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Volumn 23, Issue 5, 2000, Pages 661-679

Myosin heavy chain isoform expression following reduced neuromuscular activity: Potential regulatory mechanisms

Author keywords

Calcineurin; Hindlimb unloading; Limb immobilization; MyoD; Myogenin; Spaceflight; Spinal cord injury; Spinal cord transection; Tetrodotoxin

Indexed keywords

CALCINEURIN; CALCIUM; CYCLOSPORIN; DNA; HELIX LOOP HELIX PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN; MESSENGER RNA; MYOGENIN; MYOSIN HEAVY CHAIN; PROTEIN; TACROLIMUS; TETRODOTOXIN;

EID: 0034019038     PISSN: 0148639X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4598(200005)23:5<661::AID-MUS3>3.0.CO;2-J     Document Type: Review
Times cited : (236)

References (159)
  • 1
    • 0031694618 scopus 로고    scopus 로고
    • Activation and cellular localization of the cyclosporine A-sensitive transcription factor NF-AT in skeletal muscle cells
    • Abbot KL, Friday BB, Thaloor D, Murphy TJ, Pavlath GK. Activation and cellular localization of the cyclosporine A-sensitive transcription factor NF-AT in skeletal muscle cells. Mol Biol Cell 1998;9:2905-2916.
    • (1998) Mol Biol Cell , vol.9 , pp. 2905-2916
    • Abbot, K.L.1    Friday, B.B.2    Thaloor, D.3    Murphy, T.J.4    Pavlath, G.K.5
  • 2
    • 0027457083 scopus 로고
    • Skeletal muscle myosin heavy chain composition and resistance training
    • Adams GR, Hather BM, Baldwin KM, Dudley GA. Skeletal muscle myosin heavy chain composition and resistance training. J Appl Physiol 1993;74:911-915.
    • (1993) J Appl Physiol , vol.74 , pp. 911-915
    • Adams, G.R.1    Hather, B.M.2    Baldwin, K.M.3    Dudley, G.A.4
  • 3
    • 0021261014 scopus 로고
    • EMG activity of slow and fast ankle extensors following spinal cord transection
    • Alaimo MA, Smith JL, Roy RR, Edgerton VR. EMG activity of slow and fast ankle extensors following spinal cord transection. J Appl Physiol 1984;56:1608-1613.
    • (1984) J Appl Physiol , vol.56 , pp. 1608-1613
    • Alaimo, M.A.1    Smith, J.L.2    Roy, R.R.3    Edgerton, V.R.4
  • 4
    • 0023179135 scopus 로고
    • Electromyography of rat soleus, medial gastrocnemius, and tibialis anterior during hind limb suspension
    • Alford EK, Roy RR, Hodgson JA, Edgerton VR. Electromyography of rat soleus, medial gastrocnemius, and tibialis anterior during hind limb suspension. Exp Neurol 1987;96: 635-649.
    • (1987) Exp Neurol , vol.96 , pp. 635-649
    • Alford, E.K.1    Roy, R.R.2    Hodgson, J.A.3    Edgerton, V.R.4
  • 7
    • 0029878972 scopus 로고    scopus 로고
    • Myosin heavy chain isoform tranformation in single fibres from m. vastus lateralis in spinal cord injured individuals: Effects of long-term functional electrical stimulation
    • Andersen JL, Mohr T, Biering-Sorenson F, Galbo H, Kjaer M. Myosin heavy chain isoform tranformation in single fibres from m. vastus lateralis in spinal cord injured individuals: effects of long-term functional electrical stimulation. Pflügers Arch 1996;431:513-518.
    • (1996) Pflügers Arch , vol.431 , pp. 513-518
    • Andersen, J.L.1    Mohr, T.2    Biering-Sorenson, F.3    Galbo, H.4    Kjaer, M.5
  • 10
    • 0023820311 scopus 로고
    • Three fast myosin heavy chains in adult rat skeletal muscle
    • Bär A, Pette D. Three fast myosin heavy chains in adult rat skeletal muscle. FEBS Lett 1988;235:153-155.
    • (1988) FEBS Lett , vol.235 , pp. 153-155
    • Bär, A.1    Pette, D.2
  • 12
    • 0025727193 scopus 로고
    • Effects of lower limb unloading on skeletal muscle mass and function in humans
    • Berg HE, Dudley GA, Haggmark T, Ohlsen H, Tesch PA. Effects of lower limb unloading on skeletal muscle mass and function in humans. J Appl Physiol 1991;70:1882-1885.
    • (1991) J Appl Physiol , vol.70 , pp. 1882-1885
    • Berg, H.E.1    Dudley, G.A.2    Haggmark, T.3    Ohlsen, H.4    Tesch, P.A.5
  • 13
    • 0027250891 scopus 로고
    • Work capacity and metabolic and morphologic characteristics of the human quadriceps muscle in response to unloading
    • Berg HE, Dudley GA, Hather B, Tesch PA. Work capacity and metabolic and morphologic characteristics of the human quadriceps muscle in response to unloading. Clin Physiol 1993;13:337-347.
    • (1993) Clin Physiol , vol.13 , pp. 337-347
    • Berg, H.E.1    Dudley, G.A.2    Hather, B.3    Tesch, P.A.4
  • 15
    • 0025572707 scopus 로고
    • Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection
    • Blackwell TK, Weintraub H. Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection. Science 1990;250: 1104-1110.
    • (1990) Science , vol.250 , pp. 1104-1110
    • Blackwell, T.K.1    Weintraub, H.2
  • 16
    • 0027285581 scopus 로고
    • Quantitative EMG analysis in soleus and plantaris during hindlimb suspension and recovery
    • Blewett C, Elder GCB. Quantitative EMG analysis in soleus and plantaris during hindlimb suspension and recovery. J Appl Physiol 1993;74:2057-2066.
    • (1993) J Appl Physiol , vol.74 , pp. 2057-2066
    • Blewett, C.1    Elder, G.C.B.2
  • 18
    • 0025782887 scopus 로고
    • Molecular and cellular adaptation of muscle in response to exercise: Perspectives of various models
    • Booth FW, Thomason DB. Molecular and cellular adaptation of muscle in response to exercise: perspectives of various models. Physiol Rev 1991;71:541-585.
    • (1991) Physiol Rev , vol.71 , pp. 541-585
    • Booth, F.W.1    Thomason, D.B.2
  • 19
    • 0028048536 scopus 로고
    • Maximum shortening velocity and coexistence of myosin heavy chain isoforms in single skinned fast fibres of rat skeletal muscle
    • Bottinelli R, Betto R, Schiaffino S, Reggiani C. Maximum shortening velocity and coexistence of myosin heavy chain isoforms in single skinned fast fibres of rat skeletal muscle. J Muscle Res Cell Motil 1994;15:413-419.
    • (1994) J Muscle Res Cell Motil , vol.15 , pp. 413-419
    • Bottinelli, R.1    Betto, R.2    Schiaffino, S.3    Reggiani, C.4
  • 20
    • 0028132899 scopus 로고
    • Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres
    • Bottinelli R, Betto R, Schiaffino S, Reggiani C. Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres. J Physiol (Lond) 1994;478:341-349.
    • (1994) J Physiol (Lond) , vol.478 , pp. 341-349
    • Bottinelli, R.1    Betto, R.2    Schiaffino, S.3    Reggiani, C.4
  • 21
    • 0025857245 scopus 로고
    • Force-velocity relations and myosin heavy chain isoform compositions of skinned fibres from rat skeletal muscle
    • Bottinelli R, Schiaffino S, Reggiani C. Force-velocity relations and myosin heavy chain isoform compositions of skinned fibres from rat skeletal muscle. J Physiol (Lond) 1991;437:655-672.
    • (1991) J Physiol (Lond) , vol.437 , pp. 655-672
    • Bottinelli, R.1    Schiaffino, S.2    Reggiani, C.3
  • 23
    • 72849170594 scopus 로고
    • Differentiation of fast and slow muscles in the cat hind limb
    • Buller AJ, Eccles JC, Eccles RM. Differentiation of fast and slow muscles in the cat hind limb. J Physiol (Lond) 1960;150: 399-416.
    • (1960) J Physiol (Lond) , vol.150 , pp. 399-416
    • Buller, A.J.1    Eccles, J.C.2    Eccles, R.M.3
  • 24
    • 72849173018 scopus 로고
    • Interactions between motoneurones and muscles in respect of the characteristic speeds of their responses
    • Buller AJ, Eccles JC, Eccles RM. Interactions between motoneurones and muscles in respect of the characteristic speeds of their responses. J Physiol (Lond) 1960;150:417-439
    • (1960) J Physiol (Lond) , vol.150 , pp. 417-439
    • Buller, A.J.1    Eccles, J.C.2    Eccles, R.M.3
  • 26
    • 0031736361 scopus 로고    scopus 로고
    • Novel transitions in MHC isoforms: Separate and combined effects of thyroid hormone and mechanical unloading
    • Caiozzo VJ, Baker MJ, Baldwin KM. Novel transitions in MHC isoforms: separate and combined effects of thyroid hormone and mechanical unloading. J Appl Physiol 1998; 85:2237-2248.
    • (1998) J Appl Physiol , vol.85 , pp. 2237-2248
    • Caiozzo, V.J.1    Baker, M.J.2    Baldwin, K.M.3
  • 27
    • 0028281614 scopus 로고
    • Effect of spaceflight on skeletal muscle: Mechanical properties and myosin isoform content of a slow muscle
    • Caiozzo VJ, Baker MJ, Herrick RE, Tao M, Baldwin KM. Effect of spaceflight on skeletal muscle: mechanical properties and myosin isoform content of a slow muscle. J Appl Physiol 1994;76:1764-1773.
    • (1994) J Appl Physiol , vol.76 , pp. 1764-1773
    • Caiozzo, V.J.1    Baker, M.J.2    Herrick, R.E.3    Tao, M.4    Baldwin, K.M.5
  • 28
    • 0030766580 scopus 로고    scopus 로고
    • Single-fiber and whole muscle analyses of MHC isoform plasticity: Interaction between T3 and unloading
    • Caiozzo VJ, Baker MJ, McCue SA, Baldwin KM. Single-fiber and whole muscle analyses of MHC isoform plasticity: interaction between T3 and unloading. Am J Physiol 1997;273: C944-C952.
    • (1997) Am J Physiol , vol.273
    • Caiozzo, V.J.1    Baker, M.J.2    McCue, S.A.3    Baldwin, K.M.4
  • 29
    • 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 KM. Microgravity-induced transformations of myosin isoforms and contractile properties of skeletal muscle. J Appl Physiol 1996;81:123-132.
    • (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.6
  • 30
    • 0032909168 scopus 로고    scopus 로고
    • Fiber-type-specific transcription of the troponin I slow gene is regulated by multiple elements
    • Calvo S, Venepally P, Cheng J, Buonanno A. Fiber-type-specific transcription of the troponin I slow gene is regulated by multiple elements. Mol Cell Biol 1999;19:515-525.
    • (1999) Mol Cell Biol , vol.19 , pp. 515-525
    • Calvo, S.1    Venepally, P.2    Cheng, J.3    Buonanno, A.4
  • 32
    • 0029984552 scopus 로고    scopus 로고
    • 2+] in the development of low frequency fatigue in mouse single muscle fibres
    • 2+] in the development of low frequency fatigue in mouse single muscle fibres. J Physiol (Lond) 1996;491: 813-824.
    • (1996) J Physiol (Lond) , vol.491 , pp. 813-824
    • Chin, E.R.1    Allen, D.G.2
  • 34
    • 0345095249 scopus 로고
    • Neural cell adhesion molecule (N-CAM) accumulates in denervated and paralyzed skeletal muscles
    • Covault J, Sanes JR. Neural cell adhesion molecule (N-CAM) accumulates in denervated and paralyzed skeletal muscles. Proc Natl Acad Sci USA 1985;82:4544-4548.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4544-4548
    • Covault, J.1    Sanes, J.R.2
  • 35
    • 0033525748 scopus 로고    scopus 로고
    • 2+, calcineurin, and NF-AT
    • 2+, calcineurin, and NF-AT. Cell 1999;96: 611-614.
    • (1999) Cell , vol.96 , pp. 611-614
    • Crabtree, G.R.1
  • 36
    • 0033618462 scopus 로고    scopus 로고
    • Calcineurin is required for skeletal muscle hypertrophy
    • Dunn SE, Burns JL, Michel RN. Calcineurin is required for skeletal muscle hypertrophy. J Biol Chem 1999;274: 21908-21912.
    • (1999) J Biol Chem , vol.274 , pp. 21908-21912
    • Dunn, S.E.1    Burns, J.L.2    Michel, R.N.3
  • 37
    • 0032934716 scopus 로고    scopus 로고
    • Differential sensitivity of myosin-heavy-chain-type fibers to distinct aggregates of nerve-mediated activation
    • Dunn SE, Michel RN. Differential sensitivity of myosin-heavy-chain-type fibers to distinct aggregates of nerve-mediated activation. Pflügers Arch 1999;437:432-440.
    • (1999) Pflügers Arch , vol.437 , pp. 432-440
    • Dunn, S.E.1    Michel, R.N.2
  • 38
    • 0031751810 scopus 로고    scopus 로고
    • Early changes in muscle fiber size and gene expression in response to spinal cord transection and exercise
    • Dupont-Versteegden EE, Houle JD, Gurley CM, Peterson CA. Early changes in muscle fiber size and gene expression in response to spinal cord transection and exercise. Am J Physiol 1998;275:C1124-C1133.
    • (1998) Am J Physiol , vol.275
    • Dupont-Versteegden, E.E.1    Houle, J.D.2    Gurley, C.M.3    Peterson, C.A.4
  • 40
    • 0000397679 scopus 로고    scopus 로고
    • Neuromuscular adaptations to actual and simulated spaceflight
    • Fregly MJ, Blatteis CM, editors. New York: Oxford University Press
    • Edgerton VR, Roy RR. Neuromuscular adaptations to actual and simulated spaceflight. In: Fregly MJ, Blatteis CM, editors. Handbook of physiology - section 4: environmental physiology. Vol I. New York: Oxford University Press; 1996. p 721-763.
    • (1996) Handbook of Physiology - Section 4: Environmental Physiology , vol.1 , pp. 721-763
    • Edgerton, V.R.1    Roy, R.R.2
  • 42
    • 0025976936 scopus 로고
    • Myogenin and MyoD join a family of skeletal muscle genes regulated by electrical activity
    • Eftimie R, Brenner HR, Buonanno A. Myogenin and MyoD join a family of skeletal muscle genes regulated by electrical activity. Proc Natl Acad Sci USA 1991;88:1349-1353.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1349-1353
    • Eftimie, R.1    Brenner, H.R.2    Buonanno, A.3
  • 43
    • 0023266382 scopus 로고
    • Development of rat muscle during short-and long-term hindlimb suspension
    • Elder GCB, McComas AJ. Development of rat muscle during short-and long-term hindlimb suspension. J Appl Physiol 1987;62:1917-1923.
    • (1987) J Appl Physiol , vol.62 , pp. 1917-1923
    • Elder, G.C.B.1    McComas, A.J.2
  • 44
    • 0021345766 scopus 로고
    • Lumbosacral spinal isolation in cat: Surgical preparation and health maintenance
    • Eldridge L. Lumbosacral spinal isolation in cat: surgical preparation and health maintenance. Exp Neurol 1984;83: 318-327.
    • (1984) Exp Neurol , vol.83 , pp. 318-327
    • Eldridge, L.1
  • 45
    • 0019391116 scopus 로고
    • Alterations in cat skeletal neuromuscular junctions following prolonged inactivity
    • Eldridge L, Liebhold M, Steinbach JH. Alterations in cat skeletal neuromuscular junctions following prolonged inactivity. J Physiol (Lond) 1981;313:529-545.
    • (1981) J Physiol (Lond) , vol.313 , pp. 529-545
    • Eldridge, L.1    Liebhold, M.2    Steinbach, J.H.3
  • 47
    • 0028940809 scopus 로고
    • Sensitive detection of myosin heavy chain composition in skeletal muscle under different loading conditions
    • Fauteck SP, Kandarian SC. Sensitive detection of myosin heavy chain composition in skeletal muscle under different loading conditions. Am J Physiol 1995;268:C419-C424.
    • (1995) Am J Physiol , vol.268
    • Fauteck, S.P.1    Kandarian, S.C.2
  • 49
    • 0022476925 scopus 로고
    • Models of disuse: A comparison of hindlimb suspension and immobilization
    • Fitts RH, Metzger JM, Riley DA, Unsworth BR. Models of disuse: a comparison of hindlimb suspension and immobilization. J Appl Physiol 1986;60:1946-1953.
    • (1986) J Appl Physiol , vol.60 , pp. 1946-1953
    • Fitts, R.H.1    Metzger, J.M.2    Riley, D.A.3    Unsworth, B.R.4
  • 51
    • 0027964949 scopus 로고
    • Stretch activation, unloaded shortening velocity, and myosin heavy chain isoforms of rat skeletal muscle fibres
    • Galler S, Schmitt TL, Pette D. Stretch activation, unloaded shortening velocity, and myosin heavy chain isoforms of rat skeletal muscle fibres. J Physiol (Lond) 1994;478:513-521.
    • (1994) J Physiol (Lond) , vol.478 , pp. 513-521
    • Galler, S.1    Schmitt, T.L.2    Pette, D.3
  • 52
    • 0024392879 scopus 로고
    • Contractile function of single muscle fibers after hindlimb suspension
    • Gardetto PR, Schluter JM, Fitts RH. Contractile function of single muscle fibers after hindlimb suspension. J Appl Physiol 1989;66:2739-2749.
    • (1989) J Appl Physiol , vol.66 , pp. 2739-2749
    • Gardetto, P.R.1    Schluter, J.M.2    Fitts, R.H.3
  • 53
    • 0029745782 scopus 로고    scopus 로고
    • Effects of exercise and insulin on mitogen-activated protein kinase signaling pathways in rat skeletal muscle
    • Goodyear LJ, Chang PY, Sherwood DJ, Dufresne SD, Moller DE. Effects of exercise and insulin on mitogen-activated protein kinase signaling pathways in rat skeletal muscle. Am J Physiol 1996;271:E403-E408.
    • (1996) Am J Physiol , vol.271
    • Goodyear, L.J.1    Chang, P.Y.2    Sherwood, D.J.3    Dufresne, S.D.4    Moller, D.E.5
  • 54
    • 0025057473 scopus 로고
    • Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical ATPase and anti-myosin monoclonal antibodies
    • Gorza L. Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical ATPase and anti-myosin monoclonal antibodies. J Histochem Cytochem 1990;38:257-265.
    • (1990) J Histochem Cytochem , vol.38 , pp. 257-265
    • Gorza, L.1
  • 57
    • 0031905779 scopus 로고    scopus 로고
    • Effects of inactivity on myosin heavy chain composition and size of rat soleus fibers
    • Grossman EJ, Roy RR, Talmadge RJ, Zhong H, Edgerton VR. Effects of inactivity on myosin heavy chain composition and size of rat soleus fibers. Muscle Nerve 1998;21:375-389.
    • (1998) Muscle Nerve , vol.21 , pp. 375-389
    • Grossman, E.J.1    Roy, R.R.2    Talmadge, R.J.3    Zhong, H.4    Edgerton, V.R.5
  • 58
    • 0023686571 scopus 로고
    • Characterization of aretylcholine receptor subunits in developing and in denervated mammalian muscle
    • Gu Y, Hall ZW. Characterization of aretylcholine receptor subunits in developing and in denervated mammalian muscle. J Biol Chem 1988;263:12878-12885.
    • (1988) J Biol Chem , vol.263 , pp. 12878-12885
    • Gu, Y.1    Hall, Z.W.2
  • 59
    • 0031766017 scopus 로고    scopus 로고
    • Interaction of hyperthyroidism and hindlimb suspension on skeletal myosin heavy chain expression
    • Haddad F, Qin AX, Zeng M, McCue SA, Baldwin KM. Interaction of hyperthyroidism and hindlimb suspension on skeletal myosin heavy chain expression. J Appl Physiol 1998;85: 2227-2236.
    • (1998) J Appl Physiol , vol.85 , pp. 2227-2236
    • Haddad, F.1    Qin, A.X.2    Zeng, M.3    McCue, S.A.4    Baldwin, K.M.5
  • 61
    • 0026589341 scopus 로고
    • Skeletal muscle responses to lower limb suspension in humans
    • Hather BM, Adams GR, Tesch PA, Dudley GA. Skeletal muscle responses to lower limb suspension in humans. J Appl Physiol 1992;72:1493-1498.
    • (1992) J Appl Physiol , vol.72 , pp. 1493-1498
    • Hather, B.M.1    Adams, G.R.2    Tesch, P.A.3    Dudley, G.A.4
  • 62
    • 0024327076 scopus 로고
    • Structural and metabolic characteristics of human skeletal muscle following 30 days of simulated microgravity
    • Hikida RS, Gollnick PD, Dudley GA, Convertino VA, Buchanan P. Structural and metabolic characteristics of human skeletal muscle following 30 days of simulated microgravity. Aviat Space Environ Med 1989;60:664-670.
    • (1989) Aviat Space Environ Med , vol.60 , pp. 664-670
    • Hikida, R.S.1    Gollnick, P.D.2    Dudley, G.A.3    Convertino, V.A.4    Buchanan, P.5
  • 63
    • 0030817893 scopus 로고    scopus 로고
    • Mechanical properties and myosin heavy chain isoform composition of skinned skeletal muscle fibres from a human biopsy sample
    • Hilber K, Galler S. Mechanical properties and myosin heavy chain isoform composition of skinned skeletal muscle fibres from a human biopsy sample. Pflügers Arch 1997;434: 551-558.
    • (1997) Pflügers Arch , vol.434 , pp. 551-558
    • Hilber, K.1    Galler, S.2
  • 64
    • 0005523854 scopus 로고
    • Slow myosin heavy chains in cat jaw and limb muscles are phenotypically distinct: Expression of jaw-specific slow myosin phenotype in regenerated and chronically stimulated jaw muscles
    • Hoh JFY, Hughes S, Walker ML, Kang LDH, Everett AW. Slow myosin heavy chains in cat jaw and limb muscles are phenotypically distinct: expression of jaw-specific slow myosin phenotype in regenerated and chronically stimulated jaw muscles. Basic Appl Myol 1991;1:285-294.
    • (1991) Basic Appl Myol , vol.1 , pp. 285-294
    • Hoh, J.F.Y.1    Hughes, S.2    Walker, M.L.3    Kang, L.D.H.4    Everett, A.W.5
  • 65
    • 0031739360 scopus 로고    scopus 로고
    • Kip1, and cell cycle progression in human capillary endothelial cells by cell shape and cytoskeletal tension
    • Kip1, and cell cycle progression in human capillary endothelial cells by cell shape and cytoskeletal tension. Mol Biol Cell 1998;9:3179-3193.
    • (1998) Mol Biol Cell , vol.9 , pp. 3179-3193
    • Huang, S.1    Chen, C.S.2    Higher, D.E.3
  • 66
    • 0033519274 scopus 로고    scopus 로고
    • Myogenin induces a shift of enzyme activity from glycolytic to oxidative metabolism in muscle of transgenic mice
    • Hughes SM, Chi MM-Y, Lowry OH, Gundersen K. Myogenin induces a shift of enzyme activity from glycolytic to oxidative metabolism in muscle of transgenic mice. J Cell Biol 1999; 145:633-642.
    • (1999) J Cell Biol , vol.145 , pp. 633-642
    • Hughes, S.M.1    Chi, M.M.-Y.2    Lowry, O.H.3    Gundersen, K.4
  • 68
    • 0031044477 scopus 로고    scopus 로고
    • Myod protein is differentially accumulated in fast and slow skeletal muscle fibres and required for normal fibre type balance in rodents
    • Hughes SM, Koishi K, Rudnicki M, Maggs AM. MyoD protein is differentially accumulated in fast and slow skeletal muscle fibres and required for normal fibre type balance in rodents. Mech Dev 1997;61:151-163.
    • (1997) Mech Dev , vol.61 , pp. 151-163
    • Hughes, S.M.1    Koishi, K.2    Rudnicki, M.3    Maggs, A.M.4
  • 69
    • 0027327708 scopus 로고
    • Selective accumulation of MyoD and myogenin mRNAs in fast and slow adult skeletal muscle is controlled by innervation and hormones
    • Hughes SM, Taylor JM, Tapscott SJ, Gurley CM, Carter WJ, Peterson CA. Selective accumulation of MyoD and myogenin mRNAs in fast and slow adult skeletal muscle is controlled by innervation and hormones. Development 1993;118: 1137-1147.
    • (1993) Development , vol.118 , pp. 1137-1147
    • Hughes, S.M.1    Taylor, J.M.2    Tapscott, S.J.3    Gurley, C.M.4    Carter, W.J.5    Peterson, C.A.6
  • 70
    • 0030898325 scopus 로고    scopus 로고
    • Myosin heavy chain mRNA transform to faster isotorms in immobilized skeletal muscle: A quantitative PCR study
    • Jänkälä H, Harjola V-P, Petersen NE, Härkönen. Myosin heavy chain mRNA transform to faster isotorms in immobilized skeletal muscle: a quantitative PCR study. J Appl Physiol 1997;82:977-982.
    • (1997) J Appl Physiol , vol.82 , pp. 977-982
    • Jänkälä, H.1    Harjola, V.-P.2    Petersen, N.E.3
  • 71
    • 0025184075 scopus 로고
    • Expression of a fast fiber enzyme profile in the cat soleus after spinalization
    • Jiang B, Roy RR, Edgerton VR. Expression of a fast fiber enzyme profile in the cat soleus after spinalization. Muscle Nerve 1990;13:1037-1049.
    • (1990) Muscle Nerve , vol.13 , pp. 1037-1049
    • Jiang, B.1    Roy, R.R.2    Edgerton, V.R.3
  • 72
    • 0027411665 scopus 로고
    • Absence of a growth hormone effect on rat soleus atrophy during a 4-day spaceflight
    • Jiang B, Roy RR, Navarro C, Edgerton VR. Absence of a growth hormone effect on rat soleus atrophy during a 4-day spaceflight. J Appl Physiol 1993;74:527-531.
    • (1993) J Appl Physiol , vol.74 , pp. 527-531
    • Jiang, B.1    Roy, R.R.2    Navarro, C.3    Edgerton, V.R.4
  • 73
    • 0031824933 scopus 로고    scopus 로고
    • Quantification of myosin heavy chain mRNA in somatic and branchial arch muscles using competitive PCR
    • Jung HH, Leiber RL, Ryan AF. Quantification of myosin heavy chain mRNA in somatic and branchial arch muscles using competitive PCR. Am J Physiol 1998;275:C68-C74.
    • (1998) Am J Physiol , vol.275
    • Jung, H.H.1    Leiber, R.L.2    Ryan, A.F.3
  • 75
    • 0026600379 scopus 로고
    • Expression of type-specific MHC isoforms in rat intrafusal fibers
    • Kucera J, Walro JM, Gorza L. Expression of type-specific MHC isoforms in rat intrafusal fibers. J Histochem Cytochem 1992;40:293-307.
    • (1992) J Histochem Cytochem , vol.40 , pp. 293-307
    • Kucera, J.1    Walro, J.M.2    Gorza, L.3
  • 76
    • 0023351233 scopus 로고
    • Contractile properties and myosin isoenzymes of various kinds of Xenopus twitch muscle fibres
    • Lannergren J. Contractile properties and myosin isoenzymes of various kinds of Xenopus twitch muscle fibres. J Muscle Res Cell Motil 1987;8:260-273.
    • (1987) J Muscle Res Cell Motil , vol.8 , pp. 260-273
    • Lannergren, J.1
  • 77
    • 0027763495 scopus 로고
    • Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles
    • Larsson L, Moss RL. Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles. J Physiol (Lond) 1993;472:595-614.
    • (1993) J Physiol (Lond) , vol.472 , pp. 595-614
    • Larsson, L.1    Moss, R.L.2
  • 78
    • 0031080922 scopus 로고    scopus 로고
    • Mistl: A novel basic helix-loop-helix transcription factor exhibits a developmentally regulated expression pattern
    • Lemercier C, To RQ, Swanson BJ, Lyons GE, Konieczny SF. Mistl: a novel basic helix-loop-helix transcription factor exhibits a developmentally regulated expression pattern. Dev Biol 1997;182:101-113.
    • (1997) Dev Biol , vol.182 , pp. 101-113
    • Lemercier, C.1    To, R.Q.2    Swanson, B.J.3    Lyons, G.E.4    Konieczny, S.F.5
  • 79
    • 0031755734 scopus 로고    scopus 로고
    • EMG activity of three rat hindlimb muscles during microgravity and hypergravity phase of parabolic flight
    • Leterme D, Falempin M. EMG activity of three rat hindlimb muscles during microgravity and hypergravity phase of parabolic flight. Aviat Space Environ Med 1998;69:1065-1079.
    • (1998) Aviat Space Environ Med , vol.69 , pp. 1065-1079
    • Leterme, D.1    Falempin, M.2
  • 80
    • 0025806595 scopus 로고
    • Morphometric and neurophysiological analysis of skeletal muscle in paraplegic patients with traumatic cord lesion
    • Lotta S, Scelsi R, Alfonsi E, Saitta A, Nicolotti D, Epifani P, Carraro U. Morphometric and neurophysiological analysis of skeletal muscle in paraplegic patients with traumatic cord lesion. Paraplegia 1991;29:247-252.
    • (1991) Paraplegia , vol.29 , pp. 247-252
    • Lotta, S.1    Scelsi, R.2    Alfonsi, E.3    Saitta, A.4    Nicolotti, D.5    Epifani, P.6    Carraro, U.7
  • 81
    • 0025356677 scopus 로고
    • Disuse and passive stretch cause rapid alterations in expression of developmental and adult contractile protein genes in skeletal muscle
    • Loughna PT, Izumo S, Goldspink G, Nadal-Ginard B. Disuse and passive stretch cause rapid alterations in expression of developmental and adult contractile protein genes in skeletal muscle. Development 1990;109:217-223.
    • (1990) Development , vol.109 , pp. 217-223
    • Loughna, P.T.1    Izumo, S.2    Goldspink, G.3    Nadal-Ginard, B.4
  • 82
    • 13044258437 scopus 로고    scopus 로고
    • MyoR: A muscle-restricted basic helix-loop-helix transcription factor that anlagonizes the actions of MyoD
    • Lu J, Webb R, Richardson JA, Olson EN. MyoR: a muscle-restricted basic helix-loop-helix transcription factor that anlagonizes the actions of MyoD. Proc Natl Acad Sci USA 1999; 96:552-557.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 552-557
    • Lu, J.1    Webb, R.2    Richardson, J.A.3    Olson, E.N.4
  • 83
    • 0029091166 scopus 로고
    • Expression of extraocular inyosin heavy chain in rabbit laryngeal muscle
    • Lucas CA, Rughani A, Hoh JFY. Expression of extraocular inyosin heavy chain in rabbit laryngeal muscle. J Muscle Res Cell Motil 1995;16:368-378.
    • (1995) J Muscle Res Cell Motil , vol.16 , pp. 368-378
    • Lucas, C.A.1    Rughani, A.2    Hoh, J.F.Y.3
  • 84
    • 0033609812 scopus 로고    scopus 로고
    • Insulin and exercise decrease glycogen synthase kinase-3 activity by different mechanisms in rat skeletal muscle
    • Markuns JF, Wojtascewski JFP, Goodyear LJ. Insulin and exercise decrease glycogen synthase kinase-3 activity by different mechanisms in rat skeletal muscle. J Biol Chem 1999; 274:24896-24900.
    • (1999) J Biol Chem , vol.274 , pp. 24896-24900
    • Markuns, J.F.1    Wojtascewski, J.F.P.2    Goodyear, L.J.3
  • 85
    • 0026575960 scopus 로고
    • Influence of electrical stimulation on the morphological and metabolic properties of paralyzed muscle
    • Martin TP, Stein RB, Hoeppner PH, Reid DC. Influence of electrical stimulation on the morphological and metabolic properties of paralyzed muscle. J Appl Physiol 1992;72: 1401-1406.
    • (1992) J Appl Physiol , vol.72 , pp. 1401-1406
    • Martin, T.P.1    Stein, R.B.2    Hoeppner, P.H.3    Reid, D.C.4
  • 86
    • 0031003277 scopus 로고    scopus 로고
    • Beta-MHC transgene expression in suspended and mechanically overloaded/suspended soleus muscle of transgenic mice
    • McCarthy JJ, Fox AM, Tsika GL, Gao L, Tsika RW. Beta-MHC transgene expression in suspended and mechanically overloaded/suspended soleus muscle of transgenic mice. Am J Physiol 1997;272:R1552-R1561.
    • (1997) Am J Physiol , vol.272
    • McCarthy, J.J.1    Fox, A.M.2    Tsika, G.L.3    Gao, L.4    Tsika, R.W.5
  • 87
    • 0033553414 scopus 로고    scopus 로고
    • Segregated regulatory elements direct β-myosin heavy chain expression in response to altered muscle activity
    • McCarthy JJ, Vyas DR, Tsika GL, Tsika RW. Segregated regulatory elements direct β-myosin heavy chain expression in response to altered muscle activity. J Biol Chem 1999;274: 14270-14279.
    • (1999) J Biol Chem , vol.274 , pp. 14270-14279
    • McCarthy, J.J.1    Vyas, D.R.2    Tsika, G.L.3    Tsika, R.W.4
  • 88
    • 0027997832 scopus 로고
    • Force-velocity and power characteristics of rat soleus muscle fibers after hindlimb suspension
    • McDonald KS, Blaser CA, Fitts RH. Force-velocity and power characteristics of rat soleus muscle fibers after hindlimb suspension. J Appl Physiol 1994;77:1609-1616.
    • (1994) J Appl Physiol , vol.77 , pp. 1609-1616
    • McDonald, K.S.1    Blaser, C.A.2    Fitts, R.H.3
  • 89
    • 0027213241 scopus 로고
    • Effect of hindlimb unweighting on single soleus liber maximal shortening velocity and ATPase activity
    • McDonald KS, Fitts RH. Effect of hindlimb unweighting on single soleus liber maximal shortening velocity and ATPase activity. J Appl Physiol 1993;74:2949-2957.
    • (1993) J Appl Physiol , vol.74 , pp. 2949-2957
    • McDonald, K.S.1    Fitts, R.H.2
  • 90
    • 0028784683 scopus 로고
    • Expression of alpha-cardiac myosin heavy chain in normal and denervated rat muscle spindles
    • McWhorter DL, Walro JM, Signs SA, Wang J. Expression of alpha-cardiac myosin heavy chain in normal and denervated rat muscle spindles. Neurosci Lett 1995;200:2-4.
    • (1995) Neurosci Lett , vol.200 , pp. 2-4
    • McWhorter, D.L.1    Walro, J.M.2    Signs, S.A.3    Wang, J.4
  • 92
    • 0030570769 scopus 로고    scopus 로고
    • Regulation of inyosin heavy-chain expression in adult rat hindlimb muscles during short-term paralysis: Comparison of denervation and tetrodotoxin-induced neural inactivation
    • Michel RN, Parry DJ, Dunn SE. Regulation of inyosin heavy-chain expression in adult rat hindlimb muscles during short-term paralysis: comparison of denervation and tetrodotoxin-induced neural inactivation. FEBS Lett 1996;391:39-44.
    • (1996) FEBS Lett , vol.391 , pp. 39-44
    • Michel, R.N.1    Parry, D.J.2    Dunn, S.E.3
  • 93
    • 0032914389 scopus 로고    scopus 로고
    • Myogenin, MyoD, and myosin heavy chain isoform expression following hindlimb suspension
    • Mozdziak PE, Greaser ML, Schultz E. Myogenin, MyoD, and myosin heavy chain isoform expression following hindlimb suspension. Aviat Space Environ Med 1999;70:511-516.
    • (1999) Aviat Space Environ Med , vol.70 , pp. 511-516
    • Mozdziak, P.E.1    Greaser, M.L.2    Schultz, E.3
  • 94
    • 0027183160 scopus 로고
    • Relationship between myosin heavy chain iid isoform and fibre types in soleus muscle of the rat after hindlimb suspension
    • Oishi Y. Relationship between myosin heavy chain IId isoform and fibre types in soleus muscle of the rat after hindlimb suspension. Eur J Appl Physiol 1993;66:451-454.
    • (1993) Eur J Appl Physiol , vol.66 , pp. 451-454
    • Oishi, Y.1
  • 95
    • 0027420708 scopus 로고
    • Signal transduction pathways that regulate skeletal muscle gene expression
    • Olson EN. Signal transduction pathways that regulate skeletal muscle gene expression. Molec Endocrinol 1993;7: 1369-1378.
    • (1993) Molec Endocrinol , vol.7 , pp. 1369-1378
    • Olson, E.N.1
  • 96
    • 0026860301 scopus 로고
    • Effects of lengthened immobilization on functional and histochemical properties of rabbit tibialis anterior muscle
    • Pattullo MC, Cotter MA, Cameron NE, Barry JA. Effects of lengthened immobilization on functional and histochemical properties of rabbit tibialis anterior muscle. Exp Physiol 1992;77:433-442.
    • (1992) Exp Physiol , vol.77 , pp. 433-442
    • Pattullo, M.C.1    Cotter, M.A.2    Cameron, N.E.3    Barry, J.A.4
  • 97
    • 0025676672 scopus 로고
    • Expression of an alpha cardiac-like myosin heavy chain in muscle spindle fibres
    • Pedrossa F, Soukup T, Thornell L-E. Expression of an alpha cardiac-like myosin heavy chain in muscle spindle fibres. Histochemistry 1990;95:105-113.
    • (1990) Histochemistry , vol.95 , pp. 105-113
    • Pedrossa, F.1    Soukup, T.2    Thornell, L.-E.3
  • 98
    • 0028057809 scopus 로고
    • Expression of myosin heavy chain isoforms in developing human muscle spindles
    • Pedrossa-Domellöf F, Thornell L-E. Expression of myosin heavy chain isoforms in developing human muscle spindles. J Histochem Cytochem 1994;42:77-88.
    • (1994) J Histochem Cytochem , vol.42 , pp. 77-88
    • Pedrossa-Domellöf, F.1    Thornell, L.-E.2
  • 99
    • 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 1999;166:261-277.
    • (1999) Acta Physiol Scand , vol.166 , pp. 261-277
    • Pette, D.1    Peuker, H.2    Staron, R.S.3
  • 100
    • 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 1992;120:115-202.
    • (1992) Rev Physiol Biochem Pharmacol , vol.120 , pp. 115-202
    • Pette, D.1    Vrbova, G.2
  • 101
    • 0031757189 scopus 로고    scopus 로고
    • Differential effects of a six-day immobilization on newborn rat soleus muscles at two developmental stages
    • Picquet F, Stevens L, Butler-Browne GS, Mounier Y. Differential effects of a six-day immobilization on newborn rat soleus muscles at two developmental stages. J Muscle Res Cell Motil 1998;19:742-755.
    • (1998) J Muscle Res Cell Motil , vol.19 , pp. 742-755
    • Picquet, F.1    Stevens, L.2    Butler-Browne, G.S.3    Mounier, Y.4
  • 102
    • 0027961046 scopus 로고
    • Level of independence of motor unit properties from neuromuscular activity
    • Pierotti DJ, Roy RR, Hodgson JA, Edgerton VR. Level of independence of motor unit properties from neuromuscular activity. Muscle Nerve 1994;17:1324-1335.
    • (1994) Muscle Nerve , vol.17 , pp. 1324-1335
    • Pierotti, D.J.1    Roy, R.R.2    Hodgson, J.A.3    Edgerton, V.R.4
  • 103
    • 0028303333 scopus 로고
    • Isolation and sequence of cat jaw superfast myosin light chain-2 cDNA and evidence for the identity of its human homologue
    • Qin H, Morris B, Hoh JFY. Isolation and sequence of cat jaw superfast myosin light chain-2 cDNA and evidence for the identity of its human homologue. Biochem Biophys Res Comm 1994;200:1277-1282.
    • (1994) Biochem Biophys Res Comm , vol.200 , pp. 1277-1282
    • Qin, H.1    Morris, B.2    Hoh, J.F.Y.3
  • 104
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao A, Luo C, Hogan PG. Transcription factors of the NFAT family: regulation and function. Annu Rev Immunol 1997; 15:707-747.
    • (1997) Annu Rev Immunol , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 105
    • 0022252990 scopus 로고
    • Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition
    • Reiser PJ, Moss RL, Guilian GG, Greaser ML. Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition. J Biol Chem 1985;260:9077-9080.
    • (1985) J Biol Chem , vol.260 , pp. 9077-9080
    • Reiser, P.J.1    Moss, R.L.2    Guilian, G.G.3    Greaser, M.L.4
  • 106
    • 0023581595 scopus 로고
    • Agrin-like molecules at synaptic sites in normal, denervated, and damaged skeletal muscles
    • Reist NE, Magill C, McMahan UJ. Agrin-like molecules at synaptic sites in normal, denervated, and damaged skeletal muscles. J Cell Biol 1987;105:2457-2469.
    • (1987) J Cell Biol , vol.105 , pp. 2457-2469
    • Reist, N.E.1    Magill, C.2    McMahan, U.J.3
  • 107
    • 0031725437 scopus 로고    scopus 로고
    • Fiber size and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle
    • Rivero J-LL, Talmadge RJ, Edgerton VR. Fiber size and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle. J Muscle Res Cell Motil 1998;19:733-742.
    • (1998) J Muscle Res Cell Motil , vol.19 , pp. 733-742
    • Rivero, J.-L.L.1    Talmadge, R.J.2    Edgerton, V.R.3
  • 108
    • 0032949494 scopus 로고    scopus 로고
    • Interrelationships of myofibrillar ATPase activity and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle
    • Rivero J-LL, Talmadge RJ, Edgerton VR. Interrelationships of myofibrillar ATPase activity and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle. Histochem Cell Biol 1999;111:277-287.
    • (1999) Histochem Cell Biol , vol.111 , pp. 277-287
    • Rivero, J.-L.L.1    Talmadge, R.J.2    Edgerton, V.R.3
  • 109
    • 0029102963 scopus 로고
    • Influence of electrical stimulation of the tibialia anterior muscle in paraplegic subjects. 2. Morphological and histochemical properties
    • Rochester L, Barron MJ, Chandler CS, Sutton RA, Miller S, Johnson MA. Influence of electrical stimulation of the tibialia anterior muscle in paraplegic subjects. 2. Morphological and histochemical properties. Paraplegia 1995;33:514-522.
    • (1995) Paraplegia , vol.33 , pp. 514-522
    • Rochester, L.1    Barron, M.J.2    Chandler, C.S.3    Sutton, R.A.4    Miller, S.5    Johnson, M.A.6
  • 110
    • 0025636007 scopus 로고
    • Maximum velocity of shortening of three fibre types from horse soleus muscle: Implications for scaling with body size
    • Rome L, Sosnicki AA, Goble DO. Maximum velocity of shortening of three fibre types from horse soleus muscle: implications for scaling with body size. J Physiol (Lond) 1990;431: 173-185.
    • (1990) J Physiol (Lond) , vol.431 , pp. 173-185
    • Rome, L.1    Sosnicki, A.A.2    Goble, D.O.3
  • 111
    • 0027255924 scopus 로고
    • Fibre areas and histochemical fibre types in the quadriceps muscle of paraplegic subjects
    • Round JM, Barr FMD, Moffat B, Jones DA. Fibre areas and histochemical fibre types in the quadriceps muscle of paraplegic subjects. J Neurol Sci 1993;116:207-211.
    • (1993) J Neurol Sci , vol.116 , pp. 207-211
    • Round, J.M.1    Barr, F.M.D.2    Moffat, B.3    Jones, D.A.4
  • 112
    • 0020803294 scopus 로고
    • The fibre-type composition of the first branchial arch muscles in carnivora and primates
    • Rowlerson A, Mascarello F, Veggetti A, Carpenè E. The fibre-type composition of the first branchial arch muscles in carnivora and primates. J Muscle Res Cell Motil 1983;4:443-472.
    • (1983) J Muscle Res Cell Motil , vol.4 , pp. 443-472
    • Rowlerson, A.1    Mascarello, F.2    Veggetti, A.3    Carpenè, E.4
  • 114
    • 0022453646 scopus 로고
    • Fiber type and fiber size changes six months after low thoracic spinal cord transection in adult cats: Exercise effects
    • Roy RR, Acosta L. Fiber type and fiber size changes six months after low thoracic spinal cord transection in adult cats: exercise effects. Exp Neurol 1986;92:675-685.
    • (1986) Exp Neurol , vol.92 , pp. 675-685
    • Roy, R.R.1    Acosta, L.2
  • 115
    • 0026061367 scopus 로고
    • The plasticity of skeletal muscle: Effects of neuromuscular activity
    • Holloszy JO, editor. Baltimore: Williams & Wilkins
    • Roy RR, Baldwin KM, Edgerton VR. The plasticity of skeletal muscle: effects of neuromuscular activity. In: Holloszy JO, editor. Exercise and sport sciences reviews 19. Baltimore: Williams & Wilkins; 1991. p 269-312.
    • (1991) Exercise and Sport Sciences Reviews 19 , pp. 269-312
    • Roy, R.R.1    Baldwin, K.M.2    Edgerton, V.R.3
  • 116
    • 0029685353 scopus 로고    scopus 로고
    • Response of the neuromuscular unit to spaceflight: What has been learned from the rat model
    • Holloszy JO, editor. Baltimore: Williams & Wilkins
    • Roy RR, Baldwin KM, Edgerton VR. Response of the neuromuscular unit to spaceflight: what has been learned from the rat model. In: Holloszy JO, editor. Exercise and sport sciences reviews 24. Baltimore: Williams & Wilkins; 1996. p 399-425.
    • (1996) Exercise and Sport Sciences Reviews 24 , pp. 399-425
    • Roy, R.R.1    Baldwin, K.M.2    Edgerton, V.R.3
  • 118
    • 0026731957 scopus 로고
    • Fibre size and type adaptations to spinal isolation and cyclical passive stretch in cat hindlimb
    • Roy RR, Pierotti DJ, Flores V, Rudolph W, Edgerton VR. Fibre size and type adaptations to spinal isolation and cyclical passive stretch in cat hindlimb. J Anat 1992;180:491-499.
    • (1992) J Anat , vol.180 , pp. 491-499
    • Roy, R.R.1    Pierotti, D.J.2    Flores, V.3    Rudolph, W.4    Edgerton, V.R.5
  • 119
    • 0032933404 scopus 로고    scopus 로고
    • Differential response of fast hindlimb extensor and flexor muscles to exercise in adult spinalized cats
    • Roy RR, Talmadge RJ, Hodgson JA, Oishi V, Baldwin KM, Edgerton VR. Differential response of fast hindlimb extensor and flexor muscles to exercise in adult spinalized cats. Muscle Nerve 1999;22:230-241.
    • (1999) Muscle Nerve , vol.22 , pp. 230-241
    • Roy, R.R.1    Talmadge, R.J.2    Hodgson, J.A.3    Oishi, V.4    Baldwin, K.M.5    Edgerton, V.R.6
  • 121
    • 0026441397 scopus 로고
    • Evidence for new isoform of fast myosin heavy chain in rat skeletal muscle
    • Sawchak JA, Leung B, Shafiq SA. Evidence for new isoform of fast myosin heavy chain in rat skeletal muscle. Muscle Nerve 1992;15:1349-1353.
    • (1992) Muscle Nerve , vol.15 , pp. 1349-1353
    • Sawchak, J.A.1    Leung, B.2    Shafiq, S.A.3
  • 122
    • 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 1988; 127:1-11.
    • (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
  • 125
    • 0032538864 scopus 로고    scopus 로고
    • Expression of extraocular - superfast -myosin heavy chain in rat laryngeal muscles
    • Shiotani A, Flint PW. Expression of extraocular - superfast -myosin heavy chain in rat laryngeal muscles. NeuroReport 1998;9:3639-3642.
    • (1998) Neuroreport , vol.9 , pp. 3639-3642
    • Shiotani, A.1    Flint, P.W.2
  • 126
    • 0028566846 scopus 로고
    • Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle
    • Smerdu V, Karsch-Mizrachi I, Campione M, Leinwand L, Schiaffino S. Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle. Am J Physiol 1994;267:C1723-C1728.
    • (1994) Am J Physiol , vol.267
    • Smerdu, V.1    Karsch-Mizrachi, I.2    Campione, M.3    Leinwand, L.4    Schiaffino, S.5
  • 128
    • 0022884418 scopus 로고
    • Correlation between myofibrillar ATPase activity and myosin heavy chain composition in rabbit muscle fibers
    • Staron RS, Pette D. Correlation between myofibrillar ATPase activity and myosin heavy chain composition in rabbit muscle fibers. Histochemistry 1986;86:19-23.
    • (1986) Histochemistry , vol.86 , pp. 19-23
    • Staron, R.S.1    Pette, D.2
  • 129
    • 0027264688 scopus 로고
    • The continuum of pure and hybrid myosin heavy chain-based fibre types in rat skeletal muscle
    • Staron RS, Pette D. The continuum of pure and hybrid myosin heavy chain-based fibre types in rat skeletal muscle. Histochemistry 1993;100:149-153.
    • (1993) Histochemistry , vol.100 , pp. 149-153
    • Staron, R.S.1    Pette, D.2
  • 130
    • 0018891953 scopus 로고
    • Changes in cat muscle contractile proteins after prolonged muscle inactivity
    • Steinbach JH, Schubert D, Eldridge L. Changes in cat muscle contractile proteins after prolonged muscle inactivity. Exp Neurol 1980;67:655-669.
    • (1980) Exp Neurol , vol.67 , pp. 655-669
    • Steinbach, J.H.1    Schubert, D.2    Eldridge, L.3
  • 131
    • 0027232108 scopus 로고
    • Muscle glucose uptake in the rat after suspension with single hindlimb weightbearing
    • Stump CS, Woodman CR, Fregosi RF, Tipton CM. Muscle glucose uptake in the rat after suspension with single hindlimb weightbearing. J Appl Physiol 1993;74:2072-2078.
    • (1993) J Appl Physiol , vol.74 , pp. 2072-2078
    • Stump, C.S.1    Woodman, C.R.2    Fregosi, R.F.3    Tipton, C.M.4
  • 132
    • 0022489890 scopus 로고
    • Velocity of shortening and myosin isozymes in two types of rabbit fast-twitch muscle fibers
    • Sweeney HL, Kushmerick MJ, Mabuchi K, Gergely J, Sreter FA. Velocity of shortening and myosin isozymes in two types of rabbit fast-twitch muscle fibers. Am J Physiol 1986;251: C431-C434.
    • (1986) Am J Physiol , vol.251
    • Sweeney, H.L.1    Kushmerick, M.J.2    Mabuchi, K.3    Gergely, J.4    Sreter, F.A.5
  • 133
    • 0031979873 scopus 로고    scopus 로고
    • In vivo analysis of the myosin heavy chain IIB promoter region
    • Swoap SJ. In vivo analysis of the myosin heavy chain IIB promoter region. Am J Physiol 1998;274:C681-C687.
    • (1998) Am J Physiol , vol.274
    • Swoap, S.J.1
  • 134
    • 0025833579 scopus 로고
    • Expressions of myosin heavy chain IId isoform in rat soleus muscle during hindlimb suspension
    • Takahashi H, Wada M, Katsuta S. Expressions of myosin heavy chain IId isoform in rat soleus muscle during hindlimb suspension. Acta Physiol Scand 1991;143:131-132.
    • (1991) Acta Physiol Scand , vol.143 , pp. 131-132
    • Takahashi, H.1    Wada, M.2    Katsuta, S.3
  • 135
    • 0030586830 scopus 로고    scopus 로고
    • Myosin heavy chain composition of adult feline (Felis catus) limb and diaphragm muscles
    • Talmadge RJ, Grossman EJ, Roy RR. Myosin heavy chain composition of adult feline (Felis catus) limb and diaphragm muscles. J Exp Zool 1996;275:413-420.
    • (1996) J Exp Zool , vol.275 , pp. 413-420
    • Talmadge, R.J.1    Grossman, E.J.2    Roy, R.R.3
  • 136
    • 0027452352 scopus 로고
    • Electrophortic separation of rat skeletal muscle myosin heavy-chain isoforms
    • Talmadge RJ, Roy RR. Electrophortic separation of rat skeletal muscle myosin heavy-chain isoforms. J Appl Physiol 1993;75:2337-2340.
    • (1993) J Appl Physiol , vol.75 , pp. 2337-2340
    • Talmadge, R.J.1    Roy, R.R.2
  • 137
    • 0028935443 scopus 로고
    • Prominence of myosin heavy chain hybrid fibers in soleus muscle of spinal cord-transected rats
    • Talmadge RJ, Roy RR, Edgerton VR. Prominence of myosin heavy chain hybrid fibers in soleus muscle of spinal cord-transected rats. J Appl Physiol 1995;78:1256-1265.
    • (1995) J Appl Physiol , vol.78 , pp. 1256-1265
    • Talmadge, R.J.1    Roy, R.R.2    Edgerton, V.R.3
  • 138
    • 0030470497 scopus 로고    scopus 로고
    • Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers
    • Talmadge RJ, Roy RR, Edgerton VR. Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers. J Appl Physiol 1996;81:2540-2546.
    • (1996) J Appl Physiol , vol.81 , pp. 2540-2546
    • Talmadge, R.J.1    Roy, R.R.2    Edgerton, V.R.3
  • 139
    • 0029852897 scopus 로고    scopus 로고
    • Myosin heavy chain profile of cat soleus following chronic reduced activity or inactivity
    • Talmadge RJ, Roy RR, Edgerton VR. Myosin heavy chain profile of cat soleus following chronic reduced activity or inactivity. Muscle Nerve 1996;19:980-988.
    • (1996) Muscle Nerve , vol.19 , pp. 980-988
    • Talmadge, R.J.1    Roy, R.R.2    Edgerton, V.R.3
  • 140
    • 0033152291 scopus 로고    scopus 로고
    • Persistence of hybrid fibers in rat soleus muscle after spinal cord-transection
    • Talmadge RJ, Roy RR, Edgerton VR. Persistence of hybrid fibers in rat soleus muscle after spinal cord-transection. Anat Rec 1999;255:188-201.
    • (1999) Anat Rec , vol.255 , pp. 188-201
    • Talmadge, R.J.1    Roy, R.R.2    Edgerton, V.R.3
  • 141
    • 0029115294 scopus 로고
    • Myofibrillar ATPase activity of feline muscle fibers expressing slow and fast myosin heavy chains
    • Talmadge RJ, Roy RR, Jiang B, Edgerton VR. Myofibrillar ATPase activity of feline muscle fibers expressing slow and fast myosin heavy chains. J Histochem Cytochem 1995;43: 811-819.
    • (1995) J Histochem Cytochem , vol.43 , pp. 811-819
    • Talmadge, R.J.1    Roy, R.R.2    Jiang, B.3    Edgerton, V.R.4
  • 142
    • 0024422986 scopus 로고
    • Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle
    • Termin A, Staron RS, Pette D. Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle. Histochemistry 1989;92:453-457.
    • (1989) Histochemistry , vol.92 , pp. 453-457
    • Termin, A.1    Staron, R.S.2    Pette, D.3
  • 143
    • 0023251838 scopus 로고
    • Time course of soleus muscle myosin expression during hindlimb suspension and recovery
    • Thomason DB, Herrick RE, Surdyka D, Baldwin KM. Time course of soleus muscle myosin expression during hindlimb suspension and recovery. J Appl Physiol 1987;63:130-137.
    • (1987) J Appl Physiol , vol.63 , pp. 130-137
    • Thomason, D.B.1    Herrick, R.E.2    Surdyka, D.3    Baldwin, K.M.4
  • 144
    • 0000353039 scopus 로고
    • Function and structure in the chronically isolated lumbo-sacral spinal cord of the dog
    • Tower SS. Function and structure in the chronically isolated lumbo-sacral spinal cord of the dog. J Comp Neurol 1937; 67:109-131.
    • (1937) J Comp Neurol , vol.67 , pp. 109-131
    • Tower, S.S.1
  • 146
    • 0013435833 scopus 로고
    • Changes in myosin heavy-chain and light-chain isoforms following sustained exercise
    • Sato Y, Poortmans J, Hashimoto I, Oshida Y, editors. Basel: Karger
    • Wada M, Kikuchi K, Katsuta S. Changes in myosin heavy-chain and light-chain isoforms following sustained exercise. In: Sato Y, Poortmans J, Hashimoto I, Oshida Y, editors. Integration of medical and sports sciences. Basel: Karger; 1992. p 309-317.
    • (1992) Integration of Medical and Sports Sciences , pp. 309-317
    • Wada, M.1    Kikuchi, K.2    Katsuta, S.3
  • 149
    • 0033516510 scopus 로고    scopus 로고
    • Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: Implications for functional diversity
    • Weiss A, Schiaffino S, Leinwand LA. Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity. J Mol Biol 1999;290:61-75.
    • (1999) J Mol Biol , vol.290 , pp. 61-75
    • Weiss, A.1    Schiaffino, S.2    Leinwand, L.A.3
  • 151
    • 0025936935 scopus 로고
    • Changes of myoplasmic calcium concentration during fatigue in single mouse muscle libers
    • Westerblad H. Allen DG. Changes of myoplasmic calcium concentration during fatigue in single mouse muscle libers. J Gen Physiol 1991;98:615-635.
    • (1991) J Gen Physiol , vol.98 , pp. 615-635
    • Westerblad, H.1    Allen, D.G.2
  • 152
    • 0033023377 scopus 로고    scopus 로고
    • An E-box within the MHC IIb gene is hound by MyoD and is required for gene expression in fast muscle
    • Wheeler MT, Snyder EC, Patterson MN, Swoap SJ. An E-box within the MHC IIb gene is hound by MyoD and is required for gene expression in fast muscle. Am J Physiol 1999;276: C1069-C1078.
    • (1999) Am J Physiol , vol.276
    • Wheeler, M.T.1    Snyder, E.C.2    Patterson, M.N.3    Swoap, S.J.4
  • 155
    • 0021925453 scopus 로고
    • Co-expression of multiple myosin heavy chain genes, in addition to a tissue-specifc one, in extraocular musculature
    • Wieczorek DF, Periasamy M, Butler-Browne GS, Whalen RG, Nadal-Ginard B. Co-expression of multiple myosin heavy chain genes, in addition to a tissue-specifc one, in extraocular musculature. J Cell Biol 1985;101:618-629.
    • (1985) J Cell Biol , vol.101 , pp. 618-629
    • Wieczorek, D.F.1    Periasamy, M.2    Butler-Browne, G.S.3    Whalen, R.G.4    Nadal-Ginard, B.5
  • 156
    • 0025755995 scopus 로고
    • Differential regulation of MyoD and myogenin mRNA levels by nerve induced muscle activity
    • Witzemann V, Sakmann B. Differential regulation of MyoD and myogenin mRNA levels by nerve induced muscle activity. FEBS Lett 1991;282:259-264.
    • (1991) FEBS Lett , vol.282 , pp. 259-264
    • Witzemann, V.1    Sakmann, B.2
  • 157
    • 0031908166 scopus 로고    scopus 로고
    • A new concept in laryngeal muscle: Multiple myosin isoform types in single muscle fibers of the lateral cricoarytenoid
    • Wu YZ, Baker MJ, Crumley RL, Blanks RH, Caiozzo VJ. A new concept in laryngeal muscle: multiple myosin isoform types in single muscle fibers of the lateral cricoarytenoid. Otolaryngol Head Neck Surg 1998;118:86-94.
    • (1998) Otolaryngol Head Neck Surg , vol.118 , pp. 86-94
    • Wu, Y.Z.1    Baker, M.J.2    Crumley, R.L.3    Blanks, R.H.4    Caiozzo, V.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.