1. Cui H, Kong Y, transduction HZ-J of signal, et al. Oxidative stress, mitochondrial dysfunction, and aging. hindawi.com, https://www.hindawi.com/archive/2012/646354/citations/ (accessed 10 August 2020). [ DOI:10.1155/2012/646354] 2. Onyango I, Lu J, Rodova M, et al. Regulation of neuron mitochondrial biogenesis and relevance to brain health. Elsevier, https://www.sciencedirect.com/science/article/pii/S0925443909001677 (accessed 10 August 2020). 3. Trifunovic A, Larsson NG. Mitochondrial dysfunction as a cause of ageing. In: Journal of Internal Medicine. 2008, pp. 167-78. [ DOI:10.1111/j.1365-2796.2007.01905.x] 4. Jones JM, Datta P, Srinivasula SM, et al. Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice, www.nature.com/nature (2003, accessed 10 August 2020). [ DOI:10.1038/nature02052] 5. Genetics DW-T in, 1989 undefined. Mitochondrial DNA mutations and neuromuscular disease. Elsevier, https://www.sciencedirect.com/science/article/pii/016895258990005X (accessed 10 August 2020). 6. Lowell BB, Shulman GI. Mitochondrial Dysfunction and Type 2 Diabetes. Proc Natl Acad Sci USA 2003; 30: 5050. 7. Saxena R, Bakker P de, Singer K, et al. Comprehensive association testing of common mitochondrial DNA variation in metabolic disease. Elsevier, https://www.sciencedirect.com/science/article/pii/S0002929707600056 (accessed 10 August 2020). 8. Mercer JR. Suboptimal nutrition programs offspring metabolic health View project Mitochondrial bioenergetics and therapeutic intervention in cardiovascular disease. Elsevier. Epub ahead of print 2013. 9. Hall AR, Burke N, Dongworth RK, et al. Mitochondrial fusion and fission proteins: Novel therapeutic targets for combating cardiovascular disease. British Journal of Pharmacology 2014; 171: 1890-906. [ DOI:10.1111/bph.12516] 10. Barbosa MC, Grosso RA, Fader CM. Hallmarks of aging: An autophagic perspective. Frontiers in Endocrinology; 10. Epub ahead of print 2019. [ DOI:10.3389/fendo.2018.00790] 11. Sun N, Youle RJ, Finkel T. The Mitochondrial Basis of Aging. Molecular Cell 2016; 61: 654-66. [ DOI:10.1016/j.molcel.2016.01.028] 12. German NJ, Haigis MC. Sirtuins and the Metabolic Hurdles in Cancer. Current Biology 2015; 25: R569-R583. [ DOI:10.1016/j.cub.2015.05.012] 13. Sebastián C, Kyle Satterstrom F, Haigis MC, et al. From Sirtuin Biology to Human Diseases: An Update *. J Biol Chem 2012; 287: 42444-452. [ DOI:10.1074/jbc.R112.402768] 14. Yang W, Nagasawa K, Münch C, et al. Mitochondrial sirtuin network reveals dynamic SIRT3-dependent deacetylation in response to membrane depolarization. Elsevier, (accessed 11 August 2020). 15. Hirschey M, Shimazu T, Goetzman E, et al. SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. nature.com, https://www.nature.com/articles/nature08778 (accessed 11 August 2020). 16. Winnik S, Auwerx J, DS-E heart, et al. Protective effects of sirtuins in cardiovascular diseases: from bench to bedside. academic.oup.com, https://academic.oup.com/eurheartj/article-abstract/36/48/3404/2465994 (accessed 11 August 2020). [ DOI:10.1093/eurheartj/ehv290] 17. Kincaid B, Bossy-Wetzel E. Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration. Frontiers in Aging Neuroscience; 5. Epub ahead of print 2013. [ DOI:10.3389/fnagi.2013.00048] 18. Jeninga E, Schoonjans K, Oncogene JA-, et al. Reversible acetylation of PGC-1: connecting energy sensors and effectors to guarantee metabolic flexibility. nature.com, https://www.nature.com/articles/onc2010206 (accessed 11 August 2020). 19. Kong X, Wang R, Xue Y, et al. Sirtuin 3, a new target of PGC-1α, plays an important role in the suppression of ROS and mitochondrial biogenesis. PLoS One; 5. Epub ahead of print 2010. [ DOI:10.1371/journal.pone.0011707] 20. Palacios O, Carmona J, Michan S, et al. Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle. ncbi.nlm.nih.gov, https://www.ncbi.nlm.nih.gov/pmc/articles/pmc2815736/ (accessed 11 August 2020). 21. Shi T, Wang F, Stieren E, et al. SIRT3, a Mitochondrial Sirtuin Deacetylase, Regulates Mitochondrial Function and Thermogenesis in Brown Adipocytes*. ASBMB. DOI: 10.1074/jbc.M414670200. [ DOI:10.1074/jbc.M414670200] 22. Pillai VB, Sundaresan NR, Kim G, et al. Exogenous NAD Blocks Cardiac Hypertrophic Response via Activation of the SIRT3-LKB1-AMP-activated Kinase Pathway *. NUMBER 5 J Biol Chem 2010; 285: 3133. [ DOI:10.1074/jbc.M109.077271] 23. Ahn B, Kim H, Song S, et al. A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Natl Acad Sci, https://www.pnas.org/content/105/38/14447.short (accessed 12 August 2020). [ DOI:10.1073/pnas.0803790105] 24. Lombard DB, Tishkoff DX, Bao J. Mitochondrial sirtuins in the regulation of mitochondrial activity and metabolic adaptation. Handb Exp Pharmacol 2011; 206: 163-88. [ DOI:10.1007/978-3-642-21631-2_8] 25. Sidorova-Darmos E, Sommer R, Eubanks JH. The role of SIRT3 in the brain under physiological and pathological conditions. Front Cell Neurosci; 12. Epub ahead of print 25 July 2018. [ DOI:10.3389/fncel.2018.00196] 26. Hallows W, Lee S, National JD-P of the, et al. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Natl Acad Sci, https://www.pnas.org/content/103/27/10230.short (accessed 12 August 2020). [ DOI:10.1073/pnas.0604392103] 27. Gurd B, Holloway G, Yoshida Y, et al. In mammalian muscle, SIRT3 is present in mitochondria and not in the nucleus; and SIRT3 is upregulated by chronic muscle contraction in an adenosine. Elsevier, https://www.sciencedirect.com/science/article/pii/S0026049511003180 (accessed 12 August 2020). 28. Nisoli E, Tonello C, Cardile A, et al. Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS. science.sciencemag.org. 29. Cohen H, Miller C, Bitterman K, et al. Survival by Inducing the SIRT1 Deacetylase Calorie Restriction Promotes Mammalian Cell. science.sciencemag.org. Epub ahead of print 2010. DOI: 10.1126/science.1099196. [ DOI:10.1126/science.1099196] 30. Hirschey M, Shimazu T, Jing E, et al. SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome. Elsevier, (accessed 12 August 2020). 31. Haigis M, Mostoslavsky R, Haigis K, et al. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic β cells. Elsevier, (accessed 12 August 2020). 32. Cheng A, Yang Y, Zhou Y, et al. Mitochondrial SIRT3 mediates adaptive responses of neurons to exercise and metabolic and excitatory challenges. Elsevier, (accessed 12 August 2020). 33. Zhang H, Schools G, Lei T, et al. Resveratrol attenuates early pyramidal neuron excitability impairment and death in acute rat hippocampal slices caused by oxygen-glucose deprivation. Elsevier, (accessed 12 August 2020). 34. Karuppagounder S, Pinto J, Xu H, et al. Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer's disease. Elsevier, (accessed 12 August 2020). 35. Timmers S, Konings E, Bilet L, et al. Calorie restriction-like effects of 30 days of resveratrol supplementation on energy metabolism and metabolic profile in obese humans. Elsevier, (accessed 12 August 2020). 36. Menzies KJ, Singh K, Saleem A, et al. Sirtuin 1-mediated Effects of Exercise and Resveratrol on Mitochondrial Biogenesis *. ASBMB. Epub ahead of print 2013. [ DOI:10.1074/jbc.M112.431155] 37. Bagul PK, Katare PB, Bugga P, et al. SIRT-3 Modulation by Resveratrol Improves Mitochondrial Oxidative Phosphorylation in Diabetic Heart through Deacetylation of TFAM. mdpi.com.. 38. Zanto TP, Gazzaley A. Aging of the frontal lobe. In: Handbook of Clinical Neurology. Elsevier B.V., 2019, pp. 369-89. [ DOI:10.1016/B978-0-12-804281-6.00020-3] 39. Wong DW, Soga T, Parhar IS. Aging and chronic administration of serotonin-selective reuptake inhibitor citalopram upregulate Sirt4 gene expression in the preoptic area of male mice. Front Genet; 6. Epub ahead of print 2015. [ DOI:10.3389/fgene.2015.00281] 40. Amirazodi F, Mehrabi A, Amirazodi M, et al. The Combination Effects of Resveratrol and Swimming HIIT Exercise on Novel Object Recognition and Open-field Tasks in Aged Rats. Exp Aging Res 2020; 46: 336-58. [ DOI:10.1080/0361073X.2020.1754015] 41. Walsh RN, Cummins RA. The Open-Field Test: A Critical Review, https://psycnet.apa.org/record/1976-27066-001 (accessed 12 August 2020). 42. Ramos-Filho D, Chicaybam G, De-Souza-Ferreira E, et al. High intensity interval training (HIIT) induces specific changes in respiration and electron leakage in the mitochondria of different rat skeletal muscles. PLoS One; 10. Epub ahead of print 29 June 2015. [ DOI:10.1371/journal.pone.0131766] 43. Shafiee A, Gaeini A, MS-J of A, et al. The effect of eight week of high intensity interval training on expression of mir-210 and ephrinA3 mRNA in soleus muscle healthy male rats. jams.arakmu.ac.ir, http://jams.arakmu.ac.ir/article-1-2770-en.html (accessed 12 August 2020). 44. Iman Fathi, Maryam Noorshahi. Abbas Haghparast HF hoseini. Effect of eight-week aerobic continuous and high intensity interval training on levels of SIRT3 in skeletal muscle tissue of Wistar rats. Physiol Exerc Phys Act 1394; 8: 1277-289. 45. Karvinen S;, Silvennoinen M;, Vainio P;, et al. Effects of intrinsic aerobic capacity, aging and voluntary running on skeletal muscle sirtuins and heat shock proteins. Elsevier. Epub ahead of print 2016. [ DOI:10.1016/j.exger.2016.03.015] 46. Tao R, Vassilopoulos A, Parisiadou L, et al. Regulation of MnSOD enzymatic activity by Sirt3 connects the mitochondrial acetylome signaling networks to aging and carcinogenesis. Antioxidants and Redox Signaling 2014; 20: 1646-654. [ DOI:10.1089/ars.2013.5482] 47. White AT, Schenk S. NAD +/NADH and skeletal muscle mitochondrial adaptations to exercise. American Journal of Physiology - Endocrinology and Metabolism 2012; 303: 308-21. [ DOI:10.1152/ajpendo.00054.2012] 48. Santos-Alves E, Marques-Aleixo I, Rizo-Roca D, et al. Exercise modulates liver cellular and mitochondrial proteins related to quality control signaling. Life Sci 2015; 135: 124-30. [ DOI:10.1016/j.lfs.2015.06.007] 49. Chen T, Li J, Liu J, et al. Activation of SIRT3 by resveratrol ameliorates cardiac fibrosis and improves cardiac function via the TGF-β/smad3 pathway. Am J Physiol - Hear Circ Physiol 2015; 308: 424-34. [ DOI:10.1152/ajpheart.00454.2014] 50. Hawley JA, Joyner MJ, Green DJ. Mimicking exercise: what matters most and where to next? In: Journal of Physiology. Blackwell Publishing Ltd, 2019. Epub ahead of print 2019. 51. Sun Q, Kang R, Chen K, et al. Sirtuin 3 is required for the protective effect of Resveratrol on Manganese‐induced disruption of mitochondrial biogenesis in primary cultured neurons. J Neurochem 2020; jnc.15095. [ DOI:10.1111/jnc.15095] 52. Riccioni G, Gammone MA, Tettamanti G, et al. Resveratrol and anti-atherogenic effects. International Journal of Food Sciences and Nutrition 2015; 66: 603-10. [ DOI:10.3109/09637486.2015.1077796] 53. Muhammad MH, Allam MM. Resveratrol and/or exercise training counteract aging-associated decline of physical endurance in aged mice; targeting mitochondrial biogenesis and function. J Physiol Sci 2018; 68: 681-88. [ DOI:10.1007/s12576-017-0582-4] |
