메뉴 건너뛰기




Volumn 23, Issue 5, 1997, Pages 287-305

Muscle contraction and fatigue. The role of adenosine 5'-diphosphate and inorganic phosphate

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; PHOSPHATE;

EID: 0030906826     PISSN: 01121642     EISSN: None     Source Type: Journal    
DOI: 10.2165/00007256-199723050-00003     Document Type: Review
Times cited : (51)

References (124)
  • 1
    • 0018877621 scopus 로고
    • Crossbridge model of muscle contraction: Quantitative analysis
    • Eisenberg E, Hill TL, Chen Y. Crossbridge model of muscle contraction: quantitative analysis. Biophys J 1980; 29: 195-227
    • (1980) Biophys J , vol.29 , pp. 195-227
    • Eisenberg, E.1    Hill, T.L.2    Chen, Y.3
  • 2
    • 0021862562 scopus 로고
    • Phosphate release and force generation in skeletal muscle fibers
    • Hibberd MG, Dantzig JA, Trentham DR, et al. Phosphate release and force generation in skeletal muscle fibers. Science 1985; 228: 1317-9
    • (1985) Science , vol.228 , pp. 1317-1319
    • Hibberd, M.G.1    Dantzig, J.A.2    Trentham, D.R.3
  • 3
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley AF, Simmons RM. Proposed mechanism of force generation in striated muscle. Nature 1971; 233: 533-8
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 4
    • 0023091848 scopus 로고
    • The effect of inorganic phosphate on the ATP hydrolysis rate and the tension transients in chemically skinned rabbit psoas fibers
    • Kawai M, Guth K, Winnikes K, et al. The effect of inorganic phosphate on the ATP hydrolysis rate and the tension transients in chemically skinned rabbit psoas fibers. Pflugers Arch 1987; 408: 1-9
    • (1987) Pflugers Arch , vol.408 , pp. 1-9
    • Kawai, M.1    Guth, K.2    Winnikes, K.3
  • 5
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn RW, Taylor EW. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 1971; 10(25): 4617-24
    • (1971) Biochemistry , vol.10 , Issue.25 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 6
    • 0026711203 scopus 로고
    • Force and stiffness in glycerinated rabbit psoas fibers
    • Martyn DA, Gordon AM. Force and stiffness in glycerinated rabbit psoas fibers. J Gen Physiol 1992; 99: 795-816
    • (1992) J Gen Physiol , vol.99 , pp. 795-816
    • Martyn, D.A.1    Gordon, A.M.2
  • 7
    • 0019003415 scopus 로고
    • Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1
    • Sleep JA, Hutton RL. Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1. Biochemistry 1980; 19: 1276-83
    • (1980) Biochemistry , vol.19 , pp. 1276-1283
    • Sleep, J.A.1    Hutton, R.L.2
  • 8
    • 0018688930 scopus 로고
    • Mechanism of actomyosin adenosine triphosphatase. Evidence that adenosine 5′-triphosphate hydrolysis can occur without dissociation of the actomyosin complex
    • Stein LA, Schwarz Jr RP, Chock PB, et al. Mechanism of actomyosin adenosine triphosphatase. Evidence that adenosine 5′-triphosphate hydrolysis can occur without dissociation of the actomyosin complex. Biochemistry 1979; 18 (18): 3895-909
    • (1979) Biochemistry , vol.18 , Issue.18 , pp. 3895-3909
    • Stein, L.A.1    Schwarz Jr., R.P.2    Chock, P.B.3
  • 9
    • 8244228655 scopus 로고
    • Kinetics of ADP and AMP-PNP binding to SF-1
    • Trybus KM, Taylor EW. Kinetics of ADP and AMP-PNP binding to SF-1 [abstract]. Biophys J 1979; 25: 21a
    • (1979) Biophys J , vol.25
    • Trybus, K.M.1    Taylor, E.W.2
  • 11
    • 0018816862 scopus 로고
    • The relation between muscle physiology and muscle biochemistry
    • Eisenberg E, Green LE. The relation between muscle physiology and muscle biochemistry. Annu Rev Physiol 1980; 42: 293-309
    • (1980) Annu Rev Physiol , vol.42 , pp. 293-309
    • Eisenberg, E.1    Green, L.E.2
  • 12
    • 0025007895 scopus 로고
    • ++-sensitive cross-bridge state transition in mammalian single skeletal muscle fibers
    • ++-sensitive cross-bridge state transition in mammalian single skeletal muscle fibers. J Physiol 1990; 428: 751-64
    • (1990) J Physiol , vol.428 , pp. 751-764
    • Metzger, J.M.1    Moss, R.L.2
  • 13
    • 0018581348 scopus 로고
    • Contraction of glycerinated muscle fibers as a function of the MgATP concentration
    • Cooke R, Bialek W. Contraction of glycerinated muscle fibers as a function of the MgATP concentration. Biophys J 1979; 28: 241-58
    • (1979) Biophys J , vol.28 , pp. 241-258
    • Cooke, R.1    Bialek, W.2
  • 14
    • 0026073088 scopus 로고
    • Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle
    • Kawai M, Halvorson HR. Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle. Biophys J 1991; 59: 329-42
    • (1991) Biophys J , vol.59 , pp. 329-342
    • Kawai, M.1    Halvorson, H.R.2
  • 16
    • 0018368483 scopus 로고
    • Mechanism of actomyosin ATPase and the problem of muscle contraction
    • Taylor EW. Mechanism of actomyosin ATPase and the problem of muscle contraction. CRC Crit Rev Biochem 1979; 7: 103-64
    • (1979) CRC Crit Rev Biochem , vol.7 , pp. 103-164
    • Taylor, E.W.1
  • 17
    • 0023839774 scopus 로고
    • The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate
    • Cooke R, Franks K, Luciani G, et al. The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate. J Physiol 1988; 395: 77-97
    • (1988) J Physiol , vol.395 , pp. 77-97
    • Cooke, R.1    Franks, K.2    Luciani, G.3
  • 18
    • 0022405269 scopus 로고
    • The effects of ADP and phosphate on the contraction of muscle fibers
    • Cooke R, Pate E. The effects of ADP and phosphate on the contraction of muscle fibers. Biophys J 1985; 48: 789-98
    • (1985) Biophys J , vol.48 , pp. 789-798
    • Cooke, R.1    Pate, E.2
  • 19
    • 0021964341 scopus 로고
    • Oxygen exchange between phosphate and water accompanies culcium-regulated ATPase activity of skinned fibers from rabbit skeletal muscle
    • Hibberd MG, Webb MR, Goldman YE, et al. Oxygen exchange between phosphate and water accompanies culcium-regulated ATPase activity of skinned fibers from rabbit skeletal muscle. J Biol Chem 1985; 260 (6): 3496-500
    • (1985) J Biol Chem , vol.260 , Issue.6 , pp. 3496-3500
    • Hibberd, M.G.1    Webb, M.R.2    Goldman, Y.E.3
  • 20
    • 0022931151 scopus 로고
    • The role of orthophosphate in crossbridge kinetics in chemically skinned rabbit psoas fibers as detected with sinusoidal and step length alterations
    • Kawai M. The role of orthophosphate in crossbridge kinetics in chemically skinned rabbit psoas fibers as detected with sinusoidal and step length alterations. J Muscle Res Cell Motil 1986; 7: 421-34
    • (1986) J Muscle Res Cell Motil , vol.7 , pp. 421-434
    • Kawai, M.1
  • 21
    • 0025610206 scopus 로고
    • Inhibitory influence of phosphate and arsenate on conduction of skinned skeletal and cardiac muscle
    • Nosek TM, Leal-Cardoso JH, McLaughlin M, et al. Inhibitory influence of phosphate and arsenate on conduction of skinned skeletal and cardiac muscle. Am J Physiol 1990; 259: C933-9
    • (1990) Am J Physiol , vol.259
    • Nosek, T.M.1    Leal-Cardoso, J.H.2    McLaughlin, M.3
  • 22
    • 0024392532 scopus 로고
    • Addition of phosphate to active muscle fibers probes actomyosin states within the powerstroke
    • Pate E, Cooke R. Addition of phosphate to active muscle fibers probes actomyosin states within the powerstroke. Pflugers Arch 1989; 414: 73-81
    • (1989) Pflugers Arch , vol.414 , pp. 73-81
    • Pate, E.1    Cooke, R.2
  • 23
    • 8244253649 scopus 로고
    • The effect of phosphate on muscle isometric tension
    • Pate E, Franks K, Cooke R. The effect of phosphate on muscle isometric tension [abstract]. Biophys J 1988; 53: 568a
    • (1988) Biophys J , vol.53
    • Pate, E.1    Franks, K.2    Cooke, R.3
  • 24
    • 0025143526 scopus 로고
    • Depression of force by phosphate in skinned skeletal muscle fibers of the frog
    • Stienen GJM, Roosemalen MCM, Wilson MGA, et al. Depression of force by phosphate in skinned skeletal muscle fibers of the frog. Am J Physiol 1990; 259: C349-57
    • (1990) Am J Physiol , vol.259
    • Stienen, G.J.M.1    Roosemalen, M.C.M.2    Wilson, M.G.A.3
  • 27
    • 0014898672 scopus 로고
    • The activation by ADP and temperature increase of tension and ATPase activity of insect flight muscle
    • Abbott RH, Mannherz HG. The activation by ADP and temperature increase of tension and ATPase activity of insect flight muscle. Pflugers Arch 1970; 321: 223-32
    • (1970) Pflugers Arch , vol.321 , pp. 223-232
    • Abbott, R.H.1    Mannherz, H.G.2
  • 28
    • 0003026204 scopus 로고
    • Some factors modifying the expression of human strength
    • Ikai M, Steinhaus AH. Some factors modifying the expression of human strength. J Appl Physiol 1961; 16: 157-63
    • (1961) J Appl Physiol , vol.16 , pp. 157-163
    • Ikai, M.1    Steinhaus, A.H.2
  • 30
    • 0004189533 scopus 로고
    • Skeletal muscle: Structure and funclion
    • Harris JM, Stead L, Lukens R, editors. Malvern (PA): Lea & Febiger
    • McArdle WD, Katch FI, Katch VL. Skeletal muscle: structure and funclion In: Harris JM, Stead L, Lukens R, editors. Essentials of exercise physiology. Malvern (PA): Lea & Febiger, 1994
    • (1994) Essentials of Exercise Physiology
    • McArdle, W.D.1    Katch, F.I.2    Katch, V.L.3
  • 32
    • 8244260053 scopus 로고
    • Muscular system: Histology and physiology
    • Allen D, Callanan RJ, Breckwoldt T, editors. St Louis (MO): Moshy-Year Book, Inc.
    • Seeley RR, Stephens TD, Tate P. Muscular system: histology and physiology. In: Allen D, Callanan RJ, Breckwoldt T, editors. Anatomy and physiology, 2nd ed. St Louis (MO): Moshy-Year Book, Inc., 1992
    • (1992) Anatomy and Physiology, 2nd Ed.
    • Seeley, R.R.1    Stephens, T.D.2    Tate, P.3
  • 34
    • 0004261102 scopus 로고
    • Basic energy systems
    • Mauck S, Garrett LK, Plummer T, et al., editors. Champaign (IL): Human Kinetics
    • Wilmore JH, Costill DL. Basic energy systems. In: Mauck S, Garrett LK, Plummer T, et al., editors. Physiology of sport and exercise. Champaign (IL): Human Kinetics, 1994
    • (1994) Physiology of Sport and Exercise
    • Wilmore, J.H.1    Costill, D.L.2
  • 35
    • 0018562931 scopus 로고
    • Muscle fatigue
    • Asmussen E. Muscle fatigue. Med Sci Sports 1979; 11 (4): 313-21
    • (1979) Med Sci Sports , vol.11 , Issue.4 , pp. 313-321
    • Asmussen, E.1
  • 36
    • 0001792833 scopus 로고
    • Biochemical basis of fatigue in exercise performance: Catastrophe theory of muscular fatigue
    • Knuttgen HG, editor. Champaign (IL): Human Kinetics
    • Edwards RHT. Biochemical basis of fatigue in exercise performance: catastrophe theory of muscular fatigue. In: Knuttgen HG, editor. Biochemistry of exercise. Champaign (IL): Human Kinetics, 1983: 3-28
    • (1983) Biochemistry of Exercise , pp. 3-28
    • Edwards, R.H.T.1
  • 37
    • 77049171076 scopus 로고
    • Voluntary strength and fatigue
    • Merton PA. Voluntary strength and fatigue. J Physiol 1954; 123: 553-64
    • (1954) J Physiol , vol.123 , pp. 553-564
    • Merton, P.A.1
  • 38
    • 0023893174 scopus 로고
    • Motor drive and metabolic responses during repeated submaximal contractions in humans
    • Vollestad NK, Sejersted OM, Bahr R, et al. Motor drive and metabolic responses during repeated submaximal contractions in humans. J Appl Physiol 1988; 64 (4): 1421-7
    • (1988) J Appl Physiol , vol.64 , Issue.4 , pp. 1421-1427
    • Vollestad, N.K.1    Sejersted, O.M.2    Bahr, R.3
  • 39
    • 0014619284 scopus 로고
    • Training effect of muscular endurance by means of voluntary and electrical stimulation
    • Ikai M, Yabe K. Training effect of muscular endurance by means of voluntary and electrical stimulation. Eur J Appl Physiol 1969; 28: 55-60
    • (1969) Eur J Appl Physiol , vol.28 , pp. 55-60
    • Ikai, M.1    Yabe, K.2
  • 40
    • 0017861960 scopus 로고
    • A central nervous component in local muscle fatigue
    • Asmussen E, Mazin B. A central nervous component in local muscle fatigue. Eur J Appl Physiol 1978; 38: 9-15
    • (1978) Eur J Appl Physiol , vol.38 , pp. 9-15
    • Asmussen, E.1    Mazin, B.2
  • 41
    • 0018194441 scopus 로고
    • Central and peripheral fatigue in sustained maximum voluntary contractions of human quadriceps muscle
    • Bigland-Ritchie B, Jones DA, Hosking GP, et al. Central and peripheral fatigue in sustained maximum voluntary contractions of human quadriceps muscle. Clin Sci Mol Med 1978; 54: 609-14
    • (1978) Clin Sci Mol Med , vol.54 , pp. 609-614
    • Bigland-Ritchie, B.1    Jones, D.A.2    Hosking, G.P.3
  • 42
    • 0022531038 scopus 로고
    • Fatigue of intermittent submaximal voluntary contractions: Central and peripheral factors
    • Bigland-Ritchie B, Furbush F, Woods JJ. Fatigue of intermittent submaximal voluntary contractions: central and peripheral factors. J Appl Physiol 1986; 61: 421-9
    • (1986) J Appl Physiol , vol.61 , pp. 421-429
    • Bigland-Ritchie, B.1    Furbush, F.2    Woods, J.J.3
  • 43
    • 0013649497 scopus 로고
    • Fatigue: Neural and muscular mechanisms
    • Gandevia et al., editors. New York: Plenum Press
    • Gandevia SC. Fatigue: neural and muscular mechanisms. In: Gandevia et al., editors. Advances in experimental medicine and biology. New York: Plenum Press, 1995
    • (1995) Advances in Experimental Medicine and Biology
    • Gandevia, S.C.1
  • 44
    • 0025995239 scopus 로고
    • Cellular mechanisms of fatigue in skeletal muscle
    • Westerblad HJ, Lee A, Lannergren J, et al. Cellular mechanisms of fatigue in skeletal muscle. Am J Physiol 1991; 261: C195-209
    • (1991) Am J Physiol , vol.261
    • Westerblad, H.J.1    Lee, A.2    Lannergren, J.3
  • 45
    • 0020002105 scopus 로고
    • The absence of neuromuscular transmission failure in sustained maximal voluntary contractions
    • Bigland-Ritchie B, Kukulka CG, Lippold OCJ, et al. The absence of neuromuscular transmission failure in sustained maximal voluntary contractions. J Physiol 1982; 330: 265-78
    • (1982) J Physiol , vol.330 , pp. 265-278
    • Bigland-Ritchie, B.1    Kukulka, C.G.2    Lippold, O.C.J.3
  • 46
    • 0018460736 scopus 로고
    • Relation between force and fatiguability of red and pale skeletal muscles in man
    • Clamann HP, Broecker KT. Relation between force and fatiguability of red and pale skeletal muscles in man. Am J Phys Med 1979; 58: 70-85
    • (1979) Am J Phys Med , vol.58 , pp. 70-85
    • Clamann, H.P.1    Broecker, K.T.2
  • 47
    • 77049299403 scopus 로고
    • The relation between force and integrated electrical activity in fatigued muscle
    • Edwards RG, Lippold OC. The relation between force and integrated electrical activity in fatigued muscle. J Physiol 1956; 132: 677-81
    • (1956) J Physiol , vol.132 , pp. 677-681
    • Edwards, R.G.1    Lippold, O.C.2
  • 48
    • 0015266124 scopus 로고
    • Fatigue of maintained voluntary muscle contraction in man
    • Stephens JA, Taylor AA. Fatigue of maintained voluntary muscle contraction in man. J Physiol 1972; 220: 1-18
    • (1972) J Physiol , vol.220 , pp. 1-18
    • Stephens, J.A.1    Taylor, A.A.2
  • 49
    • 0020646147 scopus 로고
    • Electromyogram, force and relaxation time during and after continuous electrical stimulation of human skeletal muscle in situ
    • Hultman E, Sjoholm H. Electromyogram, force and relaxation time during and after continuous electrical stimulation of human skeletal muscle in situ. J Physiol 1983; 339: 33-40
    • (1983) J Physiol , vol.339 , pp. 33-40
    • Hultman, E.1    Sjoholm, H.2
  • 50
    • 0022924219 scopus 로고
    • Reflex origin for the slowing of motoneurone firing rates in fatigue of human voluntary contractions
    • Bigland-Ritchie B, Dawson NJ, Johansson RS, et al. Reflex origin for the slowing of motoneurone firing rates in fatigue of human voluntary contractions. J Physiol 1986; 379: 451-9
    • (1986) J Physiol , vol.379 , pp. 451-459
    • Bigland-Ritchie, B.1    Dawson, N.J.2    Johansson, R.S.3
  • 51
    • 8244252257 scopus 로고
    • Does a reduction in motor drive necessarily result in force loss during fatigue?
    • Knuttgen HG, Vogel JA, Poortmans J, editors. Biochemistry of exercise Champaign (IL)
    • Bigland-Ritchie B, Johansson R, Woods JJ. Does a reduction in motor drive necessarily result in force loss during fatigue? In: Knuttgen HG, Vogel JA, Poortmans J, editors. Biochemistry of exercise. Champaign (IL): Human Kinetics, 1983; 13: 864-70
    • (1983) Human Kinetics , vol.13 , pp. 864-870
    • Bigland-Ritchie, B.1    Johansson, R.2    Woods, J.J.3
  • 52
    • 0022271925 scopus 로고
    • Thixotropic behaviour of human finger flexor muscles with accompanying changes in spindle and reflex responses to stretch
    • Hagbarth KE, Hagglund JV, Nordin M. Thixotropic behaviour of human finger flexor muscles with accompanying changes in spindle and reflex responses to stretch. J Physiol 1985; 368: 323-42
    • (1985) J Physiol , vol.368 , pp. 323-342
    • Hagbarth, K.E.1    Hagglund, J.V.2    Nordin, M.3
  • 53
    • 0020644122 scopus 로고
    • Responses in muscle afferent fibers of slow conduction velocity to contractions and ischaemia in the cat
    • Mense S, Stanke M. Responses in muscle afferent fibers of slow conduction velocity to contractions and ischaemia in the cat. J Physiol 1983; 342: 383-97
    • (1983) J Physiol , vol.342 , pp. 383-397
    • Mense, S.1    Stanke, M.2
  • 54
    • 0025858777 scopus 로고
    • Effects of enhanced activity on synaptic transmission in mouse extensor digitorum longus muscle
    • Dorlochter MA, Irentchev A, Brinkers M, et al. Effects of enhanced activity on synaptic transmission in mouse extensor digitorum longus muscle. J Physiol 1991; 436: 283-92
    • (1991) J Physiol , vol.436 , pp. 283-292
    • Dorlochter, M.A.1    Irentchev, A.2    Brinkers, M.3
  • 55
    • 0346526072 scopus 로고
    • The neuromuscular junction: Structure, function, and its role in the excitation of muscle
    • Deschenes MR, Marish CM, Kraemer WJ. The neuromuscular junction: structure, function, and its role in the excitation of muscle. J Strength Condit Res 1994; 8 (2): 103-9
    • (1994) J Strength Condit Res , vol.8 , Issue.2 , pp. 103-109
    • Deschenes, M.R.1    Marish, C.M.2    Kraemer, W.J.3
  • 56
    • 0025427579 scopus 로고
    • Regulation by exercise of the pool of G4 acetylcholinesterase characterizing fast muscles: Opposite effect of running training in antagonistic muscles
    • Jasmin BJ, Gisiger V. Regulation by exercise of the pool of G4 acetylcholinesterase characterizing fast muscles: opposite effect of running training in antagonistic muscles. J Neurosci 1990; 10: 1444-54
    • (1990) J Neurosci , vol.10 , pp. 1444-1454
    • Jasmin, B.J.1    Gisiger, V.2
  • 57
    • 0028107645 scopus 로고
    • Cellular mechanisms of muscle fatigue
    • Fitts RH. Cellular mechanisms of muscle fatigue. Physiol Rev 1994; 74 (1): 49-94
    • (1994) Physiol Rev , vol.74 , Issue.1 , pp. 49-94
    • Fitts, R.H.1
  • 58
    • 0021022521 scopus 로고
    • + concentration changes in human muscles during volitional contractions
    • + concentration changes in human muscles during volitional contractions. Pflugers Arch 1983; 399: 235-7
    • (1983) Pflugers Arch , vol.399 , pp. 235-237
    • Vyskocil, F.1    Hnik, P.2    Rehfeldt, H.3
  • 59
    • 0021999938 scopus 로고
    • Water and ion shifts in skeletal muscle of humans with intense dynamic knee extension
    • Sjogaard G, Adams RP, Saltin B. Water and ion shifts in skeletal muscle of humans with intense dynamic knee extension. Am J Physiol 1985; 248: R190-6
    • (1985) Am J Physiol , vol.248
    • Sjogaard, G.1    Adams, R.P.2    Saltin, B.3
  • 60
    • 0024391412 scopus 로고
    • + from muscle during prolonged dynamic exercise
    • + from muscle during prolonged dynamic exercise. Acta Physiol Scand 1989; 136: 293-4
    • (1989) Acta Physiol Scand , vol.136 , pp. 293-294
    • Sahlin, K.1    Broberg, S.2
  • 61
    • 0000838262 scopus 로고
    • Voltage sensors and calcium channels of excitation-contraction coupling
    • Rios E, Pizarro G. Voltage sensors and calcium channels of excitation-contraction coupling. News Physiol Sci 1988; 3: 223-7
    • (1988) News Physiol Sci , vol.3 , pp. 223-227
    • Rios, E.1    Pizarro, G.2
  • 62
    • 0025869296 scopus 로고
    • The mechanical hypothesis of excitation-contraction (EC) coupling in skeletal muscle
    • Rios E, Ma J, Gonzalez A. The mechanical hypothesis of excitation-contraction (EC) coupling in skeletal muscle. J Muscle Res Cell Motil 1991; 12: 127-35
    • (1991) J Muscle Res Cell Motil , vol.12 , pp. 127-135
    • Rios, E.1    Ma, J.2    Gonzalez, A.3
  • 63
    • 0015353792 scopus 로고
    • Sodium dependence of the inward spread of activation in isolated twitch muscle fibers of the frog
    • Benzanilla F, Caupto C, Gonzalez-Serratos H, et al. Sodium dependence of the inward spread of activation in isolated twitch muscle fibers of the frog. J Physiol 1972; 223: 507-23
    • (1972) J Physiol , vol.223 , pp. 507-523
    • Benzanilla, F.1    Caupto, C.2    Gonzalez-Serratos, H.3
  • 64
    • 0015444032 scopus 로고
    • The effect of repetitive stimulation at low frequencies upon the electrical and mechanical activity of single muscle fibers
    • Grabowski W, Lobsiger EA, Luettgau HC. The effect of repetitive stimulation at low frequencies upon the electrical and mechanical activity of single muscle fibers. Pflugers Arch 1972; 334: 222-39
    • (1972) Pflugers Arch , vol.334 , pp. 222-239
    • Grabowski, W.1    Lobsiger, E.A.2    Luettgau, H.C.3
  • 65
    • 0019742898 scopus 로고
    • Muscle fatigue due to changes beyond the neuromuscular junction
    • Jones DA. Muscle fatigue due to changes beyond the neuromuscular junction. Ciba Found Symp 1981; 82: 178-96
    • (1981) Ciba Found Symp , vol.82 , pp. 178-196
    • Jones, D.A.1
  • 66
    • 0023018105 scopus 로고
    • Force and membrane potential during and after fatiguing, continuous high-frequency stimulation of single Xenopus muscle fibers
    • Lannergren J, Westerblad H. Force and membrane potential during and after fatiguing, continuous high-frequency stimulation of single Xenopus muscle fibers. Acta Physiol Scand 1986; 128: 359-68
    • (1986) Acta Physiol Scand , vol.128 , pp. 359-368
    • Lannergren, J.1    Westerblad, H.2
  • 67
    • 0023115322 scopus 로고
    • Action potential fatigue in single skeletal muscle fibers of Xenopus
    • Lannergren J, Westerblad H. Action potential fatigue in single skeletal muscle fibers of Xenopus. Acta Physiol Scand 1987; 129: 311-8
    • (1987) Acta Physiol Scand , vol.129 , pp. 311-318
    • Lannergren, J.1    Westerblad, H.2
  • 68
    • 0022539545 scopus 로고
    • Fatigue from high- And low-frequency muscle stimulation: Role of sarcolemma action potentials
    • Metzger JM, Fitts RH. Fatigue from high- and low-frequency muscle stimulation: role of sarcolemma action potentials. Exp Neurol 1986; 93: 320-33
    • (1986) Exp Neurol , vol.93 , pp. 320-333
    • Metzger, J.M.1    Fitts, R.H.2
  • 69
    • 0021827077 scopus 로고
    • Single motor unit and fiber action potentials during fatigue
    • Sandercock TG, Faulkner JA, Albers JW, et al. Single motor unit and fiber action potentials during fatigue. J Appl Physiol 1985; 58: 1073-9
    • (1985) J Appl Physiol , vol.58 , pp. 1073-1079
    • Sandercock, T.G.1    Faulkner, J.A.2    Albers, J.W.3
  • 70
    • 0019756525 scopus 로고
    • Human muscle function and fatigue
    • Edwards RHT. Human muscle function and fatigue. Ciba Found Symp 1981; 82: 1-18
    • (1981) Ciba Found Symp , vol.82 , pp. 1-18
    • Edwards, R.H.T.1
  • 71
    • 0026027988 scopus 로고
    • Role of exercise-induced potassium fluxes underlying muscle fatigue: A brief review
    • Sjogaard G. Role of exercise-induced potassium fluxes underlying muscle fatigue: a brief review. Can J Physiol Pharmacol 1991; 69: 238-45
    • (1991) Can J Physiol Pharmacol , vol.69 , pp. 238-245
    • Sjogaard, G.1
  • 72
    • 0018897686 scopus 로고
    • Potassium concentration changes in the transverse tubules of vertebrate skeletal muscle
    • Almers W. Potassium concentration changes in the transverse tubules of vertebrate skeletal muscle. Fed Proc Fed Am Soc Exp Biol 1980; 39: 1527-32
    • (1980) Fed Proc Fed Am Soc Exp Biol , vol.39 , pp. 1527-1532
    • Almers, W.1
  • 73
    • 0026541982 scopus 로고
    • Role of excitation-contraction coupling in muscle fatigue
    • Allen DG, Westerblad H, Lee JA, et al. Role of excitation-contraction coupling in muscle fatigue. Sports Med 1992; 13 (2): 116-26
    • (1992) Sports Med , vol.13 , Issue.2 , pp. 116-126
    • Allen, D.G.1    Westerblad, H.2    Lee, J.A.3
  • 74
    • 0025239042 scopus 로고
    • Spatial gradients of intracellular calcium in skeletal muscle during fatigue
    • Westerblad H, Lee JA, Lamb AG, et al. Spatial gradients of intracellular calcium in skeletal muscle during fatigue. Pflugers Arch 1990: 415: 734-40
    • (1990) Pflugers Arch , vol.415 , pp. 734-740
    • Westerblad, H.1    Lee, J.A.2    Lamb, A.G.3
  • 75
    • 0015856916 scopus 로고
    • Speed of repolarization and morphology of glycerol-treated muscle fibres
    • Nakajima S, Nakajima Y, Peachey LD. Speed of repolarization and morphology of glycerol-treated muscle fibres. J Physiol 1973; 234: 465-80
    • (1973) J Physiol , vol.234 , pp. 465-480
    • Nakajima, S.1    Nakajima, Y.2    Peachey, L.D.3
  • 76
    • 0019863867 scopus 로고
    • Density and apparent location of the sodium pump in frog sartorius muscle
    • Venosa RA, Horowicz P. Density and apparent location of the sodium pump in frog sartorius muscle. J Membr Biol 1981; 59: 225-32
    • (1981) J Membr Biol , vol.59 , pp. 225-232
    • Venosa, R.A.1    Horowicz, P.2
  • 77
    • 0023236607 scopus 로고
    • Effects of repetitive activity, ruthenium red, and elevated extracellular calcium on frog skeletal muscle: Implications for t-tubule conduction
    • Howell JN, Oetliker H. Effects of repetitive activity, ruthenium red, and elevated extracellular calcium on frog skeletal muscle: implications for t-tubule conduction. Can J Physiol Pharmacol 1987; 65: 691-6
    • (1987) Can J Physiol Pharmacol , vol.65 , pp. 691-696
    • Howell, J.N.1    Oetliker, H.2
  • 78
    • 0023358272 scopus 로고
    • Evidence for t-tubular conduction failure in frog skeletal muscle induced by elevated extracellular calcium concentration
    • Howell JN, Shankar A, Howell SG, et al. Evidence for t-tubular conduction failure in frog skeletal muscle induced by elevated extracellular calcium concentration. J Muscle Res Cell Motil 1487; 8: 229-41
    • (1487) J Muscle Res Cell Motil , vol.8 , pp. 229-241
    • Howell, J.N.1    Shankar, A.2    Howell, S.G.3
  • 79
    • 0020076965 scopus 로고
    • Muscle fatigue and the role of transverse tubules
    • Bianchi CP, Narayan S. Muscle fatigue and the role of transverse tubules. Science 1982; 215 (15): 295-6
    • (1982) Science , vol.215 , Issue.15 , pp. 295-296
    • Bianchi, C.P.1    Narayan, S.2
  • 81
    • 0024280913 scopus 로고
    • Ryanodine receptor of skeletal muscle is a gap junction-type channel
    • Ma J, Fill M, Knudson CM, et al. Ryanodine receptor of skeletal muscle is a gap junction-type channel. Science 1988; 242: 99-102
    • (1988) Science , vol.242 , pp. 99-102
    • Ma, J.1    Fill, M.2    Knudson, C.M.3
  • 82
    • 0024577369 scopus 로고
    • Effects of exercise of varying duration on sarcoplasmic reticulum function
    • Byrd S, Bode A, Klug G. Effects of exercise of varying duration on sarcoplasmic reticulum function. J Appl Physiol 1989; 66 (3): 1383-9
    • (1989) J Appl Physiol , vol.66 , Issue.3 , pp. 1383-1389
    • Byrd, S.1    Bode, A.2    Klug, G.3
  • 84
    • 0023161167 scopus 로고
    • Mechanical and structural approaches to correlation of cross-bridge action in muscle with actomyosin ATPase in solution
    • Brenner B. Mechanical and structural approaches to correlation of cross-bridge action in muscle with actomyosin ATPase in solution. Annu Rev Physiol 1987; 49: 655-72
    • (1987) Annu Rev Physiol , vol.49 , pp. 655-672
    • Brenner, B.1
  • 85
    • 0024312136 scopus 로고
    • Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers
    • Metzger JM, Greaser ML, Moss RL. Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. J Gen Physiol 1989; 93: 855-83
    • (1989) J Gen Physiol , vol.93 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 86
    • 0019447614 scopus 로고
    • Effect of Ca ion concentration on crossbridge kinetics in rabbit psoas fibers: Evidence for the presence of two Ca-activated states of thin filament
    • Kawai M, Cox RN, Brandt PW. Effect of Ca ion concentration on crossbridge kinetics in rabbit psoas fibers: evidence for the presence of two Ca-activated states of thin filament. Biophys J 1981; 35: 375-84
    • (1981) Biophys J , vol.35 , pp. 375-384
    • Kawai, M.1    Cox, R.N.2    Brandt, P.W.3
  • 87
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Potter JD, Gergely J. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J Biol Chem 1975; 250: 4628-33
    • (1975) J Biol Chem , vol.250 , pp. 4628-4633
    • Potter, J.D.1    Gergely, J.2
  • 88
    • 0025271805 scopus 로고
    • Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers
    • Metzger JM, Moss RL. Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers. Science 1990; 247: 1088-90
    • (1990) Science , vol.247 , pp. 1088-1090
    • Metzger, J.M.1    Moss, R.L.2
  • 89
    • 0024166391 scopus 로고
    • ++ insensitive tension due to reduced pH in partially troponin extracted skinned skeletal muscle fibers
    • ++ insensitive tension due to reduced pH in partially troponin extracted skinned skeletal muscle fibers. Biophys J 1988; 54: 1169-73
    • (1988) Biophys J , vol.54 , pp. 1169-1173
    • Metzger, J.M.1    Moss, R.L.2
  • 90
    • 0024007477 scopus 로고
    • ++ on cross-bridge turnover kinetics in skinned single psoas fibers: Implication for regulation of muscle contraction
    • ++ on cross-bridge turnover kinetics in skinned single psoas fibers: implication for regulation of muscle contraction. Proc Natl Acad Sci USA 1988; 85: 3265-9
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 91
    • 0021811364 scopus 로고
    • Biochemical basis of muscular fatigue associated with repetitions contractions of skeletal muscle
    • Belcastro AN, Maclean I, Gilchrist J. Biochemical basis of muscular fatigue associated with repetitions contractions of skeletal muscle [minireview]. Int J Biochem 1985; 17 (4): 447-53
    • (1985) Int J Biochem , vol.17 , Issue.4 , pp. 447-453
    • Belcastro, A.N.1    Maclean, I.2    Gilchrist, J.3
  • 92
    • 0001972554 scopus 로고
    • Fatigue mechanisms in muscle fibers
    • Gutmann E, Hnik P, editors. Prague: Czech Academy of Sciences
    • Eberstein A, Sandow A. Fatigue mechanisms in muscle fibers. In: Gutmann E, Hnik P, editors. The effect of use and disuse of neuromuscular function. Prague: Czech Academy of Sciences, 1963: 515-26
    • (1963) The Effect of Use and Disuse of Neuromuscular Function , pp. 515-526
    • Eberstein, A.1    Sandow, A.2
  • 93
    • 0025936935 scopus 로고
    • Changes of myoplasmic calcium concentration during fatigue in single mouse muscle fibers
    • Westerblad H, Allen DG. Changes of myoplasmic calcium concentration during fatigue in single mouse muscle fibers. J Gen Physiol 1991; 98: 615-35
    • (1991) J Gen Physiol , vol.98 , pp. 615-635
    • Westerblad, H.1    Allen, D.G.2
  • 94
    • 0021341434 scopus 로고
    • ++ binding of rabbit skeletal myofilaments
    • ++ binding of rabbit skeletal myofilaments. J Biol Chem 1984; 259 (5): 3181-6
    • (1984) J Biol Chem , vol.259 , Issue.5 , pp. 3181-3186
    • Blanchard, E.1    Pan, B.2    Solaro, R.3
  • 95
    • 0024661091 scopus 로고
    • Changes in intracellular milieu with fatigue of hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle
    • Godt RE, Nosek TM. Changes in intracellular milieu with fatigue of hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle. J Physiol 1989; 412: 155-80
    • (1989) J Physiol , vol.412 , pp. 155-180
    • Godt, R.E.1    Nosek, T.M.2
  • 96
    • 0026029850 scopus 로고
    • Force decline due to fatigue and intracellular acidification in isolated fibers from mouse skeletal muscle
    • Lannergren J, Westerblad H. Force decline due to fatigue and intracellular acidification in isolated fibers from mouse skeletal muscle. J Physiol 1991; 434: 307-22
    • (1991) J Physiol , vol.434 , pp. 307-322
    • Lannergren, J.1    Westerblad, H.2
  • 97
    • 0027240491 scopus 로고
    • Intracellular calcium concentration during low-frequency fatigue in isolated single fibers of mouse skeletal muscle
    • Westerblad H, Duty S, Allen DG. Intracellular calcium concentration during low-frequency fatigue in isolated single fibers of mouse skeletal muscle. J Appl Physiol 1993; 75 (1): 382-8
    • (1993) J Appl Physiol , vol.75 , Issue.1 , pp. 382-388
    • Westerblad, H.1    Duty, S.2    Allen, D.G.3
  • 98
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: Correlation with actomyosin ATPase in solution
    • Brenner B, Eisenberg E. Rate of force generation in muscle: correlation with actomyosin ATPase in solution. Proc Natl Acad Sci USA 1986; 83: 3542-6
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 99
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment I is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemankowski RF, Wiseman MO, White HD. ADP dissociation from actomyosin subfragment I is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci USA 1985: 82: 658-62
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 100
    • 0013676952 scopus 로고
    • Magnesium-ADP binding to acto-myosin-s1 and acto-heavymeromyosin
    • White HD, Magnesium-ADP binding to acto-myosin-s1 and acto-heavymeromyosin [abstract]. Biophys J 1977; 17: 40a
    • (1977) Biophys J , vol.17
    • White, H.D.1
  • 101
    • 0018078264 scopus 로고
    • Muscular fatigue investigated by phosphorous nuclear magnetic resonance
    • Dawson MJ, Gadian DG, Wilkie DR. Muscular fatigue investigated by phosphorous nuclear magnetic resonance. Nature 1978; 274: 861-6
    • (1978) Nature , vol.274 , pp. 861-866
    • Dawson, M.J.1    Gadian, D.G.2    Wilkie, D.R.3
  • 102
    • 0022069244 scopus 로고
    • Chemical changes in rat leg muscle by phosphorus nuclear magnetic resonance
    • Kushmerick MJ, Meyer RA. Chemical changes in rat leg muscle by phosphorus nuclear magnetic resonance. Am J Physiol 1985: 248: C542-9
    • (1985) Am J Physiol , vol.248
    • Kushmerick, M.J.1    Meyer, R.A.2
  • 103
    • 0025330404 scopus 로고
    • Adenine nucleotide depletion in human muscle during exercise: Causality and significance of AMP deamination
    • Sahlin K, Broberg S. Adenine nucleotide depletion in human muscle during exercise: causality and significance of AMP deamination. Int J Sports Med 1991; 11 Suppl. 2: S62-7
    • (1991) Int J Sports Med , vol.11 , Issue.2 SUPPL.
    • Sahlin, K.1    Broberg, S.2
  • 104
    • 0020335160 scopus 로고
    • The contents of high-energy phosphates in different fibre types in skeletal muscles from rat, guinea-pig, and man
    • Edstrom L, Hultman E, Sahlin K, et al. The contents of high-energy phosphates in different fibre types in skeletal muscles from rat, guinea-pig, and man. J Physiol 1982; 332: 47-58
    • (1982) J Physiol , vol.332 , pp. 47-58
    • Edstrom, L.1    Hultman, E.2    Sahlin, K.3
  • 105
    • 0018908716 scopus 로고
    • Mechanical relaxation rate and metabolism studied in fatiguing muscle by phosphorous nuclear magnetic resonance
    • Dawson MJ, Gadian DG, Wilkie DR. Mechanical relaxation rate and metabolism studied in fatiguing muscle by phosphorous nuclear magnetic resonance. J Physiol 1980; 299: 465-84
    • (1980) J Physiol , vol.299 , pp. 465-484
    • Dawson, M.J.1    Gadian, D.G.2    Wilkie, D.R.3
  • 106
    • 0021895484 scopus 로고
    • A nuclear magnetic resonance study of metabolism in the ferret heart during hypoxia and inhibition of glycolysis
    • Allen DG, Morris PG, Orchard CH, et al. A nuclear magnetic resonance study of metabolism in the ferret heart during hypoxia and inhibition of glycolysis. J Physiol 1985; 361: 185-204
    • (1985) J Physiol , vol.361 , pp. 185-204
    • Allen, D.G.1    Morris, P.G.2    Ch, O.3
  • 107
    • 0019945956 scopus 로고
    • Free energy change of ATP-hydrolysis: A causal factor of early hypoxic failure of the myocardium
    • Kammermeier H, Schmidt P, Jungling E. Free energy change of ATP-hydrolysis: a causal factor of early hypoxic failure of the myocardium. J Mol Cell Cardiol 1982; 14: 267-77
    • (1982) J Mol Cell Cardiol , vol.14 , pp. 267-277
    • Kammermeier, H.1    Schmidt, P.2    Jungling, E.3
  • 108
    • 0016756234 scopus 로고
    • The relationship of adenosine triphosphatase activity to tension and power output of insect flight muscle
    • Pybus J, Tregaer RT. The relationship of adenosine triphosphatase activity to tension and power output of insect flight muscle. J Physiol 1975; 247: 71-89
    • (1975) J Physiol , vol.247 , pp. 71-89
    • Pybus, J.1    Tregaer, R.T.2
  • 109
    • 0014990270 scopus 로고
    • Effects of inorganic phosphate on the contractile mechanism
    • Ruegg JC, Schadler M, Steiger GJ, et al. Effects of inorganic phosphate on the contractile mechanism. Pflugers Arch 1971; 325: 359-64
    • (1971) Pflugers Arch , vol.325 , pp. 359-364
    • Ruegg, J.C.1    Schadler, M.2    Steiger, G.J.3
  • 110
    • 0015399481 scopus 로고
    • Phosphate starvation and the nonlinear dynamics of insect fibrillar flight muscle
    • White DC, Thorson SJ. Phosphate starvation and the nonlinear dynamics of insect fibrillar flight muscle. J Gen Physiol 1972; 60: 307-36
    • (1972) J Gen Physiol , vol.60 , pp. 307-336
    • White, D.C.1    Thorson, S.J.2
  • 111
    • 0019496042 scopus 로고
    • Vanadate and phosphate ions reduce tension and increase cross-bridge kinetics in chemically skinned heart muscle
    • Herzig JW, Peterson JC, Ruegg JC, et al. Vanadate and phosphate ions reduce tension and increase cross-bridge kinetics in chemically skinned heart muscle. Biochim Biophys Acta 1981; 672: 191-6
    • (1981) Biochim Biophys Acta , vol.672 , pp. 191-196
    • Herzig, J.W.1    Peterson, J.C.2    Ruegg, J.C.3
  • 112
    • 0022252990 scopus 로고
    • Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition
    • Reiser PJ, Moss RL, Giulian CG, et al. Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition. J Biol Chem 1985; 260: 9077-80
    • (1985) J Biol Chem , vol.260 , pp. 9077-9080
    • Reiser, P.J.1    Moss, R.L.2    Giulian, C.G.3
  • 113
    • 0023216267 scopus 로고
    • The muliplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres: Rabbit soleus muscle
    • Staron RS, Pett D. The muliplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres: rabbit soleus muscle. Biochem J 1987; 243: 687-93
    • (1987) Biochem J , vol.243 , pp. 687-693
    • Staron, R.S.1    Pett, D.2
  • 114
    • 0025251785 scopus 로고
    • The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers
    • Millar NC, Homsher E. The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. J Biol Chem 1990; 265: 20234-40
    • (1990) J Biol Chem , vol.265 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 115
    • 0015525066 scopus 로고
    • Cooperation within actin filament in vertebrate skeletal muscle
    • Bremel RD, Weber A. Cooperation within actin filament in vertebrate skeletal muscle. Nature 1972; 238: 97-101
    • (1972) Nature , vol.238 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 116
    • 0023912104 scopus 로고
    • Muscle force and stiffness during activation and relaxation: Implications for the actomyosin ATPase
    • Brozovich FV, Yates LD, Gordon AM. Muscle force and stiffness during activation and relaxation: implications for the actomyosin ATPase. J Gen Physiol 1988; 91: 399-420
    • (1988) J Gen Physiol , vol.91 , pp. 399-420
    • Brozovich, F.V.1    Yates, L.D.2    Gordon, A.M.3
  • 117
    • 0016180488 scopus 로고
    • Theoretical formalism for the sliding filament model of contraction of striated muscle, Pt 1
    • Hill TL. Theoretical formalism for the sliding filament model of contraction of striated muscle, Pt 1. Prog Biophys Mol Biol 1974; 28: 267-340
    • (1974) Prog Biophys Mol Biol , vol.28 , pp. 267-340
    • Hill, T.L.1
  • 118
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley AF. Muscle structure and theories of contraction. Prog Biophys Mol Biol 1957; 7: 255-318
    • (1957) Prog Biophys Mol Biol , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 119
    • 0020397898 scopus 로고
    • Correlation between exponential processes and crossbridge kinetics
    • Twarog BM, Levine RJC, Dewey MM, editors. New York: Raven Press
    • Kawai M. Correlation between exponential processes and crossbridge kinetics. In: Twarog BM, Levine RJC, Dewey MM, editors. Basic biology of muscle: a comparative approach. New York: Raven Press, 1982: 109-30
    • (1982) Basic Biology of Muscle: A Comparative Approach , pp. 109-130
    • Kawai, M.1
  • 120
    • 0023201966 scopus 로고
    • It is the diprotonated inorganic phosphate that depresses force in skinned skeletal muscle fibers
    • Nosek TM, Fender KY, Godt RE, It is the diprotonated inorganic phosphate that depresses force in skinned skeletal muscle fibers. Science 1987; 236: 191-3
    • (1987) Science , vol.236 , pp. 191-193
    • Nosek, T.M.1    Fender, K.Y.2    Godt, R.E.3
  • 121
    • 0019249780 scopus 로고
    • Biphasic steady-state kinetics of myosin adenosine triphosphatase
    • Yee D, Wiedner H, Eckstein F. Biphasic steady-state kinetics of myosin adenosine triphosphatase. Eur J Biochem 1980; 133: 85-90
    • (1980) Eur J Biochem , vol.133 , pp. 85-90
    • Yee, D.1    Wiedner, H.2    Eckstein, F.3
  • 122
    • 0025906416 scopus 로고
    • Metabolic and work efficiencies during exercise in Andean natives
    • Hochachka PW, Stanley C, Matheson GO, et al. Metabolic and work efficiencies during exercise in Andean natives. J Appl Physiol 1991; 70: 1720-30
    • (1991) J Appl Physiol , vol.70 , pp. 1720-1730
    • Hochachka, P.W.1    Stanley, C.2    Matheson, G.O.3
  • 124
    • 0025853842 scopus 로고
    • Cardiovascular adaptations in Andean natives after 6 weeks of exposure to sea level
    • McKenzie CD, Goodman L, Matheson GO, et al. Cardiovascular adaptations in Andean natives after 6 weeks of exposure to sea level. J Appl Physiol 1991; 70: 2650-5
    • (1991) J Appl Physiol , vol.70 , pp. 2650-2655
    • McKenzie, C.D.1    Goodman, L.2    Matheson, G.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.