and obesity

Madkour, M. I., El-Serafi, A. T., Jahrami, H., Sherif, N. M., Hassan, R. E., Awadallah, S. M., & Faris, M. E. (2019) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2019.107801 · Cited by 112

Autophagy-dependent and -independent modulation of oxidative and organellar stress in the diabetic heart by glucose-lowering drugs

Packer, M. (2020) · Cardiovascular Diabetology · doi:10.1186/s12933-020-01041-4 · Cited by 113

Sirtuins, resveratrol and the intertwining cellular pathways connecting them

Ungurianu, A., Zanfirescu, A., & Margina, D. M. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101936 · Cited by 114

Mitochondrial network dynamics in pulmonary disease: Bridging the gap between inflammation, oxidative stress, and bioenergetics

Pokharel, M. D., Flores, A. G., Marciano, D. P., Franco, M. C., Fineman, J. R., Aggarwal, S., Wang, T., & Black, S. M. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103049 · Cited by 124

Emerging Players at the Intersection of Chondrocyte Loss of Maturational Arrest, Oxidative Stress, Senescence and Low‐Grade Inflammation in Osteoarthritis

Minguzzi, M., Cetrullo, S., D’Adamo, S., Silvestri, Y., Flamigni, F., & Borzı̀, R. M. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/3075293 · Cited by 113

Role of Deranged Energy Deprivation Signaling in the Pathogenesis of Cardiac and Renal Disease in States of Perceived Nutrient Overabundance

Packer, M. (2020) · Circulation · doi:10.1161/circulationaha.119.045561 · Cited by 113

Melatonin, clock genes and mitochondria in sepsis

Acuña-Castroviejo, D., Rahim, I., Acuña‐Fernández, C., Fernández‐Ortiz, M., Marín, J. S., Sayed, R. K. A., Díaz-Casado, M. E., Rusanova, I., López, L. C., & Escames, G. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2610-1 · Cited by 115

Progress in Nonalcoholic Fatty Liver Disease: SIRT Family Regulates Mitochondrial Biogenesis

Zeng, C., & Chen, M. (2022) · Biomolecules · doi:10.3390/biom12081079 · Cited by 108

Sirtuins' control of autophagy and mitophagy in cancer

Aventaggiato, M., Vernucci, E., Barreca, F., Russo, M. A., & Tafani, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107748 · Cited by 103

AMPK/mTOR pathway significance in healthy liver and non‐alcoholic fatty liver disease and its progression

Marcondes‐de‐Castro, I. A., Reis‐Barbosa, P. H., Marinho, T. D. S., Águila, M. B., & Mandarim‐de‐Lacerda, C. A. (2023) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.16272 · Cited by 110

Mutual Antagonism of Hypoxia-Inducible Factor Isoforms in Cardiac, Vascular, and Renal Disorders

Packer, M. (2020) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2020.05.006 · Cited by 103

Corylin reduces obesity and insulin resistance and promotes adipose tissue browning through SIRT-1 and β3-AR activation

Chen, C., Kuo, C.-H., Leu, Y., & Wang, S. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105291 · Cited by 105

Molecular Mechanisms of SGLT2 Inhibitor on Cardiorenal Protection

Hou, Y., Zheng, C., Yen, T., & Lu, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217833 · Cited by 110

Reduction in podocyte SIRT1 accelerates kidney injury in aging mice

Chuang, P. Y., Cai, W., Li, X., Fang, L., Xu, J., Yacoub, R., He, J. C., & Lee, K. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00255.2017 · Cited by 98

Mitochondria as pharmacological targets in Down syndrome

Valenti, D., Braidy, N., Rasmo, D. D., Signorile, A., Rossi, L., Atanasov, A. G., Volpicella, M., Henrion‐Caude, A., Nabavi, S. M., & Vacca, R. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.014 · Cited by 99

Altered mitochondrial metabolism in the insulin‐resistant heart

Makrecka‐Kuka, M., Liepinsh, E., Murray, A. J., Lemieux, H., Dambrova, M., Tepp, K., Puurand, M., Käämbre, T., Han, W. H., de Goede, P., et al. (2019) · Acta Physiologica · doi:10.1111/apha.13430 · Cited by 93

Accelerated Kidney Aging in Diabetes Mellitus

Guo, J., Zheng, H., Zhang, W., Lou, W., Xia, C., Han, X. T., Huang, W. J., Zhang, F., Wang, Y., & Liu, W. J. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1234059 · Cited by 101

PGC1α: Friend or Foe in Cancer?

Mastropasqua, F., Girolimetti, G., & Shoshan, M. C. (2018) · Genes · doi:10.3390/genes9010048 · Cited by 97

Melatonin Effects on Non-Alcoholic Fatty Liver Disease Are Related to MicroRNA-34a-5p/Sirt1 Axis and Autophagy

Stacchiotti, A., Grossi, I., García-Gómez, R., Patel, G. A., Salvi, A., Lavazza, A., Petro, G. D., Monsalve, M., & Rezzani, R. (2019) · Cells · doi:10.3390/cells8091053 · Cited by 93

Oxidative stress and energy metabolism abnormalities in polycystic ovary syndrome: from mechanisms to therapeutic strategies

Yan, H., Wang, L., Zhang, G., Li, N., Zhao, Y., Liu, J., Jiang, M., Du, X., Zeng, Q., Xiong, D., et al. (2024) · Reproductive Biology and Endocrinology · doi:10.1186/s12958-024-01337-0 · Cited by 107

Therapeutic role of sirtuins in neurodegenerative disease and their modulation by polyphenols

Ajami, M., Pazoki–Toroudi, H., Amani, H., Nabavi, S. F., Braidy, N., Vacca, R. A., Atanasov, A. G., MOCAN, A., & Nabavi, S. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.11.022 · Cited by 94

CD38: T Cell Immuno-Metabolic Modulator

Kar, A., Mehrotra, S., & Chatterjee, S. (2020) · Cells · doi:10.3390/cells9071716 · Cited by 94

Irisin exhibits neuroprotection by preventing mitochondrial damage in Parkinson’s disease

Zhang, X., Xu, S., Hu, Y. H., Liu, Q., Liu, C., Chai, H., Luo, Y., Jin, L., & Li, S. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00453-9 · Cited by 97

Variations in HPV function are associated with survival in squamous cell carcinoma

Gleber‐Netto, F. O., Rao, X., Guo, T. W., Xi, Y., Gao, M., Shen, L., Erikson, K., Kalu, N. N., Ren, S., Xu, G., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.124762 · Cited by 86

Critical examination of mechanisms underlying the reduction in heart failure events with SGLT2 inhibitors: identification of a molecular link between their actions to stimulate erythrocytosis and to alleviate cellular stress

Packer, M. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvaa064 · Cited by 86

CD38: An important regulator of T cell function

Li, W., Liang, L., Liao, Q., Li, Y., & Zhou, Y. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113395 · Cited by 89

Mitochondrial dysfunction and oxidative stress: Role in chronic kidney disease

Srivastava, A., Tomar, B., Sharma, D., & Rath, S. K. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121432 · Cited by 89

Antioxidant Alternatives in the Treatment of Amyotrophic Lateral Sclerosis: A Comprehensive Review

Carrera‐Juliá, S., Moreno, M. L., Barrios, C., Ortí, J. E. D. L. R., & Drehmer, E. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00063 · Cited by 87

Resveratrol inhibits paclitaxel-induced neuropathic pain by the activation of PI3K/Akt and SIRT1/PGC1α pathway

Li, X., Yang, S., Wang, L., Liu, P., Zhao, S., Li, H., Jiang, Y., Guo, Y., & Wang, X. (2019) · Journal of Pain Research · doi:10.2147/jpr.s185873 · Cited by 82

Implications of Resveratrol in Obesity and Insulin Resistance: A State-of-the-Art Review

Barber, T. M., Kabisch, S., Randeva, H. S., Pfeiffer, A. F. H., & Weickert, M. O. (2022) · Nutrients · doi:10.3390/nu14142870 · Cited by 83

Mitochondrial MicroRNAs in Aging and Neurodegenerative Diseases

John, A. A., Kubosumi, A., & Reddy, P. H. (2020) · Cells · doi:10.3390/cells9061345 · Cited by 82

Pyrroloquinoline Quinone, a Redox-Active o -Quinone, Stimulates Mitochondrial Biogenesis by Activating the SIRT1/PGC-1α Signaling Pathway

才原一浩, Kamikubo, R., Ikemoto, K., Uchida, K., & Akagawa, M. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b01185 · Cited by 79

Longevity genes, cardiac ageing, and the pathogenesis of cardiomyopathy: implications for understanding the effects of current and future treatments for heart failure

Packer, M. (2020) · European Heart Journal · doi:10.1093/eurheartj/ehaa360 · Cited by 78

The Endoplasmic Reticulum Stress Response in Neuroprogressive Diseases: Emerging Pathophysiological Role and Translational Implications

Morris, G., Puri, B. K., Walder, K. R., Berk, M., Stubbs, B., Maes, M. H. J., & Carvalho, A. F. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1028-6 · Cited by 80

Resveratrol decreases the expression of genes involved in inflammation through transcriptional regulation

Pinheiro, D. M. L., de Oliveira, A. H. S., Coutinho, L. G., Fontes-Dantas, F. L., Oliveira, R. K. D. M., Oliveira, T. T., Faustino, A. L. F., da Silva, V. L., Campos, J. T. A. D. M., Lajus, T. B. P., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.432 · Cited by 78

Sildenafil for the Treatment of Alzheimer’s Disease: A Systematic Review

Sanders, O. D. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200166 · Cited by 76

Interplay of adenosine monophosphate‐activated protein kinase/sirtuin‐1 activation and sodium influx inhibition mediates the renal benefits of sodium‐glucose co‐transporter‐2 inhibitors in type 2 diabetes: A novel conceptual framework

Packer, M. (2020) · Diabetes Obesity and Metabolism · doi:10.1111/dom.13961 · Cited by 75

Protection Against Insulin Resistance by Apolipoprotein M/Sphingosine-1-Phosphate

Kurano, M., Tsukamoto, K., Shimizu, T., Kassai, H., Nakao, K., Aiba, A., Hara, M., & Yatomi, Y. (2020) · Diabetes · doi:10.2337/db19-0811 · Cited by 74

oxLDL-Induced Trained Immunity Is Dependent on Mitochondrial Metabolic Reprogramming

Groh, L. A., Ferreira, A. V., Helder, L. S., van der Heijden, C. D. C. C., Novakovic, B., van de Westerlo, E., Matzaraki, V., Moorlag, S. J. C. F. M., de Bree, L. C. J., Koeken, V. A. C. M., et al. (2021) · Immunometabolism · doi:10.20900/immunometab20210025 · Cited by 75

Nicotinamide riboside promotes Mfn2-mediated mitochondrial fusion in diabetic hearts through the SIRT1-PGC1α-PPARα pathway

Hu, L., Guo, Y., Song, L., Wen, H., Sun, N., Wang, Y., Qi, B., Liang, Q., Geng, J., Liu, X., et al. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.03.012 · Cited by 73

Sirt1 sustains female fertility by slowing age‐related decline in oocyte quality required for post‐fertilization embryo development

Iljas, J. D., Wei, Z., & Homer, H. A. (2020) · Aging Cell · doi:10.1111/acel.13204 · Cited by 74

Mitochondrial dysfunction and beneficial effects of mitochondria-targeted small peptide SS-31 in Diabetes Mellitus and Alzheimer’s disease

Ding, X.-W., Robinson, M., Li, R., Aldhowayan, H., Geetha, T., & Babu, J. R. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105783 · Cited by 73

Insulin and Its Key Role for Mitochondrial Function/Dysfunction and Quality Control: A Shared Link between Dysmetabolism and Neurodegeneration

Galizzi, G., & Carlo, M. D. (2022) · Biology · doi:10.3390/biology11060943 · Cited by 77

Cardioprotective Properties of Kaempferol: A Review

Kamisah, Y., Jalil, J., Yunos, N. M., & Zainalabidin, S. (2023) · Plants · doi:10.3390/plants12112096 · Cited by 72

Puerarin ameliorates metabolic dysfunction-associated fatty liver disease by inhibiting ferroptosis and inflammation

Yang, M., Xia, L., Song, J., Hu, H., Zang, N., Yang, J., Zou, Y., Wang, L., Zheng, X., He, Q., et al. (2023) · Lipids in Health and Disease · doi:10.1186/s12944-023-01969-y · Cited by 72

Involvement of the SIRT1-NLRP3 pathway in the inflammatory response

Chen, H., Deng, J., Gao, H., Song, Y., Zhang, Y., Sun, J., & Zhai, J. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01177-2 · Cited by 79

Melatonin Attenuates Oxidative Stress-Induced Apoptosis of Bovine Ovarian Granulosa Cells by Promoting Mitophagy via SIRT1/FoxO1 Signaling Pathway

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