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RNA and Protein Synthesis Section 12-3 pgs 300-306

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section 12 3 rna and protein synthesis

Introduction

The nucleus, chromosomes and dna, attribution:, works cited:.

  • Shea, J. R. and Leblond, C. P. (2005). Number of nucleoli in various cell types of the mouse. Journal of Morphology , 119 (4), 425-433. http://dx.doi.org/10.1002/jmor.1051190404 .
  • Derenzini, M., Montanaro, L., and TrerΓ©, D. (2008). What the nucleolus says to a tumour pathologist. Histopathology , 54 (6), 753-762. http://dx.doi.org/10.1111/j.1365-2559.2008.03168.x .
  • Montanaro, L., TrerΓ©, D., and Derenzini, M. (2008). Nucleolus, ribosomes, and cancer. Am. J. Pathol. , 173 (2), 301-310. http://dx.doi.org/10.2353/ajpath.2008.070752 .
  • Alberts, B. Johnson, A., Lewis, J., Raff, M. Roberts, K., and Walter, P. (2002). Chromosomal DNA and its packaging in the chromatin fiber. In Molecular biology of the cell (4th ed.). New York, NY: Garland Science. Retrieved from http://www.ncbi.nlm.nih.gov/books/NBK26834/ .
  • The Nobel prize in chemistry 2009 - Press release. (2014). In Nobelprize.org . Retrieved from http://www.nobelprize.org/nobel_prizes/chemistry/laureates/2009/press.html .

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Supplementation strategies for strength and power athletes: carbohydrate, protein, and amino acid ingestion.

section 12 3 rna and protein synthesis

1. Introduction

2. pathway of adaptation model, 3. nutritional supplementation strategies, 3.1. carbohydrate ingestion, 3.1.1. glycogen resynthesis, 3.1.2. hormonal modification, 3.2. protein and amino acid ingestion, 3.2.1. protein synthesis, 3.2.2. protein type, 3.3. combined ingestion of carbohydrate, protein, and/or amino acids, 4. resistance exercise, nutrition supplementation strategies, and molecular responses, 4.1. resistance exercise and molecular responses, 4.2. interactions between resistance exercise, carbohydrate, protein, and amino acid ingestion on molecular signaling, 5. discussion, 6. conclusions, author contributions, acknowledgments, conflicts of interest.

  • Bird, S.P.; Tarpenning, K.M. Influence of circadian time structure on acute hormonal responses to a single bout of heavy-resistance exercise in weight-trained men. Chronobiol. Int. 2004 , 21 , 131–146. [ Google Scholar ] [ CrossRef ]
  • Gotshalk, L.A.; Loebel, C.C.; Nindl, B.C.; Putukian, M.; Sebastianelli, W.J.; Newton, R.U.; Hakkinen, K.; Kraemer, W.J. Hormonal responses of multiset versus single-set heavy-resistance exercise protocols. Can. J. Appl. Physiol. 1997 , 22 , 244–255. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Hakkinen, K.; Pakarinen, A. Acute hormonal responses to heavy resistance exercise in men and women at different ages. Int. J. Sports Med. 1995 , 16 , 507–513. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Izquierdo, M.; Ibanez, J.; Calbet, J.A.; Navarro-Amezqueta, I.; Gonzalez-Izal, M.; Idoate, F.; Hakkinen, K.; Kraemer, W.J.; Palacios-Sarrasqueta, M.; Almar, M.; et al. Cytokine and hormone responses to resistance training. Eur. J. Appl. Physiol. 2009 , 107 , 397–409. [ Google Scholar ] [ CrossRef ]
  • Kraemer, W.J.; Marchitelli, L.; Gordon, S.E.; Harman, E.; Dziados, J.E.; Mello, R.; Frykman, P.; McCurry, D.; Fleck, S.J. Hormonal and growth factor responses to heavy resistance exercise protocols. J. Appl. Physiol. 1990 , 69 , 1442–1450. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Raastad, T.; Bjoro, T.; Hallen, J. Hormonal responses to high- and moderate-intensity strength exercise. Eur. J. Appl. Physiol. 2000 , 82 , 121–128. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Ahtiainen, J.P.; Pakarinen, A.; Alen, M.; Kraemer, W.J.; Hakkinen, K. Muscle hypertrophy, hormonal adaptations and strength development during strength training in strength-trained and untrained men. Eur. J. Appl. Physiol. 2003 , 89 , 555–563. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Kraemer, W.J.; HΓ€kkinen, K.; Newton, R.U.; Nindl, B.C.; Volek, J.S.; McCormick, M.; Gotshalk, L.A.; Gordon, S.E.; Fleck, S.J.; Campbell, W.W.; et al. Effects of heavy-resistance training on hormonal response patterns in younger vs. older men. J. Appl. Physiol. 1999 , 87 , 982–992. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Kraemer, W.J.; Ratamess, N.A. Hormonal responses and adaptations to resistance exercise and training. Sports Med. 2005 , 35 , 339–361. [ Google Scholar ] [ CrossRef ]
  • McCall, G.E.; Byrnes, W.C.; Fleck, S.J.; Dickinson, A.; Kraemer, W.J. Acute and chronic hormonal responses to resistance training designed to promote muscle hypertrophy. Can. J. Appl. Physiol. 1999 , 24 , 96–107. [ Google Scholar ] [ CrossRef ]
  • Staron, R.S.; Karapondo, D.L.; Kraemer, W.J.; Fry, A.C.; Gordon, S.E.; Falkel, J.E.; Hagerman, F.C.; Hikida, R.S. Skeletal muscle adaptations during early phase of heavy-resistance training in men and women. J. Appl. Physiol. 1994 , 76 , 1247–1255. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Florini, J.R. Hormonal control of muscle growth. Muscle Nerve 1987 , 10 , 577–598. [ Google Scholar ] [ CrossRef ]
  • Kraemer, W.J. Endocrine responses to resistance exercise. Med. Sci. Sports Exerc. 1988 , 20 , S152–S157. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Borsheim, E.; Cree, M.G.; Tipton, K.D.; Elliott, T.A.; Aarsland, A.; Wolfe, R.R. Effect of carbohydrate intake on net muscle protein synthesis during recovery from resistance exercise. J. Appl. Physiol. 2004 , 96 , 674–678. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Tarpenning, K.M.; Wiswell, R.A.; Hawkins, S.A.; Marcell, T.J. Influence of weight training exercise and modification of hormonal response on skeletal muscle growth. J. Sci. Med. Sport 2001 , 4 , 431–446. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Thyfault, J.P.; Carper, M.J.; Richmond, S.R.; Hulver, M.W.; Potteiger, J.A. Effects of liquid carbohydrate ingestion on markers of anabolism following high-intensity resistance exercise. J. Strength Cond. Res. 2004 , 18 , 174–179. [ Google Scholar ] [ PubMed ]
  • Tipton, K.D.; Ferrando, A.A.; Phillips, S.M.; Doyle, D., Jr.; Wolfe, R.R. Postexercise net protein synthesis in human muscle from orally administered amino acids. Am. J. Physiol. Endocrinol. Metabol. 1999 , 276 , E628–E634. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Borsheim, E.; Tipton, K.D.; Wolf, S.E.; Wolfe, R.R. Essential amino acids and muscle protein recovery from resistance exercise. Am. J. Physiol. Endocrinol. Metabol. 2002 , 283 , E648–E657. [ Google Scholar ] [ CrossRef ]
  • Tipton, K.D.; Borsheim, E.; Wolf, S.E.; Sanford, A.P.; Wolfe, R.R. Acute response of net muscle protein balance reflects 24-h balance after exercise and amino acid ingestion. Am. J. Physiol. Endocrinol. Metabol. 2003 , 284 , E76–E89. [ Google Scholar ] [ CrossRef ]
  • Bird, S.P.; Mabon, T.; Pryde, M.; Feebrey, S.; Cannon, J. Triphasic multinutrient supplementation during acute resistance exercise improves session volume load and reduces muscle damage in strength-trained athletes. Nutr. Res. 2013 , 33 , 376–387. [ Google Scholar ] [ CrossRef ]
  • Kraemer, W.J.; Hatfield, D.L.; Spiering, B.A.; Vingren, J.L.; Fragala, M.S.; Ho, J.-Y.; Volek, J.S.; Anderson, J.M.; Maresh, C.M. Effects of a multi-nutrient supplement on exercise performance and hormonal responses to resistance exercise. Eur. J. Appl. Physiol. 2007 , 101 , 637–646. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Rasmussen, B.B.; Tipton, K.D.; Miller, S.L.; Wolf, S.E.; Wolfe, R.R. An oral essential amino acid-carbohydrate supplement enhances muscle protein anabolism after resistance exercise. J. Appl. Physiol. 2000 , 88 , 386–392. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Volek, J.S. Influence of nutrition on responses to resistance training. Med. Sci. Sports Exerc. 2004 , 36 , 689–696. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Andersen, L.L.; Tufekovic, G.; Zebis, M.K.; Crameri, R.M.; Verlaan, G.; Kjaer, M.; Suetta, C.; Magnusson, P.; Aagaard, P. The effect of resistance training combined with timed ingestion of protein on muscle fiber size and muscle strength. Metab.Clin. Exp. 2005 , 54 , 151–156. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Bird, S.P.; Tarpenning, K.M.; Marino, F.E. Independent and combined effects of liquid carbohydrate/essential amino acid ingestion on hormonal and muscular adaptations following resistance training in untrained men. Eur. J. Appl. Physiol. 2006 , 97 , 225–238. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • King, A.; Kwan, K.; Jukic, I.; Zinn, C.; Helms, E. Fueling for and recovering from resistance training: The periworkout nutrition practices of competitive powerlifters. Nutrition 2024 , 122 , 112389. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Rasmussen, B.B.; Phillips, S.M. Contractile and nutritional regulation of human muscle growth. Exerc. Sport Sci. Rev. 2003 , 31 , 127–131. [ Google Scholar ] [ CrossRef ]
  • Rennie, M.J.; Tipton, K.D. Protein and amino acid metabolism during and after exercise and the effects of nutrition. Annu. Rev. Nutr. 2000 , 20 , 457–483. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Rennie, M.J.; Wackerhage, H.; Spangenburg, E.E.; Booth, F.W. Control of the size of the human muscle mass. Annu. Rev. Physiol. 2004 , 66 , 799–828. [ Google Scholar ] [ CrossRef ]
  • Bird, S.P.; Tarpenning, K.M.; Marino, F.E. Designing resistance training programmes to enhance muscular fitness: A review of the acute programme variables. Sports Med. 2005 , 35 , 841–851. [ Google Scholar ] [ CrossRef ]
  • Bird, S.P.; Tarpenning, K.M.; Marino, F.E. Effects of liquid carbohydrate/essential amino acid ingestion on acute hormonal response during a single bout of resistance exercise in untrained men. Nutrition 2006 , 22 , 367–375. [ Google Scholar ] [ CrossRef ]
  • Kraemer, W.J.; Volek, J.S.; Bush, J.A.; Putukian, M.; Sebastianelli, W.J. Hormonal responses to consecutive days of heavy-resistance exercise with or without nutritional supplementation. J. Appl. Physiol. 1998 , 85 , 1544–1555. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Smilios, I.; Pilianidis, T.; Karamouzis, M.; Tokmakidis, S.P. Hormonal responses after various resistance exercise protocols. Med. Sci. Sports Exerc. 2003 , 35 , 644–654. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Williams, A.G.; Ismail, A.N.; Sharma, A.; Jones, D.A. Effects of resistance exercise volume and nutritional supplementation on anabolic and catabolic hormones. Eur. J. Appl. Physiol. 2002 , 86 , 315–321. [ Google Scholar ] [ CrossRef ]
  • Phillips, S.M. Physiologic and molecular bases of muscle hypertrophy and atrophy: Impact of resistance exercise on human skeletal muscle (protein and exercise dose effects). Appl. Physiol. Nutr. Metab. 2009 , 34 , 403–410. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Miller, S.L.; Tipton, K.D.; Chinkes, D.L.; Wolf, S.E.; Wolfe, R.R. Independent and combined effects of amino acids and glucose after resistance exercise. Med. Sci. Sports Exerc. 2003 , 35 , 449–455. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Chandler, R.M.; Byrne, H.K.; Patterson, J.G.; Ivy, J.L. Dietary supplements affect the anabolic hormones after weight-training exercise. J. Appl. Physiol. 1994 , 76 , 839–845. [ Google Scholar ] [ CrossRef ]
  • Fafournoux, P.; Bruhat, A.; Jousse, C. Amino acid regulation of gene expression. Biochem. J 2000 , 351 , 1–12. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Hamel, F.G.; Upward, J.L.; Siford, G.L.; Duckworth, W.C. Inhibition of proteasome activity by selected amino acids. Metab.Clin. Exp. 2003 , 52 , 810–814. [ Google Scholar ] [ CrossRef ]
  • Varillas-Delgado, D.; Del Coso, J.; GutiΓ©rrez-HellΓ­n, J.; Aguilar-Navarro, M.; MuΓ±oz, A.; Maestro, A.; Morencos, E. Genetics and sports performance: The present and future in the identification of talent for sports based on DNA testing. Eur. J. Appl. Physiol. 2022 , 122 , 1811–1830. [ Google Scholar ] [ CrossRef ]
  • Elia, M.; Carter, A.; Bacon, S.; Winearls, C.G.; Smith, R. Clinical usefulness of urinary 3-methylhistidine excretion in indicating muscle protein breakdown. Br. Med. J. 1981 , 282 , 351–354. [ Google Scholar ] [ CrossRef ]
  • Bird, S.P.; Tarpenning, K.M.; Marino, F.E. Liquid carbohydrate/essential amino acid ingestion during a short-term bout of resistance exercise suppresses myofibrillar protein degradation. Metab.Clin. Exp. 2006 , 55 , 570–577. [ Google Scholar ] [ CrossRef ]
  • Candow, D.G.; Burke, N.C.; Smith-Palmer, T.; Burke, D.G. Effect of whey and soy protein supplementation combined with resistance training in young adults. Int. J. Sport Nutr. Exerc. Metabol. 2006 , 16 , 233–244. [ Google Scholar ] [ CrossRef ]
  • Roy, B.D.; Fowles, J.R.; Hill, R.; Tarnopolsky, M.A. Macronutrient intake and whole body protein metabolism following resistance exercise. Med. Sci. Sports Exerc. 2000 , 32 , 1412–1418. [ Google Scholar ] [ CrossRef ]
  • Garlick, P.J.; McNurlan, M.A.; Ballmer, P.E. Influence of dietary protein intake on whole-body protein turnover in humans. Diabetes Care 1991 , 14 , 1189–1198. [ Google Scholar ] [ CrossRef ]
  • Burke, L.M.; Hawley, J.A. Fat and carbohydrate for exercise. Curr. Opin. Clin. Nutr. Metab. Care. 2006 , 9 , 476–481. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Lambert, C.P.; Frank, L.L.; Evans, W.J. Macronutrient considerations for the sport of bodybuilding. Sports Med. 2004 , 34 , 317–327. [ Google Scholar ] [ CrossRef ]
  • Biolo, G.; Tipton, K.D.; Klein, S.; Wolfe, R.R. An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein. Am. J. Physiol. Endocrinol. Metabol. 1997 , 273 , E122–E129. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Borsheim, E.; Aarsland, A.; Wolfe, R.R. Effect of an amino acid, protein, and carbohydrate mixture on net muscle protein balance after resistance exercise. Int. J. Sport Nutr. Exerc. Metabol. 2004 , 14 , 255–271. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Hulmi, J.J.; Volek, J.S.; Selanne, H.; Mero, A.A. Protein ingestion prior to strength exercise affects blood hormones and metabolism. Med. Sci. Sports Exerc. 2005 , 37 , 1990–1997. [ Google Scholar ] [ CrossRef ]
  • Koopman, R.; Wagenmakers, A.J.; Manders, R.J.; Zorenc, A.H.; Senden, J.M.; Gorselink, M.; Keizer, H.A.; van Loon, L.J. Combined ingestion of protein and free leucine with carbohydrate increases postexercise muscle protein synthesis in vivo in male subjects. Am. J. Physiol. Endocrinol. Metabol. 2005 , 288 , E645–E653. [ Google Scholar ] [ CrossRef ]
  • Roy, B.D.; Tarnopolsky, M.A.; MacDougall, J.D.; Fowles, J.; Yarasheski, K.E. Effect of glucose supplement timing on protein metabolism after resistance training. J. Appl. Physiol. 1997 , 82 , 1882–1888. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Tarpenning, K.M.; Hawkins, S.A.; Wiswell, R.A. CHO-induced blunting of cortisol response to weightlifting exercise in resistance-trained older men. Eur. J. Sport Sci. 2003 , 3 , 1–11. [ Google Scholar ] [ CrossRef ]
  • Tipton, K.D.; Rasmussen, B.B.; Miller, S.L.; Wolf, S.E.; Owens-Stovall, S.K.; Petrini, B.E.; Wolfe, R.R. Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise. Am. J. Physiol. Endocrinol. Metabol. 2001 , 281 , E197–E206. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Tipton, K.D.; Elliott, T.A.; Cree, M.G.; Wolf, S.E.; Sanford, A.P.; Wolfe, R.R. Ingestion of casein and whey proteins result in muscle anabolism after resistance exercise. Med. Sci. Sports Exerc. 2004 , 36 , 2073–2081. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Burke, D.G.; Chilibeck, P.D.; Davidson, K.S.; Candow, D.G.; Farthing, J.; Smith-Palmer, T. The effect of whey protein supplementation with and without creatine monohydrate combined with resistance training on lean tissue mass and muscle strength. Int. J. Sport Nutr. Exerc. Metabol. 2001 , 11 , 349–364. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Chromiak, J.A.; Smedley, B.; Carpenter, W.; Brown, R.; Koh, Y.S.; Lamberth, J.G.; Joe, L.A.; Abadie, B.R.; Altorfer, G. Effect of a 10-week strength training program and recovery drink on body composition, muscular strength and endurance, and anaerobic power and capacity. Nutrition 2004 , 20 , 420–427. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Cribb, P.J.; Williams, A.D.; Carey, M.F.; Hayes, A. The effect of whey isolate and resistance training on strength, body composition, and plasma glutamine. Int. J. Sport Nutr. Exerc. Metabol. 2006 , 16 , 494–509. [ Google Scholar ] [ CrossRef ]
  • Cribb, P.J.; Williams, A.D.; Hayes, A. A creatine-protein-carbohydrate supplement enhances responses to resistance training. Med. Sci. Sports Exerc. 2007 , 39 , 1960–1968. [ Google Scholar ] [ CrossRef ]
  • Ratamess, N.A.; Kraemer, W.J.; Volek, J.S.; Rubin, M.R.; Gomez, A.L.; French, D.N.; Sharman, M.J.; McGuigan, M.M.; Scheett, T.; Hakkinen, K.; et al. The effects of amino acid supplementation on muscular performance during resistance training overreaching. J. Strength Cond. Res. 2003 , 17 , 250–258. [ Google Scholar ]
  • Rankin, J.W.; Goldman, L.P.; Puglisi, M.J.; Nickols-Richardson, S.M.; Earthman, C.P.; Gwazdauskas, F.C. Effect of post-exercise supplement consumption on adaptations to resistance training. J. Am. Coll. Nutr. 2004 , 23 , 322–330. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Schoenfeld, B.J.; Aragon, A.A.; Wilborn, C.; Urbina, S.L.; Hayward, S.E.; Krieger, J. Pre- versus post-exercise protein intake has similar effects on muscular adaptations. PeerJ 2017 , 5 , e2825. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Taylor, L.W.; Wilborn, C.; Roberts, M.D.; White, A.; Dugan, K. Eight weeks of pre- and postexercise whey protein supplementation increases lean body mass and improves performance in Division III collegiate female basketball players. Appl. Physiol. Nutr. Metab. 2016 , 41 , 249–254. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Kerksick, C.M.; Rasmussen, C.J.; Lancaster, S.L.; Magu, B.; Smith, P.; Melton, C.; Greenwood, M.; Almada, A.L.; Earnest, C.P.; Kreider, R.B. The effects of protein and amino acid supplementation on performance and training adaptations during ten weeks of resistance training. J. Strength Cond. Res. 2006 , 20 , 643–653. [ Google Scholar ] [ PubMed ]
  • Conley, M.S.; Stone, M.H. Carbohydrate ingestion/supplementation for resistance exercise and training. Sports Med. 1996 , 21 , 7–17. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Haff, G.G.; Lehmkuhl, M.J.; McCoy, L.B.; Stone, M.H. Carbohydrate supplementation and resistance training. J. Strength Cond. Res. 2003 , 17 , 187–196. [ Google Scholar ] [ PubMed ]
  • Robergs, R.A.; Pearson, D.R.; Costill, D.L.; Fink, W.J.; Pascoe, D.D.; Benedict, M.A.; Lambert, C.P.; Zachweija, J.J. Muscle glycogenolysis during differing intensities of weight-resistance exercise. J. Appl. Physiol. 1991 , 70 , 1700–1706. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Tesch, P.A.; Ploutz-Snyder, L.L.; Ystrom, L.; Castro, M.J.; Dudley, G.A. Skeletal muscle glycogen loss evoked by resistance exercise. J. Strength Cond. Res. 1998 , 12 , 67–73. [ Google Scholar ]
  • Pascoe, D.D.; Costill, D.L.; Fink, W.J.; Robergs, R.A.; Zachwieja, J.J. Glycogen resynthesis in skeletal muscle following resistive exercise. Med. Sci. Sports Exerc. 1993 , 25 , 349–354. [ Google Scholar ] [ CrossRef ]
  • Roy, B.D.; Tarnopolsky, M.A. Influence of differing macronutrient intakes on muscle glycogen resynthesis after resistance exercise. J. Appl. Physiol. 1998 , 84 , 890–896. [ Google Scholar ] [ CrossRef ]
  • Haff, G.G.; Koch, A.J.; Potteiger, J.A.; Kuphal, K.E.; Magee, L.M.; Green, S.B.; Jakicic, J.J. Carbohydrate supplementation attenuates muscle glycogen loss during acute bouts of resistance exercise. Int. J. Sport Nutr. Exerc. Metabol. 2000 , 10 , 326–339. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Lambert, C.P.; Flynn, M.G.; Boone, J.B.; Michaud, T.J.; Rodriguez-Zayas, J. Effects of carbohydrate feeding on multiple-bout resistance exercise. J. Appl. Sport Sci. Res. 1991 , 5 , 192–197. [ Google Scholar ]
  • Haff, G.G.; Stone, M.H.; Warren, B.J.; Keith, R.; Johnson, R.L.; Nieman, D.C.; Williams, F.; Kirksey, K.B. The effect of carbohydrate supplementation on multiple sessions and bouts of resistance exercise. J. Strength Cond. Res. 1999 , 13 , 111–117. [ Google Scholar ]
  • Williams, A.G.; van den Oord, M.; Sharma, A.; Jones, D.A. Is glucose/amino acid supplementation after exercise an aid to strength training? Br. J. Sports Med. 2001 , 35 , 109–113. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Kraemer, W.J.; Spiering, B.A.; Volek, J.S.; Ratamess, N.A.; Sharman, M.J.; Rubin, M.R.; French, D.N.; Silvestre, R.; Hatfield, D.L.; Van Heest, J.L.; et al. Androgenic responses to resistance exercise: Effects of feeding and L-carnitine. Med. Sci. Sports Exerc. 2006 , 38 , 1288–1296. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Arfvidsson, B.; Zachrisson, H.; Moller-Loswick, A.C.; Hyltander, A.; Sandstrom, R.; Lundholm, K. Effect of systemic hyperinsulinemia on amino acid flux across human legs in postabsorptive state. Am. J. Physiol. Endocrinol. Metabol. 1991 , 260 , E46–E52. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Moller-Loswick, A.C.; Zachrisson, H.; Hyltander, A.; Korner, U.; Matthews, D.E.; Lundholm, K. Insulin selectively attenuates breakdown of nonmyofibrillar proteins in peripheral tissues of normal men. Am. J. Physiol. Endocrinol. Metabol. 1994 , 266 , E645–E652. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Koch, A.J.; Potteiger, J.A.; Chan, M.A.; Benedict, S.H.; Frey, B.B. Minimal influence of carbohydrate ingestion on the immune response following acute resistance exercise. Int. J. Sport Nutr. Exerc. Metabol. 2001 , 11 , 149–161. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Jeukendrup, A.E.; Jentjens, R. Oxidation of carbohydrate feedings during prolonged exercise: Current thoughts, guidelines and directions for future research. Sports Med. 2000 , 29 , 407–424. [ Google Scholar ] [ CrossRef ]
  • Murray, R.; Bartoli, W.P.; Eddy, D.E.; Horn, M.K. Gastric emptying and plasma deuterium accumulation following ingestion of water and two carbohydrate-electrolyte beverages. Int. J. Sport Nutr. 1997 , 7 , 144–153. [ Google Scholar ] [ CrossRef ]
  • Murray, R.; Bartoli, W.; Stofan, J.; Horn, M.; Eddy, D. A comparison of the gastric emptying characteristics of selected sports drinks. Int. J. Sport Nutr. 1999 , 9 , 263–274. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Lundholm, K.; Edstrom, S.; Ekman, L.; Karlberg, I.; Walker, P.; Schersten, T. Protein degradation in human skeletal muscle tissue: The effect of insulin, leucine, amino acids and ions. Clin. Sci. 1981 , 60 , 319–326. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Nagasawa, T.; Kido, T.; Yoshizawa, F.; Ito, Y.; Nishizawa, N. Rapid suppression of protein degradation in skeletal muscle after oral feeding of leucine in rats. J. Nutr. Biochem. 2002 , 13 , 121–127. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Biolo, G.; Maggi, S.P.; Williams, B.D.; Tipton, K.D.; Wolfe, R.R. Increased rates of muscle protein turnover and amino acid transport after resistance exercise in humans. Am. J. Physiol. Endocrinol. Metabol. 1995 , 268 , E514–E520. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Phillips, S.M.; Tipton, K.D.; Aarsland, A.; Wolf, S.E.; Wolfe, R.R. Mixed muscle protein synthesis and breakdown after resistance exercise in humans. Am. J. Physiol. Endocrinol. Metabol. 1997 , 273 , E99–E107. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Levenhagen, D.K.; Carr, C.; Carlson, M.G.; Maron, D.J.; Borel, M.J.; Flakoll, P.J. Postexercise protein intake enhances whole-body and leg protein accretion in humans. Med. Sci. Sports Exerc. 2002 , 34 , 828–837. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Bohe, J.; Low, A.; Wolfe, R.R.; Rennie, M.J. Human muscle protein synthesis is modulated by extracellular, not intramuscular amino acid availability: A dose-response study. J. Physiol. 2003 , 552 , 315–324. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Gorissen, S.H.; RΓ©mond, D.; Van Loon, L.J. The muscle protein synthetic response to food ingestion. Meat Sci. 2015 , 109 , 96–100. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Tipton, K.; Gurkin, B.; Matin, S.; Wolfe, R. Nonessential amino acids are not necessary to stimulate net muscle protein synthesis in healthy volunteers. J. Nutr. Biochem. 1999 , 10 , 89–95. [ Google Scholar ] [ CrossRef ]
  • West, D.W.; Burd, N.A.; Coffey, V.G.; Baker, S.K.; Burke, L.M.; Hawley, J.A.; Moore, D.R.; Stellingwerff, T.; Phillips, S.M. Rapid aminoacidemia enhances myofibrillar protein synthesis and anabolic intramuscular signaling responses after resistance exercise. Am. J. Clin. Nutr. 2011 , 94 , 795–803. [ Google Scholar ] [ CrossRef ]
  • Suryawan, A.; Jeyapalan, A.S.; Orellana, R.A.; Wilson, F.A.; Nguyen, H.V.; Davis, T.A. Leucine stimulates protein synthesis in skeletal muscle of neonatal pigs by enhancing mTORC1 activation. Am. J. Physiol. Endocrinol. Metabol. 2008 , 295 , E868–E875. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Breen, L.; Phillips, S.M. Nutrient interaction for optimal protein anabolism in resistance exercise. Curr. Opin. Clin. Nutr. Metab. Care 2012 , 15 , 226–232. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Zaromskyte, G.; Prokopidis, K.; Ioannidis, T.; Tipton, K.D.; Witard, O.C. Evaluating the leucine trigger hypothesis to explain the post-prandial regulation of muscle protein synthesis in young and older adults: A systematic review. Front. Nutr. 2021 , 8 , 685165. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Elliot, T.A.; Cree, M.G.; Sanford, A.P.; Wolfe, R.R.; Tipton, K.D. Milk ingestion stimulates net muscle protein synthesis following resistance exercise. Med. Sci. Sports Exerc. 2006 , 38 , 667–674. [ Google Scholar ] [ CrossRef ]
  • Wolfe, R.R. Effects of insulin on muscle tissue. Curr. Opin. Clin. Nutr. Metab. Care. 2000 , 3 , 67–71. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Biolo, G.; Williams, B.D.; Fleming, R.Y.; Wolfe, R.R. Insulin action on muscle protein kinetics and amino acid transport during recovery after resistance exercise. Diabetes 1999 , 48 , 949–957. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Manninen, A.H. Hyperinsulinaemia, hyperaminoacidaemia and post-exercise muscle anabolism: The search for the optimal recovery drink. Br. J. Sports Med. 2006 , 40 , 900–905. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Mahe, S.; Roos, N.; Benamouzig, R.; Davin, L.; Luengo, C.; Gagnon, L.; Gausserges, N.; Rautureau, J.; Tome, D. Gastrojejunal kinetics and the digestion of [15N]beta-lactoglobulin and casein in humans: The influence of the nature and quantity of the protein. Am. J. Clin. Nutr. 1996 , 63 , 546–552. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Boirie, Y.; Dangin, M.; Gachon, P.; Vasson, M.P.; Maubois, J.L.; Beaufrere, B. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc. Natl. Acad. Sci. USA 1997 , 94 , 14930–14935. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Dangin, M.; Boirie, Y.; Garcia-Rodenas, C.; Gachon, P.; Fauquant, J.; Callier, P.; Ballevre, O.; Beaufrere, B. The digestion rate of protein is an independent regulating factor of postprandial protein retention. Am. J. Physiol. Endocrinol. Metabol. 2001 , 280 , E340–E348. [ Google Scholar ] [ CrossRef ]
  • Dangin, M.; Boirie, Y.; Guillet, C.; Beaufrere, B. Influence of the protein digestion rate on protein turnover in young and elderly subjects. J. Nutr. 2002 , 132 , 3228S–3233. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Ferrando, A.A.; Wolfe, R.R.; Hirsch, K.R.; Church, D.D.; Kviatkovsky, S.A.; Roberts, M.D.; Stout, J.R.; Gonzalez, D.E.; Sowinski, R.J.; Kreider, R.B.; et al. International Society of Sports Nutrition Position Stand: Effects of essential amino acid supplementation on exercise and performance. J. Int. Soc. Sports Nutr. 2023 , 20 , 2263409. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Biolo, G.; Fleming, R.Y.; Maggi, S.P.; Wolfe, R.R. Transmembrane transport and intracellular kinetics of amino acids in human skeletal muscle. Am. J. Physiol. Endocrinol. Metabol. 1995 , 268 , E75–E84. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Drummond, M.J.; Glynn, E.L.; Fry, C.S.; Timmerman, K.L.; Volpi, E.; Rasmussen, B.B. An increase in essential amino acid availability upregulates amino acid transporter expression in human skeletal muscle. Am. J. Physiol. Endocrinol. Metabol. 2010 , 298 , E1011–E1018. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Coburn, J.W.; Housh, D.J.; Housh, T.J.; Malek, M.H.; Beck, T.W.; Cramer, J.T.; Johnson, G.O.; Donlin, P.E. Effects of leucine and whey protein supplementation during eight weeks of unilateral resistance training. J. Strength Cond. Res. 2006 , 20 , 284–291. [ Google Scholar ] [ PubMed ]
  • Deldicque, L.; Theisen, D.; Francaux, M. Regulation of mTOR by amino acids and resistance exercise in skeletal muscle. Eur. J. Appl. Physiol. 2005 , 94 , 1–10. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Gibala, M.J. Nutritional supplementation and resistance exercise: What is the evidence for enhanced skeletal muscle hypertrophy? Can. J. Appl. Physiol. 2000 , 25 , 524–535. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Gater, D.R.; Gater, D.A.; Uribe, J.M.; Bunt, J.C. Impact of nutritional supplements on body composition, strength and IGF-1. J. Appl. Sport Sci. Res. 1992 , 6 , 66–76. [ Google Scholar ]
  • Rozenek, R.; Ward, P.; Long, S.; Garhammer, J. Effects of high-calorie supplements on body composition and muscular strength following resistance training. J. Sports Med. Phys. Fitness 2002 , 42 , 340–347. [ Google Scholar ]
  • Kreider, R.B. Dietary supplements and the promotion of muscle growth with resistance exercise. Sports Med. 1999 , 27 , 97–110. [ Google Scholar ] [ CrossRef ]
  • Churchward-Venne, T.A.; Burd, N.A.; Phillips, S.M. Nutritional regulation of muscle protein synthesis with resistance exercise: Strategies to enhance anabolism. Nutr. Metab. 2012 , 9 , 40. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Atherton, P.J.; Smith, K. Muscle protein synthesis in response to nutrition and exercise. J. Physiol. 2012 , 590 , 1049–1057. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Hornberger, T.A.; Esser, K.A. Mechanotransduction and the regulation of protein synthesis in skeletal muscle. Proc. Nutr. Soc. 2004 , 63 , 331–335. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Hornberger, T.A. Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle. Int. J. Biochem. Cell. Biol. 2011 , 43 , 1267–1276. [ Google Scholar ] [ CrossRef ]
  • Hornberger, T.A.; Chien, S. Mechanical stimuli and nutrients regulate rapamycin-sensitive signaling through distinct mechanisms in skeletal muscle. J. Cell. Biochem. 2006 , 97 , 1207–1216. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Huang, J.; Manning, B.D. A complex interplay between Akt, TSC2 and the two mTOR complexes. Biochem. Soc. Trans. 2009 , 37 , 217–222. [ Google Scholar ] [ CrossRef ]
  • NavΓ©, B.T.; Ouwens, D.M.; Withers, D.J.; Alessi, D.R.; Shepherd, P.R. Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem. J. 1999 , 344 , 427–431. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Bolster, D.R.; Kubica, N.; Crozier, S.J.; Williamson, D.L.; Farrell, P.A.; Kimball, S.R.; Jefferson, L.S. Immediate response of mammalian target of rapamycin (mtor)-mediated signalling following acute resistance exercise in rat skeletal muscle. J. Physiol. 2003 , 553 , 213–220. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Kimball, S.R.; Farrell, P.A.; Jefferson, L.S. Role of insulin in translational control of protein synthesis in skeletal muscle by amino acids or exercise. J. Appl. Physiol. 2002 , 93 , 1168–1180. [ Google Scholar ] [ CrossRef ]
  • DeYoung, M.P.; Horak, P.; Sofer, A.; Sgroi, D.; Ellisen, L.W. Hypoxia regulates TSC1/2–mTOR signaling and tumor suppression through REDD1-mediated 14–3–3 shuttling. Genes. Dev. 2008 , 22 , 239–251. [ Google Scholar ] [ CrossRef ]
  • Caldow, M.K.; Thomas, E.E.; Dale, M.J.; Tomkinson, G.R.; Buckley, J.D.; Cameron-Smith, D. Early myogenic responses to acute exercise before and after resistance training in young men. Physiol. Rep. 2015 , 3 , e12511. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Gibala, M. Molecular responses to high-intensity interval exercise. Appl. Physiol. Nutr. Metab. 2009 , 34 , 428–432. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Lundberg, T.R.; Fernandez-Gonzalo, R.; Gustafsson, T.; Tesch, P.A. Aerobic exercise does not compromise muscle hypertrophy response to short-term resistance training. J. Appl. Physiol. 2013 , 114 , 81–89. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Roberts, M.D.; McCarthy, J.J.; Hornberger, T.A.; Phillips, S.M.; Mackey, A.L.; Nader, G.A.; Boppart, M.D.; Kavazis, A.N.; Reidy, P.T.; Ogasawara, R.; et al. Mechanisms of mechanical overload-induced skeletal muscle hypertrophy: Current understanding and future directions. Physiol. Rev. 2023 , 103 , 2679–2757. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Franchi, M.V.; Atherton, P.J.; Reeves, N.D.; FlΓΌck, M.; Williams, J.; Mitchell, W.K.; Selby, A.; Beltran Valls, R.M.; Narici, M.V. Architectural, functional and molecular responses to concentric and eccentric loading in human skeletal muscle. Acta Physiol. 2014 , 210 , 642–654. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Lecker, S.H.; Goldberg, A.L.; Mitch, W.E. Protein Degradation by the Ubiquitin–Proteasome Pathway in Normal and Disease States. J. Am. Soc. Nephrol. 2006 , 17 , 1807–1819. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Borgenvik, M.; AprΓ³, W.; Blomstrand, E. Intake of branched-chain amino acids influences the levels of MAFbx mRNA and MuRF-1 total protein in resting and exercising human muscle. Am. J. Physiol. Endocrinol. Metabol. 2012 , 302 , E510–E521. [ Google Scholar ] [ CrossRef ]
  • Mascher, H.; Tannerstedt, J.; Brink-Elfegoun, T.; Ekblom, B.; Gustafsson, T.; Blomstrand, E. Repeated resistance exercise training induces different changes in mRNA expression of MAFbx and MuRF-1 in human skeletal muscle. Am. J. Physiol. Endocrinol. Metabol. 2008 , 294 , E43–E51. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Stefanetti, R.J.; Lamon, S.; Wallace, M.; Vendelbo, M.H.; Russell, A.P.; Vissing, K. Regulation of ubiquitin proteasome pathway molecular markers in response to endurance and resistance exercise and training. Pflug. Arch. Eur. J. Physiol. 2015 , 467 , 1523–1537. [ Google Scholar ] [ CrossRef ]
  • Stitt, T.N.; Drujan, D.; Clarke, B.A.; Panaro, F.; Timofeyva, Y.; Kline, W.O.; Gonzalez, M.; Yancopoulos, G.D.; Glass, D.J. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting foxo transcription factors. Mol. Cell 2004 , 14 , 395–403. [ Google Scholar ] [ CrossRef ]
  • Gulati, P.; Gaspers, L.D.; Dann, S.G.; Joaquin, M.; Nobukuni, T.; Natt, F.; Kozma, S.C.; Thomas, A.P.; Thomas, G. Amino acids activate mtor complex 1 via Ca2+/CaM signaling to hVps34. Cell. Metab. 2008 , 7 , 456–465. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Takahara, T.; Amemiya, Y.; Sugiyama, R.; Maki, M.; Shibata, H. Amino acid-dependent control of mTORC1 signaling: A variety of regulatory modes. J. Biomed. Sci. 2020 , 27 , 87. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Dreyer, H.C.; Fujita, S.; Cadenas, J.G.; Chinkes, D.L.; Volpi, E.; Rasmussen, B.B. Resistance exercise increases AMPK activity and reduces 4E-BP1 phosphorylation and protein synthesis in human skeletal muscle. J. Physiol. 2006 , 576 , 613–624. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Drummond, M.J.; Rasmussen, B.B. Leucine-enriched nutrients and the regulation of mammalian target of rapamycin signalling and human skeletal muscle protein synthesis. Curr. Opin. Clin. Nutr. Metab. Care 2008 , 11 , 222–226. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Fujita, S.; Dreyer, H.C.; Drummond, M.J.; Glynn, E.L.; Cadenas, J.G.; Yoshizawa, F.; Volpi, E.; Rasmussen, B.B. Nutrient signalling in the regulation of human muscle protein synthesis. J. Physiol. 2007 , 582 , 813–823. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Atherton, P.J.; Etheridge, T.; Watt, P.W.; Wilkinson, D.; Selby, A.; Rankin, D.; Smith, K.; Rennie, M.J. Muscle full effect after oral protein: Time-dependent concordance and discordance between human muscle protein synthesis and mTORC1 signaling1234. Am. J. Clin. Nutr. 2010 , 92 , 1080–1088. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Areta, J.L.; Burke, L.M.; Camera, D.M.; West, D.W.D.; Crawshay, S.; Moore, D.R.; Stellingwerff, T.; Phillips, S.M.; Hawley, J.A.; Coffey, V.G. Reduced resting skeletal muscle protein synthesis is rescued by resistance exercise and protein ingestion following short-term energy deficit. Am. J. Physiol. Endocrinol. Metabol. 2014 , 306 , E989–E997. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Karlsson, H.K.R.; Nilsson, P.-A.; Nilsson, J.; Chibalin, A.V.; Zierath, J.R.; Blomstrand, E. Branched-chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise. Am. J. Physiol. Endocrinol. Metab. 2004 , 287 , E1–E7. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • AprΓ³, W.; Blomstrand, E. Influence of supplementation with branched-chain amino acids in combination with resistance exercise on p70S6 kinase phosphorylation in resting and exercising human skeletal muscle. Acta Physiol. 2010 , 200 , 237–248. [ Google Scholar ] [ CrossRef ]
  • Lam, F.-C.; Khan, T.M.; Faidah, H.; Haseeb, A.; Khan, A.H. Effectiveness of whey protein supplements on the serum levels of amino acid, creatinine kinase and myoglobin of athletes: A systematic review and meta-analysis. Syst. Rev. 2019 , 8 , 1–12. [ Google Scholar ] [ CrossRef ]
  • Farnfield, M.M.; Breen, L.; Carey, K.A.; Garnham, A.; Cameron-Smith, D. Activation of mTOR signalling in young and old human skeletal muscle in response to combined resistance exercise and whey protein ingestion. Appl. Physiol. Nutr. Metab. 2012 , 37 , 21–30. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Kakigi, R.; Yoshihara, T.; Ozaki, H.; Ogura, Y.; Ichinoseki-Sekine, N.; Kobayashi, H.; Naito, H. Whey protein intake after resistance exercise activates mTOR signaling in a dose-dependent manner in human skeletal muscle. Eur. J. Appl. Physiol. 2014 , 114 , 735–742. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Koopman, R.; Pennings, B.; Zorenc, A.H.G.; van Loon, L.J.C. Protein ingestion further augments S6K1 phosphorylation in skeletal muscle following resistance type exercise in males. J. Nutr. 2007 , 137 , 1880–1886. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Ferreira, M.P.; Li, R.; Cooke, M.; Kreider, R.B.; Willoughby, D.S. Periexercise coingestion of branched-chain amino acids and carbohydrate in men does not preferentially augment resistance exercise–induced increases in phosphatidylinositol 3 kinase/protein kinase B–mammalian target of rapamycin pathway markers indicative of muscle protein synthesis. Nutr. Res. 2014 , 34 , 191–198. [ Google Scholar ] [ PubMed ]
  • Burd, N.A.; Gorissen, S.H.; van Vliet, S.; Snijders, T.; van Loon, L.J.C. Differences in postprandial protein handling after beef compared with milk ingestion during postexercise recovery: A randomized controlled trial12. Am. J. Clin. Nutr. 2015 , 102 , 828–836. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Reidy, P.T.; Walker, D.K.; Dickinson, J.M.; Gundermann, D.M.; Drummond, M.J.; Timmerman, K.L.; Fry, C.S.; Borack, M.S.; Cope, M.B.; Mukherjea, R.; et al. Protein blend ingestion following resistance exercise promotes human muscle protein synthesis. J. Nutr. 2013 , 143 , 410–416. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Reidy, P.T.; Walker, D.K.; Dickinson, J.M.; Gundermann, D.M.; Drummond, M.J.; Timmerman, K.L.; Cope, M.B.; Mukherjea, R.; Jennings, K.; Volpi, E. Soy-dairy protein blend and whey protein ingestion after resistance exercise increases amino acid transport and transporter expression in human skeletal muscle. J. Appl. Physiol. 2014 , 116 , 1353–1364. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Blomstrand, E. A role for branched-chain amino acids in reducing central fatigue. J. Nutr. 2006 , 136 , 544S–547S. [ Google Scholar ] [ CrossRef ]
  • Newsholme, E. Amino acids, brain neurotransmitters and a functional link between muscle and brain that is important in sustained exercise. Adv. Myochem. 1987 , 127–138. [ Google Scholar ]
  • Davis, J.M.; Alderson, N.L.; Welsh, R.S. Serotonin and central nervous system fatigue: Nutritional considerations. Am. J. Clin. Nutr. 2000 , 72 , 573S–578S. [ Google Scholar ] [ CrossRef ]
  • Davis, J.M. Carbohydrates, branched-chain amino acids, and endurances: The central fatigue hypothesis. Int. J. Sport Nutr. Exerc. Metab. 1995 , 5 , S29–S38. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Matsumoto, K.; Koba, T.; Hamada, K.; Tsujimoto, H.; Mitsuzono, R. Branched-chain amino acid supplementation increases the lactate threshold during an incremental exercise test in trained individuals. J. Nutr. Sci. Vitaminol. 2009 , 55 , 52–58. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Hormoznejad, R.; Zare Javid, A.; Mansoori, A. Effect of BCAA supplementation on central fatigue, energy metabolism substrate and muscle damage to the exercise: A systematic review with meta-analysis. Sport Sci. Health 2019 , 15 , 265–279. [ Google Scholar ] [ CrossRef ]
  • Martinho, D.V.; Nobari, H.; Faria, A.; Field, A.; Duarte, D.; Sarmento, H. Oral branched-chain amino acids supplementation in athletes: A systematic review. Nutrients 2022 , 14 , 4002. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Aragon, A.; Schoenfeld, B. Nutrient timing revisited: Is there a post-exercise anabolic window? J. Int. Soc. Sports Nutr. 2013 , 10 , 5. [ Google Scholar ] [ CrossRef ] [ PubMed ]
  • Kerksick, C.M.; Arent, S.; Schoenfeld, B.J.; Stout, J.R.; Campbell, B.; Wilborn, C.D.; Taylor, L.; Kalman, D.; Smith-Ryan, A.E.; Kreider, R.B.; et al. International Society of Sports Nutrition Position Stand: Nutrient Timing. J. Int. Soc. Sports Nutr. 2017 , 14 , 33. [ Google Scholar ] [ CrossRef ]

Click here to enlarge figure

StudySubjectsProtocolInterventionTime CourseMeasuresOutcomes
Biolo et al. [ ]6 untrained MLower-body
4 exercises; 4–5 sets Γ— 8–10 reps; 75% 1-RM
Infusion of balanced AA mix 0.15 gΒ·kg Β·h 3 h at rest
3 h post-exercise
Muscle biopsies
A/V blood samples
MPS greater after RE (>200%) than at rest (~150%). MPB not significantly different after either condition. AA transport increased 30–100% post-ex compared to resting condition. Suggested ↑ AA availability post-ex mediates anabolic response.
Bird et al. [ , ]32 untrained M (18–29 yrs)Complete-body
8 exercises; 3 sets Γ— 10 reps; 75% 1-RM
Four groups:
EAA (6 g)
CHO (6%)
CHO+EAA
PLA
~625 mL beverage
Ingested during ex bout. Fluid volume 8.5 mL/kg
Blood sampling:
15 min intervals: 0, 15, 30, 45, 60, 75, and 90 min
Biochemical:
Cortisol; Insulin;
Testosterone;
Glucose
Urine: 3-MH
Ingestion of liquid CHO, EAA, CHO+EAA solution during exercise bout blunted exercise-induced cortisol response, CHO+EAA consumption resulting in significantly ↓ 3-MH excretion.
Borsheim et al. [ ] 6 active ind.
3 M/3 F
Lower-body
2 exercises; 18 sets Γ— 8–10 reps; 80% 1-RM
6 g EAA Γ— 2425 mL bolus EAA ingestion, 1 h and 2 h post-exMuscle biopsies 0.5, 1.5, 2.5, and 4 h post-ex
Femoral A/V blood 15 over 7 h
Net muscle protein balance ↑ following ingestion at both 1 and 2 h post-ex. The response of net balance was about twice the response to 6 g of mixed AA (Miller et al. [ ]). NEAA are not required to stimulate MPS. Suggested dose-dependent effect of EAA ingestion on MPS following RE.
Borsheim, Aarsland and Wolfe [ ]8 healthy ind.
5 M/3 F
Knee extensor exercise
10 sets Γ— 8 reps; 80% 1-RM
Two conditions:
CHO (100 g)
PAAC (17.5 g Whey + 4.9 g AA + 77.4 g CHO)
Fluid volume of 590 mL ingested 1 h post-exMuscle biopsies 0.5, 1, 2, 4 h post-ex
Femoral A/V blood
17 over 6 h
PAAC ↑ MPS to a greater extent than CHO alone. Response appeared to consist of two phases, one rapid acute phase followed by smaller delayed phase ~90 min after ingestion. Suggested that response due to insulin effect and sustained elevation in AA. Suggested that addition of whey to CHO+AA extends anabolic effect, lasting beyond first hour after intake.
Borsheim et al. [ ]16 healthy ind.
10 M/6 F
Knee extensor exercise
10 sets Γ— 8 reps; 80% 1-RM
Two groups:
Placebo (PLA)
CHO (100 g)
Beverage ingested 1 h post-exMuscle biopsies:
0.5, 1, 2, 4 h post-ex Femoral A/V blood 16 over 6 h
CHO ingestion resulted in significant ↑ in glucose and insulin concentration, no change in PLA. Corresponded with no change in net muscle protein balance in PLA, whereas net balance was improved following CHO ingestion. This response was attributed to a progressive decrease in MPB. Overall improvement small compared to AA ingestion. Suggested AA necessary for maximal anabolic response.
Hulmi et al.
[ ]
10 trained
M
Lower-body
3 exercises; 3–5 sets Γ— 1–10 reps; RM load
Two conditions:
Placebo (PLA)
PRO (17.5 g whey + 7.5 g casein)
PRO+CHO (25 g)
500 mL beverage
PLA or PRO ingested 30 min pre-ex PLUS
PRO+CHO ingested 5 min post-ex
Blood sampling:
0, 0.5, 1, and 2 h post-ex
Hormones:
Cortisol; Testosterone; Insulin; Growth Hormone
PRO intake 30 pre-ex ↑ insulin by 51.6% 5 min post-ex. However, testosterone and growth hormone were significantly ↓ 5 min post-ex compared to PLA. Concluded that PRO consumption 30 min before RE will provide a more anabolic hormonal environment by ↑ insulin and possibly testosterone uptake.
Koopman et al. [ ] 8 untrained
M
Lower-body
2 exercises; 16 sets Γ— 8 reps; 80% 1-RM
Three conditions:
CHO: 50 g
CHO+PRO: 50 g CHO+Whey: 33.3 g
CHO+PRO+Leu: 50 g CHO + 33.3 g whey + 16.6 g Leu
Post-ex ingestion
Dosage in g/L
Fluid volume 3 mLΒ·kg Β·30 min
Muscle biopsies:
0 and 6 h post-ex
A/V blood samples
16 over 6 h
Over the 6 h post-ex period, whole-body protein breakdown ↓, and whole-body protein breakdown ↑ in CHO+PRO and CHO+PRO+Leu conditions compared with CHO. This corresponded with ↑ insulin concentrations in CHO+PRO and CHO+PRO+Leu conditions than CHO. FSR ↑ in CHO+PRO+Leu compared with CHO. Concluded that co-ingestion of PRO and Leu stimulates MPS and optimizes protein balance compared with CHO only.
Miller et al.
[ ]
10 healthy ind.
6 M/4 F
Lower-body
2 exercises; 18 sets Γ— 8–10 reps; 75% 1-RM
Three conditions:
CHO: ~35 g
6 g AA mix: 2.8 g EAA/3.2 g NEEA
MIX: ~35 g CHO + 6 g AA
Beverage ingested
1 h and 2 h post-ex
Composition adjusted according to body mass
Muscle biopsies:
0.5, 1.5, 2.5, and 3.5
h post-ex
Femoral A/V blood:
8 over 4 h
Ingestion of CHO+AA (MIX) and AA significantly ↑ MPS compared to CHO; however, no differences reported between MIX and AA. Ingestion of the second drink 1 h after the first drink stimulated a similar response as to the first drink. Concluded that combined effects of CHO and AA ingestion following RE reflects sum of their individual effects. Ingestion of only EAA is required to stimulate MPS.
Rasmussen et al. [ ]6 untrained
3 M/3 F
Lower-body
2 exercises; 18 sets Γ— 8 reps; 80% 1-RM
Two conditions:
Placebo (PLA)
EAC: 6 g EAA + 35 g CHO
PLA 1 h post-ex + EAC 3 h post-ex
EAC 1 h post-ex + PLA 3 h post-ex
Muscle biopsies: 1, 2, and 4 h post-ex
A/V blood samples: 11 over 7 h period
EAC ↑ glucose and insulin concentration, MPS and muscle protein net balance at both 1 h and 3 h. No change was reported for PLA. MPB was unaffected regardless of when EAC or PLA was ingested. Timing of EAC ingestion did not affect the response MPS or muscle protein net balance, no significant difference reported between 1 h and 3 h.
Roy et al. [ ]8 young M
(20–25 yr)
Single-leg knee extensor exercise; 8 sets Γ— 10 reps; 85% 1-RM. One leg performed exercise, while other leg served as controlTwo conditions:
Placebo (PLA)
CHO (1 g/kg)
Immediately and 60 min post-exMuscle biopsies:
0 and 10 h post-ex
A/V blood samples: 14 over 10 h period
24 h urine collection
CHO ingestion resulted in significant ↑ in glucose and insulin concentrations, which corresponded with reduction in 3-MHIS and urea excretion. This was interpreted as a reduction in MPB. Suggested that net effect was anabolic and would result in more positive net muscle protein balance.
Roy et al. [ ]10 young M
(18–21 yr)
Whole-body
9 exercises; 3 sets Γ— 10 reps; 80% 1-RM
Three conditions:
Placebo (PLA)
CHO (1 g/kg)
CHO/PRO/FAT
(1 g/kg)
Immediately and 60 min post-exA/V blood samples: 13 over ~6 h periodNOLD was ~41% and ~33% greater for CHO/PRO/FAT and CHO compared with PLA at 4 h post-ex. CHO/PRO/FAT ingestion led to similar ↑ in glucose and insulin to CHO (Roy et al. 1997). No significant differences for 3-MHIS between conditions. However, the authors note that there was a directional change that was lower for the supplement conditions compared to PLA.
Tarpenning et al. [ ]5 older M
(55–64 yr)
Complete-body
9 exercises; 3 sets Γ— 10 reps; 75% 1-RM
Two conditions:
Placebo (PLA)
CHO (6%)
Beverages ingested during exercise bout
Fluid volume 8.5 mL/kg
Biochemical:
Cortisol
Free testosterone
Glucose
PLA displayed significant ↑ of 67% in plasma cortisol levels. Time of peak cortisol concentration corresponded with non-significant change in glucose levels of 8%. CHO trial resulted in a blunted cortisol response (non-significant change), corresponded with significant ↑ of 37% in glucose levels. Suggested that CHO-induced modification of cortisol response may modulate ↓ in neuroendocrine function in older individuals.
Titpon et al.
[ ]
6 untrained
3 M/3 F
Lower-body
4 exercises; 4–5 sets Γ— 8–10 reps; 75% 1-RM
Three conditions:
Placebo (PLA)
40 g mixed AA
40 g EAA
60 min post-ex 100 mL every 18–20 min until 4 h post-ex.
Fluid volume 1 liter
Muscle biopsy:
4.5 h post-ex
A/V blood samples:
5 over 7.5 h period
Both MAA and EAA produced hyperaminoacidemia, thereby ↑ muscle protein net balance similar to levels attained by infusion. Concluded that it is not necessary to include NEAA in formulation to elicit anabolic response, as muscle protein net balance was similar for MAA and EAA.
Tipton et al.
[ ]
6 active ind.
3 M/3 F
Lower-body
2 exercises; 18 sets Γ— 8 reps; 80% 1-RM
Two conditions:
Placebo (PLA)
EAC: 6 g EAA + 35 g CHO
500 mL bolus EAC
ingestion:
PRE-ex condition
POST-ex condition
Muscle biopsies:
βˆ’60, 0, 60, and 120 min
A/V blood samples:
16 over 4 h period
AA delivery and stimulation of MPS was significantly greater in PRE-ex than POST-ex. Concluded that effectiveness of EAC ingestion consumed PRE is superior to when consumed after RE. The combination of ↑ blood flow and AA availability maximizes the anabolic response to RE.
Tipton et al.
[ ]
7 healthy ind.
4 M/3 F
Knee extensor exercise
8 sets Γ— 8 reps;
80% 1-RM
Two conditions:
Resting (REST)
ES: 15 g EAA Γ— 2 +RE
350 mL bolus EAC ingestion
Pre-ex and 1 h post-ex
Muscle biopsies:
5 over 24 h period
A/V blood samples:
37 over 24 h period
FSR over full 24 h period was ~40% greater in ES. Suggested that changes in net muscle protein balance over short period (3 h) are representative of changes in net balance over 24 h period. MPS stimulated by RE and EAA ingestion is additive to balance that occurs in REST condition.
Tipton et al.
[ ]
23 healthy
M/F
Knee extensor exercise
10 sets Γ— 8 reps;
80% 1-RM
Three groups:
Placebo (PLA)
Casein (CS): 20 g
Whey (WH): 20 g
Fluid volume of 300 mL ingested 1 h post-exMuscle biopsies:
βˆ’0.5, 1, 2, 5 h post-ex
A/V blood samples:
17 over 6 h
Both CS and WH resulted in positive AA balance, initiative of net MPS. Pattern of AA appearance peaked earlier and at greater magnitude for WH than CS. Insulin concentrations mirrored this response, ↑ more rapidly WH than CS. Suggested that differences in digestive properties contributed to pattern of response. Concluded that post-ex ingestion of whole proteins may be effective in ↑ muscle size following resistance training.
StudySubjectsProtocolInterventionTime CourseMeasuresOutcomes
Andersen et al. [ ] 22 untrained M Resistance Training: 14 weeks
3 d/wk; Lower-body; 3 exercises
3–4 sets Γ— 4–15 reps; RM loads
Two groups:
PRO (16.6 g whey + 2.8 g casein + 2.8 g egg white +2.8 g L-glutamine)
CHO (25 g)
Fluid volume of 500 mL ingested immediately pre- and post-ex
Morning ingestion on non-training days
Pre- and post-
training:
Muscle fiber CSA
Muscular strength
PRO ingestion ↑ type I (18%) and type II (26%) CSA, which corresponded with 9% ↑ in vertical jump performance. No significant change reported for CHO. Interestingly, similar ↑ in peak torque were reported for both groups. Concluded that PRO ingestion has minor advantage over CHO in muscular properties (CSA and mechanical function).
Burke et al. [ ] 36 trained M
(18–31 yr)
Resistance Training: 12 weeks
4 d/wk; 2 d split (Upper/Lower-body)
4–5 sets Γ— 6–12 reps; RM loads
Three groups:
Whey: 1.2 g/kg
Whey+Cr: 1.2 g/kg + 0.1 g/kg Cr
PLA
Four equal servings across the dayPre- and post-
training:
Body composition
Muscular strength
Supplementation with combination of Whey+Cr resulted in greater increases in lean tissue mass as determined by DEXA and bench press 1-RM strength than for those who supplemented with only whey or PLA.
Chromiak et al. [ ] 41 healthy M
(18–35 yr)
Resistance Training: 10 weeks
4 d/wk; 2 d split (Upper/Lower-body) 3–4 sets Γ— 3–10 reps; RM loads
Two groups:
SUPP: 13 g whey + 4.9 g AA + 3 g Cr + 76 g CHO
CHO: (92 g)
Beverage ingested post-exPre- and post-
training:
Body composition
Muscular strength
Muscular power
Anaerobic capacity
Post-ex SUPP did not result in greater improvements in performance variables compared with CHO. However, a trend (p = 0.07) was reported towards a greater ↑ in FFM in the SUPP group.
Cribb et al. [ ]13 M
recreational bodybuilders
Resistance Training: 10 weeks
3 d/wk; Upper/Lower Split
Wks 1–2: Preparatory phase, 10–8 RM
Wks 3–6: Overload phase 1, 6 RM
Wks 7–10: Overload phase 2, 4 RM
Two groups:
WI: Whey isolate
C: Casein
Ingested 1.5 g/kg/d dose divided into 4 smaller equal serves:
Serve 1: Breakfast
Serve 2: Lunch
Serve 3: Post-workout
Serve 4: Evening
Pre- and post-
training:
Body composition
Muscular strength
Plasma glutamine
WI group demonstrated a significantly ↑ strength, LBM, and significant ↓ in fat mass compared to the C group during an intense 10 wk resistance training program.
Neither supplement influenced plasma glutamine.
Cribb et al. [ ]33 M
recreational bodybuilders
Resistance Training: 10 weeks
Whole-body; 3 exercises
Wks 1–2: Preparatory phase, 10 RM
Wks 3–6: Overload phase 1, 8–6 RM
Wks 7–10: Overload phase 2, 6–4 RM
Three groups:
PRO: Whey
PRO-CHO:
50% whey; 50% glucose
Cr-PRO-CHO: As above, plus creatine monohydrate
Ingested 1.5 g/kg/d dose divided into 3 smaller equal serves:
Serve 1: Morning
Serve 2: Post-workout (or afternoon on non-training days)
Serve 3: Before sleep
Cr supplements:
1-wk loading 0.3 g/kg/d, followed by 0.1 g/kg/d
Pre- and post-
training:
Body composition
Muscular strength
Muscle fiber CSA
Cr-containing supplement (Cr-PRO-CHO) demonstrated greater gains in 1 RM strength in three exercises, and these improvements were supported by greater hypertrophy response that was apparent at three different levels: LBM, muscle fiber CSA, and contractile protein content.
Ratamess et al. [ ]17 trained
M
Resistance Training: 4-week over-reaching program;
4 d/wk Total-body
2 weeks base: 3 sets Γ— 8–10 reps; 80% 1-RM;
2 weeks high-intensity: 3 sets Γ— 8–10 reps; RM load
Two groups:
Placebo (PLA)
AA mixture (0.4 g/kg)
PLA or AA capsules divided into three daily dosesPre- and post-
training:
Body composition
Muscular strength
Muscular power
Muscular endurance
AA supplementation was effective in attenuating reductions in strength and power output during 4 weeks of resistance training over-reaching. Furthermore, it appears that following an initial phase of high-volume, moderate-intensity RE with a phase of higher-intensity, moderate-intensity RE is effective in ↑ muscular strength in resistance-trained males.
Rankin et al. [ ] 19 untrained M (18–25 yr) Resistance Training: 10 weeks
3 d/wk; Whole-body;
7 exercises 3–5 sets Γ— 3–12 reps; 55–97% 1-RM
Two groups:
MILK (0.92 g/kg CHO + 0.21 g/kg PRO + 0.06 g/kg FAT)
CHO (125 g/kg)
Beverage ingested immediately post-ex Pre- and post-
training:
Body composition
Muscular strength
Hormone levels
Energy expenditure
The type of beverage consumed, MILK or CHO, did not have a significant effect on any performance measure. A trend was reported in the MILK group for body mass (p = 0.10) and fat free soft tissue (p = 0.13). Concluded that adaptations to resistance training were similar whether nutritional supplement of MILK or CHO was ingested immediately post-ex.
Schoenfeld et al. [ ]21 M strength trainedResistance Training: 10 weeks
3 d/wk; Whole-body;
3 sets Γ— 10 reps; 75% 1-RM
Two groups:
PRE-SUPP
POST-SUPP
Supp:
24 g PRO + 1 g CHO
Ingested immediately pre- or post-exercisePre-, mid-, and post-training:
Body composition
Muscle thickness
Muscular strength
No differences between groups across all measures. Concluded that the proposed post-exercise β€˜anabolic window’ may not be as important as ensuring adequate protein intake. The interval for protein intake to stimulate MPS may be as wide as several hours post-training depending on intake timing.
Tarpenning et al. [ ] 8 young M
(18–25 yr)
Resistance Training: 12 weeks
3 d/wk; Whole-body; 3sets Γ— 10 reps; 75% 1-RM
Two groups:
Placebo (PLA)
CHO (6%)
Beverages ingested during exercise bout
Fluid volume 8.5 mL/kg
Pre- and post-
training:
Muscle fiber CSA
Body composition
Muscular strength
Hormone levels
CHO ingestion blunted exercise-induced cortisol response (av. ↓ of 4.1%) compared to PLA (av. ↑ of 81.9%). CHO group displayed greater gains in type I and type II CSA. Reduction in cortisol response related to ↑ in muscle hypertrophy. Suggested that CHO-induced modification of cortisol response positively impacts skeletal muscle hypertrophic adaptation.
Taylor et al. [ ] 16 F NCAA DivIII basketball playersResistance Training: 8 weeks
3 d/wk; Whole-body;
3 sets Γ— 12 RM
Two groups:
WP: Whey (24 g)
MD: CHO (24 g)
Pre- and post-resistance trainingPre- and post-
training:
Body composition
Muscular strength
Performance testing
WP group, significant change in body composition (lean mass ↑ 1.4 kg; fat mass ↓ 1.0 kg); greater gains in 1 RM bench and improved pro agility time compared to MD. Concluded that 8 weeks of whey protein supplementation improved body composition and increased performance variables in previously trained female athletes.
Kerksick et al. [ ] 36 resistance-trained M
(18–50 yr)
Resistance Training: 10 weeks
4 d/wk; Split body part
2 x upper-body; 2 x lower-body; 3 sets Γ— 6–10 RM
Three groups:
WBG: Whey + BCAAs + L-glutamine
WC: Whey + casein
PLA: CHO
Ingested supplement within 2 hrs post-workout on training daysPre-, mid-, and post-training:
Body composition
Muscular strength
Muscular endurance
Anaerobic capacity
Whey + casein group showed greatest ↑ in lean mass. 1 RM for bench press and leg press significantly ↑ in all groups. Concluded that whey and casein protein supplementation significantly improve body composition via increases in lean mass.
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Bird, S.P.; Nienhuis, M.; Biagioli, B.; De Pauw, K.; Meeusen, R. Supplementation Strategies for Strength and Power Athletes: Carbohydrate, Protein, and Amino Acid Ingestion. Nutrients 2024 , 16 , 1886. https://doi.org/10.3390/nu16121886

Bird SP, Nienhuis M, Biagioli B, De Pauw K, Meeusen R. Supplementation Strategies for Strength and Power Athletes: Carbohydrate, Protein, and Amino Acid Ingestion. Nutrients . 2024; 16(12):1886. https://doi.org/10.3390/nu16121886

Bird, Stephen P., Mitch Nienhuis, Brian Biagioli, Kevin De Pauw, and Romain Meeusen. 2024. "Supplementation Strategies for Strength and Power Athletes: Carbohydrate, Protein, and Amino Acid Ingestion" Nutrients 16, no. 12: 1886. https://doi.org/10.3390/nu16121886

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