메뉴 건너뛰기




Volumn 6, Issue SEP, 2015, Pages

Potential molecular mechanisms underlying muscle fatigue mediated by reactive oxygen and nitrogen species

Author keywords

Fatigue; Muscle; Myosin; Reactive oxygen species; Tropomyosin; Troponin

Indexed keywords

CALCIUM ION; CONTRACTILE PROTEIN; MYOSIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE;

EID: 84944745220     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2015.00239     Document Type: Short Survey
Times cited : (45)

References (65)
  • 1
    • 61949405413 scopus 로고    scopus 로고
    • Fatigue in working muscles
    • Allen, D. G. (2009). Fatigue in working muscles. J. Appl. Physiol. 106, 358-359. doi: 10.1152/japplphysiol.91599.2008
    • (2009) J. Appl. Physiol , vol.106 , pp. 358-359
    • Allen, D.G.1
  • 2
    • 38349048508 scopus 로고    scopus 로고
    • Skeletal muscle fatigue: cellular mechanisms
    • Allen, D. G., Lamb, G. D., and Westerblad, H. (2008). Skeletal muscle fatigue: cellular mechanisms. Physiol. Rev. 88, 287-332. doi: 10.1152/physrev.00015.2007
    • (2008) Physiol. Rev , vol.88 , pp. 287-332
    • Allen, D.G.1    Lamb, G.D.2    Westerblad, H.3
  • 3
    • 0032103008 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide and dithiothreitol on contractile function of single skeletal muscle fibres from the mouse
    • Andrade, F. H., Reid, M. B., Allen, D. G., and Westerblad, H. (1998). Effect of hydrogen peroxide and dithiothreitol on contractile function of single skeletal muscle fibres from the mouse. J. Physiol. 509(Pt 2), 565-575. doi: 10.1111/j.1469-7793.1998.565bn.x
    • (1998) J. Physiol , vol.509 , pp. 565-575
    • Andrade, F.H.1    Reid, M.B.2    Allen, D.G.3    Westerblad, H.4
  • 4
    • 0035256776 scopus 로고    scopus 로고
    • Contractile response of skeletal muscle to low peroxide concentrations: myofibrillar calcium sensitivity as a likely target for redox-modulation
    • Andrade, F. H., Reid, M. B., and Westerblad, H. (2001). Contractile response of skeletal muscle to low peroxide concentrations: myofibrillar calcium sensitivity as a likely target for redox-modulation. FASEB J. 15, 309-311. doi: 10.1096/fj.00-0507fje
    • (2001) FASEB J , vol.15 , pp. 309-311
    • Andrade, F.H.1    Reid, M.B.2    Westerblad, H.3
  • 6
    • 0029785783 scopus 로고    scopus 로고
    • Effects of fatiguing stimulation on intracellular Na+ and K+ in frog skeletal muscle
    • Balog, E. M., and Fitts, R. H. (1996). Effects of fatiguing stimulation on intracellular Na+ and K+ in frog skeletal muscle. J. Appl. Physiol. (1985) 81, 679-685.
    • (1996) J. Appl. Physiol. (1985) , vol.81 , pp. 679-685
    • Balog, E.M.1    Fitts, R.H.2
  • 7
    • 0028305080 scopus 로고
    • Role of sarcolemma action potentials and excitability in muscle fatigue
    • Balog, E. M., Thompson, L. V., and Fitts, R. H. (1994). Role of sarcolemma action potentials and excitability in muscle fatigue. J. Appl. Physiol. (1985) 76, 2157-2162.
    • (1994) J. Appl. Physiol. (1985) , vol.76 , pp. 2157-2162
    • Balog, E.M.1    Thompson, L.V.2    Fitts, R.H.3
  • 9
    • 0024439203 scopus 로고
    • Changes in force and intracellular metabolites during fatigue of human skeletal muscle
    • Cady, E. B., Jones, D. A., Lynn, J., and Newham, D. J. (1989). Changes in force and intracellular metabolites during fatigue of human skeletal muscle. J. Physiol. 418, 311-325. doi: 10.1113/jphysiol.1989.sp017842
    • (1989) J. Physiol , vol.418 , pp. 311-325
    • Cady, E.B.1    Jones, D.A.2    Lynn, J.3    Newham, D.J.4
  • 10
    • 0035159587 scopus 로고    scopus 로고
    • Superoxide, hydroxyl radical, and hydrogen peroxide effects on single-diaphragm fiber contractile apparatus
    • Callahan, L. A., She, Z. W., and Nosek, T. M. (2001). Superoxide, hydroxyl radical, and hydrogen peroxide effects on single-diaphragm fiber contractile apparatus. J. Appl. Physiol. (1985) 90, 45-54.
    • (2001) J. Appl. Physiol. (1985) , vol.90 , pp. 45-54
    • Callahan, L.A.1    She, Z.W.2    Nosek, T.M.3
  • 11
    • 84921030936 scopus 로고    scopus 로고
    • Antioxidant treatments do not improve force recovery after fatiguing stimulation of mouse skeletal muscle fibres
    • Cheng, A. J., Bruton, J. D., Lanner, J. T., and Westerblad, H. (2015). Antioxidant treatments do not improve force recovery after fatiguing stimulation of mouse skeletal muscle fibres. J. Physiol. 593, 457-472. doi: 10.1113/jphysiol.2014.279398
    • (2015) J. Physiol , vol.593 , pp. 457-472
    • Cheng, A.J.1    Bruton, J.D.2    Lanner, J.T.3    Westerblad, H.4
  • 12
    • 37049000600 scopus 로고    scopus 로고
    • Modulation of the actomyosin interaction during fatigue of skeletal muscle
    • Cooke, R. (2007). Modulation of the actomyosin interaction during fatigue of skeletal muscle. Muscle Nerve 36, 756-777. doi: 10.1002/mus.20891
    • (2007) Muscle Nerve , vol.36 , pp. 756-777
    • Cooke, R.1
  • 13
    • 0035065484 scopus 로고    scopus 로고
    • Effects of reactive oxygen species on aspects of excitation-contraction coupling in chemically skinned rabbit diaphragm muscle fibres
    • Darnley, G. M., Duke, A. M., Steele, D. S., and MacFarlane, N. G. (2001). Effects of reactive oxygen species on aspects of excitation-contraction coupling in chemically skinned rabbit diaphragm muscle fibres. Exp. Physiol. 86, 161-168. doi: 10.1113/eph8602109
    • (2001) Exp. Physiol , vol.86 , pp. 161-168
    • Darnley, G.M.1    Duke, A.M.2    Steele, D.S.3    MacFarlane, N.G.4
  • 14
    • 84863982352 scopus 로고    scopus 로고
    • Recent insights into the molecular basis of muscular fatigue
    • Debold, E. P. (2012). Recent insights into the molecular basis of muscular fatigue. Med. Sci. Sports Exerc. 44, 1440-1452. doi: 10.1249/mss.0b013e31824cfd26
    • (2012) Med. Sci. Sports Exerc , vol.44 , pp. 1440-1452
    • Debold, E.P.1
  • 15
    • 0034871082 scopus 로고    scopus 로고
    • Hypoxia/fatigue-induced degradation of troponin I and troponin C: new insights into physiologic muscle fatigue
    • de Paula Brotto, M., van Leyen, S. A., Brotto, L. S., Jin, J. P., Nosek, C. M., and Nosek, T. M. (2001). Hypoxia/fatigue-induced degradation of troponin I and troponin C: new insights into physiologic muscle fatigue. Pflugers Arch. 442, 738-744. doi: 10.1007/s004240100587
    • (2001) Pflugers Arch , vol.442 , pp. 738-744
    • de Paula Brotto, M.1    van Leyen, S.A.2    Brotto, L.S.3    Jin, J.P.4    Nosek, C.M.5    Nosek, T.M.6
  • 16
    • 79954573855 scopus 로고    scopus 로고
    • Differential effects of peroxynitrite on contractile protein properties in fast-and slow-twitch skeletal muscle fibers of rat
    • Dutka, T. L., Mollica, J. P., and Lamb, G. D. (2011). Differential effects of peroxynitrite on contractile protein properties in fast-and slow-twitch skeletal muscle fibers of rat. J. Appl. Physiol. (1985) 110, 705-716. doi: 10.1152/japplphysiol.00739.2010
    • (2011) J. Appl. Physiol. (1985) , vol.110 , pp. 705-716
    • Dutka, T.L.1    Mollica, J.P.2    Lamb, G.D.3
  • 17
    • 37749005452 scopus 로고    scopus 로고
    • Muscle fatigue: what, why and how it influences muscle function
    • Enoka, R. M., and Duchateau, J. (2007). Muscle fatigue: what, why and how it influences muscle function. J. Physiol. 586, 11-23. doi: 10.1113/jphysiol.2007.139477
    • (2007) J. Physiol , vol.586 , pp. 11-23
    • Enoka, R.M.1    Duchateau, J.2
  • 18
    • 79957982990 scopus 로고    scopus 로고
    • Effectiveness of sulfur-containing antioxidants in delaying skeletal muscle fatigue
    • Ferreira, L. F., Campbell, K. S., and Reid, M. B. (2011). Effectiveness of sulfur-containing antioxidants in delaying skeletal muscle fatigue. Med. Sci. Sports Exerc. 43, 1025-1031. doi: 10.1249/MSS.0b013e3182019a78
    • (2011) Med. Sci. Sports Exerc , vol.43 , pp. 1025-1031
    • Ferreira, L.F.1    Campbell, K.S.2    Reid, M.B.3
  • 19
    • 41549110976 scopus 로고    scopus 로고
    • Muscle-derived ROS and thiol regulation in muscle fatigue
    • Ferreira, L. F., and Reid, M. B. (2008). Muscle-derived ROS and thiol regulation in muscle fatigue. J. Appl. Physiol. (1985) 104, 853-860. doi: 10.1152/japplphysiol.00953.2007
    • (2008) J. Appl. Physiol. (1985) , vol.104 , pp. 853-860
    • Ferreira, L.F.1    Reid, M.B.2
  • 20
    • 0028107645 scopus 로고
    • Cellular mechanisms of muscle fatigue
    • Fitts, R. H. (1994). Cellular mechanisms of muscle fatigue. Physiol. Rev. 74, 49-94.
    • (1994) Physiol. Rev , vol.74 , pp. 49-94
    • Fitts, R.H.1
  • 21
    • 0030460709 scopus 로고    scopus 로고
    • Muscle fatigue: the cellular aspects
    • Fitts, R. H. (1996). Muscle fatigue: the cellular aspects. Am. J. Sports Med. 24, S9-S13.
    • (1996) Am. J. Sports Med , vol.24 , pp. S9-S13
    • Fitts, R.H.1
  • 22
    • 33847660853 scopus 로고    scopus 로고
    • Use and abuse of exogenous H2O2 in studies of signal transduction
    • Forman, H. J. (2007). Use and abuse of exogenous H2O2 in studies of signal transduction. Free Radic. Biol. Med. 42, 926-932. doi: 10.1016/j.freeradbiomed.2007.01.011
    • (2007) Free Radic. Biol. Med , vol.42 , pp. 926-932
    • Forman, H.J.1
  • 23
    • 44349116066 scopus 로고    scopus 로고
    • Structural basis for the regulation of muscle contraction by troponin and tropomyosin
    • Galinska-Rakoczy, A., Engel, P., Xu, C., Jung, H., Craig, R., Tobacman, L. S., et al. (2008). Structural basis for the regulation of muscle contraction by troponin and tropomyosin. J. Mol. Biol. 379, 929-935. doi: 10.1016/j.jmb.2008.04.062
    • (2008) J. Mol. Biol , vol.379 , pp. 929-935
    • Galinska-Rakoczy, A.1    Engel, P.2    Xu, C.3    Jung, H.4    Craig, R.5    Tobacman, L.S.6
  • 24
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A. M., Homsher, E., and Regnier, M. (2000). Regulation of contraction in striated muscle. Physiol. Rev. 80, 853-924.
    • (2000) Physiol. Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 25
    • 84880448252 scopus 로고    scopus 로고
    • Accessibility of myofilament cysteines and effects on ATPase depend on the activation state during exposure to oxidants
    • Gross, S. M., and Lehman, S. L. (2013). Accessibility of myofilament cysteines and effects on ATPase depend on the activation state during exposure to oxidants. PLoS ONE 8:e69110. doi: 10.1371/journal.pone.0069110
    • (2013) PLoS ONE , vol.8
    • Gross, S.M.1    Lehman, S.L.2
  • 26
    • 84902462980 scopus 로고    scopus 로고
    • Cell culture, oxidative stress, and antioxidants: avoiding pitfalls
    • Halliwell, B. (2014). Cell culture, oxidative stress, and antioxidants: avoiding pitfalls. Biomed. J. 37, 99-105. doi: 10.4103/2319-4170.128725
    • (2014) Biomed. J , vol.37 , pp. 99-105
    • Halliwell, B.1
  • 27
    • 84866282500 scopus 로고    scopus 로고
    • Antioxidants and skeletal muscle performance: "common knowledge" vs. experimental evidence
    • Hern�ndez, A., Cheng, A., and Westerblad, H. (2012). Antioxidants and skeletal muscle performance: "common knowledge" vs. experimental evidence. Front. Physiol. 3:46. doi: 10.3389/fphys.2012.00046
    • (2012) Front. Physiol , vol.3 , pp. 46
    • Hern�ndez, A.1    Cheng, A.2    Westerblad, H.3
  • 28
    • 0023897239 scopus 로고
    • Muscle action potential propagation velocity changes during activity
    • Juel, C. (1988). Muscle action potential propagation velocity changes during activity. Muscle Nerve 11, 714-719. doi: 10.1002/mus.880110707
    • (1988) Muscle Nerve , vol.11 , pp. 714-719
    • Juel, C.1
  • 29
    • 84896734328 scopus 로고    scopus 로고
    • Effects of N-acetylcysteine on isolated mouse skeletal muscle: contractile properties, temperature dependence, and metabolism
    • Katz, A., Hern�ndez, A., Caballero, D. M., Briceno, J. F., Amezquita, L. V., Kosterina, N., et al. (2014). Effects of N-acetylcysteine on isolated mouse skeletal muscle: contractile properties, temperature dependence, and metabolism. Pflugers Arch. 466, 577-585. doi: 10.1007/s00424-013-1331-z
    • (2014) Pflugers Arch , vol.466 , pp. 577-585
    • Katz, A.1    Hern�ndez, A.2    Caballero, D.M.3    Briceno, J.F.4    Amezquita, L.V.5    Kosterina, N.6
  • 30
    • 81855199913 scopus 로고    scopus 로고
    • Structural and functional impact of site-directed methionine oxidation in myosin
    • Klein, J. C., Moen, R. J., Smith, E. A., Titus, M. A., and Thomas, D. D. (2011). Structural and functional impact of site-directed methionine oxidation in myosin. Biochemistry 50, 10318-10327. doi: 10.1021/bi201279u
    • (2011) Biochemistry , vol.50 , pp. 10318-10327
    • Klein, J.C.1    Moen, R.J.2    Smith, E.A.3    Titus, M.A.4    Thomas, D.D.5
  • 31
    • 0037232657 scopus 로고    scopus 로고
    • Effects of oxidation and reduction on contractile function in skeletal muscle fibres of the rat
    • Lamb, G. D., and Posterino, G. S. (2003). Effects of oxidation and reduction on contractile function in skeletal muscle fibres of the rat. J. Physiol. 546, 149-163. doi: 10.1113/jphysiol.2002.027896
    • (2003) J. Physiol , vol.546 , pp. 149-163
    • Lamb, G.D.1    Posterino, G.S.2
  • 32
    • 0025972457 scopus 로고
    • Changes in tetanic and resting [Ca2+]i during fatigue and recovery of single muscle fibres from Xenopus laevis
    • Lee, J. A., Westerblad, H., and Allen, D. G. (1991). Changes in tetanic and resting [Ca2+]i during fatigue and recovery of single muscle fibres from Xenopus laevis. J. Physiol. 433, 307-326. doi: 10.1113/jphysiol.1991.sp018427
    • (1991) J. Physiol , vol.433 , pp. 307-326
    • Lee, J.A.1    Westerblad, H.2    Allen, D.G.3
  • 33
    • 0026508552 scopus 로고
    • Depression of peak force without altering calcium sensitivity by the superoxide anion in chemically skinned cardiac muscle of rat
    • MacFarlane, N. G., and Miller, D. J. (1992). Depression of peak force without altering calcium sensitivity by the superoxide anion in chemically skinned cardiac muscle of rat. Circ. Res. 70, 1217-1224. doi: 10.1161/01.RES.70.6.1217
    • (1992) Circ. Res , vol.70 , pp. 1217-1224
    • MacFarlane, N.G.1    Miller, D.J.2
  • 34
    • 0031951413 scopus 로고    scopus 로고
    • Sulfhydryl oxidation modifies the calcium dependence of ryanodine-sensitive calcium channels of excitable cells
    • Marengo, J. J., Hidalgo, C., and Bull, R. (1998). Sulfhydryl oxidation modifies the calcium dependence of ryanodine-sensitive calcium channels of excitable cells. Biophys. J. 74, 1263-1277. doi: 10.1016/S0006-3495(98)77840-3
    • (1998) Biophys. J , vol.74 , pp. 1263-1277
    • Marengo, J.J.1    Hidalgo, C.2    Bull, R.3
  • 35
    • 33748905385 scopus 로고    scopus 로고
    • N-acetylcysteine attenuates the decline in muscle Na+,K+-pump activity and delays fatigue during prolonged exercise in humans
    • McKenna, M. J., Medved, I., Goodman, C. A., Brown, M. J., Bjorksten, A. R., Murphy, K. T., et al. (2006). N-acetylcysteine attenuates the decline in muscle Na+,K+-pump activity and delays fatigue during prolonged exercise in humans. J. Physiol. 576, 279-288. doi: 10.1113/jphysiol.2006.115352
    • (2006) J. Physiol , vol.576 , pp. 279-288
    • McKenna, M.J.1    Medved, I.2    Goodman, C.A.3    Brown, M.J.4    Bjorksten, A.R.5    Murphy, K.T.6
  • 36
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1, evidence for three states of the thin filament
    • McKillop, D. F., and Geeves, M. A. (1993). Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 65, 693-701. doi: 10.1016/S0006-3495(93)81110-X
    • (1993) Biophys. J , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 37
    • 4644240045 scopus 로고    scopus 로고
    • N-acetylcysteine enhances muscle cysteine and glutathione availability and attenuates fatigue during prolonged exercise in endurance-trained individuals
    • Medved, I., Brown, M. J., Bjorksten, A. R., Murphy, K. T., Petersen, A. C., Sostaric, S., et al. (2004). N-acetylcysteine enhances muscle cysteine and glutathione availability and attenuates fatigue during prolonged exercise in endurance-trained individuals. J. Appl. Physiol (1985) 97, 1477-1485. doi: 10.1152/japplphysiol.00371.2004
    • (2004) J. Appl. Physiol (1985) , vol.97 , pp. 1477-1485
    • Medved, I.1    Brown, M.J.2    Bjorksten, A.R.3    Murphy, K.T.4    Petersen, A.C.5    Sostaric, S.6
  • 38
    • 77049171076 scopus 로고
    • Voluntary strength and fatigue
    • Merton, P. A. (1954). Voluntary strength and fatigue. J. Physiol. 123, 553-564. doi: 10.1113/jphysiol.1954.sp005070
    • (1954) J. Physiol , vol.123 , pp. 553-564
    • Merton, P.A.1
  • 40
    • 84891827279 scopus 로고    scopus 로고
    • Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins
    • Moen, R. J., Klein, J. C., and Thomas, D. D. (2014b). Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins. Exerc. Sport Sci. Rev. 42, 30-36. doi: 10.1249/JES.0000000000000004
    • (2014) Exerc. Sport Sci. Rev , vol.42 , pp. 30-36
    • Moen, R.J.1    Klein, J.C.2    Thomas, D.D.3
  • 41
    • 84858226713 scopus 로고    scopus 로고
    • S-glutathionylation of troponin I (fast) increases contractile apparatus Ca2+ sensitivity in fast-twitch muscle fibres of rats and humans
    • Mollica, J. P., Dutka, T. L., Merry, T. L., Lamboley, C. R., McConell, G. K., McKenna, M. J., et al. (2012). S-glutathionylation of troponin I (fast) increases contractile apparatus Ca2+ sensitivity in fast-twitch muscle fibres of rats and humans. J. Physiol. 590, 1443-1463. doi: 10.1113/jphysiol.2011.224535
    • (2012) J. Physiol , vol.590 , pp. 1443-1463
    • Mollica, J.P.1    Dutka, T.L.2    Merry, T.L.3    Lamboley, C.R.4    McConell, G.K.5    McKenna, M.J.6
  • 42
    • 17444408539 scopus 로고    scopus 로고
    • Reactive oxygen species reduce myofibrillar Ca2+ sensitivity in fatiguing mouse skeletal muscle at 37 degrees C
    • Moopanar, T. R., and Allen, D. G. (2005). Reactive oxygen species reduce myofibrillar Ca2+ sensitivity in fatiguing mouse skeletal muscle at 37 degrees C. J. Physiol. 564, 189-199. doi: 10.1113/jphysiol.2005.083519
    • (2005) J. Physiol , vol.564 , pp. 189-199
    • Moopanar, T.R.1    Allen, D.G.2
  • 43
    • 33645880764 scopus 로고    scopus 로고
    • The activity-induced reduction of myofibrillar Ca2+ sensitivity in mouse skeletal muscle is reversed by dithiothreitol
    • Moopanar, T. R., and Allen, D. G. (2006). The activity-induced reduction of myofibrillar Ca2+ sensitivity in mouse skeletal muscle is reversed by dithiothreitol. J. Physiol. 571, 191-200. doi: 10.1113/jphysiol.2005.101105
    • (2006) J. Physiol , vol.571 , pp. 191-200
    • Moopanar, T.R.1    Allen, D.G.2
  • 44
    • 79551589217 scopus 로고    scopus 로고
    • Redox state of troponin C cysteine in the D/E helix alters the C-domain affinity for the thin filament of vertebrate striated muscle
    • Pinto, J. R., de Sousa, V. P., and Sorenson, M. M. (2011). Redox state of troponin C cysteine in the D/E helix alters the C-domain affinity for the thin filament of vertebrate striated muscle. Biochim. Biophys. Acta 1810, 391-397. doi: 10.1016/j.bbagen.2010.11.008
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 391-397
    • Pinto, J.R.1    de Sousa, V.P.2    Sorenson, M.M.3
  • 45
    • 70350396980 scopus 로고    scopus 로고
    • High temperature does not alter fatigability in intact mouse skeletal muscle fibres
    • Place, N., Yamada, T., Zhang, S. J., Westerblad, H., and Bruton, J. D. (2009). High temperature does not alter fatigability in intact mouse skeletal muscle fibres. J. Physiol. 587, 4717-4724. doi: 10.1113/jphysiol.2009.176883
    • (2009) J. Physiol , vol.587 , pp. 4717-4724
    • Place, N.1    Yamada, T.2    Zhang, S.J.3    Westerblad, H.4    Bruton, J.D.5
  • 46
    • 0037444666 scopus 로고    scopus 로고
    • Effects of oxidation and cytosolic redox conditions on excitation-contraction coupling in rat skeletal muscle
    • Posterino, G. S., Cellini, M. A., and Lamb, G. D. (2003). Effects of oxidation and cytosolic redox conditions on excitation-contraction coupling in rat skeletal muscle. J. Physiol. 547, 807-823. doi: 10.1113/jphysiol.2002.035204
    • (2003) J. Physiol , vol.547 , pp. 807-823
    • Posterino, G.S.1    Cellini, M.A.2    Lamb, G.D.3
  • 47
    • 80051667908 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress in humans: cause and consequences
    • Powers, S. K., Nelson, W. B., and Hudson, M. B. (2011). Exercise-induced oxidative stress in humans: cause and consequences. Free Radic. Biol. Med. 51, 942-950. doi: 10.1016/j.freeradbiomed.2010.12.009
    • (2011) Free Radic. Biol. Med , vol.51 , pp. 942-950
    • Powers, S.K.1    Nelson, W.B.2    Hudson, M.B.3
  • 48
    • 55849141926 scopus 로고    scopus 로고
    • Changes in actin structural transitions associated with oxidative inhibition of muscle contraction
    • Prochniewicz, E., Spakowicz, D., and Thomas, D. D. (2008). Changes in actin structural transitions associated with oxidative inhibition of muscle contraction. Biochemistry 47, 11811-11817. doi: 10.1021/bi801080x
    • (2008) Biochemistry , vol.47 , pp. 11811-11817
    • Prochniewicz, E.1    Spakowicz, D.2    Thomas, D.D.3
  • 49
    • 65649152969 scopus 로고    scopus 로고
    • Iron injections in mice increase skeletal muscle iron content, induce oxidative stress and reduce exercise performance
    • Reardon, T. F., and Allen, D. G. (2009a). Iron injections in mice increase skeletal muscle iron content, induce oxidative stress and reduce exercise performance. Exp. Physiol. 94, 720-730. doi: 10.1113/expphysiol.2008.046045
    • (2009) Exp. Physiol , vol.94 , pp. 720-730
    • Reardon, T.F.1    Allen, D.G.2
  • 50
    • 70350397898 scopus 로고    scopus 로고
    • Time to fatigue is increased in mouse muscle at 37 degrees C; the role of iron and reactive oxygen species
    • Reardon, T. F., and Allen, D. G. (2009b). Time to fatigue is increased in mouse muscle at 37 degrees C; the role of iron and reactive oxygen species. J. Physiol. 587, 4705-4716. doi: 10.1113/jphysiol.2009.173005
    • (2009) J. Physiol , vol.587 , pp. 4705-4716
    • Reardon, T.F.1    Allen, D.G.2
  • 51
    • 0035143723 scopus 로고    scopus 로고
    • Invited Review: redox modulation of skeletal muscle contraction: what we know and what we don't
    • Reid, M. B. (2001a). Invited Review: redox modulation of skeletal muscle contraction: what we know and what we don't. J. Appl. Physiol. (1985) 90, 724-731.
    • (2001) J. Appl. Physiol. (1985) , vol.90 , pp. 724-731
    • Reid, M.B.1
  • 52
    • 0035092313 scopus 로고    scopus 로고
    • Nitric oxide, reactive oxygen species, and skeletal muscle contraction
    • Reid, M. B. (2001b). Nitric oxide, reactive oxygen species, and skeletal muscle contraction. Med. Sci. Sports Exerc. 33, 371-376. doi: 10.1097/00005768-200103000-00006
    • (2001) Med. Sci. Sports Exerc , vol.33 , pp. 371-376
    • Reid, M.B.1
  • 53
    • 0027948093 scopus 로고
    • N-acetylcysteine inhibits muscle fatigue in humans
    • Reid, M. B., Stokic, D. S., Koch, S. M., Khawli, F. A., and Leis, A. A. (1994). N-acetylcysteine inhibits muscle fatigue in humans. J. Clin. Invest. 94, 2468-2474. doi: 10.1172/JCI117615
    • (1994) J. Clin. Invest , vol.94 , pp. 2468-2474
    • Reid, M.B.1    Stokic, D.S.2    Koch, S.M.3    Khawli, F.A.4    Leis, A.A.5
  • 54
    • 80052820002 scopus 로고    scopus 로고
    • Role of superoxide-nitric oxide interactions in the accelerated age-related loss of muscle mass in mice lacking Cu, Zn superoxide dismutase
    • Sakellariou, G. K., Pye, D., Vasilaki, A., Zibrik, L., Palomero, J., Kabayo, T., et al. (2011). Role of superoxide-nitric oxide interactions in the accelerated age-related loss of muscle mass in mice lacking Cu, Zn superoxide dismutase. Aging Cell 10, 749-760. doi: 10.1111/j.1474-9726.2011.00709.x
    • (2011) Aging Cell , vol.10 , pp. 749-760
    • Sakellariou, G.K.1    Pye, D.2    Vasilaki, A.3    Zibrik, L.4    Palomero, J.5    Kabayo, T.6
  • 55
    • 84872433353 scopus 로고    scopus 로고
    • Studies of mitochondrial and nonmitochondrial sources implicate nicotinamide adenine dinucleotide phosphate oxidase(s) in the increased skeletal muscle superoxide generation that occurs during contractile activity
    • Sakellariou, G. K., Vasilaki, A., Palomero, J., Kayani, A., Zibrik, L., McArdle, A., et al. (2013). Studies of mitochondrial and nonmitochondrial sources implicate nicotinamide adenine dinucleotide phosphate oxidase(s) in the increased skeletal muscle superoxide generation that occurs during contractile activity. Antioxid. Redox. Signal. 18, 603-621. doi: 10.1089/ars.2012.4623
    • (2013) Antioxid. Redox. Signal , vol.18 , pp. 603-621
    • Sakellariou, G.K.1    Vasilaki, A.2    Palomero, J.3    Kayani, A.4    Zibrik, L.5    McArdle, A.6
  • 57
    • 84901301773 scopus 로고    scopus 로고
    • Effect of N-acetylcysteine on cycling performance after intensified training
    • Slattery, K. M., Dascombe, B., Wallace, L. K., Bentley, D. J., and Coutts, A. J. (2014). Effect of N-acetylcysteine on cycling performance after intensified training. Med. Sci. Sports Exerc. 46, 1114-1123. doi: 10.1249/MSS.0000000000000222
    • (2014) Med. Sci. Sports Exerc , vol.46 , pp. 1114-1123
    • Slattery, K.M.1    Dascombe, B.2    Wallace, L.K.3    Bentley, D.J.4    Coutts, A.J.5
  • 58
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre, J., Buckingham, J. A., Roebuck, S. J., and Brand, M. D. (2002). Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277, 44784-44790. doi: 10.1074/jbc.M207217200
    • (2002) J. Biol. Chem , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 59
    • 0035949671 scopus 로고    scopus 로고
    • Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
    • Sun, J., Xin, C., Eu, J. P., Stamler, J. S., and Meissner, G. (2001). Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO. Proc. Natl. Acad. Sci.U.S.A. 98, 11158-11162. doi: 10.1073/pnas.201289098
    • (2001) Proc. Natl. Acad. Sci.U.S.A , vol.98 , pp. 11158-11162
    • Sun, J.1    Xin, C.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 60
    • 0037424471 scopus 로고    scopus 로고
    • Nitric oxide, NOC-12, and S-nitrosoglutathione modulate the skeletal muscle calcium release channel/ryanodine receptor by different mechanisms. An allosteric function for O2 in S-nitrosylation of the channel
    • Sun, J., Xu, L., Eu, J. P., Stamler, J. S., and Meissner, G. (2003). Nitric oxide, NOC-12, and S-nitrosoglutathione modulate the skeletal muscle calcium release channel/ryanodine receptor by different mechanisms. An allosteric function for O2 in S-nitrosylation of the channel. J. Biol. Chem. 278, 8184-8189. doi: 10.1074/jbc.M211940200
    • (2003) J. Biol. Chem , vol.278 , pp. 8184-8189
    • Sun, J.1    Xu, L.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 61
    • 0037588762 scopus 로고    scopus 로고
    • Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form
    • Takeda, S., Yamashita, A., Maeda, K., and Ma�da, Y. (2003). Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. Nature 424, 35-41. doi: 10.1038/nature01780
    • (2003) Nature , vol.424 , pp. 35-41
    • Takeda, S.1    Yamashita, A.2    Maeda, K.3    Ma�da, Y.4
  • 62
    • 0036850893 scopus 로고    scopus 로고
    • (2+)-activation properties of rat skeletal muscle exposed to elevated physiological temperatures
    • (2+)-activation properties of rat skeletal muscle exposed to elevated physiological temperatures. J. Physiol. 544, 765-776. doi: 10.1113/jphysiol.2002.024968
    • (2002) J. Physiol , vol.544 , pp. 765-776
    • van der Poel, C.1    Stephenson, D.G.2
  • 63
    • 34547115458 scopus 로고    scopus 로고
    • Effects of elevated physiological temperatures on sarcoplasmic reticulum function in mechanically skinned muscle fibers of the rat
    • van der Poel, C., and Stephenson, D. G. (2007). Effects of elevated physiological temperatures on sarcoplasmic reticulum function in mechanically skinned muscle fibers of the rat. Am. J. Physiol. Cell Physiol. 293, C133-C141. doi: 10.1152/ajpcell.00052.2007
    • (2007) Am. J. Physiol. Cell Physiol , vol.293 , pp. C133-C141
    • van der Poel, C.1    Stephenson, D.G.2
  • 64
    • 80052985519 scopus 로고    scopus 로고
    • Emerging roles of ROS/RNS in muscle function and fatigue
    • Westerblad, H., and Allen, D. G. (2011). Emerging roles of ROS/RNS in muscle function and fatigue. Antioxid. Redox. Signal. 15, 2487-2499. doi: 10.1089/ars.2011.3909
    • (2011) Antioxid. Redox. Signal , vol.15 , pp. 2487-2499
    • Westerblad, H.1    Allen, D.G.2
  • 65


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.