메뉴 건너뛰기




Volumn 52, Issue 2, 2012, Pages 419-436

Intracellular Energetic Units regulate metabolism in cardiac cells

Author keywords

Cardiomyocytes; Mitochondria; Regulation; Respiration; Systems Biology; Tubulin

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BETA TUBULIN; CONNEXIN 43; CREATINE; CREATINE PHOSPHATE; DESMIN; MALONYL COENZYME A DECARBOXYLASE; MITOCHONDRIAL CREATINE KINASE; PHOSPHATE; PLECTIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 84055182290     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2011.07.015     Document Type: Review
Times cited : (50)

References (204)
  • 1
    • 0036500993 scopus 로고    scopus 로고
    • Systems biology: a brief overview
    • Kitano H. Systems biology: a brief overview. Science 2002, 295:1662-1664.
    • (2002) Science , vol.295 , pp. 1662-1664
    • Kitano, H.1
  • 2
    • 0036499997 scopus 로고    scopus 로고
    • Modeling the heart-from genes to cells to the whole organ
    • Noble D. Modeling the heart-from genes to cells to the whole organ. Science 2002, 295:1678-1682.
    • (2002) Science , vol.295 , pp. 1678-1682
    • Noble, D.1
  • 4
    • 33845585832 scopus 로고    scopus 로고
    • Systems biology approaches to metabolic and cardiovascular disorders: network perspectives of cardiovascular metabolism
    • Weiss J.N., Yang L., Qu Z. Systems biology approaches to metabolic and cardiovascular disorders: network perspectives of cardiovascular metabolism. J Lipid Res 2006, 47:2355-2366.
    • (2006) J Lipid Res , vol.47 , pp. 2355-2366
    • Weiss, J.N.1    Yang, L.2    Qu, Z.3
  • 8
    • 37349057040 scopus 로고    scopus 로고
    • Claude Bernard, the first systems biologist, and the future of physiology
    • Noble D. Claude Bernard, the first systems biologist, and the future of physiology. Exp Physiol 2008, 93:16-26.
    • (2008) Exp Physiol , vol.93 , pp. 16-26
    • Noble, D.1
  • 9
    • 37349029422 scopus 로고    scopus 로고
    • Scale relativity theory and integrative systems biology: 1. Founding principles and scale laws
    • Auffray C., Nottale L. Scale relativity theory and integrative systems biology: 1. Founding principles and scale laws. Prog Biophys Mol Biol 2008, 97:79-114.
    • (2008) Prog Biophys Mol Biol , vol.97 , pp. 79-114
    • Auffray, C.1    Nottale, L.2
  • 10
    • 63449096024 scopus 로고    scopus 로고
    • Philosophical basis and some historical aspects of systems biology: from Hegel to Noble - applications for bioenergetic research
    • Saks V., Monge C., Guzun R. Philosophical basis and some historical aspects of systems biology: from Hegel to Noble - applications for bioenergetic research. Int J Mol Sci 2009, 10:1161-1192.
    • (2009) Int J Mol Sci , vol.10 , pp. 1161-1192
    • Saks, V.1    Monge, C.2    Guzun, R.3
  • 12
    • 0001249135 scopus 로고
    • The regulation of the energy output of the heart
    • Starling E.H., Visscher M.B. The regulation of the energy output of the heart. J Physiol 1927, 62:243-261.
    • (1927) J Physiol , vol.62 , pp. 243-261
    • Starling, E.H.1    Visscher, M.B.2
  • 14
    • 0037015915 scopus 로고    scopus 로고
    • Ernest Henry Starling, his predecessors, and the "Law of the Heart"
    • Katz A.M. Ernest Henry Starling, his predecessors, and the "Law of the Heart". Circulation 2002, 106:2986-2992.
    • (2002) Circulation , vol.106 , pp. 2986-2992
    • Katz, A.M.1
  • 16
    • 47949122658 scopus 로고    scopus 로고
    • The Frank-Starling mechanism in vertebrate cardiac myocytes
    • Shiels H.A., White E. The Frank-Starling mechanism in vertebrate cardiac myocytes. J Exp Biol 2008, 211:2005-2013.
    • (2008) J Exp Biol , vol.211 , pp. 2005-2013
    • Shiels, H.A.1    White, E.2
  • 18
    • 0000072442 scopus 로고
    • About mechanism of phosphorylation, respiratory coupling
    • Belitzer V.A., Tsybakova E.T. About mechanism of phosphorylation, respiratory coupling. Biokhimiya 1939, 4:516-534.
    • (1939) Biokhimiya , vol.4 , pp. 516-534
    • Belitzer, V.A.1    Tsybakova, E.T.2
  • 21
    • 0026712942 scopus 로고
    • Ultrastructural quantitation of mitochondria and myofilaments in cardiac muscle from 10 different animal species including man
    • Barth E., Stammler G., Speiser B., Schaper J. Ultrastructural quantitation of mitochondria and myofilaments in cardiac muscle from 10 different animal species including man. J Mol Cell Cardiol 1992, 24:669-681.
    • (1992) J Mol Cell Cardiol , vol.24 , pp. 669-681
    • Barth, E.1    Stammler, G.2    Speiser, B.3    Schaper, J.4
  • 22
    • 0019471878 scopus 로고
    • Transport of energy in muscle: the phosphorylcreatine shuttle
    • Bessman S.P., Geiger P.J. Transport of energy in muscle: the phosphorylcreatine shuttle. Science 1981, 211:448-452.
    • (1981) Science , vol.211 , pp. 448-452
    • Bessman, S.P.1    Geiger, P.J.2
  • 23
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shuttle
    • Bessman S.P., Carpenter C.L. The creatine-creatine phosphate energy shuttle. Annu Rev Biochem 1985, 54:831-862.
    • (1985) Annu Rev Biochem , vol.54 , pp. 831-862
    • Bessman, S.P.1    Carpenter, C.L.2
  • 24
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis
    • Wallimann T., Wyss M., Brdiczka D., Nicolay K., Eppenberger H.M. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis. Biochem J 1992, 281:21-40.
    • (1992) Biochem J , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 25
    • 84889285565 scopus 로고    scopus 로고
    • The phosphocreatine circuit: molecular and cellular physiology of creatine kinases, sensitivity to free radicals, and enhancement by creatine supplementation
    • Wiley-VCH, GmbH, Weinheim, Germany, V. Saks (Ed.)
    • Wallimann T., Tokarska-Schlattner M., Neumann D., Epand R.F., Andres R.H., Widmer H.R., et al. The phosphocreatine circuit: molecular and cellular physiology of creatine kinases, sensitivity to free radicals, and enhancement by creatine supplementation. Molecular system bioenergetics energy for life 2007, 195-264. Wiley-VCH, GmbH, Weinheim, Germany. V. Saks (Ed.).
    • (2007) Molecular system bioenergetics energy for life , pp. 195-264
    • Wallimann, T.1    Tokarska-Schlattner, M.2    Neumann, D.3    Epand, R.F.4    Andres, R.H.5    Widmer, H.R.6
  • 26
    • 44649192887 scopus 로고    scopus 로고
    • The creatine kinase phosphotransfer network: thermodynamic and kinetic considerations, the impact of the mitochondrial outer membrane and modelling approaches
    • Springer, Dordrecht, M. Wyss, G. Salomons (Eds.)
    • Saks V., Anmann T., Guzun R., Kaambre T., Sikk P., Schlattner U., et al. The creatine kinase phosphotransfer network: thermodynamic and kinetic considerations, the impact of the mitochondrial outer membrane and modelling approaches. Creatine and Creatine Kinase in Health and Disease 2007, 27-66. Springer, Dordrecht. M. Wyss, G. Salomons (Eds.).
    • (2007) Creatine and Creatine Kinase in Health and Disease , pp. 27-66
    • Saks, V.1    Anmann, T.2    Guzun, R.3    Kaambre, T.4    Sikk, P.5    Schlattner, U.6
  • 27
    • 44649108365 scopus 로고    scopus 로고
    • Metabolic compartmentation - a system level property of muscle cells: real problems of diffusion in living cells
    • Saks V., Beraud N., Wallimann T. Metabolic compartmentation - a system level property of muscle cells: real problems of diffusion in living cells. Int J Mol Sci 2008, 9:751-767.
    • (2008) Int J Mol Sci , vol.9 , pp. 751-767
    • Saks, V.1    Beraud, N.2    Wallimann, T.3
  • 29
    • 77953811727 scopus 로고    scopus 로고
    • Structure-function relationships in feedback regulation of energy fluxes in vivo in health and disease: mitochondrial interactosome
    • Saks V., Guzun R., Timohhina N., Tepp K., Varikmaa M., Monge C., et al. Structure-function relationships in feedback regulation of energy fluxes in vivo in health and disease: mitochondrial interactosome. Biochim Biophys Acta 2010, 1797:678-697.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 678-697
    • Saks, V.1    Guzun, R.2    Timohhina, N.3    Tepp, K.4    Varikmaa, M.5    Monge, C.6
  • 30
    • 84889354603 scopus 로고    scopus 로고
    • Integrated and organized cellular energetic systems: theories of cell energetics, compartmentation and metabolic channeling
    • Wiley-VCH, GmbH, Weinheim, Germany, V. Saks (Ed.)
    • Saks V., Monge C., Anmann T., Dzeja P. Integrated and organized cellular energetic systems: theories of cell energetics, compartmentation and metabolic channeling. Molecular system bioenergetics energy for life 2007, 59-110. Wiley-VCH, GmbH, Weinheim, Germany. V. Saks (Ed.).
    • (2007) Molecular system bioenergetics energy for life , pp. 59-110
    • Saks, V.1    Monge, C.2    Anmann, T.3    Dzeja, P.4
  • 31
    • 77950897710 scopus 로고    scopus 로고
    • Application of the principles of systems biology and Wiener's cybernetics for analysis of regulation of energy fluxes in muscle cells in vivo
    • Guzun R., Saks V. Application of the principles of systems biology and Wiener's cybernetics for analysis of regulation of energy fluxes in muscle cells in vivo. Int J Mol Sci 2010, 11:982-1019.
    • (2010) Int J Mol Sci , vol.11 , pp. 982-1019
    • Guzun, R.1    Saks, V.2
  • 32
    • 67649588894 scopus 로고    scopus 로고
    • Regulation of respiration controlled by mitochondrial creatine kinase in permeabilized cardiac cells in situ. Importance of system level properties
    • Guzun R., Timohhina N., Tepp K., Monge C., Kaambre T., Sikk P., et al. Regulation of respiration controlled by mitochondrial creatine kinase in permeabilized cardiac cells in situ. Importance of system level properties. Biochim Biophys Acta 2009, 1787:1089-1105.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1089-1105
    • Guzun, R.1    Timohhina, N.2    Tepp, K.3    Monge, C.4    Kaambre, T.5    Sikk, P.6
  • 33
    • 80052791662 scopus 로고    scopus 로고
    • Systems bioenergetics of creatine kinase networks: physiological roles of creatine and phosphocreatine in regulation of cardiac cell function
    • Guzun R., Timohhina N., Tepp K., Gonzalez-Granillo M., Shevchuk I., Chekulayev V., et al. Systems bioenergetics of creatine kinase networks: physiological roles of creatine and phosphocreatine in regulation of cardiac cell function. Amino Acids 2011, 40:1333-1348.
    • (2011) Amino Acids , vol.40 , pp. 1333-1348
    • Guzun, R.1    Timohhina, N.2    Tepp, K.3    Gonzalez-Granillo, M.4    Shevchuk, I.5    Chekulayev, V.6
  • 36
    • 79957937929 scopus 로고    scopus 로고
    • Targeting fatty acid and carbohydrate oxidation-a novel therapeutic intervention in the ischemic and failing heart
    • Jaswal J.S., Keung W., Wang W., Ussher J.R., Lopaschuk G.D. Targeting fatty acid and carbohydrate oxidation-a novel therapeutic intervention in the ischemic and failing heart. Biochim Biophys Acta 2011, 1813:1333-1350.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1333-1350
    • Jaswal, J.S.1    Keung, W.2    Wang, W.3    Ussher, J.R.4    Lopaschuk, G.D.5
  • 37
    • 1842389677 scopus 로고
    • Relationship between carbohydrate and lipid metabolism and the energy balance of heart muscle
    • Neely J., Morgan H. Relationship between carbohydrate and lipid metabolism and the energy balance of heart muscle. Annu Rev Physiol 1974, 36:413-459.
    • (1974) Annu Rev Physiol , vol.36 , pp. 413-459
    • Neely, J.1    Morgan, H.2
  • 38
    • 0000668980 scopus 로고
    • Cardiac metabolism
    • Bing R.J. Cardiac metabolism. Physiol Rev 1965, 45:171-213.
    • (1965) Physiol Rev , vol.45 , pp. 171-213
    • Bing, R.J.1
  • 39
    • 50449119332 scopus 로고
    • Metabolism of the human heart. II. Studies on fat, ketone and amino acid metabolism
    • Bing R.J., Siegel A., Ungar I., Gilbert M. Metabolism of the human heart. II. Studies on fat, ketone and amino acid metabolism. Am J Med 1954, 16:504-515.
    • (1954) Am J Med , vol.16 , pp. 504-515
    • Bing, R.J.1    Siegel, A.2    Ungar, I.3    Gilbert, M.4
  • 40
    • 0032452225 scopus 로고    scopus 로고
    • Regulatory interactions between lipids and carbohydrates: the glucose fatty acid cycle after 35years
    • Randle P.J. Regulatory interactions between lipids and carbohydrates: the glucose fatty acid cycle after 35years. Diabetes Metab Rev 1998, 14:263-283.
    • (1998) Diabetes Metab Rev , vol.14 , pp. 263-283
    • Randle, P.J.1
  • 41
    • 50549202600 scopus 로고
    • The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus
    • Randle P.J., Garland P.B., Hales C.N., Newsholme E.A. The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus. Lancet 1963, 1:785-789.
    • (1963) Lancet , vol.1 , pp. 785-789
    • Randle, P.J.1    Garland, P.B.2    Hales, C.N.3    Newsholme, E.A.4
  • 42
    • 34547095116 scopus 로고
    • Regulation of glucose uptake by muscle. 6. Fructose 1,6-diphosphatase activity of rat heart and rat diaphragm
    • Newsholme E.A., Randle P.J. Regulation of glucose uptake by muscle. 6. Fructose 1,6-diphosphatase activity of rat heart and rat diaphragm. Biochem J 1962, 83:387-392.
    • (1962) Biochem J , vol.83 , pp. 387-392
    • Newsholme, E.A.1    Randle, P.J.2
  • 44
    • 69049098306 scopus 로고    scopus 로고
    • The Randle cycle revisited: a new head for an old hat
    • Hue L., Taegtmeyer H. The Randle cycle revisited: a new head for an old hat. Am J Physiol Endocrinol Metab 2009, 297:E578-E591.
    • (2009) Am J Physiol Endocrinol Metab , vol.297
    • Hue, L.1    Taegtmeyer, H.2
  • 45
    • 34147093330 scopus 로고    scopus 로고
    • In appreciation of Sir Philip Randle: the glucose-fatty acid cycle
    • Sugden M.C. In appreciation of Sir Philip Randle: the glucose-fatty acid cycle. Br J Nutr 2007, 97:809-813.
    • (2007) Br J Nutr , vol.97 , pp. 809-813
    • Sugden, M.C.1
  • 46
    • 0018336297 scopus 로고
    • Mitochondrial function in the heart
    • Williamson J.R. Mitochondrial function in the heart. Annu Rev Physiol 1979, 41:485-506.
    • (1979) Annu Rev Physiol , vol.41 , pp. 485-506
    • Williamson, J.R.1
  • 47
    • 0017071201 scopus 로고
    • Coordination of citric acid cycle activity with electron transport flux
    • Williamson J.R., Ford C., Illingworth J., Safer B. Coordination of citric acid cycle activity with electron transport flux. Circ Res 1976, 38(Suppl. 1):I39-I51.
    • (1976) Circ Res , vol.38 , Issue.SUPPL. 1
    • Williamson, J.R.1    Ford, C.2    Illingworth, J.3    Safer, B.4
  • 48
    • 0015349584 scopus 로고
    • The effects of increased heart work on the tricarboxylate cycle and its interactions with glycolysis in the perfused rat heart
    • Neely J.R., Denton R.M., England P.J., Randle P.J. The effects of increased heart work on the tricarboxylate cycle and its interactions with glycolysis in the perfused rat heart. Biochem J 1972, 128:147-159.
    • (1972) Biochem J , vol.128 , pp. 147-159
    • Neely, J.R.1    Denton, R.M.2    England, P.J.3    Randle, P.J.4
  • 49
    • 0021741946 scopus 로고
    • Role of glycolytic products in damage to ischemic myocardium. Dissociation of adenosine triphosphate levels and recovery of function of reperfused ischemic hearts
    • Neely J.R., Grotyohann L.W. Role of glycolytic products in damage to ischemic myocardium. Dissociation of adenosine triphosphate levels and recovery of function of reperfused ischemic hearts. Circ Res 1984, 55:816-824.
    • (1984) Circ Res , vol.55 , pp. 816-824
    • Neely, J.R.1    Grotyohann, L.W.2
  • 50
    • 0015424759 scopus 로고
    • Myocardial utilization of carbohydrate and lipids
    • Neely J.R., Rovetto M.J., Oram J.F. Myocardial utilization of carbohydrate and lipids. Prog Cardiovasc Dis 1972, 15:289-329.
    • (1972) Prog Cardiovasc Dis , vol.15 , pp. 289-329
    • Neely, J.R.1    Rovetto, M.J.2    Oram, J.F.3
  • 51
    • 0015818068 scopus 로고
    • Effects of ischemia on function and metabolism of the isolated working rat heart
    • Neely J.R., Rovetto M.J., Whitmer J.T., Morgan H.E. Effects of ischemia on function and metabolism of the isolated working rat heart. Am J Physiol 1973, 225:651-658.
    • (1973) Am J Physiol , vol.225 , pp. 651-658
    • Neely, J.R.1    Rovetto, M.J.2    Whitmer, J.T.3    Morgan, H.E.4
  • 52
    • 0018371606 scopus 로고
    • Control of maximum rates of glycolysis in rat cardiac muscle
    • Kobayashi K., Neely J.R. Control of maximum rates of glycolysis in rat cardiac muscle. Circ Res 1979, 44:166-175.
    • (1979) Circ Res , vol.44 , pp. 166-175
    • Kobayashi, K.1    Neely, J.R.2
  • 53
    • 0021223549 scopus 로고
    • Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane
    • Sumegi B., Srere P.A. Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane. J Biol Chem 1984, 259:8748-8752.
    • (1984) J Biol Chem , vol.259 , pp. 8748-8752
    • Sumegi, B.1    Srere, P.A.2
  • 54
    • 0034141634 scopus 로고    scopus 로고
    • Preliminary evidence for the existence of specific functional assemblies between enzymes of the beta-oxidation pathway and the respiratory chain
    • Parker A., Engel P.C. Preliminary evidence for the existence of specific functional assemblies between enzymes of the beta-oxidation pathway and the respiratory chain. Biochem J 2000, 345:429-435.
    • (2000) Biochem J , vol.345 , pp. 429-435
    • Parker, A.1    Engel, P.C.2
  • 55
    • 77956902886 scopus 로고    scopus 로고
    • Evidence for physical association of mitochondrial fatty acid oxidation and oxidative phosphorylation complexes
    • Wang Y., Mohsen A.W., Mihalik S.J., Goetzman E.S., Vockley J. Evidence for physical association of mitochondrial fatty acid oxidation and oxidative phosphorylation complexes. J Biol Chem 2010, 285:29834-29841.
    • (2010) J Biol Chem , vol.285 , pp. 29834-29841
    • Wang, Y.1    Mohsen, A.W.2    Mihalik, S.J.3    Goetzman, E.S.4    Vockley, J.5
  • 56
    • 33845335159 scopus 로고    scopus 로고
    • Molecular system bioenergetics: regulation of substrate supply in response to heart energy demands
    • Saks V., Favier R., Guzun R., Schlattner U., Wallimann T. Molecular system bioenergetics: regulation of substrate supply in response to heart energy demands. J Physiol 2006, 577:769-777.
    • (2006) J Physiol , vol.577 , pp. 769-777
    • Saks, V.1    Favier, R.2    Guzun, R.3    Schlattner, U.4    Wallimann, T.5
  • 57
    • 80054978144 scopus 로고    scopus 로고
    • Mitochondrial approaches to protect against cardiac ischemia and reperfusion injury
    • Camara A.K., Bienengraeber M., Stowe D.F. Mitochondrial approaches to protect against cardiac ischemia and reperfusion injury. Front Physiol 2011, 2:13.
    • (2011) Front Physiol , vol.2 , pp. 13
    • Camara, A.K.1    Bienengraeber, M.2    Stowe, D.F.3
  • 58
    • 79551494641 scopus 로고    scopus 로고
    • Metabolic modulation in heart failure: high time for a definitive clinical trial
    • Ashrafian H., Neubauer S. Metabolic modulation in heart failure: high time for a definitive clinical trial. Heart (British Cardiac Society) 2011, 97:267-268.
    • (2011) Heart (British Cardiac Society) , vol.97 , pp. 267-268
    • Ashrafian, H.1    Neubauer, S.2
  • 59
    • 0000379911 scopus 로고
    • Oxidative phosphorylations; role of inorganic phosphate and acceptor systems in control of metabolic rates
    • Lardy H.A., Wellman H. Oxidative phosphorylations; role of inorganic phosphate and acceptor systems in control of metabolic rates. J Biol Chem 1952, 195:215-224.
    • (1952) J Biol Chem , vol.195 , pp. 215-224
    • Lardy, H.A.1    Wellman, H.2
  • 60
    • 0001433788 scopus 로고
    • A method for the localization of sites for oxidative phosphorylation
    • Chance B., Williams G.R. A method for the localization of sites for oxidative phosphorylation. Nature 1955, 176:250-254.
    • (1955) Nature , vol.176 , pp. 250-254
    • Chance, B.1    Williams, G.R.2
  • 61
    • 0031680036 scopus 로고    scopus 로고
    • Role of mitochondrial calcium transport in the control of substrate oxidation
    • Hansford R.G., Zorov D. Role of mitochondrial calcium transport in the control of substrate oxidation. Mol Cell Biochem 1998, 184:359-369.
    • (1998) Mol Cell Biochem , vol.184 , pp. 359-369
    • Hansford, R.G.1    Zorov, D.2
  • 62
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • McCormack J.G., Halestrap A.P., Denton R.M. Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol Rev 1990, 70:391-425.
    • (1990) Physiol Rev , vol.70 , pp. 391-425
    • McCormack, J.G.1    Halestrap, A.P.2    Denton, R.M.3
  • 63
    • 0022505605 scopus 로고
    • Relation between work and phosphate metabolite in the in vivo paced mammalian heart
    • Balaban R.S., Kantor H.L., Katz L.A., Briggs R.W. Relation between work and phosphate metabolite in the in vivo paced mammalian heart. Science 1986, 232:1121-1123.
    • (1986) Science , vol.232 , pp. 1121-1123
    • Balaban, R.S.1    Kantor, H.L.2    Katz, L.A.3    Briggs, R.W.4
  • 65
    • 0027254547 scopus 로고
    • Effect of cardiac work on electrical potential gradient across mitochondrial membrane in perfused hearts
    • Wan B., Dounen C., Duszynsky J., Salama G., Vary TC K.F.L. Effect of cardiac work on electrical potential gradient across mitochondrial membrane in perfused hearts. Am J Physiol Cell Physiol 1993, 265:H453-H460.
    • (1993) Am J Physiol Cell Physiol , vol.265
    • Wan, B.1    Dounen, C.2    Duszynsky, J.3    Salama, G.4    Vary, T.C.K.F.L.5
  • 66
    • 0016835347 scopus 로고
    • Respiratory control in isolated perfused rat heart. Role of the equilibrium relations between the mitochondrial electron carriers and the adenylate system
    • Hassinen I.E., Hiltunen K. Respiratory control in isolated perfused rat heart. Role of the equilibrium relations between the mitochondrial electron carriers and the adenylate system. Biochim Biophys Acta 1975, 408:319-330.
    • (1975) Biochim Biophys Acta , vol.408 , pp. 319-330
    • Hassinen, I.E.1    Hiltunen, K.2
  • 67
    • 33846907051 scopus 로고    scopus 로고
    • A biophysical model of the mitochondrial respiratory system and oxidative phosphorylation
    • Beard D.A. A biophysical model of the mitochondrial respiratory system and oxidative phosphorylation. PLoS Comput Biol 2005, 1:e36.
    • (2005) PLoS Comput Biol , vol.1
    • Beard, D.A.1
  • 68
    • 33749339635 scopus 로고    scopus 로고
    • Modeling of oxygen transport and cellular energetics explains observations on in vivo cardiac energy metabolism
    • Beard D.A. Modeling of oxygen transport and cellular energetics explains observations on in vivo cardiac energy metabolism. PLoS Comput Biol 2006, 2:e107.
    • (2006) PLoS Comput Biol , vol.2
    • Beard, D.A.1
  • 70
    • 64949168663 scopus 로고    scopus 로고
    • Roles of the creatine kinase system and myoglobin in maintaining energetic state in the working heart
    • Wu F., Beard D.A. Roles of the creatine kinase system and myoglobin in maintaining energetic state in the working heart. BMC Syst Biol 2009, 3:22.
    • (2009) BMC Syst Biol , vol.3 , pp. 22
    • Wu, F.1    Beard, D.A.2
  • 71
    • 78650054962 scopus 로고    scopus 로고
    • 31 P saturation transfer spectroscopy predicts differential intracellular association of ATP and ADP in skeletal muscle
    • 31 P saturation transfer spectroscopy predicts differential intracellular association of ATP and ADP in skeletal muscle. J Biol Chem 2010, 285:39588-39596.
    • (2010) J Biol Chem , vol.285 , pp. 39588-39596
    • Nabuurs, C.1    Huijbregts, B.2    Wieringa, B.3    Hibers, C.W.4    Heerschap, A.5
  • 72
    • 0036089588 scopus 로고    scopus 로고
    • Load dependence of ventricular performance explained by model of calcium-myofilament interactions
    • Shimizu J., Todaka K., Burkhoff D. Load dependence of ventricular performance explained by model of calcium-myofilament interactions. Am J Physiol Heart Circ Physiol 2002, 282:H1081-H1091.
    • (2002) Am J Physiol Heart Circ Physiol , vol.282
    • Shimizu, J.1    Todaka, K.2    Burkhoff, D.3
  • 73
    • 0036773295 scopus 로고    scopus 로고
    • Cardiac energy metabolism homeostasis: role of cytosolic calcium
    • Balaban R.S. Cardiac energy metabolism homeostasis: role of cytosolic calcium. J Mol Cell Cardiol 2002, 34:1259-1271.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 1259-1271
    • Balaban, R.S.1
  • 74
    • 77649175105 scopus 로고    scopus 로고
    • Matching ATP supply and demand in mammalian heart: in vivo, in vitro, and in silico perspectives
    • Yaniv Y., Juhaszova M., Nuss H.B., Wang S., Zorov D.B., Lakatta E.G., et al. Matching ATP supply and demand in mammalian heart: in vivo, in vitro, and in silico perspectives. Ann N Y Acad Sci 2010, 1188:133-142.
    • (2010) Ann N Y Acad Sci , vol.1188 , pp. 133-142
    • Yaniv, Y.1    Juhaszova, M.2    Nuss, H.B.3    Wang, S.4    Zorov, D.B.5    Lakatta, E.G.6
  • 75
    • 68649120751 scopus 로고    scopus 로고
    • Mitochondrial calcium as a key regulator of mitochondrial ATP production in mammalian cells
    • Griffiths E.J., Rutter G.A. Mitochondrial calcium as a key regulator of mitochondrial ATP production in mammalian cells. Biochim Biophys Acta 2009, 1787:1324-1333.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1324-1333
    • Griffiths, E.J.1    Rutter, G.A.2
  • 76
    • 67650688732 scopus 로고    scopus 로고
    • Regulation of mitochondrial Ca(2+) and its effects on energetics and redox balance in normal and failing heart
    • Liu T., O'Rourke B. Regulation of mitochondrial Ca(2+) and its effects on energetics and redox balance in normal and failing heart. J Bioenerg Biomembr 2009, 41:127-132.
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 127-132
    • Liu, T.1    O'Rourke, B.2
  • 78
    • 33748096830 scopus 로고    scopus 로고
    • Open-system non-equilibrium steady state: statistical thermodynamics, fluctuations, and chemical oscillations
    • Qian H. Open-system non-equilibrium steady state: statistical thermodynamics, fluctuations, and chemical oscillations. J Phys Chem 2006, 110:15063-15074.
    • (2006) J Phys Chem , vol.110 , pp. 15063-15074
    • Qian, H.1
  • 80
    • 77958505514 scopus 로고    scopus 로고
    • Quantitative analysis of cellular metabolic dissipative, self-organized structures
    • de la Fuente I.M. Quantitative analysis of cellular metabolic dissipative, self-organized structures. Int J Mol Sci 2010, 11:3540-3599.
    • (2010) Int J Mol Sci , vol.11 , pp. 3540-3599
    • de la Fuente, I.M.1
  • 81
    • 77958505514 scopus 로고    scopus 로고
    • Quantitative analysis of cellular metabolic dissipative, self-organized structures
    • de la Fuente I.M. Quantitative analysis of cellular metabolic dissipative, self-organized structures. Int J Mol Sci 2011, 11:3540-3599.
    • (2011) Int J Mol Sci , vol.11 , pp. 3540-3599
    • de la Fuente, I.M.1
  • 86
    • 0035795177 scopus 로고    scopus 로고
    • Functional complexes of mitochondria with Ca, MgATPases of myofibrils and sarcoplasmic reticulum in muscle cells
    • Seppet E.K., Kaambre T., Sikk P., Tiivel T., Vija H., Tonkonogi M., et al. Functional complexes of mitochondria with Ca, MgATPases of myofibrils and sarcoplasmic reticulum in muscle cells. Biochim Biophys Acta 2001, 1504:379-395.
    • (2001) Biochim Biophys Acta , vol.1504 , pp. 379-395
    • Seppet, E.K.1    Kaambre, T.2    Sikk, P.3    Tiivel, T.4    Vija, H.5    Tonkonogi, M.6
  • 89
    • 77953022226 scopus 로고    scopus 로고
    • Spark-induced sparks as a mechanism of intracellular calcium alternans in cardiac myocytes
    • Rovetti R., Cui X., Garfinkel A., Weiss J.N., Qu Z. Spark-induced sparks as a mechanism of intracellular calcium alternans in cardiac myocytes. Circ Res 2010, 106:1582-1591.
    • (2010) Circ Res , vol.106 , pp. 1582-1591
    • Rovetti, R.1    Cui, X.2    Garfinkel, A.3    Weiss, J.N.4    Qu, Z.5
  • 90
    • 0002228335 scopus 로고
    • Ultrastructure of cardiac muscle
    • Raven, New York, H. Fozzard, E. Haber, R. Jennings, A. Katz, H. Morgan (Eds.)
    • Sommer J., Jennings R. Ultrastructure of cardiac muscle. The heart and cardiovascular system 1986, 61-100. Raven, New York. H. Fozzard, E. Haber, R. Jennings, A. Katz, H. Morgan (Eds.).
    • (1986) The heart and cardiovascular system , pp. 61-100
    • Sommer, J.1    Jennings, R.2
  • 91
    • 0014544519 scopus 로고
    • The ultrastructure of the cat myocardium. I. Ventricular papillary muscle
    • Fawcett D.W., McNutt N.S. The ultrastructure of the cat myocardium. I. Ventricular papillary muscle. J Cell Biol 1969, 42:1-45.
    • (1969) J Cell Biol , vol.42 , pp. 1-45
    • Fawcett, D.W.1    McNutt, N.S.2
  • 94
    • 67650691143 scopus 로고    scopus 로고
    • Mitochondrial dynamics in heart cells: very low amplitude high frequency fluctuations in adult cardiomyocytes and flow motion in non beating Hl-1 cells
    • Beraud N., Pelloux S., Usson Y., Kuznetsov A.V., Ronot X., Tourneur Y., et al. Mitochondrial dynamics in heart cells: very low amplitude high frequency fluctuations in adult cardiomyocytes and flow motion in non beating Hl-1 cells. J Bioenerg Biomembr 2009, 41:195-214.
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 195-214
    • Beraud, N.1    Pelloux, S.2    Usson, Y.3    Kuznetsov, A.V.4    Ronot, X.5    Tourneur, Y.6
  • 95
    • 0037007227 scopus 로고    scopus 로고
    • Mitochondria are morphologically and functionally heterogeneous within cells
    • Collins T.J., Berridge M.J., Lipp P., Bootman M.D. Mitochondria are morphologically and functionally heterogeneous within cells. EMBO J 2002, 21:1616-1627.
    • (2002) EMBO J , vol.21 , pp. 1616-1627
    • Collins, T.J.1    Berridge, M.J.2    Lipp, P.3    Bootman, M.D.4
  • 96
    • 0038609470 scopus 로고    scopus 로고
    • Mitochondria are morphologically heterogeneous within cells
    • Collins T.J., Bootman M.D. Mitochondria are morphologically heterogeneous within cells. J Exp Biol 2003, 206:1993-2000.
    • (2003) J Exp Biol , vol.206 , pp. 1993-2000
    • Collins, T.J.1    Bootman, M.D.2
  • 98
    • 77951949766 scopus 로고    scopus 로고
    • Complex patterns of mitochondrial dynamics in human pancreatic cells revealed by fluorescent confocal imaging
    • Kuznetsov A.V., Hermann M., Troppmair J., Margreiter R., Hengster P. Complex patterns of mitochondrial dynamics in human pancreatic cells revealed by fluorescent confocal imaging. J Cell Mol Med 2010, 14:417-425.
    • (2010) J Cell Mol Med , vol.14 , pp. 417-425
    • Kuznetsov, A.V.1    Hermann, M.2    Troppmair, J.3    Margreiter, R.4    Hengster, P.5
  • 99
    • 0034596947 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS)-induced ROS release: a new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes
    • Zorov D.B., Filburn C.R., Klotz L.O., Zweier J.L., Sollott S.J. Reactive oxygen species (ROS)-induced ROS release: a new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes. J Exp Med 2000, 192:1001-1014.
    • (2000) J Exp Med , vol.192 , pp. 1001-1014
    • Zorov, D.B.1    Filburn, C.R.2    Klotz, L.O.3    Zweier, J.L.4    Sollott, S.J.5
  • 100
    • 67149094710 scopus 로고    scopus 로고
    • Heterogeneity of mitochondria and mitochondrial function within cells as another level of mitochondrial complexity
    • Kuznetsov A.V., Margreiter R. Heterogeneity of mitochondria and mitochondrial function within cells as another level of mitochondrial complexity. Int J Mol Sci 2009, 10:1911-1929.
    • (2009) Int J Mol Sci , vol.10 , pp. 1911-1929
    • Kuznetsov, A.V.1    Margreiter, R.2
  • 101
    • 4444240180 scopus 로고    scopus 로고
    • A mitochondrial oscillator dependent on reactive oxygen species
    • Cortassa S., Aon M.A., Winslow R.L., O'Rourke B. A mitochondrial oscillator dependent on reactive oxygen species. Biophys J 2004, 87:2060-2073.
    • (2004) Biophys J , vol.87 , pp. 2060-2073
    • Cortassa, S.1    Aon, M.A.2    Winslow, R.L.3    O'Rourke, B.4
  • 102
    • 0037376919 scopus 로고    scopus 로고
    • Live cell imaging using confocal microscopy induces intracellular calcium transients and cell death
    • Knight M.M., Roberts S.R., Lee D.A., Bader D.L. Live cell imaging using confocal microscopy induces intracellular calcium transients and cell death. Am J Physiol Cell Physiol 2003, 284:C1083-C1089.
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Knight, M.M.1    Roberts, S.R.2    Lee, D.A.3    Bader, D.L.4
  • 103
    • 47549096022 scopus 로고    scopus 로고
    • Superoxide flashes in single mitochondria
    • Wang W., Fang H., Groom L., Cheng A., Zhang W., Liu J., et al. Superoxide flashes in single mitochondria. Cell 2008, 134:279-290.
    • (2008) Cell , vol.134 , pp. 279-290
    • Wang, W.1    Fang, H.2    Groom, L.3    Cheng, A.4    Zhang, W.5    Liu, J.6
  • 104
    • 33745616352 scopus 로고    scopus 로고
    • Mitochondrial subpopulations and heterogeneity revealed by confocal imaging: possible physiological role?
    • Kuznetsov A.V., Troppmair J., Sucher R., Hermann M., Saks V., Margreiter R. Mitochondrial subpopulations and heterogeneity revealed by confocal imaging: possible physiological role?. Biochim Biophys Acta 2006, 1757:686-691.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 686-691
    • Kuznetsov, A.V.1    Troppmair, J.2    Sucher, R.3    Hermann, M.4    Saks, V.5    Margreiter, R.6
  • 105
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: dynamic organelles in disease, aging, and development
    • Chan D.C. Mitochondria: dynamic organelles in disease, aging, and development. Cell 2006, 125:1241-1252.
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 106
    • 27744491193 scopus 로고    scopus 로고
    • Emerging functions of mammalian mitochondrial fusion and fission
    • Spec No. 2
    • Chen H., Chan D.C. Emerging functions of mammalian mitochondrial fusion and fission. Hum Mol Genet 2005, 14:R283-R289. Spec No. 2.
    • (2005) Hum Mol Genet , vol.14
    • Chen, H.1    Chan, D.C.2
  • 107
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • Chen H., Chomyn A., Chan D.C. Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem 2005, 280:26185-26192.
    • (2005) J Biol Chem , vol.280 , pp. 26185-26192
    • Chen, H.1    Chomyn, A.2    Chan, D.C.3
  • 108
    • 0035487808 scopus 로고    scopus 로고
    • The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis
    • Frank S., Gaume B., Bergmann-Leitner E.S., Leitner W.W., Robert E.G., Catez F., et al. The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis. Dev Cell 2001, 1:515-525.
    • (2001) Dev Cell , vol.1 , pp. 515-525
    • Frank, S.1    Gaume, B.2    Bergmann-Leitner, E.S.3    Leitner, W.W.4    Robert, E.G.5    Catez, F.6
  • 110
    • 78149407069 scopus 로고    scopus 로고
    • Mitochondrial fission and fusion and their roles in the heart
    • Kane L.A., Youle R.J. Mitochondrial fission and fusion and their roles in the heart. J Mol Med (Berlin, Germany) 2010, 88:971-979.
    • (2010) J Mol Med (Berlin, Germany) , vol.88 , pp. 971-979
    • Kane, L.A.1    Youle, R.J.2
  • 111
    • 77649337197 scopus 로고    scopus 로고
    • Distinctions and similarities of cell bioenergetics and the role of mitochondria in hypoxia, cancer, and embryonic development
    • Jezek P., Plecita-Hlavata L., Smolkova K., Rossignol R. Distinctions and similarities of cell bioenergetics and the role of mitochondria in hypoxia, cancer, and embryonic development. Int J Biochem Cell Biol 2010, 42:604-622.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 604-622
    • Jezek, P.1    Plecita-Hlavata, L.2    Smolkova, K.3    Rossignol, R.4
  • 113
    • 0043166392 scopus 로고    scopus 로고
    • Dynamics of mitochondrial morphology in healthy cells and during apoptosis
    • Karbowski M., Youle R.J. Dynamics of mitochondrial morphology in healthy cells and during apoptosis. Cell Death Differ 2003, 10:870-880.
    • (2003) Cell Death Differ , vol.10 , pp. 870-880
    • Karbowski, M.1    Youle, R.J.2
  • 114
    • 0014458555 scopus 로고
    • Formation of gigantic mitochondria in hypoxic isolated perfused rat hearts
    • Sun C.N., Dhalla N.S., Olson R.E. Formation of gigantic mitochondria in hypoxic isolated perfused rat hearts. Experientia 1969, 25:763-764.
    • (1969) Experientia , vol.25 , pp. 763-764
    • Sun, C.N.1    Dhalla, N.S.2    Olson, R.E.3
  • 115
    • 34548170490 scopus 로고    scopus 로고
    • Mitofusin-2 is a major determinant of oxidative stress-mediated heart muscle cell apoptosis
    • Shen T., Zheng M., Cao C., Chen C., Tang J., Zhang W., et al. Mitofusin-2 is a major determinant of oxidative stress-mediated heart muscle cell apoptosis. J Biol Chem 2007, 282:23354-23361.
    • (2007) J Biol Chem , vol.282 , pp. 23354-23361
    • Shen, T.1    Zheng, M.2    Cao, C.3    Chen, C.4    Tang, J.5    Zhang, W.6
  • 116
    • 34249697100 scopus 로고    scopus 로고
    • Muscle intermediate filaments and their links to membranes and membranous organelles
    • Capetanaki Y., Bloch R.J., Kouloumenta A., Mavroidis M., Psarras S. Muscle intermediate filaments and their links to membranes and membranous organelles. Exp Cell Res 2007, 313:2063-2076.
    • (2007) Exp Cell Res , vol.313 , pp. 2063-2076
    • Capetanaki, Y.1    Bloch, R.J.2    Kouloumenta, A.3    Mavroidis, M.4    Psarras, S.5
  • 117
    • 0039064824 scopus 로고
    • Mitochondria are associated with microtubules and not with intermediate filaments in cultured fibroblasts
    • Ball E.H., Singer S.J. Mitochondria are associated with microtubules and not with intermediate filaments in cultured fibroblasts. Proc Natl Acad Sci USA 1982, 79:123-126.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 123-126
    • Ball, E.H.1    Singer, S.J.2
  • 118
    • 0020469904 scopus 로고
    • Putative association of mitochondria with a subpopulation of intermediate-sized filaments in cultured human skin fibroblasts
    • Mose-Larsen P., Bravo R., Fey S.J., Small J.V., Celis J.E. Putative association of mitochondria with a subpopulation of intermediate-sized filaments in cultured human skin fibroblasts. Cell 1982, 31:681-692.
    • (1982) Cell , vol.31 , pp. 681-692
    • Mose-Larsen, P.1    Bravo, R.2    Fey, S.J.3    Small, J.V.4    Celis, J.E.5
  • 119
    • 0020326774 scopus 로고
    • Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method
    • Hirokawa N. Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method. J Cell Biol 1982, 94:129-142.
    • (1982) J Cell Biol , vol.94 , pp. 129-142
    • Hirokawa, N.1
  • 120
    • 0008688565 scopus 로고
    • Association of mitochondria with microtubules in cultured cells
    • Heggeness M.H., Simon M., Singer S.J. Association of mitochondria with microtubules in cultured cells. Proc Natl Acad Sci USA 1978, 75:3863-3866.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3863-3866
    • Heggeness, M.H.1    Simon, M.2    Singer, S.J.3
  • 121
    • 0031661650 scopus 로고    scopus 로고
    • Cytoskeleton and mitochondrial morphology and function
    • Rappaport L., Oliviero P., Samuel J.L. Cytoskeleton and mitochondrial morphology and function. Mol Cell Biochem 1998, 184:101-105.
    • (1998) Mol Cell Biochem , vol.184 , pp. 101-105
    • Rappaport, L.1    Oliviero, P.2    Samuel, J.L.3
  • 122
    • 33745601933 scopus 로고    scopus 로고
    • The relationship between mitochondrial shape and function and the cytoskeleton
    • Anesti V., Scorrano L. The relationship between mitochondrial shape and function and the cytoskeleton. Biochim Biophys Acta 2006, 1757:692-699.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 692-699
    • Anesti, V.1    Scorrano, L.2
  • 123
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon A.M., Homsher E., Regnier M. Regulation of contraction in striated muscle. Physiol Rev 2000, 80:853-924.
    • (2000) Physiol Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 124
    • 77955292999 scopus 로고    scopus 로고
    • Mass spectrometry analysis of C-terminal posttranslational modifications of tubulins
    • Redeker V. Mass spectrometry analysis of C-terminal posttranslational modifications of tubulins. Methods Cell Biol 2010, 95:77-103.
    • (2010) Methods Cell Biol , vol.95 , pp. 77-103
    • Redeker, V.1
  • 125
    • 0030709242 scopus 로고    scopus 로고
    • Multiple forms of tubulin: different gene products and covalent modifications
    • Luduena R.F. Multiple forms of tubulin: different gene products and covalent modifications. Int Rev Cytol 1998, 178:207-275.
    • (1998) Int Rev Cytol , vol.178 , pp. 207-275
    • Luduena, R.F.1
  • 126
    • 84855986261 scopus 로고    scopus 로고
    • Evolution and coevolution of tubulin's carboxy-terminal tails and mitochondria
    • Nova Science Publishers, USA, O.L. Svensson (Ed.)
    • Sackett D.L. Evolution and coevolution of tubulin's carboxy-terminal tails and mitochondria. Mitochondria: structure, functions and dysfunctions 2010, 441-470. Nova Science Publishers, USA. O.L. Svensson (Ed.).
    • (2010) Mitochondria: structure, functions and dysfunctions , pp. 441-470
    • Sackett, D.L.1
  • 127
    • 0037134782 scopus 로고    scopus 로고
    • Coherent and robust modulation of a metabolic network by cytoskeletal organization and dynamics
    • Aon M.A., Cortassa S. Coherent and robust modulation of a metabolic network by cytoskeletal organization and dynamics. Biophys Chem 2002, 97:213-231.
    • (2002) Biophys Chem , vol.97 , pp. 213-231
    • Aon, M.A.1    Cortassa, S.2
  • 128
    • 0842345404 scopus 로고    scopus 로고
    • The fractal architecture of cytoplasmic organization: scaling, kinetics and emergence in metabolic networks
    • Aon M.A., O'Rourke B., Cortassa S. The fractal architecture of cytoplasmic organization: scaling, kinetics and emergence in metabolic networks. Mol Cell Biochem 2004, 256-257:169-184.
    • (2004) Mol Cell Biochem , pp. 169-184
    • Aon, M.A.1    O'Rourke, B.2    Cortassa, S.3
  • 129
    • 77949654407 scopus 로고    scopus 로고
    • Study of possible interactions of tubulin, microtubular network, and STOP protein with mitochondria in muscle cells
    • Guerrero K., Monge C., Bruckner A., Puurand U., Kadaja L., Kaambre T., et al. Study of possible interactions of tubulin, microtubular network, and STOP protein with mitochondria in muscle cells. Mol Cell Biochem 2010, 337:239-249.
    • (2010) Mol Cell Biochem , vol.337 , pp. 239-249
    • Guerrero, K.1    Monge, C.2    Bruckner, A.3    Puurand, U.4    Kadaja, L.5    Kaambre, T.6
  • 130
    • 0040553757 scopus 로고    scopus 로고
    • Alternative binding of two sequential glycolytic enzymes to microtubules. Molecular studies in the phosphofructokinase/aldolase/microtubule system
    • Vertessy B.G., Orosz F., Kovacs J., Ovadi J. Alternative binding of two sequential glycolytic enzymes to microtubules. Molecular studies in the phosphofructokinase/aldolase/microtubule system. J Biol Chem 1997, 272:25542-25546.
    • (1997) J Biol Chem , vol.272 , pp. 25542-25546
    • Vertessy, B.G.1    Orosz, F.2    Kovacs, J.3    Ovadi, J.4
  • 131
    • 68149097082 scopus 로고    scopus 로고
    • Plasma membrane tubulin
    • Wolff J. Plasma membrane tubulin. Biochim Biophys Acta 2009, 1788:1415-1433.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1415-1433
    • Wolff, J.1
  • 132
    • 0033678504 scopus 로고    scopus 로고
    • The cytoskeleton and related proteins in the human failing heart
    • Kostin S., Hein S., Arnon E., Scholz D., Schaper J. The cytoskeleton and related proteins in the human failing heart. Heart Fail Rev 2000, 5:271-280.
    • (2000) Heart Fail Rev , vol.5 , pp. 271-280
    • Kostin, S.1    Hein, S.2    Arnon, E.3    Scholz, D.4    Schaper, J.5
  • 134
    • 0020553952 scopus 로고
    • Effects of microtubule-disrupting agents on insulin binding and degradation in isolated cardiocytes from adult rat
    • Eckel J., Reinauer H. Effects of microtubule-disrupting agents on insulin binding and degradation in isolated cardiocytes from adult rat. Hoppe Seylers Z Physiol Chem 1983, 364:845-850.
    • (1983) Hoppe Seylers Z Physiol Chem , vol.364 , pp. 845-850
    • Eckel, J.1    Reinauer, H.2
  • 135
    • 0032550231 scopus 로고    scopus 로고
    • Cytoskeletal role in the transition from compensated to decompensated hypertrophy during adult canine left ventricular pressure overloading
    • Tagawa H., Koide M., Sato H., Zile M.R., Carabello B.A., Cooper Gt Cytoskeletal role in the transition from compensated to decompensated hypertrophy during adult canine left ventricular pressure overloading. Circ Res 1998, 82:751-761.
    • (1998) Circ Res , vol.82 , pp. 751-761
    • Tagawa, H.1    Koide, M.2    Sato, H.3    Zile, M.R.4    Carabello, B.A.5    Cooper, G.6
  • 136
    • 0025202947 scopus 로고
    • Associations between beta-tubulin and mitochondria in adult isolated heart myocytes as shown by immunofluorescence and immunoelectron microscopy
    • Saetersdal T., Greve G., Dalen H. Associations between beta-tubulin and mitochondria in adult isolated heart myocytes as shown by immunofluorescence and immunoelectron microscopy. Histochemistry 1990, 95:1-10.
    • (1990) Histochemistry , vol.95 , pp. 1-10
    • Saetersdal, T.1    Greve, G.2    Dalen, H.3
  • 137
    • 0036276158 scopus 로고    scopus 로고
    • Disorganization of the desmin cytoskeleton and mitochondrial dysfunction in plectin-related epidermolysis bullosa simplex with muscular dystrophy
    • Schroder R., Kunz W.S., Rouan F., Pfendner E., Tolksdorf K., Kappes-Horn K., et al. Disorganization of the desmin cytoskeleton and mitochondrial dysfunction in plectin-related epidermolysis bullosa simplex with muscular dystrophy. J Neuropathol Exp Neurol 2002, 61:520-530.
    • (2002) J Neuropathol Exp Neurol , vol.61 , pp. 520-530
    • Schroder, R.1    Kunz, W.S.2    Rouan, F.3    Pfendner, E.4    Tolksdorf, K.5    Kappes-Horn, K.6
  • 138
    • 44149113780 scopus 로고    scopus 로고
    • Myofiber integrity depends on desmin network targeting to Z-disks and costameres via distinct plectin isoforms
    • Konieczny P., Fuchs P., Reipert S., Kunz W.S., Zeold A., Fischer I., et al. Myofiber integrity depends on desmin network targeting to Z-disks and costameres via distinct plectin isoforms. J Cell Biol 2008, 181:667-681.
    • (2008) J Cell Biol , vol.181 , pp. 667-681
    • Konieczny, P.1    Fuchs, P.2    Reipert, S.3    Kunz, W.S.4    Zeold, A.5    Fischer, I.6
  • 139
    • 60549111399 scopus 로고    scopus 로고
    • Muscular integrity-a matter of interlinking distinct structures via plectin
    • Konieczny P., Wiche G. Muscular integrity-a matter of interlinking distinct structures via plectin. Adv Exp Med Biol 2008, 642:165-175.
    • (2008) Adv Exp Med Biol , vol.642 , pp. 165-175
    • Konieczny, P.1    Wiche, G.2
  • 140
    • 0344668724 scopus 로고    scopus 로고
    • Plectin 5'-transcript diversity: short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms
    • Rezniczek G.A., Abrahamsberg C., Fuchs P., Spazierer D., Wiche G. Plectin 5'-transcript diversity: short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms. Hum Mol Genet 2003, 12:3181-3194.
    • (2003) Hum Mol Genet , vol.12 , pp. 3181-3194
    • Rezniczek, G.A.1    Abrahamsberg, C.2    Fuchs, P.3    Spazierer, D.4    Wiche, G.5
  • 141
    • 33947722764 scopus 로고    scopus 로고
    • Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with beta-dystroglycan
    • Rezniczek G.A., Konieczny P., Nikolic B., Reipert S., Schneller D., Abrahamsberg C., et al. Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with beta-dystroglycan. J Cell Biol 2007, 176:965-977.
    • (2007) J Cell Biol , vol.176 , pp. 965-977
    • Rezniczek, G.A.1    Konieczny, P.2    Nikolic, B.3    Reipert, S.4    Schneller, D.5    Abrahamsberg, C.6
  • 142
    • 45349095416 scopus 로고    scopus 로고
    • Plectin isoform 1b mediates mitochondrion-intermediate filament network linkage and controls organelle shape
    • Winter L., Abrahamsberg C., Wiche G. Plectin isoform 1b mediates mitochondrion-intermediate filament network linkage and controls organelle shape. J Cell Biol 2008, 181:903-911.
    • (2008) J Cell Biol , vol.181 , pp. 903-911
    • Winter, L.1    Abrahamsberg, C.2    Wiche, G.3
  • 143
    • 0032539911 scopus 로고    scopus 로고
    • HL-1 cells: a cardiac muscle cell line that contracts and retains phenotypic characteristics of the adult cardiomyocyte
    • Claycomb W.C., Lanson N.A., Stallworth B.S., Egeland D.B., Delcaprio A., Bahinski A., et al. HL-1 cells: a cardiac muscle cell line that contracts and retains phenotypic characteristics of the adult cardiomyocyte. Proc Natl Acad Sci USA 1998, 95:2979-2984.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2979-2984
    • Claycomb, W.C.1    Lanson, N.A.2    Stallworth, B.S.3    Egeland, D.B.4    Delcaprio, A.5    Bahinski, A.6
  • 144
    • 28344436619 scopus 로고    scopus 로고
    • Non beating HL-1 cells for confocal microscopy. Application to mitochondrial functions during cardiac preconditioning
    • Pelloux S., Robillard J., Ferrera R., Bilbaut A., Ojeda C., Saks V., et al. Non beating HL-1 cells for confocal microscopy. Application to mitochondrial functions during cardiac preconditioning. Prog Biophys Mol Biol 2006, 90:270-298.
    • (2006) Prog Biophys Mol Biol , vol.90 , pp. 270-298
    • Pelloux, S.1    Robillard, J.2    Ferrera, R.3    Bilbaut, A.4    Ojeda, C.5    Saks, V.6
  • 145
    • 85047679967 scopus 로고
    • Ca, Mg-ATPase activity of permeabilised rat heart cells and its functional coupling to oxidative phosphorylation of the cells
    • Kummel L. Ca, Mg-ATPase activity of permeabilised rat heart cells and its functional coupling to oxidative phosphorylation of the cells. Cardiovasc Res 1988, 22:359-367.
    • (1988) Cardiovasc Res , vol.22 , pp. 359-367
    • Kummel, L.1
  • 146
    • 0025801213 scopus 로고
    • In vivo regulation of mitochondrial respiration in cardiomyocytes: specific restrictions for intracellular diffusion of ADP
    • Saks V.A., Belikova Y.O., Kuznetsov A.V. In vivo regulation of mitochondrial respiration in cardiomyocytes: specific restrictions for intracellular diffusion of ADP. Biochim Biophys Acta 1991, 1074:302-311.
    • (1991) Biochim Biophys Acta , vol.1074 , pp. 302-311
    • Saks, V.A.1    Belikova, Y.O.2    Kuznetsov, A.V.3
  • 147
    • 0027324149 scopus 로고
    • Retarded diffusion of ADP in cardiomyocytes: possible role of mitochondrial outer membrane and creatine kinase in cellular regulation of oxidative phosphorylation
    • Saks V.A., Vasil'eva E., Belikova Yu O., Kuznetsov A.V., Lyapina S., Petrova L., et al. Retarded diffusion of ADP in cardiomyocytes: possible role of mitochondrial outer membrane and creatine kinase in cellular regulation of oxidative phosphorylation. Biochim Biophys Acta 1993, 1144:134-148.
    • (1993) Biochim Biophys Acta , vol.1144 , pp. 134-148
    • Saks, V.A.1    Vasil'eva, E.2    Belikova Yu, O.3    Kuznetsov, A.V.4    Lyapina, S.5    Petrova, L.6
  • 148
    • 10344258540 scopus 로고    scopus 로고
    • Striking differences between the kinetics of regulation of respiration by ADP in slow-twitch and fast-twitch muscles in vivo
    • Kuznetsov A.V., Tiivel T., Sikk P., Kaambre T., Kay L., Daneshrad Z., et al. Striking differences between the kinetics of regulation of respiration by ADP in slow-twitch and fast-twitch muscles in vivo. Eur J Biochem/FEBS 1996, 241:909-915.
    • (1996) Eur J Biochem/FEBS , vol.241 , pp. 909-915
    • Kuznetsov, A.V.1    Tiivel, T.2    Sikk, P.3    Kaambre, T.4    Kay, L.5    Daneshrad, Z.6
  • 149
    • 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., Kuznetsov A.V. 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 , pp. 155-192
    • Saks, V.A.1    Khuchua, Z.A.2    Vasilyeva, E.V.3    Belikova, O.4    Kuznetsov, A.V.5
  • 150
    • 0028946589 scopus 로고
    • Control of cellular respiration in vivo by mitochondrial outer membrane and by creatine kinase. A new speculative hypothesis: possible involvement of mitochondrial-cytoskeleton interactions
    • Saks V.A., Kuznetsov A.V., Khuchua Z.A., Vasilyeva E.V., Belikova J.O., Kesvatera T., et al. Control of cellular respiration in vivo by mitochondrial outer membrane and by creatine kinase. A new speculative hypothesis: possible involvement of mitochondrial-cytoskeleton interactions. J Mol Cell Cardiol 1995, 27:625-645.
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 625-645
    • Saks, V.A.1    Kuznetsov, A.V.2    Khuchua, Z.A.3    Vasilyeva, E.V.4    Belikova, J.O.5    Kesvatera, T.6
  • 151
    • 44949185670 scopus 로고    scopus 로고
    • Analysis of mitochondrial function in situ in permeabilized muscle fibers, tissues and cells
    • Kuznetsov A.V., Veksler V., Gellerich F.N., Saks V., Margreiter R., Kunz W.S. Analysis of mitochondrial function in situ in permeabilized muscle fibers, tissues and cells. Nat Protoc 2008, 3:965-976.
    • (2008) Nat Protoc , vol.3 , pp. 965-976
    • Kuznetsov, A.V.1    Veksler, V.2    Gellerich, F.N.3    Saks, V.4    Margreiter, R.5    Kunz, W.S.6
  • 152
    • 0037251713 scopus 로고    scopus 로고
    • Possible role of cytoskeleton in intracellular arrangement and regulation of mitochondria
    • Appaix F., Kuznetsov A.V., Usson Y., Kay L., Andrienko T., Olivares J., et al. Possible role of cytoskeleton in intracellular arrangement and regulation of mitochondria. Exp Physiol 2003, 88:175-190.
    • (2003) Exp Physiol , vol.88 , pp. 175-190
    • Appaix, F.1    Kuznetsov, A.V.2    Usson, Y.3    Kay, L.4    Andrienko, T.5    Olivares, J.6
  • 154
    • 52449104836 scopus 로고    scopus 로고
    • VDAC regulation: role of cytosolic proteins and mitochondrial lipids
    • Rostovtseva T.K., Bezrukov S.M. VDAC regulation: role of cytosolic proteins and mitochondrial lipids. J Bioenerg Biomembr 2008, 40:163-170.
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 163-170
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 155
    • 54949088596 scopus 로고    scopus 로고
    • Regulation of respiration in brain mitochondria and synaptosomes: restrictions of ADP diffusion in situ, roles of tubulin, and mitochondrial creatine kinase
    • Monge C., Beraud N., Kuznetsov A.V., Rostovtseva T., Sackett D., Schlattner U., et al. Regulation of respiration in brain mitochondria and synaptosomes: restrictions of ADP diffusion in situ, roles of tubulin, and mitochondrial creatine kinase. Mol Cell Biochem 2008, 318:147-165.
    • (2008) Mol Cell Biochem , vol.318 , pp. 147-165
    • Monge, C.1    Beraud, N.2    Kuznetsov, A.V.3    Rostovtseva, T.4    Sackett, D.5    Schlattner, U.6
  • 156
    • 0019972152 scopus 로고
    • Interaction of tubulin with rat liver mitochondria
    • Bernier-Valentin F., Rousset B. Interaction of tubulin with rat liver mitochondria. J Biol Chem 1982, 257:7092-7099.
    • (1982) J Biol Chem , vol.257 , pp. 7092-7099
    • Bernier-Valentin, F.1    Rousset, B.2
  • 157
    • 0037072776 scopus 로고    scopus 로고
    • Tubulin is an inherent component of mitochondrial membranes that interacts with the voltage-dependent anion channel
    • Carre M., Andre N., Carles G., Borghi H., Brichese L., Briand C., et al. Tubulin is an inherent component of mitochondrial membranes that interacts with the voltage-dependent anion channel. J Biol Chem 2002, 277:33664-33669.
    • (2002) J Biol Chem , vol.277 , pp. 33664-33669
    • Carre, M.1    Andre, N.2    Carles, G.3    Borghi, H.4    Brichese, L.5    Briand, C.6
  • 158
    • 33751509690 scopus 로고    scopus 로고
    • Different kinetics of the regulation of respiration in permeabilized cardiomyocytes and in HL-1 cardiac cells. Importance of cell structure/organization for respiration regulation
    • Anmann T., Guzun R., Beraud N., Pelloux S., Kuznetsov A.V., Kogerman L., et al. Different kinetics of the regulation of respiration in permeabilized cardiomyocytes and in HL-1 cardiac cells. Importance of cell structure/organization for respiration regulation. Biochim Biophys Acta 2006, 1757:1597-1606.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 1597-1606
    • Anmann, T.1    Guzun, R.2    Beraud, N.3    Pelloux, S.4    Kuznetsov, A.V.5    Kogerman, L.6
  • 159
    • 44649191628 scopus 로고    scopus 로고
    • Distinct organization of energy metabolism in HL-1 cardiac cell line and cardiomyocytes
    • Eimre M., Paju K., Pelloux S., Beraud N., Roosimaa M., Kadaja L., et al. Distinct organization of energy metabolism in HL-1 cardiac cell line and cardiomyocytes. Biochim Biophys Acta 2008, 1777:514-524.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 514-524
    • Eimre, M.1    Paju, K.2    Pelloux, S.3    Beraud, N.4    Roosimaa, M.5    Kadaja, L.6
  • 160
    • 65249086769 scopus 로고    scopus 로고
    • Comparative analysis of the bioenergetics of adult cardiomyocytes and nonbeating HL-1 cells: respiratory chain activities, glycolytic enzyme profiles, and metabolic fluxes
    • Monge C., Beraud N., Tepp K., Pelloux S., Chahboun S., Kaambre T., et al. Comparative analysis of the bioenergetics of adult cardiomyocytes and nonbeating HL-1 cells: respiratory chain activities, glycolytic enzyme profiles, and metabolic fluxes. Can J Physiol Pharmacol 2009, 87:318-326.
    • (2009) Can J Physiol Pharmacol , vol.87 , pp. 318-326
    • Monge, C.1    Beraud, N.2    Tepp, K.3    Pelloux, S.4    Chahboun, S.5    Kaambre, T.6
  • 161
    • 68749106797 scopus 로고    scopus 로고
    • Direct measurement of energy fluxes from mitochondria into cytoplasm in permeabilized cardiac cells in situ: some evidence for Mitochondrial Interactosome
    • Timohhina N., Guzun R., Tepp K., Monge C., Varikmaa M., Vija H., et al. Direct measurement of energy fluxes from mitochondria into cytoplasm in permeabilized cardiac cells in situ: some evidence for Mitochondrial Interactosome. J Bioenerg Biomembr 2009, 41:259-275.
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 259-275
    • Timohhina, N.1    Guzun, R.2    Tepp, K.3    Monge, C.4    Varikmaa, M.5    Vija, H.6
  • 162
    • 29344468308 scopus 로고    scopus 로고
    • Metabolite channeling: creatine kinase microcompartments
    • Academic Press, New York, USA, W.J. Lennarz, M.D. Lane (Eds.)
    • Schlattner U., Wallimann T. Metabolite channeling: creatine kinase microcompartments. Encyclopedia of biological chemistry 2004, 646-651. Academic Press, New York, USA. W.J. Lennarz, M.D. Lane (Eds.).
    • (2004) Encyclopedia of biological chemistry , pp. 646-651
    • Schlattner, U.1    Wallimann, T.2
  • 164
    • 52049113898 scopus 로고    scopus 로고
    • The ADP and ATP transport in mitochondria and its carrier
    • Klingenberg M. The ADP and ATP transport in mitochondria and its carrier. Biochim Biophys Acta 2008, 1778:1978-2021.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1978-2021
    • Klingenberg, M.1
  • 166
    • 0020214568 scopus 로고
    • Creatine kinase of heart mitochondria: changes in its kinetic properties induced by coupling to oxidative phosphorylation
    • Jacobus W.E., Saks V.A. Creatine kinase of heart mitochondria: changes in its kinetic properties induced by coupling to oxidative phosphorylation. Arch Biochem Biophys 1982, 219:167-178.
    • (1982) Arch Biochem Biophys , vol.219 , pp. 167-178
    • Jacobus, W.E.1    Saks, V.A.2
  • 167
    • 0024545098 scopus 로고
    • Heart mitochondrial creatine kinase revisited: the outer mitochondrial membrane is not important for coupling of phosphocreatine production to oxidative phosphorylation
    • Kuznetsov A.V., Khuchua Z.A., Vassil'eva E.V., Medved'eva N.V., Saks V.A. Heart mitochondrial creatine kinase revisited: the outer mitochondrial membrane is not important for coupling of phosphocreatine production to oxidative phosphorylation. Arch Biochem Biophys 1989, 268:176-190.
    • (1989) Arch Biochem Biophys , vol.268 , pp. 176-190
    • Kuznetsov, A.V.1    Khuchua, Z.A.2    Vassil'eva, E.V.3    Medved'eva, N.V.4    Saks, V.A.5
  • 168
    • 84900949800 scopus 로고    scopus 로고
    • Mechanisms and modeling of energy transfer between and among intracellular compartments
    • Springer Science and Business Media, New York-Boston, USA, G. Dienel, G. Gibson (Eds.)
    • Saks V.A., Vendelin M., Aliev M.K., Kekelidze T., Engelbrecht J. Mechanisms and modeling of energy transfer between and among intracellular compartments. Handbook of neurochemistry and molecular neurobiology 2007, 815-860. Springer Science and Business Media, New York-Boston, USA. 3rd ed. G. Dienel, G. Gibson (Eds.).
    • (2007) Handbook of neurochemistry and molecular neurobiology , pp. 815-860
    • Saks, V.A.1    Vendelin, M.2    Aliev, M.K.3    Kekelidze, T.4    Engelbrecht, J.5
  • 169
    • 0021243540 scopus 로고
    • Effect of creatine kinase activity on mitochondrial ADP/ATP transport. Evidence for a functional interaction
    • Barbour R.L., Ribaudo J., Chan S.H. Effect of creatine kinase activity on mitochondrial ADP/ATP transport. Evidence for a functional interaction. J Biol Chem 1984, 259:8246-8251.
    • (1984) J Biol Chem , vol.259 , pp. 8246-8251
    • Barbour, R.L.1    Ribaudo, J.2    Chan, S.H.3
  • 170
    • 0023093812 scopus 로고
    • Specific inhibition of ATP-ADP translocase in cardiac mitoplasts by antibodies against mitochondrial creatine kinase
    • Saks V.A., Khuchua Z.A., Kuznetsov A.V. Specific inhibition of ATP-ADP translocase in cardiac mitoplasts by antibodies against mitochondrial creatine kinase. Biochim Biophys Acta 1987, 891:138-144.
    • (1987) Biochim Biophys Acta , vol.891 , pp. 138-144
    • Saks, V.A.1    Khuchua, Z.A.2    Kuznetsov, A.V.3
  • 171
    • 0023124963 scopus 로고
    • Oxidative phosphorylation of creatine by respiring pig heart mitochondria in the absence of added adenine nucleotides
    • Kim I.H., Lee H.J. Oxidative phosphorylation of creatine by respiring pig heart mitochondria in the absence of added adenine nucleotides. Biochem Int 1987, 14:103-110.
    • (1987) Biochem Int , vol.14 , pp. 103-110
    • Kim, I.H.1    Lee, H.J.2
  • 172
    • 0842345400 scopus 로고    scopus 로고
    • VDAC: the channel at the interface between mitochondria and the cytosol
    • Colombini M. VDAC: the channel at the interface between mitochondria and the cytosol. Mol Cell Biochem 2004, 256-257:107-115.
    • (2004) Mol Cell Biochem , pp. 107-115
    • Colombini, M.1
  • 173
    • 68249126139 scopus 로고    scopus 로고
    • The published 3D structure of the VDAC channel: native or not?
    • Colombini M. The published 3D structure of the VDAC channel: native or not?. Trends Biochem Sci 2009, 34:382-389.
    • (2009) Trends Biochem Sci , vol.34 , pp. 382-389
    • Colombini, M.1
  • 174
    • 0020402772 scopus 로고
    • Control of heart mitochondrial oxygen consumption by creatine kinase: the importance of enzyme localization
    • Gellerich F., Saks V.A. Control of heart mitochondrial oxygen consumption by creatine kinase: the importance of enzyme localization. Biochem Biophys Res Commun 1982, 105:1473-1481.
    • (1982) Biochem Biophys Res Commun , vol.105 , pp. 1473-1481
    • Gellerich, F.1    Saks, V.A.2
  • 175
    • 3843147327 scopus 로고    scopus 로고
    • Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP
    • Chen C., Ko Y., Delannoy M., Ludtke S.J., Chiu W., Pedersen P.L. Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP. J Biol Chem 2004, 279:31761-31768.
    • (2004) J Biol Chem , vol.279 , pp. 31761-31768
    • Chen, C.1    Ko, Y.2    Delannoy, M.3    Ludtke, S.J.4    Chiu, W.5    Pedersen, P.L.6
  • 176
    • 77950907315 scopus 로고    scopus 로고
    • Mitochondrial VDAC and its complexes
    • Wiley-VCH, GmbH, Weinheim, Germany, V. Saks (Ed.)
    • Brdiszka D. Mitochondrial VDAC and its complexes. Molecular system bioenergetics energy for life 2007, 165-194. Wiley-VCH, GmbH, Weinheim, Germany. V. Saks (Ed.).
    • (2007) Molecular system bioenergetics energy for life , pp. 165-194
    • Brdiszka, D.1
  • 177
    • 0031806216 scopus 로고    scopus 로고
    • The sensor regions of VDAC are translocated from within the membrane to the surface during gating processes
    • Song J., Midson C., Blachly-Dyson E., Forte M., Colombini M. The sensor regions of VDAC are translocated from within the membrane to the surface during gating processes. Biophys J 1998, 74:2926-2944.
    • (1998) Biophys J , vol.74 , pp. 2926-2944
    • Song, J.1    Midson, C.2    Blachly-Dyson, E.3    Forte, M.4    Colombini, M.5
  • 178
    • 0018391707 scopus 로고
    • Compartmentation and communication in living cells. Ligand conduction: a general catalytic principal in chemical, osmotic and chemiosmotic reaction systems
    • Mitchell P. Compartmentation and communication in living cells. Ligand conduction: a general catalytic principal in chemical, osmotic and chemiosmotic reaction systems. Eur J Biochem 1979, 95:1-20.
    • (1979) Eur J Biochem , vol.95 , pp. 1-20
    • Mitchell, P.1
  • 179
    • 79956144642 scopus 로고    scopus 로고
    • A postreductionist framework for protein biochemistry
    • Laue T., Demeler B. A postreductionist framework for protein biochemistry. Nat Chem Biol 2011, 7:331-334.
    • (2011) Nat Chem Biol , vol.7 , pp. 331-334
    • Laue, T.1    Demeler, B.2
  • 180
    • 79551585807 scopus 로고    scopus 로고
    • Metabolic control analysis of integrated energy metabolism in permeabilized cardiomyocytes - experimental study
    • Tepp K., Timohhina N., Chekulayev V., Shevchuk I., Kaambre T., Saks V. Metabolic control analysis of integrated energy metabolism in permeabilized cardiomyocytes - experimental study. Acta Biochim Pol 2010, 57:421-430.
    • (2010) Acta Biochim Pol , vol.57 , pp. 421-430
    • Tepp, K.1    Timohhina, N.2    Chekulayev, V.3    Shevchuk, I.4    Kaambre, T.5    Saks, V.6
  • 182
    • 0027456261 scopus 로고
    • Metabolic channelling and control of the flux
    • Kholodenko B.N., Westerhoff H.V. Metabolic channelling and control of the flux. FEBS Lett 1993, 320:71-74.
    • (1993) FEBS Lett , vol.320 , pp. 71-74
    • Kholodenko, B.N.1    Westerhoff, H.V.2
  • 184
    • 0036242350 scopus 로고    scopus 로고
    • Cyclical changes in high-energy phosphates during the cardiac cycle by pacing-Gated 31P nuclear magnetic resonance
    • Honda H., Tanaka K., Akita N., Haneda T. Cyclical changes in high-energy phosphates during the cardiac cycle by pacing-Gated 31P nuclear magnetic resonance. Circ J 2002, 66:80-86.
    • (2002) Circ J , vol.66 , pp. 80-86
    • Honda, H.1    Tanaka, K.2    Akita, N.3    Haneda, T.4
  • 185
    • 0034747224 scopus 로고    scopus 로고
    • Temporal fluctuations of myocardia high-energy phosphate metabolite with the cardiac cycle
    • Spindler M., Illing B., Horn M., de Groot M., Ertl G., Neubauer S. Temporal fluctuations of myocardia high-energy phosphate metabolite with the cardiac cycle. Basic Res Cardiol 2001, 96:553-556.
    • (2001) Basic Res Cardiol , vol.96 , pp. 553-556
    • Spindler, M.1    Illing, B.2    Horn, M.3    de Groot, M.4    Ertl, G.5    Neubauer, S.6
  • 186
    • 0030992292 scopus 로고    scopus 로고
    • Compartmentalized energy transfer in cardiomyocytes: use of mathematical modeling for analysis of in vivo regulation of respiration
    • Aliev M.K., Saks V.A. Compartmentalized energy transfer in cardiomyocytes: use of mathematical modeling for analysis of in vivo regulation of respiration. Biophys J 1997, 73:428-445.
    • (1997) Biophys J , vol.73 , pp. 428-445
    • Aliev, M.K.1    Saks, V.A.2
  • 187
    • 0029988948 scopus 로고    scopus 로고
    • Metabolic control and metabolic capacity: two aspects of creatine kinase functioning in the cells
    • Saks V.A., Ventura-Clapier R., Aliev M.K. Metabolic control and metabolic capacity: two aspects of creatine kinase functioning in the cells. Biochim Biophys Acta 1996, 1274:81-88.
    • (1996) Biochim Biophys Acta , vol.1274 , pp. 81-88
    • Saks, V.A.1    Ventura-Clapier, R.2    Aliev, M.K.3
  • 188
    • 0034086313 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiration in heart cells analyzed by reaction-diffusion model of energy transfer
    • Vendelin M., Kongas O., Saks V. Regulation of mitochondrial respiration in heart cells analyzed by reaction-diffusion model of energy transfer. Am J Physiol Cell Physiol 2000, 278:C747-C764.
    • (2000) Am J Physiol Cell Physiol , vol.278
    • Vendelin, M.1    Kongas, O.2    Saks, V.3
  • 189
    • 0034043681 scopus 로고    scopus 로고
    • Role of the creatine/phosphocreatine system in the regulation of mitochondrial respiration
    • Saks V.A., Kongas O., Vendelin M., Kay L. Role of the creatine/phosphocreatine system in the regulation of mitochondrial respiration. Acta Physiol Scand 2000, 168:635-641.
    • (2000) Acta Physiol Scand , vol.168 , pp. 635-641
    • Saks, V.A.1    Kongas, O.2    Vendelin, M.3    Kay, L.4
  • 191
    • 33846001693 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase activity prevents reactive oxygen species generation: antioxidant role of mitochondrial kinase-dependent ADP re-cycling activity
    • Meyer L.E., Machado L.B., Santiago A.P., da-Silva W.S., De Felice F.G., Holub O., et al. Mitochondrial creatine kinase activity prevents reactive oxygen species generation: antioxidant role of mitochondrial kinase-dependent ADP re-cycling activity. J Biol Chem 2006, 281:37361-37371.
    • (2006) J Biol Chem , vol.281 , pp. 37361-37371
    • Meyer, L.E.1    Machado, L.B.2    Santiago, A.P.3    da-Silva, W.S.4    De Felice, F.G.5    Holub, O.6
  • 192
    • 0038381490 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for microcompartmentation
    • Dolder M., Walzel B., Speer O., Schlattner U., Wallimann T. Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for microcompartmentation. J Biol Chem 2003, 278:17760-17766.
    • (2003) J Biol Chem , vol.278 , pp. 17760-17766
    • Dolder, M.1    Walzel, B.2    Speer, O.3    Schlattner, U.4    Wallimann, T.5
  • 193
    • 77953809992 scopus 로고    scopus 로고
    • Redox-optimized ROS balance: a unifying hypothesis
    • Aon M.A., Cortassa S., O'Rourke B. Redox-optimized ROS balance: a unifying hypothesis. Biochim Biophys Acta 2010, 1797:865-877.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 865-877
    • Aon, M.A.1    Cortassa, S.2    O'Rourke, B.3
  • 195
    • 0035259181 scopus 로고    scopus 로고
    • Calcium, cross-bridges, and the Frank-Starling relationship
    • Fuchs F., Smith S.H. Calcium, cross-bridges, and the Frank-Starling relationship. News Physiol Sci 2001, 16:5-10.
    • (2001) News Physiol Sci , vol.16 , pp. 5-10
    • Fuchs, F.1    Smith, S.H.2
  • 196
    • 84889281594 scopus 로고    scopus 로고
    • Integration of adenylate kinase and glycolytic and clycogenolytic circuits in cellular energetics
    • Wiley-VCH, GmbH, Weinheim, Germany, V. Saks (Ed.)
    • Dzeja P., Chung S., Terzic A. Integration of adenylate kinase and glycolytic and clycogenolytic circuits in cellular energetics. Molecular system bioenergetics energy for life 2007, 195-264. Wiley-VCH, GmbH, Weinheim, Germany. V. Saks (Ed.).
    • (2007) Molecular system bioenergetics energy for life , pp. 195-264
    • Dzeja, P.1    Chung, S.2    Terzic, A.3
  • 197
    • 33947239659 scopus 로고    scopus 로고
    • The failing heart-an engine out of fuel
    • Neubauer S. The failing heart-an engine out of fuel. N Engl J Med 2007, 356:1140-1151.
    • (2007) N Engl J Med , vol.356 , pp. 1140-1151
    • Neubauer, S.1
  • 199
    • 14144256552 scopus 로고    scopus 로고
    • ATP flux through creatine kinase in the normal, stressed, and failing human heart
    • Weiss R.G., Gerstenblith G., Bottomley P.A. ATP flux through creatine kinase in the normal, stressed, and failing human heart. Proc Natl Acad Sci USA 2005, 102:808-813.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 808-813
    • Weiss, R.G.1    Gerstenblith, G.2    Bottomley, P.A.3
  • 200
    • 33751569205 scopus 로고    scopus 로고
    • On the hypothesis that the failing heart is energy starved: lessons learned from the metabolism of ATP and creatine
    • Ingwall J.S. On the hypothesis that the failing heart is energy starved: lessons learned from the metabolism of ATP and creatine. Curr Hypertens Rep 2006, 8:457-464.
    • (2006) Curr Hypertens Rep , vol.8 , pp. 457-464
    • Ingwall, J.S.1
  • 201
    • 3342967512 scopus 로고    scopus 로고
    • Is the failing heart energy starved? On using chemical energy to support cardiac function
    • Ingwall J.S., Weiss R.G. Is the failing heart energy starved? On using chemical energy to support cardiac function. Circ Res 2004, 95:135-145.
    • (2004) Circ Res , vol.95 , pp. 135-145
    • Ingwall, J.S.1    Weiss, R.G.2
  • 203
    • 67651237070 scopus 로고    scopus 로고
    • Exercise training, energy metabolism, and heart failure. Applied physiology, nutrition, and metabolism
    • Ventura-Clapier R. Exercise training, energy metabolism, and heart failure. Applied physiology, nutrition, and metabolism. Physiologie Appliquee, Nutrition et Metabolisme 2009, 34:336-339.
    • (2009) Physiologie Appliquee, Nutrition et Metabolisme , vol.34 , pp. 336-339
    • Ventura-Clapier, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.