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Volumn 11, Issue 8, 2011, Pages 1413-1428

2-D DIGE analysis of the mitochondrial proteome from human skeletal muscle reveals time course-dependent remodelling in response to 14 consecutive days of endurance exercise training

Author keywords

2 D DIGE; Biomedicine; Exercise training; Mitochondrial proteome; Skeletal muscle

Indexed keywords

ADENOSINE TRIPHOSPHATE; MITOCHONDRIAL PROTEIN;

EID: 79953727541     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000597     Document Type: Article
Times cited : (59)

References (74)
  • 1
    • 0035985859 scopus 로고    scopus 로고
    • Waging war on physical inactivity: using modern molecular ammunition against an ancient enemy
    • Booth, F. W., Chakravarthy, M. V., Gordon, S. E., Spangenburg, E. E., Waging war on physical inactivity: using modern molecular ammunition against an ancient enemy. J. Appl. Physiol. 2002, 93, 3-30.
    • (2002) J. Appl. Physiol. , vol.93 , pp. 3-30
    • Booth, F.W.1    Chakravarthy, M.V.2    Gordon, S.E.3    Spangenburg, E.E.4
  • 2
    • 65649117349 scopus 로고    scopus 로고
    • Cardiorespiratory fitness as a quantitative predictor of all-cause mortality and cardiovascular events in healthy men and women: a meta-analysis
    • Kodama, S., Saito, K., Tanaka, S., Maki, M. et al., Cardiorespiratory fitness as a quantitative predictor of all-cause mortality and cardiovascular events in healthy men and women: a meta-analysis. J. Am. Med. Assoc. 2009, 301, 2024-2035.
    • (2009) J. Am. Med. Assoc. , vol.301 , pp. 2024-2035
    • Kodama, S.1    Saito, K.2    Tanaka, S.3    Maki, M.4
  • 3
    • 4644235275 scopus 로고    scopus 로고
    • Exercise as a therapeutic intervention for the prevention and treatment of insulin resistance
    • Hawley, J. A., Exercise as a therapeutic intervention for the prevention and treatment of insulin resistance. Diabetes Metab. Res. Rev. 2004, 20, 383-393.
    • (2004) Diabetes Metab. Res. Rev. , vol.20 , pp. 383-393
    • Hawley, J.A.1
  • 4
    • 33746012931 scopus 로고    scopus 로고
    • Functional, structural and molecular plasticity of mammalian skeletal muscle in response to exercise stimuli
    • Fluck, M., Functional, structural and molecular plasticity of mammalian skeletal muscle in response to exercise stimuli. J. Exp. Biol. 2006, 209, 2239-2248.
    • (2006) J. Exp. Biol. , vol.209 , pp. 2239-2248
    • Fluck, M.1
  • 5
    • 33746009957 scopus 로고    scopus 로고
    • Coordination of metabolic plasticity in skeletal muscle
    • Hood, D. A., Irrcher, I., Ljubicic, V., Joseph, A. M., Coordination of metabolic plasticity in skeletal muscle. J. Exp. Biol. 2006, 209, 2265-2275.
    • (2006) J. Exp. Biol. , vol.209 , pp. 2265-2275
    • Hood, D.A.1    Irrcher, I.2    Ljubicic, V.3    Joseph, A.M.4
  • 6
    • 0021343295 scopus 로고
    • Adaptations of skeletal muscle to endurance exercise and their metabolic consequences
    • Holloszy, J. O., Coyle, E. F., Adaptations of skeletal muscle to endurance exercise and their metabolic consequences. J. Appl. Physiol. 1984, 56, 831-838.
    • (1984) J. Appl. Physiol. , vol.56 , pp. 831-838
    • Holloszy, J.O.1    Coyle, E.F.2
  • 7
    • 0014198263 scopus 로고
    • Biochemical adaptations in muscle. Effects of exercise on mitochondrial oxygen uptake and respiratory enzyme activity in skeletal muscle
    • Holloszy, J. O., Biochemical adaptations in muscle. Effects of exercise on mitochondrial oxygen uptake and respiratory enzyme activity in skeletal muscle. J. Biol. Chem. 1967, 242, 2278-2282.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2278-2282
    • Holloszy, J.O.1
  • 8
    • 12344305124 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and type 2 diabetes
    • Lowell, B. B., Shulman, G. I., Mitochondrial dysfunction and type 2 diabetes. Science 2005, 307, 384-387.
    • (2005) Science , vol.307 , pp. 384-387
    • Lowell, B.B.1    Shulman, G.I.2
  • 9
    • 77449155964 scopus 로고    scopus 로고
    • Proteomics analysis of human skeletal muscle reveals novel abnormalities in obesity and type 2 diabetes
    • Hwang, H., Bowen, B. P., Lefort, N., Flynn, C. R. et al., Proteomics analysis of human skeletal muscle reveals novel abnormalities in obesity and type 2 diabetes. Diabetes 2010, 59, 33-42.
    • (2010) Diabetes , vol.59 , pp. 33-42
    • Hwang, H.1    Bowen, B.P.2    Lefort, N.3    Flynn, C.R.4
  • 10
    • 58149345928 scopus 로고    scopus 로고
    • Endurance exercise as a countermeasure for aging
    • Lanza, I. R., Short, D. K., Short, K. R., Raghavakaimal, S. et al., Endurance exercise as a countermeasure for aging. Diabetes 2008, 57, 2933-2942.
    • (2008) Diabetes , vol.57 , pp. 2933-2942
    • Lanza, I.R.1    Short, D.K.2    Short, K.R.3    Raghavakaimal, S.4
  • 11
    • 17844391820 scopus 로고    scopus 로고
    • Proteome analysis of skeletal muscle from obese and morbidly obese women
    • Hittel, D. S., Hathout, Y., Hoffman, E. P., Houmard, J. A., Proteome analysis of skeletal muscle from obese and morbidly obese women. Diabetes 2005, 54, 1283-1288.
    • (2005) Diabetes , vol.54 , pp. 1283-1288
    • Hittel, D.S.1    Hathout, Y.2    Hoffman, E.P.3    Houmard, J.A.4
  • 12
    • 0038576291 scopus 로고    scopus 로고
    • Proteome analysis reveals phosphorylation of ATP synthase beta-subunit in human skeletal muscle and proteins with potential roles in type 2 diabetes
    • Hojlund, K., Wrzesinski, K., Larsen, P. M., Fey, S. J. et al., Proteome analysis reveals phosphorylation of ATP synthase beta-subunit in human skeletal muscle and proteins with potential roles in type 2 diabetes. J. Biol. Chem. 2003, 278, 10436-10442.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10436-10442
    • Hojlund, K.1    Wrzesinski, K.2    Larsen, P.M.3    Fey, S.J.4
  • 13
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: a single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M. E., Minden, J. S., Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 14
    • 27744583045 scopus 로고    scopus 로고
    • All about DIGE: quantification technology for differential-display 2D-gel proteomics
    • Lilley, K. S., Friedman, D. B., All about DIGE: quantification technology for differential-display 2D-gel proteomics. Expert Rev. Proteomics 2004, 1, 401-409.
    • (2004) Expert Rev. Proteomics , vol.1 , pp. 401-409
    • Lilley, K.S.1    Friedman, D.B.2
  • 15
    • 70949099713 scopus 로고    scopus 로고
    • Proteomic investigation of changes in human vastus lateralis muscle in response to interval-exercise training
    • Holloway, K. V., O'Gorman, M., Woods, P., Morton, J. P. et al., Proteomic investigation of changes in human vastus lateralis muscle in response to interval-exercise training. Proteomics 2009, 9, 5155-5174.
    • (2009) Proteomics , vol.9 , pp. 5155-5174
    • Holloway, K.V.1    O'Gorman, M.2    Woods, P.3    Morton, J.P.4
  • 16
    • 52449135519 scopus 로고    scopus 로고
    • Changes in the rat skeletal muscle proteome induced by moderate-intensity endurance exercise
    • Burniston, J. G., Changes in the rat skeletal muscle proteome induced by moderate-intensity endurance exercise. Biochim. Biophys. Acta 2008, 1784, 1077-1086.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1077-1086
    • Burniston, J.G.1
  • 17
    • 50949084931 scopus 로고    scopus 로고
    • Mitochondrial comparative proteomics: strengths and pitfalls
    • Mathy, G., Sluse, F. E., Mitochondrial comparative proteomics: strengths and pitfalls. Biochim. Biophys. Acta 2008, 1777, 1072-1077.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1072-1077
    • Mathy, G.1    Sluse, F.E.2
  • 18
    • 0030054370 scopus 로고    scopus 로고
    • Mitochondrial enzymes increase in muscle in response to 7-10 days of cycle exercise
    • Spina, R. J., Chi, M. M., Hopkins, M. G., Nemeth, P. M. et al., Mitochondrial enzymes increase in muscle in response to 7-10 days of cycle exercise. J. Appl. Physiol. 1996, 80, 2250-2254.
    • (1996) J. Appl. Physiol. , vol.80 , pp. 2250-2254
    • Spina, R.J.1    Chi, M.M.2    Hopkins, M.G.3    Nemeth, P.M.4
  • 19
    • 0033011789 scopus 로고    scopus 로고
    • Effect of short-term training on mitochondrial ATP production rate in human skeletal muscle
    • Starritt, E. C., Angus, D., Hargreaves, M., Effect of short-term training on mitochondrial ATP production rate in human skeletal muscle. J. Appl. Physiol. 1999, 86, 450-454.
    • (1999) J. Appl. Physiol. , vol.86 , pp. 450-454
    • Starritt, E.C.1    Angus, D.2    Hargreaves, M.3
  • 20
    • 0020024468 scopus 로고
    • Suction applied to a muscle biopsy maximizes sample size
    • Evans, W. J., Phinney, S. D., Young, V. R., Suction applied to a muscle biopsy maximizes sample size. Med. Sci. Sports Exerc. 1982, 14, 101-102.
    • (1982) Med. Sci. Sports Exerc. , vol.14 , pp. 101-102
    • Evans, W.J.1    Phinney, S.D.2    Young, V.R.3
  • 21
    • 33845997409 scopus 로고    scopus 로고
    • Proteomic screening of glucose-responsive and glucose non-responsive MIN-6 beta cells reveals differential expression of proteins involved in protein folding, secretion and oxidative stress
    • Dowling, P., O'Driscoll, L., O'Sullivan, F., Dowd, A. et al., Proteomic screening of glucose-responsive and glucose non-responsive MIN-6 beta cells reveals differential expression of proteins involved in protein folding, secretion and oxidative stress. Proteomics 2006, 6, 6578-6587.
    • (2006) Proteomics , vol.6 , pp. 6578-6587
    • Dowling, P.1    O'Driscoll, L.2    O'Sullivan, F.3    Dowd, A.4
  • 22
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V. et al., In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 2006, 1, 2856-2860.
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4
  • 23
    • 67650553054 scopus 로고    scopus 로고
    • MitoMiner, an integrated database for the storage and analysis of mitochondrial proteomics data
    • Smith, A. C., Robinson, A. J., MitoMiner, an integrated database for the storage and analysis of mitochondrial proteomics data. Mol. Cell. Proteomics 2009, 8, 1324-1337.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1324-1337
    • Smith, A.C.1    Robinson, A.J.2
  • 24
    • 55749085987 scopus 로고    scopus 로고
    • Proteomics of mitochondrial inner and outer membranes
    • Distler, A. M., Kerner, J., Hoppel, C. L., Proteomics of mitochondrial inner and outer membranes. Proteomics 2008, 8, 4066-4082.
    • (2008) Proteomics , vol.8 , pp. 4066-4082
    • Distler, A.M.1    Kerner, J.2    Hoppel, C.L.3
  • 25
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner, F., Foster, L. J., Campanaro, S., Valle, G. et al., Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol. Cell. Proteomics 2006, 5, 608-619.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4
  • 26
    • 67651151024 scopus 로고    scopus 로고
    • Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS
    • Lefort, N., Yi, Z., Bowen, B., Glancy, B. et al., Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS. J. Proteomics 2009, 72, 1046-1060.
    • (2009) J. Proteomics , vol.72 , pp. 1046-1060
    • Lefort, N.1    Yi, Z.2    Bowen, B.3    Glancy, B.4
  • 27
    • 73149108205 scopus 로고    scopus 로고
    • Proteomic DIGE analysis of the mitochondria-enriched fraction from aged rat skeletal muscle
    • O'Connell, K., Ohlendieck, K., Proteomic DIGE analysis of the mitochondria-enriched fraction from aged rat skeletal muscle. Proteomics 2009, 9, 5509-5524.
    • (2009) Proteomics , vol.9 , pp. 5509-5524
    • O'Connell, K.1    Ohlendieck, K.2
  • 28
    • 0035112481 scopus 로고    scopus 로고
    • Invited review: contractile activity-induced mitochondrial biogenesis in skeletal muscle
    • Hood, D. A., Invited review: contractile activity-induced mitochondrial biogenesis in skeletal muscle. J. Appl. Physiol. 2001, 90, 1137-1157.
    • (2001) J. Appl. Physiol. , vol.90 , pp. 1137-1157
    • Hood, D.A.1
  • 29
    • 0024551620 scopus 로고
    • Muscle energetics during prolonged cycling after exercise hypervolemia
    • Green, H. J., Jones, L. L., Houston, M. E., Ball-Burnett, M. E. et al., Muscle energetics during prolonged cycling after exercise hypervolemia. J. Appl. Physiol. 1989, 66, 622-631.
    • (1989) J. Appl. Physiol. , vol.66 , pp. 622-631
    • Green, H.J.1    Jones, L.L.2    Houston, M.E.3    Ball-Burnett, M.E.4
  • 30
    • 0028816442 scopus 로고
    • Adaptations in muscle metabolism to prolonged voluntary exercise and training
    • Green, H. J., Jones, S., Ball-Burnett, M., Farrance, B. et al., Adaptations in muscle metabolism to prolonged voluntary exercise and training. J. Appl. Physiol. 1995, 78, 138-145.
    • (1995) J. Appl. Physiol. , vol.78 , pp. 138-145
    • Green, H.J.1    Jones, S.2    Ball-Burnett, M.3    Farrance, B.4
  • 31
    • 0022994155 scopus 로고
    • Chronic stimulation of mammalian muscle: changes in enzymes of six metabolic pathways
    • Henriksson, J., Chi, M. M., Hintz, C. S., Young, D. A. et al., Chronic stimulation of mammalian muscle: changes in enzymes of six metabolic pathways. Am. J. Physiol. 1986, 251, C614-C632.
    • (1986) Am. J. Physiol. , vol.251
    • Henriksson, J.1    Chi, M.M.2    Hintz, C.S.3    Young, D.A.4
  • 32
    • 45149104369 scopus 로고    scopus 로고
    • Training at high exercise intensity promotes qualitative adaptations of mitochondrial function in human skeletal muscle
    • Daussin, F. N., Zoll, J., Ponsot, E., Dufour, S. P. et al., Training at high exercise intensity promotes qualitative adaptations of mitochondrial function in human skeletal muscle. J. Appl. Physiol. 2008, 104, 1436-1441.
    • (2008) J. Appl. Physiol. , vol.104 , pp. 1436-1441
    • Daussin, F.N.1    Zoll, J.2    Ponsot, E.3    Dufour, S.P.4
  • 33
    • 77951738458 scopus 로고    scopus 로고
    • A practical model of low-volume high-intensity interval training induces mitochondrial biogenesis in human skeletal muscle: potential mechanisms
    • Little, J. P., Safdar, A., Wilkin, G. P., Tarnopolsky, M. A. et al., A practical model of low-volume high-intensity interval training induces mitochondrial biogenesis in human skeletal muscle: potential mechanisms. J. Physiol. 2010, 588, 1011-1022.
    • (2010) J. Physiol. , vol.588 , pp. 1011-1022
    • Little, J.P.1    Safdar, A.2    Wilkin, G.P.3    Tarnopolsky, M.A.4
  • 34
    • 0023424197 scopus 로고
    • Differential effectiveness of yeast cytochrome c oxidase subunit genes results from differences in expression not function
    • Trueblood, C. E., Poyton, R. O., Differential effectiveness of yeast cytochrome c oxidase subunit genes results from differences in expression not function. Mol. Cell. Biol. 1987, 7, 3520-3526.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3520-3526
    • Trueblood, C.E.1    Poyton, R.O.2
  • 35
    • 0026480393 scopus 로고
    • Selective removal of subunit VIb increases the activity of cytochrome c oxidase
    • Weishaupt, A., Kadenbach, B., Selective removal of subunit VIb increases the activity of cytochrome c oxidase. Biochemistry 1992, 31, 11477-11481.
    • (1992) Biochemistry , vol.31 , pp. 11477-11481
    • Weishaupt, A.1    Kadenbach, B.2
  • 36
    • 0021339157 scopus 로고
    • Enzyme levels in pools of microdissected human muscle fibres of identified type. Adaptive response to exercise
    • Essen-Gustavsson, B., Henriksson, J., Enzyme levels in pools of microdissected human muscle fibres of identified type. Adaptive response to exercise. Acta Physiol. Scand. 1984, 120, 505-515.
    • (1984) Acta Physiol. Scand. , vol.120 , pp. 505-515
    • Essen-Gustavsson, B.1    Henriksson, J.2
  • 37
    • 0014968409 scopus 로고
    • Mitochondrial citric acid cycle and related enzymes: adaptive response to exercise
    • Holloszy, J. O., Oscai, L. B., Don, I. J., Mole, P. A., Mitochondrial citric acid cycle and related enzymes: adaptive response to exercise. Biochem. Biophys. Res. Commun. 1970, 40, 1368-1373.
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 1368-1373
    • Holloszy, J.O.1    Oscai, L.B.2    Don, I.J.3    Mole, P.A.4
  • 38
    • 0017164457 scopus 로고
    • Skeletal muscle enzyme alterations after sprint and endurance training
    • Hickson, R. C., Heusner, W. W., Van Huss, W. D., Skeletal muscle enzyme alterations after sprint and endurance training. J. Appl. Physiol. 1976, 40, 868-871.
    • (1976) J. Appl. Physiol. , vol.40 , pp. 868-871
    • Hickson, R.C.1    Heusner, W.W.2    Van Huss, W.D.3
  • 39
    • 0022970635 scopus 로고
    • Malate-aspartate and alpha-glycerophosphate shuttle enzyme levels in human skeletal muscle: methodological considerations and effect of endurance training
    • Schantz, P. G., Sjoberg, B., Svedenhag, J., Malate-aspartate and alpha-glycerophosphate shuttle enzyme levels in human skeletal muscle: methodological considerations and effect of endurance training. Acta Physiol. Scand. 1986, 128, 397-407.
    • (1986) Acta Physiol. Scand. , vol.128 , pp. 397-407
    • Schantz, P.G.1    Sjoberg, B.2    Svedenhag, J.3
  • 40
    • 11144326391 scopus 로고    scopus 로고
    • Exercise training increases electron and substrate shuttling proteins in muscle of overweight men and women with the metabolic syndrome
    • Hittel, D. S., Kraus, W. E., Tanner, C. J., Houmard, J. A. et al., Exercise training increases electron and substrate shuttling proteins in muscle of overweight men and women with the metabolic syndrome. J. Appl. Physiol. 2005, 98, 168-179.
    • (2005) J. Appl. Physiol. , vol.98 , pp. 168-179
    • Hittel, D.S.1    Kraus, W.E.2    Tanner, C.J.3    Houmard, J.A.4
  • 41
    • 0035893452 scopus 로고    scopus 로고
    • The role of phosphorylcreatine and creatine in the regulation of mitochondrial respiration in human skeletal muscle
    • Walsh, B., Tonkonogi, M., Soderlund, K., Hultman, E. et al., The role of phosphorylcreatine and creatine in the regulation of mitochondrial respiration in human skeletal muscle. J. Physiol. 2001, 537, 971-978.
    • (2001) J. Physiol. , vol.537 , pp. 971-978
    • Walsh, B.1    Tonkonogi, M.2    Soderlund, K.3    Hultman, E.4
  • 42
    • 0035990408 scopus 로고    scopus 로고
    • Physical exercise and mitochondrial function in human skeletal muscle
    • Tonkonogi, M., Sahlin, K., Physical exercise and mitochondrial function in human skeletal muscle. Exerc. Sport Sci. Rev. 2002, 30, 129-137.
    • (2002) Exerc. Sport Sci. Rev. , vol.30 , pp. 129-137
    • Tonkonogi, M.1    Sahlin, K.2
  • 43
    • 0028017703 scopus 로고
    • Metabolic compartmentation and substrate channelling in muscle cells. Role of coupled creatine kinases in in vivo regulation of cellular respiration - a synthesis
    • Saks, V. A., Khuchua, Z. A., Vasilyeva, E. V., Belikova, O. Y. et al., Metabolic compartmentation and substrate channelling in muscle cells. Role of coupled creatine kinases in in vivo regulation of cellular respiration - a synthesis. Mol. Cell. Biochem. 1994, 133-134, 155-192.
    • (1994) Mol. Cell. Biochem. , vol.133-134 , pp. 155-192
    • Saks, V.A.1    Khuchua, Z.A.2    Vasilyeva, E.V.3    Belikova, O.Y.4
  • 44
    • 21344434137 scopus 로고    scopus 로고
    • Impaired voluntary running capacity of creatine kinase-deficient mice
    • Momken, I., Lechene, P., Koulmann, N., Fortin, D. et al., Impaired voluntary running capacity of creatine kinase-deficient mice. J. Physiol. 2005, 565, 951-964.
    • (2005) J. Physiol. , vol.565 , pp. 951-964
    • Momken, I.1    Lechene, P.2    Koulmann, N.3    Fortin, D.4
  • 45
    • 0037101919 scopus 로고    scopus 로고
    • Physical activity changes the regulation of mitochondrial respiration in human skeletal muscle
    • Zoll, J., Sanchez, H., N'Guessan, B., Ribera, F. et al., Physical activity changes the regulation of mitochondrial respiration in human skeletal muscle. J. Physiol. 2002, 543, 191-200.
    • (2002) J. Physiol. , vol.543 , pp. 191-200
    • Zoll, J.1    Sanchez, H.2    N'Guessan, B.3    Ribera, F.4
  • 46
    • 0023044179 scopus 로고
    • The complete primary structure of GTP:AMP phosphotransferase from beef heart mitochondria
    • Tomasselli, A. G., Frank, R., Schiltz, E., The complete primary structure of GTP:AMP phosphotransferase from beef heart mitochondria. FEBS Lett. 1986, 202, 303-308.
    • (1986) FEBS Lett. , vol.202 , pp. 303-308
    • Tomasselli, A.G.1    Frank, R.2    Schiltz, E.3
  • 47
    • 0029566293 scopus 로고
    • Strain-dependent occurrence of functional GTP:AMP phosphotransferase (AK3) in Saccharomyces cerevisiae
    • Schricker, R., Magdolen, V., Strobel, G., Bogengruber, E. et al., Strain-dependent occurrence of functional GTP:AMP phosphotransferase (AK3) in Saccharomyces cerevisiae. J. Biol. Chem. 1995, 270, 31103-31110.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31103-31110
    • Schricker, R.1    Magdolen, V.2    Strobel, G.3    Bogengruber, E.4
  • 48
    • 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
  • 49
    • 0022260872 scopus 로고
    • Endurance training in humans: aerobic capacity and structure of skeletal muscle
    • Hoppeler, H., Howald, H., Conley, K., Lindstedt, S. L. et al., Endurance training in humans: aerobic capacity and structure of skeletal muscle. J. Appl. Physiol. 1985, 59, 320-327.
    • (1985) J. Appl. Physiol. , vol.59 , pp. 320-327
    • Hoppeler, H.1    Howald, H.2    Conley, K.3    Lindstedt, S.L.4
  • 50
    • 0017625186 scopus 로고
    • Effects of endurance exercise on cytochrome C turnover in skeletal muscle
    • Booth, F., Effects of endurance exercise on cytochrome C turnover in skeletal muscle. Ann. NY Acad. Sci. 1977, 301, 431-439.
    • (1977) Ann. NY Acad. Sci. , vol.301 , pp. 431-439
    • Booth, F.1
  • 51
    • 67651120134 scopus 로고    scopus 로고
    • The exercise-induced stress response of skeletal muscle, with specific emphasis on humans
    • Morton, J. P., Kayani, A. C., McArdle, A., Drust, B., The exercise-induced stress response of skeletal muscle, with specific emphasis on humans. Sports Med. 2009, 39, 643-662.
    • (2009) Sports Med. , vol.39 , pp. 643-662
    • Morton, J.P.1    Kayani, A.C.2    McArdle, A.3    Drust, B.4
  • 52
    • 0031888307 scopus 로고    scopus 로고
    • Transient regulation of c-fos, alpha B-crystallin, and hsp70 in muscle during recovery from contractile activity
    • Neufer, P. D., Ordway, G. A., Williams, R. S., Transient regulation of c-fos, alpha B-crystallin, and hsp70 in muscle during recovery from contractile activity. Am. J. Physiol. 1998, 274, C341-C346.
    • (1998) Am. J. Physiol. , vol.274
    • Neufer, P.D.1    Ordway, G.A.2    Williams, R.S.3
  • 53
    • 66349132499 scopus 로고    scopus 로고
    • Reduced carbohydrate availability does not modulate training-induced heat shock protein adaptations but does upregulate oxidative enzyme activity in human skeletal muscle
    • Morton, J. P., Croft, L., Bartlett, J. D., Maclaren, D. P. et al., Reduced carbohydrate availability does not modulate training-induced heat shock protein adaptations but does upregulate oxidative enzyme activity in human skeletal muscle. J. Appl. Physiol. 2009, 106, 1513-1521.
    • (2009) J. Appl. Physiol. , vol.106 , pp. 1513-1521
    • Morton, J.P.1    Croft, L.2    Bartlett, J.D.3    Maclaren, D.P.4
  • 54
    • 0028234368 scopus 로고
    • Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria
    • Hohfeld, J., Hartl, F. U., Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. J. Cell. Biol. 1994, 126, 305-315.
    • (1994) J. Cell. Biol. , vol.126 , pp. 305-315
    • Hohfeld, J.1    Hartl, F.U.2
  • 55
    • 77954399940 scopus 로고    scopus 로고
    • Overexpression of HSP10 in skeletal muscle of transgenic mice prevents the age-related fall in maximum tetanic force generation and muscle Cross-Sectional Area
    • Kayani, A. C., Close, G. L., Dillmann, W. H., Mestril, R. et al., Overexpression of HSP10 in skeletal muscle of transgenic mice prevents the age-related fall in maximum tetanic force generation and muscle Cross-Sectional Area. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2010, 299, R268-R276.
    • (2010) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.299
    • Kayani, A.C.1    Close, G.L.2    Dillmann, W.H.3    Mestril, R.4
  • 56
    • 33947518803 scopus 로고    scopus 로고
    • Chaperone properties of mammalian mitochondrial translation elongation factor Tu
    • Suzuki, H., Ueda, T., Taguchi, H., Takeuchi, N., Chaperone properties of mammalian mitochondrial translation elongation factor Tu. J. Biol. Chem. 2007, 282, 4076-4084.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4076-4084
    • Suzuki, H.1    Ueda, T.2    Taguchi, H.3    Takeuchi, N.4
  • 58
    • 2442534124 scopus 로고    scopus 로고
    • ERp57 is a multifunctional thiol-disulfide oxidoreductase
    • Frickel, E. M., Frei, P., Bouvier, M., Stafford, W. F. et al., ERp57 is a multifunctional thiol-disulfide oxidoreductase. J. Biol. Chem. 2004, 279, 18277-18287.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18277-18287
    • Frickel, E.M.1    Frei, P.2    Bouvier, M.3    Stafford, W.F.4
  • 59
    • 50849127125 scopus 로고    scopus 로고
    • ERp57-associated mitochondrial micro-calpain truncates apoptosis-inducing factor
    • Ozaki, T., Yamashita, T., Ishiguro, S., ERp57-associated mitochondrial micro-calpain truncates apoptosis-inducing factor. Biochim. Biophys. Acta 2008, 1783, 1955-1963.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1955-1963
    • Ozaki, T.1    Yamashita, T.2    Ishiguro, S.3
  • 60
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller, F. L., Liu, Y., Van, R. H., Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 2004, 279, 49064-49073.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van, R.H.3
  • 61
    • 77950340598 scopus 로고    scopus 로고
    • Oxidative stress in skeletal muscle causes severe disturbance of exercise activity without muscle atrophy
    • Kuwahara, H., Horie, T., Ishikawa, S., Tsuda, C. et al., Oxidative stress in skeletal muscle causes severe disturbance of exercise activity without muscle atrophy. Free Radic. Biol. Med. 2010, 48, 1252-1262.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 1252-1262
    • Kuwahara, H.1    Horie, T.2    Ishikawa, S.3    Tsuda, C.4
  • 62
    • 0027372086 scopus 로고
    • High intensity training-induced changes in skeletal muscle antioxidant enzyme activity
    • Criswell, D., Powers, S., Dodd, S., Lawler, J. et al., High intensity training-induced changes in skeletal muscle antioxidant enzyme activity. Med. Sci. Sports Exerc. 1993, 25, 1135-1140.
    • (1993) Med. Sci. Sports Exerc. , vol.25 , pp. 1135-1140
    • Criswell, D.1    Powers, S.2    Dodd, S.3    Lawler, J.4
  • 63
    • 74049129489 scopus 로고    scopus 로고
    • Reactive oxygen species are signalling molecules for skeletal muscle adaptation
    • Powers, S. K., Duarte, J., Kavazis, A. N., Talbert, E. E., Reactive oxygen species are signalling molecules for skeletal muscle adaptation. Exp. Physiol. 2010, 95, 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
  • 64
    • 6344277177 scopus 로고    scopus 로고
    • Myoglobin: an essential hemoprotein in striated muscle
    • Ordway, G. A., Garry, D. J., Myoglobin: an essential hemoprotein in striated muscle. J. Exp. Biol. 2004, 207, 3441-3446.
    • (2004) J. Exp. Biol. , vol.207 , pp. 3441-3446
    • Ordway, G.A.1    Garry, D.J.2
  • 65
    • 0019370898 scopus 로고
    • Skeletal muscle cytochrome c and myoglobin, endurance, and frequency of training
    • Hickson, R. C., Skeletal muscle cytochrome c and myoglobin, endurance, and frequency of training. J. Appl. Physiol. 1981, 51, 746-749.
    • (1981) J. Appl. Physiol. , vol.51 , pp. 746-749
    • Hickson, R.C.1
  • 66
    • 0024504584 scopus 로고
    • Electrostimulation-induced increases in fatty acid-binding protein and myoglobin in rat fast-twitch muscle and comparison with tissue levels in heart
    • Kaufmann, M., Simoneau, J. A., Veerkamp, J. H., Pette, D., Electrostimulation-induced increases in fatty acid-binding protein and myoglobin in rat fast-twitch muscle and comparison with tissue levels in heart. FEBS Lett. 1989, 245, 181-184.
    • (1989) FEBS Lett. , vol.245 , pp. 181-184
    • Kaufmann, M.1    Simoneau, J.A.2    Veerkamp, J.H.3    Pette, D.4
  • 67
    • 0020533521 scopus 로고
    • Dissociation of training effects on skeletal muscle mitochondrial enzymes and myoglobin in man
    • Svedenhag, J., Henriksson, J., Sylven, C., Dissociation of training effects on skeletal muscle mitochondrial enzymes and myoglobin in man. Acta Physiol. Scand. 1983, 117, 213-218.
    • (1983) Acta Physiol. Scand. , vol.117 , pp. 213-218
    • Svedenhag, J.1    Henriksson, J.2    Sylven, C.3
  • 68
    • 1642420443 scopus 로고    scopus 로고
    • Adaptations in human muscle sarcoplasmic reticulum to prolonged submaximal training
    • Green, H. J., Ballantyne, C. S., MacDougall, J. D., Tarnopolsky, M. A. et al., Adaptations in human muscle sarcoplasmic reticulum to prolonged submaximal training. J. Appl. Physiol. 2003, 94, 2034-2042.
    • (2003) J. Appl. Physiol. , vol.94 , pp. 2034-2042
    • Green, H.J.1    Ballantyne, C.S.2    MacDougall, J.D.3    Tarnopolsky, M.A.4
  • 69
    • 34047219171 scopus 로고    scopus 로고
    • SERCA pump isoforms: their role in calcium transport and disease
    • Periasamy, M., Kalyanasundaram, A., SERCA pump isoforms: their role in calcium transport and disease. Muscle Nerve 2007, 35, 430-442.
    • (2007) Muscle Nerve , vol.35 , pp. 430-442
    • Periasamy, M.1    Kalyanasundaram, A.2
  • 70
    • 0030765223 scopus 로고    scopus 로고
    • Role of sarcoplasmic/endoplasmic-reticulum Ca2+-ATPases in mediating Ca2+waves and local Ca2+-release microdomains in cultured glia
    • Simpson, P. B., Russell, J. T., Role of sarcoplasmic/endoplasmic-reticulum Ca2+-ATPases in mediating Ca2+waves and local Ca2+-release microdomains in cultured glia. Biochem. J. 1997, 325, 239-247.
    • (1997) Biochem. J. , vol.325 , pp. 239-247
    • Simpson, P.B.1    Russell, J.T.2
  • 71
    • 34948886835 scopus 로고    scopus 로고
    • Proteomic profiling of chronic low-frequency stimulated fast muscle
    • Donoghue, P., Doran, P., Wynne, K., Pedersen, K. et al., Proteomic profiling of chronic low-frequency stimulated fast muscle. Proteomics 2007, 7, 3417-3430.
    • (2007) Proteomics , vol.7 , pp. 3417-3430
    • Donoghue, P.1    Doran, P.2    Wynne, K.3    Pedersen, K.4
  • 72
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: gene regulation and functional significance
    • Schiaffino, S., Reggiani, C., Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 1996, 76, 371-423.
    • (1996) Physiol. Rev. , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 73
    • 77952741352 scopus 로고    scopus 로고
    • TRIM72, a novel negative feedback regulator of myogenesis, is transcriptionally activated by the synergism of MyoD (or myogenin) and MEF2
    • Jung, S. Y., Ko, Y. G., TRIM72, a novel negative feedback regulator of myogenesis, is transcriptionally activated by the synergism of MyoD (or myogenin) and MEF2. Biochem. Biophys. Res. Commun. 2010, 396, 238-245.
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 238-245
    • Jung, S.Y.1    Ko, Y.G.2
  • 74
    • 38049147787 scopus 로고    scopus 로고
    • MEF2: a central regulator of diverse developmental programs
    • Potthoff, M. J., Olson, E. N., MEF2: a central regulator of diverse developmental programs. Development 2007, 134, 4131-4140.
    • (2007) Development , vol.134 , pp. 4131-4140
    • Potthoff, M.J.1    Olson, E.N.2


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