1. Stefani GP, Baldissera G, Nunes RB, Heck TG, Rhoden CR. Metabolic syndrome and DNA damage: the interplay of environmental and lifestyle factors in the development of metabolic dysfunction. Open J Endocr Metab Dis. 2015;05(07):65–76. [Google Scholar]
2. Pearson-Stuttard J, Zhou B, Kontis V, Bentham J, Gunter MJ, Ezzati M. Worldwide burden of cancer attributable to diabetes and high body-mass index: a comparative risk assessment. Lancet Diabetes Endocrinol. 2018;6(6):e6–e15. [PMC free article] [PubMed] [Google Scholar]
3. Xue R, et al. Hydrogen sulfide treatment promotes glucose uptake by increasing insulin receptor sensitivity and ameliorates kidney lesions in type 2 diabetes. Antioxid Redox Signal. 2013;19(1):5–23. [PMC free article] [PubMed] [Google Scholar]
4. Fogelholm M, et al. PREVIEW: prevention of diabetes through lifestyle intervention and population studies in Europe and around the world. Design, methods, and baseline participant description of an adult cohort enrolled into a three-year randomised clinical trial. Nutrients. 2017;9(6):632. [PMC free article] [PubMed] [Google Scholar]
5. Maeda A, et al. piperine promotes glucose uptake through ROS-dependent activation of the CAMKK/AMPK signaling pathway in skeletal muscle. Mol Nutr Food Res. 2018;62(11):1–11. [PubMed] [Google Scholar]
6. Lin SC, Hardie DG. AMPK: sensing glucose as well as cellular energy status. Cell Metab. 2018;27(2):299–313. [PubMed] [Google Scholar]
7. Hardie DG. AMPK: positive and negative regulation, and its role in whole-body energy homeostasis. Curr Opin Cell Biol. 2015;33:1–7. [PubMed] [Google Scholar]
8. Duan J, et al. Protective effect of butin against ischemia/reperfusion-induced myocardial injury in diabetic mice: involvement of the AMPK/GSK-3β/Nrf2 signaling pathway. Sci Rep. 2017;7:1–14. [PMC free article] [PubMed] [Google Scholar]
9. Liu Z-J, et al. OGG1 involvement in high glucose-mediated enhancement of bupivacaine-induced oxidative DNA damage in SH-SY5Y cells. Oxid Med Cell Longev. 2015;2015:1–11. [PMC free article] [PubMed] [Google Scholar]
10. Algire C, et al. Metformin reduces endogenous reactive oxygen species and associated DNA damage. Cancer Prev Res. 2012;5(4):536–543. [PubMed] [Google Scholar]
11. Hardie DG, Schaffer BE, Brunet A. AMPK: an energy-sensing pathway with multiple inputs and outputs. Trends Cell Biol. 2016;26(3):190–201. [PMC free article] [PubMed] [Google Scholar]
12. Hardie DG. AMPK—sensing energy while talking to other signaling pathways. Cell Metab. 2014;20(6):939–952. [PMC free article] [PubMed] [Google Scholar]
13. Towler MC, Hardie DG. AMP-activated protein kinase in metabolic control and insulin signaling. Circ Res. 2007;100(3):328–341. [PubMed] [Google Scholar]
14. McBride A, Hardie DG. AMP-activated protein kinase—a sensor of glycogen as well as AMP and ATP? Acta Physiol. 2009;196(1):99–113. [PubMed] [Google Scholar]
15. Cheung PCF. Charasterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding. Biochem J. 2000;346:659–669. [PMC free article] [PubMed] [Google Scholar]
16. Gu X, et al. Deconvoluting AMP-activated protein kinase (AMPK) adenine nucleotide binding and sensing. J Biol Chem. 2017;292(30):12653–12666. [PMC free article] [PubMed] [Google Scholar]
17. Bateman A. The structure of a domain common to archaebacteria and the hom*ocystinuria disease protein. Trends Biochem Sci. 1997;22(1):12–13. [PubMed] [Google Scholar]
18. Morales-Alamo D, Calbet JAL. AMPK signaling in skeletal muscle during exercise: Role of reactive oxygen and nitrogen species. Free Radic Biol Med. 2016;98:68–77. [PubMed] [Google Scholar]
19. Xiao B, et al. Structure of mammalian AMPK and its regulation by ADP. Nature. 2011;472(7342):230–233. [PMC free article] [PubMed] [Google Scholar]
20. Hardie DG. Role of AMP-activated protein kinase in the metabolic syndrome and in heart disease. FEBS Lett. 2008;582(1):81–89. [PubMed] [Google Scholar]
21. Hawley SA, et al. Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J Biol. 2003;2(4):28. [PMC free article] [PubMed] [Google Scholar]
22. Hawley SA, Edelman AM, Carling D, Selbert MA, Hardie DG, Goldstein EG. 5′-AMP activates the AMP-activated protein kinase cascade, and Ca 2+ /calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. J Biol Chem. 1995;270(45):27186–27191. [PubMed] [Google Scholar]
23. Davies SP, Helps NR, Cohen PTW, Hardie DG. 5′-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2Cα and native bovine protein phosphatase-2Ac. FEBS Lett. 1995;377(3):421–425. [PubMed] [Google Scholar]
24. Hardie DG, Carling D, Gamblin SJ. AMP-activated protein kinase: also regulated by ADP? Trends Biochem Sci. 2011;36(9):470–477. [PubMed] [Google Scholar]
25. Chen X, et al. The role of sodium hydrosulfide in attenuating the aging process via PI3K/AKT and CaMKKβ/AMPK pathways. Redox Biol. 2017;12(April):987–1003. [PMC free article] [PubMed] [Google Scholar]
26. Hawley SA, et al. Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase. Cell Metab. 2005;2(1):9–19. [PubMed] [Google Scholar]
27. Leclerc GM, Leclerc GJ, Fu G, Barredo JC. AMPK-induced activation of Akt by AICAR is mediated by IGF-1R dependent and independent mechanisms in acute lymphoblastic leukemia. J Mol Signal. 2010;5:1–13. [PMC free article] [PubMed] [Google Scholar]
28. Inoue E, Yamauchi J. AMP-activated protein kinase regulates PEPCK gene expression by direct phosphorylation of a novel zinc finger transcription factor. Biochem Biophys Res Commun. 2006;351(4):793–799. [PubMed] [Google Scholar]
29. Hunter RW, et al. Metformin reduces liver glucose production by inhibition of fructose-1-6-bisphosphatase. Nat Med. 2018;24:1395–1406. [PMC free article] [PubMed] [Google Scholar]
30. Logie L, Zoe M, Allwood JW, Mcdougall G, Beall C, Rena G. Regulation of hepatic glucose production and AMPK by AICAR but not by metformin depends on drug uptake through the equilibrative nucleoside transporter 1 (ENT1) Diabetes Obes Metab. 2018;20:2748–2758. [PMC free article] [PubMed] [Google Scholar]
31. Göransson O, et al. Mechanism of action of A-769662, a valuable tool for activation of AMP-activated protein kinase. J Biol Chem. 2007;282(45):32549–32560. [PMC free article] [PubMed] [Google Scholar]
32. Lee SH, Mantzoros C, Kim YB. Resveratrol: is selectivity opening the key to therapeutic effects? Metabolism. 2012;61(3):289–290. [PubMed] [Google Scholar]
33. Howell JJ, et al. Metformin inhibits hepatic mTORC1 signaling via dose-dependent mechanisms involving AMPK and the TSC complex. Cell Metab. 2017;25(2):463–471. [PMC free article] [PubMed] [Google Scholar]
34. Kang C, Kim E. Synergistic effect of curcumin and insulin on muscle cell glucose metabolism. Food Chem Toxicol. 2010;48(8–9):2366–2373. [PubMed] [Google Scholar]
35. Tsuda S, Egawa T, Ma X, Oshima R, Kurogi E, Hayashi T. Coffee polyphenol caffeic acid but not chlorogenic acid increases 5’AMP-activated protein kinase and insulin-independent glucose transport in rat skeletal muscle. J Nutr Biochem. 2012;23(11):1403–1409. [PubMed] [Google Scholar]
36. Reiter CEN, Kim JA, Quon MJ. Green tea polyphenol epigallocatechin gallate reduces endothelin-1 expression and secretion in vascular endothelial cells: roles for AMP-activated protein kinase, Akt, and FOXO1. Endocrinology. 2010;151(1):103–114. [PMC free article] [PubMed] [Google Scholar]
37. Cairns RA, Harris IS, Mak TW. Regulation of cancer cell metabolism. Nat Rev Cancer. 2011;11(2):85–95. [PubMed] [Google Scholar]
38. Jones RG, Thompson CB. Tumor suppressors and cell metabolism: a recipe for cancer growth. Genes Dev. 2009;23(5):537–548. [PMC free article] [PubMed] [Google Scholar]
39. Lage R, Diéguez C, Vidal-Puig A, López M. AMPK: a metabolic gauge regulating whole-body energy homeostasis. Trends Mol Med. 2008;14(12):539–549. [PubMed] [Google Scholar]
40. Fijałkowski F, Jarzyna R. Rola podwzgórzowej kinazy białkowej aktywowanej przez AMP w kontroli pobierania pokarmu Role of hypothalamic AMP-activated protein kinase in the control of food intake. Postepy Hig Med Dosw. 2010;64:231–243. [PubMed] [Google Scholar]
41. Simone S, Gorin Y, Velagapudi C, Abboud HE, Habib SL. Mechanism of oxidative DNA damage in diabetes tuberin inactivation and downregulation of DNA repair enzyme 8-Oxo-7,8-dihydro-2J-deoxyguanosine-DNA glycosylase OBJECTIVE—to investigate potential mechanisms of oxidative DNA damage in a rat model of type 1 d. Diabetes. 2008;57:2626–2636. [PMC free article] [PubMed] [Google Scholar]
42. Cao Y, et al. Interaction of FoxO1 and TSC2 induces insulin resistance through activation of the mammalian target of rapamycin/p70 S6K pathway. J Biol Chem. 2006;281(52):40242–40251. [PubMed] [Google Scholar]
43. Zhao Y, et al. ROS signaling under metabolic stress: cross-talk between AMPK and AKT pathway. Mol Cancer. 2017;16(79):1–12. [PMC free article] [PubMed] [Google Scholar]
44. Zhang Y, Chen J, Zeng Y, Huang D, Xu Q. Biomedicine & pharmacotherapy involvement of AMPK activation in the inhibition of hepatic gluconeogenesis by Ficus carica leaf extract in diabetic mice and HepG2 cells. Biome Pharmacother. 2019;109:188–194. [PubMed] [Google Scholar]
45. Na R-S, Ma C, Liu Q-R, Wu L-M, Zheng X-L, Liu Z-W. Itraconazole attenuates hepatic gluconeogenesis and promotes glucose uptake by regulating AMPK pathway. Exp Ther Med. 2018;15:2165–2171. [PMC free article] [PubMed] [Google Scholar]
46. Qi X, et al. Follicle-stimulating hormone enhances hepatic gluconeogenesis by GRK2-mediated AMPK hyperphosphorylation at Ser485 in mice. Diabetologia. 2018;61(324):1180–1192. [PubMed] [Google Scholar]
47. Marsin AS, et al. Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia. Curr Biol. 2000;10(20):1247–1255. [PubMed] [Google Scholar]
48. Wu S-B, Wei Y-H. AMPK-mediated increase of glycolysis as an adaptive response to oxidative stress in human cells: Implication of the cell survival in mitochondrial diseases. Biochim Biophys Acta Mol Basis Dis. 2012;1822(2):233–247. [PubMed] [Google Scholar]
49. Hutton JC, O’Brien RM. Glucose-6-phosphatase catalytic subunit gene family. J Biol Chem. 2009;284(43):29241–29245. [PMC free article] [PubMed] [Google Scholar]
50. Carling D. Branching out on AMPK regulation. Cell Metab. 2009;9(1):7–8. [PubMed] [Google Scholar]
51. Janzen NR, Whitfield J, Hoffman NJ. Interactive roles for AMPK and glycogen from cellular energy sensing to exercise metabolism. Int. J. Mol. Sci. 2018;19(11):3344. [PMC free article] [PubMed] [Google Scholar]
52. Hardie DG, Pan DA. Regulation of fatty acid synthesis and oxidation by the AMP-activated protein kinase. Biochem Soc Trans. 2002;30(Pt 6):1064–1070. [PubMed] [Google Scholar]
53. Sambandam N, Lopaschuk GD. AMP-activated protein kinase (AMPK) control of fatty acid and glucose metabolism in the ischemic heart. Prog Lipid Res. 2003;42(3):238–256. [PubMed] [Google Scholar]
54. Gaussin V, Ching YP, Hue L, Skarlas P, Hardie DG. Distinct type-2A protein phosphatases activate HMGCoA reductase and acetyl-CoA carboxylase in liver. FEBS Lett. 1997;413(1):115–118. [PubMed] [Google Scholar]
55. Maier T, Leibundgut M, Ban N. The crystal structure of a mammalian fatty acid synthase. Science. 2008;321(5894):1315–1322. [PubMed] [Google Scholar]
56. Asturias FJ, et al. Structure and molecular organization of mammalian fatty acid synthase. Nat Struct Mol Biol. 2005;12(3):225–232. [PubMed] [Google Scholar]
57. Smith S, Witkowski A, Joshi AK. Structural and functional organization of the animal fatty acid synthase. Prog Lipid Res. 2003;42(4):289–317. [PubMed] [Google Scholar]
58. Salminen A, Kaarniranta K. AMP-activated protein kinase (AMPK) controls the aging process via an integrated signaling network. Ageing Res Rev. 2012;11(2):230–241. [PubMed] [Google Scholar]
59. Greer EL, et al. An AMPK-FOXO pathway mediates longevity induced by a novel method of dietary restriction in C. elegans. Curr Biol. 2007;17(19):1646–1656. [PMC free article] [PubMed] [Google Scholar]
60. Luo Z, et al. AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice. Cell Metab. 2011;13(4):376–388. [PMC free article] [PubMed] [Google Scholar]
61. Liangpunsakul S, Zeng Y, Lu C, Sozio MS, Crabb DW. Activated AMPK inhibits PPAR-α and PPAR-γ transcriptional activity in hepatoma cells. Am J Physiol Liver Physiol. 2011;301(4):G739–G747. [PMC free article] [PubMed] [Google Scholar]
62. Kang SWS, et al. AMPK activation prevents and reverses drug-induced mitochondrial and hepatocyte injury by promoting mitochondrial fusion and function. PLoS ONE. 2016;11(10):e0165638. [PMC free article] [PubMed] [Google Scholar]
63. Dorn GW, Vega RB, Kelly DP. Mitochondrial biogenesis and dynamics in the developing and diseased heart. Genes Dev. 2015;29(19):1981–1991. [PMC free article] [PubMed] [Google Scholar]
64. Yakes FM, Van Houten B. Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress. Proc Natl Acad Sci. 1997;94(2):514–519. [PMC free article] [PubMed] [Google Scholar]
65. Farmer T, Naslavsky N, Caplan S. Tying trafficking to fusion and fission at the mighty mitochondria. Traffic. 2018;19(8):569–577. [PMC free article] [PubMed] [Google Scholar]
66. Toyama EQ, et al. AMP-activated protein kinase mediates mitochondrial fission in response to energy stress. Science. 2016;351(6270):275–282. [PMC free article] [PubMed] [Google Scholar]
67. Smart DJ, Chipman JK, Hodges NJ. Activity of OGG1 variants in the repair of pro-oxidant-induced 8-oxo-2′-deoxyguanosine. DNA Repair (Amst) 2006;5(11):1337–1345. [PubMed] [Google Scholar]
68. Li X, Imlay JA. Improved measurements of scant hydrogen peroxide enable experiments that define its threshold of toxicity for Escherichia coli. Free Radic Biol Med. 2018;120:217–227. [PMC free article] [PubMed] [Google Scholar]
69. Gruber CC, Walker GC. Incomplete base excision repair contributes to cell death from antibiotics and other stresses. DNA Repair (Amst) 2018;71:108–117. [PMC free article] [PubMed] [Google Scholar]
70. Eastman A, Barry MA. The origins of DNA breaks: a consequence of DNA damage. Cancer Investig. 1992;10:229–240. [PubMed] [Google Scholar]
71. Imlay JA. The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium. Nat Rev Microbiol. 2013;11(7):443–454. [PMC free article] [PubMed] [Google Scholar]
72. Marnett LJ. Oxyradicals and DNA damage. Carcinogenesis. 2000;21(3):361–370. [PubMed] [Google Scholar]
73. Habib SL, Yadav A, Kidane D, Weiss RH, Liang S. Novel protective mechanism of reducing renal cell damage in diabetes: activation AMPK by AICAR increased NRF2/OGG1 proteins and reduced oxidative DNA damage. Cell Cycle. 2016;15(22):3048–3059. [PMC free article] [PubMed] [Google Scholar]
74. Woyda-Płoszczyca A, Jarmuszkiewicz W. Udział białek rozprzęgających w modulacji funkcji mitochondriów—perspektywy terapeutyczne. Postepy Biochem. 2008;54(2):188–197. [PubMed] [Google Scholar]
75. Eid HM, Vallerand D, Muhammad A, Durst T, Haddad PS, Martineau LC. Structural constraints and the importance of lipophilicity for the mitochondrial uncoupling activity of naturally occurring caffeic acid esters with potential for the treatment of insulin resistance. Biochem Pharmacol. 2010;79(3):444–454. [PubMed] [Google Scholar]
76. Finkel T. Signal transduction by reactive oxygen species. J Cell Biol. 2011;194(1):7–15. [PMC free article] [PubMed] [Google Scholar]
77. Ducommun S, et al. Motif af fi nity and mass spectrometry proteomic approach for the discovery of cellular AMPK targets: identification of mitochondrial fi ssion factor as a new AMPK substrate. Cell Signal. 2015;27(5):978–988. [PubMed] [Google Scholar]
78. Zheng Q, et al. Iron overload promotes mitochondrial fragmentation in mesenchymal stromal cells from myelodysplastic syndrome patients through activation of the AMPK/MFF/Drp1 pathway. Cell Death Dis. 2018;9:1–12. [PMC free article] [PubMed] [Google Scholar]
79. Zheng L, et al. Mitochondrial phosphoenolpyruvate carboxykinase regulates osteogenic differentiation by modulating AMPK/ULK1-dependent autophagy. Stem Cells J. 2019;37:1542–1555. [PMC free article] [PubMed] [Google Scholar]
80. Jang JE, et al. AMPK–ULK1-mediated autophagy confers resistance to BET inhibitor JQ1 in acute myeloid leukemia stem cells. Clin Cancer Res. 2017;4(19):2781–2795. [PubMed] [Google Scholar]
81. Laker RC, et al. Ampk phosphorylation of Ulk1 is required for targeting of mitochondria to lysosomes in exerciseinduced mitophagy. Nat Commun. 2017;8:1–13. [PMC free article] [PubMed] [Google Scholar]
82. Russell RC, et al. ULK1 induces autophagy by phosphorylating Beclin-1 and activating Vps34 lipid kinase. Nat Cell Biol. 2013;15(7):741–750. [PMC free article] [PubMed] [Google Scholar]
83. Alexander A, Walker CL. The role of LKB1 and AMPK in cellular responses to stress and damage. FEBS Lett. 2011;585(7):952–957. [PubMed] [Google Scholar]
84. Mihaylova MM, Shaw RJ. The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. Nat Cell Biol. 2011;13(9):1016–1023. [PMC free article] [PubMed] [Google Scholar]
85. Martina JA, et al. MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy. 2012;8(6):903–917. [PMC free article] [PubMed] [Google Scholar]
86. Li J, Han YR, Plummer MR, Herrup K. Cytoplasmic ATM in neurons modulates synaptic function. Curr Biol. 2009;19(24):2091–2096. [PMC free article] [PubMed] [Google Scholar]
87. Shen K, Wang Y, Brooks SC, Raz A, Wang YA. ATM is activated by mitotic stress and suppresses centrosome amplification in primary but not in tumor cells. J Cell Biochem. 2006;99(5):1267–1274. [PubMed] [Google Scholar]
88. Ui A, et al. Possible involvement of LKB1-AMPK signaling in non-hom*ologous end joining. Oncogene. 2014;33(13):1640–1648. [PMC free article] [PubMed] [Google Scholar]
89. Chung JH. The role of DNA-PK in aging and energy metabolism. FEBS J. 2018;285(11):1959–1972. [PMC free article] [PubMed] [Google Scholar]
90. Tian X, Seluanov A, Gorbunova V. Beyond making ends meet: DNA-PK, metabolism, and aging. Cell Metab. 2017;25(5):991–992. [PubMed] [Google Scholar]
91. Park SJ, et al. DNA-PK promotes the mitochondrial, metabolic, and physical decline that occurs during aging. Cell Metab. 2017;25(5):1135–1146.e7. [PMC free article] [PubMed] [Google Scholar]
92. Choi YJ, et al. Deletion of individual Ku subunits in mice causes an NHEJ-independent phenotype potentially by altering apurinic/apyrimidinic site repair. PLoS ONE. 2014;9(1):1–9. [PMC free article] [PubMed] [Google Scholar]
93. Torres-Gonzalez M, Gawlowski T, Kocalis H, Scott BT, Dillmann WH, Wh D. Mitochondrial 8-oxoguanine glycosylase decreases mitochondrial fragmentation and improves mitochondrial function in H9C2 cells under oxidative stress conditions. Am J Physiol Cell Physiol. 2018;306(3):C221–C229. [PMC free article] [PubMed] [Google Scholar]
94. Carter RJ, Parsons JL. Base excision repair, a pathway regulated by posttranslational modifications. Mol Cell Biol. 2016;36(10):1426–1437. [PMC free article] [PubMed] [Google Scholar]
95. Roos WP, Thomas AD, Kaina B. DNA damage and the balance between survival and death in cancer biology. Nat Rev Cancer. 2016;16(1):20–33. [PubMed] [Google Scholar]
96. Huang Q, Shen HM. To die or to live: the dual role of poly(ADP-ribose) polymerase-1 in autophagy and necrosis under oxidative stress and DNA damage. Autophagy. 2009;5(2):273–276. [PubMed] [Google Scholar]
97. Godon C, et al. PARP inhibition versus PARP-1 silencing: different outcomes in terms of single-strand break repair and radiation susceptibility. Nucleic Acids Res. 2008;36(13):4454–4464. [PMC free article] [PubMed] [Google Scholar]
98. Chen LY, Wang Y, Terkeltaub R, Liu-Bryan R. Activation of AMPK-SIRT3 signaling is chondroprotective by preserving mitochondrial DNA integrity and function. Osteoarthr Cartil. 2018;26(11):1539–1550. [PMC free article] [PubMed] [Google Scholar]
99. De Souza-Pinto NC, et al. Repair of 8-oxodeoxyguanosine lesions in mitochondrial DNA depends on the oxoguanine DNA glycosylase (OGG1) gene and 8-oxoguanine accumulates in the mitochondrial DNA of OGG1-defective mice. Cancer Res. 2001;61(14):5378–5381. [PubMed] [Google Scholar]
100. Liu-Bryan R, Wang Y, Terkeltaub R. AMP-activated protein kinase (AMPK) limits mitochondrial DNA damage in human knee OA chondrocytes by upregulation of SIRT3 and the DNA repair enzyme OGG1. Osteoarthr Cartil. 2015;23(2015):A157–A158. [Google Scholar]
101. Hou X, Zeng H, He X, Chen JX. Sirt3 is essential for apelin-induced angiogenesis in post-myocardial infarction of diabetes. J Cell Mol Med. 2015;19(1):53–61. [PMC free article] [PubMed] [Google Scholar]
102. Jing E, et al. Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production. Proc Natl Acad Sci. 2011;108(35):14608–14613. [PMC free article] [PubMed] [Google Scholar]
103. Bagul P, Katare P, Banerjee SK, Dinda A, Bugga P. SIRT-3 modulation by resveratrol improves mitochondrial oxidative phosphorylation in diabetic heart through deacetylation of TFAM. Cells. 2018;7(12):235. [PMC free article] [PubMed] [Google Scholar]
104. Habib SL, Kasinath BS, Arya RR, Vexler S, Velagapudi C. Novel mechanism of reducing tumourigenesis: upregulation of the DNA repair enzyme OGG1 by rapamycin-mediated AMPK activation and mTOR inhibition. Eur J Cancer. 2010;46(15):2806–2820. [PubMed] [Google Scholar]
