메뉴 건너뛰기




Volumn 1862, Issue 4, 2016, Pages 716-724

Evaluation of in vivo mitochondrial bioenergetics in skeletal muscle using NMR and optical methods

Author keywords

Bioenergetics; In vivo spectroscopy; Mitochondria; NIRS; NMR; Skeletal muscle

Indexed keywords

ADENOSINE TRIPHOSPHATE; OXYGEN;

EID: 84958212270     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2015.12.019     Document Type: Review
Times cited : (20)

References (106)
  • 1
    • 0023645086 scopus 로고
    • Influence of mitochondrial content on the sensitivity of respiratory control
    • Dudley G.A., Tullson P.C., Terjung R.L. Influence of mitochondrial content on the sensitivity of respiratory control. J. Biol. Chem. 1987, 262:9109-9114.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9109-9114
    • Dudley, G.A.1    Tullson, P.C.2    Terjung, R.L.3
  • 2
    • 1642422773 scopus 로고    scopus 로고
    • Mitochondrial free radical production and cell signaling
    • Cadenas E. Mitochondrial free radical production and cell signaling. Mol. Asp. Med. 2004, 25:17-26.
    • (2004) Mol. Asp. Med. , vol.25 , pp. 17-26
    • Cadenas, E.1
  • 3
    • 78650068036 scopus 로고    scopus 로고
    • Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates
    • Garcia J., Han D., Sancheti H., Yap L.P., Kaplowitz N., Cadenas E. Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates. J. Biol. Chem. 2010, 285:39646-39654.
    • (2010) J. Biol. Chem. , vol.285 , pp. 39646-39654
    • Garcia, J.1    Han, D.2    Sancheti, H.3    Yap, L.P.4    Kaplowitz, N.5    Cadenas, E.6
  • 6
    • 0034686014 scopus 로고    scopus 로고
    • Calcium signal transmission between ryanodine receptors and mitochondria
    • Szalai G., Csordas G., Hantash B.M., Thomas A.P., Hajnoczky G. Calcium signal transmission between ryanodine receptors and mitochondria. J. Biol. Chem. 2000, 275:15305-15313.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15305-15313
    • Szalai, G.1    Csordas, G.2    Hantash, B.M.3    Thomas, A.P.4    Hajnoczky, G.5
  • 7
    • 79953180902 scopus 로고    scopus 로고
    • Assessing mitochondrial dysfunction in cells
    • Brand M.D., Nicholls D.G. Assessing mitochondrial dysfunction in cells. Biochem. J. 2011, 435:297-312.
    • (2011) Biochem. J. , vol.435 , pp. 297-312
    • Brand, M.D.1    Nicholls, D.G.2
  • 13
    • 0025047553 scopus 로고
    • Skeletal-muscle metabolism is a major determinant of resting energy-expenditure
    • Zurlo F., Larson K., Bogardus C., Ravussin E. Skeletal-muscle metabolism is a major determinant of resting energy-expenditure. J. Clin. Invest. 1990, 86:1423-1427.
    • (1990) J. Clin. Invest. , vol.86 , pp. 1423-1427
    • Zurlo, F.1    Larson, K.2    Bogardus, C.3    Ravussin, E.4
  • 18
    • 0026732710 scopus 로고
    • Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi
    • Kushmerick M.J., Moerland T.S., Wiseman R.W. Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:7521-7525.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 7521-7525
    • Kushmerick, M.J.1    Moerland, T.S.2    Wiseman, R.W.3
  • 19
    • 0027163887 scopus 로고
    • Separate measures of ATP utilization and recovery in human skeletal muscle
    • Blei M.L., Conley K.E., Kushmerick M.J. Separate measures of ATP utilization and recovery in human skeletal muscle. J. Physiol. 1993, 465:203-222.
    • (1993) J. Physiol. , vol.465 , pp. 203-222
    • Blei, M.L.1    Conley, K.E.2    Kushmerick, M.J.3
  • 20
    • 80055109581 scopus 로고    scopus 로고
    • Noninvasive in vivo small animal MRI and MRS: basic experimental procedures
    • 1592
    • Lee D., Marcinek D. Noninvasive in vivo small animal MRI and MRS: basic experimental procedures. J. Vis. Exp. 2009 Oct, 20(32). (pii: 1592). 10.3791/1592.
    • (2009) J. Vis. Exp. , vol.20 , Issue.32
    • Lee, D.1    Marcinek, D.2
  • 22
    • 0032530353 scopus 로고    scopus 로고
    • Glycolysis is independent of oxygenation state in stimulated human skeletal muscle in vivo
    • Conley K.E., Kushmerick M.J., Jubrias S.A. Glycolysis is independent of oxygenation state in stimulated human skeletal muscle in vivo. J. Physiol. 1998, 511(Pt 3):935-945.
    • (1998) J. Physiol. , vol.511 , pp. 935-945
    • Conley, K.E.1    Kushmerick, M.J.2    Jubrias, S.A.3
  • 25
    • 0024840087 scopus 로고
    • Linear dependence of muscle phosphocreatine kinetics on total creatine content
    • Meyer R.A. Linear dependence of muscle phosphocreatine kinetics on total creatine content. Am. J. Physiol. 1989, 257:C1149-C1157.
    • (1989) Am. J. Physiol. , vol.257 , pp. C1149-C1157
    • Meyer, R.A.1
  • 27
    • 0030953950 scopus 로고    scopus 로고
    • Linear dependence of muscle phosphocreatine kinetics on oxidative capacity
    • Paganini A.T., Foley J.M., Meyer R.A. Linear dependence of muscle phosphocreatine kinetics on oxidative capacity. Am. J. Physiol. 1997, 272:C501-C510.
    • (1997) Am. J. Physiol. , vol.272 , pp. C501-C510
    • Paganini, A.T.1    Foley, J.M.2    Meyer, R.A.3
  • 31
    • 0023919905 scopus 로고
    • A linear model of muscle respiration explains monoexponential phosphocreatine changes
    • Meyer R.A. A linear model of muscle respiration explains monoexponential phosphocreatine changes. Am. J. Physiol. 1988, 254:C548-C553.
    • (1988) Am. J. Physiol. , vol.254 , pp. C548-C553
    • Meyer, R.A.1
  • 34
    • 81555207945 scopus 로고    scopus 로고
    • Reduced coupling of oxidative phosphorylation in vivo precedes electron transport chain defects due to mild oxidative stress in mice
    • Siegel M.P., Kruse S.E., Knowels G., Salmon A., Beyer R., Xie H., Van Remmen H., Smith S.R., Marcinek D.J. Reduced coupling of oxidative phosphorylation in vivo precedes electron transport chain defects due to mild oxidative stress in mice. PLoS One 2011, 6.
    • (2011) PLoS One , vol.6
    • Siegel, M.P.1    Kruse, S.E.2    Knowels, G.3    Salmon, A.4    Beyer, R.5    Xie, H.6    Van Remmen, H.7    Smith, S.R.8    Marcinek, D.J.9
  • 38
    • 0035155343 scopus 로고    scopus 로고
    • Bioenergetics at low oxygen: dependence of respiration and phosphorylation on oxygen and adenosine diphosphate supply
    • Gnaiger E. Bioenergetics at low oxygen: dependence of respiration and phosphorylation on oxygen and adenosine diphosphate supply. Respir. Physiol. 2001, 128:277-297.
    • (2001) Respir. Physiol. , vol.128 , pp. 277-297
    • Gnaiger, E.1
  • 39
    • 0035746163 scopus 로고    scopus 로고
    • Limits to sustainable muscle performance: interaction between glycolysis and oxidative phosphorylation
    • Conley K.E., Kemper W.F., Crowther G.J. Limits to sustainable muscle performance: interaction between glycolysis and oxidative phosphorylation. J. Exp. Biol. 2001, 204:3189-3194.
    • (2001) J. Exp. Biol. , vol.204 , pp. 3189-3194
    • Conley, K.E.1    Kemper, W.F.2    Crowther, G.J.3
  • 40
    • 33847752716 scopus 로고    scopus 로고
    • Mitochondrial function, fibre types and ageing: new insights from human muscle in vivo
    • Conley K.E., Amara C.E., Jubrias S.A., Marcinek D.J. Mitochondrial function, fibre types and ageing: new insights from human muscle in vivo. Exp. Physiol. 2007, 92:333-339.
    • (2007) Exp. Physiol. , vol.92 , pp. 333-339
    • Conley, K.E.1    Amara, C.E.2    Jubrias, S.A.3    Marcinek, D.J.4
  • 42
    • 84871200918 scopus 로고    scopus 로고
    • Defects in mitochondrial localization and ATP synthesis in the mdx mouse model of Duchenne muscular dystrophy are not alleviated by PDE5 inhibition
    • Percival J.M., Siegel M.P., Knowels G., Marcinek D.J. Defects in mitochondrial localization and ATP synthesis in the mdx mouse model of Duchenne muscular dystrophy are not alleviated by PDE5 inhibition. Hum. Mol. Genet. 2013, 22:153-167.
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 153-167
    • Percival, J.M.1    Siegel, M.P.2    Knowels, G.3    Marcinek, D.J.4
  • 45
    • 0034234773 scopus 로고    scopus 로고
    • Oxidative capacity and ageing in human muscle
    • Conley K.E., Jubrias S.A., Esselman P.C. Oxidative capacity and ageing in human muscle. J. Physiol. 2000, 526(Pt 1):203-210.
    • (2000) J. Physiol. , vol.526 , pp. 203-210
    • Conley, K.E.1    Jubrias, S.A.2    Esselman, P.C.3
  • 47
    • 84919723503 scopus 로고    scopus 로고
    • Effect of age on in vivo oxidative capacity in two locomotory muscles of the leg
    • Tevald M.A., Foulis S.A., Kent J.A. Effect of age on in vivo oxidative capacity in two locomotory muscles of the leg. Age 2014, 36:9713.
    • (2014) Age , vol.36 , pp. 9713
    • Tevald, M.A.1    Foulis, S.A.2    Kent, J.A.3
  • 48
    • 0032834249 scopus 로고    scopus 로고
    • Magnetic coupling of creatine/phosphocreatine protons in rat skeletal muscle, as studied by (1)H-magnetization transfer MRS
    • Kruiskamp M.J., de Graaf R.A., van Vliet G., Nicolay K. Magnetic coupling of creatine/phosphocreatine protons in rat skeletal muscle, as studied by (1)H-magnetization transfer MRS. Magn. Reson. Med. 1999, 42:665-672.
    • (1999) Magn. Reson. Med. , vol.42 , pp. 665-672
    • Kruiskamp, M.J.1    de Graaf, R.A.2    van Vliet, G.3    Nicolay, K.4
  • 49
    • 0031978279 scopus 로고    scopus 로고
    • Magnetization transfer attenuates metabolite signals in tumorous and contralateral animal brain: in vivo observations by proton NMR spectroscopy
    • Roell S.A., Dreher W., Busch E., Leibfritz D. Magnetization transfer attenuates metabolite signals in tumorous and contralateral animal brain: in vivo observations by proton NMR spectroscopy. Magn. Reson. Med. 1998, 39:742-748.
    • (1998) Magn. Reson. Med. , vol.39 , pp. 742-748
    • Roell, S.A.1    Dreher, W.2    Busch, E.3    Leibfritz, D.4
  • 50
    • 0032866248 scopus 로고    scopus 로고
    • Combining CW and pulsed saturation allows in vivo quantitation of magnetization transfer observed for total creatine by (1)H-NMR-spectroscopy of rat brain
    • Roell S.A., Dreher W., Leibfritz D. Combining CW and pulsed saturation allows in vivo quantitation of magnetization transfer observed for total creatine by (1)H-NMR-spectroscopy of rat brain. Magn. Reson. Med. 1999, 42:222-227.
    • (1999) Magn. Reson. Med. , vol.42 , pp. 222-227
    • Roell, S.A.1    Dreher, W.2    Leibfritz, D.3
  • 52
    • 0033399059 scopus 로고    scopus 로고
    • Altered creatine kinase enzyme kinetics in diabetic cardiomyopathy. A(31)P NMR magnetization transfer study of the intact beating rat heart
    • Spindler M., Saupe K.W., Tian R., Ahmed S., Matlib M.A., Ingwall J.S. Altered creatine kinase enzyme kinetics in diabetic cardiomyopathy. A(31)P NMR magnetization transfer study of the intact beating rat heart. J. Mol. Cell. Cardiol. 1999, 31:2175-2189.
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 2175-2189
    • Spindler, M.1    Saupe, K.W.2    Tian, R.3    Ahmed, S.4    Matlib, M.A.5    Ingwall, J.S.6
  • 54
    • 65449187906 scopus 로고    scopus 로고
    • Assessment of in vivo mitochondrial metabolism by magnetic resonance spectroscopy
    • Befroy D.E., Falk Petersen K., Rothman D.L., Shulman G.I. Assessment of in vivo mitochondrial metabolism by magnetic resonance spectroscopy. Methods Enzymol. 2009, 457:373-393.
    • (2009) Methods Enzymol. , vol.457 , pp. 373-393
    • Befroy, D.E.1    Falk Petersen, K.2    Rothman, D.L.3    Shulman, G.I.4
  • 57
    • 70349568691 scopus 로고    scopus 로고
    • Microarray analysis suggests that burn injury results in mitochondrial dysfunction in human skeletal muscle
    • Tzika A.A., Mintzopoulos D., Mindrinos M., Zhang J., Rahme L.G., Tompkins R.G. Microarray analysis suggests that burn injury results in mitochondrial dysfunction in human skeletal muscle. Int. J. Mol. Med. 2009, 24:387-392.
    • (2009) Int. J. Mol. Med. , vol.24 , pp. 387-392
    • Tzika, A.A.1    Mintzopoulos, D.2    Mindrinos, M.3    Zhang, J.4    Rahme, L.G.5    Tompkins, R.G.6
  • 58
    • 0024473889 scopus 로고
    • 31P NMR magnetization-transfer measurements of ATP turnover during steady-state isometric muscle contraction in the rat hind limb in vivo
    • 31P NMR magnetization-transfer measurements of ATP turnover during steady-state isometric muscle contraction in the rat hind limb in vivo. Biochemistry 1989, 28:4887-4893.
    • (1989) Biochemistry , vol.28 , pp. 4887-4893
    • Brindle, K.M.1    Blackledge, M.J.2    Challiss, R.A.3    Radda, G.K.4
  • 59
    • 0023335702 scopus 로고
    • NMR studies of kinetics in cells and tissues
    • Brindle K.M., Campbell I.D. NMR studies of kinetics in cells and tissues. Q. Rev. Biophys. 1987, 19:159-182.
    • (1987) Q. Rev. Biophys. , vol.19 , pp. 159-182
    • Brindle, K.M.1    Campbell, I.D.2
  • 62
    • 40549142436 scopus 로고    scopus 로고
    • 31P magnetic resonance saturation transfer measurements of Pi/ATP exchange in insulin-resistant skeletal muscle
    • (author reply E643-644)
    • 31P magnetic resonance saturation transfer measurements of Pi/ATP exchange in insulin-resistant skeletal muscle. Am. J. Physiol. Endocrinol. Metab. 2008, 294:E640-E642. (author reply E643-644).
    • (2008) Am. J. Physiol. Endocrinol. Metab. , vol.294 , pp. E640-E642
    • Kemp, G.J.1
  • 63
    • 84864389207 scopus 로고    scopus 로고
    • What do magnetic resonance-based measurements of P→ATP flux tell us about skeletal muscle metabolism?
    • Kemp G.J., Brindle K.M. What do magnetic resonance-based measurements of P→ATP flux tell us about skeletal muscle metabolism?. Diabetes 2012, 61:1927-1934.
    • (2012) Diabetes , vol.61 , pp. 1927-1934
    • Kemp, G.J.1    Brindle, K.M.2
  • 68
    • 37549059884 scopus 로고    scopus 로고
    • Progress of near-infrared spectroscopy and topography for brain and muscle clinical applications
    • Wolf M., Ferrari M., Quaresima V. Progress of near-infrared spectroscopy and topography for brain and muscle clinical applications. J. Biomed. Opt. 2007, 12:062104.
    • (2007) J. Biomed. Opt. , vol.12 , pp. 062104
    • Wolf, M.1    Ferrari, M.2    Quaresima, V.3
  • 72
    • 77955048300 scopus 로고    scopus 로고
    • Resting muscle oxygen consumption by near-infrared spectroscopy in peripheral arterial disease: a parameter to be considered in a clinical setting?
    • Malagoni A.M., Felisatti M., Mandini S., Mascoli F., Manfredini R., Basaglia N., Zamboni P., Manfredini F. Resting muscle oxygen consumption by near-infrared spectroscopy in peripheral arterial disease: a parameter to be considered in a clinical setting?. Angiology 2010, 61:530-536.
    • (2010) Angiology , vol.61 , pp. 530-536
    • Malagoni, A.M.1    Felisatti, M.2    Mandini, S.3    Mascoli, F.4    Manfredini, R.5    Basaglia, N.6    Zamboni, P.7    Manfredini, F.8
  • 73
    • 84876738299 scopus 로고    scopus 로고
    • Skeletal muscle metabolism in endurance athletes with near-infrared spectroscopy
    • Brizendine J.T., Ryan T.E., Larson R.D., McCully K.K. Skeletal muscle metabolism in endurance athletes with near-infrared spectroscopy. Med. Sci. Sports Exerc. 2013, 45:869-875.
    • (2013) Med. Sci. Sports Exerc. , vol.45 , pp. 869-875
    • Brizendine, J.T.1    Ryan, T.E.2    Larson, R.D.3    McCully, K.K.4
  • 74
    • 0027053881 scopus 로고
    • Muscle oxygenation by fast near infrared spectrophotometry (NIRS) in ischemic forearm
    • De Blasi R.A., Quaglia E., Gasparetto A., Ferrari M. Muscle oxygenation by fast near infrared spectrophotometry (NIRS) in ischemic forearm. Adv. Exp. Med. Biol. 1992, 316:163-172.
    • (1992) Adv. Exp. Med. Biol. , vol.316 , pp. 163-172
    • De Blasi, R.A.1    Quaglia, E.2    Gasparetto, A.3    Ferrari, M.4
  • 78
    • 77957667744 scopus 로고    scopus 로고
    • Simultaneous optical spectroscopic measurement of hemoglobin and myoglobin saturations and cytochrome aa3 oxidation in vivo
    • Arakaki L.S., Ciesielski W.A., Thackray B.D., Feigl E.O., Schenkman K.A. Simultaneous optical spectroscopic measurement of hemoglobin and myoglobin saturations and cytochrome aa3 oxidation in vivo. Appl. Spectrosc. 2010, 64:973-979.
    • (2010) Appl. Spectrosc. , vol.64 , pp. 973-979
    • Arakaki, L.S.1    Ciesielski, W.A.2    Thackray, B.D.3    Feigl, E.O.4    Schenkman, K.A.5
  • 80
    • 0027241092 scopus 로고
    • Control of the effective P/O ratio of oxidative phosphorylation in liver mitochondria and hepatocytes
    • Brand M.D., Harper M.E., Taylor H.C. Control of the effective P/O ratio of oxidative phosphorylation in liver mitochondria and hepatocytes. Biochem. J. 1993, 291(Pt 3):739-748.
    • (1993) Biochem. J. , vol.291 , pp. 739-748
    • Brand, M.D.1    Harper, M.E.2    Taylor, H.C.3
  • 81
    • 0029935666 scopus 로고    scopus 로고
    • P/O ratios reassessed: mitochondrial P/O ratios consistently exceed 1.5 with succinate and 2.5 with NAD-linked substrates
    • Lee C.P., Gu Q., Xiong Y., Mitchell R.A., Ernster L. P/O ratios reassessed: mitochondrial P/O ratios consistently exceed 1.5 with succinate and 2.5 with NAD-linked substrates. FASEB J. 1996, 10:345-350.
    • (1996) FASEB J. , vol.10 , pp. 345-350
    • Lee, C.P.1    Gu, Q.2    Xiong, Y.3    Mitchell, R.A.4    Ernster, L.5
  • 82
    • 0006598177 scopus 로고
    • The ups and downs of P/O ratios: (and the question of non-integral coupling stoichiometries for oxidative phosphorylation and related processes)
    • Ferguson S.J. The ups and downs of P/O ratios: (and the question of non-integral coupling stoichiometries for oxidative phosphorylation and related processes). Trends Biochem. Sci. 1986, 11:351-353.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 351-353
    • Ferguson, S.J.1
  • 83
    • 29244481672 scopus 로고    scopus 로고
    • Reduced mitochondrial coupling in vivo alters cellular energetics in aged mouse skeletal muscle
    • Marcinek D.J., Schenkman K.A., Ciesielski W.A., Lee D., Conley K.E. Reduced mitochondrial coupling in vivo alters cellular energetics in aged mouse skeletal muscle. J. Physiol. 2005, 569:467-473.
    • (2005) J. Physiol. , vol.569 , pp. 467-473
    • Marcinek, D.J.1    Schenkman, K.A.2    Ciesielski, W.A.3    Lee, D.4    Conley, K.E.5
  • 84
    • 84864250056 scopus 로고    scopus 로고
    • Noninvasive evaluation of skeletal muscle mitochondrial capacity with near-infrared spectroscopy: correcting for blood volume changes
    • Ryan T.E., Erickson M.L., Brizendine J.T., Young H.J., McCully K.K. Noninvasive evaluation of skeletal muscle mitochondrial capacity with near-infrared spectroscopy: correcting for blood volume changes. J. Appl. Physiol. 2012, 113:175-183.
    • (2012) J. Appl. Physiol. , vol.113 , pp. 175-183
    • Ryan, T.E.1    Erickson, M.L.2    Brizendine, J.T.3    Young, H.J.4    McCully, K.K.5
  • 86
    • 0021814235 scopus 로고
    • 2 and phosphorylcreatine level. Implications for the control of respiration
    • 2 and phosphorylcreatine level. Implications for the control of respiration. J. Gen. Physiol. 1985, 86:135-165.
    • (1985) J. Gen. Physiol. , vol.86 , pp. 135-165
    • Mahler, M.1
  • 87
    • 0030898874 scopus 로고    scopus 로고
    • Regulation analysis of energy metabolism
    • Brand M.D. Regulation analysis of energy metabolism. J. Exp. Biol. 1997, 200:193-202.
    • (1997) J. Exp. Biol. , vol.200 , pp. 193-202
    • Brand, M.D.1
  • 88
    • 84905217954 scopus 로고    scopus 로고
    • Assessment of in vivo skeletal muscle mitochondrial respiratory capacity in humans by near-infrared spectroscopy: a comparison with in situ measurements
    • Ryan T.E., Brophy P., Lin C.T., Hickner R.C., Neufer P.D. Assessment of in vivo skeletal muscle mitochondrial respiratory capacity in humans by near-infrared spectroscopy: a comparison with in situ measurements. J. Physiol. 2014, 592:3231-3241.
    • (2014) J. Physiol. , vol.592 , pp. 3231-3241
    • Ryan, T.E.1    Brophy, P.2    Lin, C.T.3    Hickner, R.C.4    Neufer, P.D.5
  • 89
    • 84884813517 scopus 로고    scopus 로고
    • Near-infrared assessments of skeletal muscle oxidative capacity in persons with spinal cord injury
    • Erickson M.L., Ryan T.E., Young H.J., McCully K.K. Near-infrared assessments of skeletal muscle oxidative capacity in persons with spinal cord injury. Eur. J. Appl. Physiol. 2013, 113:2275-2283.
    • (2013) Eur. J. Appl. Physiol. , vol.113 , pp. 2275-2283
    • Erickson, M.L.1    Ryan, T.E.2    Young, H.J.3    McCully, K.K.4
  • 91
    • 0026563676 scopus 로고
    • NMR determination of the TCA cycle rate and alpha-ketoglutarate/glutamate exchange rate in rat brain
    • Mason G.F., Rothman D.L., Behar K.L., Shulman R.G. NMR determination of the TCA cycle rate and alpha-ketoglutarate/glutamate exchange rate in rat brain. J. Cereb. Blood Flow Metab. 1992, 12:434-447.
    • (1992) J. Cereb. Blood Flow Metab. , vol.12 , pp. 434-447
    • Mason, G.F.1    Rothman, D.L.2    Behar, K.L.3    Shulman, R.G.4
  • 92
    • 34248141686 scopus 로고    scopus 로고
    • Impaired mitochondrial substrate oxidation in muscle of insulin-resistant offspring of type 2 diabetic patients
    • Befroy D.E., Petersen K.F., Dufour S., Mason G.F., de Graaf R.A., Rothman D.L., Shulman G.I. Impaired mitochondrial substrate oxidation in muscle of insulin-resistant offspring of type 2 diabetic patients. Diabetes 2007, 56:1376-1381.
    • (2007) Diabetes , vol.56 , pp. 1376-1381
    • Befroy, D.E.1    Petersen, K.F.2    Dufour, S.3    Mason, G.F.4    de Graaf, R.A.5    Rothman, D.L.6    Shulman, G.I.7
  • 97
    • 65649106160 scopus 로고    scopus 로고
    • Modular regulation analysis of integrative effects of hypoxia on the energetics of contracting skeletal muscle in vivo
    • Beuste C., Miraux S., Deschodt-Arsac V.J., Thiaudiere E., Franconi J.M., Diolez P., Arsac L.M. Modular regulation analysis of integrative effects of hypoxia on the energetics of contracting skeletal muscle in vivo. Biochem. J. 2009, 420:67-72.
    • (2009) Biochem. J. , vol.420 , pp. 67-72
    • Beuste, C.1    Miraux, S.2    Deschodt-Arsac, V.J.3    Thiaudiere, E.4    Franconi, J.M.5    Diolez, P.6    Arsac, L.M.7
  • 99
    • 0035059633 scopus 로고    scopus 로고
    • Large energetic adaptations of elderly muscle to resistance and endurance training
    • Jubrias S.A., Esselman P.C., Price L.B., Cress M.E., Conley K.E. Large energetic adaptations of elderly muscle to resistance and endurance training. J. Appl. Physiol. 2001, 90:1663-1670.
    • (2001) J. Appl. Physiol. , vol.90 , pp. 1663-1670
    • Jubrias, S.A.1    Esselman, P.C.2    Price, L.B.3    Cress, M.E.4    Conley, K.E.5
  • 100
    • 79957576648 scopus 로고    scopus 로고
    • Bioenergetic function in cardiovascular cells: the importance of the reserve capacity and its biological regulation
    • Sansbury B.E., Jones S.P., Riggs D.W., Darley-Usmar V.M., Hill B.G. Bioenergetic function in cardiovascular cells: the importance of the reserve capacity and its biological regulation. Chem. Biol. Interact. 2011, 191:288-295.
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 288-295
    • Sansbury, B.E.1    Jones, S.P.2    Riggs, D.W.3    Darley-Usmar, V.M.4    Hill, B.G.5
  • 101
    • 73249150574 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle cell bioenergetic function by protein glutathiolation
    • Hill B.G., Higdon A.N., Dranka B.P., Darley-Usmar V.M. Regulation of vascular smooth muscle cell bioenergetic function by protein glutathiolation. Biochim. Biophys. Acta 2010, 1797:285-295.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 285-295
    • Hill, B.G.1    Higdon, A.N.2    Dranka, B.P.3    Darley-Usmar, V.M.4
  • 102
    • 84923912767 scopus 로고    scopus 로고
    • S-glutathionylation reactions in mitochondrial function and disease
    • Mailloux R.J., Willmore W.G. S-glutathionylation reactions in mitochondrial function and disease. Front. Cell Dev. Biol. 2014, 2:68.
    • (2014) Front. Cell Dev. Biol. , vol.2 , pp. 68
    • Mailloux, R.J.1    Willmore, W.G.2
  • 103
    • 54049146740 scopus 로고    scopus 로고
    • Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of CYS residues in decreasing oxidative damage
    • Hurd T.R., Requejo R., Filipovska A., Brown S., Prime T.A., Robinson A.J., Fearnley I.M., Murphy M.P. Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of CYS residues in decreasing oxidative damage. J. Biolog. Chem. 2008, 283:24801-24815.
    • (2008) J. Biolog. Chem. , vol.283 , pp. 24801-24815
    • Hurd, T.R.1    Requejo, R.2    Filipovska, A.3    Brown, S.4    Prime, T.A.5    Robinson, A.J.6    Fearnley, I.M.7    Murphy, M.P.8
  • 104
    • 37849043898 scopus 로고    scopus 로고
    • Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: glutathionylation and protection of lipoic acid
    • Applegate M.A., Humphries K.M., Szweda L.I. Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: glutathionylation and protection of lipoic acid. Biochemistry 2008, 47:473-478.
    • (2008) Biochemistry , vol.47 , pp. 473-478
    • Applegate, M.A.1    Humphries, K.M.2    Szweda, L.I.3
  • 106
    • 84888199189 scopus 로고    scopus 로고
    • Activity-induced changes in skeletal muscle metabolism measured with optical spectroscopy
    • Ryan T.E., Southern W.M., Brizendine J.T., McCully K.K. Activity-induced changes in skeletal muscle metabolism measured with optical spectroscopy. Med. Sci. Sports Exerc. 2013, 45:2346-2352.
    • (2013) Med. Sci. Sports Exerc. , vol.45 , pp. 2346-2352
    • Ryan, T.E.1    Southern, W.M.2    Brizendine, J.T.3    McCully, K.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.