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Volumn 19, Issue 4, 2008, Pages 207-215

Mechanisms through which sulfur amino acids control protein metabolism and oxidative status

Author keywords

Amino acid signaling; Cysteine; Methionine; Oxidative stress; Protein turnover

Indexed keywords

ANTIOXIDANT; CYSTEINE; GLUTATHIONE; GLUTATHIONE DISULFIDE; MAMMALIAN TARGET OF RAPAMYCIN; MESSENGER RNA; METHIONINE; METHIONINE SULFOXIDE REDUCTASE; PHOSPHOTRANSFERASE; REACTIVE OXYGEN METABOLITE; SULFATE; SULFUR AMINO ACID; TAURINE;

EID: 39849110778     PISSN: 09552863     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2007.05.006     Document Type: Review
Times cited : (226)

References (97)
  • 1
    • 0041059591 scopus 로고    scopus 로고
    • Integration of protein metabolism within the whole body and between organs
    • Lobley G.E., White A., and MacRae J.C. (Eds), EAAP Publication, Wageningen (Netherlands)
    • Nieto R., and Lobley G.E. Integration of protein metabolism within the whole body and between organs. In: Lobley G.E., White A., and MacRae J.C. (Eds). Protein metabolism and nutrition vol. 96 (1999), EAAP Publication, Wageningen (Netherlands) 69-99
    • (1999) Protein metabolism and nutrition , vol.96 , pp. 69-99
    • Nieto, R.1    Lobley, G.E.2
  • 2
    • 4244154841 scopus 로고
    • Métabolisme protéique chez le poulet en croissance. Effet des protéines alimentaires
    • Tesseraud S. Métabolisme protéique chez le poulet en croissance. Effet des protéines alimentaires. INRA Productions Animales 8 (1995) 197-212
    • (1995) INRA Productions Animales , vol.8 , pp. 197-212
    • Tesseraud, S.1
  • 3
    • 0029188005 scopus 로고
    • Nutrient regulation of skeletal muscle protein metabolism in animals. The involvement of hormones and substrates
    • Grizard J., Dardevet D., Papet I., Mosoni L., Patureau-Mirand P., Attaix D., et al. Nutrient regulation of skeletal muscle protein metabolism in animals. The involvement of hormones and substrates. Nutr Res Rev 8 (1995) 67-91
    • (1995) Nutr Res Rev , vol.8 , pp. 67-91
    • Grizard, J.1    Dardevet, D.2    Papet, I.3    Mosoni, L.4    Patureau-Mirand, P.5    Attaix, D.6
  • 4
    • 0003638496 scopus 로고    scopus 로고
    • Regulation of muscle growth and development
    • Lobley G.E., White A., and MacRae J.C. (Eds), EAAP Publication, Wageningen (Netherlands)
    • Grizard J., Picard B., Dardevet D., Balage M., and Rochon C. Regulation of muscle growth and development. In: Lobley G.E., White A., and MacRae J.C. (Eds). Protein metabolism and nutrition vol. 96 (1999), EAAP Publication, Wageningen (Netherlands) 177-201
    • (1999) Protein metabolism and nutrition , vol.96 , pp. 177-201
    • Grizard, J.1    Picard, B.2    Dardevet, D.3    Balage, M.4    Rochon, C.5
  • 5
    • 0002902303 scopus 로고    scopus 로고
    • Nutritional and hormonal control of muscle and peripheral tissue metabolism in farm species
    • Lobley G.E. Nutritional and hormonal control of muscle and peripheral tissue metabolism in farm species. Livest Production Sci 56 (1998) 91-114
    • (1998) Livest Production Sci , vol.56 , pp. 91-114
    • Lobley, G.E.1
  • 6
    • 84974379418 scopus 로고
    • Nutrition and whole-body protein turnover in the chicken in relation to mammalian species
    • Muramatsu T. Nutrition and whole-body protein turnover in the chicken in relation to mammalian species. Nutr Res Rev 3 (1990) 211-228
    • (1990) Nutr Res Rev , vol.3 , pp. 211-228
    • Muramatsu, T.1
  • 8
    • 0024548847 scopus 로고
    • Influence of nutrient intake on protein turnover
    • McNurlan M.A., and Garlick P.J. Influence of nutrient intake on protein turnover. Diabetes Metab Rev 5 (1989) 165-189
    • (1989) Diabetes Metab Rev , vol.5 , pp. 165-189
    • McNurlan, M.A.1    Garlick, P.J.2
  • 9
    • 33646788078 scopus 로고    scopus 로고
    • Comparative species utilization and toxicity of sulfur amino acids
    • Baker D.H. Comparative species utilization and toxicity of sulfur amino acids. J Nutr 136 6 (2006) 1670S-1675S
    • (2006) J Nutr , vol.136 , Issue.6
    • Baker, D.H.1
  • 10
    • 0022772947 scopus 로고
    • The effect of single essential amino acid deprivation on chick growth and nitrogen and energy balances at ad libitum- and equalized-food intakes
    • Kino K., and Okumura J. The effect of single essential amino acid deprivation on chick growth and nitrogen and energy balances at ad libitum- and equalized-food intakes. Poult Sci 65 9 (1986) 1728-1735
    • (1986) Poult Sci , vol.65 , Issue.9 , pp. 1728-1735
    • Kino, K.1    Okumura, J.2
  • 11
    • 0028799371 scopus 로고
    • Methionine deficiency decreases protein accretion and synthesis but not tRNA acylation in muscles of chicks
    • Barnes D.M., Calvert C.C., and Klasing K.C. Methionine deficiency decreases protein accretion and synthesis but not tRNA acylation in muscles of chicks. J Nutr 125 10 (1995) 2623-2630
    • (1995) J Nutr , vol.125 , Issue.10 , pp. 2623-2630
    • Barnes, D.M.1    Calvert, C.C.2    Klasing, K.C.3
  • 12
    • 0003045315 scopus 로고
    • Utilization of precursors for l-amino acids
    • D'Mello J.P.F. (Ed), CAB International, Wallingford (UK)
    • Baker D.H. Utilization of precursors for l-amino acids. In: D'Mello J.P.F. (Ed). Amino acids in farm animal nutrition (1994), CAB International, Wallingford (UK) 37-61
    • (1994) Amino acids in farm animal nutrition , pp. 37-61
    • Baker, D.H.1
  • 13
    • 0027373986 scopus 로고
    • Intestinal absorption and renal excretion of dietary methionine sources by the growing chicken
    • Esteve-Garcia E., and Austic R.E. Intestinal absorption and renal excretion of dietary methionine sources by the growing chicken. J Nutr Biochem 4 (1993) 576-587
    • (1993) J Nutr Biochem , vol.4 , pp. 576-587
    • Esteve-Garcia, E.1    Austic, R.E.2
  • 14
    • 0031225879 scopus 로고    scopus 로고
    • Performance, breast meat yield and abdominal fat deposition of male broiler chickens fed diets supplemented with dl-methionine or dl-methionine hydroxy analogue free acid
    • Esteve-Garcia E., and Llaurado L.L. Performance, breast meat yield and abdominal fat deposition of male broiler chickens fed diets supplemented with dl-methionine or dl-methionine hydroxy analogue free acid. Br Poult Sci 38 4 (1997) 397-404
    • (1997) Br Poult Sci , vol.38 , Issue.4 , pp. 397-404
    • Esteve-Garcia, E.1    Llaurado, L.L.2
  • 15
    • 0036614980 scopus 로고    scopus 로고
    • Relative effectiveness of methionine hydroxy analog compared to dl-methionine in broiler chickens
    • Lemme A., Hoehler D., Brennan J.J., and Mannion P.F. Relative effectiveness of methionine hydroxy analog compared to dl-methionine in broiler chickens. Poult Sci 81 6 (2002) 838-845
    • (2002) Poult Sci , vol.81 , Issue.6 , pp. 838-845
    • Lemme, A.1    Hoehler, D.2    Brennan, J.J.3    Mannion, P.F.4
  • 16
    • 0029300494 scopus 로고
    • Biological efficacy and absorption of dl-methionine hydroxy analogue free acid compared to dl-methionine in chickens as affected by heat stress
    • Rostagno H.S., and Barbosa W.A. Biological efficacy and absorption of dl-methionine hydroxy analogue free acid compared to dl-methionine in chickens as affected by heat stress. Br Poult Sci 36 2 (1995) 303-312
    • (1995) Br Poult Sci , vol.36 , Issue.2 , pp. 303-312
    • Rostagno, H.S.1    Barbosa, W.A.2
  • 17
    • 0029936656 scopus 로고    scopus 로고
    • Methionine and 2-hydroxy-4-methylthiobutanoic acid are partially converted to nonabsorbed compounds during passage through the small intestine and heat exposure does not affect small intestinal absorption of methionine sources in broiler chicks
    • Maenz D.D., and Engele-Schaan C. Methionine and 2-hydroxy-4-methylthiobutanoic acid are partially converted to nonabsorbed compounds during passage through the small intestine and heat exposure does not affect small intestinal absorption of methionine sources in broiler chicks. J Nutr 126 (1996) 1438-1444
    • (1996) J Nutr , vol.126 , pp. 1438-1444
    • Maenz, D.D.1    Engele-Schaan, C.2
  • 18
    • 0010043261 scopus 로고
    • Metabolism of methionine and its nutritional analogs
    • Saunderson C.L. Metabolism of methionine and its nutritional analogs. Poult Int 30 (1991) 34-38
    • (1991) Poult Int , vol.30 , pp. 34-38
    • Saunderson, C.L.1
  • 19
    • 33645819562 scopus 로고    scopus 로고
    • Oligomers are not the limiting factor in the absorption of dl-2-hydroxy-4-(methylthio)butanoic acid in the chicken small intestine
    • Martin-Venegas R., Soriano-Garcia J.F., Vinardell M.P., Geraert P.A., and Ferrer R. Oligomers are not the limiting factor in the absorption of dl-2-hydroxy-4-(methylthio)butanoic acid in the chicken small intestine. Poult Sci 85 1 (2006) 56-63
    • (2006) Poult Sci , vol.85 , Issue.1 , pp. 56-63
    • Martin-Venegas, R.1    Soriano-Garcia, J.F.2    Vinardell, M.P.3    Geraert, P.A.4    Ferrer, R.5
  • 20
    • 0021086336 scopus 로고
    • Utilization of supplemental methionine sources by primary cultures of chick hepatocytes
    • Dibner J.J. Utilization of supplemental methionine sources by primary cultures of chick hepatocytes. J Nutr 113 10 (1983) 2116-2123
    • (1983) J Nutr , vol.113 , Issue.10 , pp. 2116-2123
    • Dibner, J.J.1
  • 21
    • 0345168959 scopus 로고    scopus 로고
    • Dietary cysteine reduces the methionine requirement by an equal proportion in both parenterally and enterally fed piglets
    • Shoveller A.K., Brunton J.A., House J.D., Pencharz P.B., and Ball R.O. Dietary cysteine reduces the methionine requirement by an equal proportion in both parenterally and enterally fed piglets. J Nutr 133 12 (2003) 4215-4224
    • (2003) J Nutr , vol.133 , Issue.12 , pp. 4215-4224
    • Shoveller, A.K.1    Brunton, J.A.2    House, J.D.3    Pencharz, P.B.4    Ball, R.O.5
  • 22
    • 0034578346 scopus 로고    scopus 로고
    • Cysteine and glutathione in catabolic states
    • Proteins, peptides and amino acids in enteral nutrition. Fürst P., and Young V. (Eds), Vevey/S. Karger AG, Basel
    • Breuille D., and Obled C. Cysteine and glutathione in catabolic states. In: Fürst P., and Young V. (Eds). Proteins, peptides and amino acids in enteral nutrition. Nestlé Nutrition Workshop Series Clinical & Performance Program, Nestec Ltd. vol. 3 (2000), Vevey/S. Karger AG, Basel 173-197
    • (2000) Nestlé Nutrition Workshop Series Clinical & Performance Program, Nestec Ltd. , vol.3 , pp. 173-197
    • Breuille, D.1    Obled, C.2
  • 23
    • 0036517075 scopus 로고    scopus 로고
    • Metabolic bases of amino acid requirements in acute diseases
    • Obled C., Papet I., and Breuille D. Metabolic bases of amino acid requirements in acute diseases. Curr Opin Clin Nutr Metab Care 5 2 (2002) 189-197
    • (2002) Curr Opin Clin Nutr Metab Care , vol.5 , Issue.2 , pp. 189-197
    • Obled, C.1    Papet, I.2    Breuille, D.3
  • 25
    • 0034109894 scopus 로고    scopus 로고
    • Glutathione turnover is increased during the acute phase of sepsis in rats
    • Malmezat T., Breuille D., Capitan P., Mirand P.P., and Obled C. Glutathione turnover is increased during the acute phase of sepsis in rats. J Nutr 130 5 (2000) 1239-1246
    • (2000) J Nutr , vol.130 , Issue.5 , pp. 1239-1246
    • Malmezat, T.1    Breuille, D.2    Capitan, P.3    Mirand, P.P.4    Obled, C.5
  • 26
    • 0031885973 scopus 로고    scopus 로고
    • Metabolism of cysteine is modified during the acute phase of sepsis in rats
    • Malmezat T., Breuille D., Pouyet C., Mirand P.P., and Obled C. Metabolism of cysteine is modified during the acute phase of sepsis in rats. J Nutr 128 1 (1998) 97-105
    • (1998) J Nutr , vol.128 , Issue.1 , pp. 97-105
    • Malmezat, T.1    Breuille, D.2    Pouyet, C.3    Mirand, P.P.4    Obled, C.5
  • 27
    • 33644851743 scopus 로고    scopus 로고
    • Methionine kinetics are altered in the elderly both in the basal state and after vaccination
    • Mercier S., Breuille D., Buffiere C., Gimonet J., Papet I., Mirand P.P., et al. Methionine kinetics are altered in the elderly both in the basal state and after vaccination. Am J Clin Nutr 83 2 (2006) 291-298
    • (2006) Am J Clin Nutr , vol.83 , Issue.2 , pp. 291-298
    • Mercier, S.1    Breuille, D.2    Buffiere, C.3    Gimonet, J.4    Papet, I.5    Mirand, P.P.6
  • 28
    • 33750080166 scopus 로고    scopus 로고
    • Conversion of the methionine hydroxy analogue, dl-2-hydroxy-(4-methylthio) butanoic acid, to sulfur-containing amino acids in the chicken small intestine
    • Martin-Venegas R., Geraert P.A., and Ferrer R. Conversion of the methionine hydroxy analogue, dl-2-hydroxy-(4-methylthio) butanoic acid, to sulfur-containing amino acids in the chicken small intestine. Poult Sci 85 (2006) 1932-1938
    • (2006) Poult Sci , vol.85 , pp. 1932-1938
    • Martin-Venegas, R.1    Geraert, P.A.2    Ferrer, R.3
  • 29
    • 0347627140 scopus 로고    scopus 로고
    • Amino acid signalling and the integration of metabolism
    • Meijer A.J., and Dubbelhuis P. Amino acid signalling and the integration of metabolism. Biochem Biophys Res Commun 313 (2004) 397-403
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 397-403
    • Meijer, A.J.1    Dubbelhuis, P.2
  • 30
    • 0036440779 scopus 로고    scopus 로고
    • Regulation of mammalian translation factors by nutrients
    • Proud C.G. Regulation of mammalian translation factors by nutrients. Eur J Biochem 269 (2002) 5338-5349
    • (2002) Eur J Biochem , vol.269 , pp. 5338-5349
    • Proud, C.G.1
  • 31
    • 33744505375 scopus 로고    scopus 로고
    • Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1
    • Um S.H., D'Alessio D., and Thomas G. Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1. Cell Metab 3 6 (2006) 393-402
    • (2006) Cell Metab , vol.3 , Issue.6 , pp. 393-402
    • Um, S.H.1    D'Alessio, D.2    Thomas, G.3
  • 33
    • 2442463314 scopus 로고    scopus 로고
    • Molecular mechanisms through which amino acids mediate signaling through the mammalian target of rapamycin
    • Kimball S.R., and Jefferson L.S. Molecular mechanisms through which amino acids mediate signaling through the mammalian target of rapamycin. Curr Opin Clin Nutr Metab Care 7 (2004) 39-44
    • (2004) Curr Opin Clin Nutr Metab Care , vol.7 , pp. 39-44
    • Kimball, S.R.1    Jefferson, L.S.2
  • 34
    • 33644868345 scopus 로고    scopus 로고
    • New functions for amino acids: effects on gene transcription and translation
    • Kimball S.R., and Jefferson L.S. New functions for amino acids: effects on gene transcription and translation. Am J Clin Nutr 83 (2006) 500S-507S
    • (2006) Am J Clin Nutr , vol.83
    • Kimball, S.R.1    Jefferson, L.S.2
  • 35
    • 0347627139 scopus 로고    scopus 로고
    • mTOR-mediated regulation of translation factors by amino acids
    • Proud C.G. mTOR-mediated regulation of translation factors by amino acids. Biochem Biophys Res Communications 313 (2004) 429-436
    • (2004) Biochem Biophys Res Communications , vol.313 , pp. 429-436
    • Proud, C.G.1
  • 36
    • 33646548305 scopus 로고    scopus 로고
    • The amino acid sensitive TOR pathway from yeast to mammals
    • Dann S.G., and Thomas G. The amino acid sensitive TOR pathway from yeast to mammals. FEBS Lett 580 (2006) 2821-2829
    • (2006) FEBS Lett , vol.580 , pp. 2821-2829
    • Dann, S.G.1    Thomas, G.2
  • 37
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • Pain V.M. Initiation of protein synthesis in eukaryotic cells. Eur J Biochem 236 (1996) 747-771
    • (1996) Eur J Biochem , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 38
    • 0033005366 scopus 로고    scopus 로고
    • Eukaryotic initiation factor eIF2
    • Kimball S.R. Eukaryotic initiation factor eIF2. Int J Biochem Cell Biol 31 (1999) 25-29
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 25-29
    • Kimball, S.R.1
  • 39
    • 0033604521 scopus 로고    scopus 로고
    • Ribosomal S6 kinase signalling and the control of translation
    • Dufner A., and Thomas G. Ribosomal S6 kinase signalling and the control of translation. Exp Cell Res 253 (1999) 100-109
    • (1999) Exp Cell Res , vol.253 , pp. 100-109
    • Dufner, A.1    Thomas, G.2
  • 40
    • 0033761629 scopus 로고    scopus 로고
    • Synthesis of the translational apparatus is regulated at the translational level
    • Meyuhas O. Synthesis of the translational apparatus is regulated at the translational level. Eur J Biochem 267 (2000) 6321-6330
    • (2000) Eur J Biochem , vol.267 , pp. 6321-6330
    • Meyuhas, O.1
  • 41
    • 0035881470 scopus 로고    scopus 로고
    • Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase
    • Wang X., Li W., Williams M., Terada N., Alessi D.R., and Proud C.G. Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase. EMBO J 20 16 (2001) 4370-4379
    • (2001) EMBO J , vol.20 , Issue.16 , pp. 4370-4379
    • Wang, X.1    Li, W.2    Williams, M.3    Terada, N.4    Alessi, D.R.5    Proud, C.G.6
  • 42
    • 0035971180 scopus 로고    scopus 로고
    • The TOR kinases link nutrient sensing to cell growth
    • Rohde J., Heitman J., and Cardenas M.E. The TOR kinases link nutrient sensing to cell growth. J Biol Chem 276 (2001) 9583-9586
    • (2001) J Biol Chem , vol.276 , pp. 9583-9586
    • Rohde, J.1    Heitman, J.2    Cardenas, M.E.3
  • 43
    • 0037306190 scopus 로고    scopus 로고
    • Insulin/IGF and target of rapamycin signaling: a TOR de force in growth control
    • Oldham S., and Hafen E. Insulin/IGF and target of rapamycin signaling: a TOR de force in growth control. Trends Cell Biol 13 2 (2003) 79-85
    • (2003) Trends Cell Biol , vol.13 , Issue.2 , pp. 79-85
    • Oldham, S.1    Hafen, E.2
  • 45
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S., Loewith R., and Hall M.N. TOR signaling in growth and metabolism. Cell 124 3 (2006) 471-484
    • (2006) Cell , vol.124 , Issue.3 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 46
    • 0037431012 scopus 로고    scopus 로고
    • Amino acid availability regulates S6K1 and protein synthesis in avian insulin-insensitive QM7 myoblasts
    • Tesseraud S., Bigot K., and Taouis M. Amino acid availability regulates S6K1 and protein synthesis in avian insulin-insensitive QM7 myoblasts. FEBS Lett 540 1-3 (2003) 176-180
    • (2003) FEBS Lett , vol.540 , Issue.1-3 , pp. 176-180
    • Tesseraud, S.1    Bigot, K.2    Taouis, M.3
  • 47
    • 0037178781 scopus 로고    scopus 로고
    • Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action
    • Hara K., Long X., Yoshino K., Oshiro N., Hidayat S., Tokunaga C., et al. Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell 110 (2002) 177-189
    • (2002) Cell , vol.110 , pp. 177-189
    • Hara, K.1    Long, X.2    Yoshino, K.3    Oshiro, N.4    Hidayat, S.5    Tokunaga, C.6
  • 48
    • 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., Lorberg A., Crespo J.L., Bonenfant D., et al. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol Cell 10 3 (2002) 457-468
    • (2002) Mol Cell , vol.10 , Issue.3 , pp. 457-468
    • Loewith, R.1    Jacinto, E.2    Wullschleger, S.3    Lorberg, A.4    Crespo, J.L.5    Bonenfant, D.6
  • 49
    • 0037178786 scopus 로고    scopus 로고
    • mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • Kim D.H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., et al. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110 (2002) 163-175
    • (2002) Cell , vol.110 , pp. 163-175
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5    Erdjument-Bromage, H.6
  • 50
    • 0037623417 scopus 로고    scopus 로고
    • GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR
    • Kim D.H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V., Erdjument-Bromage H., et al. GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. Mol Cell 11 (2003) 895-904
    • (2003) Mol Cell , vol.11 , pp. 895-904
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    Latek, R.R.4    Guntur, K.V.5    Erdjument-Bromage, H.6
  • 52
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • Sarbassov D.D., Ali S.M., Kim D.H., Guertin D.A., Latek R.R., Erdjument-Bromage H., et al. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 14 (2004) 1296-1302
    • (2004) Curr Biol , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1    Ali, S.M.2    Kim, D.H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6
  • 53
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov D.D., Guertin D.A., Ali S.M., and Sabatini D.M. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307 (2005) 1098-1101
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 54
    • 21244458013 scopus 로고    scopus 로고
    • Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR phosphorylates its hydrophobic motif site
    • Ali S.M., and Sabatini D.M. Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR phosphorylates its hydrophobic motif site. J Biol Chem 280 20 (2005) 19445-19448
    • (2005) J Biol Chem , vol.280 , Issue.20 , pp. 19445-19448
    • Ali, S.M.1    Sabatini, D.M.2
  • 56
    • 26444575415 scopus 로고    scopus 로고
    • Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase
    • Nobukuni T., Joaquin M., Roccio M., Dann S.G., Kim S.Y., Gulati P., et al. Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase. Proc Natl Acad Sci U S A 102 (2005) 14238-14243
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14238-14243
    • Nobukuni, T.1    Joaquin, M.2    Roccio, M.3    Dann, S.G.4    Kim, S.Y.5    Gulati, P.6
  • 57
    • 21244480367 scopus 로고    scopus 로고
    • The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses
    • Smith E.M., Finn S.G., Tee A.R., Browne G.J., and Proud C.G. The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses. J Biol Chem 280 19 (2005) 18717-18727
    • (2005) J Biol Chem , vol.280 , Issue.19 , pp. 18717-18727
    • Smith, E.M.1    Finn, S.G.2    Tee, A.R.3    Browne, G.J.4    Proud, C.G.5
  • 58
    • 32244435285 scopus 로고    scopus 로고
    • Regulation of the small GTPase Rheb by amino acids
    • Roccio M., Bos J.L., and Zwartkruis F.J. Regulation of the small GTPase Rheb by amino acids. Oncogene 25 5 (2006) 657-664
    • (2006) Oncogene , vol.25 , Issue.5 , pp. 657-664
    • Roccio, M.1    Bos, J.L.2    Zwartkruis, F.J.3
  • 59
    • 25444457577 scopus 로고    scopus 로고
    • hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase
    • Byfield M.P., Murray J.T., and Backer J.M. hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase. J Biol Chem 280 (2005) 33076-33082
    • (2005) J Biol Chem , vol.280 , pp. 33076-33082
    • Byfield, M.P.1    Murray, J.T.2    Backer, J.M.3
  • 60
    • 0347986620 scopus 로고    scopus 로고
    • Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes
    • Tassa A., Roux M.P., Attaix D., and Bechet D.M. Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes. Biochem J 376 Pt 3 (2003) 577-586
    • (2003) Biochem J , vol.376 , Issue.PART 3 , pp. 577-586
    • Tassa, A.1    Roux, M.P.2    Attaix, D.3    Bechet, D.M.4
  • 62
    • 23944525331 scopus 로고    scopus 로고
    • Altered responses in skeletal muscle protein turnover during aging in anabolic and catabolic periods
    • Attaix D., Mosoni L., Dardevet D., Combaret L., Mirand P.P., and Grizard J. Altered responses in skeletal muscle protein turnover during aging in anabolic and catabolic periods. Int J Biochem Cell Biol 37 10 (2005) 1962-1973
    • (2005) Int J Biochem Cell Biol , vol.37 , Issue.10 , pp. 1962-1973
    • Attaix, D.1    Mosoni, L.2    Dardevet, D.3    Combaret, L.4    Mirand, P.P.5    Grizard, J.6
  • 63
    • 23944456384 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy and atrophy signaling pathways
    • Glass D.J. Skeletal muscle hypertrophy and atrophy signaling pathways. Int J Biochem Cell Biol 37 (2005) 1974-1984
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 1974-1984
    • Glass, D.J.1
  • 64
    • 17844399802 scopus 로고    scopus 로고
    • Molecular signaling pathways regulating muscle proteolysis during atrophy
    • Franch H.A., and Price S.R. Molecular signaling pathways regulating muscle proteolysis during atrophy. Curr Opin Clin Nutr Metab Care 8 (2005) 271-275
    • (2005) Curr Opin Clin Nutr Metab Care , vol.8 , pp. 271-275
    • Franch, H.A.1    Price, S.R.2
  • 65
    • 23944501319 scopus 로고    scopus 로고
    • Signal-transduction networks and the regulation of muscle protein degradation
    • Szewczyk N.J., and Jacobson L.A. Signal-transduction networks and the regulation of muscle protein degradation. Int J Biochem Cell Biol 37 10 (2005) 1997-2011
    • (2005) Int J Biochem Cell Biol , vol.37 , Issue.10 , pp. 1997-2011
    • Szewczyk, N.J.1    Jacobson, L.A.2
  • 66
    • 1242272070 scopus 로고    scopus 로고
    • Induction of CHOP expression by amino acid limitation requires both ATF4 expression and ATF2 phosphorylation
    • Averous J., Bruhat A., Jousse C., Carraro V., Thiel G., and Fafournoux P. Induction of CHOP expression by amino acid limitation requires both ATF4 expression and ATF2 phosphorylation. J Biol Chem 279 7 (2004) 5288-5297
    • (2004) J Biol Chem , vol.279 , Issue.7 , pp. 5288-5297
    • Averous, J.1    Bruhat, A.2    Jousse, C.3    Carraro, V.4    Thiel, G.5    Fafournoux, P.6
  • 67
    • 0346996344 scopus 로고    scopus 로고
    • Regulation of global and specific mRNA translation by oral administration of branched-chain amino acids
    • Kimball S.R., and Jefferson L.S. Regulation of global and specific mRNA translation by oral administration of branched-chain amino acids. Biochem Biophys Res Communications 313 (2004) 423-427
    • (2004) Biochem Biophys Res Communications , vol.313 , pp. 423-427
    • Kimball, S.R.1    Jefferson, L.S.2
  • 68
    • 31544466776 scopus 로고    scopus 로고
    • Signaling pathways and molecular mechanisms through which branched-chain amino acids mediate translational control of protein synthesis
    • Kimball S.R., and Jefferson L.S. Signaling pathways and molecular mechanisms through which branched-chain amino acids mediate translational control of protein synthesis. J Nutr 136 Suppl 1 (2006) 227S-231S
    • (2006) J Nutr , vol.136 , Issue.SUPPL. 1
    • Kimball, S.R.1    Jefferson, L.S.2
  • 69
    • 0347627142 scopus 로고    scopus 로고
    • Regulation of protein synthesis by branched-chain amino acids in vivo
    • Yoshizawa F. Regulation of protein synthesis by branched-chain amino acids in vivo. Biochem Biophys Res Communications 313 2 (2004) 417-422
    • (2004) Biochem Biophys Res Communications , vol.313 , Issue.2 , pp. 417-422
    • Yoshizawa, F.1
  • 70
    • 0034703021 scopus 로고    scopus 로고
    • Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin-independent signaling pathway
    • Mordier S., Deval C., Bechet D., Tassa A., and Ferrara M. Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin-independent signaling pathway. J Biol Chem 275 38 (2000) 29900-29906
    • (2000) J Biol Chem , vol.275 , Issue.38 , pp. 29900-29906
    • Mordier, S.1    Deval, C.2    Bechet, D.3    Tassa, A.4    Ferrara, M.5
  • 71
    • 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., and Abe H. Leucine suppresses myofibrillar proteolysis by down-regulating ubiquitin-proteasome pathway in chick skeletal muscles. Biochem Biophys Res Communications 336 (2005) 660-666
    • (2005) Biochem Biophys Res Communications , vol.336 , pp. 660-666
    • Nakashima, K.1    Ishida, A.2    Yamazaki, M.3    Abe, H.4
  • 73
    • 0036687146 scopus 로고    scopus 로고
    • Nutrient-hormone interaction in the ovine liver: methionine supply selectively modulates growth hormone-induced IGF-I gene expression
    • Stubbs A.K., Wheelhouse N.M., Lomax M.A., and Hazlerigg D.G. Nutrient-hormone interaction in the ovine liver: methionine supply selectively modulates growth hormone-induced IGF-I gene expression. J Endocrinol 174 2 (2002) 335-341
    • (2002) J Endocrinol , vol.174 , Issue.2 , pp. 335-341
    • Stubbs, A.K.1    Wheelhouse, N.M.2    Lomax, M.A.3    Hazlerigg, D.G.4
  • 74
    • 20144387009 scopus 로고    scopus 로고
    • The GCN2 kinase biases feeding behavior to maintain amino acid homeostasis in omnivores
    • Maurin A.C., Jousse C., Averous J., Parry L., Bruhat A., and Cherasse Y. The GCN2 kinase biases feeding behavior to maintain amino acid homeostasis in omnivores. Cell Metab 1 4 (2005) 273-277
    • (2005) Cell Metab , vol.1 , Issue.4 , pp. 273-277
    • Maurin, A.C.1    Jousse, C.2    Averous, J.3    Parry, L.4    Bruhat, A.5    Cherasse, Y.6
  • 75
    • 0034306249 scopus 로고    scopus 로고
    • Amino acid regulation of gene expression
    • Fafournoux P., Bruhat A., and Jousse C. Amino acid regulation of gene expression. Biochem J 351 (2000) 1-12
    • (2000) Biochem J , vol.351 , pp. 1-12
    • Fafournoux, P.1    Bruhat, A.2    Jousse, C.3
  • 76
    • 0037905795 scopus 로고    scopus 로고
    • Recent advances in the understanding of amino acid regulation of gene expression
    • Averous J., Bruhat A., Mordier S., and Fafournoux P. Recent advances in the understanding of amino acid regulation of gene expression. J Nutr 133 (2003) 2040S-2045S
    • (2003) J Nutr , vol.133
    • Averous, J.1    Bruhat, A.2    Mordier, S.3    Fafournoux, P.4
  • 78
    • 0027959628 scopus 로고
    • Inhibition by N-acetyl-l-cysteine of interleukin-6 mRNA induction and activation of NF kappa B by tumor necrosis factor alpha in a mouse fibroblastic cell line, Balb/3T3
    • Shibanuma M., Kuroki T., and Nose K. Inhibition by N-acetyl-l-cysteine of interleukin-6 mRNA induction and activation of NF kappa B by tumor necrosis factor alpha in a mouse fibroblastic cell line, Balb/3T3. FEBS Lett 353 1 (1994) 62-66
    • (1994) FEBS Lett , vol.353 , Issue.1 , pp. 62-66
    • Shibanuma, M.1    Kuroki, T.2    Nose, K.3
  • 81
    • 22144482049 scopus 로고    scopus 로고
    • Nutritional and functional importance of intestinal sulfur amino acid metabolism
    • Shoveller A.K., Stoll B., Ball R.O., and Burrin D.G. Nutritional and functional importance of intestinal sulfur amino acid metabolism. J Nutr 135 7 (2005) 1609-1612
    • (2005) J Nutr , vol.135 , Issue.7 , pp. 1609-1612
    • Shoveller, A.K.1    Stoll, B.2    Ball, R.O.3    Burrin, D.G.4
  • 82
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • Moskovitz J. Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Biochim Biophys Acta 1703 2 (2005) 213-219
    • (2005) Biochim Biophys Acta , vol.1703 , Issue.2 , pp. 213-219
    • Moskovitz, J.1
  • 83
    • 12844277331 scopus 로고    scopus 로고
    • Protein maintenance in aging and replicative senescence: a role for the peptide methionine sulfoxide reductases
    • Petropoulos I., and Friguet B. Protein maintenance in aging and replicative senescence: a role for the peptide methionine sulfoxide reductases. Biochim Biophys Acta 1703 2 (2005) 261-266
    • (2005) Biochim Biophys Acta , vol.1703 , Issue.2 , pp. 261-266
    • Petropoulos, I.1    Friguet, B.2
  • 84
    • 21844456289 scopus 로고    scopus 로고
    • Glutathionylation of two cysteine residues in paired domainregulates DNA binding activity of Pax-8
    • Cao X., Kambe F., Lu X., Kobayashi N., Ohmori S., and Seo H. Glutathionylation of two cysteine residues in paired domainregulates DNA binding activity of Pax-8. J Biol Chem 280 27 (2005) 25901-25906
    • (2005) J Biol Chem , vol.280 , Issue.27 , pp. 25901-25906
    • Cao, X.1    Kambe, F.2    Lu, X.3    Kobayashi, N.4    Ohmori, S.5    Seo, H.6
  • 85
    • 0036249836 scopus 로고    scopus 로고
    • Irreversible thiol oxidation in carbonic anhydrase III: protection by S-glutathiolation and detection in aging rats
    • Mallis R.J., Hamann M.J., Zhao W., Zhang T., Hendrich S., and Thomas J.A. Irreversible thiol oxidation in carbonic anhydrase III: protection by S-glutathiolation and detection in aging rats. Biol Chem 383 3-4 (2002) 649-662
    • (2002) Biol Chem , vol.383 , Issue.3-4 , pp. 649-662
    • Mallis, R.J.1    Hamann, M.J.2    Zhao, W.3    Zhang, T.4    Hendrich, S.5    Thomas, J.A.6
  • 87
    • 12844264123 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
    • Weissbach H., Resnick L., and Brot N. Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. Biochim Biophys Acta 1703 2 (2005) 203-212
    • (2005) Biochim Biophys Acta , vol.1703 , Issue.2 , pp. 203-212
    • Weissbach, H.1    Resnick, L.2    Brot, N.3
  • 89
    • 0035339675 scopus 로고    scopus 로고
    • Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging
    • Petropoulos I., Mary J., Perichon M., and Friguet B. Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging. Biochem J 355 Pt 3 (2001) 819-825
    • (2001) Biochem J , vol.355 , Issue.PART 3 , pp. 819-825
    • Petropoulos, I.1    Mary, J.2    Perichon, M.3    Friguet, B.4
  • 90
    • 0028967490 scopus 로고
    • Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage
    • Moskovitz J., Rahman M.A., Strassman J., Yancey S.O., Kushner S.R., Brot N., et al. Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J Bacteriol 177 3 (1995) 502-507
    • (1995) J Bacteriol , vol.177 , Issue.3 , pp. 502-507
    • Moskovitz, J.1    Rahman, M.A.2    Strassman, J.3    Yancey, S.O.4    Kushner, S.R.5    Brot, N.6
  • 91
    • 0036674242 scopus 로고    scopus 로고
    • Dietary protein modifies hepatic gene expression associated with oxidative stress responsiveness in growing pigs
    • Schwerin M., Dorroch U., Beyer M., Swalve H., Metges C.C., and Junghans P. Dietary protein modifies hepatic gene expression associated with oxidative stress responsiveness in growing pigs. FASEB J 16 10 (2002) 1322-1324
    • (2002) FASEB J , vol.16 , Issue.10 , pp. 1322-1324
    • Schwerin, M.1    Dorroch, U.2    Beyer, M.3    Swalve, H.4    Metges, C.C.5    Junghans, P.6
  • 92
    • 33745597874 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress, aging and caloric restriction: the protein and methionine connection
    • Pamplona R., and Barja G. Mitochondrial oxidative stress, aging and caloric restriction: the protein and methionine connection. Biochim Biophys Acta 1757 (2006) 496-508
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 496-508
    • Pamplona, R.1    Barja, G.2
  • 93
    • 33745970444 scopus 로고    scopus 로고
    • Methionine restriction decreases mitochondrial oxygen radical generation and leak as well as oxidative damage to mitochondrial DNA and proteins
    • Sanz A., Caro P., Ayala V., Portero-Otin M., Pamplona R., and Barja G. Methionine restriction decreases mitochondrial oxygen radical generation and leak as well as oxidative damage to mitochondrial DNA and proteins. FASEB J 20 8 (2006) 1064-1073
    • (2006) FASEB J , vol.20 , Issue.8 , pp. 1064-1073
    • Sanz, A.1    Caro, P.2    Ayala, V.3    Portero-Otin, M.4    Pamplona, R.5    Barja, G.6
  • 94
    • 20844451550 scopus 로고    scopus 로고
    • Modulation of insulin action by dietary proteins and amino acids: role of the mammalian target of rapamycin nutrient sensing pathway
    • Tremblay F., Jacques H., and Marette A. Modulation of insulin action by dietary proteins and amino acids: role of the mammalian target of rapamycin nutrient sensing pathway. Curr Opin Clin Nutr Metab Care 8 (2005) 457-462
    • (2005) Curr Opin Clin Nutr Metab Care , vol.8 , pp. 457-462
    • Tremblay, F.1    Jacques, H.2    Marette, A.3
  • 96
    • 29244439931 scopus 로고    scopus 로고
    • A leucine-supplemented diet restores the defective postprandial inhibition of proteasome- dependent proteolysis in aged rat skeletal muscle
    • Combaret L., Dardevet D., Rieu I., Pouch M.N., Bechet D., Taillandier D., et al. A leucine-supplemented diet restores the defective postprandial inhibition of proteasome- dependent proteolysis in aged rat skeletal muscle. J Physiol 569 Pt 2 (2005) 489-499
    • (2005) J Physiol , vol.569 , Issue.PART 2 , pp. 489-499
    • Combaret, L.1    Dardevet, D.2    Rieu, I.3    Pouch, M.N.4    Bechet, D.5    Taillandier, D.6
  • 97
    • 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., Nguyen H.V., Kimball S.R., Jefferson L.S., et al. Regulation of cardiac and skeletal muscle protein synthesis by individual branched-chain amino acids in neonatal pigs. Am J Physiol 290 4 (2006) E612-E621
    • (2006) Am J Physiol , vol.290 , Issue.4
    • Escobar, J.1    Frank, J.W.2    Suryawan, A.3    Nguyen, H.V.4    Kimball, S.R.5    Jefferson, L.S.6


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