1. Population Division, Department of Economic and Social Affairs, United Nations. World population aging 2019 highlights. New York: United Nations;2019. p. 11–4.
2. Kim G, Kim JH. Impact of skeletal muscle mass on metabolic health. Endocrinol Metab (Seoul). 2020; 35:1–6.
Article
3. Jung HW. Visualizing domains of comprehensive geriatric assessments to grasp frailty spectrum in older adults with a radar chart. Ann Geriatr Med Res. 2020; 24:55–6.
Article
4. Cruz-Jentoft AJ, Sayer AA. Sarcopenia. Lancet. 2019; 393:2636–46.
Article
5. Chen X, Mao G, Leng SX. Frailty syndrome: an overview. Clin Interv Aging. 2014; 9:433–41.
6. Anker SD, Morley JE, von Haehling S. Welcome to the ICD-10 code for sarcopenia. J Cachexia Sarcopenia Muscle. 2016; 7:512–4.
Article
7. Baumgartner RN, Koehler KM, Gallagher D, Romero L, Heymsfield SB, Ross RR, et al. Epidemiology of sarcopenia among the elderly in New Mexico. Am J Epidemiol. 1998; 147:755–63.
Article
8. Lauretani F, Russo CR, Bandinelli S, Bartali B, Cavazzini C, Di Iorio A, et al. Age-associated changes in skeletal muscles and their effect on mobility: an operational diagnosis of sarcopenia. J Appl Physiol (1985). 2003; 95:1851–60.
Article
9. Cruz-Jentoft AJ, Baeyens JP, Bauer JM, Boirie Y, Cederholm T, Landi F, et al. Sarcopenia: European consensus on definition and diagnosis. Report of the European Working Group on sarcopenia in older people. Age Ageing. 2010; 39:412–23.
Article
10. Cruz-Jentoft AJ, Bahat G, Bauer J, Boirie Y, Bruyere O, Cederholm T, et al. Sarcopenia: revised European consensus on definition and diagnosis. Age Ageing. 2019; 48:16–31.
Article
11. Chen LK, Woo J, Assantachai P, Auyeung TW, Chou MY, Iijima K, et al. Asian Working Group for sarcopenia: 2019 consensus update on sarcopenia diagnosis and treatment. J Am Med Dir Assoc. 2020; 21:300–7.
Article
12. Fielding RA, Vellas B, Evans WJ, Bhasin S, Morley JE, Newman AB, et al. Sarcopenia: an undiagnosed condition in older adults. Current consensus definition: prevalence, etiology, and consequences. International Working Group on Sarcopenia. J Am Med Dir Assoc. 2011; 12:249–56.
Article
13. McLean RR, Kiel DP. Developing consensus criteria for sarcopenia: an update. J Bone Miner Res. 2015; 30:588–92.
Article
14. Iannuzzi-Sucich M, Prestwood KM, Kenny AM. Prevalence of sarcopenia and predictors of skeletal muscle mass in healthy, older men and women. J Gerontol A Biol Sci Med Sci. 2002; 57:M772–7.
Article
15. Liu X, Hao Q, Hou L, Xia X, Zhao W, Zhang Y, et al. Ethnic groups differences in the prevalence of sarcopenia using the AWGS criteria. J Nutr Health Aging. 2020; 24:665–71.
Article
16. Pacifico J, Geerlings MAJ, Reijnierse EM, Phassouliotis C, Lim WK, Maier AB. Prevalence of sarcopenia as a comorbid disease: a systematic review and meta-analysis. Exp Gerontol. 2020; 131:110801.
Article
17. Cuthbertson D, Smith K, Babraj J, Leese G, Waddell T, Atherton P, et al. Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. FASEB J. 2005; 19:422–4.
Article
18. Kim IY, Park S, Jang J, Wolfe RR. Understanding muscle protein dynamics: technical considerations for advancing sarcopenia research. Ann Geriatr Med Res. 2020; 24:157–65.
Article
19. Timmerman KL, Lee JL, Fujita S, Dhanani S, Dreyer HC, Fry CS, et al. Pharmacological vasodilation improves insulin-stimulated muscle protein anabolism but not glucose utilization in older adults. Diabetes. 2010; 59:2764–71.
Article
20. Colleluori G, Aguirre L, Phadnis U, Fowler K, Armamento-Villareal R, Sun Z, et al. Aerobic plus resistance exercise in obese older adults improves muscle protein synthesis and preserves myocellular quality despite weight loss. Cell Metab. 2019; 30:261–73.
Article
21. Moore DR, Churchward-Venne TA, Witard O, Breen L, Burd NA, Tipton KD, et al. Protein ingestion to stimulate myofibrillar protein synthesis requires greater relative protein intakes in healthy older versus younger men. J Gerontol A Biol Sci Med Sci. 2015; 70:57–62.
Article
22. Funai K, Parkington JD, Carambula S, Fielding RA. Age-associated decrease in contraction-induced activation of downstream targets of Akt/mTor signaling in skeletal muscle. Am J Physiol Regul Integr Comp Physiol. 2006; 290:R1080–6.
Article
23. Talbot J, Maves L. Skeletal muscle fiber type: using insights from muscle developmental biology to dissect targets for susceptibility and resistance to muscle disease. Wiley Interdiscip Rev Dev Biol. 2016; 5:518–34.
Article
24. Lexell J. Human aging, muscle mass, and fiber type composition. J Gerontol A Biol Sci Med Sci. 1995; 50(Spec No):11–6.
25. Nilwik R, Snijders T, Leenders M, Groen BB, van Kranenburg J, Verdijk LB, et al. The decline in skeletal muscle mass with aging is mainly attributed to a reduction in type II muscle fiber size. Exp Gerontol. 2013; 48:492–8.
Article
26. Short KR, Vittone JL, Bigelow ML, Proctor DN, Coenen-Schimke JM, Rys P, et al. Changes in myosin heavy chain mRNA and protein expression in human skeletal muscle with age and endurance exercise training. J Appl Physiol (1985). 2005; 99:95–102.
Article
27. Klitgaard H, Zhou M, Schiaffino S, Betto R, Salviati G, Saltin B. Ageing alters the myosin heavy chain composition of single fibres from human skeletal muscle. Acta Physiol Scand. 1990; 140:55–62.
Article
28. Lexell J, Downham DY. The occurrence of fibre-type grouping in healthy human muscle: a quantitative study of cross-sections of whole vastus lateralis from men between 15 and 83 years. Acta Neuropathol. 1991; 81:377–81.
Article
29. Wallace DC. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu Rev Genet. 2005; 39:359–407.
Article
30. Spinelli JB, Haigis MC. The multifaceted contributions of mitochondria to cellular metabolism. Nat Cell Biol. 2018; 20:745–54.
Article
31. Chan DC. Mitochondria: dynamic organelles in disease, aging, and development. Cell. 2006; 125:1241–52.
Article
32. Lopez-Otin C, Blasco MA, Partridge L, Serrano M, Kroemer G. The hallmarks of aging. Cell. 2013; 153:1194–217.
Article
33. Chabi B, Ljubicic V, Menzies KJ, Huang JH, Saleem A, Hood DA. Mitochondrial function and apoptotic susceptibility in aging skeletal muscle. Aging Cell. 2008; 7:2–12.
Article
34. Lin MT, Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature. 2006; 443:787–95.
Article
35. Migliavacca E, Tay SKH, Patel HP, Sonntag T, Civiletto G, McFarlane C, et al. Mitochondrial oxidative capacity and NAD+ biosynthesis are reduced in human sarcopenia across ethnicities. Nat Commun. 2019; 10:5808.
Article
36. Rygiel KA, Picard M, Turnbull DM. The ageing neuromuscular system and sarcopenia: a mitochondrial perspective. J Physiol. 2016; 594:4499–512.
Article
37. Lundt S, Zhang N, Wang X, Polo-Parada L, Ding S. The effect of NAMPT deletion in projection neurons on the function and structure of neuromuscular junction (NMJ) in mice. Sci Rep. 2020; 10:99.
Article
38. Scarpulla RC, Vega RB, Kelly DP. Transcriptional integration of mitochondrial biogenesis. Trends Endocrinol Metab. 2012; 23:459–66.
Article
39. Sun N, Youle RJ, Finkel T. The mitochondrial basis of aging. Mol Cell. 2016; 61:654–66.
Article
40. Masiero E, Agatea L, Mammucari C, Blaauw B, Loro E, Komatsu M, et al. Autophagy is required to maintain muscle mass. Cell Metab. 2009; 10:507–15.
Article
41. Pyo JO, Yoo SM, Ahn HH, Nah J, Hong SH, Kam TI, et al. Overexpression of Atg5 in mice activates autophagy and extends lifespan. Nat Commun. 2013; 4:2300.
Article
42. Ryu D, Mouchiroud L, Andreux PA, Katsyuba E, Moullan N, Nicolet-Dit-Felix AA, et al. Urolithin A induces mitophagy and prolongs lifespan in C. elegans and increases muscle function in rodents. Nat Med. 2016; 22:879–88.
Article
43. Andreux PA, Blanco-Bose W, Ryu D, Burdet F, Ibberson M, Aebischer P, et al. The mitophagy activator urolithin A is safe and induces a molecular signature of improved mitochondrial and cellular health in humans. Nat Metab. 2019; 1:595–603.
Article
44. Fang EF, Hou Y, Palikaras K, Adriaanse BA, Kerr JS, Yang B, et al. Mitophagy inhibits amyloid-β and tau pathology and reverses cognitive deficits in models of Alzheimer’s disease. Nat Neurosci. 2019; 22:401–12.
Article
45. Eisenberg T, Abdellatif M, Schroeder S, Primessnig U, Stekovic S, Pendl T, et al. Cardioprotection and lifespan extension by the natural polyamine spermidine. Nat Med. 2016; 22:1428–38.
Article
46. Katsyuba E, Romani M, Hofer D, Auwerx J. NAD+ homeostasis in health and disease. Nat Metab. 2020; 2:9–31.
Article
47. Gomes AP, Price NL, Ling AJ, Moslehi JJ, Montgomery MK, Rajman L, et al. Declining NAD(+) induces a pseudohypoxic state disrupting nuclear-mitochondrial communication during aging. Cell. 2013; 155:1624–38.
Article
48. Camacho-Pereira J, Tarrago MG, Chini CCS, Nin V, Escande C, Warner GM, et al. CD38 dictates age-related NAD decline and mitochondrial dysfunction through an SIRT3-dependent mechanism. Cell Metab. 2016; 23:1127–39.
Article
49. Frederick DW, Loro E, Liu L, Davila A Jr, Chellappa K, Silverman IM, et al. Loss of NAD homeostasis leads to progressive and reversible degeneration of skeletal muscle. Cell Metab. 2016; 24:269–82.
Article
50. Goody MF, Henry CA. A need for NAD+ in muscle development, homeostasis, and aging. Skelet Muscle. 2018; 8:9.
Article
51. Zhang H, Ryu D, Wu Y, Gariani K, Wang X, Luan P, et al. NAD+ repletion improves mitochondrial and stem cell function and enhances life span in mice. Science. 2016; 352:1436–43.
Article
52. Kang BE, Choi JY, Stein S, Ryu D. Implications of NAD+ boosters in translational medicine. Eur J Clin Invest. 2020; 50:e13334.
53. Elhassan YS, Kluckova K, Fletcher RS, Schmidt MS, Garten A, Doig CL, et al. Nicotinamide riboside augments the aged human skeletal muscle NAD+ metabolome and induces transcriptomic and anti-inflammatory signatures. Cell Rep. 2019; 28:1717–28.
Article
54. Tarrago MG, Chini CCS, Kanamori KS, Warner GM, Caride A, de Oliveira GC, et al. A potent and specific CD38 inhibitor ameliorates age-related metabolic dysfunction by reversing tissue NAD+ decline. Cell Metab. 2018; 27:1081–95.
Article
55. Ryu D, Zhang H, Ropelle ER, Sorrentino V, Mazala DA, Mouchiroud L, et al. NAD+ repletion improves muscle function in muscular dystrophy and counters global PARylation. Sci Transl Med. 2016; 8:361ra139.
56. Claflin DR, Jackson MJ, Brooks SV. Age affects the contraction-induced mitochondrial redox response in skeletal muscle. Front Physiol. 2015; 6:21.
Article
57. Lee SJ. Regulation of muscle mass by myostatin. Annu Rev Cell Dev Biol. 2004; 20:61–86.
Article
58. McPherron AC, Lawler AM, Lee SJ. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature. 1997; 387:83–90.
Article
59. Amthor H, Macharia R, Navarrete R, Schuelke M, Brown SC, Otto A, et al. Lack of myostatin results in excessive muscle growth but impaired force generation. Proc Natl Acad Sci U S A. 2007; 104:1835–40.
Article
60. Schuelke M, Wagner KR, Stolz LE, Hubner C, Riebel T, Komen W, et al. Myostatin mutation associated with gross muscle hypertrophy in a child. N Engl J Med. 2004; 350:2682–8.
Article
61. Hansen J, Brandt C, Nielsen AR, Hojman P, Whitham M, Febbraio MA, et al. Exercise induces a marked increase in plasma follistatin: evidence that follistatin is a contraction-induced hepatokine. Endocrinology. 2011; 152:164–71.
Article
62. Chang YC, Liu HW, Chan YC, Hu SH, Liu MY, Chang SJ. The green tea polyphenol epigallocatechin-3-gallate attenuates age-associated muscle loss via regulation of miR-486–5p and myostatin. Arch Biochem Biophys. 2020; 692:108511.
Article
63. Bergen HR 3rd, Farr JN, Vanderboom PM, Atkinson EJ, White TA, Singh RJ, et al. Myostatin as a mediator of sarcopenia versus homeostatic regulator of muscle mass: insights using a new mass spectrometry-based assay. Skelet Muscle. 2015; 5:21.
Article
64. Yarasheski KE, Bhasin S, Sinha-Hikim I, Pak-Loduca J, Gonzalez-Cadavid NF. Serum myostatin-immunoreactive protein is increased in 60–92 year old women and men with muscle wasting. J Nutr Health Aging. 2002; 6:343–8.
65. Ratkevicius A, Joyson A, Selmer I, Dhanani T, Grierson C, Tommasi AM, et al. Serum concentrations of myostatin and myostatin-interacting proteins do not differ between young and sarcopenic elderly men. J Gerontol A Biol Sci Med Sci. 2011; 66:620–6.
Article
66. Hofmann M, Halper B, Oesen S, Franzke B, Stuparits P, Tschan H, et al. Serum concentrations of insulin-like growth factor-1, members of the TGF-beta superfamily and follistatin do not reflect different stages of dynapenia and sarcopenia in elderly women. Exp Gerontol. 2015; 64:35–45.
Article
67. Schafer MJ, Atkinson EJ, Vanderboom PM, Kotajarvi B, White TA, Moore MM, et al. Quantification of GDF11 and myostatin in human aging and cardiovascular disease. Cell Metab. 2016; 23:1207–15.
Article
68. GTEx Consortium. Human genomics. The Genotype-Tissue Expression (GTEx) pilot analysis: multitissue gene regulation in humans. Science. 2015; 348:648–60.
69. Sinha M, Jang YC, Oh J, Khong D, Wu EY, Manohar R, et al. Restoring systemic GDF11 levels reverses age-related dysfunction in mouse skeletal muscle. Science. 2014; 344:649–52.
Article
70. Egerman MA, Cadena SM, Gilbert JA, Meyer A, Nelson HN, Swalley SE, et al. GDF11 increases with age and inhibits skeletal muscle regeneration. Cell Metab. 2015; 22:164–74.
Article
71. Egerman MA, Glass DJ. The role of GDF11 in aging and skeletal muscle, cardiac and bone homeostasis. Crit Rev Biochem Mol Biol. 2019; 54:174–83.
Article
72. Zimmers TA, Jiang Y, Wang M, Liang TW, Rupert JE, Au ED, et al. Exogenous GDF11 induces cardiac and skeletal muscle dysfunction and wasting. Basic Res Cardiol. 2017; 112:48.
Article
73. Zhou Y, Sharma N, Dukes D, Myzithras MB, Gupta P, Khalil A, et al. GDF11 treatment attenuates the recovery of skeletal muscle function after injury in older rats. AAPS J. 2017; 19:431–7.
Article
74. Jin Q, Qiao C, Li J, Xiao B, Li J, Xiao X. A GDF11/myostatin inhibitor, GDF11 propeptide-Fc, increases skeletal muscle mass and improves muscle strength in dystrophic mdx mice. Skelet Muscle. 2019; 9:16.
Article
75. Mullican SE, Lin-Schmidt X, Chin CN, Chavez JA, Furman JL, Armstrong AA, et al. GFRAL is the receptor for GDF15 and the ligand promotes weight loss in mice and nonhuman primates. Nat Med. 2017; 23:1150–7.
Article
76. Yang L, Chang CC, Sun Z, Madsen D, Zhu H, Padkjaer SB, et al. GFRAL is the receptor for GDF15 and is required for the anti-obesity effects of the ligand. Nat Med. 2017; 23:1158–66.
Article
77. Ryu MJ, Kim SJ, Kim YK, Choi MJ, Tadi S, Lee MH, et al. Crif1 deficiency reduces adipose OXPHOS capacity and triggers inflammation and insulin resistance in mice. PLoS Genet. 2013; 9:e1003356.
Article
78. Chung HK, Ryu D, Kim KS, Chang JY, Kim YK, Yi HS, et al. Growth differentiation factor 15 is a myomitokine governing systemic energy homeostasis. J Cell Biol. 2017; 216:149–65.
Article
79. Moon JS, Goeminne LJE, Kim JT, Tian JW, Kim SH, Nga HT, et al. Growth differentiation factor 15 protects against the aging-mediated systemic inflammatory response in humans and mice. Aging Cell. 2020; 19:e13195.
Article
80. Emmerson PJ, Wang F, Du Y, Liu Q, Pickard RT, Gonciarz MD, et al. The metabolic effects of GDF15 are mediated by the orphan receptor GFRAL. Nat Med. 2017; 23:1215–9.
Article
81. Hsu JY, Crawley S, Chen M, Ayupova DA, Lindhout DA, Higbee J, et al. Non-homeostatic body weight regulation through a brainstem-restricted receptor for GDF15. Nature. 2017; 550:255–9.
Article
82. Lerner L, Tao J, Liu Q, Nicoletti R, Feng B, Krieger B, et al. MAP3K11/GDF15 axis is a critical driver of cancer cachexia. J Cachexia Sarcopenia Muscle. 2016; 7:467–82.
Article
83. Jones JE, Cadena SM, Gong C, Wang X, Chen Z, Wang SX, et al. Supraphysiologic administration of GDF11 induces cachexia in part by upregulating GDF15. Cell Rep. 2018; 22:1522–30.
Article
84. Suriben R, Chen M, Higbee J, Oeffinger J, Ventura R, Li B, et al. Antibody-mediated inhibition of GDF15-GFRAL activity reverses cancer cachexia in mice. Nat Med. 2020; 26:1264–70.
Article
85. Arumugam M, Raes J, Pelletier E, Le Paslier D, Yamada T, Mende DR, et al. Enterotypes of the human gut microbiome. Nature. 2011; 473:174–80.
Article
86. Yatsunenko T, Rey FE, Manary MJ, Trehan I, Dominguez-Bello MG, Contreras M, et al. Human gut microbiome viewed across age and geography. Nature. 2012; 486:222–7.
Article
87. Ticinesi A, Nouvenne A, Cerundolo N, Catania P, Prati B, Tana C, et al. Gut microbiota, muscle mass and function in aging: a focus on physical frailty and sarcopenia. Nutrients. 2019; 11:1633.
Article
88. Nay K, Jollet M, Goustard B, Baati N, Vernus B, Pontones M, et al. Gut bacteria are critical for optimal muscle function: a potential link with glucose homeostasis. Am J Physiol Endocrinol Metab. 2019; 317:E158–71.
Article
89. Claesson MJ, Jeffery IB, Conde S, Power SE, O’Connor EM, Cusack S, et al. Gut microbiota composition correlates with diet and health in the elderly. Nature. 2012; 488:178–84.
Article
90. Vaiserman AM, Koliada AK, Marotta F. Gut microbiota: a player in aging and a target for anti-aging intervention. Ageing Res Rev. 2017; 35:36–45.
Article
91. Koh A, Molinaro A, Stahlman M, Khan MT, Schmidt C, Manneras-Holm L, et al. Microbially produced imidazole propionate impairs insulin signaling through mTORC1. Cell. 2018; 175:947–61.
Article
92. Enoki Y, Watanabe H, Arake R, Sugimoto R, Imafuku T, Tominaga Y, et al. Indoxyl sulfate potentiates skeletal muscle atrophy by inducing the oxidative stress-mediated expression of myostatin and atrogin-1. Sci Rep. 2016; 6:32084.
Article
93. Lahiri S, Kim H, Garcia-Perez I, Reza MM, Martin KA, Kundu P, et al. The gut microbiota influences skeletal muscle mass and function in mice. Sci Transl Med. 2019; 11:eaan5662.
Article
94. Manickam R, Oh HYP, Tan CK, Paramalingam E, Wahli W. Metronidazole causes skeletal muscle atrophy and modulates muscle chronometabolism. Int J Mol Sci. 2018; 19:2418.
Article
95. Blacher E, Bashiardes S, Shapiro H, Rothschild D, Mor U, Dori-Bachash M, et al. Potential roles of gut microbiome and metabolites in modulating ALS in mice. Nature. 2019; 572:474–80.
Article
96. Grosicki GJ, Fielding RA, Lustgarten MS. Gut microbiota contribute to age-related changes in skeletal muscle size, composition, and function: biological basis for a gut-muscle axis. Calcif Tissue Int. 2018; 102:433–42.
Article
97. Symons TB, Sheffield-Moore M, Wolfe RR, Paddon-Jones D. A moderate serving of high-quality protein maximally stimulates skeletal muscle protein synthesis in young and elderly subjects. J Am Diet Assoc. 2009; 109:1582–6.
Article
98. Kim IY, Schutzler S, Schrader A, Spencer H, Kortebein P, Deutz NE, et al. Quantity of dietary protein intake, but not pattern of intake, affects net protein balance primarily through differences in protein synthesis in older adults. Am J Physiol Endocrinol Metab. 2015; 308:E21–8.
Article
99. Bauer J, Biolo G, Cederholm T, Cesari M, Cruz-Jentoft AJ, Morley JE, et al. Evidence-based recommendations for optimal dietary protein intake in older people: a position paper from the PROT-AGE Study Group. J Am Med Dir Assoc. 2013; 14:542–59.
Article
100. McGlory C, van Vliet S, Stokes T, Mittendorfer B, Phillips SM. The impact of exercise and nutrition on the regulation of skeletal muscle mass. J Physiol. 2019; 597:1251–8.
Article
101. Dillon EL, Sheffield-Moore M, Paddon-Jones D, Gilkison C, Sanford AP, Casperson SL, et al. Amino acid supplementation increases lean body mass, basal muscle protein synthesis, and insulin-like growth factor-I expression in older women. J Clin Endocrinol Metab. 2009; 94:1630–7.
Article
102. Cruz-Jentoft AJ, Landi F, Schneider SM, Zuniga C, Arai H, Boirie Y, et al. Prevalence of and interventions for sarcopenia in ageing adults: a systematic review. Report of the International Sarcopenia Initiative (EWGSOP and IWGS). Age Ageing. 2014; 43:748–59.
Article
103. Cortassa S, Caceres V, Bell LN, O’Rourke B, Paolocci N, Aon MA. From metabolomics to fluxomics: a computational procedure to translate metabolite profiles into metabolic fluxes. Biophys J. 2015; 108:163–72.
Article
104. Narkar VA, Downes M, Yu RT, Embler E, Wang YX, Banayo E, et al. AMPK and PPARdelta agonists are exercise mimetics. Cell. 2008; 134:405–15.
105. Kim JA, Roy RR, Zhong H, Alaynick WA, Embler E, Jang C, et al. PPARδ preserves a high resistance to fatigue in the mouse medial gastrocnemius after spinal cord transection. Muscle Nerve. 2016; 53:287–96.
Article
106. Mosti MP, Stunes AK, Ericsson M, Pullisaar H, Reseland JE, Shabestari M, et al. Effects of the peroxisome proliferator-activated receptor (PPAR)-δ agonist GW501516 on bone and muscle in ovariectomized rats. Endocrinology. 2014; 155:2178–89.
Article
107. Sahebkar A, Chew GT, Watts GF. New peroxisome proliferator-activated receptor agonists: potential treatments for atherogenic dyslipidemia and non-alcoholic fatty liver disease. Expert Opin Pharmacother. 2014; 15:493–503.
Article
108. Kadayat TM, Shrestha A, Jeon YH, An H, Kim J, Cho SJ, et al. Targeting peroxisome proliferator-activated receptor delta (PPARδ): a medicinal chemistry perspective. J Med Chem. 2020; 63:10109–34.
Article
109. Winder WW, Hardie DG. Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise. Am J Physiol. 1996; 270(2 Pt 1):E299–304.
Article
110. Wojtaszewski JF, Nielsen P, Hansen BF, Richter EA, Kiens B. Isoform-specific and exercise intensity-dependent activation of 5′-AMP-activated protein kinase in human skeletal muscle. J Physiol. 2000; 528(Pt 1):221–6.
Article
111. Hardie DG, Schaffer BE, Brunet A. AMPK: an energy-sensing pathway with multiple inputs and outputs. Trends Cell Biol. 2016; 26:190–201.
Article
112. Steinberg GR, O’Neill HM, Dzamko NL, Galic S, Naim T, Koopman R, et al. Whole body deletion of AMP-activated protein kinase {beta}2 reduces muscle AMPK activity and exercise capacity. J Biol Chem. 2010; 285:37198–209.
113. Thomas MM, Wang DC, D’Souza DM, Krause MP, Layne AS, Criswell DS, et al. Muscle-specific AMPK β1β2-null mice display a myopathy due to loss of capillary density in nonpostural muscles. FASEB J. 2014; 28:2098–107.
Article
114. Bujak AL, Crane JD, Lally JS, Ford RJ, Kang SJ, Rebalka IA, et al. AMPK activation of muscle autophagy prevents fasting-induced hypoglycemia and myopathy during aging. Cell Metab. 2015; 21:883–90.
Article
115. Lantier L, Mounier R, Leclerc J, Pende M, Foretz M, Viollet B. Coordinated maintenance of muscle cell size control by AMP-activated protein kinase. FASEB J. 2010; 24:3555–61.
Article
116. Mu J, Barton ER, Birnbaum MJ. Selective suppression of AMP-activated protein kinase in skeletal muscle: update on ‘lazy mice’. Biochem Soc Trans. 2003; 31(Pt 1):236–41.
Article
117. Thomson DM. The role of AMPK in the regulation of skeletal muscle size, hypertrophy, and regeneration. Int J Mol Sci. 2018; 19:3125.
Article
118. Winder WW, Holmes BF, Rubink DS, Jensen EB, Chen M, Holloszy JO. Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle. J Appl Physiol (1985). 2000; 88:2219–26.
Article
119. Pauly M, Chabi B, Favier FB, Vanterpool F, Matecki S, Fouret G, et al. Combined strategies for maintaining skeletal muscle mass and function in aging: myostatin inactivation and AICAR-associated oxidative metabolism induction. J Gerontol A Biol Sci Med Sci. 2015; 70:1077–87.
Article
120. Ljubicic V, Miura P, Burt M, Boudreault L, Khogali S, Lunde JA, et al. Chronic AMPK activation evokes the slow, oxidative myogenic program and triggers beneficial adaptations in mdx mouse skeletal muscle. Hum Mol Genet. 2011; 20:3478–93.
Article
121. Pauly M, Daussin F, Burelle Y, Li T, Godin R, Fauconnier J, et al. AMPK activation stimulates autophagy and ameliorates muscular dystrophy in the mdx mouse diaphragm. Am J Pathol. 2012; 181:583–92.
Article
122. Hall DT, Griss T, Ma JF, Sanchez BJ, Sadek J, Tremblay AMK, et al. The AMPK agonist 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR), but not metformin, prevents inflammation-associated cachectic muscle wasting. EMBO Mol Med. 2018; 10:e8307.
123. Myers RW, Guan HP, Ehrhart J, Petrov A, Prahalada S, Tozzo E, et al. Systemic pan-AMPK activator MK-8722 improves glucose homeostasis but induces cardiac hypertrophy. Science. 2017; 357:507–11.
Article
124. Esquejo RM, Salatto CT, Delmore J, Albuquerque B, Reyes A, Shi Y, et al. Activation of liver AMPK with PF-06409577 corrects NAFLD and lowers cholesterol in rodent and primate preclinical models. EBioMedicine. 2018; 31:122–32.
Article
125. Menzies KJ, Singh K, Saleem A, Hood DA. Sirtuin 1-mediated effects of exercise and resveratrol on mitochondrial biogenesis. J Biol Chem. 2013; 288:6968–79.
Article
126. Lagouge M, Argmann C, Gerhart-Hines Z, Meziane H, Lerin C, Daussin F, et al. Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha. Cell. 2006; 127:1109–22.
Article
127. Timmers S, Konings E, Bilet L, Houtkooper RH, van de Weijer T, Goossens GH, et al. Calorie restriction-like effects of 30 days of resveratrol supplementation on energy metabolism and metabolic profile in obese humans. Cell Metab. 2011; 14:612–22.
Article
128. Dufour CR, Wilson BJ, Huss JM, Kelly DP, Alaynick WA, Downes M, et al. Genome-wide orchestration of cardiac functions by the orphan nuclear receptors ERRalpha and gamma. Cell Metab. 2007; 5:345–56.
129. Rangwala SM, Wang X, Calvo JA, Lindsley L, Zhang Y, Deyneko G, et al. Estrogen-related receptor gamma is a key regulator of muscle mitochondrial activity and oxidative capacity. J Biol Chem. 2010; 285:22619–29.
130. Lee SJ, McPherron AC. Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci U S A. 2001; 98:9306–11.
Article
131. Amato AA, Sivakumar K, Goyal N, David WS, Salajegheh M, Praestgaard J, et al. Treatment of sporadic inclusion body myositis with bimagrumab. Neurology. 2014; 83:2239–46.
Article
132. Tillner J, Posch MG, Wagner F, Teichert L, Hijazi Y, Einig C, et al. A novel dual glucagon-like peptide and glucagon receptor agonist SAR425899: Results of randomized, placebo-controlled first-in-human and first-in-patient trials. Diabetes Obes Metab. 2019; 21:120–8.
Article
133. Tai J, Liu W, Li Y, Li L, Holscher C. Neuroprotective effects of a triple GLP-1/GIP/glucagon receptor agonist in the APP/PS1 transgenic mouse model of Alzheimer’s disease. Brain Res. 2018; 1678:64–74.
Article
134. Dollerup OL, Chubanava S, Agerholm M, Sondergard SD, Altıntas A, Moller AB, et al. Nicotinamide riboside does not alter mitochondrial respiration, content or morphology in skeletal muscle from obese and insulin-resistant men. J Physiol. 2020; 598:731–54.
Article
135. Mills KF, Yoshida S, Stein LR, Grozio A, Kubota S, Sasaki Y, et al. Long-term administration of nicotinamide mononucleotide mitigates age-associated physiological decline in mice. Cell Metab. 2016; 24:795–806.
Article
136. Guo S, Chen Q, Sun Y, Chen J. Nicotinamide protects against skeletal muscle atrophy in streptozotocin-induced diabetic mice. Arch Physiol Biochem. 2019; 125:470–7.
Article
137. Wilkinson DJ, Brook MS, Smith K, Atherton PJ. Stable isotope tracers and exercise physiology: past, present and future. J Physiol. 2017; 595:2873–82.
Article
138. Hellerstein MK. New stable isotope-mass spectrometric techniques for measuring fluxes through intact metabolic pathways in mammalian systems: introduction of moving pictures into functional genomics and biochemical phenotyping. Metab Eng. 2004; 6:85–100.
Article
139. Hinkley JM, Cornnell HH, Standley RA, Chen EY, Narain NR, Greenwood BP, et al. Older adults with sarcopenia have distinct skeletal muscle phosphodiester, phosphocreatine, and phospholipid profiles. Aging Cell. 2020; 19:e13135.
Article
140. Makimura H, Stanley TL, Sun N, Hrovat MI, Systrom DM, Grinspoon SK. The association of growth hormone parameters with skeletal muscle phosphocreatine recovery in adult men. J Clin Endocrinol Metab. 2011; 96:817–23.
Article