Gil Hernández A, Sánchez de Medina C. Síntesis, degradación y recambio de las proteínas. En: Gil A (editor). Tratado de Nutrición. Tomo II. Madrid: Editorial Médica Panamericana; 2017. pp. 177-216.
Dumont NA, Bentzinger CF, Sincennes M-C, et al. Satellite cells and skeletal muscle regeneration. Compar Physiol 2015;5:1027-59.
DOI: 10.1002/cphy.c140068
Ørtenblad N, Nielsen J, Boushel R, et al. The muscle fiber profiles, mitochondrial content, and enzyme activities of the exceptionally well-trained arm and leg muscles of elite cross-country skiers. Front Physiol 2018;9:1-11.
DOI: 10.3389/fphys.2018.01031
Sass FA, Fuchs M, Pumberger M, et al. Immunology guides skeletal muscle regeneration. Int J Mol Sci 2018;19:1-19.
DOI: 10.3390/ijms19030835
Uezumi A, Fukada S, Yamamoto N, et al. Identification and characterization of PDGFR+ mesenchymal progenitors in human skeletal muscle. Cell Death Dis 2014;5:1-10.
DOI: 10.1038/cddis.2014.161
Malecova B, Gatto S, Etxaniz U, et al. Dynamics of cellular states of fibro-adipogenic progenitors during myogenesis and muscular dystrophy. Nat Commun 2018;9:3670.
DOI: 10.1038/s41467-018-06068-6
Prado CM, Purcell SA, Alish C, et al. Implications of low muscle mass across the continuum of care: a narrative review. Ann Med 2018;0:1-39.
DOI: 10.1080/07853890.2018.1511918
Nachit M, Leclercq IA. Emerging awareness on the importance of skeletal muscle in liver diseases: time to dig deeper into mechanisms. Clin Sci 2019;133:465-81.
DOI: 10.1042/CS20180421
Cruz-Jentoft AJ, Bahat G, Bauer J, et al. Sarcopenia: revised European consensus on definition and diagnosis. Age Ageing 2018;48:16-31.
DOI: 10.1093/ageing/afy169
González Gallego J, González Gross M, Rodríguez Huertas JF. Nutrición en la actividad física y deportiva. En: Gil. A (editor). Tratado de Nutrición. Tomo III. Madrid: Editorial Médica Panamericana; 2017. pp. 465-96.
Proud CG. Amino acids and mTOR signalling in anabolic function. Biochem Soc Trans 2007;35:1187-90.
DOI: 10.1042/BST0351187
Bolster DR, Crozier SJ, Kimball SR, et al. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J Biol Chem 2002;277:23977-80.
DOI: 10.1074/jbc.C200171200
Gómez Llorente C, Gil Hernández A. Regulación de la expresión génica mediada por compuestos nitrogenados. En: Gil A (editor). Tratado de Nutrición. Tomo II. Madrid: Editorial Médica Panamericana; 2017. pp. 281-307.
Carbone JW, McClung JP, Pasiakos SM. Skeletal Muscle Responses to Negative Energy Balance: Effects of Dietary Protein. Adv Nutr 2012;3:119-26.
DOI: 10.3945/an.111.001792
Carbone JW, McClung JP, Pasiakos SM. Recent Advances in the Characterization of Skeletal Muscle and Whole-Body Protein Responses to Dietary Protein and Exercise during Negative Energy Balance. Adv Nutr 2019;10:70-9.
DOI: 10.1093/advances/nmy087
Ben-Nissan G, Sharon M. Regulating the 20S proteasome ubiquitin-independent degradation pathway. Biomolecules 2014;4:862-84.
DOI: 10.3390/biom4030862
Doyle A, Zhang G, Abdel Fattah EA, et al. Toll-like receptor 4 mediates lipopolysaccharide-induced muscle catabolism via coordinate activation of ubiquitin-proteasome and autophagy-lysosome pathways. FASEB J 2011;25:99-110.
DOI: 10.1096/fj.10-164152
Du J, Wang X, Miereles C, et al. Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 2004;113:115-23.
DOI: 10.1172/JCI18330
Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002;82:373-428.
DOI: 10.1152/physrev.00027.2001
Drummond MJ, Rasmussen BB. 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;11:222-6.
DOI: 10.1097/MCO.0b013e3282fa17fb
Nair KS, Schwartz RG, Welle S. Leucine as a regulator of whole body and skeletal muscle protein metabolism in humans. Am J Physiol 1992;263:E928-34.
DOI: 10.1152/ajpendo.1992.263.5.E928
Nakashima K, Ishida A, Yamazaki M, et al. Leucine suppresses myofibrillar proteolysis by down-regulating ubiquitin-proteasome pathway in chick skeletal muscles. Biochem Biophys Res Commun 2005;336:660-6.
DOI: 10.1016/j.bbrc.2005.08.138
FAO/WHO/UNU. Energy and Protein Requirements: Report of an FAO/WHO/UNU Expert Consultation. WHO Tech Rept Ser 1985;724.
Kurpad AV, Raj T, El-Khoury A, et al. Daily requirement for and splanchnic uptake of leucine in healthy adult Indians. Am J Clin Nutr 2001;74:747-55.
DOI: 10.1093/ajcn/74.6.747
Young VR, Borgonha S. Nitrogen and amino acid requirements: the Massachusetts Institute of Technology amino acid requirement pattern. J Nutr 2000;130:1841S-9S.
DOI: 10.1093/jn/130.7.1841S
Glynn EL, Fry CS, Drummond MJ, et al. Excess leucine intake enhances muscle anabolic signaling but not net protein anabolism in young men and women. J Nutr 2010;140:1970-6.
DOI: 10.3945/jn.110.127647
Whitham M, Febbraio MA. The ever-expanding myokinome: discovery challenges and therapeutic implications. Nat Rev Drug Discov 2016;15:719-29.
DOI: 10.1038/nrd.2016.153
Whitham M, Parker BL, Friedrichsen M, et al. Extracellular vesicles provide a means for tissue crosstalk during exercise. Cell Metab 2018;27:237-51.
DOI: 10.1016/j.cmet.2017.12.001
Carnac G, Ricaud S, Vernus B, et al. Myostatin: biology and clinical relevance. Mini Reviews in Medicinal Chemistry 2006;6:765-70.
DOI: 10.2174/138955706777698642
Leal LG, Lopes MA, Batista ML. Physical exercise-induced myokines and muscle-adipose tissue crosstalk: a review of current knowledge and the implications for health and metabolic diseases. Front Physiol 2018;9:1307.
DOI: 10.3389/fphys.2018.01307
Sánchez Pozo A, Gil Hernández A. Metabolismo lipídico tisular. En: Gil A (editor). Tratado de Nutrición. Tomo I. Madrid: Editorial Médica Panamericana; 2017. pp. 131-54.