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Volumn 25, Issue 2, 2004, Pages 107-117

Inorganic phosphate affects the pCa-force relationship more than the pCa-ATPase by increasing the rate of dissociation of force generating cross-bridges in skinned fibers from both EDL and soleus muscles of the rat

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); PHOSPHATE;

EID: 4043077144     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:JURE.0000035841.04314.16     Document Type: Article
Times cited : (11)

References (65)
  • 1
    • 0018881743 scopus 로고
    • Regulation and kinetics of the actin-myosin-ATP interaction
    • Adelstein RS and Eisenberg E (1980) Regulation and kinetics of the actin-myosin-ATP interaction. Ann Rev Biochem 49: 921-956.
    • (1980) Ann Rev Biochem , vol.49 , pp. 921-956
    • Adelstein, R.S.1    Eisenberg, E.2
  • 2
    • 0343820075 scopus 로고    scopus 로고
    • Ca(2+) measurements in skinned cardiac fibers: Effects of Mg(2+) on Ca(2+) activation of force and fiber ATPase
    • Allen K, Xu YY and Kerrick WG (2000) Ca(2+) measurements in skinned cardiac fibers: effects of Mg(2+) on Ca(2+) activation of force and fiber ATPase. J Appl Physiol 88: 180-185.
    • (2000) J Appl Physiol , vol.88 , pp. 180-185
    • Allen, K.1    Xu, Y.Y.2    Kerrick, W.G.3
  • 3
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc Natl Acad Sci USA 85: 3265-3269.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 4
    • 0028001707 scopus 로고
    • Fluo-3 signals associated with potassium contractures in single amphibian muscle fibers
    • Caputo C and Bolanos P (1994) Fluo-3 signals associated with potassium contractures in single amphibian muscle fibers. J Physiol (Lond) 481: 119-128.
    • (1994) J Physiol (Lond) , vol.481 , pp. 119-128
    • Caputo, C.1    Bolanos, P.2
  • 5
    • 0018594325 scopus 로고
    • Irreversible thiophosphorylation and activation of tension in functionally skinned rabbit item strips by [35S]ATP gamma S
    • Cassidy P, Hoar PE and Kerrick WGL (1979) Irreversible thiophosphorylation and activation of tension in functionally skinned rabbit item strips by [35S]ATP gamma S. J Biol Chem 254: 11148-11153.
    • (1979) J Biol Chem , vol.254 , pp. 11148-11153
    • Cassidy, P.1    Hoar, P.E.2    Kerrick, W.G.L.3
  • 6
    • 0019977525 scopus 로고
    • Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin
    • Chalovich JM and Eisenberg E (1982) Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin. J Biol Chem 257: 2432-2437.
    • (1982) J Biol Chem , vol.257 , pp. 2432-2437
    • Chalovich, J.M.1    Eisenberg, E.2
  • 7
    • 0023839774 scopus 로고
    • The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate
    • Cooke R, Franks K, Luciani GB and Pate E (1988) The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate. J Physiol (Lond) 395: 77-97.
    • (1988) J Physiol (Lond) , vol.395 , pp. 77-97
    • Cooke, R.1    Franks, K.2    Luciani, G.B.3    Pate, E.4
  • 8
    • 0035369435 scopus 로고    scopus 로고
    • Role of myoplasmic phosphate in contractile function of skeletal muscle: Studies on creatine kinase-deficient mice
    • Dahlstedt AJ, Katz A and Westerblad H (2001) Role of myoplasmic phosphate in contractile function of skeletal muscle: studies on creatine kinase-deficient mice. J Physiol 533: 379-388.
    • (2001) J Physiol , vol.533 , pp. 379-388
    • Dahlstedt, A.J.1    Katz, A.2    Westerblad, H.3
  • 9
    • 0028955956 scopus 로고
    • Protein kinase a does not alter economy of force maintenance in skinned rat cardiac trabeculae
    • de Tombe PP and Stienen GJ (1995) Protein kinase A does not alter economy of force maintenance in skinned rat cardiac trabeculae. Circ Res 76: 734-741.
    • (1995) Circ Res , vol.76 , pp. 734-741
    • De Tombe, P.P.1    Stienen, G.J.2
  • 10
    • 0027470787 scopus 로고
    • Dissociation of [H+] from fatigue in human muscle detected by high time resolution 31P-NMR
    • Degroot M, Massie BM, Boska M, Gober J, Miller RG and Weiner MW (1993) Dissociation of [H+] from fatigue in human muscle detected by high time resolution 31P-NMR. Muscle Nerve 16: 91-98.
    • (1993) Muscle Nerve , vol.16 , pp. 91-98
    • Degroot, M.1    Massie, B.M.2    Boska, M.3    Gober, J.4    Miller, R.G.5    Weiner, M.W.6
  • 11
    • 0016589363 scopus 로고
    • 2+-activated tension generation of skinned skeletal muscle fibers
    • 2+-activated tension generation of skinned skeletal muscle fibers. J Gen Physiol 66: 427-444.
    • (1975) J Gen Physiol , vol.66 , pp. 427-444
    • Donaldson, S.K.1    Kerrick, W.G.2
  • 12
    • 0014111898 scopus 로고
    • Troponin as the Ca++-receptive protein in the contractile system
    • Ebashi S, Ebashi F and Kodama A (1967) Troponin as the Ca++-receptive protein in the contractile system. J Biochem (Tokyo) 62: 137-138.
    • (1967) J Biochem (Tokyo) , vol.62 , pp. 137-138
    • Ebashi, S.1    Ebashi, F.2    Kodama, A.3
  • 13
    • 0028337558 scopus 로고
    • Influence of phosphate and pH on myofibrillar ATPase activity and force in skinned cardiac trabeculae from rat
    • Ebus JP, Stienen GJ and Elzinga G (1994) Influence of phosphate and pH on myofibrillar ATPase activity and force in skinned cardiac trabeculae from rat. J Physiol (Lond) 476: 501-516.
    • (1994) J Physiol (Lond) , vol.476 , pp. 501-516
    • Ebus, J.P.1    Stienen, G.J.2    Elzinga, G.3
  • 14
    • 0021992946 scopus 로고
    • Muscle contraction and free energy transduction in biological systems
    • Eisenberg E and Hill TL (1985) Muscle contraction and free energy transduction in biological systems. Science 227: 999-1006.
    • (1985) Science , vol.227 , pp. 999-1006
    • Eisenberg, E.1    Hill, T.L.2
  • 15
    • 0021287106 scopus 로고
    • The kinetics of magnesium adenosine triphosphate cleavage in skinned muscle fibers of the rabbit
    • Ferenczi MA, Homsher E and Trentham DR (1984) The kinetics of magnesium adenosine triphosphate cleavage in skinned muscle fibers of the rabbit. J Physiol (Lond) 352: 575-599.
    • (1984) J Physiol (Lond) , vol.352 , pp. 575-599
    • Ferenczi, M.A.1    Homsher, E.2    Trentham, D.R.3
  • 16
    • 0027515534 scopus 로고
    • Cross-bridges affect both TnC structure and calcium affinity in muscle fibers
    • Gordon AM and Ridgway EB (1993) Cross-bridges affect both TnC structure and calcium affinity in muscle fibers. Adv Exp Med Biol 332: 183-192.
    • (1993) Adv Exp Med Biol , vol.332 , pp. 183-192
    • Gordon, A.M.1    Ridgway, E.B.2
  • 17
    • 0018941153 scopus 로고
    • ATPase activity in rapidly activated skinned muscle fibers
    • Griffiths PJ, Guth K, Kuhn HJ and Ruegg JC (1980) ATPase activity in rapidly activated skinned muscle fibers. Pflugers Arch 387: 167-173.
    • (1980) Pflugers Arch , vol.387 , pp. 167-173
    • Griffiths, P.J.1    Guth, K.2    Kuhn, H.J.3    Ruegg, J.C.4
  • 18
    • 0023032843 scopus 로고
    • Perfusion cuvette for the simultaneous measurement of mechanical, optical and energetic parameters of skinned muscle fibers
    • Guth K and Wojciechowski R (1986) Perfusion cuvette for the simultaneous measurement of mechanical, optical and energetic parameters of skinned muscle fibers. Pflugers Arch 407: 552-557.
    • (1986) Pflugers Arch , vol.407 , pp. 552-557
    • Guth, K.1    Wojciechowski, R.2
  • 19
    • 0016610095 scopus 로고
    • X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle
    • Haselgrove JC (1975) X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. J Mol Biol 92: 113-143.
    • (1975) J Mol Biol , vol.92 , pp. 113-143
    • Haselgrove, J.C.1
  • 20
    • 0030969083 scopus 로고    scopus 로고
    • ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibers: A real time phosphate assay
    • He ZH, Chillingworth RK, Brune M, Corrie JE, Trentham DR, Webb MR and Ferenczi MA (1997) ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibers: a real time phosphate assay. J Physiol 501: 125-148.
    • (1997) J Physiol , vol.501 , pp. 125-148
    • He, Z.H.1    Chillingworth, R.K.2    Brune, M.3    Corrie, J.E.4    Trentham, D.R.5    Webb, M.R.6    Ferenczi, M.A.7
  • 23
    • 0020549120 scopus 로고
    • Active shortening retards the decline of the intracellular calcium transient in mammalian heart muscle
    • Housmans PR, Lee NK and Blinks JR (1983) Active shortening retards the decline of the intracellular calcium transient in mammalian heart muscle. Science 221: 159-161.
    • (1983) Science , vol.221 , pp. 159-161
    • Housmans, P.R.1    Lee, N.K.2    Blinks, J.R.3
  • 24
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley AF (1957) Muscle structure and theories of contraction. Prog Biophys 7: 255-318.
    • (1957) Prog Biophys , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 25
    • 0028878144 scopus 로고
    • Strain sensitivity and turnover rate of low force cross-bridges in contracting skeletal muscle fibers in the presence of phosphate
    • Iwamoto H (1995) Strain sensitivity and turnover rate of low force cross-bridges in contracting skeletal muscle fibers in the presence of phosphate. Biophys J 68: 243-250.
    • (1995) Biophys J , vol.68 , pp. 243-250
    • Iwamoto, H.1
  • 26
    • 0027163347 scopus 로고
    • Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers
    • Kawai M and Zhao Y (1993) Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers. Biophys J 65: 638-651.
    • (1993) Biophys J , vol.65 , pp. 638-651
    • Kawai, M.1    Zhao, Y.2
  • 27
    • 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, Haist C and Ruegg JC (1987) The effect of inorganic phosphate on the ATP hydrolysis rate and the tension transients in chemically skinned rabbit psoas fibers. Pflugers Arch 408: 1-9.
    • (1987) Pflugers Arch , vol.408 , pp. 1-9
    • Kawai, M.1    Guth, K.2    Winnikes, K.3    Haist, C.4    Ruegg, J.C.5
  • 28
    • 0027504562 scopus 로고
    • Elementary steps of contraction probed by sinusoidal analysis technique in rabbit psoas fibers
    • Kawai M, Zhao Y and Halvorson HR (1993) Elementary steps of contraction probed by sinusoidal analysis technique in rabbit psoas fibers. Adv Exp Med Biol 332: 567-577.
    • (1993) Adv Exp Med Biol , vol.332 , pp. 567-577
    • Kawai, M.1    Zhao, Y.2    Halvorson, H.R.3
  • 29
    • 0022560216 scopus 로고
    • The effects of inorganic phosphate and creatine phosphate on force production in skinned muscles from rat ventricle
    • Kentish JC (1986) The effects of inorganic phosphate and creatine phosphate on force production in skinned muscles from rat ventricle. J Physiol (Lond) 370: 585-604.
    • (1986) J Physiol (Lond) , vol.370 , pp. 585-604
    • Kentish, J.C.1
  • 30
    • 0026009517 scopus 로고
    • Combined inhibitory actions of acidosis and phosphate on maximum force production in rat skinned cardiac muscle
    • Kentish JC (1991) Combined inhibitory actions of acidosis and phosphate on maximum force production in rat skinned cardiac muscle. Pflugers Arch 419: 310-318.
    • (1991) Pflugers Arch , vol.419 , pp. 310-318
    • Kentish, J.C.1
  • 31
    • 0016626085 scopus 로고
    • Disruption of the sarcolemma of mammalian skeletal muscle fibers by homogenization
    • Kerrick WG and Krasner B (1975) Disruption of the sarcolemma of mammalian skeletal muscle fibers by homogenization. J Appl Physiol 39: 1052-1055.
    • (1975) J Appl Physiol , vol.39 , pp. 1052-1055
    • Kerrick, W.G.1    Krasner, B.2
  • 33
    • 0023042009 scopus 로고
    • Structural changes during activation of frog muscle studied by time- Resolved X-ray diffraction
    • Kress M, Huxley HE, Faruqi AR and Hendrix J (1986) Structural changes during activation of frog muscle studied by time- resolved X-ray diffraction. J Mol Biol 188: 325-342.
    • (1986) J Mol Biol , vol.188 , pp. 325-342
    • Kress, M.1    Huxley, H.E.2    Faruqi, A.R.3    Hendrix, J.4
  • 34
    • 0019945363 scopus 로고
    • Force and ATPase rate in skinned skeletal muscle fibers
    • Kushmerick MJ and Krasner B (1982) Force and ATPase rate in skinned skeletal muscle fibers. Fed Proc 41: 2232-2237.
    • (1982) Fed Proc , vol.41 , pp. 2232-2237
    • Kushmerick, M.J.1    Krasner, B.2
  • 35
    • 0032940756 scopus 로고    scopus 로고
    • A diazo-2 study of relaxation mechanisms in frog and barnacle muscle fibers: Effects of pH, MgADP, and inorganic phosphate
    • Lipscomb S, Palmer RE, Li Q, Allhouse LD, Miller T, Potter JD and Ashley CC (1999) A diazo-2 study of relaxation mechanisms in frog and barnacle muscle fibers: effects of pH, MgADP, and inorganic phosphate. Pflugers Arch 437: 204-212.
    • (1999) Pflugers Arch , vol.437 , pp. 204-212
    • Lipscomb, S.1    Palmer, R.E.2    Li, Q.3    Allhouse, L.D.4    Miller, T.5    Potter, J.D.6    Ashley, C.C.7
  • 36
    • 0027315793 scopus 로고
    • Tension transients initiated by photogeneration of MgADP in skinned skeletal muscle fibers
    • Lu Z, Moss RL and Walker JW (1993) Tension transients initiated by photogeneration of MgADP in skinned skeletal muscle fibers. J Gen Physiol 101: 867-888.
    • (1993) J Gen Physiol , vol.101 , pp. 867-888
    • Lu, Z.1    Moss, R.L.2    Walker, J.W.3
  • 37
    • 0028210495 scopus 로고
    • Kinetic mechanism of myofibril ATPase
    • Ma YZ and Taylor EW (1994) Kinetic mechanism of myofibril ATPase. Biophys J 66: 1542-1553.
    • (1994) Biophys J , vol.66 , pp. 1542-1553
    • Ma, Y.Z.1    Taylor, E.W.2
  • 38
    • 0026711203 scopus 로고
    • Force and stiffness in glycerinated rabbit psoas fibers. Effects of calcium and elevated phosphate
    • Martyn DA and Gordon AM (1992) Force and stiffness in glycerinated rabbit psoas fibers. Effects of calcium and elevated phosphate. J Gen Physiol 99: 795-816.
    • (1992) J Gen Physiol , vol.99 , pp. 795-816
    • Martyn, D.A.1    Gordon, A.M.2
  • 39
    • 0024312136 scopus 로고
    • Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle
    • Metzger JM, Greaser ML and Moss RL (1989) Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle. J Gen Physiol 93: 855-883.
    • (1989) J Gen Physiol , vol.93 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 40
    • 0025251785 scopus 로고
    • The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. A steady-state and transient kinetic study
    • Millar NC and Homsher E (1990) The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. A steady-state and transient kinetic study. J Biol Chem 265: 20234-20240.
    • (1990) J Biol Chem , vol.265 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 41
    • 0026735649 scopus 로고
    • Kinetics of force generation and phosphate release in skinned rabbit soleus muscle fibers
    • Millar NC and Homsher E (1992) Kinetics of force generation and phosphate release in skinned rabbit soleus muscle fibers. Am J Physiol 262: C1239-C1245.
    • (1992) Am J Physiol , vol.262
    • Millar, N.C.1    Homsher, E.2
  • 42
    • 0026611165 scopus 로고
    • 2+ regulation of mechanical properties of striated muscle. Mechanistic studies using extraction and replacement of regulatory proteins
    • 2+ regulation of mechanical properties of striated muscle. Mechanistic studies using extraction and replacement of regulatory proteins. Circ Res 70: 865-884.
    • (1992) Circ Res , vol.70 , pp. 865-884
    • Moss, R.L.1
  • 44
    • 0025610206 scopus 로고
    • Inhibitory influence of phosphate and arsenate on contraction of skinned skeletal and cardiac muscle
    • Nosek TM, Leal-Cardoso JH, McLaughlin M and Godt RE (1990) Inhibitory influence of phosphate and arsenate on contraction of skinned skeletal and cardiac muscle. Am J Physiol 259: C933-C939.
    • (1990) Am J Physiol , vol.259
    • Nosek, T.M.1    Leal-Cardoso, J.H.2    McLaughlin, M.3    Godt, R.E.4
  • 45
    • 0028170185 scopus 로고
    • 2+ sensitivity of mammalian skinned cardiac and skeletal muscle fibers
    • 2+ sensitivity of mammalian skinned cardiac and skeletal muscle fibers. J Physiol (Lond) 480: 45-60.
    • (1994) J Physiol (Lond) , vol.480 , pp. 45-60
    • Palmer, S.1    Kentish, J.C.2
  • 47
    • 0014877448 scopus 로고
    • The relation between calcium and contraction kinetics in skinned muscle fibers
    • Podolsky RJ and Teichholz LE (1970) The relation between calcium and contraction kinetics in skinned muscle fibers. J Physiol (Lond) 211: 19-35.
    • (1970) J Physiol (Lond) , vol.211 , pp. 19-35
    • Podolsky, R.J.1    Teichholz, L.E.2
  • 48
    • 0028140519 scopus 로고
    • Myofibrillar ATPase activity and mechanical performance of skinned fibers from rabbit psoas muscle
    • published erratum appears in J Physiol (Lond) (1995) 483(Pt 3): 811
    • Potma EJ, Stienen GJ, Barends JP and Elzinga G (1994) Myofibrillar ATPase activity and mechanical performance of skinned fibers from rabbit psoas muscle [published erratum appears in J Physiol (Lond) (1995) 483(Pt 3): 811]. J Physiol (Lond) 474: 303-317.
    • (1994) J Physiol (Lond) , vol.474 , pp. 303-317
    • Potma, E.J.1    Stienen, G.J.2    Barends, J.P.3    Elzinga, G.4
  • 49
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Potter JD and Gergely J (1975) The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J Biol Chem 250: 4628-4633.
    • (1975) J Biol Chem , vol.250 , pp. 4628-4633
    • Potter, J.D.1    Gergely, J.2
  • 50
    • 0025745301 scopus 로고
    • Function of the N-terminal calcium-binding sites in cardiac/slow troponin C assessed in fast skeletal muscle fibers
    • Putkey JA, Liu W and Sweeney HL (1991) Function of the N-terminal calcium-binding sites in cardiac/slow troponin C assessed in fast skeletal muscle fibers. J Biol Chem 266: 14,881-14,884.
    • (1991) J Biol Chem , vol.266 , pp. 14881-14884
    • Putkey, J.A.1    Liu, W.2    Sweeney, H.L.3
  • 51
    • 0036409388 scopus 로고    scopus 로고
    • Activation of striated muscle: Nearest-neighbor regulatory-unit and cross-bridge influence on myofilament kinetics
    • Robinson JM, Wang Y, Kerrick WGL and Cheung HC (2002) Activation of striated muscle: nearest-neighbor regulatory-unit and cross-bridge influence on myofilament kinetics. J Mol Biol 322: 1065-1088.
    • (2002) J Mol Biol , vol.322 , pp. 1065-1088
    • Robinson, J.M.1    Wang, Y.2    Kerrick, W.G.L.3    Cheung, H.C.4
  • 52
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemankowski RF, Wiseman MO and White HD (1985) ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci USA 82: 658-662.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 53
    • 33750856767 scopus 로고    scopus 로고
    • Effect of pH, phosphate, and ADP on relaxation of myocardium after photolysis of diazo-2
    • Simnett SJ, Johns EC, Lipscomb S, Mulligan IP and Ashley CC (1998) Effect of pH, phosphate, and ADP on relaxation of myocardium after photolysis of diazo-2. Am J Physiol 275: H951-H960.
    • (1998) Am J Physiol , vol.275
    • Simnett, S.J.1    Johns, E.C.2    Lipscomb, S.3    Mulligan, I.P.4    Ashley, C.C.5
  • 54
    • 0019003415 scopus 로고
    • Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1
    • Sleep JA and Hutton RL (1980) Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1. Biochemistry 19: 1276-1283.
    • (1980) Biochemistry , vol.19 , pp. 1276-1283
    • Sleep, J.A.1    Hutton, R.L.2
  • 55
    • 0028006097 scopus 로고
    • The calcium sensitizer EMD 53998 antagonizes phosphate-induced increases in energy cost of isometric tension in cardiac skinned fibers
    • Strauss JD, Bletz C and Ruegg JC (1994) The calcium sensitizer EMD 53998 antagonizes phosphate-induced increases in energy cost of isometric tension in cardiac skinned fibers. Eur J Pharmacol 252: 219-224.
    • (1994) Eur J Pharmacol , vol.252 , pp. 219-224
    • Strauss, J.D.1    Bletz, C.2    Ruegg, J.C.3
  • 56
    • 0025061076 scopus 로고
    • Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: Implications for regulation of actin-myosin interaction
    • Sweeney HL and Stull JT (1990) Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction. Proc Natl Acad Sci USA 87: 414-418.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 414-418
    • Sweeney, H.L.1    Stull, J.T.2
  • 57
    • 0018340994 scopus 로고
    • A fluorimetric method for continuously assaying ATPase: Application to small specimens of glycerol-extracted muscle fibers
    • Takashi R and Putnam S (1979) A fluorimetric method for continuously assaying ATPase: application to small specimens of glycerol-extracted muscle fibers. Anal Biochem 92: 375-382.
    • (1979) Anal Biochem , vol.92 , pp. 375-382
    • Takashi, R.1    Putnam, S.2
  • 58
    • 0026097954 scopus 로고
    • Kinetic studies on the association and dissociation of myosin subfragment 1 and actin
    • Taylor EW (1991) Kinetic studies on the association and dissociation of myosin subfragment 1 and actin. J Biol Chem 266: 294-302.
    • (1991) J Biol Chem , vol.266 , pp. 294-302
    • Taylor, E.W.1
  • 60
    • 0026609631 scopus 로고
    • 2+ on the kinetics of phosphate release in skeletal muscle
    • 2+ on the kinetics of phosphate release in skeletal muscle. J Biol Chem 267: 2459-2466.
    • (1992) J Biol Chem , vol.267 , pp. 2459-2466
    • Walker, J.W.1    Lu, Z.2    Moss, R.L.3
  • 61
    • 0036088350 scopus 로고    scopus 로고
    • The off rate of Ca(2+) from troponin C is regulated by force-generating cross bridges in skeletal muscle
    • Wang Y and Kerrick WG (2002) The off rate of Ca(2+) from troponin C is regulated by force-generating cross bridges in skeletal muscle. J Appl Physiol 92: 2409-2418.
    • (2002) J Appl Physiol , vol.92 , pp. 2409-2418
    • Wang, Y.1    Kerrick, W.G.2
  • 62
    • 0033383559 scopus 로고    scopus 로고
    • Troponin C regulates the rate constant for the dissociation of force- Generating myosin cross-bridges in cardiac muscle
    • Wang Y, Xu Y, Guth K and Kerrick WG (1999) Troponin C regulates the rate constant for the dissociation of force- generating myosin cross-bridges in cardiac muscle. J Muscle Res Cell Motil 20: 645-653.
    • (1999) J Muscle Res Cell Motil , vol.20 , pp. 645-653
    • Wang, Y.1    Xu, Y.2    Guth, K.3    Kerrick, W.G.4
  • 64
    • 0027287625 scopus 로고
    • Kinetics of binding and hydrolysis of a series of nucleoside triphosphates by actomyosin-S1. Relationship between solution rate constants and properties of muscle fibers
    • White HD, Belknap B and Jiang W (1993) Kinetics of binding and hydrolysis of a series of nucleoside triphosphates by actomyosin-S1. Relationship between solution rate constants and properties of muscle fibers. J Biol Chem 268: 10,039-10,045.
    • (1993) J Biol Chem , vol.268 , pp. 10039-10045
    • White, H.D.1    Belknap, B.2    Jiang, W.3
  • 65
    • 0020000247 scopus 로고
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils. J Biol Chem 257: 7678-7683.
    • (1982) J Biol Chem , vol.257 , pp. 7678-7683
    • Zot, H.G.1    Potter, J.D.2


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