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Volumn 23, Issue 1, 2012, Pages 187-199

Nutrition Strategies to Improve Physical Capabilities in Duchenne Muscular Dystrophy

Author keywords

Duchenne muscular dystrophy; Nutraceuticals; Nutrition; Physical activity

Indexed keywords

ALANINE; ARGININE; DEFLAZACORT; EPIGALLOCATECHIN GALLATE; GLUTAMINE; GREEN TEA EXTRACT; INITIATION FACTOR 4E BINDING PROTEIN 1; LEUCINE; MAMMALIAN TARGET OF RAPAMYCIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; NUTRACEUTICAL; PLACEBO; PREDNISOLONE; TAURINE;

EID: 84855732052     PISSN: 10479651     EISSN: 15581381     Source Type: Journal    
DOI: 10.1016/j.pmr.2011.11.010     Document Type: Review
Times cited : (16)

References (75)
  • 1
    • 0036591684 scopus 로고    scopus 로고
    • Muscular dystrophies involving the dystrophin-glycoprotein complex: an overview of current mouse models
    • Durbeej M., Campbell K.P. Muscular dystrophies involving the dystrophin-glycoprotein complex: an overview of current mouse models. Curr Opin Genet Dev 2002, 12(3):349-361.
    • (2002) Curr Opin Genet Dev , vol.12 , Issue.3 , pp. 349-361
    • Durbeej, M.1    Campbell, K.P.2
  • 2
    • 0036087342 scopus 로고    scopus 로고
    • Function and genetics of dystrophin and dystrophin-related proteins in muscle
    • Blake D.J., Weir A., Newey S.E., et al. Function and genetics of dystrophin and dystrophin-related proteins in muscle. Physiol Rev 2002, 82(2):291-329.
    • (2002) Physiol Rev , vol.82 , Issue.2 , pp. 291-329
    • Blake, D.J.1    Weir, A.2    Newey, S.E.3
  • 3
    • 33749015734 scopus 로고    scopus 로고
    • Molecular mechanisms of muscular dystrophies: old and new players
    • Davies K.E., Nowak K.J. Molecular mechanisms of muscular dystrophies: old and new players. Nat Rev Mol Cell Biol 2006, 7(10):762-773.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.10 , pp. 762-773
    • Davies, K.E.1    Nowak, K.J.2
  • 4
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • Ervasti J.M., Ohlendieck K., Kahl S.D., et al. Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature 1990, 345(6273):315-319.
    • (1990) Nature , vol.345 , Issue.6273 , pp. 315-319
    • Ervasti, J.M.1    Ohlendieck, K.2    Kahl, S.D.3
  • 5
    • 0027460658 scopus 로고
    • Dystrophin protects the sarcolemma from stresses developed during muscle contraction
    • Petrof B.J., Shrager J.B., Stedman H.H., et al. Dystrophin protects the sarcolemma from stresses developed during muscle contraction. Proc Natl Acad Sci USA 1993, 90(8):3710-3714.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.8 , pp. 3710-3714
    • Petrof, B.J.1    Shrager, J.B.2    Stedman, H.H.3
  • 6
    • 0031908112 scopus 로고    scopus 로고
    • The molecular basis of activity-induced muscle injury in Duchenne muscular dystrophy
    • Petrof B.J. The molecular basis of activity-induced muscle injury in Duchenne muscular dystrophy. Mol Cell Biochem 1998, 179(1-2):111-123.
    • (1998) Mol Cell Biochem , vol.179 , Issue.1-2 , pp. 111-123
    • Petrof, B.J.1
  • 7
    • 72149108443 scopus 로고    scopus 로고
    • Diagnosis and management of Duchenne muscular dystrophy, part 1: diagnosis, and pharmacological and psychosocial management
    • Bushby K., Finkel R., Birnkrant D.J., et al. Diagnosis and management of Duchenne muscular dystrophy, part 1: diagnosis, and pharmacological and psychosocial management. Lancet Neurol 2010, 9(1):77-93.
    • (2010) Lancet Neurol , vol.9 , Issue.1 , pp. 77-93
    • Bushby, K.1    Finkel, R.2    Birnkrant, D.J.3
  • 8
    • 70149093185 scopus 로고    scopus 로고
    • Areview of nutrition in Duchenne muscular dystrophy
    • Davidson Z.E., Truby H. Areview of nutrition in Duchenne muscular dystrophy. JHum Nutr Diet 2009, 22(5):383-393.
    • (2009) JHum Nutr Diet , vol.22 , Issue.5 , pp. 383-393
    • Davidson, Z.E.1    Truby, H.2
  • 9
    • 53049095685 scopus 로고    scopus 로고
    • Endurance capacity in maturing mdx mice is markedly enhanced by combined voluntary wheel running and green tea extract
    • Call J.A., Voelker K.A., Wolff A.V., et al. Endurance capacity in maturing mdx mice is markedly enhanced by combined voluntary wheel running and green tea extract. JAppl Physiol 2008, 105(3):923-932.
    • (2008) JAppl Physiol , vol.105 , Issue.3 , pp. 923-932
    • Call, J.A.1    Voelker, K.A.2    Wolff, A.V.3
  • 10
    • 76549130473 scopus 로고    scopus 로고
    • Diagnosis and management of Duchenne muscular dystrophy, part 2: implementation of multidisciplinary care
    • Bushby K., Finkel R., Birnkrant D.J., et al. Diagnosis and management of Duchenne muscular dystrophy, part 2: implementation of multidisciplinary care. Lancet Neurol 2010, 9(2):177-189.
    • (2010) Lancet Neurol , vol.9 , Issue.2 , pp. 177-189
    • Bushby, K.1    Finkel, R.2    Birnkrant, D.J.3
  • 11
    • 38949130017 scopus 로고    scopus 로고
    • Biology of the striated muscle dystrophin-glycoprotein complex
    • Ervasti J.M., Sonnemann K.J. Biology of the striated muscle dystrophin-glycoprotein complex. Int Rev Cytol 2008, 265:191-225.
    • (2008) Int Rev Cytol , vol.265 , pp. 191-225
    • Ervasti, J.M.1    Sonnemann, K.J.2
  • 12
    • 0036839039 scopus 로고    scopus 로고
    • Molecular pathophysiology of myofiber injury in deficiencies of the dystrophin-glycoprotein complex
    • Petrof B.J. Molecular pathophysiology of myofiber injury in deficiencies of the dystrophin-glycoprotein complex. Am J Phys Med Rehabil 2002, 81(Suppl 11):S162-S174.
    • (2002) Am J Phys Med Rehabil , vol.81 , Issue.SUPPL. 11
    • Petrof, B.J.1
  • 13
    • 84855746841 scopus 로고    scopus 로고
    • Enhancing translation: Guidelines for standard pre-clinical experiments in mdx mice
    • [Epub ahead of print]
    • Willmann R., De Luca A., Benatar M., et al. Enhancing translation: Guidelines for standard pre-clinical experiments in mdx mice. Neuromuscul Disord 2011, [Epub ahead of print].
    • (2011) Neuromuscul Disord
    • Willmann, R.1    De Luca, A.2    Benatar, M.3
  • 14
    • 63749096532 scopus 로고    scopus 로고
    • Mammalian animal models for Duchenne muscular dystrophy
    • Willmann R., Possekel S., Dubach-Powell J., et al. Mammalian animal models for Duchenne muscular dystrophy. Neuromuscul Disord 2009, 19(4):241-249.
    • (2009) Neuromuscul Disord , vol.19 , Issue.4 , pp. 241-249
    • Willmann, R.1    Possekel, S.2    Dubach-Powell, J.3
  • 15
    • 33846050073 scopus 로고    scopus 로고
    • Recommendations to define exercise prescription for Duchenne muscular dystrophy
    • Grange R.W., Call J.A. Recommendations to define exercise prescription for Duchenne muscular dystrophy. Exerc Sport Sci Rev 2007, 35(1):12-17.
    • (2007) Exerc Sport Sci Rev , vol.35 , Issue.1 , pp. 12-17
    • Grange, R.W.1    Call, J.A.2
  • 16
    • 79953063911 scopus 로고    scopus 로고
    • Exercise and Duchenne muscular dystrophy: toward evidence-based exercise prescription
    • Markert C.D., Ambrosio F., Call J.A., et al. Exercise and Duchenne muscular dystrophy: toward evidence-based exercise prescription. Muscle Nerve 2011, 43(4):464-478.
    • (2011) Muscle Nerve , vol.43 , Issue.4 , pp. 464-478
    • Markert, C.D.1    Ambrosio, F.2    Call, J.A.3
  • 17
    • 0014141634 scopus 로고
    • Studies of the carrier state in the Duchenne type of muscular dystrophy. I. Effect of exercise on serum creatine kinase activity
    • Hudgson P., Gardner-Medwin D., Pennington R.J., et al. Studies of the carrier state in the Duchenne type of muscular dystrophy. I. Effect of exercise on serum creatine kinase activity. JNeurol Neurosurg Psychiatry 1967, 30(5):416-419.
    • (1967) JNeurol Neurosurg Psychiatry , vol.30 , Issue.5 , pp. 416-419
    • Hudgson, P.1    Gardner-Medwin, D.2    Pennington, R.J.3
  • 18
    • 0017597748 scopus 로고
    • Exercise performance in 6-to-11-year-old boys with Duchenne muscular dystrophy
    • Sockolov R., Irwin B., Dressendorfer R.H., et al. Exercise performance in 6-to-11-year-old boys with Duchenne muscular dystrophy. Arch Phys Med Rehabil 1977, 58(5):195-201.
    • (1977) Arch Phys Med Rehabil , vol.58 , Issue.5 , pp. 195-201
    • Sockolov, R.1    Irwin, B.2    Dressendorfer, R.H.3
  • 19
    • 33144472648 scopus 로고    scopus 로고
    • Measurement of energy expenditure
    • Levine J.A. Measurement of energy expenditure. Public Health Nutr 2005, 8(7A):1123-1132.
    • (2005) Public Health Nutr , vol.8 , Issue.7 A , pp. 1123-1132
    • Levine, J.A.1
  • 20
    • 0032088943 scopus 로고    scopus 로고
    • American College of Sports Medicine Position Stand. The recommended quantity and quality of exercise for developing and maintaining cardiorespiratory and muscular fitness, and flexibility in healthy adults
    • American College of Sports Medicine Position Stand. The recommended quantity and quality of exercise for developing and maintaining cardiorespiratory and muscular fitness, and flexibility in healthy adults. Med Sci Sports Exerc 1998, 30(6):975-991.
    • (1998) Med Sci Sports Exerc , vol.30 , Issue.6 , pp. 975-991
  • 21
    • 0036133699 scopus 로고    scopus 로고
    • Creatine supplementation reduces skeletal muscle degeneration and enhances mitochondrial function in mdx mice
    • Passaquin A.C., Renard M., Kay L., et al. Creatine supplementation reduces skeletal muscle degeneration and enhances mitochondrial function in mdx mice. Neuromuscul Disord 2002, 12(2):174-182.
    • (2002) Neuromuscul Disord , vol.12 , Issue.2 , pp. 174-182
    • Passaquin, A.C.1    Renard, M.2    Kay, L.3
  • 22
    • 0036823498 scopus 로고    scopus 로고
    • Pharmacological control of cellular calcium handling in dystrophic skeletal muscle
    • Ruegg U.T., Nicolas-Metral V., Challet C., et al. Pharmacological control of cellular calcium handling in dystrophic skeletal muscle. Neuromuscul Disord 2002, 12(Suppl 1):S155-S161.
    • (2002) Neuromuscul Disord , vol.12 , Issue.SUPPL. 1
    • Ruegg, U.T.1    Nicolas-Metral, V.2    Challet, C.3
  • 23
    • 33646234945 scopus 로고    scopus 로고
    • Persistent and improved functional gain in mdx dystrophic mice after treatment with L-arginine and deflazacort
    • Archer J.D., Vargas C.C., Anderson J.E. Persistent and improved functional gain in mdx dystrophic mice after treatment with L-arginine and deflazacort. FASEB J 2006, 20(6):738-740.
    • (2006) FASEB J , vol.20 , Issue.6 , pp. 738-740
    • Archer, J.D.1    Vargas, C.C.2    Anderson, J.E.3
  • 24
    • 0031911224 scopus 로고    scopus 로고
    • Oral glutamine slows down whole body protein breakdown in Duchenne muscular dystrophy
    • Hankard R.G., Hammond D., Haymond M.W., et al. Oral glutamine slows down whole body protein breakdown in Duchenne muscular dystrophy. Pediatr Res 1998, 43(2):222-226.
    • (1998) Pediatr Res , vol.43 , Issue.2 , pp. 222-226
    • Hankard, R.G.1    Hammond, D.2    Haymond, M.W.3
  • 25
    • 33646694779 scopus 로고    scopus 로고
    • Oral glutamine and amino acid supplementation inhibit whole-body protein degradation in children with Duchenne muscular dystrophy
    • Mok E., Eleouet-Da Violante C., Daubrosse C., et al. Oral glutamine and amino acid supplementation inhibit whole-body protein degradation in children with Duchenne muscular dystrophy. Am J Clin Nutr 2006, 83(4):823-828.
    • (2006) Am J Clin Nutr , vol.83 , Issue.4 , pp. 823-828
    • Mok, E.1    Eleouet-Da Violante, C.2    Daubrosse, C.3
  • 26
    • 33846194248 scopus 로고    scopus 로고
    • Duchenne muscular dystrophy: focus on pharmaceutical and nutritional interventions
    • Radley H.G., De Luca A., Lynch G.S., et al. Duchenne muscular dystrophy: focus on pharmaceutical and nutritional interventions. Int J Biochem Cell Biol 2007, 39(3):469-477.
    • (2007) Int J Biochem Cell Biol , vol.39 , Issue.3 , pp. 469-477
    • Radley, H.G.1    De Luca, A.2    Lynch, G.S.3
  • 27
    • 0032531046 scopus 로고    scopus 로고
    • Effects of iron deprivation on the pathology and stress protein expression in murine X-linked muscular dystrophy
    • Bornman L., Rossouw H., Gericke G.S., et al. Effects of iron deprivation on the pathology and stress protein expression in murine X-linked muscular dystrophy. Biochem Pharmacol 1998, 56(6):751-757.
    • (1998) Biochem Pharmacol , vol.56 , Issue.6 , pp. 751-757
    • Bornman, L.1    Rossouw, H.2    Gericke, G.S.3
  • 28
    • 0034100628 scopus 로고    scopus 로고
    • Dystrophin mutations predict cellular susceptibility to oxidative stress
    • Disatnik M.H., Chamberlain J.S., Rando T.A. Dystrophin mutations predict cellular susceptibility to oxidative stress. Muscle Nerve 2000, 23(5):784-792.
    • (2000) Muscle Nerve , vol.23 , Issue.5 , pp. 784-792
    • Disatnik, M.H.1    Chamberlain, J.S.2    Rando, T.A.3
  • 29
    • 0032569827 scopus 로고    scopus 로고
    • Evidence of oxidative stress in mdx mouse muscle: studies of the pre-necrotic state
    • Disatnik M.H., Dhawan J., Yu Y., et al. Evidence of oxidative stress in mdx mouse muscle: studies of the pre-necrotic state. JNeurol Sci 1998, 161(1):77-84.
    • (1998) JNeurol Sci , vol.161 , Issue.1 , pp. 77-84
    • Disatnik, M.H.1    Dhawan, J.2    Yu, Y.3
  • 30
    • 0022966378 scopus 로고
    • Free radicals: a potential pathogenic mechanism in inherited muscular dystrophy
    • Murphy M.E., Kehrer J.P. Free radicals: a potential pathogenic mechanism in inherited muscular dystrophy. Life Sci 1986, 39(24):2271-2278.
    • (1986) Life Sci , vol.39 , Issue.24 , pp. 2271-2278
    • Murphy, M.E.1    Kehrer, J.P.2
  • 31
    • 0030861564 scopus 로고    scopus 로고
    • Oxidative stress as a potential pathogenic mechanism in an animal model of Duchenne muscular dystrophy
    • Ragusa R.J., Chow C.K., Porter J.D. Oxidative stress as a potential pathogenic mechanism in an animal model of Duchenne muscular dystrophy. Neuromuscul Disord 1997, 7(6-7):379-386.
    • (1997) Neuromuscul Disord , vol.7 , Issue.6-7 , pp. 379-386
    • Ragusa, R.J.1    Chow, C.K.2    Porter, J.D.3
  • 32
    • 0032007205 scopus 로고    scopus 로고
    • Muscle cells from mdx mice have an increased susceptibility to oxidative stress
    • Rando T.A., Disatnik M.H., Yu Y., et al. Muscle cells from mdx mice have an increased susceptibility to oxidative stress. Neuromuscul Disord 1998, 8(1):14-21.
    • (1998) Neuromuscul Disord , vol.8 , Issue.1 , pp. 14-21
    • Rando, T.A.1    Disatnik, M.H.2    Yu, Y.3
  • 33
    • 0036194789 scopus 로고    scopus 로고
    • Green tea extract decreases muscle necrosis in mdx mice and protects against reactive oxygen species
    • Buetler T.M., Renard M., Offord E.A., et al. Green tea extract decreases muscle necrosis in mdx mice and protects against reactive oxygen species. Am J Clin Nutr 2002, 75(4):749-753.
    • (2002) Am J Clin Nutr , vol.75 , Issue.4 , pp. 749-753
    • Buetler, T.M.1    Renard, M.2    Offord, E.A.3
  • 34
    • 33644854044 scopus 로고    scopus 로고
    • Green tea extract and its major polyphenol (-)-epigallocatechin gallate improve muscle function in a mouse model for Duchenne muscular dystrophy
    • Dorchies O.M., Wagner S., Vuadens O., et al. Green tea extract and its major polyphenol (-)-epigallocatechin gallate improve muscle function in a mouse model for Duchenne muscular dystrophy. Am J Physiol Cell Physiol 2006, 290(2):C616-C625.
    • (2006) Am J Physiol Cell Physiol , vol.290 , Issue.2
    • Dorchies, O.M.1    Wagner, S.2    Vuadens, O.3
  • 35
    • 77953537515 scopus 로고    scopus 로고
    • Green tea extract decreases muscle pathology and NF-kappaB immunostaining in regenerating muscle fibers of mdx mice
    • Evans N.P., Call J.A., Bassaganya-Riera J., et al. Green tea extract decreases muscle pathology and NF-kappaB immunostaining in regenerating muscle fibers of mdx mice. Clin Nutr 2010, 29(3):391-398.
    • (2010) Clin Nutr , vol.29 , Issue.3 , pp. 391-398
    • Evans, N.P.1    Call, J.A.2    Bassaganya-Riera, J.3
  • 36
    • 0033980371 scopus 로고    scopus 로고
    • Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increase eIF4F formation
    • Anthony J.C., Anthony T.G., Kimball S.R., et al. Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increase eIF4F formation. JNutr 2000, 130:139-145.
    • (2000) JNutr , vol.130 , pp. 139-145
    • Anthony, J.C.1    Anthony, T.G.2    Kimball, S.R.3
  • 37
    • 0023519957 scopus 로고
    • Leucine, glucose, and energy metabolism after 3 days of fasting in healthy human subjects
    • Nair K.S., Woolf P.D., Welle S.L., et al. Leucine, glucose, and energy metabolism after 3 days of fasting in healthy human subjects. Am J Clin Nutr 1987, 46(4):557-562.
    • (1987) Am J Clin Nutr , vol.46 , Issue.4 , pp. 557-562
    • Nair, K.S.1    Woolf, P.D.2    Welle, S.L.3
  • 38
    • 32444435321 scopus 로고    scopus 로고
    • Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise
    • Norton L.E., Layman D.K. Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise. JNutr 2006, 136(2):533S-537S.
    • (2006) JNutr , vol.136 , Issue.2
    • Norton, L.E.1    Layman, D.K.2
  • 39
    • 0035100128 scopus 로고    scopus 로고
    • Nitrogen shuttling between neurons and glial cells during glutamate synthesis
    • Lieth E., LaNoue K.F., Berkich D.A., et al. Nitrogen shuttling between neurons and glial cells during glutamate synthesis. JNeurochem 2001, 76(6):1712-1723.
    • (2001) JNeurochem , vol.76 , Issue.6 , pp. 1712-1723
    • Lieth, E.1    LaNoue, K.F.2    Berkich, D.A.3
  • 40
    • 70349604105 scopus 로고    scopus 로고
    • Regulation of muscle protein degradation, not synthesis, by dietary leucine in rats fed a protein-deficient diet
    • Sugawara T., Ito Y., Nishizawa N., et al. Regulation of muscle protein degradation, not synthesis, by dietary leucine in rats fed a protein-deficient diet. Amino Acids 2009, 37(4):609-616.
    • (2009) Amino Acids , vol.37 , Issue.4 , pp. 609-616
    • Sugawara, T.1    Ito, Y.2    Nishizawa, N.3
  • 41
    • 33646084399 scopus 로고    scopus 로고
    • Regulation of cardiac and skeletal muscle protein synthesis by individual branched-chain amino acids in neonatal pigs
    • Escobar J., Frank J.W., Suryawan A., et al. Regulation of cardiac and skeletal muscle protein synthesis by individual branched-chain amino acids in neonatal pigs. Am J Physiol Endocrinol Metab 2006, 290:612-621.
    • (2006) Am J Physiol Endocrinol Metab , vol.290 , pp. 612-621
    • Escobar, J.1    Frank, J.W.2    Suryawan, A.3
  • 42
    • 17444390819 scopus 로고    scopus 로고
    • Physiological rise in plasma leucine stimulates muscle protein synthesis in neonatal pigs by enhancing translation initiation factor activation
    • Escobar J., Frank J.W., Suryawan A., et al. Physiological rise in plasma leucine stimulates muscle protein synthesis in neonatal pigs by enhancing translation initiation factor activation. Am J Physiol Endocrinol Metab 2005, 288(5):E914-E921.
    • (2005) Am J Physiol Endocrinol Metab , vol.288 , Issue.5
    • Escobar, J.1    Frank, J.W.2    Suryawan, A.3
  • 43
    • 37149026351 scopus 로고    scopus 로고
    • Amino acid availability and age affect the leucine stimulation of protein synthesis and eIF4F formation in muscle
    • Escobar J., Frank J.W., Suryawan A., et al. Amino acid availability and age affect the leucine stimulation of protein synthesis and eIF4F formation in muscle. Am J Physiol Endocrinol Metab 2007, 293(6):E1615-E1621.
    • (2007) Am J Physiol Endocrinol Metab , vol.293 , Issue.6
    • Escobar, J.1    Frank, J.W.2    Suryawan, A.3
  • 44
    • 0021130551 scopus 로고
    • Clinical investigation in Duchenne muscular dystrophy: IV. Double-blind controlled trial of leucine
    • Mendell J.R., Griggs R.C., Moxley R.T., et al. Clinical investigation in Duchenne muscular dystrophy: IV. Double-blind controlled trial of leucine. Muscle Nerve 1984, 7(7):535-541.
    • (1984) Muscle Nerve , vol.7 , Issue.7 , pp. 535-541
    • Mendell, J.R.1    Griggs, R.C.2    Moxley, R.T.3
  • 45
    • 77957661352 scopus 로고    scopus 로고
    • Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice
    • D'Antona G., Ragni M., Cardile A., et al. Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice. Cell Metab 2010, 12(4):362-372.
    • (2010) Cell Metab , vol.12 , Issue.4 , pp. 362-372
    • D'Antona, G.1    Ragni, M.2    Cardile, A.3
  • 46
    • 0033808169 scopus 로고    scopus 로고
    • Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway
    • Anthony J.C., Yoshizawa F., Anthony T.G., et al. Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. JNutr 2000, 130(10):2413-2419.
    • (2000) JNutr , vol.130 , Issue.10 , pp. 2413-2419
    • Anthony, J.C.1    Yoshizawa, F.2    Anthony, T.G.3
  • 47
    • 0016824053 scopus 로고
    • Leucine. A possible regulator of protein turnover in muscle
    • Buse M.G., Reid S.S. Leucine. A possible regulator of protein turnover in muscle. JClin Invest 1975, 56:1250-1261.
    • (1975) JClin Invest , vol.56 , pp. 1250-1261
    • Buse, M.G.1    Reid, S.S.2
  • 48
    • 0036238940 scopus 로고    scopus 로고
    • Branched-chain amino acids: a role in skeletal muscle proteolysis in catabolic states?
    • Busquets S., Alvarez B., Lopez-Soriano F.J., et al. Branched-chain amino acids: a role in skeletal muscle proteolysis in catabolic states?. JCell Physiol 2002, 191(3):283-289.
    • (2002) JCell Physiol , vol.191 , Issue.3 , pp. 283-289
    • Busquets, S.1    Alvarez, B.2    Lopez-Soriano, F.J.3
  • 49
    • 0016431688 scopus 로고
    • Effects of insulin, glucose, and amino acids on protein turnover in rat diaphragm
    • Fulks R.M., Li J.B., Goldberg A.L. Effects of insulin, glucose, and amino acids on protein turnover in rat diaphragm. JBiol Chem 1975, 250(1):290-298.
    • (1975) JBiol Chem , vol.250 , Issue.1 , pp. 290-298
    • Fulks, R.M.1    Li, J.B.2    Goldberg, A.L.3
  • 50
    • 0021259503 scopus 로고
    • Effects of leucine on invitro protein synthesis and degradation in rat skeletal muscles
    • Hong S.O., Layman D.K. Effects of leucine on invitro protein synthesis and degradation in rat skeletal muscles. JNutr 1984, 114:1204-1212.
    • (1984) JNutr , vol.114 , pp. 1204-1212
    • Hong, S.O.1    Layman, D.K.2
  • 51
    • 24644499561 scopus 로고    scopus 로고
    • Leucine suppresses myofibrillar proteolysis by down-regulating ubiquitin-proteasome pathway in chick skeletal muscles
    • 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(2):660-666.
    • (2005) Biochem Biophys Res Commun , vol.336 , Issue.2 , pp. 660-666
    • Nakashima, K.1    Ishida, A.2    Yamazaki, M.3
  • 52
    • 78650510609 scopus 로고    scopus 로고
    • MTOR: from growth signal integration to cancer, diabetes and ageing
    • Zoncu R., Efeyan A., Sabatini D.M. mTOR: from growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol 2011, 12(1):21-35.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.1 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 53
    • 48649085816 scopus 로고    scopus 로고
    • Regulation of TORC1 by Rag GTPases in nutrient response
    • Kim E., Goraksha-Hicks P., Li L., et al. Regulation of TORC1 by Rag GTPases in nutrient response. Nat Cell Biol 2008, 10(8):935-945.
    • (2008) Nat Cell Biol , vol.10 , Issue.8 , pp. 935-945
    • Kim, E.1    Goraksha-Hicks, P.2    Li, L.3
  • 54
    • 45849105156 scopus 로고    scopus 로고
    • The Rag GTPases bind raptor andmediate amino acid signaling to mTORC1
    • Sancak Y., Peterson T.R., Shaul Y.D., et al. The Rag GTPases bind raptor andmediate amino acid signaling to mTORC1. Science 2008, 320(5882):1496-1501.
    • (2008) Science , vol.320 , Issue.5882 , pp. 1496-1501
    • Sancak, Y.1    Peterson, T.R.2    Shaul, Y.D.3
  • 55
    • 34548028705 scopus 로고    scopus 로고
    • 4E-binding protein 1: a key molecular "funnel factor" in human cancer with clinical implications
    • Armengol G., Rojo F., Castellvi J., et al. 4E-binding protein 1: a key molecular "funnel factor" in human cancer with clinical implications. Cancer Res 2007, 67(16):7551-7555.
    • (2007) Cancer Res , vol.67 , Issue.16 , pp. 7551-7555
    • Armengol, G.1    Rojo, F.2    Castellvi, J.3
  • 57
    • 0032560521 scopus 로고    scopus 로고
    • Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway
    • Scott P.H., Brunn G.J., Kohn A.D., et al. Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway. Proc Natl Acad Sci USA 1998, 95(13):7772-7777.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.13 , pp. 7772-7777
    • Scott, P.H.1    Brunn, G.J.2    Kohn, A.D.3
  • 58
    • 77954235821 scopus 로고    scopus 로고
    • Targeting mTOR: prospects for mTOR complex 2 inhibitors in cancer therapy
    • Sparks C.A., Guertin D.A. Targeting mTOR: prospects for mTOR complex 2 inhibitors in cancer therapy. Oncogene 2010, 29(26):3733-3744.
    • (2010) Oncogene , vol.29 , Issue.26 , pp. 3733-3744
    • Sparks, C.A.1    Guertin, D.A.2
  • 59
    • 0036753494 scopus 로고    scopus 로고
    • Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control
    • Loewith R., Jacinto E., Wullschleger S., et al. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol Cell 2002, 10(3):457-468.
    • (2002) Mol Cell , vol.10 , Issue.3 , pp. 457-468
    • Loewith, R.1    Jacinto, E.2    Wullschleger, S.3
  • 60
    • 67349241955 scopus 로고    scopus 로고
    • DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival
    • Peterson T.R., Laplante M., Thoreen C.C., et al. DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival. Cell 2009, 137(5):873-886.
    • (2009) Cell , vol.137 , Issue.5 , pp. 873-886
    • Peterson, T.R.1    Laplante, M.2    Thoreen, C.C.3
  • 61
    • 79953216041 scopus 로고    scopus 로고
    • Evidence for direct activation of mTORC2 kinase activity by phosphatidylinositol 3,4,5-trisphosphate
    • Gan X., Wang J., Su B., et al. Evidence for direct activation of mTORC2 kinase activity by phosphatidylinositol 3,4,5-trisphosphate. JBiol Chem 2011, 286(13):10998-11002.
    • (2011) JBiol Chem , vol.286 , Issue.13 , pp. 10998-11002
    • Gan, X.1    Wang, J.2    Su, B.3
  • 62
    • 33646023695 scopus 로고    scopus 로고
    • Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB
    • Sarbassov D.D., Ali S.M., Sengupta S., et al. Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB. Mol Cell 2006, 22(2):159-168.
    • (2006) Mol Cell , vol.22 , Issue.2 , pp. 159-168
    • Sarbassov, D.D.1    Ali, S.M.2    Sengupta, S.3
  • 63
    • 35348832340 scopus 로고    scopus 로고
    • Identification of IRS-1 Ser-1101 as a target of S6K1 in nutrient- and obesity-induced insulin resistance
    • Tremblay F., Brule S., Um S.H., et al. Identification of IRS-1 Ser-1101 as a target of S6K1 in nutrient- and obesity-induced insulin resistance. Proc Natl Acad Sci USA 2007, 104:14056-14061.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14056-14061
    • Tremblay, F.1    Brule, S.2    Um, S.H.3
  • 64
    • 33744505375 scopus 로고    scopus 로고
    • Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1
    • Um S.H., D'Alessio D., Thomas G. Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1. Cell Metab 2006, 3:393-402.
    • (2006) Cell Metab , vol.3 , pp. 393-402
    • Um, S.H.1    D'Alessio, D.2    Thomas, G.3
  • 65
    • 80055027842 scopus 로고    scopus 로고
    • Mammalian target of rapamycin: a central node of complex signaling cascades
    • Dobashi Y., Watanabe Y., Miwa C., et al. Mammalian target of rapamycin: a central node of complex signaling cascades. Int J Clin Exp Pathol 2011, 4(5):476-495.
    • (2011) Int J Clin Exp Pathol , vol.4 , Issue.5 , pp. 476-495
    • Dobashi, Y.1    Watanabe, Y.2    Miwa, C.3
  • 66
    • 70350545722 scopus 로고    scopus 로고
    • Characterization of Rictor phosphorylation sites reveals direct regulation of mTOR complex 2 by S6K1
    • Dibble C.C., Asara J.M., Manning B.D. Characterization of Rictor phosphorylation sites reveals direct regulation of mTOR complex 2 by S6K1. Mol Cell Biol 2009, 29(21):5657-5670.
    • (2009) Mol Cell Biol , vol.29 , Issue.21 , pp. 5657-5670
    • Dibble, C.C.1    Asara, J.M.2    Manning, B.D.3
  • 67
    • 79958696694 scopus 로고    scopus 로고
    • The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling
    • Hsu P.P., Kang S.A., Rameseder J., et al. The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling. Science 2011, 332(6035):1317-1322.
    • (2011) Science , vol.332 , Issue.6035 , pp. 1317-1322
    • Hsu, P.P.1    Kang, S.A.2    Rameseder, J.3
  • 68
    • 79958696336 scopus 로고    scopus 로고
    • Phosphoproteomic analysis identifies Grb10 as an mTORC1 substrate that negatively regulates insulin signaling
    • Yu Y., Yoon S.O., Poulogiannis G., et al. Phosphoproteomic analysis identifies Grb10 as an mTORC1 substrate that negatively regulates insulin signaling. Science 2011, 332(6035):1322-1326.
    • (2011) Science , vol.332 , Issue.6035 , pp. 1322-1326
    • Yu, Y.1    Yoon, S.O.2    Poulogiannis, G.3
  • 69
    • 0035291054 scopus 로고    scopus 로고
    • Effect of a leucine-supplemented diet on body composition changes in pregnant rats bearing Walker 256 tumor
    • Ventrucci G., Mello M.A., Gomes-Marcondes M.C. Effect of a leucine-supplemented diet on body composition changes in pregnant rats bearing Walker 256 tumor. Braz J Med Biol Res 2001, 34(3):333-338.
    • (2001) Braz J Med Biol Res , vol.34 , Issue.3 , pp. 333-338
    • Ventrucci, G.1    Mello, M.A.2    Gomes-Marcondes, M.C.3
  • 70
    • 0242659264 scopus 로고    scopus 로고
    • Aleucine-supplemented diet improved protein content of skeletal muscle in young tumor-bearing rats
    • Gomes-Marcondes M.C., Ventrucci G., Toledo M.T., et al. Aleucine-supplemented diet improved protein content of skeletal muscle in young tumor-bearing rats. Braz J Med Biol Res 2003, 36(11):1589-1594.
    • (2003) Braz J Med Biol Res , vol.36 , Issue.11 , pp. 1589-1594
    • Gomes-Marcondes, M.C.1    Ventrucci, G.2    Toledo, M.T.3
  • 71
    • 33747068292 scopus 로고    scopus 로고
    • Nutrition modulation of cachexia/proteolysis
    • Siddiqui R., Pandya D., Harvey K., et al. Nutrition modulation of cachexia/proteolysis. Nutr Clin Pract 2006, 21(2):155-167.
    • (2006) Nutr Clin Pract , vol.21 , Issue.2 , pp. 155-167
    • Siddiqui, R.1    Pandya, D.2    Harvey, K.3
  • 72
    • 33947729996 scopus 로고    scopus 로고
    • Leucine-rich dietalters the eukaryotic translation initiation factors expression in skeletal muscle of tumour-bearing rats
    • Ventrucci G., Mello M.A., Gomes-Marcondes M.C., et al. Leucine-rich dietalters the eukaryotic translation initiation factors expression in skeletal muscle of tumour-bearing rats. BMC Cancer 2007, 7:42.
    • (2007) BMC Cancer , vol.7 , pp. 42
    • Ventrucci, G.1    Mello, M.A.2    Gomes-Marcondes, M.C.3
  • 73
    • 31544449110 scopus 로고    scopus 로고
    • Therapeutic use of branched-chain amino acids in burn, trauma, and sepsis
    • De Bandt J.P., Cynober L. Therapeutic use of branched-chain amino acids in burn, trauma, and sepsis. JNutr 2006, 136(Suppl 1):308S-313S.
    • (2006) JNutr , vol.136 , Issue.SUPPL. 1
    • De Bandt, J.P.1    Cynober, L.2
  • 74
    • 34548074950 scopus 로고    scopus 로고
    • Nutrient signaling components controlling protein synthesis in striated muscle
    • Vary T.C., Lynch C.J. Nutrient signaling components controlling protein synthesis in striated muscle. JNutr 2007, 137(8):1835-1843.
    • (2007) JNutr , vol.137 , Issue.8 , pp. 1835-1843
    • Vary, T.C.1    Lynch, C.J.2
  • 75
    • 0037215644 scopus 로고    scopus 로고
    • Enhanced dystrophic progression in mdx mice by exercise and beneficial effects of taurine and insulin-like growth factor-1
    • De Luca A., Pierno S., Liantonio A., et al. Enhanced dystrophic progression in mdx mice by exercise and beneficial effects of taurine and insulin-like growth factor-1. JPharmacol Exp Ther 2003, 304(1):453-463.
    • (2003) JPharmacol Exp Ther , vol.304 , Issue.1 , pp. 453-463
    • De Luca, A.1    Pierno, S.2    Liantonio, A.3


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