메뉴 건너뛰기




Volumn 51, Issue 5, 2011, Pages 942-950

Exercise-induced oxidative stress in humans: Cause and consequences

Author keywords

Free radicals; Mitochondria; Muscle fatigue; Reactive oxygen species; Skeletal muscle

Indexed keywords

ACETYLCYSTEINE; ALPHA TOCOPHEROL; ANTIOXIDANT; ARACHIDONIC ACID; ASCORBIC ACID; HEAT SHOCK PROTEIN 72; HYDROGEN PEROXIDE; HYDROQUINONE; HYDROXYL RADICAL; MYOSIN HEAVY CHAIN; NITRIC OXIDE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1BETA; PHOSPHOLIPASE A2; QUERCETIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; RYANODINE RECEPTOR; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; TROPONIN C; XANTHINE OXIDASE;

EID: 80051667908     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.12.009     Document Type: Review
Times cited : (347)

References (160)
  • 1
    • 32444433202 scopus 로고    scopus 로고
    • Free radicals, metals and antioxidants in oxidative stress-induced cancer
    • DOI 10.1016/j.cbi.2005.12.009, PII S0009279705004333
    • M. Valko, C.J. Rhodes, J. Moncol, M. Izakovic, and M. Mazur Free radicals, metals and antioxidants in oxidative stress-induced cancer Chem. Biol. Interact. 160 2006 1 40 (Pubitemid 43227479)
    • (2006) Chemico-Biological Interactions , vol.160 , Issue.1 , pp. 1-40
    • Valko, M.1    Rhodes, C.J.2    Moncol, J.3    Izakovic, M.4    Mazur, M.5
  • 2
    • 0037217892 scopus 로고    scopus 로고
    • Regulation of cancer metastasis by stress pathways
    • DOI 10.1023/A:1022590402748
    • K. Xie, and S. Huang Regulation of cancer metastasis by stress pathways Clin. Exp. Metastasis 20 2003 31 43 (Pubitemid 36308134)
    • (2003) Clinical and Experimental Metastasis , vol.20 , Issue.1 , pp. 31-43
    • Xie, K.1    Huang, S.2
  • 3
    • 70350700901 scopus 로고    scopus 로고
    • Oxidative stress, diabetes, and diabetic complications
    • W. Wei, Q. Liu, Y. Tan, L. Liu, X. Li, and L. Cai Oxidative stress, diabetes, and diabetic complications Hemoglobin 33 2009 370 377
    • (2009) Hemoglobin , vol.33 , pp. 370-377
    • Wei, W.1    Liu, Q.2    Tan, Y.3    Liu, L.4    Li, X.5    Cai, L.6
  • 4
    • 67649678412 scopus 로고    scopus 로고
    • Oxidative stress in diabetes and Alzheimer's disease
    • V.P. Reddy, X. Zhu, G. Perry, and M.A. Smith Oxidative stress in diabetes and Alzheimer's disease J. Alzheimers Dis. 16 2009 763 774
    • (2009) J. Alzheimers Dis. , vol.16 , pp. 763-774
    • Reddy, V.P.1    Zhu, X.2    Perry, G.3    Smith, M.A.4
  • 5
    • 40749093652 scopus 로고    scopus 로고
    • Role of physical activity in diabetes management and prevention
    • C. Hayes, and A. Kriska Role of physical activity in diabetes management and prevention J. Am. Diet. Assoc. 108 2008 S19 S23
    • (2008) J. Am. Diet. Assoc. , vol.108
    • Hayes, C.1    Kriska, A.2
  • 6
    • 72449194805 scopus 로고    scopus 로고
    • Exercise training, lipid regulation, and insulin action: A tangled web of cause and effect
    • W.E. Kraus, and C.A. Slentz Exercise training, lipid regulation, and insulin action: a tangled web of cause and effect Obesity (Silver Spring) 17 Suppl. 3 2009 S21 S26
    • (2009) Obesity (Silver Spring) , vol.17 , Issue.SUPPL. 3
    • Kraus, W.E.1    Slentz, C.A.2
  • 7
    • 0033782023 scopus 로고    scopus 로고
    • Sedentary habits, health, and function in older women and men
    • S.N. Blair, and M. Wei Sedentary habits, health, and function in older women and men Am. J. Health Promot. 15 2000 1 8
    • (2000) Am. J. Health Promot. , vol.15 , pp. 1-8
    • Blair, S.N.1    Wei, M.2
  • 8
    • 0035012889 scopus 로고    scopus 로고
    • Is physical activity or physical fitness more important in defining health benefits?
    • discussion S419-320
    • S.N. Blair, Y. Cheng, and J.S. Holder Is physical activity or physical fitness more important in defining health benefits? Med. Sci. Sports Exerc. 33 2001 S379 S399 discussion S419-320
    • (2001) Med. Sci. Sports Exerc. , vol.33
    • Blair, S.N.1    Cheng, Y.2    Holder, J.S.3
  • 10
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W. Droge Free radicals in the physiological control of cell function Physiol. Rev. 82 2002 47 95 (Pubitemid 34654215)
    • (2002) Physiological Reviews , vol.82 , Issue.1 , pp. 47-95
    • Droge, W.1
  • 11
    • 77749254802 scopus 로고    scopus 로고
    • P38 MAPK links oxidative stress to autophagy-related gene expression in cachectic muscle wasting
    • J.M. McClung, A.R. Judge, S.K. Powers, and Z. Yan p38 MAPK links oxidative stress to autophagy-related gene expression in cachectic muscle wasting Am. J. Physiol. Cell Physiol. 298 2010 C542 C549
    • (2010) Am. J. Physiol. Cell Physiol. , vol.298
    • McClung, J.M.1    Judge, A.R.2    Powers, S.K.3    Yan, Z.4
  • 13
    • 74049129489 scopus 로고    scopus 로고
    • Reactive oxygen species are signalling molecules for skeletal muscle adaptation
    • S.K. Powers, J. Duarte, A.N. Kavazis, and E.E. Talbert Reactive oxygen species are signalling molecules for skeletal muscle adaptation Exp. Physiol. 95 2010 1 9
    • (2010) Exp. Physiol. , vol.95 , pp. 1-9
    • Powers, S.K.1    Duarte, J.2    Kavazis, A.N.3    Talbert, E.E.4
  • 14
    • 55949118714 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress: Cellular mechanisms and impact on muscle force production
    • S.K. Powers, and M.J. Jackson Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production Physiol. Rev. 88 2008 1243 1276
    • (2008) Physiol. Rev. , vol.88 , pp. 1243-1276
    • Powers, S.K.1    Jackson, M.J.2
  • 16
    • 0842346333 scopus 로고    scopus 로고
    • Free radical biology - Terminology and critical thinking
    • DOI 10.1016/S0014-5793(03)01526-6
    • A. Azzi, K.J.A. Davies, and F. Kelly Free radical biology-terminology and critical thinking FEBS Lett. 558 2004 3 6 (Pubitemid 38167400)
    • (2004) FEBS Letters , vol.558 , Issue.1-3 , pp. 3-6
    • Azzi, A.1    Davies, K.J.A.2    Kelly, F.3
  • 17
    • 33744962865 scopus 로고    scopus 로고
    • Redefining oxidative stress
    • DOI 10.1089/ars.2006.8.1865
    • D.P. Jones Redefining oxidative stress Antioxid. Redox Signaling 8 2006 1865 1879 (Pubitemid 44726359)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.9-10 , pp. 1865-1879
    • Jones, D.P.1
  • 18
    • 84882816411 scopus 로고    scopus 로고
    • Oxidative stress
    • G. Fink, Elsevier Amsterdam
    • H. Sies, and D. Jones Oxidative stress G. Fink, Encyclopedia of Stress 2007 Elsevier Amsterdam 45 48
    • (2007) Encyclopedia of Stress , pp. 45-48
    • Sies, H.1    Jones, D.2
  • 20
    • 0028258398 scopus 로고
    • Metabolic and antioxidant enzyme activities in the diaphragm: Effects of acute exercise
    • J.M. Lawler, S.K. Powers, H. Van Dijk, T. Visser, M.J. Kordus, and L.L. Ji Metabolic and antioxidant enzyme activities in the diaphragm: effects of acute exercise Respir. Physiol. 96 1994 139 149 (Pubitemid 24135393)
    • (1994) Respiration Physiology , vol.96 , Issue.2-3 , pp. 139-149
    • Lawler, J.M.1    Powers, S.K.2    Van Dijk, H.3    Visser, T.4    Kordus, M.J.5    Ji, L.L.6
  • 26
    • 0027730593 scopus 로고
    • Acute exercise and skeletal muscle antioxidant and metabolic enzymes: Effects of fiber type and age
    • J.M. Lawler, S.K. Powers, T. Visser, H. Van Dijk, M.J. Kordus, and L.L. Ji Acute exercise and skeletal muscle antioxidant and metabolic enzymes: effects of fiber type and age Am. J. Physiol. 265 1993 R1344 R1350
    • (1993) Am. J. Physiol. , vol.265
    • Lawler, J.M.1    Powers, S.K.2    Visser, T.3    Van Dijk, H.4    Kordus, M.J.5    Ji, L.L.6
  • 27
    • 70349840473 scopus 로고    scopus 로고
    • Blood as a reactive species generator and redox status regulator during exercise
    • M.G. Nikolaidis, and A.Z. Jamurtas Blood as a reactive species generator and redox status regulator during exercise Arch. Biochem. Biophys. 490 2009 77 84
    • (2009) Arch. Biochem. Biophys. , vol.490 , pp. 77-84
    • Nikolaidis, M.G.1    Jamurtas, A.Z.2
  • 28
    • 1442290124 scopus 로고    scopus 로고
    • Overexpression of HSP70 in mouse skeletal muscle protects against muscle damage and age-related muscle dysfunction
    • A. McArdle, W.H. Dillmann, R. Mestril, J.A. Faulkner, and M.J. Jackson Overexpression of HSP70 in mouse skeletal muscle protects against muscle damage and age-related muscle dysfunction FASEB J. 18 2004 355 357
    • (2004) FASEB J. , vol.18 , pp. 355-357
    • McArdle, A.1    Dillmann, W.H.2    Mestril, R.3    Faulkner, J.A.4    Jackson, M.J.5
  • 29
    • 0023269405 scopus 로고
    • Current concepts: Immunology - Neutrophils in human diseases
    • H.L. Malech, and J.I. Gallin Current concepts: immunology. Neutrophils in human diseases N. Engl. J. Med. 317 1987 687 694 (Pubitemid 17138195)
    • (1987) New England Journal of Medicine , vol.317 , Issue.11 , pp. 687-694
    • Malech, H.L.1    Gallin, J.I.2
  • 30
    • 0001812997 scopus 로고    scopus 로고
    • Free radical chemistry
    • C.K. Sen, L. Packer, O. Hanninen, Elsevier Amsterdam
    • K.D. Asmus, and M. Bonifacic Free radical chemistry C.K. Sen, L. Packer, O. Hanninen, Handbook of Oxidants and Antioxidants 2000 Elsevier Amsterdam 3 54
    • (2000) Handbook of Oxidants and Antioxidants , pp. 3-54
    • Asmus, K.D.1    Bonifacic, M.2
  • 31
    • 41549110976 scopus 로고    scopus 로고
    • Muscle-derived ROS and thiol regulation in muscle fatigue
    • DOI 10.1152/japplphysiol.00953.2007
    • L.F. Ferreira, and M.B. Reid Muscle-derived ROS and thiol regulation in muscle fatigue J. Appl. Physiol. 104 2008 853 860 (Pubitemid 351468816)
    • (2008) Journal of Applied Physiology , vol.104 , Issue.3 , pp. 853-860
    • Ferreira, L.F.1    Reid, M.B.2
  • 33
    • 34347379422 scopus 로고    scopus 로고
    • Hypoxia-induced reactive oxygen species formation in skeletal muscle
    • DOI 10.1152/japplphysiol.01298.2006
    • T.L. Clanton Hypoxia-induced reactive oxygen species formation in skeletal muscle J. Appl. Physiol. 102 2007 2379 2388 (Pubitemid 47082406)
    • (2007) Journal of Applied Physiology , vol.102 , Issue.6 , pp. 2379-2388
    • Clanton, T.L.1
  • 36
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide: General properties and effect of hyperbaric oxygen
    • A. Boveris, and B. Chance The mitochondrial generation of hydrogen peroxide: general properties and effect of hyperbaric oxygen Biochem. J. 134 1973 707 716
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 37
    • 0016148483 scopus 로고
    • Superoxide radicals as precursors of mitochondrial hydrogen peroxide
    • G. Loschen, A. Azzi, C. Richter, and L. Flohe Superoxide radicals as precursors of mitochondrial hydrogen peroxide FEBS Lett. 42 1974 68 72
    • (1974) FEBS Lett. , vol.42 , pp. 68-72
    • Loschen, G.1    Azzi, A.2    Richter, C.3    Flohe, L.4
  • 38
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in States 4 and 3, organ specificity, and relation to aging and longevity
    • DOI 10.1023/A:1005427919188
    • G. Barja Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity J. Bioenerg. Biomembr. 31 1999 347 366 (Pubitemid 30058570)
    • (1999) Journal of Bioenergetics and Biomembranes , vol.31 , Issue.4 , pp. 347-366
    • Barja, G.1
  • 39
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • DOI 10.1074/jbc.M407715200
    • F.L. Muller, Y. Liu, and H. Van Remmen Complex III releases superoxide to both sides of the inner mitochondrial membrane J. Biol. Chem. 279 2004 49064 49073 (Pubitemid 39625788)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 40
    • 0029197575 scopus 로고
    • Free radicals and exercise: Effects of nutritional antioxidant supplementation
    • M. Kanter Free radicals and exercise: effects of nutritional antioxidant supplementation Exerc. Sport Sci. Rev. 23 1995 375 397
    • (1995) Exerc. Sport Sci. Rev. , vol.23 , pp. 375-397
    • Kanter, M.1
  • 41
    • 0038342017 scopus 로고    scopus 로고
    • Oxidative stress, exercise, and antioxidant supplementation
    • DOI 10.1016/S0300-483X(03)00151-3
    • M.L. Urso, and P.M. Clarkson Oxidative stress, exercise, and antioxidant supplementation Toxicology 189 2003 41 54 (Pubitemid 36733566)
    • (2003) Toxicology , vol.189 , Issue.1-2 , pp. 41-54
    • Urso, M.L.1    Clarkson, P.M.2
  • 42
    • 34147142547 scopus 로고    scopus 로고
    • The production of reactive oxygen and nitrogen species by skeletal muscle
    • DOI 10.1152/japplphysiol.01102.2006
    • M.J. Jackson, D. Pye, and J. Palomero The production of reactive oxygen and nitrogen species by skeletal muscle J. Appl. Physiol. 102 2007 1664 1670 (Pubitemid 46571066)
    • (2007) Journal of Applied Physiology , vol.102 , Issue.4 , pp. 1664-1670
    • Jackson, M.J.1    Pye, D.2    Palomero, J.3
  • 43
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • DOI 10.1074/jbc.M207217200
    • J. St-Pierre, J.A. Buckingham, S.J. Roebuck, and M.D. Brand Topology of superoxide production from different sites in the mitochondrial electron transport chain J. Biol. Chem. 277 2002 44784 44790 (Pubitemid 36159072)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 45
    • 0035109274 scopus 로고    scopus 로고
    • Mitochondria in exercise-induced oxidative stress
    • S. Di Meo, and P. Venditti Mitochondria in exercise-induced oxidative stress Biol. Signals Recept. 10 2001 125 140 (Pubitemid 32171163)
    • (2001) Biological Signals and Receptors , vol.10 , Issue.1-2 , pp. 125-140
    • Di Meo, S.1    Venditti, P.2
  • 46
    • 0030874890 scopus 로고    scopus 로고
    • ADP-Regulation of mitochondrial free radical production is different with complex I- or complex II-linked substrates: Implications for the exercise paradox and brain hypermetabolism
    • DOI 10.1023/A:1022458010266
    • A. Herrero, and G. Barja ADP-regulation of mitochondrial free radical production is different with complex I- or complex II-linked substrates: implications for the exercise paradox and brain hypermetabolism J. Bioenerg. Biomembr. 29 1997 241 249 (Pubitemid 27371725)
    • (1997) Journal of Bioenergetics and Biomembranes , vol.29 , Issue.3 , pp. 241-249
    • Herrero, A.1    Barja, G.2
  • 47
    • 25444500448 scopus 로고    scopus 로고
    • Differential susceptibility of subsarcolemmal and intermyofibrillar mitochondria to apoptotic stimuli
    • P.J. Adhihetty, V. Ljubicic, K.J. Menzies, and D.A. Hood Differential susceptibility of subsarcolemmal and intermyofibrillar mitochondria to apoptotic stimuli Am. J. Physiol. Cell Physiol. 289 2005 C994 C1001
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289
    • Adhihetty, P.J.1    Ljubicic, V.2    Menzies, K.J.3    Hood, D.A.4
  • 50
    • 37849035153 scopus 로고    scopus 로고
    • Free radicals generated by contracting muscle: By-products of metabolism or key regulators of muscle function?
    • M.J. Jackson Free radicals generated by contracting muscle: by-products of metabolism or key regulators of muscle function? Free Radic. Biol. Med. 44 2008 132 141
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 132-141
    • Jackson, M.J.1
  • 51
    • 1542373629 scopus 로고    scopus 로고
    • NADH Oxidase Activity of Rat Cardiac Sarcoplasmic Reticulum Regulates Calcium-Induced Calcium Release
    • DOI 10.1161/01.RES.0000115554.65513.7C
    • G. Cherednichenko, A.V. Zima, W. Feng, S. Schaefer, L.A. Blatter, and I.N. Pessah NADH oxidase activity of rat cardiac sarcoplasmic reticulum regulates calcium-induced calcium release Circ. Res. 94 2004 478 486 (Pubitemid 38326283)
    • (2004) Circulation Research , vol.94 , Issue.4 , pp. 478-486
    • Cherednichenko, G.1    Zima, A.V.2    Feng, W.3    Schaefer, S.4    Blatter, L.A.5    Pessah, I.N.6
  • 52
    • 0038508928 scopus 로고    scopus 로고
    • Skeletal muscle sarcoplasmic reticulum contains a NADH-dependent oxidase that generates superoxide
    • R. Xia, J.A. Webb, L.L. Gnall, K. Cutler, and J.J. Abramson Skeletal muscle sarcoplasmic reticulum contains a NADH-dependent oxidase that generates superoxide Am. J. Physiol. Cell Physiol. 285 2003 C215 C221
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Xia, R.1    Webb, J.A.2    Gnall, L.L.3    Cutler, K.4    Abramson, J.J.5
  • 53
    • 33748755208 scopus 로고    scopus 로고
    • A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation
    • DOI 10.1074/jbc.M600451200
    • C. Hidalgo, G. Sanchez, G. Barrientos, and P. Aracena-Parks A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation J. Biol. Chem. 281 2006 26473 26482 (Pubitemid 44401856)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26473-26482
    • Hidalgo, C.1    Sanchez, G.2    Barrientos, G.3    Aracena-Parks, P.4
  • 56
    • 4444304505 scopus 로고    scopus 로고
    • Release of reactive oxygen and nitrogen species from contracting skeletal muscle cells
    • DOI 10.1016/j.freeradbiomed.2004.06.026, PII S0891584904004976
    • D.M. Pattwell, A. McArdle, J.E. Morgan, T.A. Patridge, and M.J. Jackson Release of reactive oxygen and nitrogen species from contracting skeletal muscle cells Free Radic. Biol. Med. 37 2004 1064 1072 (Pubitemid 39172132)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.7 , pp. 1064-1072
    • Patwell, D.M.1    McArdle, A.2    Morgan, J.E.3    Patridge, T.A.4    Jackson, M.J.5
  • 57
    • 0026438910 scopus 로고
    • Reactive oxygen in skeletal muscle. I. Intracellular oxidant kinetics and fatigue in vitro
    • M.B. Reid, K.E. Haack, K.M. Franchek, P.A. Valberg, L. Kobzik, and M.S. West Reactive oxygen in skeletal muscle. I. Intracellular oxidant kinetics and fatigue in vitro J. Appl. Physiol. 73 1992 1797 1804
    • (1992) J. Appl. Physiol. , vol.73 , pp. 1797-1804
    • Reid, M.B.1    Haack, K.E.2    Franchek, K.M.3    Valberg, P.A.4    Kobzik, L.5    West, M.S.6
  • 58
    • 0026448466 scopus 로고
    • Reactive oxygen in skeletal muscle. II. Extracellular release of free radicals
    • M.B. Reid, T. Shoji, M.R. Moody, and M.L. Entman Reactive oxygen in skeletal muscle. II. Extracellular release of free radicals J. Appl. Physiol. 73 1992 1805 1809
    • (1992) J. Appl. Physiol. , vol.73 , pp. 1805-1809
    • Reid, M.B.1    Shoji, T.2    Moody, M.R.3    Entman, M.L.4
  • 61
    • 6344285417 scopus 로고    scopus 로고
    • Endothelial cell superoxide generation: Regulation and relevance for cardiovascular pathophysiology
    • J.M. Li, and A.M. Shah Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology Am. J. Physiol. Regul. Integr. Comp. Physiol. 287 2004 R1014 R1030
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.287
    • Li, J.M.1    Shah, A.M.2
  • 62
    • 20444430042 scopus 로고    scopus 로고
    • Multiple proteins with single activities or a single protein with multiple activities: The conundrum of cell surface NADH oxidoreductases
    • DOI 10.1016/j.bbabio.2005.03.006, PII S0005272805000885
    • D.J. Scarlett, P.M. Herst, and M.V. Berridge Multiple proteins with single activities or a single protein with multiple activities: the conundrum of cell surface NADH oxidoreductases Biochim. Biophys. Acta 1708 2005 108 119 (Pubitemid 40798535)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1708 , Issue.1 , pp. 108-119
    • Scarlett, D.-J.G.1    Herst, P.M.2    Berridge, M.V.3
  • 63
    • 1342346692 scopus 로고    scopus 로고
    • Quinone oxidoreductases of the plasma membrane
    • D.J. Morré Quinone oxidoreductases of the plasma membrane Meth. Enzymol. 378 2004 179 199
    • (2004) Meth. Enzymol. , vol.378 , pp. 179-199
    • Morré, D.J.1
  • 64
    • 0038010637 scopus 로고    scopus 로고
    • A hypothesis for the minimal overall structure of the mammalian plasma membrane redox system
    • DOI 10.1007/s00709-002-0061-4
    • A.D. de Grey A hypothesis for the minimal overall structure of the mammalian plasma membrane redox system Protoplasma 221 2003 3 9 (Pubitemid 36658578)
    • (2003) Protoplasma , vol.221 , Issue.1-2 , pp. 3-9
    • De Grey, A.D.N.J.1
  • 65
  • 66
    • 0037067321 scopus 로고    scopus 로고
    • phox
    • DOI 10.1074/jbc.M203630200
    • X. Zhao, E.A. Bey, F.B. Wientjes, and M.K. Cathcart Cytosolic phospholipase A2 (cPLA2) regulation of human monocyte NADPH oxidase activity: cPLA2 affects translocation but not phosphorylation of p67(phox) and p47(phox) J. Biol. Chem. 277 2002 25385 25392 (Pubitemid 34951850)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25385-25392
    • Zhao, X.1    Bey, E.A.2    Wientjes, F.B.3    Cathcart, M.K.4
  • 68
    • 33645969808 scopus 로고    scopus 로고
    • 2 modulates cytosolic oxidant activity and contractile function in murine skeletal muscle cells
    • DOI 10.1152/japplphysiol.00873.2005
    • M.C. Gong, S. Arbogast, Z. Guo, J. Mathenia, W. Su, and M.B. Reid Calcium-independent phospholipase A2 modulates cytosolic oxidant activity and contractile function in murine skeletal muscle cells J. Appl. Physiol. 100 2006 399 405 (Pubitemid 43671587)
    • (2006) Journal of Applied Physiology , vol.100 , Issue.2 , pp. 399-405
    • Gong, M.C.1    Arbogast, S.2    Guo, Z.3    Mathenia, J.4    Su, W.5    Reid, M.B.6
  • 70
    • 68249135143 scopus 로고    scopus 로고
    • NADPH oxidase-derived reactive oxygen species in skeletal muscle modulates the exercise pressor reflex
    • H.J. Wang, Y.X. Pan, W.Z. Wang, I.H. Zucker, and W. Wang NADPH oxidase-derived reactive oxygen species in skeletal muscle modulates the exercise pressor reflex J. Appl. Physiol. 107 2009 450 459
    • (2009) J. Appl. Physiol. , vol.107 , pp. 450-459
    • Wang, H.J.1    Pan, Y.X.2    Wang, W.Z.3    Zucker, I.H.4    Wang, W.5
  • 71
    • 23844540597 scopus 로고    scopus 로고
    • Decreasing xanthine oxidase-mediated oxidative stress prevents useful cellular adaptations to exercise in rats
    • DOI 10.1113/jphysiol.2004.080564
    • M.C. Gomez-Cabrera, C. Borras, F.V. Pallardo, J. Sastre, L.L. Ji, and J. Vina Decreasing xanthine oxidase-mediated oxidative stress prevents useful cellular adaptations to exercise in rats J. Physiol. 567 2005 113 120 (Pubitemid 41167309)
    • (2005) Journal of Physiology , vol.567 , Issue.1 , pp. 113-120
    • Gomez-Cabrera, M.-C.1    Borras, C.2    Pallardo, F.V.3    Sastre, J.4    Ji, L.L.5    Vina, J.6
  • 74
    • 0347628958 scopus 로고    scopus 로고
    • Xanthine oxidase and activated neutrophils cause oxidative damage to skeletal muscle after contractile claudication
    • A.R. Judge, and S.L. Dodd Xanthine oxidase and activated neutrophils cause oxidative damage to skeletal muscle after contractile claudication Am. J. Physiol. Heart Circ. Physiol. 286 2004 H252 H256
    • (2004) Am. J. Physiol. Heart Circ. Physiol. , vol.286
    • Judge, A.R.1    Dodd, S.L.2
  • 75
    • 0029847635 scopus 로고    scopus 로고
    • Effect of sprint cycle training on activities of antioxidant enzymes in human skeletal muscle
    • Y. Hellsten, F.S. Apple, and B. Sjodin Effect of sprint cycle training on activities of antioxidant enzymes in human skeletal muscle J. Appl. Physiol. 81 1996 1484 1487 (Pubitemid 26349596)
    • (1996) Journal of Applied Physiology , vol.81 , Issue.4 , pp. 1484-1487
    • Hellsten, Y.1    Apple, F.S.2    Sjodin, B.3
  • 76
    • 37849040918 scopus 로고    scopus 로고
    • Free radicals and muscle fatigue: Of ROS, canaries, and the IOC
    • M.B. Reid Free radicals and muscle fatigue: of ROS, canaries, and the IOC Free Radic. Biol. Med. 44 2008 169 179
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 169-179
    • Reid, M.B.1
  • 77
    • 0035092313 scopus 로고    scopus 로고
    • Nitric oxide, reactive oxygen species, and skeletal muscle contraction
    • M.B. Reid Nitric oxide, reactive oxygen species, and skeletal muscle contraction Med. Sci. Sports Exerc. 33 2001 371 376 (Pubitemid 32209654)
    • (2001) Medicine and Science in Sports and Exercise , vol.33 , Issue.3 , pp. 371-376
    • Reid, M.B.1
  • 78
    • 0035143723 scopus 로고    scopus 로고
    • Invited review: Redox modulation of skeletal muscle contraction: What we know and what we don't
    • M.B. Reid Redox modulation of skeletal muscle contraction: what we know and what we don't J. Appl. Physiol. 90 2001 724 731 (Pubitemid 32118935)
    • (2001) Journal of Applied Physiology , vol.90 , Issue.2 , pp. 724-731
    • Reid, M.B.1
  • 79
    • 34247855762 scopus 로고    scopus 로고
    • Free radical-mediated skeletal muscle dysfunction in inflammatory conditions
    • DOI 10.1152/japplphysiol.01138.2006
    • G.S. Supinski, and L.A. Callahan Free radical-mediated skeletal muscle dysfunction in inflammatory conditions J. Appl. Physiol. 102 2007 2056 2063 (Pubitemid 46701978)
    • (2007) Journal of Applied Physiology , vol.102 , Issue.5 , pp. 2056-2063
    • Supinski, G.S.1    Callahan, L.A.2
  • 80
    • 0027425836 scopus 로고
    • Reactive oxygen in skeletal muscle. III. Contractility of unfatigued muscle
    • M.B. Reid, F.A. Khawli, and M.R. Moody Reactive oxygen in skeletal muscle. III. Contractility of unfatigued muscle J. Appl. Physiol. 75 1993 1081 1087 (Pubitemid 23289594)
    • (1993) Journal of Applied Physiology , vol.75 , Issue.3 , pp. 1081-1087
    • Reid, M.B.1    Khawli, F.A.2    Moody, M.R.3
  • 81
    • 0028283630 scopus 로고
    • Dimethyl sulfoxide depresses skeletal muscle contractility
    • M.B. Reid, and M.R. Moody Dimethyl sulfoxide depresses skeletal muscle contractility J. Appl. Physiol. 76 1994 2186 2190 (Pubitemid 24158655)
    • (1994) Journal of Applied Physiology , vol.76 , Issue.5 , pp. 2186-2190
    • Reid, M.B.1    Moody, M.R.2
  • 84
    • 0034783773 scopus 로고    scopus 로고
    • Spinal and supraspinal factors in human muscle fatigue
    • S.C. Gandevia Spinal and supraspinal factors in human muscle fatigue Physiol. Rev. 81 2001 1725 1789 (Pubitemid 32951808)
    • (2001) Physiological Reviews , vol.81 , Issue.4 , pp. 1725-1789
    • Gandevia, S.C.1
  • 86
    • 0025975806 scopus 로고
    • Free radicals may contribute to oxidative skeletal muscle fatigue
    • J.K. Barclay, and M. Hansel Free radicals may contribute to oxidative skeletal muscle fatigue Can. J. Physiol. Pharmacol. 69 1991 279 284
    • (1991) Can. J. Physiol. Pharmacol. , vol.69 , pp. 279-284
    • Barclay, J.K.1    Hansel, M.2
  • 88
    • 0030900650 scopus 로고    scopus 로고
    • N-acetylcysteine administration alters the response to inspiratory loading in oxygen-supplemented rats
    • G.S. Supinski, D. Stofan, R. Ciufo, and A. DiMarco N-acetylcysteine administration alters the response to inspiratory loading in oxygen-supplemented rats J. Appl. Physiol. 82 1997 1119 1125 (Pubitemid 27172313)
    • (1997) Journal of Applied Physiology , vol.82 , Issue.4 , pp. 1119-1125
    • Supinski, G.S.1    Stofan, D.2    Ciufo, R.3    DiMarco, A.4
  • 89
    • 17444408539 scopus 로고    scopus 로고
    • 2+ sensitivity in fatiguing mouse skeletal muscle at 37°C
    • DOI 10.1113/jphysiol.2005.083519
    • 2+ sensitivity in fatiguing mouse skeletal muscle at 37 °C J. Physiol. 564 2005 189 199 (Pubitemid 40542197)
    • (2005) Journal of Physiology , vol.564 , Issue.1 , pp. 189-199
    • Moopanar, T.R.1    Allen, D.G.2
  • 90
    • 0028236878 scopus 로고
    • N-acetylcysteine depresses contractile function and inhibits fatigue of diaphragm in vitro
    • F.A. Khawli, and M.B. Reid N-acetylcysteine depresses contractile function and inhibits fatigue of diaphragm in vitro J. Appl. Physiol. 77 1994 317 324 (Pubitemid 24226152)
    • (1994) Journal of Applied Physiology , vol.77 , Issue.1 , pp. 317-324
    • Khawli, F.A.1    Reid, M.B.2
  • 91
    • 67650087619 scopus 로고    scopus 로고
    • L-2-Oxothiazolidine-4-carboxylate reverses glutathione oxidation and delays fatigue of skeletal muscle in vitro
    • L.F. Ferreira, L.A. Gilliam, and M.B. Reid L-2-Oxothiazolidine-4- carboxylate reverses glutathione oxidation and delays fatigue of skeletal muscle in vitro J. Appl. Physiol. 107 2009 211 216
    • (2009) J. Appl. Physiol. , vol.107 , pp. 211-216
    • Ferreira, L.F.1    Gilliam, L.A.2    Reid, M.B.3
  • 92
    • 0025165279 scopus 로고
    • Spin-trappers and vitamin e prolong endurance to muscle fatigue in mice
    • G.P. Novelli, G. Bracciotti, and S. Falsini Spin-trappers and vitamin E prolong endurance to muscle fatigue in mice Free Radic. Biol. Med. 8 1990 9 13
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 9-13
    • Novelli, G.P.1    Bracciotti, G.2    Falsini, S.3
  • 93
    • 77951230033 scopus 로고    scopus 로고
    • Effects of a flavonoid extract from Cynomorium songaricum on the swimming endurance of rats
    • F.R. Yu, Y. Liu, Y.Z. Cui, E.Q. Chan, M.R. Xie, P.P. McGuire, and F.H. Yu Effects of a flavonoid extract from Cynomorium songaricum on the swimming endurance of rats Am. J. Chin. Med. 38 2010 65 73
    • (2010) Am. J. Chin. Med. , vol.38 , pp. 65-73
    • Yu, F.R.1    Liu, Y.2    Cui, Y.Z.3    Chan, E.Q.4    Xie, M.R.5    McGuire, P.P.6    Yu, F.H.7
  • 96
    • 33645969578 scopus 로고    scopus 로고
    • Redox modulation of contractile function in respiratory and limb skeletal muscle
    • M.A. Smith, and M.B. Reid Redox modulation of contractile function in respiratory and limb skeletal muscle Respir. Physiol. Neurobiol. 151 2006 229 241
    • (2006) Respir. Physiol. Neurobiol. , vol.151 , pp. 229-241
    • Smith, M.A.1    Reid, M.B.2
  • 97
    • 0031917017 scopus 로고    scopus 로고
    • Effects of S-nitroso-N-acetylcysteine on contractile function of reperfused skeletal muscle
    • L.E. Chen, A.V. Seaber, R.M. Nasser, J.S. Stamler, and J.R. Urbaniak Effects of S-nitroso-N-acetylcysteine on contractile function of reperfused skeletal muscle Am. J. Physiol. 274 1998 R822 R829
    • (1998) Am. J. Physiol. , vol.274
    • Chen, L.E.1    Seaber, A.V.2    Nasser, R.M.3    Stamler, J.S.4    Urbaniak, J.R.5
  • 98
    • 0028046502 scopus 로고
    • Nitric oxide in skeletal muscle
    • DOI 10.1038/372546a0
    • L. Kobzik, M.B. Reid, D.S. Bredt, and J.S. Stamler Nitric oxide in skeletal muscle Nature 372 1994 546 548 (Pubitemid 24368535)
    • (1994) Nature , vol.372 , Issue.6506 , pp. 546-548
    • Kobzik, L.1    Reid, M.B.2    Bredt, D.S.3    Stamler, J.S.4
  • 99
    • 4644240045 scopus 로고    scopus 로고
    • N-acetylcysteine enhances muscle cysteine and glutathione availability and attenuates fatigue during prolonged exercise in endurance-trained individuals
    • DOI 10.1152/japplphysiol.00371.2004
    • I. Medved, M.J. Brown, A.R. Bjorksten, K.T. Murphy, A.C. Petersen, S. Sostaric, X. Gong, and M.J. McKenna N-acetylcysteine enhances muscle cysteine and glutathione availability and attenuates fatigue during prolonged exercise in endurance-trained individuals J. Appl. Physiol. 97 2004 1477 1485 (Pubitemid 39299368)
    • (2004) Journal of Applied Physiology , vol.97 , Issue.4 , 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    Gong, X.7    McKenna, M.J.8
  • 101
    • 0346102467 scopus 로고    scopus 로고
    • Effects of intravenous N-acetylcysteine infusion on time to fatigue and potassium regulation during prolonged cycling exercise
    • DOI 10.1152/japplphysiol.00458.2003
    • I. Medved, M.J. Brown, A.R. Bjorksten, and M.J. McKenna Effects of intravenous N-acetylcysteine infusion on time to fatigue and potassium regulation during prolonged cycling exercise J. Appl. Physiol. 96 2004 211 217 (Pubitemid 38032003)
    • (2004) Journal of Applied Physiology , vol.96 , Issue.1 , pp. 211-217
    • Medved, I.1    Brown, M.J.2    Bjorksten, A.R.3    McKenna, M.J.4
  • 102
    • 27144533632 scopus 로고    scopus 로고
    • Effects of N-acetylcysteine on glutathione oxidation and fatigue during handgrip exercise
    • DOI 10.1002/mus.20385
    • Y. Matuszczak, M. Farid, J. Jones, S. Lansdowne, M.A. Smith, A.A. Taylor, and M.B. Reid Effects of N-acetylcysteine on glutathione oxidation and fatigue during handgrip exercise Muscle Nerve 32 2005 633 638 (Pubitemid 41504850)
    • (2005) Muscle and Nerve , vol.32 , Issue.5 , pp. 633-638
    • Matuszczak, Y.1    Farid, M.2    Jones, J.3    Lansdowne, S.4    Smith, M.A.5    Taylor, A.A.6    Reid, M.B.7
  • 105
    • 57749112938 scopus 로고    scopus 로고
    • Effects of N-acetylcysteine on respiratory muscle fatigue during heavy exercise
    • M.K. Kelly, R.J. Wicker, T.J. Barstow, and C.A. Harms Effects of N-acetylcysteine on respiratory muscle fatigue during heavy exercise Respir. Physiol. Neurobiol. 165 2009 67 72
    • (2009) Respir. Physiol. Neurobiol. , vol.165 , pp. 67-72
    • Kelly, M.K.1    Wicker, R.J.2    Barstow, T.J.3    Harms, C.A.4
  • 106
    • 1842481121 scopus 로고    scopus 로고
    • Antioxidant properties of N-acetylcysteine: Their relevance in relation to chronic obstructive pulmonary disease
    • DOI 10.1183/09031936.04.00016804
    • P.N. Dekhuijzen Antioxidant properties of N-acetylcysteine: their relevance in relation to chronic obstructive pulmonary disease Eur. Respir. J. 23 2004 629 636 (Pubitemid 38456009)
    • (2004) European Respiratory Journal , vol.23 , Issue.4 , pp. 629-636
    • Dekhuijzen, P.N.R.1
  • 107
    • 0032039959 scopus 로고    scopus 로고
    • Clinical applications of N-acetylcysteine
    • G.S. Kelly Clinical applications of N-acetylcysteine Altern. Med. Rev. 3 1998 114 127 (Pubitemid 128709607)
    • (1998) Alternative Medicine Review , vol.3 , Issue.2 , pp. 114-127
    • Kelly, G.S.1
  • 108
    • 0027942825 scopus 로고
    • Effects of N-acetylcysteine on in vitro diaphragm function are temperature dependent
    • P.T. Diaz, E. Brownstein, and T.L. Clanton Effects of N-acetylcysteine on in vitro diaphragm function are temperature dependent J. Appl. Physiol. 77 1994 2434 2439 (Pubitemid 24346457)
    • (1994) Journal of Applied Physiology , vol.77 , Issue.5 , pp. 2434-2439
    • Diaz, P.T.1    Brownstein, E.2    Clanton, T.L.3
  • 109
    • 0037377633 scopus 로고    scopus 로고
    • N-acetylcysteine infusion alters blood redox status but not time to fatigue during intense exercise in humans
    • I. Medved, M.J. Brown, A.R. Bjorksten, J.A. Leppik, S. Sostaric, and M.J. McKenna N-acetylcysteine infusion alters blood redox status but not time to fatigue during intense exercise in humans J. Appl. Physiol. 94 2003 1572 1582 (Pubitemid 36348838)
    • (2003) Journal of Applied Physiology , vol.94 , Issue.4 , pp. 1572-1582
    • Medved, I.1    Brown, M.J.2    Bjorksten, A.R.3    Leppik, J.A.4    Sostaric, S.5    McKenna, M.J.6
  • 110
    • 0028510365 scopus 로고
    • Alpha-Tocopherol supplementation in racing cyclists during extreme endurance training
    • L. Rokitzki, E. Logemann, G. Huber, E. Keck, and J. Keul alpha-Tocopherol supplementation in racing cyclists during extreme endurance training Int. J. Sport Nutr. 4 1994 253 264
    • (1994) Int. J. Sport Nutr. , vol.4 , pp. 253-264
    • Rokitzki, L.1    Logemann, E.2    Huber, G.3    Keck, E.4    Keul, J.5
  • 112
    • 0026919561 scopus 로고
    • Effects of coenzyme athletic performance system as an ergogenic aid on endurance performance to exhaustion
    • I.P. Snider, T.L. Bazzarre, S.D. Murdoch, and A. Goldfarb Effects of coenzyme athletic performance system as an ergogenic aid on endurance performance to exhaustion Int. J. Sport Nutr. 2 1992 272 286
    • (1992) Int. J. Sport Nutr. , vol.2 , pp. 272-286
    • Snider, I.P.1    Bazzarre, T.L.2    Murdoch, S.D.3    Goldfarb, A.4
  • 113
    • 0346186188 scopus 로고    scopus 로고
    • Effects of Vitamin E and C Supplementation Either Alone or in Combination on Exercise-Induced Lipid Peroxidation in Trained Cyclists
    • DOI 10.1519/1533-4287(2003)017<0792:EOVEAC>2.0.CO;2
    • R.J. Bryant, J. Ryder, P. Martino, J. Kim, and B.W. Craig Effects of vitamin E and C supplementation either alone or in combination on exercise-induced lipid peroxidation in trained cyclists J. Strength Cond. Res. 17 2003 792 800 (Pubitemid 37524266)
    • (2003) Journal of Strength and Conditioning Research , vol.17 , Issue.4 , pp. 792-800
    • Bryant, R.J.1    Ryder, J.2    Martino, P.3    Kim, J.4    Craig, B.W.5
  • 114
    • 33750214346 scopus 로고    scopus 로고
    • Effects of vitamin E supplementation on oxidative stress at rest and after exercise to exhaustion in athletic students
    • A.A. Gaeini, N. Rahnama, and M.R. Hamedinia Effects of vitamin E supplementation on oxidative stress at rest and after exercise to exhaustion in athletic students J. Sports Med. Phys. Fitness 46 2006 458 461 (Pubitemid 44606457)
    • (2006) Journal of Sports Medicine and Physical Fitness , vol.46 , Issue.3 , pp. 458-461
    • Gaeini, A.A.1    Rahnama, N.2    Hamedinia, M.R.3
  • 118
    • 0024401147 scopus 로고
    • Critical sulfhydryls regulate calcium release from sarcoplasmic reticulum
    • DOI 10.1007/BF00812073
    • J.J. Abramson, and G. Salama Critical sulfhydryls regulate calcium release from sarcoplasmic reticulum J. Bioenerg. Biomembr. 21 1989 283 294 (Pubitemid 19143574)
    • (1989) Journal of Bioenergetics and Biomembranes , vol.21 , Issue.2 , pp. 283-294
    • Abramson, J.J.1    Salama, G.2
  • 119
    • 0034115793 scopus 로고    scopus 로고
    • Oxidative modification of ion channel activity of ryanodine receptor
    • K. Anzai, K. Ogawa, T. Ozawa, and H. Yamamoto Oxidative modification of ion channel activity of ryanodine receptor Antioxid. Redox Signaling 2 2000 35 40 (Pubitemid 30202451)
    • (2000) Antioxidants and Redox Signaling , vol.2 , Issue.1 , pp. 35-40
    • Anzai, K.1    Ogawa, K.2    Ozawa, T.3    Yamamoto, H.4
  • 120
    • 0034110595 scopus 로고    scopus 로고
    • Functional role of hyperreactive sulfhydryl moieties within the ryanodine receptor complex
    • I.N. Pessah, and W. Feng Functional role of hyperreactive sulfhydryl moieties within the ryanodine receptor complex Antioxid. Redox Signaling 2 2000 17 25 (Pubitemid 30202449)
    • (2000) Antioxidants and Redox Signaling , vol.2 , Issue.1 , pp. 17-25
    • Pessah, I.N.1    Feng, W.2
  • 124
    • 34147092002 scopus 로고    scopus 로고
    • Redox sensitivity of the ryanodine receptor interaction with FK506-binding protein
    • DOI 10.1074/jbc.M607590200
    • S. Zissimopoulos, N. Docrat, and F.A. Lai Redox sensitivity of the ryanodine receptor interaction with FK506-binding protein J. Biol. Chem. 282 2007 6976 6983 (Pubitemid 47093660)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 6976-6983
    • Zissimopoulos, S.1    Docrat, N.2    Lai, F.A.3
  • 125
    • 0035844120 scopus 로고    scopus 로고
    • Classes of thiols that influence the activity of the skeletal muscle calcium release channel
    • J. Sun, L. Xu, J.P. Eu, J.S. Stamler, and G. Meissner Classes of thiols that influence the activity of the skeletal muscle calcium release channel J. Biol. Chem. 276 2001 15625 15630
    • (2001) J. Biol. Chem. , vol.276 , pp. 15625-15630
    • Sun, J.1    Xu, L.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 126
    • 33745198418 scopus 로고    scopus 로고
    • Redox regulation of cardiac calcium channels and transporters
    • A.V. Zima, and L.A. Blatter Redox regulation of cardiac calcium channels and transporters Cardiovasc. Res. 71 2006 310 321
    • (2006) Cardiovasc. Res. , vol.71 , pp. 310-321
    • Zima, A.V.1    Blatter, L.A.2
  • 127
    • 0031015476 scopus 로고    scopus 로고
    • 2+-ATPase function by direct attack on the ATP binding site
    • 2+-ATPase function by direct attack on the ATP binding site Circ. Res. 80 1997 76 81 (Pubitemid 27030371)
    • (1997) Circulation Research , vol.80 , Issue.1 , pp. 76-81
    • Xu, K.Y.1    Zweier, J.L.2    Becker, L.C.3
  • 131
    • 0017087533 scopus 로고
    • Effect of bridging the two essential thiols of myosin on its spectral and actin-binding properties
    • M. Burke, F. Reisler, and W.F. Harrington Effect of bridging the two essential thiols of myosin on its spectral and actin-binding properties Biochemistry 15 1976 1923 1927
    • (1976) Biochemistry , vol.15 , pp. 1923-1927
    • Burke, M.1    Reisler, F.2    Harrington, W.F.3
  • 133
    • 0021414667 scopus 로고
    • The effect of myosin sulphydryl modification on the mechanics of fibre contraction
    • M.S. Crowder, and R. Cooke The effect of myosin sulphydryl modification on the mechanics of fibre contraction J. Muscle Res. Cell Motil. 5 1984 131 146
    • (1984) J. Muscle Res. Cell Motil. , vol.5 , pp. 131-146
    • Crowder, M.S.1    Cooke, R.2
  • 134
    • 0029814873 scopus 로고    scopus 로고
    • Differential susceptibility of human skeletal muscle proteins to free radical induced oxidative damage: A histochemical, immunocytochemical and electron microscopical study in vitro
    • DOI 10.1007/s004010050527
    • J.W. Haycock, P. Jones, J.B. Harris, and D. Mantle Differential susceptibility of human skeletal muscle proteins to free radical induced oxidative damage: a histochemical, immunocytochemical and electron microscopical study in vitro Acta Neuropathol. 92 1996 331 340 (Pubitemid 26317099)
    • (1996) Acta Neuropathologica , vol.92 , Issue.4 , pp. 331-340
    • Haycock, J.W.1    Jones, P.2    Harris, J.B.3    Mantle, D.4
  • 135
    • 0032103008 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide and dithiothreitol on contractile function of single skeletal muscle fibres from the mouse
    • DOI 10.1111/j.1469-7793.1998.565bn.x
    • F.H. Andrade, M.B. Reid, D.G. Allen, and H. Westerblad Effect of hydrogen peroxide and dithiothreitol on contractile function of single skeletal muscle fibres from the mouse J. Physiol. 509 Pt 2 1998 565 575 (Pubitemid 28287013)
    • (1998) Journal of Physiology , vol.509 , Issue.2 , pp. 565-575
    • Andrade, F.H.1    Reid, M.B.2    Allen, D.G.3    Westerblad, H.4
  • 136
    • 0035256776 scopus 로고    scopus 로고
    • Contractile response of skeletal muscle to low peroxide concentrations: Myofibrillar calcium sensitivity as a likely target for redox-modulation
    • F.H. Andrade, M.B. Reid, and H. Westerblad Contractile response of skeletal muscle to low peroxide concentrations: myofibrillar calcium sensitivity as a likely target for redox-modulation FASEB J. 15 2001 309 311
    • (2001) FASEB J. , vol.15 , pp. 309-311
    • Andrade, F.H.1    Reid, M.B.2    Westerblad, H.3
  • 137
    • 42149086522 scopus 로고    scopus 로고
    • Hydroxyl radical and glutathione interactions alter calcium sensitivity and maximum force of the contractile apparatus in rat skeletal muscle fibres
    • DOI 10.1113/jphysiol.2007.150516
    • R.M. Murphy, T.L. Dutka, and G.D. Lamb Hydroxyl radical and glutathione interactions alter calcium sensitivity and maximum force of the contractile apparatus in rat skeletal muscle fibres J. Physiol. 586 2008 2203 2216 (Pubitemid 351540511)
    • (2008) Journal of Physiology , vol.586 , Issue.8 , pp. 2203-2216
    • Murphy, R.M.1    Dutka, T.L.2    Lamb, G.D.3
  • 139
    • 33646409838 scopus 로고    scopus 로고
    • Oxidation of myosin heavy chain and reduction in force production in hyperthyroid rat soleus
    • T. Yamada, T. Mishima, M. Sakamoto, M. Sugiyama, S. Matsunaga, and M. Wada Oxidation of myosin heavy chain and reduction in force production in hyperthyroid rat soleus J. Appl. Physiol. 100 2006 1520 1526
    • (2006) J. Appl. Physiol. , vol.100 , pp. 1520-1526
    • Yamada, T.1    Mishima, T.2    Sakamoto, M.3    Sugiyama, M.4    Matsunaga, S.5    Wada, M.6
  • 142
    • 0034441873 scopus 로고    scopus 로고
    • 2+-activation of single permeabilized fibres from fast- and slow-twitch skeletal muscles of rats
    • DOI 10.1023/A:1010344008224
    • 2+-activation of single permeabilized fibres from fast- and slow-twitch skeletal muscles of rats J. Muscle Res. Cell Motil. 21 2000 747 752 (Pubitemid 32423409)
    • (2000) Journal of Muscle Research and Cell Motility , vol.21 , Issue.8 , pp. 747-752
    • Plant, D.R.1    Lynch, G.S.2    Williams, D.A.3
  • 146
    • 58349118928 scopus 로고    scopus 로고
    • Interactions between ROS and AMP kinase activity in the regulation of PGC-1alpha transcription in skeletal muscle cells
    • I. Irrcher, V. Ljubicic, and D.A. Hood Interactions between ROS and AMP kinase activity in the regulation of PGC-1alpha transcription in skeletal muscle cells Am. J. Physiol. Cell Physiol. 296 2009 C116 C123
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296
    • Irrcher, I.1    Ljubicic, V.2    Hood, D.A.3
  • 147
    • 9244223545 scopus 로고    scopus 로고
    • Preconditioning of skeletal muscle against contraction-induced damage: The role of adaptations to oxidants in mice
    • DOI 10.1113/jphysiol.2004.069914
    • F. McArdle, S. Spiers, H. Aldemir, A. Vasilaki, A. Beaver, L. Iwanejko, A. McArdle, and M.J. Jackson Preconditioning of skeletal muscle against contraction-induced damage: the role of adaptations to oxidants in mice J. Physiol. 561 2004 233 244 (Pubitemid 39549479)
    • (2004) Journal of Physiology , vol.561 , Issue.1 , pp. 233-244
    • McArdle, F.1    Spiers, S.2    Aldemir, H.3    Vasilaki, A.4    Beaver, A.5    Iwanejko, L.6    McArdle, A.7    Jackson, M.J.8
  • 148
    • 0141791457 scopus 로고    scopus 로고
    • Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes
    • Y.P. Li, Y. Chen, A.S. Li, and M.B. Reid Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes Am. J. Physiol. Cell Physiol. 285 2003 C806 C812
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Li, Y.P.1    Chen, Y.2    Li, A.S.3    Reid, M.B.4
  • 149
    • 34247473444 scopus 로고    scopus 로고
    • A reducing redox environment promotes C2C12 myogenesis: Implications for regeneration in aged muscle
    • DOI 10.1016/j.cellbi.2006.11.027, PII S1065699506002939
    • J.M. Hansen, M. Klass, C. Harris, and M. Csete A reducing redox environment promotes C2C12 myogenesis: implications for regeneration in aged muscle Cell Biol. Int. 31 2007 546 553 (Pubitemid 46660641)
    • (2007) Cell Biology International , vol.31 , Issue.6 , pp. 546-553
    • Hansen, J.M.1    Klass, M.2    Harris, C.3    Csete, M.4
  • 150
    • 0033231361 scopus 로고    scopus 로고
    • Regulation of antioxidant enzyme gene expression in response to oxidative stress and during differentiation of mouse skeletal muscle
    • DOI 10.1016/S0891-5849(99)00166-5, PII S0891584999001665
    • A.A. Franco, R.S. Odom, and T.A. Rando Regulation of antioxidant enzyme gene expression in response to oxidative stress and during differentiation of mouse skeletal muscle Free Radic. Biol. Med. 27 1999 1122 1132 (Pubitemid 29507485)
    • (1999) Free Radical Biology and Medicine , vol.27 , Issue.9-10 , pp. 1122-1132
    • Franco, A.A.1    Odom, R.S.2    Rando, T.A.3
  • 151
    • 33748313028 scopus 로고    scopus 로고
    • The contraction induced increase in gene expression of peroxisome proliferator-activated receptor (PPAR)-γ coactivator 1α (PGC-1α), mitochondrial uncoupling protein 3 (UCP3) and hexokinase II (HKII) in primary rat skeletal muscle cells is dependent on reactive oxygen species
    • DOI 10.1016/j.bbamcr.2006.06.010, PII S0167488906001467
    • L.R. Silveira, H. Pilegaard, K. Kusuhara, R. Curi, and Y. Hellsten The contraction induced increase in gene expression of peroxisome proliferator-activated receptor (PPAR)-gamma coactivator 1alpha (PGC-1alpha), mitochondrial uncoupling protein 3 (UCP3) and hexokinase II (HKII) in primary rat skeletal muscle cells is dependent on reactive oxygen species Biochim. Biophys. Acta 1763 2006 969 976 (Pubitemid 44332599)
    • (2006) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1763 , Issue.9 , pp. 969-976
    • Silveira, L.R.1    Pilegaard, H.2    Kusuhara, K.3    Curi, R.4    Hellsten, Y.5
  • 155
    • 38149131289 scopus 로고    scopus 로고
    • Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance
    • M.C. Gomez-Cabrera, E. Domenech, M. Romagnoli, A. Arduini, C. Borras, F.V. Pallardo, J. Sastre, and J. Vina Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance Am. J. Clin. Nutr. 87 2008 142 149
    • (2008) Am. J. Clin. Nutr. , vol.87 , pp. 142-149
    • Gomez-Cabrera, M.C.1    Domenech, E.2    Romagnoli, M.3    Arduini, A.4    Borras, C.5    Pallardo, F.V.6    Sastre, J.7    Vina, J.8
  • 157
    • 34248525050 scopus 로고    scopus 로고
    • Targeting lipoic acid to mitochondria: Synthesis and characterization of a triphenylphosphonium-conjugated α-lipoyl derivative
    • DOI 10.1016/j.freeradbiomed.2007.02.033, PII S0891584907001888
    • S.E. Brown, M.F. Ross, A. Sanjuan-Pla, A.R. Manas, R.A. Smith, and M.P. Murphy Targeting lipoic acid to mitochondria: synthesis and characterization of a triphenylphosphonium-conjugated α-lipoyl derivative Free Radic. Biol. Med. 42 2007 1766 1780 (Pubitemid 46759581)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.12 , pp. 1766-1780
    • Brown, S.E.1    Ross, M.F.2    Sanjuan-Pla, A.3    Manas, A.-R.B.4    Smith, R.A.J.5    Murphy, M.P.6
  • 158
    • 33847071146 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria by conjugation to lipophilic cations
    • M.P. Murphy, and R.A. Smith Targeting antioxidants to mitochondria by conjugation to lipophilic cations Annu. Rev. Pharmacol. Toxicol. 47 2007 629 656
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 629-656
    • Murphy, M.P.1    Smith, R.A.2
  • 159
    • 21744450416 scopus 로고    scopus 로고
    • Targeting an antioxidant to mitochondria decreases cardiac ischemia-reperfusion injury
    • DOI 10.1096/fj.05-3718com
    • V.J. Adlam, J.C. Harrison, C.M. Porteous, A.M. James, R.A. Smith, M.P. Murphy, and I.A. Sammut Targeting an antioxidant to mitochondria decreases cardiac ischemia-reperfusion injury FASEB J. 19 2005 1088 1095 (Pubitemid 40946434)
    • (2005) FASEB Journal , vol.19 , Issue.9 , pp. 1088-1095
    • Adlam, V.J.1    Harrison, J.C.2    Porteous, C.M.3    James, A.M.4    Smith, R.A.J.5    Murphy, M.P.6    Sammut, I.A.7
  • 160
    • 4544370680 scopus 로고    scopus 로고
    • Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury
    • DOI 10.1074/jbc.M402999200
    • K. Zhao, G.M. Zhao, D. Wu, Y. Soong, A.V. Birk, P.W. Schiller, and H.H. Szeto Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury J. Biol. Chem. 279 2004 34682 34690 (Pubitemid 39318098)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34682-34690
    • Zhao, K.1    Zhao, G.-M.2    Wu, D.3    Soong, Y.4    Birk, A.V.5    Schiller, P.W.6    Szeto, H.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.