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Volumn 2, Issue 2, 2012, Pages 1441-1462

Respiratory muscle plasticity

Author keywords

[No Author keywords available]

Indexed keywords

MUSCLE PROTEIN;

EID: 84862165719     PISSN: None     EISSN: 20404603     Source Type: Journal    
DOI: 10.1002/cphy.c110050     Document Type: Article
Times cited : (30)

References (283)
  • 1
    • 0029058357 scopus 로고
    • Plasticity of myonuclear number in hypertrophied and atrophied mammalian skeletal muscle fibers
    • Allen DL, Monke SR, Talmadge RJ, Roy RR, Edgerton VR. Plasticity of myonuclear number in hypertrophied and atrophied mammalian skeletal muscle fibers. J Appl Physiol 78: 1969-1976, 1995.
    • (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
  • 2
    • 33646419774 scopus 로고    scopus 로고
    • Denervation effects on myonuclear domain size of rat diaphragm fibers
    • Aravamudan B, Mantilla CB, Zhan WZ, Sieck GC. Denervation effects on myonuclear domain size of rat diaphragm fibers. J Appl Physiol 100: 1617-1622, 2006.
    • (2006) J Appl Physiol , vol.100 , pp. 1617-1622
    • Aravamudan, B.1    Mantilla, C.B.2    Zhan, W.Z.3    Sieck, G.C.4
  • 3
    • 68249161970 scopus 로고    scopus 로고
    • The effect of denervation on protein synthesis and degradation in adult rat diaphragm muscle
    • Argadine HM, Hellyer NJ, Mantilla CB, Zhan WZ, Sieck GC. The effect of denervation on protein synthesis and degradation in adult rat diaphragm muscle. J Appl Physiol 107: 438-444, 2009.
    • (2009) J Appl Physiol , vol.107 , pp. 438-444
    • Argadine, H.M.1    Hellyer, N.J.2    Mantilla, C.B.3    Zhan, W.Z.4    Sieck, G.C.5
  • 4
    • 79251576152 scopus 로고    scopus 로고
    • Intracellular signaling pathways regulating net protein balance following diaphragm muscle denervation
    • Argadine HM, Mantilla CB, Zhan WZ, Sieck GC. Intracellular signaling pathways regulating net protein balance following diaphragm muscle denervation. Am J Physiol Cell Physiol 300: C318-C327, 2011.
    • (2011) Am J Physiol Cell Physiol , vol.300
    • Argadine, H.M.1    Mantilla, C.B.2    Zhan, W.Z.3    Sieck, G.C.4
  • 5
    • 0032948278 scopus 로고    scopus 로고
    • Phosphorylation of p70(S6k) correlates with increased skeletal muscle mass following resistance exercise
    • Baar K, Esser K. Phosphorylation of p70(S6k) correlates with increased skeletal muscle mass following resistance exercise. Am J Physiol 276: C120-127, 1999.
    • (1999) Am J Physiol , vol.276
    • Baar, K.1    Esser, K.2
  • 6
    • 0035168989 scopus 로고    scopus 로고
    • Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle
    • Baldwin KM, and Haddad F. Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle. J Appl Physiol 90: 345-357, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 345-357
    • Baldwin, K.M.1    Haddad, F.2
  • 8
    • 0015011589 scopus 로고
    • Histochemical, biochemical, and contractile properties of red, white, and intermediate fibers
    • Barnard RJ, Edgerton VR, Furukawa T, Peter JB. Histochemical, biochemical, and contractile properties of red, white, and intermediate fibers. Am J Physiol 220: 410-414, 1971.
    • (1971) Am J Physiol , vol.220 , pp. 410-414
    • Barnard, R.J.1    Edgerton, V.R.2    Furukawa, T.3    Peter, J.B.4
  • 9
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W, Walz J, Zuhl F, Seemuller E. The proteasome: Paradigm of a self-compartmentalizing protease. Cell 92: 367-380, 1998.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 10
    • 33644687189 scopus 로고    scopus 로고
    • Reduction of skeletal muscle atrophy by a proteasome inhibitor in a rat model of denervation
    • Beehler BC, Sleph PG, Benmassaoud L, Grover GJ. Reduction of skeletal muscle atrophy by a proteasome inhibitor in a rat model of denervation. Exp Biol Med (Maywood) 231: 335-341, 2006.
    • (2006) Exp Biol Med (Maywood) , vol.231 , pp. 335-341
    • Beehler, B.C.1    Sleph, P.G.2    Benmassaoud, L.3    Grover, G.J.4
  • 11
    • 64649093555 scopus 로고    scopus 로고
    • Mitochondrial fusion and division: Regulation and role in cell viability
    • Benard G, Karbowski M. Mitochondrial fusion and division: Regulation and role in cell viability. Semin Cell Dev Biol 20: 365-374, 2009.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 365-374
    • Benard, G.1    Karbowski, M.2
  • 12
    • 0035019007 scopus 로고    scopus 로고
    • Identification and characterization of members of the FKHR (FOX O) subclass of winged-helix transcription factors in the mouse
    • Biggs WH, III, Cavenee WK, Arden KC. Identification and characterization of members of the FKHR (FOX O) subclass of winged-helix transcription factors in the mouse. Mamm Genome 12: 416-425, 2001.
    • (2001) Mamm Genome , vol.12 , pp. 416-425
    • Biggs III, W.H.1    Cavenee, W.K.2    Arden, K.C.3
  • 13
    • 0033595011 scopus 로고    scopus 로고
    • Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of thewinged helix transcription factor FKHR1
    • Biggs WH, III, Meisenhelder J, Hunter T, Cavenee WK, Arden KC. Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of thewinged helix transcription factor FKHR1. Proc Natl Acad Sci U S A 96: 7421-7426, 1999.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 7421-7426
    • Biggs III, W.H.1    Meisenhelder, J.2    Hunter, T.3    Cavenee, W.K.4    Arden, K.C.5
  • 18
    • 0037025356 scopus 로고    scopus 로고
    • AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling
    • Bolster DR, Crozier SJ, Kimball SR, Jefferson LS. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J Biol Chem 277: 23977-23980, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 23977-23980
    • Bolster, D.R.1    Crozier, S.J.2    Kimball, S.R.3    Jefferson, L.S.4
  • 19
    • 0030661803 scopus 로고    scopus 로고
    • Molecular events underlying skeletal muscle atrophy and the development of effective countermeasures
    • Booth FW, Criswell DS. Molecular events underlying skeletal muscle atrophy and the development of effective countermeasures. Int J Sports Med 18(Suppl 4): S265-S269, 1997.
    • (1997) Int J Sports Med , vol.18 , Issue.SUPPL. 4
    • Booth, F.W.1    Criswell, D.S.2
  • 20
    • 0016809456 scopus 로고
    • Dissociation between nerve-muscle transmission and nerve trophic effects on rat diaphragm using type D botulinum toxin
    • Bray JJ, Harris AJ. Dissociation between nerve-muscle transmission and nerve trophic effects on rat diaphragm using type D botulinum toxin. J Physiol 253: 53-77, 1975.
    • (1975) J Physiol , vol.253 , pp. 53-77
    • Bray, J.J.1    Harris, A.J.2
  • 21
    • 0014864488 scopus 로고
    • Muscle fiber types: Howmany and what kind?
    • Brooke MH, Kaiser KK. Muscle fiber types: Howmany and what kind? Arch Neurol 23: 369-379, 1970.
    • (1970) Arch Neurol , vol.23 , pp. 369-379
    • Brooke, M.H.1    Kaiser, K.K.2
  • 24
    • 72849173018 scopus 로고
    • Interactions between motoneurones and muscles in respect of the characteristic speeds of responses
    • Buller AJ, Eccles JC, Eccles RM. Interactions between motoneurones and muscles in respect of the characteristic speeds of responses. J Physiol 150: 417-439, 1960.
    • (1960) J Physiol , vol.150 , pp. 417-439
    • Buller, A.J.1    Eccles, J.C.2    Eccles, R.M.3
  • 25
    • 0015024658 scopus 로고
    • The force-velocity characteristics of cat fast and slow-twitch skeletal muscle following crossinnervation
    • Buller AJ, Kean AJC, Ranatunga KW. The force-velocity characteristics of cat fast and slow-twitch skeletal muscle following crossinnervation. J Physiol 213: 66P-67P, 1971.
    • (1971) J Physiol , vol.213
    • Buller, A.J.1    Kean, A.J.C.2    Ranatunga, K.W.3
  • 26
    • 0014630458 scopus 로고
    • Enzymic properties of myosin in fast and slow twitch muscles of the cat following crossinnervation
    • Buller AJ, Mommaerts WF, Seraydarian K. Enzymic properties of myosin in fast and slow twitch muscles of the cat following crossinnervation. J Physiol 205: 581-597, 1969.
    • (1969) J Physiol , vol.205 , pp. 581-597
    • Buller, A.J.1    Mommaerts, W.F.2    Seraydarian, K.3
  • 27
    • 0000076646 scopus 로고
    • Motor units: Anatomy, physiology and functional organization
    • Peachey LD, editor Bethesda, MD: The American Physiological Society
    • Burke RE. Motor units: Anatomy, physiology and functional organization. In: Peachey LD, editor. Handbook of Physiology: The Nervous System, Motor Control. Bethesda, MD: The American Physiological Society, 1981, p. 345-422.
    • (1981) Handbook of Physiology: The Nervous System, Motor Control , pp. 345-422
    • Burke, R.E.1
  • 28
    • 0019965997 scopus 로고
    • An HRP study of the relation between cell size and motor unit type in cat ankle extensor motoneurons
    • Burke RE, Fleshman JW, Glenn LL, Lev-Tov A, O'Donovan MJ, Pinter MJ. An HRP study of the relation between cell size and motor unit type in cat ankle extensor motoneurons. J Comp Neurol 209: 17-28, 1982.
    • (1982) J Comp Neurol , vol.209 , pp. 17-28
    • Burke, R.E.1    Fleshman, J.W.2    Glenn, L.L.3    Lev-Tov, A.4    O'Donovan, M.J.5    Pinter, M.J.6
  • 29
    • 0015687892 scopus 로고
    • Physiological types and histochemical profiles in motor units of the cat gastrocnemius
    • Burke RE, Levine DN, Tsairis P, Zajac FE, III. Physiological types and histochemical profiles in motor units of the cat gastrocnemius. J Physiol 234: 723-748, 1973.
    • (1973) J Physiol , vol.234 , pp. 723-748
    • Burke, R.E.1    Levine, D.N.2    Tsairis, P.3    Zajac III, F.E.4
  • 30
    • 0015156701 scopus 로고
    • Mammalian motor units: Physiological-histochemical correlation in three types in cat gastrocnemius
    • Burke RE, Levine DN, Zajac FE, III. Mammalian motor units: Physiological-histochemical correlation in three types in cat gastrocnemius. Science 174: 709-712, 1971.
    • (1971) Science , vol.174 , pp. 709-712
    • Burke, R.E.1    Levine, D.N.2    Zajac III, F.E.3
  • 33
    • 0030055292 scopus 로고    scopus 로고
    • Microgravity-induced transformations of myosin isoforms and contractile properties of skeletal muscle
    • Caiozzo VJ, Haddad F, Baker MJ, Herrick RE, Prietto N, Baldwin KMg. Microgravity-induced transformations of myosin isoforms and contractile properties of skeletal muscle. J Appl Physiol 81: 123-132, 1996.
    • (1996) J Appl Physiol , vol.81 , pp. 123-132
    • Caiozzo, V.J.1    Haddad, F.2    Baker, M.J.3    Herrick, R.E.4    Prietto, N.5    Baldwin, K.M.G.6
  • 35
    • 0041320828 scopus 로고    scopus 로고
    • Novel regulatory mechanisms of mTOR signaling
    • Chen J. Novel regulatory mechanisms of mTOR signaling. Curr Top Microbiol Immunol 279: 245-257, 2004.
    • (2004) Curr Top Microbiol Immunol , vol.279 , pp. 245-257
    • Chen, J.1
  • 36
    • 0037429779 scopus 로고    scopus 로고
    • The deaf and the dumb: The biology of ErbB-2 and ErbB-3
    • Citri A, Skaria KB, Yarden Y. The deaf and the dumb: The biology of ErbB-2 and ErbB-3. Exp Cell Res 284: 54-65, 2003.
    • (2003) Exp Cell Res , vol.284 , pp. 54-65
    • Citri, A.1    Skaria, K.B.2    Yarden, Y.3
  • 38
    • 0026006501 scopus 로고
    • Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families
    • Coffer PJ, Woodgett JR. Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families. Eur J Biochem 201: 475-481, 1991.
    • (1991) Eur J Biochem , vol.201 , pp. 475-481
    • Coffer, P.J.1    Woodgett, J.R.2
  • 41
    • 62449266454 scopus 로고    scopus 로고
    • TORC-specific phosphorylation of mammalian target of rapamycin (mTOR): Phospho-Ser2481 is a marker for intact mTOR signaling complex 2
    • Copp J, Manning G, Hunter T. TORC-specific phosphorylation of mammalian target of rapamycin (mTOR): Phospho-Ser2481 is a marker for intact mTOR signaling complex 2. Cancer Res 69: 1821-1827, 2009.
    • (2009) Cancer Res , vol.69 , pp. 1821-1827
    • Copp, J.1    Manning, G.2    Hunter, T.3
  • 42
    • 85047689953 scopus 로고
    • 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMPactivated protein kinase in intact cells?
    • Corton JM, Gillespie JG, Hawley SA, Hardie DG. 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMPactivated protein kinase in intact cells? Eur J Biochem 229: 558-565, 1995.
    • (1995) Eur J Biochem , vol.229 , pp. 558-565
    • Corton, J.M.1    Gillespie, J.G.2    Hawley, S.A.3    Hardie, D.G.4
  • 43
    • 0023547077 scopus 로고
    • Exercise-induced satellite cell activation in growing and mature skeletal muscle
    • Darr KC, Schultz D. Exercise-induced satellite cell activation in growing and mature skeletal muscle. J Appl Physiol 63: 1816-1821, 1987.
    • (1987) J Appl Physiol , vol.63 , pp. 1816-1821
    • Darr, K.C.1    Schultz, D.2
  • 44
    • 0031046883 scopus 로고    scopus 로고
    • Effect of hyperinflation on the diaphragm
    • De Troyer A. Effect of hyperinflation on the diaphragm. Eur Respir J 10: 708-713, 1997.
    • (1997) Eur Respir J , vol.10 , pp. 708-713
    • De Troyer, A.1
  • 45
    • 0021181415 scopus 로고
    • Coordination between rib cage muscles and diaphragm during quiet breathing in humans
    • De Troyer A, Estenne M. Coordination between rib cage muscles and diaphragm during quiet breathing in humans. J Appl Physiol 57: 899-906, 1984.
    • (1984) J Appl Physiol , vol.57 , pp. 899-906
    • De Troyer, A.1    Estenne, M.2
  • 46
    • 0028356253 scopus 로고
    • Contribution of the rib cage inspiratory muscles to breathing in baboons
    • De Troyer A, Farkas GA. Contribution of the rib cage inspiratory muscles to breathing in baboons. Respir Physiol 97: 135-146, 1994.
    • (1994) Respir Physiol , vol.97 , pp. 135-146
    • De Troyer, A.1    Farkas, G.A.2
  • 47
    • 15544366320 scopus 로고    scopus 로고
    • Respiratory action of the intercostal muscles
    • De Troyer A, Kirkwood PA, Wilson TA. Respiratory action of the intercostal muscles. Physiol Rev 85: 717-756, 2005.
    • (2005) Physiol Rev , vol.85 , pp. 717-756
    • De Troyer, A.1    Kirkwood, P.A.2    Wilson, T.A.3
  • 48
    • 0030938477 scopus 로고    scopus 로고
    • Hyperinflation and respiratory muscle interaction
    • Decramer M. Hyperinflation and respiratory muscle interaction. Eur Respir J 10: 934-941, 1997.
    • (1997) Eur Respir J , vol.10 , pp. 934-941
    • Decramer, M.1
  • 49
    • 0021709787 scopus 로고
    • Respiratory changes in parasternal intercostal length
    • Decramer M, De Troyer A. Respiratory changes in parasternal intercostal length. J Appl Physiol 57: 1254-1260, 1984.
    • (1984) J Appl Physiol , vol.57 , pp. 1254-1260
    • Decramer, M.1    De Troyer, A.2
  • 52
    • 0035890654 scopus 로고    scopus 로고
    • Identification of cathepsin L as a differentially expressed message associated with skeletal musclewasting
    • Deval C, Mordier S, Obled C, Bechet D, Combaret L, Attaix D, Ferrara M. Identification of cathepsin L as a differentially expressed message associated with skeletal musclewasting. Biochem J 360: 143-150, 2001.
    • (2001) Biochem J , vol.360 , pp. 143-150
    • Deval, C.1    Mordier, S.2    Obled, C.3    Bechet, D.4    Combaret, L.5    Attaix, D.6    Ferrara, M.7
  • 53
    • 0023137044 scopus 로고
    • Correlation of recruitment order with axonal conduction velocity for supraspinally driven diaphragmatic motor units
    • Dick TE, Kong FJ, Berger AJ. Correlation of recruitment order with axonal conduction velocity for supraspinally driven diaphragmatic motor units. J Neurophysiol 57: 245-259, 1987.
    • (1987) J Neurophysiol , vol.57 , pp. 245-259
    • Dick, T.E.1    Kong, F.J.2    Berger, A.J.3
  • 54
    • 69749083989 scopus 로고
    • Recruitment order of diaphragmatic motor units obeys Hennemans's size principle
    • Sieck GC, Gandevia SC, Cameron WE, editors. New York: Alan R. Liss
    • Dick TE, Kong FJ, Berger AJ. Recruitment order of diaphragmatic motor units obeys Hennemans's size principle. In: Sieck GC, Gandevia SC, Cameron WE, editors. Respiratory Muscles and Their Neuromotor Control. New York: Alan R. Liss, 1987, p. 249-261.
    • (1987) Respiratory Muscles and Their Neuromotor Control , pp. 249-261
    • Dick, T.E.1    Kong, F.J.2    Berger, A.J.3
  • 55
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • Du J, Wang X, Miereles C, Bailey JL, Debigare R, Zheng B, Price SR, Mitch WE. Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 113: 115-123, 2004.
    • (2004) J Clin Invest , vol.113 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereles, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6    Price, S.R.7    Mitch, W.E.8
  • 56
    • 34447626457 scopus 로고    scopus 로고
    • Aging enhances a mechanically-induced reduction in tendon strength by an active process involving matrix metalloproteinase activity
    • Dudhia J, Scott CM, Draper ER, Heinegard D, Pitsillides AA, Smith RK. Aging enhances a mechanically-induced reduction in tendon strength by an active process involving matrix metalloproteinase activity. Aging Cell 6: 547-556, 2007.
    • (2007) Aging Cell , vol.6 , pp. 547-556
    • Dudhia, J.1    Scott, C.M.2    Draper, E.R.3    Heinegard, D.4    Pitsillides, A.A.5    Smith, R.K.6
  • 58
    • 0027193962 scopus 로고
    • Satellite cells from slow rat muscle express slow myosin under appropriate culture conditions
    • Dusterhoft S, and Pette D. Satellite cells from slow rat muscle express slow myosin under appropriate culture conditions. Differentiation 53: 25-33, 1993.
    • (1993) Differentiation , vol.53 , pp. 25-33
    • Dusterhoft, S.1    Pette, D.2
  • 59
    • 12644254374 scopus 로고
    • Problems of plasticity and organization at simplest levels of mammalian central nervous system
    • Eccles JC. Problems of plasticity and organization at simplest levels of mammalian central nervous system. Perspect Biol Med 1: 379-396, 1958.
    • (1958) Perspect Biol Med , vol.1 , pp. 379-396
    • Eccles, J.C.1
  • 60
    • 0024435359 scopus 로고
    • Oxidative capacity and capillary density of diaphragm motor units
    • Enad JG, Fournier M, Sieck GC. Oxidative capacity and capillary density of diaphragm motor units. J Appl Physiol 67: 620-627, 1989.
    • (1989) J Appl Physiol , vol.67 , pp. 620-627
    • Enad, J.G.1    Fournier, M.2    Sieck, G.C.3
  • 61
    • 70350365514 scopus 로고    scopus 로고
    • Neurotrophins induce neuregulin release through protein kinase Cdelta activation
    • Esper RM, Loeb JA. Neurotrophins induce neuregulin release through protein kinase Cdelta activation. J Biol Chem284: 26251-26260, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 26251-26260
    • Esper, R.M.1    Loeb, J.A.2
  • 62
    • 0020576567 scopus 로고
    • Diaphragm in emphysematous hamsters: Sarcomere adaptability
    • Farkas GA, Roussos C. Diaphragm in emphysematous hamsters: Sarcomere adaptability. J Appl Physiol 54: 1635-1640, 1983.
    • (1983) J Appl Physiol , vol.54 , pp. 1635-1640
    • Farkas, G.A.1    Roussos, C.2
  • 63
    • 1842599025 scopus 로고
    • A quantitative comparison between the energy liberated and the work performed by the isolated sartorius muscle of the frog
    • Fenn WO. A quantitative comparison between the energy liberated and the work performed by the isolated sartorius muscle of the frog. J Physiol 58: 175-203, 1923.
    • (1923) J Physiol , vol.58 , pp. 175-203
    • Fenn, W.O.1
  • 64
    • 0023916792 scopus 로고
    • Mechanical properties of muscle units in the cat diaphragm
    • Fournier M, Sieck GC. Mechanical properties of muscle units in the cat diaphragm. J Neurophysiol 59: 1055-1066, 1988.
    • (1988) J Neurophysiol , vol.59 , pp. 1055-1066
    • Fournier, M.1    Sieck, G.C.2
  • 65
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy
    • Furuno K, Goodman MN, Goldberg AL. Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. J Biol Chem 265: 8550-8557, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 8550-8557
    • Furuno, K.1    Goodman, M.N.2    Goldberg, A.L.3
  • 66
    • 0025167044 scopus 로고
    • Activation of human respiratory muscles during different voluntary manoeuvres
    • Gandevia SC, McKenzie DK, Plassman BL. Activation of human respiratory muscles during different voluntary manoeuvres. J Physiol 428: 387-403, 1990.
    • (1990) J Physiol , vol.428 , pp. 387-403
    • Gandevia, S.C.1    McKenzie, D.K.2    Plassman, B.L.3
  • 67
    • 0020071664 scopus 로고
    • Effects of denervation on the distribution of myosin isozymes in skeletal muscle fibers
    • Gauthier GF, Hobbs AW. Effects of denervation on the distribution of myosin isozymes in skeletal muscle fibers. Exp Neurol 76: 331-346, 1982.
    • (1982) Exp Neurol , vol.76 , pp. 331-346
    • Gauthier, G.F.1    Hobbs, A.W.2
  • 69
    • 0034057272 scopus 로고    scopus 로고
    • Expression of myosin heavy-chain isoforms in the respiratory muscles following inspiratory resistive breathing
    • Gea J, Hamid Q, Czaika G, Zhu E, Mohan-Ram V, Goldspink G, Grassino A. Expression of myosin heavy-chain isoforms in the respiratory muscles following inspiratory resistive breathing. Am J Respir Crit Care Med 161: 1274-1278, 2000.
    • (2000) Am J Respir Crit Care Med , vol.161 , pp. 1274-1278
    • Gea, J.1    Hamid, Q.2    Czaika, G.3    Zhu, E.4    Mohan-Ram, V.5    Goldspink, G.6    Grassino, A.7
  • 70
    • 0043130652 scopus 로고    scopus 로고
    • Denervationinduced changes in myosin heavy chain expression in the rat diaphragm muscle
    • Geiger PC, Bailey JP, Zhan WZ, Mantilla CB, Sieck GC. Denervationinduced changes in myosin heavy chain expression in the rat diaphragm muscle. J Appl Physiol 95: 611-619, 2003.
    • (2003) J Appl Physiol , vol.95 , pp. 611-619
    • Geiger, P.C.1    Bailey, J.P.2    Zhan, W.Z.3    Mantilla, C.B.4    Sieck, G.C.5
  • 71
    • 33845439850 scopus 로고    scopus 로고
    • Mechanisms underlying myosin heavy chain expression during development of the rat diaphragm muscle
    • Geiger PC, Bailey JP, Mantilla CB, Zhan WZ, Sieck GC. Mechanisms underlying myosin heavy chain expression during development of the rat diaphragm muscle. J Appl Physiol 101: 1546-1555, 2006.
    • (2006) J Appl Physiol , vol.101 , pp. 1546-1555
    • Geiger, P.C.1    Bailey, J.P.2    Mantilla, C.B.3    Zhan, W.Z.4    Sieck, G.C.5
  • 72
  • 73
    • 0035109086 scopus 로고    scopus 로고
    • Effect of unilateral denervation on maximum specific force in rat diaphragm muscle fibers
    • Geiger PC, Cody MJ, Macken RL, Bayrd ME, Sieck GC. Effect of unilateral denervation on maximum specific force in rat diaphragm muscle fibers. J Appl Physiol 90: 1196-1204, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 1196-1204
    • Geiger, P.C.1    Cody, M.J.2    Macken, R.L.3    Bayrd, M.E.4    Sieck, G.C.5
  • 74
    • 0035172673 scopus 로고    scopus 로고
    • Mechanisms underlying increased force generation by rat diaphragm muscle fibers during development
    • Geiger PC, Cody MJ, Macken RL, Bayrd ME, Sieck GC. Mechanisms underlying increased force generation by rat diaphragm muscle fibers during development. J Appl Physiol 90: 380-388, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 380-388
    • Geiger, P.C.1    Cody, M.J.2    Macken, R.L.3    Bayrd, M.E.4    Sieck, G.C.5
  • 75
    • 0033871523 scopus 로고    scopus 로고
    • Maximum specific force depends on myosin heavy chain content in rat diaphragm muscle fibers
    • Geiger PC, Cody MJ, Macken RL, Sieck GC. Maximum specific force depends on myosin heavy chain content in rat diaphragm muscle fibers. J Appl Physiol 89: 695-703, 2000.
    • (2000) J Appl Physiol , vol.89 , pp. 695-703
    • Geiger, P.C.1    Cody, M.J.2    Macken, R.L.3    Sieck, G.C.4
  • 76
    • 0032756372 scopus 로고    scopus 로고
    • Force-calcium relationship depends on myosin heavy chain and troponin isoforms in rat diaphragm muscle fibers
    • Geiger PC, Cody MJ, Sieck GC. Force-calcium relationship depends on myosin heavy chain and troponin isoforms in rat diaphragm muscle fibers. J Appl Physiol 87: 1894-1900, 1999.
    • (1999) J Appl Physiol , vol.87 , pp. 1894-1900
    • Geiger, P.C.1    Cody, M.J.2    Sieck, G.C.3
  • 77
    • 0032520009 scopus 로고    scopus 로고
    • 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway
    • Gingras AC, Kennedy SG, O'Leary MA, Sonenberg N, Hay N. 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway. Genes Dev 12: 502-513, 1998.
    • (1998) Genes Dev , vol.12 , pp. 502-513
    • Gingras, A.C.1    Kennedy, S.G.2    O'Leary, M.A.3    Sonenberg, N.4    Hay, N.5
  • 78
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • Glass DJ. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat Cell Biol 5: 87-90, 2003.
    • (2003) Nat Cell Biol , vol.5 , pp. 87-90
    • Glass, D.J.1
  • 80
    • 0036850342 scopus 로고    scopus 로고
    • Voluntary exercise induces a BDNF-mediated mechanism that promotes neuroplasticity
    • Gomez-Pinilla F, Ying Z, Roy RR, Molteni R, Edgerton VR. Voluntary exercise induces a BDNF-mediated mechanism that promotes neuroplasticity. J Neurophysiol 88: 2187-2195, 2002.
    • (2002) J Neurophysiol , vol.88 , pp. 2187-2195
    • Gomez-Pinilla, F.1    Ying, Z.2    Roy, R.R.3    Molteni, R.4    Edgerton, V.R.5
  • 81
    • 0013905848 scopus 로고
    • Tension development in highly stretched vertebrate muscle fibres
    • Gordon AM, Huxley AF, Julian FJ. Tension development in highly stretched vertebrate muscle fibres. J Physiol 184: 143-169, 1966a.
    • (1966) J Physiol , vol.184 , pp. 143-169
    • Gordon, A.M.1    Huxley, A.F.2    Julian, F.J.3
  • 82
    • 0013905011 scopus 로고
    • The variation in isometric tension with sarcomere length in vertebrate muscle fibres
    • Gordon AM, Huxley AF, Julian FJ. The variation in isometric tension with sarcomere length in vertebrate muscle fibres. J Physiol 184: 170-192, 1966b.
    • (1966) J Physiol , vol.184 , pp. 170-192
    • Gordon, A.M.1    Huxley, A.F.2    Julian, F.J.3
  • 83
    • 0027938363 scopus 로고
    • Changes in satellite cell mitotic activity during acute period of unilateral diaphragm denervation
    • Gosselin LE, Brice G, Carlson B, Prakash YS, Sieck GC. Changes in satellite cell mitotic activity during acute period of unilateral diaphragm denervation. J Appl Physiol 77: 1128-1134, 1994.
    • (1994) J Appl Physiol , vol.77 , pp. 1128-1134
    • Gosselin, L.E.1    Brice, G.2    Carlson, B.3    Prakash, Y.S.4    Sieck, G.C.5
  • 84
    • 0028805452 scopus 로고
    • Changes in diaphragm muscle collagen gene expression after acute unilateral denervation
    • Gosselin LE, Sieck GC, Aleff RA, Martinez DA, Vailas AC. Changes in diaphragm muscle collagen gene expression after acute unilateral denervation. J Appl Physiol 79: 1249-1254, 1995.
    • (1995) J Appl Physiol , vol.79 , pp. 1249-1254
    • Gosselin, L.E.1    Sieck, G.C.2    Aleff, R.A.3    Martinez, D.A.4    Vailas, A.C.5
  • 86
    • 34848861463 scopus 로고    scopus 로고
    • The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor
    • Greer EL, Oskoui PR, Banko MR, Maniar JM, Gygi MP, Gygi SP, Brunet A. The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor. J Biol Chem 282: 30107-30119, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 30107-30119
    • Greer, E.L.1    Oskoui, P.R.2    Banko, M.R.3    Maniar, J.M.4    Gygi, M.P.5    Gygi, S.P.6    Brunet, A.7
  • 87
    • 38049056893 scopus 로고    scopus 로고
    • Evaluation and management of respiratory muscle dysfunction in ALS
    • Gregory SA. Evaluation and management of respiratory muscle dysfunction in ALS. Neuro Rehabilitation 22: 435-443, 2007.
    • (2007) Neuro Rehabilitation , vol.22 , pp. 435-443
    • Gregory, S.A.1
  • 88
    • 0031935916 scopus 로고    scopus 로고
    • Determination of muscle contractile properties: The importance of the nerve
    • Gundersen K. Determination of muscle contractile properties: The importance of the nerve. Acta Physiol Scand 162: 333-341, 1998.
    • (1998) Acta Physiol Scand , vol.162 , pp. 333-341
    • Gundersen, K.1
  • 91
    • 2942518272 scopus 로고    scopus 로고
    • Differential regulation of the phosphoinositide 3-kinase and MAP kinase pathways by hepatocyte growth factor vs. insulin-like growth factor-I in myogenic cells
    • Halevy O, Cantley LC. Differential regulation of the phosphoinositide 3-kinase and MAP kinase pathways by hepatocyte growth factor vs. insulin-like growth factor-I in myogenic cells. Exp Cell Res 297: 224-234, 2004.
    • (2004) Exp Cell Res , vol.297 , pp. 224-234
    • Halevy, O.1    Cantley, L.C.2
  • 92
    • 0038517075 scopus 로고    scopus 로고
    • ATP consumption rate per cross bridge depends on myosin heavy chain isoform
    • Han YS, Geiger PC, Cody MJ, Macken RL, Sieck GC. ATP consumption rate per cross bridge depends on myosin heavy chain isoform. J Appl Physiol 94: 2188-2196, 2003.
    • (2003) J Appl Physiol , vol.94 , pp. 2188-2196
    • Han, Y.S.1    Geiger, P.C.2    Cody, M.J.3    Macken, R.L.4    Sieck, G.C.5
  • 93
    • 0031007065 scopus 로고    scopus 로고
    • The AMP-activated protein kinase-fuel gauge of the mammalian cell?
    • Hardie DG, Carling D. The AMP-activated protein kinase-fuel gauge of the mammalian cell? Eur J Biochem 246: 259-273, 1997.
    • (1997) Eur J Biochem , vol.246 , pp. 259-273
    • Hardie, D.G.1    Carling, D.2
  • 94
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N, Sonenberg N. Upstream and downstream of mTOR. Genes Dev 18: 1926-1945, 2004.
    • (2004) Genes Dev , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 96
    • 0000977079 scopus 로고
    • Relation between size of neurons and their susceptibility to discharge
    • Henneman E. Relation between size of neurons and their susceptibility to discharge. Science 126: 1345-1346, 1957.
    • (1957) Science , vol.126 , pp. 1345-1346
    • Henneman, E.1
  • 97
    • 0001019836 scopus 로고
    • Functional organization of motoneuron pool and its inputs
    • Brookhart JM, Mountcastle VB, editors. Bethesda: American Physiological Society
    • Henneman E, Mendell LM. Functional organization of motoneuron pool and its inputs. In: Brookhart JM, Mountcastle VB, editors. Handbook of Physiology. Bethesda: American Physiological Society, 1981, p. 423-507.
    • (1981) Handbook of Physiology , pp. 423-507
    • Henneman, E.1    Mendell, L.M.2
  • 98
    • 2942702696 scopus 로고
    • Functional significance of cell size in spinal motoneurons
    • Henneman E, Somjen G, Carpenter DO. Functional significance of cell size in spinal motoneurons. J Neurophysiol 28: 560-580, 1965.
    • (1965) J Neurophysiol , vol.28 , pp. 560-580
    • Henneman, E.1    Somjen, G.2    Carpenter, D.O.3
  • 99
    • 0030988362 scopus 로고    scopus 로고
    • Daily durations of spontaneous activity in cat's ankle muscles. Exp
    • Hensbergen E, Kernell D. Daily durations of spontaneous activity in cat's ankle muscles. Exp Brain Res 115: 325-332, 1997.
    • (1997) Brain Res , vol.115 , pp. 325-332
    • Hensbergen, E.1    Kernell, D.2
  • 100
    • 0020541181 scopus 로고
    • Central respiratory drive and recruitment order of phrenic and inspiratory laryngeal motoneurones
    • Hilaire G, Gauthier P, Monteau R. Central respiratory drive and recruitment order of phrenic and inspiratory laryngeal motoneurones. Respir Physiol 51: 341-359, 1983.
    • (1983) Respir Physiol , vol.51 , pp. 341-359
    • Hilaire, G.1    Gauthier, P.2    Monteau, R.3
  • 101
    • 0013339592 scopus 로고
    • Determination of recruitment order of phrenic motoneurons
    • Sieck GC, Gandevia SC, Cameron WE, editors. New York: Alan R. Liss
    • Hilaire G, Monteau R, Khatib M. Determination of recruitment order of phrenic motoneurons. In: Sieck GC, Gandevia SC, Cameron WE, editors. Respiratory Muscles and Their Neuromotor Control. New York: Alan R. Liss, 1987, p. 249-261.
    • (1987) Respiratory Muscles and Their Neuromotor Control , pp. 249-261
    • Hilaire, G.1    Monteau, R.2    Khatib, M.3
  • 103
    • 77949714047 scopus 로고    scopus 로고
    • Interplay between the inspiratory and postural functions of the human parasternal intercostal muscles
    • Hudson AL, Butler JE, Gandevia SC, De Troyer A. Interplay between the inspiratory and postural functions of the human parasternal intercostal muscles. J Neurophysiol 103: 1622-1629, 2010.
    • (2010) J Neurophysiol , vol.103 , pp. 1622-1629
    • Hudson, A.L.1    Butler, J.E.2    Gandevia, S.C.3    De Troyer, A.4
  • 104
    • 11144317940 scopus 로고    scopus 로고
    • Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy
    • Hunter RB, Kandarian SC. Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy. J Clin Invest 114: 1504-1511, 2004.
    • (2004) J Clin Invest , vol.114 , pp. 1504-1511
    • Hunter, R.B.1    Kandarian, S.C.2
  • 106
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley AF. Muscle structure and theories of contraction. Prog Biophysics Biophys Chem 7: 255-318, 1957.
    • (1957) Prog Biophysics Biophys Chem , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 108
    • 0037312507 scopus 로고    scopus 로고
    • Tor signalling in bugs, brain and brawn
    • Jacinto E, Hall MN. Tor signalling in bugs, brain and brawn. Nat Rev Mol Cell Biol 4: 117-126, 2003.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 117-126
    • Jacinto, E.1    Hall, M.N.2
  • 109
    • 0032967514 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 is the predominant insulin-regulated eukaryotic initiation factor 2B kinase in skeletal muscle
    • Jefferson LS, Fabian JR, Kimball SR. Glycogen synthase kinase-3 is the predominant insulin-regulated eukaryotic initiation factor 2B kinase in skeletal muscle. Int J Biochem Cell Biol 31: 191-200, 1999.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 191-200
    • Jefferson, L.S.1    Fabian, J.R.2    Kimball, S.R.3
  • 110
    • 0028895952 scopus 로고
    • Neuregulins are concentrated at nerve-muscle synapses and activate ACh-receptor gene expression
    • Jo SA, Zhu X, Marchionni MA, Burden SJ. Neuregulins are concentrated at nerve-muscle synapses and activate ACh-receptor gene expression. Nature 373: 158-161, 1995.
    • (1995) Nature , vol.373 , pp. 158-161
    • Jo, S.A.1    Zhu, X.2    Marchionni, M.A.3    Burden, S.J.4
  • 111
    • 0023221672 scopus 로고
    • Electrical properties of phrenic motoneurons in the cat: Correlation with inspiratory drive
    • Jodkowski JS, Viana F, Dick TE, Berger AJ. Electrical properties of phrenic motoneurons in the cat: Correlation with inspiratory drive. J Neurophysiol 58: 105-124, 1987.
    • (1987) J Neurophysiol , vol.58 , pp. 105-124
    • Jodkowski, J.S.1    Viana, F.2    Dick, T.E.3    Berger, A.J.4
  • 112
    • 0025882091 scopus 로고
    • Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily
    • Jones PF, Jakubowicz T, Pitossi FJ, Maurer F, Hemmings BA. Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily. Proc Natl Acad Sci U S A 88: 4171-4175, 1991.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 4171-4175
    • Jones, P.F.1    Jakubowicz, T.2    Pitossi, F.J.3    Maurer, F.4    Hemmings, B.A.5
  • 113
    • 33745221937 scopus 로고    scopus 로고
    • Role of AMPK in skeletal muscle metabolic regulation and adaptation in relation to exercise
    • Jorgensen SB, Richter EA, Wojtaszewski JF. Role of AMPK in skeletal muscle metabolic regulation and adaptation in relation to exercise. J Physiol 574: 17-31, 2006.
    • (2006) J Physiol , vol.574 , pp. 17-31
    • Jorgensen, S.B.1    Richter, E.A.2    Wojtaszewski, J.F.3
  • 115
    • 77954454429 scopus 로고    scopus 로고
    • Metalloproteinase-dependent cleavage of neuregulin and autocrine stimulation of vascular endothelial cells
    • Kalinowski A, Plowes NJ, Huang Q, Berdejo-Izquierdo C, Russell RR, Russell KS. Metalloproteinase-dependent cleavage of neuregulin and autocrine stimulation of vascular endothelial cells. FASEB J 24: 2567-2575, 2010.
    • (2010) FASEB J , vol.24 , pp. 2567-2575
    • Kalinowski, A.1    Plowes, N.J.2    Huang, Q.3    Berdejo-Izquierdo, C.4    Russell, R.R.5    Russell, K.S.6
  • 116
    • 4544358547 scopus 로고    scopus 로고
    • Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated Type I (slow twitch/red muscle) fiber genes, and impaired glycemic control
    • Kamei Y, Miura S, Suzuki M, Kai Y, Mizukami J, Taniguchi T, Mochida K, Hata T, Matsuda J, Aburatani H, Nishino I, Ezaki O. Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated Type I (slow twitch/red muscle) fiber genes, and impaired glycemic control. J Biol Chem279: 41114-41123, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 41114-41123
    • Kamei, Y.1    Miura, S.2    Suzuki, M.3    Kai, Y.4    Mizukami, J.5    Taniguchi, T.6    Mochida, K.7    Hata, T.8    Matsuda, J.9    Aburatani, H.10    Nishino, I.11    Ezaki, O.12
  • 117
    • 0027971637 scopus 로고
    • Respiratory muscle compensation for unilateral or bilateral hemidiaphragm paralysis in awake canines
    • Katagiri M, Young RN, Platt RS, Kieser TM, Easton PA. Respiratory muscle compensation for unilateral or bilateral hemidiaphragm paralysis in awake canines. J Appl Physiol 77: 1972-1982, 1994.
    • (1994) J Appl Physiol , vol.77 , pp. 1972-1982
    • Katagiri, M.1    Young, R.N.2    Platt, R.S.3    Kieser, T.M.4    Easton, P.A.5
  • 118
    • 0018236997 scopus 로고
    • Developmental pattern of muscle fiber types in human ventilatory muscles
    • Keens TG, Bryan AC, Levison H, Ianuzzo CD. Developmental pattern of muscle fiber types in human ventilatory muscles. J Appl Physiol 44: 909-913, 1978.
    • (1978) J Appl Physiol , vol.44 , pp. 909-913
    • Keens, T.G.1    Bryan, A.C.2    Levison, H.3    Ianuzzo, C.D.4
  • 120
    • 33646077675 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) activating agents cause dephosphorylation of Akt and glycogen synthase kinase-3
    • King TD, Song L, Jope RS. AMP-activated protein kinase (AMPK) activating agents cause dephosphorylation of Akt and glycogen synthase kinase-3. Biochem Pharmacol 71: 1637-1647, 2006.
    • (2006) Biochem Pharmacol , vol.71 , pp. 1637-1647
    • King, T.D.1    Song, L.2    Jope, R.S.3
  • 121
    • 0032079873 scopus 로고    scopus 로고
    • Regulation of translation initiation factors by signal transduction
    • Kleijn M, Scheper GC, Voorma HO, Thomas AA. Regulation of translation initiation factors by signal transduction. Eur J Biochem 253: 531-544, 1998.
    • (1998) Eur J Biochem , vol.253 , pp. 531-544
    • Kleijn, M.1    Scheper, G.C.2    Voorma, H.O.3    Thomas, A.A.4
  • 122
    • 0022900772 scopus 로고
    • Firing properties and hypercapnic responses of single phrenic motor axons in the rat
    • Kong FJ, Berger AJ. Firing properties and hypercapnic responses of single phrenic motor axons in the rat. J Appl Physiol 61: 1999-2004, 1986.
    • (1986) J Appl Physiol , vol.61 , pp. 1999-2004
    • Kong, F.J.1    Berger, A.J.2
  • 123
    • 33744529772 scopus 로고    scopus 로고
    • Scoliosis and the respiratory system
    • Koumbourlis AC. Scoliosis and the respiratory system. Paediatr Respir Rev 7: 152-160, 2006.
    • (2006) Paediatr Respir Rev , vol.7 , pp. 152-160
    • Koumbourlis, A.C.1
  • 124
    • 77956623574 scopus 로고    scopus 로고
    • Coordinated maintenance of muscle cell size control by AMP-activated protein kinase
    • Lantier L, Mounier R, Leclerc J, Pende M, Foretz M, Viollet B. Coordinated maintenance of muscle cell size control by AMP-activated protein kinase. FASEB J 24: 3555-3561, 2010.
    • (2010) FASEB J , vol.24 , pp. 3555-3561
    • Lantier, L.1    Mounier, R.2    Leclerc, J.3    Pende, M.4    Foretz, M.5    Viollet, B.6
  • 125
    • 0028229205 scopus 로고
    • Modification in activity of medullary respiratory-related neurons for vocalization and swallowing
    • Larson CR, Yajima Y, Ko P. Modification in activity of medullary respiratory-related neurons for vocalization and swallowing. J Neurophysiol 71: 2294-2304, 1994.
    • (1994) J Neurophysiol , vol.71 , pp. 2294-2304
    • Larson, C.R.1    Yajima, Y.2    Ko, P.3
  • 126
    • 13244298415 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway
    • Latres E, Amini AR, Amini AA, Griffiths J, Martin FJ, Wei Y, Lin HC, Yancopoulos GD, Glass DJ. Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J Biol Chem 280: 2737-2744, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 2737-2744
    • Latres, E.1    Amini, A.R.2    Amini, A.A.3    Griffiths, J.4    Martin, F.J.5    Wei, Y.6    Lin, H.C.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 128
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states
    • Lecker SH, Solomon V, Mitch WE, Goldberg AL. Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J Nutr 129: 227S-237S, 1999.
    • (1999) J Nutr , vol.129
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 129
    • 2542496898 scopus 로고    scopus 로고
    • Regulation of muscle protein degradation: Coordinated control of apoptotic and ubiquitinproteasome systems by phosphatidylinositol 3 kinase
    • Lee SW, Dai G, Hu Z, Wang X, Du J, Mitch WE. Regulation of muscle protein degradation: Coordinated control of apoptotic and ubiquitinproteasome systems by phosphatidylinositol 3 kinase. J Am Soc Nephrol 15: 1537-1545, 2004.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 1537-1545
    • Lee, S.W.1    Dai, G.2    Hu, Z.3    Wang, X.4    Du, J.5    Mitch, W.E.6
  • 130
    • 0028829716 scopus 로고
    • Response of the inspiratory intercostal [correction of intercoastal] muscles to increased inertial loads
    • Legrand A, Cappello M, De Troyer A. Response of the inspiratory intercostal [correction of intercoastal] muscles to increased inertial loads. Respir Physiol 102: 17-27, 1995.
    • (1995) Respir Physiol , vol.102 , pp. 17-27
    • Legrand, A.1    Cappello, M.2    De Troyer, A.3
  • 132
    • 33744938146 scopus 로고    scopus 로고
    • Effect of severe short-termmalnutrition on diaphragmmuscle signal transduction pathways influencing protein turnover
    • Lewis MI, Bodine SC, Kamangar N, Xu X, Da X, Fournier M. Effect of severe short-termmalnutrition on diaphragmmuscle signal transduction pathways influencing protein turnover. J Appl Physiol 100: 1799-1806, 2006.
    • (2006) J Appl Physiol , vol.100 , pp. 1799-1806
    • Lewis, M.I.1    Bodine, S.C.2    Kamangar, N.3    Xu, X.4    Da, X.5    Fournier, M.6
  • 134
    • 0042128821 scopus 로고    scopus 로고
    • Influence of varying degrees of malnutrition on IGF-I expression in the rat diaphragm
    • Lewis MI, Li H, Huang ZS, Biring MS, Cercek B, Fournier M. Influence of varying degrees of malnutrition on IGF-I expression in the rat diaphragm. J Appl Physiol 95: 555-562, 2003.
    • (2003) J Appl Physiol , vol.95 , pp. 555-562
    • Lewis, M.I.1    Li, H.2    Huang, Z.S.3    Biring, M.S.4    Cercek, B.5    Fournier, M.6
  • 135
    • 0025311937 scopus 로고
    • Effect of acute nutritional deprivation on diaphragm structure and function
    • Lewis MI, Sieck GC. Effect of acute nutritional deprivation on diaphragm structure and function. J Appl Physiol 68: 1938-1944, 1990.
    • (1990) J Appl Physiol , vol.68 , pp. 1938-1944
    • Lewis, M.I.1    Sieck, G.C.2
  • 136
    • 0026553103 scopus 로고
    • Adaptations of the diaphragm in emphysema
    • Lewis MI, Zhan WZ, Sieck GC. Adaptations of the diaphragm in emphysema. J Appl Physiol 72: 934-943, 1992.
    • (1992) J Appl Physiol , vol.72 , pp. 934-943
    • Lewis, M.I.1    Zhan, W.Z.2    Sieck, G.C.3
  • 137
    • 0023856536 scopus 로고
    • What is the cause of the ageing atrophy? Total number, size and proportion of different fiber types studied in whole vastus lateralis muscle from 15- to 83-year-old men
    • Lexell J, Taylor CC, Sjostrom M. What is the cause of the ageing atrophy? Total number, size and proportion of different fiber types studied in whole vastus lateralis muscle from 15- to 83-year-old men. J Neurol Sci 84: 275-294, 1988.
    • (1988) J Neurol Sci , vol.84 , pp. 275-294
    • Lexell, J.1    Taylor, C.C.2    Sjostrom, M.3
  • 138
    • 0000591785 scopus 로고
    • Recruitment and some other factors of reflex inhibition
    • Liddell EGT, Sherrington CS. Recruitment and some other factors of reflex inhibition. Proc R Soc Lond (Biol) 97: 488-518, 1925.
    • (1925) Proc R Soc Lond (Biol) , vol.97 , pp. 488-518
    • Liddell, E.G.T.1    Sherrington, C.S.2
  • 140
    • 0037088909 scopus 로고    scopus 로고
    • Neuregulin expression at neuromuscular synapses is modulated by synaptic activity and neurotrophic factors
    • Loeb JA, Hmadcha A, Fischbach GD, Land SJ, Zakarian VL. Neuregulin expression at neuromuscular synapses is modulated by synaptic activity and neurotrophic factors. J Neurosci 22: 2206-2214, 2002.
    • (2002) J Neurosci , vol.22 , pp. 2206-2214
    • Loeb, J.A.1    Hmadcha, A.2    Fischbach, G.D.3    Land, S.J.4    Zakarian, V.L.5
  • 141
    • 0031805660 scopus 로고    scopus 로고
    • The neuregulin precursor proARIA is processed to ARIA after expression on the cell surface by a protein kinase C-enhanced mechanism
    • Loeb JA, Susanto ET, Fischbach GD. The neuregulin precursor proARIA is processed to ARIA after expression on the cell surface by a protein kinase C-enhanced mechanism. Mol Cell Neurosci 11: 77-91, 1998.
    • (1998) Mol Cell Neurosci , vol.11 , pp. 77-91
    • Loeb, J.A.1    Susanto, E.T.2    Fischbach, G.D.3
  • 142
    • 0019977492 scopus 로고
    • Action of the diaphragm on the rib cage inferred from a force-balance analysis
    • Loring SH, Mead J. Action of the diaphragm on the rib cage inferred from a force-balance analysis. J Appl Physiol 53: 756-760, 1982.
    • (1982) J Appl Physiol , vol.53 , pp. 756-760
    • Loring, S.H.1    Mead, J.2
  • 145
    • 34247603597 scopus 로고    scopus 로고
    • Synaptic vesicle pools at diaphragm neuromuscular junctions vary with motoneuron soma, not axon terminal, inactivity
    • Mantilla CB, Rowley KL, Zhan WZ, Fahim MA, Sieck GC. Synaptic vesicle pools at diaphragm neuromuscular junctions vary with motoneuron soma, not axon terminal, inactivity. Neurosci 146: 178-189, 2007.
    • (2007) Neurosci , vol.146 , pp. 178-189
    • Mantilla, C.B.1    Rowley, K.L.2    Zhan, W.Z.3    Fahim, M.A.4    Sieck, G.C.5
  • 147
    • 0037372430 scopus 로고    scopus 로고
    • Invited review:Mechanisms underlying motor unit plasticity in the respiratory system
    • Mantilla CB, Sieck GC. Invited review:Mechanisms underlying motor unit plasticity in the respiratory system. J Appl Physiol 94: 1230-1241, 2003.
    • (2003) J Appl Physiol , vol.94 , pp. 1230-1241
    • Mantilla, C.B.1    Sieck, G.C.2
  • 148
    • 49649120920 scopus 로고    scopus 로고
    • Key aspects of phrenic motoneuron and diaphragm muscle development during the perinatal period
    • Mantilla CB, Sieck GC. Key aspects of phrenic motoneuron and diaphragm muscle development during the perinatal period. J Appl Physiol 104: 1818-1827, 2008.
    • (2008) J Appl Physiol , vol.104 , pp. 1818-1827
    • Mantilla, C.B.1    Sieck, G.C.2
  • 149
    • 72049130271 scopus 로고    scopus 로고
    • Neuromuscular adaptations to respiratory muscle inactivity
    • Mantilla CB, Sieck GC. Neuromuscular adaptations to respiratory muscle inactivity. Respir Physiol Neurobiol 169: 133-140, 2009.
    • (2009) Respir Physiol Neurobiol , vol.169 , pp. 133-140
    • Mantilla, C.B.1    Sieck, G.C.2
  • 150
    • 53849100999 scopus 로고    scopus 로고
    • Trophic factor expression in phrenic motor neurons
    • Mantilla CB, Sieck GC. Trophic factor expression in phrenic motor neurons. Respir Physiol Neurobiol 164: 252-262, 2008.
    • (2008) Respir Physiol Neurobiol , vol.164 , pp. 252-262
    • Mantilla, C.B.1    Sieck, G.C.2
  • 153
    • 0042750799 scopus 로고    scopus 로고
    • Akt and PI 3-kinase signaling in cardiomyocyte hypertrophy and survival
    • Matsui T, Nagoshi T, Rosenzweig A. Akt and PI 3-kinase signaling in cardiomyocyte hypertrophy and survival. Cell Cycle 2: 220-223, 2003.
    • (2003) Cell Cycle , vol.2 , pp. 220-223
    • Matsui, T.1    Nagoshi, T.2    Rosenzweig, A.3
  • 156
    • 0019986247 scopus 로고
    • Analysis of volume displacement and length changes of the diaphragm during breathing
    • Mead J, Loring SH. Analysis of volume displacement and length changes of the diaphragm during breathing. J Appl Physiol 53: 750-755, 1982.
    • (1982) J Appl Physiol , vol.53 , pp. 750-755
    • Mead, J.1    Loring, S.H.2
  • 157
    • 0014039731 scopus 로고
    • Significance of the relationship between lung recoil and maximum expiratory flow
    • Mead J, Turner JM, Macklem PT, Little JB. Significance of the relationship between lung recoil and maximum expiratory flow. J Appl Physiol 22: 95-108, 1967.
    • (1967) J Appl Physiol , vol.22 , pp. 95-108
    • Mead, J.1    Turner, J.M.2    Macklem, P.T.3    Little, J.B.4
  • 158
    • 0026713728 scopus 로고
    • Discharge patterns of phrenic motoneurons during fictive coughing and vomiting in decerebrate cats
    • Milano S, Grelot L, Bianchi AL, Iscoe S. Discharge patterns of phrenic motoneurons during fictive coughing and vomiting in decerebrate cats. J Appl Physiol 73: 1626-1636, 1992.
    • (1992) J Appl Physiol , vol.73 , pp. 1626-1636
    • Milano, S.1    Grelot, L.2    Bianchi, A.L.3    Iscoe, S.4
  • 159
    • 0025192548 scopus 로고
    • Diaphragmatic and external intercostal muscle control during vomiting: Behavior of inspiratory bulbospinal neurons
    • Miller AD, Nonaka S, Lakos SF, Tan LK. Diaphragmatic and external intercostal muscle control during vomiting: Behavior of inspiratory bulbospinal neurons. J Neurophysiol 63(1): 31-36, 1990.
    • (1990) J Neurophysiol , vol.63 , Issue.1 , pp. 31-36
    • Miller, A.D.1    Nonaka, S.2    Lakos, S.F.3    Tan, L.K.4
  • 160
    • 0028849768 scopus 로고
    • Myoneural interactions affect diaphragm muscle adaptations to inactivity
    • Miyata H, Zhan WZ, Prakash YS, Sieck GC. Myoneural interactions affect diaphragm muscle adaptations to inactivity. J Appl Physiol 79: 1640-1649, 1995.
    • (1995) J Appl Physiol , vol.79 , pp. 1640-1649
    • Miyata, H.1    Zhan, W.Z.2    Prakash, Y.S.3    Sieck, G.C.4
  • 161
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 15: 1101-1111, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 162
    • 0021853029 scopus 로고
    • Central determination of recruitment order: Intracellular study of phrenic motoneurons
    • Monteau R, Khatib M, Hilaire G. Central determination of recruitment order: Intracellular study of phrenic motoneurons. Neurosci Lett 56: 341-346, 1985.
    • (1985) Neurosci Lett , vol.56 , pp. 341-346
    • Monteau, R.1    Khatib, M.2    Hilaire, G.3
  • 163
    • 34548450714 scopus 로고    scopus 로고
    • AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes
    • Nakashima K, Yakabe Y. AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes. Biosci Biotechnol Biochem 71: 1650-1656, 2007.
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 1650-1656
    • Nakashima, K.1    Yakabe, Y.2
  • 164
    • 0026055844 scopus 로고
    • Effect of aging on human adductor pollicis muscle function
    • Narici MV, Bordini M, Cerretelli P. Effect of aging on human adductor pollicis muscle function. J Appl Physiol 71: 1277-1281, 1991.
    • (1991) J Appl Physiol , vol.71 , pp. 1277-1281
    • Narici, M.V.1    Bordini, M.2    Cerretelli, P.3
  • 165
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • Nave BT, Ouwens M, Withers DJ, Alessi DR, Shepherd PR. Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem J 344(Pt 2): 427-431, 1999.
    • (1999) Biochem J , vol.344 , Issue.PART 2 , pp. 427-431
    • Nave, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 167
  • 168
    • 68049100485 scopus 로고    scopus 로고
    • Sepsis and AMPK activation by AICAR differentially regulate Fox O-1, -3 and -4 mRNA in striated muscle
    • Nystrom GJ, Lang CH. Sepsis and AMPK activation by AICAR differentially regulate Fox O-1, -3 and -4 mRNA in striated muscle. Int J Clin Exp Med 1: 50-63, 2008.
    • (2008) Int J Clin Exp Med , vol.1 , pp. 50-63
    • Nystrom, G.J.1    Lang, C.H.2
  • 169
    • 0037047098 scopus 로고    scopus 로고
    • A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification
    • Pallafacchina G, Calabria E, Serrano AL, Kalhovde JM, Schiaffino S. A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification. Proc Natl Acad Sci U S A 99: 9213-9218, 2002.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9213-9218
    • Pallafacchina, G.1    Calabria, E.2    Serrano, A.L.3    Kalhovde, J.M.4    Schiaffino, S.5
  • 170
    • 0028894746 scopus 로고
    • Developmental changes in chest wall compliance in infancy and early childhood
    • Papastamelos C, Panitch HB, England SE, Allen JL. Developmental changes in chest wall compliance in infancy and early childhood. J Appl Physiol 78: 179-184, 1995.
    • (1995) J Appl Physiol , vol.78 , pp. 179-184
    • Papastamelos, C.1    Panitch, H.B.2    England, S.E.3    Allen, J.L.4
  • 171
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function
    • Pause A, Belsham GJ, Gingras AC, Donze O, Lin TA, Lawrence JC, Jr, Sonenberg N. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. Nature 371: 762-767, 1994.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donze, O.4    Lin, T.A.5    Lawrence Jr., J.C.6    Sonenberg, N.7
  • 172
    • 0015493810 scopus 로고
    • Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits
    • Peter JB, Barnard RJ, Edgerton VR, Gillespie CA, Stempel KE. Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry 11: 2627-2633, 1972.
    • (1972) Biochemistry , vol.11 , pp. 2627-2633
    • Peter, J.B.1    Barnard, R.J.2    Edgerton, V.R.3    Gillespie, C.A.4    Stempel, K.E.5
  • 173
    • 0034629365 scopus 로고    scopus 로고
    • FKBP12-rapamycinassociated protein (FRAP) autophosphorylates at serine 2481 under translationally repressive conditions
    • Peterson RT, Beal PA, Comb MJ, Schreiber SL. FKBP12-rapamycinassociated protein (FRAP) autophosphorylates at serine 2481 under translationally repressive conditions. J Biol Chem 275: 7416-7423, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 7416-7423
    • Peterson, R.T.1    Beal, P.A.2    Comb, M.J.3    Schreiber, S.L.4
  • 174
    • 0035116376 scopus 로고    scopus 로고
    • Historical Perspectives: Plasticity of mammalian skeletal muscle
    • Pette D. Historical Perspectives: Plasticity of mammalian skeletal muscle. J Appl Physiol 90: 1119-1124, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 1119-1124
    • Pette, D.1
  • 175
    • 0017065471 scopus 로고
    • Time dependent effects on contractile properties, fibre population, myosin light chains and enzymes of energy metabolism in intermittently and continuously stimulated fast twitch muscles of the rabbit
    • Pette D, Muller W, Leisner E, Vrbova G. Time dependent effects on contractile properties, fibre population, myosin light chains and enzymes of energy metabolism in intermittently and continuously stimulated fast twitch muscles of the rabbit. Pflugers Arch 364: 103-112, 1976.
    • (1976) Pflugers Arch , vol.364 , pp. 103-112
    • Pette, D.1    Muller, W.2    Leisner, E.3    Vrbova, G.4
  • 176
    • 0032875219 scopus 로고    scopus 로고
    • The impact of biochemical methods for single muscle fibre analysis
    • Pette D, Peuker H, Staron RS. The impact of biochemical methods for single muscle fibre analysis. Acta Physiol Scand 166: 261-277, 1999.
    • (1999) Acta Physiol Scand , vol.166 , pp. 261-277
    • Pette, D.1    Peuker, H.2    Staron, R.S.3
  • 177
    • 0015915804 scopus 로고
    • Effects of long-term electrical stimulation on some contractile and metabolic characteristics of fast rabbit muscles
    • Pette D, Smith ME, Staudte HW, Vrbova G. Effects of long-term electrical stimulation on some contractile and metabolic characteristics of fast rabbit muscles. Pflugers Arch 338: 257-272, 1973.
    • (1973) Pflugers Arch , vol.338 , pp. 257-272
    • Pette, D.1    Smith, M.E.2    Staudte, H.W.3    Vrbova, G.4
  • 178
    • 0031023872 scopus 로고    scopus 로고
    • Mammalian skeletal muscle fiber type transitions
    • Pette D, Staron RS. Mammalian skeletal muscle fiber type transitions. Int Rev Cytol 170: 143-223, 1997.
    • (1997) Int Rev Cytol , vol.170 , pp. 143-223
    • Pette, D.1    Staron, R.S.2
  • 179
    • 0034665188 scopus 로고    scopus 로고
    • Myosin isoforms, muscle fiber types, and transitions
    • Pette D, Staron RS. Myosin isoforms, muscle fiber types, and transitions. Microsc Res Tech 50: 500-509, 2000.
    • (2000) Microsc Res Tech , vol.50 , pp. 500-509
    • Pette, D.1    Staron, R.S.2
  • 180
    • 0026450106 scopus 로고
    • Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation
    • Pette D, Vrbova G. Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation. Rev Physiol Biochem Pharmacol 120: 115-202, 1992.
    • (1992) Rev Physiol Biochem Pharmacol , vol.120 , pp. 115-202
    • Pette, D.1    Vrbova, G.2
  • 181
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart CM. Ubiquitin in chains. Trends Biochem Sci 25: 544-548, 2000.
    • (2000) Trends Biochem Sci , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 182
    • 53549124415 scopus 로고    scopus 로고
    • Motor responses of the sternocleidomastoid muscle in patients with amyotrophic lateral sclerosis
    • Pinto S, de Carvalho M. Motor responses of the sternocleidomastoid muscle in patients with amyotrophic lateral sclerosis. Muscle Nerve 38: 1312-1317, 2008.
    • (2008) Muscle Nerve , vol.38 , pp. 1312-1317
    • Pinto, S.1    de Carvalho, M.2
  • 184
    • 70350517753 scopus 로고    scopus 로고
    • Prolonged mechanical ventilation alters diaphragmatic structure and function
    • Powers SK, Kavazis AN, Levine S. Prolonged mechanical ventilation alters diaphragmatic structure and function. Crit Care Med 37: S347-S353, 2009.
    • (2009) Crit Care Med , vol.37
    • Powers, S.K.1    Kavazis, A.N.2    Levine, S.3
  • 187
    • 0033007547 scopus 로고    scopus 로고
    • Inactivity-induced remodeling of neuromuscular junctions in rat diaphragmatic muscle
    • Prakash YS, Miyata H, Zhan WZ, Sieck GC. Inactivity-induced remodeling of neuromuscular junctions in rat diaphragmatic muscle. Muscle Nerve 22: 307-319, 1999.
    • (1999) Muscle Nerve , vol.22 , pp. 307-319
    • Prakash, Y.S.1    Miyata, H.2    Zhan, W.Z.3    Sieck, G.C.4
  • 188
    • 84939404283 scopus 로고
    • Adaptations of diaphragm neuromuscular junction following inactivity
    • Prakash YS, Zhan WZ, Miyata H, Sieck GC. Adaptations of diaphragm neuromuscular junction following inactivity. Acta Anat (Basel) 154: 147-161, 1995.
    • (1995) Acta Anat (Basel) , vol.154 , pp. 147-161
    • Prakash, Y.S.1    Zhan, W.Z.2    Miyata, H.3    Sieck, G.C.4
  • 190
    • 0026465921 scopus 로고
    • Protein phosphorylation in translational control
    • Proud CG. Protein phosphorylation in translational control. Curr Top Cell Regul 32: 243-369, 1992.
    • (1992) Curr Top Cell Regul , vol.32 , pp. 243-369
    • Proud, C.G.1
  • 193
    • 0030009739 scopus 로고    scopus 로고
    • A reevaluation of the capbinding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate
    • Rau M, Ohlmann T, Morley SJ, Pain VM. A reevaluation of the capbinding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate. J Biol Chem 271: 8983-8990, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 8983-8990
    • Rau, M.1    Ohlmann, T.2    Morley, S.J.3    Pain, V.M.4
  • 194
    • 0033006919 scopus 로고    scopus 로고
    • eIF4E activity is regulated at multiple levels
    • Raught B, Gingras AC. eIF4E activity is regulated at multiple levels. Int J Biochem Cell Biol 31: 43-57, 1999.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 43-57
    • Raught, B.1    Gingras, A.C.2
  • 195
    • 84862199865 scopus 로고    scopus 로고
    • Systems biology: A four-step process
    • Chien S, Chen PC, Fung YC, editors. Singapore: World Scientific Publishing Co
    • Reed JL, Palsson BO. Systems biology: A four-step process. In: Chien S, Chen PC, Fung YC, editors. An Introductory Text to Bioengineering, Singapore: World Scientific Publishing Co, 2008, p. 387-399.
    • (2008) An Introductory Text to Bioengineering , pp. 387-399
    • Reed, J.L.1    Palsson, B.O.2
  • 196
    • 79951581392 scopus 로고    scopus 로고
    • Inhibition of IkappaB kinase alpha (IKKalpha) or IKKbeta (IKKbeta) plus forkhead box O (Foxo) abolishes skeletal muscle atrophy
    • Reed SA, Senf SM, Cornwell EW, Kandarian SC, Judge AR. Inhibition of IkappaB kinase alpha (IKKalpha) or IKKbeta (IKKbeta) plus forkhead box O (Foxo) abolishes skeletal muscle atrophy. Biochem Biophys Res Commun 405: 491-496, 2011.
    • (2011) Biochem Biophys Res Commun , vol.405 , pp. 491-496
    • Reed, S.A.1    Senf, S.M.2    Cornwell, E.W.3    Kandarian, S.C.4    Judge, A.R.5
  • 197
    • 0142219824 scopus 로고    scopus 로고
    • Activity-dependent plasticity of transmitter release from nerve terminals in rat fast and slow muscles
    • Reid B, Martinov VN, Nja A, Lomo T, Bewick GS. Activity-dependent plasticity of transmitter release from nerve terminals in rat fast and slow muscles. J Neurosci 23: 9340-9348, 2003.
    • (2003) J Neurosci , vol.23 , pp. 9340-9348
    • Reid, B.1    Martinov, V.N.2    Nja, A.3    Lomo, T.4    Bewick, G.S.5
  • 198
    • 0037123438 scopus 로고    scopus 로고
    • Control of Ser2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load
    • Reynolds THt, Bodine SC, Lawrence JC, Jr. Control of Ser2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load. J Biol Chem 277: 17657-17662, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 17657-17662
    • Reynolds, T.H.T.1    Bodine, S.C.2    Lawrence Jr., J.C.3
  • 199
    • 0018965440 scopus 로고
    • Effects of contraction force and frequency on postexercise hyperemia in human calf muscles
    • Richardson D, Shewchuk R. Effects of contraction force and frequency on postexercise hyperemia in human calf muscles. J Appl Physiol 49: 649-654, 1980.
    • (1980) J Appl Physiol , vol.49 , pp. 649-654
    • Richardson, D.1    Shewchuk, R.2
  • 205
    • 61949363968 scopus 로고    scopus 로고
    • Skeletal muscle eEF2 and 4EBP1 phosphorylation during endurance exercise is dependent on intensity and muscle fiber type
    • Rose AJ, Bisiani B, Vistisen B, Kiens B, Richter EA. Skeletal muscle eEF2 and 4EBP1 phosphorylation during endurance exercise is dependent on intensity and muscle fiber type. Am J Physiol Regul Integr Comp Physiol 296: R326-R333, 2009.
    • (2009) Am J Physiol Regul Integr Comp Physiol , vol.296
    • Rose, A.J.1    Bisiani, B.2    Vistisen, B.3    Kiens, B.4    Richter, E.A.5
  • 206
    • 0028338899 scopus 로고
    • Satellite cell activity is required for hypertrophy of overloaded adult rat muscle
    • Rosenblatt JD, Yong D, Parry DJ. Satellite cell activity is required for hypertrophy of overloaded adult rat muscle. Muscle Nerve 17: 608-613, 1994.
    • (1994) Muscle Nerve , vol.17 , pp. 608-613
    • Rosenblatt, J.D.1    Yong, D.2    Parry, D.J.3
  • 207
    • 0022413089 scopus 로고
    • Function and fatigue of respiratory muscles
    • Roussos C. Function and fatigue of respiratory muscles. Chest 88: 124S-132S, 1985.
    • (1985) Chest , vol.88
    • Roussos, C.1
  • 209
    • 0022257888 scopus 로고
    • Biochemical and physiological changes in overloaded rat fast- and slowtwitch ankle extensors
    • Roy RR, Baldwin KM, Martin TP, Chimarusti SP, Edgerton VR. Biochemical and physiological changes in overloaded rat fast- and slowtwitch ankle extensors. J Appl Physiol 59: 639-646, 1985.
    • (1985) J Appl Physiol , vol.59 , pp. 639-646
    • Roy, R.R.1    Baldwin, K.M.2    Martin, T.P.3    Chimarusti, S.P.4    Edgerton, V.R.5
  • 210
    • 0032818177 scopus 로고    scopus 로고
    • Modulation of myonuclear number in functionally overloaded and exercised rat plantaris fibers
    • Roy RR, Monke SR, Allen DL, Edgerton VR. Modulation of myonuclear number in functionally overloaded and exercised rat plantaris fibers. J Appl Physiol 87: 634-642, 1999.
    • (1999) J Appl Physiol , vol.87 , pp. 634-642
    • Roy, R.R.1    Monke, S.R.2    Allen, D.L.3    Edgerton, V.R.4
  • 211
    • 33846015010 scopus 로고    scopus 로고
    • Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases
    • Sacheck JM, Hyatt JP, Raffaello A, Jagoe RT, Roy RR, Edgerton VR, Lecker SH, Goldberg AL. Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases. Faseb J 21: 140-155, 2007.
    • (2007) Faseb J , vol.21 , pp. 140-155
    • Sacheck, J.M.1    Hyatt, J.P.2    Raffaello, A.3    Jagoe, R.T.4    Roy, R.R.5    Edgerton, V.R.6    Lecker, S.H.7    Goldberg, A.L.8
  • 212
    • 4544293878 scopus 로고    scopus 로고
    • IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
    • Sacheck JM, Ohtsuka A, McLary SC, Goldberg AL. IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1. Am J Physiol Endocrinol Metab 287: E591-601, 2004.
    • (2004) Am J Physiol Endocrinol Metab , vol.287
    • Sacheck, J.M.1    Ohtsuka, A.2    McLary, S.C.3    Goldberg, A.L.4
  • 213
    • 0028021566 scopus 로고
    • The mechanism by which epidermal growth factor inhibits glycogen synthase kinase 3 in A431 cells
    • Saito Y, Vandenheede JR, Cohen P. The mechanism by which epidermal growth factor inhibits glycogen synthase kinase 3 in A431 cells. Biochem J 303(Pt 1): 27-31, 1994.
    • (1994) Biochem J , vol.303 , Issue.PART 1 , pp. 27-31
    • Saito, Y.1    Vandenheede, J.R.2    Cohen, P.3
  • 214
    • 0014508666 scopus 로고
    • The influence of activity on some contractile characteristics of mammalian fast and slow muscles
    • Salmons S, Vrbova G. The influence of activity on some contractile characteristics of mammalian fast and slow muscles. J Physiol 201: 535-549, 1969.
    • (1969) J Physiol , vol.201 , pp. 535-549
    • Salmons, S.1    Vrbova, G.2
  • 215
    • 49049083353 scopus 로고    scopus 로고
    • Signaling in muscle atrophy and hypertrophy
    • Sandri M. Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda) 23: 160-170, 2008.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 160-170
    • Sandri, M.1
  • 217
    • 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 DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 14: 1296-1302, 2004.
    • (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    Tempst, P.7    Sabatini, D.M.8
  • 219
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307: 1098-1101, 2005.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 220
    • 0036082131 scopus 로고    scopus 로고
    • Altered diaphragm contractile properties with controlled mechanical ventilation
    • Sassoon CS, Caiozzo VJ, Manka A, Sieck GC. Altered diaphragm contractile properties with controlled mechanical ventilation. J Appl Physiol 92: 2585-2595, 2002.
    • (2002) J Appl Physiol , vol.92 , pp. 2585-2595
    • Sassoon, C.S.1    Caiozzo, V.J.2    Manka, A.3    Sieck, G.C.4
  • 221
    • 4444372263 scopus 로고    scopus 로고
    • Assist-control mechanical ventilation attenuates ventilator-induced diaphragmatic dysfunction
    • Sassoon CS, Zhu E, Caiozzo VJ. Assist-control mechanical ventilation attenuates ventilator-induced diaphragmatic dysfunction. Am J Respir Crit Care Med 170: 626-632, 2004.
    • (2004) Am J Respir Crit Care Med , vol.170 , pp. 626-632
    • Sassoon, C.S.1    Zhu, E.2    Caiozzo, V.J.3
  • 222
  • 223
    • 0023898573 scopus 로고
    • Embryonic and neonatal myosin heavy chain in denervated and paralyzed rat skeletal muscle
    • Schiaffino S, Gorza L, Pitton G, Saggin L, Ausoni S, Sartore S, Lomo T. Embryonic and neonatal myosin heavy chain in denervated and paralyzed rat skeletal muscle. Dev Biol 127: 1-11, 1988.
    • (1988) Dev Biol , vol.127 , pp. 1-11
    • Schiaffino, S.1    Gorza, L.2    Pitton, G.3    Saggin, L.4    Ausoni, S.5    Sartore, S.6    Lomo, T.7
  • 225
    • 0028060295 scopus 로고
    • Myosin isoforms in mammalian skeletal muscle
    • Schiaffino S Reggiani C. Myosin isoforms in mammalian skeletal muscle. J Appl Physiol 77: 493-501, 1994.
    • (1994) J Appl Physiol , vol.77 , pp. 493-501
    • Schiaffino, S.1    Reggiani, C.2
  • 226
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • Schiaffino S, Reggiani C. Molecular diversity of myofibrillar proteins: Gene regulation and functional significance. Physiol Rev 76: 371-423, 1996.
    • (1996) Physiol Rev , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 227
    • 0033136116 scopus 로고    scopus 로고
    • Toward metabolic phenomics: Analysis of genomic data using flux balances
    • Schilling CH, Edwards JS, Palsson BO. Toward metabolic phenomics: Analysis of genomic data using flux balances. Biotechnol Prog 15: 288-295, 1999.
    • (1999) Biotechnol Prog , vol.15 , pp. 288-295
    • Schilling, C.H.1    Edwards, J.S.2    Palsson, B.O.3
  • 228
    • 0022271052 scopus 로고
    • Response of satellite cells to focal skeletal muscle injury
    • Schultz E, Jaryszak DL, Valliere CR. Response of satellite cells to focal skeletal muscle injury. Muscle And Nerve 8: 217-222, 1985.
    • (1985) Muscle And Nerve , vol.8 , pp. 217-222
    • Schultz, E.1    Jaryszak, D.L.2    Valliere, C.R.3
  • 229
    • 55549101931 scopus 로고    scopus 로고
    • Hsp70 overexpression inhibits NF-kappaB and Foxo3a transcriptional activities and prevents skeletal muscle atrophy
    • Senf SM, Dodd SL, McClung JM, Judge AR. Hsp70 overexpression inhibits NF-kappaB and Foxo3a transcriptional activities and prevents skeletal muscle atrophy. FASEB J 22: 3836-3845, 2008.
    • (2008) FASEB J , vol.22 , pp. 3836-3845
    • Senf, S.M.1    Dodd, S.L.2    McClung, J.M.3    Judge, A.R.4
  • 230
    • 0033679673 scopus 로고    scopus 로고
    • 4E-BP1 and S6K1: Translational integration sites for nutritional and hormonal information in muscle
    • Shah OJ, Anthony JC, Kimball SR, Jefferson LS. 4E-BP1 and S6K1: Translational integration sites for nutritional and hormonal information in muscle. Am J Physiol Endocrinol Metab 279: E715-E729, 2000.
    • (2000) Am J Physiol Endocrinol Metab , vol.279
    • Shah, O.J.1    Anthony, J.C.2    Kimball, S.R.3    Jefferson, L.S.4
  • 233
    • 0000546367 scopus 로고
    • Some functional problems attaching to convergence
    • Sherrington CS. Some functional problems attaching to convergence. Proc R Soc Lond (Biol) 105: 332-362, 1929.
    • (1929) Proc R Soc Lond (Biol) , vol.105 , pp. 332-362
    • Sherrington, C.S.1
  • 234
    • 0023940555 scopus 로고
    • Diaphragm muscle: Structural and functional organization
    • Sieck GC. Diaphragm muscle: Structural and functional organization. Clin Chest Med 9: 195-210, 1988.
    • (1988) Clin Chest Med , vol.9 , pp. 195-210
    • Sieck, G.C.1
  • 235
    • 0025933705 scopus 로고
    • Diaphragm motor units and their response to altered use
    • Sieck GC. Diaphragm motor units and their response to altered use. Sem Respir Med 12: 258-269, 1991.
    • (1991) Sem Respir Med , vol.12 , pp. 258-269
    • Sieck, G.C.1
  • 236
    • 0000948480 scopus 로고
    • Neural control of the inspiratory pump
    • Sieck GC. Neural control of the inspiratory pump. NIPS 6: 260-264, 1991.
    • (1991) NIPS , vol.6 , pp. 260-264
    • Sieck, G.C.1
  • 237
    • 0028114132 scopus 로고
    • Physiological effects of diaphragm muscle denervation and disuse
    • Fanburg BL, Sicilian L, editors. Philadelphia, PA: W. B. Saunders Company
    • Sieck GC. Physiological effects of diaphragm muscle denervation and disuse. In: Fanburg BL, Sicilian L, editors. Clinics in Chest Medicine: Respiratory Dysfunction in Neuromuscular Disease, Philadelphia, PA: W. B. Saunders Company, 1994, p. 641-659.
    • (1994) Clinics in Chest Medicine: Respiratory Dysfunction in Neuromuscular Disease , pp. 641-659
    • Sieck, G.C.1
  • 238
    • 0024401724 scopus 로고
    • Diaphragm motor unit recruitment during ventilatory and nonventilatory behaviors
    • Sieck GC Fournier M. Diaphragm motor unit recruitment during ventilatory and nonventilatory behaviors. J Appl Physiol 66: 2539-2545, 1989.
    • (1989) J Appl Physiol , vol.66 , pp. 2539-2545
    • Sieck, G.C.1    Fournier, M.2
  • 239
    • 0000142578 scopus 로고
    • Developmental aspects of diaphragm muscle cells: Structural and functional organization
    • Haddad GG, Farber JP, editors. New York: Marcel Dekker
    • Sieck GC, Fournier M. Developmental aspects of diaphragm muscle cells: Structural and functional organization. In: Haddad GG, Farber JP, editors. Developmental Neurobiology of Breathing. New York: Marcel Dekker, 1991, p. 375-428.
    • (1991) Developmental Neurobiology of Breathing , pp. 375-428
    • Sieck, G.C.1    Fournier, M.2
  • 240
    • 0024570218 scopus 로고
    • Fiber type composition of muscle units in the cat diaphragm
    • Sieck GC, Fournier M, Enad JG. Fiber type composition of muscle units in the cat diaphragm. Neurosci Lett 97: 29-34, 1989.
    • (1989) Neurosci Lett , vol.97 , pp. 29-34
    • Sieck, G.C.1    Fournier, M.2    Enad, J.G.3
  • 241
    • 0030054948 scopus 로고    scopus 로고
    • Myosin phenotype and SDH enzyme variability among motor unit fibers
    • Sieck GC, Fournier M, Prakash YS, Blanco CE. Myosin phenotype and SDH enzyme variability among motor unit fibers. J Appl Physiol 80: 2179-2189, 1996.
    • (1996) J Appl Physiol , vol.80 , pp. 2179-2189
    • Sieck, G.C.1    Fournier, M.2    Prakash, Y.S.3    Blanco, C.E.4
  • 242
    • 0024338496 scopus 로고
    • Effects of undernutrition on diaphragm fiber size, SDH activity, and fatigue resistance
    • Sieck GC, Lewis MI, Blanco CE. Effects of undernutrition on diaphragm fiber size, SDH activity, and fatigue resistance. J Appl Physiol 66: 2196-2205, 1989.
    • (1989) J Appl Physiol , vol.66 , pp. 2196-2205
    • Sieck, G.C.1    Lewis, M.I.2    Blanco, C.E.3
  • 243
    • 41449114776 scopus 로고    scopus 로고
    • Effect of mechanical ventilation on the diaphragm
    • Sieck GC, Mantilla CB. Effect of mechanical ventilation on the diaphragm. N Engl J Med 358: 1392-1394, 2008.
    • (2008) N Engl J Med , vol.358 , pp. 1392-1394
    • Sieck, G.C.1    Mantilla, C.B.2
  • 244
    • 0030883150 scopus 로고    scopus 로고
    • Cross bridge kinetics in respiratory muscles
    • Sieck GC, Prakash YS. Cross bridge kinetics in respiratory muscles. Eur Respir J 10: 2147-2158, 1997.
    • (1997) Eur Respir J , vol.10 , pp. 2147-2158
    • Sieck, G.C.1    Prakash, Y.S.2
  • 245
    • 0031159930 scopus 로고    scopus 로고
    • Morphological adaptations of neuromuscular junctions depend on fiber type
    • Sieck GC, Prakash YS. Morphological adaptations of neuromuscular junctions depend on fiber type. Can J Appl Physiol 22: 197-230, 1997.
    • (1997) Can J Appl Physiol , vol.22 , pp. 197-230
    • Sieck, G.C.1    Prakash, Y.S.2
  • 246
    • 0037405869 scopus 로고    scopus 로고
    • Changes in actomyosin ATP consumption rate in rat diaphragm muscle fibers during postnatal development
    • Sieck GC, Prakash YS, Han YS, Fang YH, Geiger PC, Zhan WZ. Changes in actomyosin ATP consumption rate in rat diaphragm muscle fibers during postnatal development. J Appl Physiol 94: 1896-1902, 2003.
    • (2003) J Appl Physiol , vol.94 , pp. 1896-1902
    • Sieck, G.C.1    Prakash, Y.S.2    Han, Y.S.3    Fang, Y.H.4    Geiger, P.C.5    Zhan, W.Z.6
  • 248
    • 0028871718 scopus 로고
    • SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle
    • Sieck GC, Zhan WZ, Prakash YS, Daood MJ, Watchko JF. SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle. J Appl Physiol 79: 1629-1639, 1995.
    • (1995) J Appl Physiol , vol.79 , pp. 1629-1639
    • Sieck, G.C.1    Zhan, W.Z.2    Prakash, Y.S.3    Daood, M.J.4    Watchko, J.F.5
  • 249
    • 0347723879 scopus 로고    scopus 로고
    • The Akt-regulated forkhead transcription factor FOXO3a controls endothelial cell viability through modulation of the caspase-8 inhibitor FLIP
    • Skurk C, Maatz H, Kim HS, Yang J, Abid MR, Aird WC, Walsh K. The Akt-regulated forkhead transcription factor FOXO3a controls endothelial cell viability through modulation of the caspase-8 inhibitor FLIP. J Biol Chem 279: 1513-1525, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 1513-1525
    • Skurk, C.1    Maatz, H.2    Kim, H.S.3    Yang, J.4    Abid, M.R.5    Aird, W.C.6    Walsh, K.7
  • 250
    • 77649180164 scopus 로고    scopus 로고
    • Sepsis increases the expression and activity of the transcription factor Forkhead Box O 1 (FOXO1) in skeletal muscle by a glucocorticoiddependent mechanism
    • Smith IJ, Alamdari N, O'Neal P, Gonnella P, Aversa Z, Hasselgren PO. Sepsis increases the expression and activity of the transcription factor Forkhead Box O 1 (FOXO1) in skeletal muscle by a glucocorticoiddependent mechanism. Int J Biochem Cell Biol 42: 701-711, 2010.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 701-711
    • Smith, I.J.1    Alamdari, N.2    O'Neal, P.3    Gonnella, P.4    Aversa, Z.5    Hasselgren, P.O.6
  • 251
    • 0017140415 scopus 로고
    • Spontaneous activity in denervated mouse diaphragm muscle
    • Smith JW, Thesleff S. Spontaneous activity in denervated mouse diaphragm muscle. J Physiol 257: 171-186, 1976.
    • (1976) J Physiol , vol.257 , pp. 171-186
    • Smith, J.W.1    Thesleff, S.2
  • 252
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitinproteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • Solomon V, Goldberg AL. Importance of the ATP-ubiquitinproteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. J Biol Chem 271: 26690-26697, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 255
    • 0001704972 scopus 로고
    • Motoneurons, motor units, and the size principle
    • Rosenberg RN, editor. New York: Churchill Livingstone
    • Stuart DG, Enoka RM. Motoneurons, motor units, and the size principle. In: Rosenberg RN, editor. The Clinical Neurosciences. New York: Churchill Livingstone, 1983, p. 471-517.
    • (1983) The Clinical Neurosciences , pp. 471-517
    • Stuart, D.G.1    Enoka, R.M.2
  • 258
    • 1842339868 scopus 로고    scopus 로고
    • Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
    • Tawa NE, Jr, Odessey R, Goldberg AL. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J Clin Invest 100: 197-203, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 197-203
    • Tawa Jr., N.E.1    Odessey, R.2    Goldberg, A.L.3
  • 259
    • 17144470129 scopus 로고    scopus 로고
    • Changes in myofibrillar protein composition of human diaphragm elicited by congestive heart failure
    • Tikunov BA, Mancini D, Levine S. Changes in myofibrillar protein composition of human diaphragm elicited by congestive heart failure. J Mol Cell Cardiol 28: 2537-2541, 1996.
    • (1996) J Mol Cell Cardiol , vol.28 , pp. 2537-2541
    • Tikunov, B.A.1    Mancini, D.2    Levine, S.3
  • 260
    • 70349253984 scopus 로고    scopus 로고
    • AMP-activated protein kinase enhances the expression of muscle-specific ubiquitin ligases despite its activation of IGF-1/Akt signaling in C2C12 myotubes
    • Tong JF, Yan X, Zhu MJ, Du M. AMP-activated protein kinase enhances the expression of muscle-specific ubiquitin ligases despite its activation of IGF-1/Akt signaling in C2C12 myotubes. J Cell Biochem 108: 458-468, 2009.
    • (2009) J Cell Biochem , vol.108 , pp. 458-468
    • Tong, J.F.1    Yan, X.2    Zhu, M.J.3    Du, M.4
  • 261
    • 0034554838 scopus 로고    scopus 로고
    • The Agrin/Mu SK signaling pathway is spatially segregated from the neuregulin/ErbB receptor signaling pathway at the neuromuscular junction
    • Trinidad JC, Fischbach GD, Cohen JB. The Agrin/Mu SK signaling pathway is spatially segregated from the neuregulin/ErbB receptor signaling pathway at the neuromuscular junction. J Neurosci 20: 8762-8770, 2000.
    • (2000) J Neurosci , vol.20 , pp. 8762-8770
    • Trinidad, J.C.1    Fischbach, G.D.2    Cohen, J.B.3
  • 262
    • 2942726155 scopus 로고    scopus 로고
    • The ins and outs of FoxO shuttling: Mechanisms of FoxO translocation and transcriptional regulation
    • Van Der Heide LP, Hoekman MF, Smidt MP. The ins and outs of FoxO shuttling: Mechanisms of FoxO translocation and transcriptional regulation. Biochem J 380: 297-309, 2004.
    • (2004) Biochem J , vol.380 , pp. 297-309
    • Van Der Heide, L.P.1    Hoekman, M.F.2    Smidt, M.P.3
  • 263
    • 59649104233 scopus 로고    scopus 로고
    • The IkappaB kinases IKKalpha and IKKbeta are necessary and sufficient for skeletal muscle atrophy
    • Van Gammeren D, Damrauer JS, Jackman RW, Kandarian SC. The IkappaB kinases IKKalpha and IKKbeta are necessary and sufficient for skeletal muscle atrophy. FASEB J 23: 362-370, 2009.
    • (2009) FASEB J , vol.23 , pp. 362-370
    • Van Gammeren, D.1    Damrauer, J.S.2    Jackman, R.W.3    Kandarian, S.C.4
  • 268
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco I, Sawyers CL. The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat Rev Cancer 2: 489-501, 2002.
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 269
    • 33749431713 scopus 로고    scopus 로고
    • The mTOR pathway in the control of protein synthesis
    • Wang X, Proud CG. The mTOR pathway in the control of protein synthesis. Physiology (Bethesda) 21: 362-369, 2006.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 362-369
    • Wang, X.1    Proud, C.G.2
  • 270
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz AJ, Flynn A, Proud CG, Cooper JA. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. Embo J 16: 1909-1920, 1997.
    • (1997) Embo J , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 271
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo
    • Waskiewicz AJ, Johnson JC, Penn B, Mahalingam M, Kimball SR, Cooper JA. Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol Cell Biol 19: 1871-1880, 1999.
    • (1999) Mol Cell Biol , vol.19 , pp. 1871-1880
    • Waskiewicz, A.J.1    Johnson, J.C.2    Penn, B.3    Mahalingam, M.4    Kimball, S.R.5    Cooper, J.A.6
  • 272
    • 0032498112 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor eIF2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin
    • Welsh GI, Miller CM, Loughlin AJ, Price NT, Proud CG. Regulation of eukaryotic initiation factor eIF2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett 421: 125-130, 1998.
    • (1998) FEBS Lett , vol.421 , pp. 125-130
    • Welsh, G.I.1    Miller, C.M.2    Loughlin, A.J.3    Price, N.T.4    Proud, C.G.5
  • 273
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • Welsh GI, Proud CG. Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem J 294(Pt 3): 625-629, 1993.
    • (1993) Biochem J , vol.294 , Issue.PART 3 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 274
    • 0029736744 scopus 로고    scopus 로고
    • Isometric force and maximal shortening velocity of single muscle fibers from elite master runners
    • Widrick JJ, Trappe SW, Blaser CA, Costill DL, Fitts RH. Isometric force and maximal shortening velocity of single muscle fibers from elite master runners. Am J Physiol 271: c666-c675, 1996.
    • (1996) Am J Physiol , vol.271
    • Widrick, J.J.1    Trappe, S.W.2    Blaser, C.A.3    Costill, D.L.4    Fitts, R.H.5
  • 275
    • 33745836687 scopus 로고    scopus 로고
    • Time course changes in signaling pathways and protein synthesis in C2C12 myotubes following AMPK activation by AICAR
    • Williamson DL, Bolster DR, Kimball SR, Jefferson LS. Time course changes in signaling pathways and protein synthesis in C2C12 myotubes following AMPK activation by AICAR. Am J Physiol Endocrinol Metab 291: E80-E89, 2006.
    • (2006) Am J Physiol Endocrinol Metab , vol.291
    • Williamson, D.L.1    Bolster, D.R.2    Kimball, S.R.3    Jefferson, L.S.4
  • 276
    • 33750320417 scopus 로고    scopus 로고
    • The skeletal muscle satellite cell: The stem cell that came in from the cold
    • Zammit PS, Partridge TA, Yablonka-Reuveni Z. The skeletal muscle satellite cell: The stem cell that came in from the cold. J Histochem Cytochem 54: 1177-1191, 2006.
    • (2006) J Histochem Cytochem , vol.54 , pp. 1177-1191
    • Zammit, P.S.1    Partridge, T.A.2    Yablonka-Reuveni, Z.3
  • 277
    • 0021816236 scopus 로고
    • Membrane electrical properties and prediction of motor-unit type of medial gastrocnemius motoneurons in the cat
    • Zengel JE, Reid SA, Sypert GW, Munson JB. Membrane electrical properties and prediction of motor-unit type of medial gastrocnemius motoneurons in the cat. J Neurophysiol 53(5): 1323-1344, 1985.
    • (1985) J Neurophysiol , vol.53 , Issue.5 , pp. 1323-1344
    • Zengel, J.E.1    Reid, S.A.2    Sypert, G.W.3    Munson, J.B.4
  • 279
    • 0030900652 scopus 로고    scopus 로고
    • Metabolic and phenotypic adaptations of diaphragm muscle fiberswith inactivation
    • Zhan WZ, Miyata H, Prakash YS, Sieck GC. Metabolic and phenotypic adaptations of diaphragm muscle fiberswith inactivation. JAppl Physiol 82: 1145-1153, 1997.
    • (1997) JAppl Physiol , vol.82 , pp. 1145-1153
    • Zhan, W.Z.1    Miyata, H.2    Prakash, Y.S.3    Sieck, G.C.4
  • 280
    • 0026598072 scopus 로고
    • Adaptations of diaphragm and medial gastrocnemius muscles to inactivity
    • Zhan WZ, Sieck GC. Adaptations of diaphragm and medial gastrocnemius muscles to inactivity. J Appl Physiol 72: 1445-1453, 1992.
    • (1992) J Appl Physiol , vol.72 , pp. 1445-1453
    • Zhan, W.Z.1    Sieck, G.C.2
  • 281
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao J, Brault JJ, Schild A, Cao P, Sandri M, Schiaffino S, Lecker SH, Goldberg AL. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 6: 472-483, 2007.
    • (2007) Cell Metab , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6    Lecker, S.H.7    Goldberg, A.L.8
  • 282
    • 29544442617 scopus 로고    scopus 로고
    • Effects of inactivity on fiber size and myonuclear number in rat soleus muscle
    • Zhong H, Roy RR, Siengthai B, Edgerton VR. Effects of inactivity on fiber size and myonuclear number in rat soleus muscle. J Appl Physiol 99: 1494-1499, 2005.
    • (2005) J Appl Physiol , vol.99 , pp. 1494-1499
    • Zhong, H.1    Roy, R.R.2    Siengthai, B.3    Edgerton, V.R.4
  • 283
    • 0028971642 scopus 로고
    • Neuregulin receptors, erbB3 and erbB4, are localized at neuromuscular synapses
    • Zhu X, Lai C, Thomas S, Burden SJ. Neuregulin receptors, erbB3 and erbB4, are localized at neuromuscular synapses. EMBO J 14: 5842-5848, 1995.
    • (1995) EMBO J , vol.14 , pp. 5842-5848
    • Zhu, X.1    Lai, C.2    Thomas, S.3    Burden, S.J.4


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