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Volumn 32, Issue 12, 2011, Pages 905-911

Muscle protein turnover in endurance training: A review

Author keywords

endurance training; oxidative capacity; protein turnover; skeletal muscle

Indexed keywords

MUSCLE PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 82655168765     PISSN: 01724622     EISSN: 14393964     Source Type: Journal    
DOI: 10.1055/s-0031-1284339     Document Type: Review
Times cited : (13)

References (110)
  • 1
    • 26844471344 scopus 로고    scopus 로고
    • Models to explain fatigue during prolonged endurance cycling
    • DOI 10.2165/00007256-200535100-00004
    • Abbiss C R, Lauren P B. Models to explain fatigue during prolonged endurance cycling. Sports Med: 2005; 35 865 898 (Pubitemid 41464512)
    • (2005) Sports Medicine , vol.35 , Issue.10 , pp. 865-898
    • Abbiss, C.R.1    Laursen, P.B.2
  • 2
    • 70450210400 scopus 로고    scopus 로고
    • Physiological role of myosin light and heavy chain isoforms in fast- and slow-twitch muscles: Effect of exercise
    • Alev K, Kaasik P, Pehme A, Aru M, Parring A-M, Elart A, Seene T. Physiological role of myosin light and heavy chain isoforms in fast- and slow-twitch muscles: effect of exercise. Biol Sport: 2009; 26 215 234
    • (2009) Biol Sport , vol.26 , pp. 215-234
    • Alev, K.1    Kaasik, P.2    Pehme, A.3    Aru, M.4    Parring, A.-M.5    Elart, A.6    Seene, T.7
  • 3
    • 0029058357 scopus 로고
    • Plasticity of myonuclear number in hypertrophied and atrophied mammalian skeletal muscle fibres
    • Allen D L, Monke S R, Talmadge R J, Roy R R, Edgerton V R. Plasticity of myonuclear number in hypertrophied and atrophied mammalian skeletal muscle fibres. J Appl Physiol. 1995; 78 1969 1976
    • (1995) J Appl Physiol , vol.78 , pp. 1969-1976
    • Allen, D.L.1    Monke, S.R.2    Talmadge, R.J.3    Roy, R.R.4    Edgerton, V.R.5
  • 4
    • 0032833852 scopus 로고    scopus 로고
    • Myonuclear domains in muscle adaptation and disease
    • DOI 10.1002/(SICI)1097-4598(199910)22:10<1350::AID-MUS3>3.0.CO;2-8
    • Allen D L, Roy R R, Edgerton V R. Myonuclear domains in muscle adaptation and disease. Muscle Nerve: 1999; 22 1350 1360 (Pubitemid 29468418)
    • (1999) Muscle and Nerve , vol.22 , Issue.10 , pp. 1350-1360
    • Allen, D.L.1    Roy, R.R.2    Reggie Edgerton, V.3
  • 5
    • 0034265759 scopus 로고    scopus 로고
    • Muscle genes and athletic performance
    • Andreson J, Schjerling P, Saltin B. Muscle genes and athletic performance. Sci Am: 2000; 283 48 55
    • (2000) Sci Am , vol.283 , pp. 48-55
    • Andreson, J.1    Schjerling, P.2    Saltin, B.3
  • 6
    • 0025744624 scopus 로고
    • Mechanisms of exercise-induced muscle fibre injury
    • Armstrong R B, Warren G L, Warren J A. Mechanisms of exercise-induced muscle fibre injury. Sports Med: 1991; 12 184 207
    • (1991) Sports Med , vol.12 , pp. 184-207
    • Armstrong, R.B.1    Warren, G.L.2    Warren, J.A.3
  • 8
    • 1442332885 scopus 로고    scopus 로고
    • Sadenosine Monophosphate-Activated Protein Kinase, Metabolism and Exercise
    • DOI 10.2165/00007256-200434020-00003
    • Aschenbach W G, Sakamoto K, Goodyear L J. Sadenosine monophosphate- activated protein kinase, metabolism and exercise. Sports Med: 2004; 34 91 103 (Pubitemid 38283127)
    • (2004) Sports Medicine , vol.34 , Issue.2 , pp. 91-103
    • Aschenbach, W.G.1    Sakamoto, K.2    Goodyear, L.J.3
  • 9
    • 0035168989 scopus 로고    scopus 로고
    • Invited review: Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle
    • Baldwin K M, Haddad F. Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle. J Appl Physiol: 2001; 90 345 357 (Pubitemid 32038537)
    • (2001) Journal of Applied Physiology , vol.90 , Issue.1 , pp. 345-357
    • Baldwin, K.M.1    Haddad, F.2
  • 10
    • 0036838249 scopus 로고    scopus 로고
    • Skeletal muscle plasticity: Cellular and molecular responses to altered physical activity paradigms
    • DOI 10.1097/00002060-200211001-00006
    • Baldwin K M, Haddad F. Skeletal muscle plasticity: cellular and molecular responses to altered physical activity paradigms. Am J Phys Med Rehabil: 2002; 81 S40 S51 (Pubitemid 35192965)
    • (2002) American Journal of Physical Medicine and Rehabilitation , vol.81 , Issue.11 SUPPL.
    • Baldwin, K.M.1    Haddad, F.2
  • 13
    • 1842296939 scopus 로고    scopus 로고
    • Maximum rate of oxygen uptake by human skeletal muscle in relation to maximal activities of enzymes in the Krebs cycle
    • DOI 10.1111/j.1469-7793.1997.455bn.x
    • Blomstrand E, Rdegran G, Saltin B. Maximum rate of oxygen uptake by human skeletal muscle in relation to maximal activities of enzymes in the Krebs cycle. J Physiol: 1997; 501 455 460 (Pubitemid 27280819)
    • (1997) Journal of Physiology , vol.501 , Issue.2 , pp. 455-460
    • Blomstrand, E.1    Radegran, G.2    Saltin, B.3
  • 15
    • 0035165415 scopus 로고    scopus 로고
    • Functional heterogeneity of mammalian single muscle fibres: Do myosin isoforms tell the whole story?
    • DOI 10.1007/s004240100700
    • Bottinelli R. Functional heterogeneity of mammalian single muscle fibres: do myosin isoforms tell the whole story? Pflugers Arch: 2001; 443 6 17 (Pubitemid 33070885)
    • (2001) Pflugers Archiv European Journal of Physiology , vol.443 , Issue.1 , pp. 6-17
    • Bottinelli, R.1
  • 16
    • 0028132899 scopus 로고
    • Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres
    • Bottinelli R, Betto R, Schiaffino S, Reggiani C. Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres. J Physiol: 1994; 478 341 349 (Pubitemid 24232204)
    • (1994) Journal of Physiology , vol.478 , Issue.2 , pp. 341-349
    • Bottinelli, R.1    Betto, R.2    Schiaffino, S.3    Reggiani, C.4
  • 20
    • 84912449809 scopus 로고
    • Skeletal muscle cell mass and growth A review: The concept of the DNA unit
    • Cheek D, Holt A, Hill D, Talbert J. Skeletal muscle cell mass and growth A review: the concept of the DNA unit. Pediatr Res: 1971; 3 312 328
    • (1971) Pediatr Res , vol.3 , pp. 312-328
    • Cheek, D.1    Holt, A.2    Hill, D.3    Talbert, J.4
  • 21
    • 34548371839 scopus 로고    scopus 로고
    • The molecular bases of training adaptation
    • DOI 10.2165/00007256-200737090-00001
    • Coffey V G, Hawley J A. The molecular bases of training adaptation. Sports Med: 2007; 37 737 763 (Pubitemid 47347390)
    • (2007) Sports Medicine , vol.37 , Issue.9 , pp. 737-763
    • Coffey, V.G.1    Hawley, J.A.2
  • 22
    • 0015177822 scopus 로고
    • Muscle glycogen utilization during prolonged exercise on successive days
    • Costill D L, Bowers L, Branam G, Sparks K. Muscle glycogen utilization during prolonged exercise on successive days. J Appl Physiol: 1971; 31 834 838
    • (1971) J Appl Physiol , vol.31 , pp. 834-838
    • Costill, D.L.1    Bowers, L.2    Branam, G.3    Sparks, K.4
  • 23
    • 36048981374 scopus 로고    scopus 로고
    • Genes, environment and sport performance: Why the nature-nurture dualism is no longer relevant
    • DOI 10.2165/00007256-200737110-00004
    • Davids K, Baker J. Genes environment and sport performance: why the nature-nature dualism is no longer relevant. Sports Med: 2007; 37 961 980 (Pubitemid 350085747)
    • (2007) Sports Medicine , vol.37 , Issue.11 , pp. 961-980
    • Davids, K.1    Baker, J.2
  • 25
    • 0026315384 scopus 로고
    • Control of myosin heavy chain expression: Interaction of hypothyroidism and hindlimb suspension
    • Diffee G M, Haddad F, Herrick R E, Baldwin K M. Control of myosin heavy chain expression: interaction of hypothyroidism and hindlimb suspension. Am J Physiol: 1991; 261 1099 1106
    • (1991) Am J Physiol , vol.261 , pp. 1099-1106
    • Diffee, G.M.1    Haddad, F.2    Herrick, R.E.3    Baldwin, K.M.4
  • 26
    • 0035109274 scopus 로고    scopus 로고
    • Mitochondria in exercise-induced oxidative stress
    • Di Meo S, Venditti P. Mitochondria in exercise-induced oxidative stress. Biol Signals Recept: 2001; 10 125 140 (Pubitemid 32171163)
    • (2001) Biological Signals and Receptors , vol.10 , Issue.1-2 , pp. 125-140
    • Di Meo, S.1    Venditti, P.2
  • 27
    • 22344444732 scopus 로고    scopus 로고
    • The role of apoptosis in age-related skeletal muscle atrophy
    • DOI 10.2165/00007256-200535060-00002
    • Dirks A, Leeuwenburgh C. The role of apoptosis in age-related skeletal muscle atrophy. Sports Med: 2005; 35 473 483 (Pubitemid 41002968)
    • (2005) Sports Medicine , vol.35 , Issue.6 , pp. 473-483
    • Dirks, A.J.1    Leeuwenburgh, C.2
  • 28
    • 0018081270 scopus 로고
    • Turnover rates of muscle protein in cardiac and skeletal muscles of dog, fowl, rat and mouse: Turnover rate related to muscle function
    • Earl C A, Laurent G J, Everett A W, Bounin C M, Sparrow M P. Turnover rates of muscle protein in cardiac and skeletal muscles of dog, flow, rat and mouse: turnover rate related to muscle function. Aust J Exp Biol Med Sci: 1978; 56 265 277 (Pubitemid 9004944)
    • (1978) Australian Journal of Experimental Biology and Medical Science , vol.56 , Issue.3 , pp. 265-277
    • Earl, C.A.1    Laurent, G.J.2    Everett, A.W.3
  • 29
    • 0026332365 scopus 로고
    • Regulation of skeletal muscle fibre size, shape and function
    • Edgerton V R, Roy R R. Regulation of skeletal muscle fibre size, shape and function. J Biomech: 1991; 24 123 133
    • (1991) J Biomech , vol.24 , pp. 123-133
    • Edgerton, V.R.1    Roy, R.R.2
  • 30
    • 33746012931 scopus 로고    scopus 로고
    • Functional, structural and molecular plasticity of mammalian skeletal muscle in response to exercise stimuli
    • Flck M. Functional, structural and molecular plasticity of mammalian skeletal muscle in response to exercise stimuli. J Exp Biol: 2006; 209 2239 2248
    • (2006) J Exp Biol , vol.209 , pp. 2239-2248
    • Flck, M.1
  • 31
    • 0037610288 scopus 로고    scopus 로고
    • Molecular basis of skeletal muscle plasticity from gene to form and function
    • Flck M, Hoppeler H. Molecular basis of skeletal muscle plasticity from gene to form and function. Rev Physiol Biochem Pharmacol: 2003; 146 159 216
    • (2003) Rev Physiol Biochem Pharmacol , vol.146 , pp. 159-216
    • Flck, M.1    Hoppeler, H.2
  • 32
    • 74049113776 scopus 로고    scopus 로고
    • Relative proportions of hybrid fibres are unaffected by 6 weeks of running exercise in mouse skeletal muscles
    • Glaser B W, You G, Zhang M, Medler S. Relative proportions of hybrid fibres are unaffected by 6 weeks of running exercise in mouse skeletal muscles. Exp Physiol: 2010; 95 211 221
    • (2010) Exp Physiol , vol.95 , pp. 211-221
    • Glaser, B.W.1    You, G.2    Zhang, M.3    Medler, S.4
  • 33
    • 4344609104 scopus 로고    scopus 로고
    • Changes in contractile activation characteristics of rat fast and slow skeletal muscle fibres during regeneration
    • DOI 10.1113/jphysiol.2004.066217
    • Gregorevic P, Plant D R, Stupka N, Lynch G S. Changes in contractile activation characteristics of rat fast and slow skeletal muscle fibres during regeneration. J Physiol: 2004; 558 549 560 (Pubitemid 39117601)
    • (2004) Journal of Physiology , vol.558 , Issue.2 , pp. 549-560
    • Gregorevic, P.1    Plant, D.R.2    Stupka, N.3    Lynch, G.S.4
  • 35
    • 33644943620 scopus 로고    scopus 로고
    • AMPK: A key sensor of fuel and energy status in skeletal muscle
    • DOI 10.1152/physiol.00044.2005
    • Hardie D G, Sakamoto K. AMPK: a key sensor of fuel and energy status in skeletal muscle. Physiology: 2006; 21 48 60 (Pubitemid 43752517)
    • (2006) Physiology , vol.21 , Issue.1 , pp. 48-60
    • Hardie, D.G.1    Sakamoto, K.2
  • 36
    • 25844457252 scopus 로고    scopus 로고
    • The influence of endurance and resistance exercise on muscle capillarization in the elderly: A review
    • DOI 10.1111/j.1365-201X.2005.01461.x
    • Harris B A. The influence of endurance and resistance exercise on muscle capillarization in the elderly: a review. Acta Physiol Scand: 2005; 185 89 97 (Pubitemid 41392352)
    • (2005) Acta Physiologica Scandinavica , vol.185 , Issue.2 , pp. 89-97
    • Harris, B.A.1
  • 37
    • 0027959627 scopus 로고
    • Binding of the amino-terminal region of myosin alkali 1 light-chain to actin and its effect on actin-myosin interaction
    • DOI 10.1021/bi00209a013
    • Hayashibara T, Miyanishi T. Binding of the amino-terminal region of myosin alkali 1 light chain to actin and its effect on actin-myosin interaction. Biochemistry: 1994; 33 12821 12827 (Pubitemid 24352872)
    • (1994) Biochemistry , vol.33 , Issue.43 , pp. 12821-12827
    • Hayashibara, T.1    Miyanishi, T.2
  • 38
    • 0034467677 scopus 로고    scopus 로고
    • Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria
    • DOI 10.1023/A:1005626712319
    • Herrero A, Barja G. Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria. J Bioenerg Biomembr: 2000; 32 609 615 (Pubitemid 32204237)
    • (2000) Journal of Bioenergetics and Biomembranes , vol.32 , Issue.6 , pp. 609-615
    • Herrero, A.1    Barja, G.2
  • 39
    • 17644436228 scopus 로고
    • Separate turnover of cytochrome c and myoglobin in the red types of skeletal muscle
    • Hickson R C, Rosenkoetter M A. Separate turnover of cytochrome c and myoglobin in the red types of skeletal muscle. Am J Physiol: 1981; 241 C140 C144
    • (1981) Am J Physiol , vol.241
    • Hickson, R.C.1    Rosenkoetter, M.A.2
  • 40
    • 0016888751 scopus 로고
    • Biochemical adaptation to endurance exercise in muscle
    • Holloszy J O, Booth F W. Biochemical adaptation to endurance exercise in muscle. Annu Rev Physiol: 1976; 38 273 291
    • (1976) Annu Rev Physiol , vol.38 , pp. 273-291
    • Holloszy, J.O.1    Booth, F.W.2
  • 41
    • 0035112481 scopus 로고    scopus 로고
    • Invited review: Contractile activity-induced mitochondrial biogenesis in skeletal muscle
    • Hood D A. Contractile activity-induced mitochondrial biogenesis in skeletal muscle. J Appl Physiol: 2001; 90 1137 1157 (Pubitemid 32171405)
    • (2001) Journal of Applied Physiology , vol.90 , Issue.3 , pp. 1137-1157
    • Hood, D.A.1
  • 42
    • 67651237067 scopus 로고    scopus 로고
    • Mechanisms of exercise-induced mitochondrial biogenesis in skeletal muscle
    • Hood D A. Mechanisms of exercise-induced mitochondrial biogenesis in skeletal muscle. Appl Physiol Nutr Metab: 2009; 34 465 472
    • (2009) Appl Physiol Nutr Metab , vol.34 , pp. 465-472
    • Hood, D.A.1
  • 43
    • 0344500696 scopus 로고    scopus 로고
    • In vitro motility speed of slow myosin extracted from single soleus fibres from young and old rats
    • DOI 10.1111/j.1469-7793.1999.00463.x
    • Hk P, Li X, Sleep J, Hughes S, Larsson L. In vitro motility speed of slow myosin extracted from single soleus fibres from young and old rats. J Physiol: 1999; 520 463 471 (Pubitemid 29511910)
    • (1999) Journal of Physiology , vol.520 , Issue.2 , pp. 463-471
    • Hook, P.1    Li, X.2    Sleep, J.3    Hughes, S.4    Larsson, L.5
  • 44
    • 0026234937 scopus 로고
    • Conditions for oxygen and substrate transport in muscles in exercising mammals
    • Hoppeler H, Billeter R. Conditions for oxygen and substrate transport in muscles in exercising mammals. J Exp Biol: 1991; 160 263 283
    • (1991) J Exp Biol , vol.160 , pp. 263-283
    • Hoppeler, H.1    Billeter, R.2
  • 45
    • 0022260872 scopus 로고
    • Endurance training in humans: Aerobic capacity and structure of skeletal muscle
    • Hoppeler H, Howald H, Conley K, Lindstedt S, Classen H, Vock P, Weibel E. Endurance training in humans: aerobic capacity and structure of skeletal muscle. J Appl Physiol: 1985; 59 320 327 (Pubitemid 15249855)
    • (1985) Journal of Applied Physiology , vol.59 , Issue.2 , pp. 320-327
    • Hoppeler, H.1    Howald, H.2    Conley, K.3
  • 46
    • 58649097755 scopus 로고    scopus 로고
    • Four weeks of speed endurance training reduces energy expenditure during exercise and maintains muscle oxidative capacity despite a reduction in training volume
    • Iaia F M, Hellsten Y, Nielsen J J, Fernstrm M, Sahlin K, Bangsbo J. Four weeks of speed endurance training reduces energy expenditure during exercise and maintains muscle oxidative capacity despite a reduction in training volume. J Appl Physiol: 2009; 106 73 80
    • (2009) J Appl Physiol , vol.106 , pp. 73-80
    • Iaia, F.M.1    Hellsten, Y.2    Nielsen, J.J.3    Fernstrm, M.4    Sahlin, K.5    Bangsbo, J.6
  • 49
    • 0026354739 scopus 로고
    • Molecular mechanisms of skeletal muscle adaptations to exercise
    • Karas R H, Williams R S. Molecular mechanisms of skeletal muscle adaptations to exercise. Trends Cardiovasc Med: 1991; 341 346
    • (1991) Trends Cardiovasc Med , pp. 341-346
    • Karas, R.H.1    Williams, R.S.2
  • 50
    • 0023552561 scopus 로고
    • Volume density and distribution of mitochondria in myocardial growth and hypertrophy
    • DOI 10.1016/0034-5687(87)90010-7
    • Kayar S R, Banchero N. Volume density and distribution of mitochondria in myocardial growth and hypertrophy. Respir Physiol: 1987; 70 275 286 (Pubitemid 18045499)
    • (1987) Respiration Physiology , vol.70 , Issue.3 , pp. 275-286
    • Kayar, S.R.1    Banchero, N.2
  • 51
    • 35948973942 scopus 로고    scopus 로고
    • Exercise pattern influences skeletal muscle hybrid fibers of runners and nonrunners
    • DOI 10.1249/mss.0b013e3181453546, PII 0000576820071100000012
    • Kohn T A, Essen-Gustavsson B, Myburgh K H. Exercise pattern influences skeletal muscle hybrid fibres of runners and nonrunners. Med Sci Sports Exerc: 2007; 39 1977 1984 (Pubitemid 350073361)
    • (2007) Medicine and Science in Sports and Exercise , vol.39 , Issue.11 , pp. 1977-1984
    • Kohn, T.A.1    Essen-Gustavsson, B.2    Myburgh, K.H.3
  • 52
    • 0027763495 scopus 로고
    • Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles
    • Larsson L, Moss R L. Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles. J Physiol: 1993; 472 595 614 (Pubitemid 24015023)
    • (1993) Journal of Physiology , vol.472 , pp. 595-614
    • Larsson, L.1    Moss, R.L.2
  • 53
    • 77956484579 scopus 로고    scopus 로고
    • Training for intense exercise performance: High-intensity or high-volume training
    • doi: 10.1111/j.1600-0838.2010.01184.x
    • Laursen P B. Training for intense exercise performance: high-intensity or high-volume training? Scand J Med Sci Sports: 2010; Suppl 2 1 10 doi: 10.1111/j.1600-0838.2010.01184.x
    • (2010) Scand J Med Sci Sports , vol.2 , Issue.SUPPL , pp. 1-10
    • Laursen, P.B.1
  • 54
    • 0036155430 scopus 로고    scopus 로고
    • The scientific basis for high-intensity interval training: Optimising training programmes and maximising performance in highly trained endurance athletes
    • Laursen P, Jenkins D. The scientific basis for big high-intensity interval training: optimising training programmes and maximising performance in highly trained endurance athletes. Sports Med: 2002; 32 53 73 (Pubitemid 34093709)
    • (2002) Sports Medicine , vol.32 , Issue.1 , pp. 53-73
    • Laursen, P.B.1    Jenkins, D.G.2
  • 58
    • 0018139113 scopus 로고
    • Effect of nutrition on protein turnover in skeletal muscle
    • Millward D, Waterlow J. Effect of nutrition on protein turnover in skeletal muscle. Fed Proc: 1978; 37 2283 2290 (Pubitemid 8373660)
    • (1978) Federation Proceedings , vol.37 , Issue.9 , pp. 2283-2290
    • Millward, D.J.1    Waterlow, J.C.2
  • 59
    • 3543109158 scopus 로고    scopus 로고
    • Evaluation by blue native polyacrylamide electrophoresis colorimetric staining of the effects of physical exercise on the activities of mitochondrial complexes in rat muscle
    • Molnar A M, Alves A A, Pereira-da-Silva L, Macedo D V, Dabbeni-Sala F. Evaluation by blue native polyacrylamide electrophoresis colorimetric staining of the effects of physical exercise on the activities of mitochondrial complexes in rat muscle. Braz J Med Biol Res: 2004; 37 939 947 (Pubitemid 39029112)
    • (2004) Brazilian Journal of Medical and Biological Research , vol.37 , Issue.7 , pp. 939-947
    • Molnar, A.M.1    Alves, A.A.2    Pereira-da-Silva, L.3    Macedo, D.V.4    Dabbeni-Sala, F.5
  • 60
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • DOI 10.1074/jbc.M407715200
    • Muller F L, Liu Y, Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J Biol Chem: 2004; 279 49064 49073 (Pubitemid 39625788)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 61
    • 0021840236 scopus 로고
    • Whole-body protein turnover in chicks at early stages of growth
    • Muramatsu T, Okumura J. Whole-body protein turnover in chicks at early stages of growth. J Nutr: 1985; 115 483 490 (Pubitemid 15083805)
    • (1985) Journal of Nutrition , vol.115 , Issue.4 , pp. 483-490
    • Muramatsu, T.1    Okumura, J.-I.2
  • 62
    • 33750736640 scopus 로고    scopus 로고
    • Concurrent strength and endurance training: From molecules to man
    • DOI 10.1249/01.mss.0000233795.39282.33
    • Nader G A. Concurrent strength and endurance training: from molecules to man. Med Sci Sports Exerc. 2006; 38 1965 1970 (Pubitemid 44707802)
    • (2006) Medicine and Science in Sports and Exercise , vol.38 , Issue.11 , pp. 1965-1970
    • Nader, G.A.1
  • 63
    • 0034200874 scopus 로고    scopus 로고
    • Physiological models to understand exercise fatigue and the adaptations that predict or enhance athletic performance
    • Noakes T D. Physiological models to understand exercise fatigue and the adaptations that predict or enhance athletic performance. Scand J Med Sci Sports: 2000; 10 123 145
    • (2000) Scand J Med Sci Sports , vol.10 , pp. 123-145
    • Noakes, T.D.1
  • 64
    • 58149133630 scopus 로고    scopus 로고
    • Dietary protein recommendations and the prevention of sarcopenia
    • Paddon-Jones D, Rasmussen B B. Dietary protein recommendations and the prevention of sarcopenia. Curr Opin Clin Nutr Metab Care: 2009; 12 86 90
    • (2009) Curr Opin Clin Nutr Metab Care , vol.12 , pp. 86-90
    • Paddon-Jones, D.1    Rasmussen, B.B.2
  • 65
    • 0035116376 scopus 로고    scopus 로고
    • Historical perspectives: Plasticity of mammalian skeletal muscle
    • Pette D. Historical perspectives: Plasticity of mammalian skeletal muscle. J Appl Physiol: 2001; 90 1119 1124
    • (2001) J Appl Physiol , vol.90 , pp. 1119-1124
    • Pette, D.1
  • 66
    • 0036690310 scopus 로고    scopus 로고
    • The adaptative potential of skeletal muscle fibres
    • Pette D. The adaptative potential of skeletal muscle fibres. Can J Appl Physiol: 2002; 27 423 448
    • (2002) Can J Appl Physiol , vol.27 , pp. 423-448
    • Pette, D.1
  • 67
    • 0031888291 scopus 로고    scopus 로고
    • Training effects on the contractile apparatus
    • DOI 10.1046/j.1365-201X.1998.0296e.x
    • Pette D. Training effects on the contractile apparatus. Acta Physiol Scand: 1998; 162 367 376 (Pubitemid 28121416)
    • (1998) Acta Physiologica Scandinavica , vol.162 , Issue.3 , pp. 367-376
    • Pette, D.1
  • 68
    • 0035006873 scopus 로고    scopus 로고
    • Transitions of muscle fiber phenotypic profiles
    • Pette D, Staron R S. Transitions of muscle fibre phenotypic profiles. Histochem Cell Biol: 2001; 115 359 372 (Pubitemid 32467749)
    • (2001) Histochemistry and Cell Biology , vol.115 , Issue.5 , pp. 359-372
    • Pette, D.1    Staron, R.S.2
  • 69
    • 55949118714 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress: Cellular mechanisms and impact on muscle force production
    • Powers S K, Jackson M J. Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production. Physiol Rev: 2008; 88 1243 1276
    • (2008) Physiol Rev , vol.88 , pp. 1243-1276
    • Powers, S.K.1    Jackson, M.J.2
  • 70
    • 33751547244 scopus 로고    scopus 로고
    • Muscle fatigue during high-intensity exercise in children
    • DOI 10.2165/00007256-200636120-00004
    • Ratel S, Duche P, Williams G A. Muscle fatigue during high-intensity exercise in children. Sports Med: 2006; 36 1031 1065 (Pubitemid 44837808)
    • (2006) Sports Medicine , vol.36 , Issue.12 , pp. 1031-1065
    • Ratel, S.1    Duche, P.2    Williams, C.A.3
  • 71
    • 0025860820 scopus 로고
    • Enzyme-activities of fatty acid oxidation and the respiratory chain in chronically stimulated fast-twitch muscle of the rabbit
    • Reichmann H, Wasl R, Simoneau J A, Pette D. Enzyme-activities of fatty acid oxidation and the respiratory chain in chronically stimulated fast-twitch muscle of the rabbit. Plugers Arch: 1991; 418 572 574
    • (1991) Plugers Arch , vol.418 , pp. 572-574
    • Reichmann, H.1    Wasl, R.2    Simoneau, J.A.3    Pette, D.4
  • 72
    • 0033834961 scopus 로고    scopus 로고
    • Protein and amino acid metabolism during and after exercise and the effects of nutrition
    • Rennie M, Tipton K. Protein and amino acid metabolism during and after exercise and the effects of nutrition. Annu Rev Nutr: 2000; 20 457 483
    • (2000) Annu Rev Nutr , vol.20 , pp. 457-483
    • Rennie, M.1    Tipton, K.2
  • 73
    • 0032949494 scopus 로고    scopus 로고
    • Interrelationships of myofibrillar ATPase activity and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle
    • DOI 10.1007/s004180050358
    • Rivero J L, Talmadge R J, Edgerton V R. Interrelationships of myofibrillar ATPase activity and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle. Histochem Cell Biol: 1999; 111 277 287 (Pubitemid 29155518)
    • (1999) Histochemistry and Cell Biology , vol.111 , Issue.4 , pp. 277-287
    • Rivero, J.-L.L.1    Talmadge, R.J.2    Edgerton, V.R.3
  • 74
    • 2042541410 scopus 로고    scopus 로고
    • Is skeletal muscle oxidative capacity decreased in old age?
    • DOI 10.2165/00007256-200434040-00002
    • Russ D W, Kent-Braun J A. Is skeletal muscle oxidative capacity decreased in old age? Sports Med: 2004; 34 221 229 (Pubitemid 38534746)
    • (2004) Sports Medicine , vol.34 , Issue.4 , pp. 221-229
    • Russ, D.W.1    Kent-Braun, J.A.2
  • 77
    • 0025913239 scopus 로고
    • HSP70 and other possible heat shock or oxidative stress proteins are induced in skeletal muscle, heart, and liver during exercise
    • Salo D, Donovan C, Davies K. HSP 70 and other possible heat schock or oxidative stress proteins are induced in skeletal muscle, heart and liver during exercise. Free Radic Biol Med: 1991; 11 239 246 (Pubitemid 121003919)
    • (1991) Free Radical Biology and Medicine , vol.11 , Issue.3 , pp. 239-246
    • Salo, D.C.1    Donovan, C.M.2    Davies, K.J.A.3
  • 78
    • 0034082628 scopus 로고    scopus 로고
    • Dynamics of nuclei of muscle fibers and connective tissue cells in normal and denervated rat muscles
    • DOI 10.1002/(SICI)1097-4598(200004)23:4<617::AID-MUS22>3.0.CO;2-Y
    • Schmalbruch H, Lewis D M. Dynamics of nuclei of muscle fibres and connective tissue cells in normal and denervated rat muscles. Muscle Nerve: 2000; 23 617 626 (Pubitemid 30164789)
    • (2000) Muscle and Nerve , vol.23 , Issue.4 , pp. 617-626
    • Schmalbruch, H.1    Lewis, D.M.2
  • 80
    • 0344850801 scopus 로고
    • Studies in protein metabolism. VII. the metabolism of tyrosine
    • Schoenheimer R, Ratner S, Rittenberg D. Studies in protein metabolism. VII. The metabolism of tyrosine. J Biol Chem: 1939; 127 333 344
    • (1939) J Biol Chem , vol.127 , pp. 333-344
    • Schoenheimer, R.1    Ratner, S.2    Rittenberg, D.3
  • 81
    • 0025862931 scopus 로고
    • Effect of muscular activity on the turnover rate of actin and myosin heavy and light chains in different types of skeletal muscle
    • Seene T, Alev K. Effect of muscular activity on the turnover rate of actin and myosin heavy and light chains in different types of skeletal muscle. Int J Sports Med: 1991; 12 204 207
    • (1991) Int J Sports Med , vol.12 , pp. 204-207
    • Seene, T.1    Alev, K.2
  • 82
    • 34247373881 scopus 로고    scopus 로고
    • Changes in fast-twitch muscle oxidative capacity and myosin isoforms modulation during endurance training
    • Seene T, Alev K, Kaasik P, Pehme A. Changes in fast-twitch muscle oxidative capacity and myosin isoforms modulation during endurance training. J Sports Med Phys Fitness: 2007; 47 124 132
    • (2007) J Sports Med Phys Fitness , vol.47 , pp. 124-132
    • Seene, T.1    Alev, K.2    Kaasik, P.3    Pehme, A.4
  • 84
    • 0022971074 scopus 로고
    • Effect of muscular activity on the turnover rate of actin and myosin heavy and light chains in different types of skeletal muscle. I. Changes in the turnover rate of myosin and actin during and after single-bout physical activity
    • Seene T, Alev K, Pehme A. Effect of muscular activity on the turnover rate of actin and myosin heavy and light chains in different types of skeletal muscle. I. Changes in the turnover rate of myosin and actin during and after single-bout physical activity. Int J Sports Med: 1986; 7 287 290 (Pubitemid 17210857)
    • (1986) International Journal of Sports Medicine , vol.7 , Issue.5 , pp. 287-290
    • Seene, T.1    Alev, K.2    Pehme, A.3
  • 85
    • 4544339483 scopus 로고    scopus 로고
    • Composition and turnover of contractile proteins in volume-overtrained skeletal muscle
    • DOI 10.1055/s-2004-820935
    • Seene T, Kaasik P, Alev K, Pehme A, Riso E M. Composition and turnover of contractile proteins in volume-overtrained skeletal muscle. Int J Sports Med: 2004; 25 438 445 (Pubitemid 39222925)
    • (2004) International Journal of Sports Medicine , vol.25 , Issue.6 , pp. 438-445
    • Seene, T.1    Kaasik, P.2    Alev, K.3    Pehme, A.4    Riso, E.M.5
  • 87
    • 77949993012 scopus 로고    scopus 로고
    • Structural rearrangements in contractile apparatus and resulting skeletal muscle remodelling: Effect of exercise training
    • Seene T, Kaasik P, Umnova M. Structural rearrangements in contractile apparatus and resulting skeletal muscle remodelling: effect of exercise training. J Sports Med Phys Fitness: 2009; 49 410 423
    • (2009) J Sports Med Phys Fitness , vol.49 , pp. 410-423
    • Seene, T.1    Kaasik, P.2    Umnova, M.3
  • 88
    • 82655161405 scopus 로고
    • Relations between the changes in the turnover rate of contractile proteins, activation of satellite cells and ultra-structural response of neuromuscular junctions in the fast-oxidative-glycolytic muscle fibres in endurance trained rats
    • Seene T, Umnova M. Relations between the changes in the turnover rate of contractile proteins, activation of satellite cells and ultra-structural response of neuromuscular junctions in the fast-oxidative-glycolytic muscle fibres in endurance trained rats. Basic Appl Myology: 1992; 1 539 546
    • (1992) Basic Appl Myology , vol.1 , pp. 539-546
    • Seene, T.1    Umnova, M.2
  • 93
    • 0034910559 scopus 로고    scopus 로고
    • Hybrid skeletal muscle fibres: A rare or common phenomenon?
    • DOI 10.1046/j.1440-1681.2001.03505.x
    • Stephenson G M. Hybrid skeletal muscle fibres: a rare or common phenomenon? Clin Exp Pharmacol Physiol: 2001; 28 692 702 (Pubitemid 32729101)
    • (2001) Clinical and Experimental Pharmacology and Physiology , vol.28 , Issue.8 , pp. 692-702
    • Stephenson, G.M.M.1
  • 95
    • 0033715778 scopus 로고    scopus 로고
    • Effects of unweighting and clenbuterol on myosin light and heavy chains in fast and slow muscles of rat
    • Stevens L, Firinga C, Gohlsch B, Bastide B, Mounier Y, Pette D. Effects of unweighting and clenbuterol on myosin light and heavy chains in fast and slow muscles of rat. Am J Physiol: 2000; 279 C1558 C1563
    • (2000) Am J Physiol , vol.279
    • Stevens, L.1    Firinga, C.2    Gohlsch, B.3    Bastide, B.4    Mounier, Y.5    Pette, D.6
  • 96
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • DOI 10.1016/S1097-2765(04)00211-4, PII S1097276504002114
    • 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 (Pubitemid 38591410)
    • (2004) Molecular Cell , vol.14 , Issue.3 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3    Panaro, F.4    Timofeyva, Y.5    Kline, W.O.6    Gonzalez, M.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 97
    • 0023905464 scopus 로고
    • Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibres
    • Sweeney H L, Kushmeric M J, Mahuchi K, Sreter F A, Gerery J. Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibres. J Biol Chem: 1988; 263 9034 9039
    • (1988) J Biol Chem , vol.263 , pp. 9034-9039
    • Sweeney, H.L.1    Kushmeric, M.J.2    Mahuchi, K.3    Sreter, F.A.4    Gerery, J.5
  • 98
    • 0022542030 scopus 로고
    • Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles
    • Swynghedauw B. Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles. Physiol Rev: 1986; 66 710 771 (Pubitemid 16074022)
    • (1986) Physiological Reviews , vol.66 , Issue.3 , pp. 710-771
    • Swynghedauw, B.1
  • 101
    • 63849130333 scopus 로고    scopus 로고
    • AMPK control of fat metabolism in skeletal muscle
    • Thomson D M, Winder W W. AMPK control of fat metabolism in skeletal muscle. Acta Physiol (Oxf): 2009; 196 147 154
    • (2009) Acta Physiol (Oxf) , vol.196 , pp. 147-154
    • Thomson, D.M.1    Winder, W.W.2
  • 102
    • 0031888710 scopus 로고    scopus 로고
    • Exercise-induced changes in protein metabolism
    • DOI 10.1046/j.1365-201X.1998.00306.x
    • Tipton K, Wolfe R. Exercise-induced changes in protein metabolism. Acta Physiol Scand: 1998; 162 377 387 (Pubitemid 28121417)
    • (1998) Acta Physiologica Scandinavica , vol.162 , Issue.3 , pp. 377-387
    • Tipton, K.D.1    Wolfe, R.R.2
  • 103
    • 0028107277 scopus 로고
    • Cytoplasm-to-myonucleus ratios and succinate dehydrogenase activities in adult rat slow and fast muscle fibers
    • DOI 10.1007/BF00305374
    • Tseng B S, Kasper C E, Edgerton V R. Cytoplasm-to-myonucleus ratios and succinate dehydrogenase activities in adult rat slow and fast muscle fibres. Cell Tissue Res: 1994; 275 39 49 (Pubitemid 24002627)
    • (1994) Cell and Tissue Research , vol.275 , Issue.1 , pp. 39-49
    • Tseng, B.S.1    Kasper, C.E.2    Edgerton, V.R.3
  • 105
    • 78049350199 scopus 로고    scopus 로고
    • Jaspers RT. the muscle fibre type-fibre size paradox: Hypertrophy or oxidative metabolism
    • van Wessel T, de Haan A, van der Laarse W J. Jaspers RT. The muscle fibre type-fibre size paradox: hypertrophy or oxidative metabolism? Eur J Appl Physiol: 2010; 110 665 694
    • (2010) Eur J Appl Physiol , vol.110 , pp. 665-694
    • Van Wessel, T.1    De Haan, A.2    Van Der Laarse, W.J.3
  • 106
    • 0027195505 scopus 로고
    • Relationships between alkali light-chain complement and myosin heavy-chain isoforms in single fast-twitch fibers of rat and rabbit
    • Wada M, Pette D. Relationships between alkali light-chain complement and myosin heavy-chain isoforms in single fast-twitch fibres of rat and rabbit. Eur J Biochem: 1993; 214 157 161 (Pubitemid 23168530)
    • (1993) European Journal of Biochemistry , vol.214 , Issue.1 , pp. 157-161
    • Wada, M.1    Pette, D.2
  • 107
    • 0035016280 scopus 로고    scopus 로고
    • Plasticity of skeletal myosin in endurance-trained rats (I). A quantitative study
    • DOI 10.1007/s004210100402
    • Wahrmann J P, Winand R, Rieu M. Plasticity of skeletal myosin in endurance-trained rats (I). A quantitative study. Eur J Appl Physiol: 2001; 84 367 372 (Pubitemid 32471939)
    • (2001) European Journal of Applied Physiology , vol.84 , Issue.5 , pp. 367-372
    • Wahrmann, J.P.1    Winand, R.2    Rieu, M.3
  • 109
    • 57349187147 scopus 로고    scopus 로고
    • Skeletal muscle adaptation and performance responses to once a day versus twice every second day endurance training regimens
    • Yeo W K, Paton C D, Garnham A P, Burke L M, Carey A L, Hawley J A. Skeletal muscle adaptation and performance responses to once a day versus twice every second day endurance training regimens. J Appl Physiol: 2008; 105 1462 1470
    • (2008) J Appl Physiol , vol.105 , pp. 1462-1470
    • Yeo, W.K.1    Paton, C.D.2    Garnham, A.P.3    Burke, L.M.4    Carey, A.L.5    Hawley, J.A.6


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