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Volumn 213, Issue 1, 2015, Pages 84-106

Modular organization of cardiac energy metabolism: energy conversion, transfer and feedback regulation

Author keywords

cardiac metabolism; creatine kinase; mitochondria; respiration regulation

Indexed keywords

ADENINE NUCLEOTIDE; ADENOSINE TRIPHOSPHATE; CREATINE;

EID: 84965087797     PISSN: 17481708     EISSN: 17481716     Source Type: Journal    
DOI: 10.1111/apha.12287     Document Type: Review
Times cited : (43)

References (173)
  • 1
    • 0037025324 scopus 로고    scopus 로고
    • Coupling of cell energetics with membrane metabolic sensing. Integrative signaling through creatine kinase phosphotransfer disrupted by M-CK gene knock-out
    • Abraham, M.R., Selivanov, V.A., Hodgson, D.M., Pucar, D., Zingman, L.V., Wieringa, B., Dzeja, P.P., Alekseev, A.E. & Terzic, A. 2002. Coupling of cell energetics with membrane metabolic sensing. Integrative signaling through creatine kinase phosphotransfer disrupted by M-CK gene knock-out. J Biol Chem 277, 24427–24434.
    • (2002) J Biol Chem , vol.277 , pp. 24427-24434
    • Abraham, M.R.1    Selivanov, V.A.2    Hodgson, D.M.3    Pucar, D.4    Zingman, L.V.5    Wieringa, B.6    Dzeja, P.P.7    Alekseev, A.E.8    Terzic, A.9
  • 3
    • 84055172512 scopus 로고    scopus 로고
    • Compartmentation of membrane processes and nucleotide dynamics in diffusion-restricted cardiac cell microenvironment
    • Alekseev, A.E., Reyes, S., Selivanov, V.A., Dzeja, P.P. & Terzic, A. 2012. Compartmentation of membrane processes and nucleotide dynamics in diffusion-restricted cardiac cell microenvironment. J Mol Cell Cardiol 52, 401–409.
    • (2012) J Mol Cell Cardiol , vol.52 , pp. 401-409
    • Alekseev, A.E.1    Reyes, S.2    Selivanov, V.A.3    Dzeja, P.P.4    Terzic, A.5
  • 4
    • 0027199664 scopus 로고
    • Quantitative analysis of the ‘phosphocreatine shuttle’: i. A probability approach to the description of phosphocreatine production in the coupled creatine kinase-ATP/ADP translocase-oxidative phosphorylation reactions in heart mitochondria
    • Aliev, M.K. & Saks, V.A. 1993. Quantitative analysis of the ‘phosphocreatine shuttle’: i. A probability approach to the description of phosphocreatine production in the coupled creatine kinase-ATP/ADP translocase-oxidative phosphorylation reactions in heart mitochondria. Biochim Biophys Acta 1143, 291–300.
    • (1993) Biochim Biophys Acta , vol.1143 , pp. 291-300
    • Aliev, M.K.1    Saks, V.A.2
  • 5
    • 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. 1997. Compartmentalized energy transfer in cardiomyocytes: use of mathematical modeling for analysis of in vivo regulation of respiration. Biophys J 73, 428–445.
    • (1997) Biophys J , vol.73 , pp. 428-445
    • Aliev, M.K.1    Saks, V.A.2
  • 6
    • 84055217238 scopus 로고    scopus 로고
    • Molecular system bioenergics of the heart: experimental studies of metabolic compartmentation and energy fluxes versus computer modeling
    • Aliev, M., Guzun, R., Karu-Varikmaa, M., Kaambre, T., Wallimann, T. & Saks, V. 2011. Molecular system bioenergics of the heart: experimental studies of metabolic compartmentation and energy fluxes versus computer modeling. Int J Mol Sci 12, 9296–9331.
    • (2011) Int J Mol Sci , vol.12 , pp. 9296-9331
    • Aliev, M.1    Guzun, R.2    Karu-Varikmaa, M.3    Kaambre, T.4    Wallimann, T.5    Saks, V.6
  • 7
    • 0035910495 scopus 로고    scopus 로고
    • Altered mitochondrial sensitivity for ADP and maintenance of creatine-stimulated respiration in oxidative striated muscles from VDAC1-deficient mice
    • Anflous, K., Armstrong, D.D. & Craigen, W.J. 2001. Altered mitochondrial sensitivity for ADP and maintenance of creatine-stimulated respiration in oxidative striated muscles from VDAC1-deficient mice. J Biol Chem 276, 1954–1960.
    • (2001) J Biol Chem , vol.276 , pp. 1954-1960
    • Anflous, K.1    Armstrong, D.D.2    Craigen, W.J.3
  • 8
    • 33847135285 scopus 로고    scopus 로고
    • VDAC1 serves as a mitochondrial binding site for hexokinase in oxidative muscles
    • Anflous-Pharayra, K., Cai, Z.-J. & Craigen, W.J. 2007. VDAC1 serves as a mitochondrial binding site for hexokinase in oxidative muscles. Biochim Biophys Acta 1767, 136–142.
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 136-142
    • Anflous-Pharayra, K.1    Cai, Z.-J.2    Craigen, W.J.3
  • 9
    • 78249279991 scopus 로고    scopus 로고
    • VDAC3 has differing mitochondrial functions in two types of striated muscles
    • Anflous-Pharayra, K., Lee, N., Armstrong, D.L. & Craigen, W.J. 2011. VDAC3 has differing mitochondrial functions in two types of striated muscles. Biochim Biophys Acta 1807, 150–156.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 150-156
    • Anflous-Pharayra, K.1    Lee, N.2    Armstrong, D.L.3    Craigen, W.J.4
  • 11
    • 0242582202 scopus 로고    scopus 로고
    • Synchronized whole cell oscillations in mitochondrial metabolism triggered by a local release of reactive oxygen species in cardiac myocytes
    • Aon, M.A., Cortassa, S., Marbán, E. & O'Rourke, B. 2003. Synchronized whole cell oscillations in mitochondrial metabolism triggered by a local release of reactive oxygen species in cardiac myocytes. J Biol Chem 278, 44735–44744.
    • (2003) J Biol Chem , vol.278 , pp. 44735-44744
    • Aon, M.A.1    Cortassa, S.2    Marbán, E.3    O'Rourke, B.4
  • 12
    • 56149123045 scopus 로고    scopus 로고
    • On the network properties of mitochondria
    • In, V. Saks, (ed.), Wiley-VCH Verlag GmbH & KGaA, Germany
    • Aon, M.A., Cortassa, S. & O'Rourke, B. 2007. On the network properties of mitochondria. In: V. Saks (ed.) Molecular System Bioenergetics. Energy for Life, pp. 111–135. Wiley-VCH Verlag GmbH & KGaA, Germany.
    • (2007) Molecular System Bioenergetics. Energy for Life , pp. 111-135
    • Aon, M.A.1    Cortassa, S.2    O'Rourke, B.3
  • 13
    • 0036773295 scopus 로고    scopus 로고
    • Cardiac energy metabolism homeostasis: role of cytosolic calcium
    • Balaban, R.S. 2002. Cardiac energy metabolism homeostasis: role of cytosolic calcium. J Mol Cell Cardiol 34, 1259–1271.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 1259-1271
    • Balaban, R.S.1
  • 14
    • 67349244350 scopus 로고    scopus 로고
    • Domestication of the cardiac mitochondrion for energy conversion
    • Balaban, R.S. 2009. Domestication of the cardiac mitochondrion for energy conversion. J Mol Cell Cardiol 46, 832–841.
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 832-841
    • Balaban, R.S.1
  • 15
    • 84864004879 scopus 로고    scopus 로고
    • Perspectives on: SGP symposium on mitochondrial physiology and medicine: metabolichomeostasis of the heart
    • Balaban, R.S. 2012. Perspectives on: SGP symposium on mitochondrial physiology and medicine: metabolichomeostasis of the heart. J Gen Physiol 139, 407–414.
    • (2012) J Gen Physiol , vol.139 , pp. 407-414
    • Balaban, R.S.1
  • 16
    • 79959830121 scopus 로고    scopus 로고
    • Interpretation of ³¹P NMR saturation transfer experiments: what you can't see might confuse you. Focus on “Standard magnetic resonance-based measurements of the Pi→ATP rate do not index the rate of oxidative phosphorylation in cardiac and skeletal muscles
    • Balaban, R.S. & Koretsky, A.P. 2011. Interpretation of ³¹P NMR saturation transfer experiments: what you can't see might confuse you. Focus on “Standard magnetic resonance-based measurements of the Pi→ATP rate do not index the rate of oxidative phosphorylation in cardiac and skeletal muscles”. Am J Physiol Cell Physiol 301, C12–C15.
    • (2011) Am J Physiol Cell Physiol , vol.301 , pp. C12-C15
    • Balaban, R.S.1    Koretsky, A.P.2
  • 17
    • 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. 1986. Relation between work and phosphate metabolite in the in vivo paced mammalian heart. Science 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
  • 18
    • 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. & Saks, V. 2009. 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 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    Saks, V.7
  • 19
    • 33747599910 scopus 로고    scopus 로고
    • Cardiac myocytes Ca2+ and Na+ regulation in normal and failing hearts
    • Bers, D.M. & Despa, S. 2006. Cardiac myocytes Ca2+ and Na+ regulation in normal and failing hearts. J Pharmacol Sci 100, 315–322.
    • (2006) J Pharmacol Sci , vol.100 , pp. 315-322
    • Bers, D.M.1    Despa, S.2
  • 20
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shuttle
    • Bessman, S.P. & Carpenter, C.L. 1985. The creatine-creatine phosphate energy shuttle. Annu Rev Biochem 54, 831–862.
    • (1985) Annu Rev Biochem , vol.54 , pp. 831-862
    • Bessman, S.P.1    Carpenter, C.L.2
  • 21
    • 0033840893 scopus 로고    scopus 로고
    • Glycolysis supports calcium uptake by the sarcoplasmic reticulum in skinned ventricular fibres of mice deficient in mitochondrial and cytosolic creatine kinase
    • Boehm, E., Ventura-Clapier, R., Mateo, P., Lechène, P. & Veksler, V. 2000. Glycolysis supports calcium uptake by the sarcoplasmic reticulum in skinned ventricular fibres of mice deficient in mitochondrial and cytosolic creatine kinase. J Mol Cell Cardiol 32, 891–902.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 891-902
    • Boehm, E.1    Ventura-Clapier, R.2    Mateo, P.3    Lechène, P.4    Veksler, V.5
  • 22
    • 0036872241 scopus 로고    scopus 로고
    • Desmin cytoskeleton: a potential regulator of muscle mitochondrial behavior and function
    • Capetanaki, Y. 2002. Desmin cytoskeleton: a potential regulator of muscle mitochondrial behavior and function. Trends Cardiovasc Med 12, 339–348.
    • (2002) Trends Cardiovasc Med , vol.12 , pp. 339-348
    • Capetanaki, Y.1
  • 23
    • 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. 2007. Muscle intermediate filaments and their links to membranes and membranous organelles. Exp Cell Res 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
  • 24
    • 0037072776 scopus 로고    scopus 로고
    • Tubulin is an inherent component of mitochondrial membranes that interacts with the voltage-dependent anion channel
    • Carré, M., André, N., Carles, G., Borghi, H., Brichese, L., Briand, C. & Braguer, D. 2002. Tubulin is an inherent component of mitochondrial membranes that interacts with the voltage-dependent anion channel. J Biol Chem 277, 33664–33669.
    • (2002) J Biol Chem , vol.277 , pp. 33664-33669
    • Carré, M.1    André, N.2    Carles, G.3    Borghi, H.4    Brichese, L.5    Briand, C.6    Braguer, D.7
  • 25
    • 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. 2004. 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 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
  • 26
    • 70449724857 scopus 로고    scopus 로고
    • Mitochondrial OPA1, apoptosis, and heart failure
    • Chen, L., Gong, Q., Stice, J.P. & Knowlton, A.A. 2009. Mitochondrial OPA1, apoptosis, and heart failure. Cardiovasc Res 84, 91–99.
    • (2009) Cardiovasc Res , vol.84 , pp. 91-99
    • Chen, L.1    Gong, Q.2    Stice, J.P.3    Knowlton, A.A.4
  • 27
    • 84856109625 scopus 로고    scopus 로고
    • Mitochondrial fusion is essential for organelle function and cardiac homeostasis
    • Chen, Y., Liu, Y. & Dorn, G.W. II 2012. Mitochondrial fusion is essential for organelle function and cardiac homeostasis. Circ Res 109, 1327–1331.
    • (2012) Circ Res , vol.109 , pp. 1327-1331
    • Chen, Y.1    Liu, Y.2    Dorn, G.W.3
  • 28
  • 29
    • 84884647487 scopus 로고    scopus 로고
    • Homoarginine levels are regulated by L-arginine:glycine amidinotransferase and affect stroke outcome: results from human and murine studies
    • Choe, C.U., Atzler, D., Wild, P.S., Carter, A.M., Böger, R.H., Ojeda, F., Simova, O., Stockebrand, M., Lackner, K., Nabuurs, C. et al. 2013. Homoarginine levels are regulated by L-arginine:glycine amidinotransferase and affect stroke outcome: results from human and murine studies. Circulation 128, 1451–1461.
    • (2013) Circulation , vol.128 , pp. 1451-1461
    • Choe, C.U.1    Atzler, D.2    Wild, P.S.3    Carter, A.M.4    Böger, R.H.5    Ojeda, F.6    Simova, O.7    Stockebrand, M.8    Lackner, K.9    Nabuurs, C.10
  • 30
    • 57649217415 scopus 로고    scopus 로고
    • Developmental restructuring of the creatine kinase system integrates mitochondrial energetics with stem cell cardiogenesis
    • Chung, S., Dzeja, P.P., Faustino, R.S. & Terzic, A. 2008. Developmental restructuring of the creatine kinase system integrates mitochondrial energetics with stem cell cardiogenesis. Ann N Y Acad Sci 1147, 254–263.
    • (2008) Ann N Y Acad Sci , vol.1147 , pp. 254-263
    • Chung, S.1    Dzeja, P.P.2    Faustino, R.S.3    Terzic, A.4
  • 31
    • 84872831805 scopus 로고    scopus 로고
    • Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system
    • Chung, H.S., Wang, S.B., Venkatraman, V., Murray, C.I. & Van Eyk, J.E. 2013. Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system. Circ Res 112, 382–392.
    • (2013) Circ Res , vol.112 , pp. 382-392
    • Chung, H.S.1    Wang, S.B.2    Venkatraman, V.3    Murray, C.I.4    Van Eyk, J.E.5
  • 32
    • 68249126139 scopus 로고    scopus 로고
    • The published 3D structure of the VDAC channel: native or not?
    • Colombini, M. 2009. The published 3D structure of the VDAC channel: native or not? Trends Biochem Sci 34, 382–389.
    • (2009) Trends Biochem Sci , vol.34 , pp. 382-389
    • Colombini, M.1
  • 33
    • 67149129940 scopus 로고    scopus 로고
    • Control and regulation of integrated mitochondrial function in metabolic and transport networks
    • Cortassa, S., O'Rourke, B., Winslow, R.L. & Aon, M.A. 2009. Control and regulation of integrated mitochondrial function in metabolic and transport networks. Int J Mol Sci 10, 1500–1513.
    • (2009) Int J Mol Sci , vol.10 , pp. 1500-1513
    • Cortassa, S.1    O'Rourke, B.2    Winslow, R.L.3    Aon, M.A.4
  • 38
    • 84871762432 scopus 로고    scopus 로고
    • Mitochondrial dynamics in heart disease
    • Dorn, G.W. II 2013. Mitochondrial dynamics in heart disease. Biochim Biophys Acta 1833, 233–241.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 233-241
    • Dorn, G.W.1
  • 39
    • 0033804351 scopus 로고    scopus 로고
    • Metabolic control of contractile performance in isolated perfused rat heart. Analysis of experimental data by reaction:diffusion mathematical model
    • Dos Santos, P., Aliev, M.K., Diolez, P., Duclos, F., Besse, P., Bonoron-Adèle, S., Sikk, P., Canioni, P. & Saks, V.A. 2000. Metabolic control of contractile performance in isolated perfused rat heart. Analysis of experimental data by reaction:diffusion mathematical model. J Mol Cell Cardiol 32, 1703–1734.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 1703-1734
    • Dos Santos, P.1    Aliev, M.K.2    Diolez, P.3    Duclos, F.4    Besse, P.5    Bonoron-Adèle, S.6    Sikk, P.7    Canioni, P.8    Saks, V.A.9
  • 40
    • 0038037716 scopus 로고    scopus 로고
    • Phosphotransfer networks and cellular energetics
    • Dzeja, P.P. & Terzic, A. 2003. Phosphotransfer networks and cellular energetics. J Exp Biol 206, 2039–2047.
    • (2003) J Exp Biol , vol.206 , pp. 2039-2047
    • Dzeja, P.P.1    Terzic, A.2
  • 41
    • 0031680034 scopus 로고    scopus 로고
    • Adenylate kinase: kinetic behavior in intact cells indicates it is integral to multiple cellular processes
    • Dzeja, P.P., Zeleznikar, R.J. & Goldberg, N.D. 1998. Adenylate kinase: kinetic behavior in intact cells indicates it is integral to multiple cellular processes. Mol Cell Biochem 184, 169–182.
    • (1998) Mol Cell Biochem , vol.184 , pp. 169-182
    • Dzeja, P.P.1    Zeleznikar, R.J.2    Goldberg, N.D.3
  • 42
    • 0842323771 scopus 로고    scopus 로고
    • Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice
    • Dzeja, P.P., Terzic, A. & Wieringa, B. 2004. Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice. Mol Cell Biochem 256–257, 13–27.
    • (2004) Mol Cell Biochem , vol.256-257 , pp. 13-27
    • Dzeja, P.P.1    Terzic, A.2    Wieringa, B.3
  • 43
    • 79955689542 scopus 로고    scopus 로고
    • Developmental enhancement of adenylate kinase-AMPK metabolic signaling axis supports stem cell cardiac differentiation
    • Dzeja, P.P., Chung, S., Faustino, R.S., Behfar, A. & Terzic, A. 2011a. Developmental enhancement of adenylate kinase-AMPK metabolic signaling axis supports stem cell cardiac differentiation. PLoS One 6, e19300.
    • (2011) PLoS One , vol.6
    • Dzeja, P.P.1    Chung, S.2    Faustino, R.S.3    Behfar, A.4    Terzic, A.5
  • 44
    • 80054978355 scopus 로고    scopus 로고
    • Rearrangement of energetic and substrate utilization networks compensate for chronic myocardial creatine kinase deficiency
    • Dzeja, P.P., Hoyer, K., Tian, R., Zhang, S., Nemutlu, E., Spindler, M. & Ingwall, J.S. 2011b. Rearrangement of energetic and substrate utilization networks compensate for chronic myocardial creatine kinase deficiency. J Physiol 589, 5193–5211.
    • (2011) J Physiol , vol.589 , pp. 5193-5211
    • Dzeja, P.P.1    Hoyer, K.2    Tian, R.3    Zhang, S.4    Nemutlu, E.5    Spindler, M.6    Ingwall, J.S.7
  • 45
    • 0029099344 scopus 로고
    • Cytoplasmic cellular structures control permeability of outer mitochondrial membrane for ADP and oxidative phosphorylation in rat liver cells
    • Fontaine, E.M., Keriel, C., Lantuejoul, S., Rigoulet, M., Leverve, X.M. & Saks, V.A. 1995. Cytoplasmic cellular structures control permeability of outer mitochondrial membrane for ADP and oxidative phosphorylation in rat liver cells. Biochem Biophys Res Commun 213, 138–146.
    • (1995) Biochem Biophys Res Commun , vol.213 , pp. 138-146
    • Fontaine, E.M.1    Keriel, C.2    Lantuejoul, S.3    Rigoulet, M.4    Leverve, X.M.5    Saks, V.A.6
  • 46
    • 79959824208 scopus 로고    scopus 로고
    • Standard magnetic resonance-based measurements of the Pi→ATP rate do not index the rate of oxidative phosphorylation in cardiac and skeletal muscles
    • From, A.H.L. & Ugurbil, K. 2011. Standard magnetic resonance-based measurements of the Pi→ATP rate do not index the rate of oxidative phosphorylation in cardiac and skeletal muscles. Am J Physiol Cell Physiol, 301, C1–11.
    • (2011) Am J Physiol Cell Physiol , vol.301 , pp. C1-11
    • From, A.H.L.1    Ugurbil, K.2
  • 47
    • 33745698398 scopus 로고    scopus 로고
    • Titin/connectin-based modulation of the Frank-Starling mechanism of the heart
    • Fukuda, N. & Granzier, H.L. 2005. Titin/connectin-based modulation of the Frank-Starling mechanism of the heart. J Muscle Res Cell Motil 26, 319–323.
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 319-323
    • Fukuda, N.1    Granzier, H.L.2
  • 48
    • 0034614288 scopus 로고    scopus 로고
    • Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle
    • Fukuda, N., Kajiwara, H., Ishiwata, S. & Kurihara, S. 2000. Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle. Circ Res 86, E1–E6.
    • (2000) Circ Res , vol.86 , pp. E1-E6
    • Fukuda, N.1    Kajiwara, H.2    Ishiwata, S.3    Kurihara, S.4
  • 49
    • 84879676359 scopus 로고    scopus 로고
    • Dissipation, generalized free energy, and a self-consistent nonequilibrium thermodynamics of chemically driven open subsystems
    • Ge, H. & Qian, H. 2013. Dissipation, generalized free energy, and a self-consistent nonequilibrium thermodynamics of chemically driven open subsystems. Phys Rev E Stat Nonlin Soft Matter Phys 87, 062125.
    • (2013) Phys Rev E Stat Nonlin Soft Matter Phys , vol.87 , pp. 062125
    • Ge, H.1    Qian, H.2
  • 50
    • 0020402772 scopus 로고
    • Control of heart mitochondrial oxygen consumption by creatine kinase: the importance of enzyme localization
    • Gellerich, F. & Saks, V.A. 1982. Control of heart mitochondrial oxygen consumption by creatine kinase: the importance of enzyme localization. Biochem Biophys Res Commun 105, 1473–1481.
    • (1982) Biochem Biophys Res Commun , vol.105 , pp. 1473-1481
    • Gellerich, F.1    Saks, V.A.2
  • 51
    • 84859560882 scopus 로고    scopus 로고
    • Role of mitochondrial Ca2+ in the regulation of cellular energetics
    • Glancy, B. & Balaban, R.S. 2012. Role of mitochondrial Ca2+ in the regulation of cellular energetics. Biochemistry 51, 2959–2973.
    • (2012) Biochemistry , vol.51 , pp. 2959-2973
    • Glancy, B.1    Balaban, R.S.2
  • 52
    • 0001877146 scopus 로고
    • An allosteric enzyme model with positive feedback applied to glycolytic oscillations
    • Goldbeter, A. & Nicolis, G. 1976. An allosteric enzyme model with positive feedback applied to glycolytic oscillations. Progr Theor Biol 4, 65–160.
    • (1976) Progr Theor Biol , vol.4 , pp. 65-160
    • Goldbeter, A.1    Nicolis, G.2
  • 54
    • 0033622118 scopus 로고    scopus 로고
    • In vivo 31P-NMR Spectroscopy of ATP and Phosphocreatine in Rat Skeletal Muscle
    • de Graaf, R.A., Van Kranenburg, A. & Nicolay, K. 2000. In vivo 31P-NMR Spectroscopy of ATP and Phosphocreatine in Rat Skeletal Muscle. Biophys J 78, 1657–1664.
    • (2000) Biophys J , vol.78 , pp. 1657-1664
    • de Graaf, R.A.1    Van Kranenburg, A.2    Nicolay, K.3
  • 55
    • 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., Brückner, A., Puurand, U., Kadaja, L., Käämbre, T., Seppet, E. & Saks, V. 2010. Study of possible interactions of tubulin, microtubular network, and STOP protein with mitochondria in muscle cells. Mol Cell Biochem 337, 239–249.
    • (2010) Mol Cell Biochem , vol.337 , pp. 239-249
    • Guerrero, K.1    Monge, C.2    Brückner, A.3    Puurand, U.4    Kadaja, L.5    Käämbre, T.6    Seppet, E.7    Saks, V.8
  • 56
    • 68649108571 scopus 로고    scopus 로고
    • Characteristics and possible functions of mitochondrial Ca(2+) transport mechanisms
    • Gunter, T.E. & Sheu, S.-S. 2009. Characteristics and possible functions of mitochondrial Ca(2+) transport mechanisms. Biochim Biophys Acta 1787, 1291–1308.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1291-1308
    • Gunter, T.E.1    Sheu, S.-S.2
  • 57
    • 84885084776 scopus 로고    scopus 로고
    • Creatine kinase-overexpression improves myocardial energetics, contractile dysfunction and survival in murine Doxorubicin cardiotoxicity
    • Gupta, A., Rohlfsen, C., Leppo, M.K., Chacko, V.P., Wang, Y., Steenbergen, C. & Weiss, R.G. 2013. Creatine kinase-overexpression improves myocardial energetics, contractile dysfunction and survival in murine Doxorubicin cardiotoxicity. PLoS One 8, e74675.
    • (2013) PLoS One , vol.8
    • Gupta, A.1    Rohlfsen, C.2    Leppo, M.K.3    Chacko, V.P.4    Wang, Y.5    Steenbergen, C.6    Weiss, R.G.7
  • 58
    • 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. 2010. 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 11, 982–1019.
    • (2010) Int J Mol Sci , vol.11 , pp. 982-1019
    • Guzun, R.1    Saks, V.2
  • 59
    • 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., Kuznetsov, A.V., Pison, C. & Saks, V. 2009. Regulation of respiration controlled by mitochondrial creatine kinase in permeabilized cardiac cells in situ. Importance of system level properties. Biochim Biophys Acta 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    Kuznetsov, A.V.7    Pison, C.8    Saks, V.9
  • 61
    • 0022790702 scopus 로고
    • The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
    • Hackenbrock, C.R., Chazotte, B. & Gupte, S.S. 1986. The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport. J Bioenerg Biomembr 18, 331–368.
    • (1986) J Bioenerg Biomembr , vol.18 , pp. 331-368
    • Hackenbrock, C.R.1    Chazotte, B.2    Gupte, S.S.3
  • 62
    • 66849134930 scopus 로고    scopus 로고
    • Three-dimensional electron microscopy reveals new details of membrane systems for Ca2+ signaling in the heart
    • Hayashi, T., Martone, M.E., Yu, Z., Thor, A., Doi, M., Holst, M.J., Ellisman, M.H. & Hoshijima, M. 2009. Three-dimensional electron microscopy reveals new details of membrane systems for Ca2+ signaling in the heart. J Cell Sci 122, 1005–1013.
    • (2009) J Cell Sci , vol.122 , pp. 1005-1013
    • Hayashi, T.1    Martone, M.E.2    Yu, Z.3    Thor, A.4    Doi, M.5    Holst, M.J.6    Ellisman, M.H.7    Hoshijima, M.8
  • 63
    • 49649099046 scopus 로고    scopus 로고
    • In vivo magnetic resonance spectroscopy of transgenic mice with altered expression of guanidinoacetate methyl transferase and creatine kinase isoenzymes
    • In, G.S. Salomons, &, M. Wyss, (eds), Springer, Zurich, Switzerland
    • Heerschap, A., Kan, H.E., Nabuurs, C.I.H.C., Renema, W.K., Isbrandt, D. & Wieringa, B. 2007. In vivo magnetic resonance spectroscopy of transgenic mice with altered expression of guanidinoacetate methyl transferase and creatine kinase isoenzymes. In: G.S. Salomons & M. Wyss (eds) Creatine and Creatine Kinase in Health and Disease, pp. 119–148. Springer, Zurich, Switzerland.
    • (2007) Creatine and Creatine Kinase in Health and Disease , pp. 119-148
    • Heerschap, A.1    Kan, H.E.2    Nabuurs, C.I.H.C.3    Renema, W.K.4    Isbrandt, D.5    Wieringa, B.6
  • 65
    • 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. 2002. Cyclical changes in high-energy phosphates during the cardiac cycle by pacing-Gated 31P nuclear magnetic resonance. Circ J 66, 80–86.
    • (2002) Circ J , vol.66 , pp. 80-86
    • Honda, H.1    Tanaka, K.2    Akita, N.3    Haneda, T.4
  • 66
    • 0035834158 scopus 로고    scopus 로고
    • Chronic phosphocreatine depletion by the creatine analogue beta-guanidinopropionate is associated with increased mortality and loss of ATP in rats after myocardial infarction
    • Horn, M., Remkes, H., Strömer, H., Dienesch, C. & Neubauer, S. 2001. Chronic phosphocreatine depletion by the creatine analogue beta-guanidinopropionate is associated with increased mortality and loss of ATP in rats after myocardial infarction. Circulation 104, 1844–1849.
    • (2001) Circulation , vol.104 , pp. 1844-1849
    • Horn, M.1    Remkes, H.2    Strömer, H.3    Dienesch, C.4    Neubauer, S.5
  • 67
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang, X., Holden, H.M. & Raushel, F.M. 2001. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu Rev Biochem 70, 149–180.
    • (2001) Annu Rev Biochem , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.M.3
  • 69
    • 81855184470 scopus 로고    scopus 로고
    • Colchicine reduces postoperative atrial fibrillation: results of the Colchicine for the Prevention of the Postpericardiotomy Syndrome (COPPS) atrial fibrillation substudy
    • Imazio, M., Brucato, A., Ferrazzi, P., Rovere, M.E., Gandino, A., Cemin, R., Ferrua, S., Belli, R., Maestroni, S., Simon, C. et al. 2011. Colchicine reduces postoperative atrial fibrillation: results of the Colchicine for the Prevention of the Postpericardiotomy Syndrome (COPPS) atrial fibrillation substudy. Circulation 124, 2290–2295.
    • (2011) Circulation , vol.124 , pp. 2290-2295
    • Imazio, M.1    Brucato, A.2    Ferrazzi, P.3    Rovere, M.E.4    Gandino, A.5    Cemin, R.6    Ferrua, S.7    Belli, R.8    Maestroni, S.9    Simon, C.10
  • 70
    • 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. 2006. On the hypothesis that the failing heart is energy starved: lessons learned from the metabolism of ATP and creatine. Curr Hypertens Rep 8, 457–464.
    • (2006) Curr Hypertens Rep , vol.8 , pp. 457-464
    • Ingwall, J.S.1
  • 71
    • 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. 2004. Is the failing heart energy starved? On using chemical energy to support cardiac function. Circ Res 95, 135–145.
    • (2004) Circ Res , vol.95 , pp. 135-145
    • Ingwall, J.S.1    Weiss, R.G.2
  • 72
    • 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. 1982. Creatine kinase of heart mitochondria: changes in its kinetic properties induced by coupling to oxidative phosphorylation. Arch Biochem Biophys 219, 167–178.
    • (1982) Arch Biochem Biophys , vol.219 , pp. 167-178
    • Jacobus, W.E.1    Saks, V.A.2
  • 74
    • 0035920253 scopus 로고    scopus 로고
    • Energetic crosstalk between organelles: architectural integration of energy production and utilization
    • Kaasik, A., Veksler, V., Boehm, E., Novotova, M., Minajeva, A. & Ventura-Clapier, R. 2001. Energetic crosstalk between organelles: architectural integration of energy production and utilization. Circ Res 89, 153–159.
    • (2001) Circ Res , vol.89 , pp. 153-159
    • Kaasik, A.1    Veksler, V.2    Boehm, E.3    Novotova, M.4    Minajeva, A.5    Ventura-Clapier, R.6
  • 75
    • 6444239258 scopus 로고    scopus 로고
    • Phosphorylated guanidinoacetate partly compensates for the lack of phosphocreatine in skeletal muscle of mice lacking guanidinoacetate methyltransferase
    • Kan, H.E., Renema, W.K.J., Isbrandt, D. & Heerschap, A. 2004. Phosphorylated guanidinoacetate partly compensates for the lack of phosphocreatine in skeletal muscle of mice lacking guanidinoacetate methyltransferase. J Physiol 560, 219–229.
    • (2004) J Physiol , vol.560 , pp. 219-229
    • Kan, H.E.1    Renema, W.K.J.2    Isbrandt, D.3    Heerschap, A.4
  • 76
    • 0012679726 scopus 로고
    • Structure of the heart and cardiac muscle
    • In, Raven Press, New York
    • Katz, A.M. 1992. Structure of the heart and cardiac muscle. In: Physiology of the Heart, pp. 1–36. Raven Press, New York.
    • (1992) Physiology of the Heart , pp. 1-36
    • Katz, A.M.1
  • 77
    • 84872806941 scopus 로고    scopus 로고
    • Integrating mitochondrial energetics, redox and ROS metabolic networks: a two-compartment model
    • Kembro, J.M., Aon, M.A., Winslow, R.L., O'Rourke, B. & Cortassa, S. 2013. Integrating mitochondrial energetics, redox and ROS metabolic networks: a two-compartment model. Biophys J 104, 332–343.
    • (2013) Biophys J , vol.104 , pp. 332-343
    • Kembro, J.M.1    Aon, M.A.2    Winslow, R.L.3    O'Rourke, B.4    Cortassa, S.5
  • 78
    • 84864389207 scopus 로고    scopus 로고
    • What do magnetic resonance-based measurements of Pi→ATP flux tell us about skeletal muscle metabolism?
    • Kemp, G.J. & Brindle, K.M. 2012. What do magnetic resonance-based measurements of Pi→ATP flux tell us about skeletal muscle metabolism? Diabetes 61, 1927–1934.
    • (2012) Diabetes , vol.61 , pp. 1927-1934
    • Kemp, G.J.1    Brindle, K.M.2
  • 79
    • 0027456261 scopus 로고
    • Metabolic channelling and control of the flux
    • Kholodenko, B.N. & Westerhoff, H.V. 1993. Metabolic channelling and control of the flux. FEBS Lett 320, 71–74.
    • (1993) FEBS Lett , vol.320 , pp. 71-74
    • Kholodenko, B.N.1    Westerhoff, H.V.2
  • 80
    • 0032483521 scopus 로고    scopus 로고
    • Octamer formation and coupling of cardiac sarcomeric mitochondrial creatine kinase are mediated by charged N-terminal residues
    • Khuchua, Z.A., Qin, W., Boero, J., Cheng, J., Payne, R.M., Saks, V.A. & Strauss, A.W. 1998. Octamer formation and coupling of cardiac sarcomeric mitochondrial creatine kinase are mediated by charged N-terminal residues. J Biol Chem 273, 22990–22996.
    • (1998) J Biol Chem , vol.273 , pp. 22990-22996
    • Khuchua, Z.A.1    Qin, W.2    Boero, J.3    Cheng, J.4    Payne, R.M.5    Saks, V.A.6    Strauss, A.W.7
  • 81
    • 0034494381 scopus 로고    scopus 로고
    • Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ
    • Kraft, T., Hornemann, T., Stolz, M., Nier, V. & Wallimann, T. 2000. Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ. J Muscle Res Cell Motil 21, 691–703.
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 691-703
    • Kraft, T.1    Hornemann, T.2    Stolz, M.3    Nier, V.4    Wallimann, T.5
  • 84
    • 84859763834 scopus 로고    scopus 로고
    • Regulation of mitochondrial function by voltage dependent anion channels in ethanol metabolism and the Warburg effect
    • Lemasters, J.J., Holmuhamedov, E.L., Czerny, C., Zhong, Z. & Maldonado, E.N. 2012. Regulation of mitochondrial function by voltage dependent anion channels in ethanol metabolism and the Warburg effect. Biochim Biophys Acta 1818, 1536–1544.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1536-1544
    • Lemasters, J.J.1    Holmuhamedov, E.L.2    Czerny, C.3    Zhong, Z.4    Maldonado, E.N.5
  • 85
    • 17044455914 scopus 로고    scopus 로고
    • Inborn errors of creatine metabolism and epilepsy: clinical features, diagnosis, and treatment
    • Leuzzi, V. 2002. Inborn errors of creatine metabolism and epilepsy: clinical features, diagnosis, and treatment. J Child Neurol 17(Suppl 3), 3S89–3S97.
    • (2002) J Child Neurol , vol.17 , pp. 3S89-3S97
    • Leuzzi, V.1
  • 86
    • 0024456931 scopus 로고
    • Studies on the interaction between mitochondria and the cytoskeleton
    • Lindén, M., Nelson, B.D., Loncar, D. & Leterrier, J.F. 1989. Studies on the interaction between mitochondria and the cytoskeleton. J Bioenerg Biomembr 21, 507–518.
    • (1989) J Bioenerg Biomembr , vol.21 , pp. 507-518
    • Lindén, M.1    Nelson, B.D.2    Loncar, D.3    Leterrier, J.F.4
  • 87
    • 67650688732 scopus 로고    scopus 로고
    • Regulation of mitochondrial Ca2+ and its effects on energetics and redox balance in normal and failing heart
    • Liu, T. & O'Rourke, B. 2009. Regulation of mitochondrial Ca2+ and its effects on energetics and redox balance in normal and failing heart. J Bioenerg Biomembr 41, 127–132.
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 127-132
    • Liu, T.1    O'Rourke, B.2
  • 88
    • 77955980416 scopus 로고    scopus 로고
    • Energy metabolic phenotype of the cardiomyocyte during development, differentiation, and postnatal maturation
    • Lopaschuk, G.D. & Jaswal, J.S. 2010. Energy metabolic phenotype of the cardiomyocyte during development, differentiation, and postnatal maturation. J Cardiovasc Pharmacol 56, 130–140.
    • (2010) J Cardiovasc Pharmacol , vol.56 , pp. 130-140
    • Lopaschuk, G.D.1    Jaswal, J.S.2
  • 90
    • 34548050205 scopus 로고    scopus 로고
    • Excitation-contraction coupling and mitochondrial energetics
    • Maack, C. & O'Rourke, B. 2007. Excitation-contraction coupling and mitochondrial energetics. Basic Res Cardiol 102, 369–392.
    • (2007) Basic Res Cardiol , vol.102 , pp. 369-392
    • Maack, C.1    O'Rourke, B.2
  • 91
    • 0030046478 scopus 로고    scopus 로고
    • Traveling NADH and proton waves during oscillatory glycolysis in vitro
    • Mair, T. & Müller, S.C. 1996. Traveling NADH and proton waves during oscillatory glycolysis in vitro. J Biol Chem 271, 627–630.
    • (1996) J Biol Chem , vol.271 , pp. 627-630
    • Mair, T.1    Müller, S.C.2
  • 92
    • 78650332649 scopus 로고    scopus 로고
    • Free tubulin modulates mitochondrial membrane potential in cancer cells
    • Maldonado, E.N., Patnaik, J., Mullins, M.R. & Lemasters, J.J. 2010. Free tubulin modulates mitochondrial membrane potential in cancer cells. Cancer Res 70, 10192–10201.
    • (2010) Cancer Res , vol.70 , pp. 10192-10201
    • Maldonado, E.N.1    Patnaik, J.2    Mullins, M.R.3    Lemasters, J.J.4
  • 93
    • 33745737928 scopus 로고    scopus 로고
    • Structure and dynamics of the mitochondrial inner membrane cristae
    • Mannella, C.A. 2006. Structure and dynamics of the mitochondrial inner membrane cristae. Biochim Biophys Acta 1763, 542–548.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 542-548
    • Mannella, C.A.1
  • 94
    • 33646172301 scopus 로고    scopus 로고
    • Mathematical modeling of mitochondrial adenine nucleotide translocase
    • Metelkin, E., Goryanin, I. & Demin, O. 2006. Mathematical modeling of mitochondrial adenine nucleotide translocase. Biophys J 90, 423–432.
    • (2006) Biophys J , vol.90 , pp. 423-432
    • Metelkin, E.1    Goryanin, I.2    Demin, O.3
  • 95
    • 0018391707 scopus 로고
    • The Ninth Sir Hans Krebs Lecture. Compartmentation and communication in living systems. Ligand conduction: a general catalytic principle in chemical, osmotic and chemiosmotic reaction systems
    • Mitchell, P. 1979. The Ninth Sir Hans Krebs Lecture. Compartmentation and communication in living systems. Ligand conduction: a general catalytic principle in chemical, osmotic and chemiosmotic reaction systems. FEBS J 95, 1–20.
    • (1979) FEBS J , vol.95 , pp. 1-20
    • Mitchell, P.1
  • 96
    • 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., Vendelin, M. & Saks, V.A. 2008. Regulation of respiration in brain mitochondria and synaptosomes: restrictions of ADP diffusion in situ, roles of tubulin, and mitochondrial creatine kinase. Mol Cell Biochem 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    Vendelin, M.7    Saks, V.A.8
  • 99
    • 78650054962 scopus 로고    scopus 로고
    • 31P saturation transfer spectroscopy predicts differential intracellular macromolecular association of ATP and ADP in skeletal muscle
    • Nabuurs, C., Huijbregts, B., Wieringa, B., Hilbers, C.W. & Heerschap, A. 2010. 31P saturation transfer spectroscopy predicts differential intracellular macromolecular association of ATP and ADP in skeletal muscle. J Biol Chem 285, 39588–39596.
    • (2010) J Biol Chem , vol.285 , pp. 39588-39596
    • Nabuurs, C.1    Huijbregts, B.2    Wieringa, B.3    Hilbers, C.W.4    Heerschap, A.5
  • 101
    • 84859531669 scopus 로고    scopus 로고
    • Dynamic phosphometabolomic profiling of human tissues and transgenic models by 18O-assisted ³¹P NMR and mass spectrometry
    • Nemutlu, E., Zhang, S., Gupta, A., Juranic, N.O., Macura, S.I., Terzic, A., Jahangir, A. & Dzeja, P. 2012. Dynamic phosphometabolomic profiling of human tissues and transgenic models by 18O-assisted ³¹P NMR and mass spectrometry. Physiol Genomics 44, 386–402.
    • (2012) Physiol Genomics , vol.44 , pp. 386-402
    • Nemutlu, E.1    Zhang, S.2    Gupta, A.3    Juranic, N.O.4    Macura, S.I.5    Terzic, A.6    Jahangir, A.7    Dzeja, P.8
  • 102
    • 33947239659 scopus 로고    scopus 로고
    • The failing heart–an engine out of fuel
    • Neubauer, S. 2007. The failing heart–an engine out of fuel. N Engl J Med 356, 1140–1151.
    • (2007) N Engl J Med , vol.356 , pp. 1140-1151
    • Neubauer, S.1
  • 104
    • 84872678868 scopus 로고    scopus 로고
    • Low-dose colchicine for secondary prevention of cardiovascular disease
    • Nidorf, S.M., Eikelboom, J.W., Budgeon, C.A. & Thompson, P.L. 2013. Low-dose colchicine for secondary prevention of cardiovascular disease. J Am Coll Cardiol 61, 404–410.
    • (2013) J Am Coll Cardiol , vol.61 , pp. 404-410
    • Nidorf, S.M.1    Eikelboom, J.W.2    Budgeon, C.A.3    Thompson, P.L.4
  • 105
    • 84891900055 scopus 로고    scopus 로고
    • Colchicine for secondary prevention of cardiovascular disease
    • Nidorf, S.M., Eikelboom, J.W. & Thompson, P.L. 2014. Colchicine for secondary prevention of cardiovascular disease. Curr Atheroscler Rep 16, 391.
    • (2014) Curr Atheroscler Rep , vol.16 , pp. 391
    • Nidorf, S.M.1    Eikelboom, J.W.2    Thompson, P.L.3
  • 106
    • 77952236126 scopus 로고    scopus 로고
    • Inhibiting mitochondrial fission protects the heart against ischemia/reperfusion injury
    • Ong, S.B., Subrayan, S., Lim, S.Y., Yellon, D.M., Davidson, S.M. & Hausenloy, D.J. 2010. Inhibiting mitochondrial fission protects the heart against ischemia/reperfusion injury. Circulation 121, 2012–2022.
    • (2010) Circulation , vol.121 , pp. 2012-2022
    • Ong, S.B.1    Subrayan, S.2    Lim, S.Y.3    Yellon, D.M.4    Davidson, S.M.5    Hausenloy, D.J.6
  • 108
    • 0242322432 scopus 로고    scopus 로고
    • Quantitative analysis of spontaneous mitochondrial depolarizations
    • O'Reilly, C.M., Fogarty, K.E., Drummond, R.M., Tuft, R.A. & Walsh, J.V. Jr 2003. Quantitative analysis of spontaneous mitochondrial depolarizations. Biophys J 85, 3350–3357.
    • (2003) Biophys J , vol.85 , pp. 3350-3357
    • O'Reilly, C.M.1    Fogarty, K.E.2    Drummond, R.M.3    Tuft, R.A.4    Walsh, J.V.5
  • 109
    • 26844554628 scopus 로고    scopus 로고
    • Mitochondrial ion channels: gatekeepers of life and death
    • O'Rourke, B., Cortassa, S. & Aon, M.A. 2005. Mitochondrial ion channels: gatekeepers of life and death. Physiology (Bethesda, MD), 20, 303–315.
    • (2005) Physiology (Bethesda, MD) , vol.20 , pp. 303-315
    • O'Rourke, B.1    Cortassa, S.2    Aon, M.A.3
  • 110
    • 84872253728 scopus 로고    scopus 로고
    • The effect of the creatine analogue beta-guanidinopropionic acid on energy metabolism: a systematic review
    • Oudman, I., Clark, J.F. & Brewster, L.M. 2013. The effect of the creatine analogue beta-guanidinopropionic acid on energy metabolism: a systematic review. PLoS One 8, e52879.
    • (2013) PLoS One , vol.8
    • Oudman, I.1    Clark, J.F.2    Brewster, L.M.3
  • 111
    • 0842345408 scopus 로고    scopus 로고
    • On the origin of intracellular compartmentation and organized metabolic systems
    • Ovádi, J. & Saks, V. 2004. On the origin of intracellular compartmentation and organized metabolic systems. Mol Cell Biochem 256–257, 5–12.
    • (2004) Mol Cell Biochem , vol.256-257 , pp. 5-12
    • Ovádi, J.1    Saks, V.2
  • 112
    • 0033991699 scopus 로고    scopus 로고
    • Macromolecular compartmentation and channeling
    • Ovádi, J. & Srere, P.A. 2000. Macromolecular compartmentation and channeling. Int Rev Cytol 192, 255–280.
    • (2000) Int Rev Cytol , vol.192 , pp. 255-280
    • Ovádi, J.1    Srere, P.A.2
  • 114
    • 44349158269 scopus 로고    scopus 로고
    • Progressive decrease of phosphocreatine, creatine and creatine kinase in skeletal muscle upon transformation to sarcoma
    • Patra, S., Bera, S., SinhaRoy, S., Ghoshal, S., Ray, S., Basu, A., Schlattner, U., Wallimann, T. & Ray, M. 2008. Progressive decrease of phosphocreatine, creatine and creatine kinase in skeletal muscle upon transformation to sarcoma. FEBS J 275, 3236–3247.
    • (2008) FEBS J , vol.275 , pp. 3236-3247
    • Patra, S.1    Bera, S.2    SinhaRoy, S.3    Ghoshal, S.4    Ray, S.5    Basu, A.6    Schlattner, U.7    Wallimann, T.8    Ray, M.9
  • 115
    • 38349121902 scopus 로고    scopus 로고
    • Transport ATPases into the year 2008: a brief overview related to types, structures, functions and roles in health and disease
    • Pedersen, P.L. 2007. Transport ATPases into the year 2008: a brief overview related to types, structures, functions and roles in health and disease. J Bioenerg Biomembr 39, 349–355.
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 349-355
    • Pedersen, P.L.1
  • 116
    • 84860521662 scopus 로고    scopus 로고
    • Regulation of oxidative phosphorylation complex activity: effects of tissue-specific metabolic stress within an allometric series and acute changes in workload
    • Phillips, D., Covian, R., Aponte, A.M., Glancy, B., Taylor, J.F., Chess, D. & Balaban, R.S. 2012. Regulation of oxidative phosphorylation complex activity: effects of tissue-specific metabolic stress within an allometric series and acute changes in workload. Am J Physiol Regul Integr Comp Physio 302, R1034–R1048.
    • (2012) Am J Physiol Regul Integr Comp Physio , vol.302 , pp. R1034-R1048
    • Phillips, D.1    Covian, R.2    Aponte, A.M.3    Glancy, B.4    Taylor, J.F.5    Chess, D.6    Balaban, R.S.7
  • 119
    • 0035977066 scopus 로고    scopus 로고
    • Cellular energetics in the preconditioned state: protective role for phosphotransfer reactions captured by 18O-assisted 31P NMR
    • Pucar, D., Dzeja, P.P., Bast, P., Juranic, N., Macura, S. & Terzic, A. 2001. Cellular energetics in the preconditioned state: protective role for phosphotransfer reactions captured by 18O-assisted 31P NMR. J Biol Chem 276, 44812–44819.
    • (2001) J Biol Chem , vol.276 , pp. 44812-44819
    • Pucar, D.1    Dzeja, P.P.2    Bast, P.3    Juranic, N.4    Macura, S.5    Terzic, A.6
  • 120
    • 33748096830 scopus 로고    scopus 로고
    • Open-system nonequilibrium steady state: statistical thermodynamics, fluctuations, and chemical oscillations
    • Qian, H. 2006. Open-system nonequilibrium steady state: statistical thermodynamics, fluctuations, and chemical oscillations. J Phys Chem B 110, 15063–15074.
    • (2006) J Phys Chem B , vol.110 , pp. 15063-15074
    • Qian, H.1
  • 121
    • 33644847375 scopus 로고    scopus 로고
    • Microdomains of intracellular Ca2+: molecular determinants and functional consequences
    • Rizzuto, R. & Pozzan, T. 2006. Microdomains of intracellular Ca2+: molecular determinants and functional consequences. Physiol Rev 86, 369–408.
    • (2006) Physiol Rev , vol.86 , pp. 369-408
    • Rizzuto, R.1    Pozzan, T.2
  • 122
    • 84859763173 scopus 로고    scopus 로고
    • Control of mitochondrial outer membrane permeability: VDAC regulation by dimeric tubulin and cytosolic proteins
    • In, O.L. Svensson, (ed.), Nova Biomedical Books, New York
    • Rostovtseva, T.K. 2010. Control of mitochondrial outer membrane permeability: VDAC regulation by dimeric tubulin and cytosolic proteins. In: O.L. Svensson (ed.) Mitochondria: Structure, Functions and Dysfunctions, pp. 607–634. Nova Biomedical Books, New York.
    • (2010) Mitochondria: Structure, Functions and Dysfunctions , pp. 607-634
    • Rostovtseva, T.K.1
  • 124
    • 84895342780 scopus 로고    scopus 로고
    • Evolution and coevolution of tubulin's carboxy-terminal tails and mitochondria
    • In, O.L. Svensson, (ed.), Nova Biomedical Books, New York
    • Sackett, D. 2010. Evolution and coevolution of tubulin's carboxy-terminal tails and mitochondria. In: O.L. Svensson (ed.) Mitochondria: Structure, Function and Dysfunction, pp. 789–810. Nova Biomedical Books, New York.
    • (2010) Mitochondria: Structure, Function and Dysfunction , pp. 789-810
    • Sackett, D.1
  • 125
    • 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. 1990. Associations between beta-tubulin and mitochondria in adult isolated heart myocytes as shown by immunofluorescence and immunoelectron microscopy. Histochemistry 95, 1–10.
    • (1990) Histochemistry , vol.95 , pp. 1-10
    • Saetersdal, T.1    Greve, G.2    Dalen, H.3
  • 127
    • 0021860981 scopus 로고
    • Creatine kinase of rat heart mitochondria. The demonstration of functional coupling to oxidative phosphorylation in an inner membrane-matrix preparation
    • Saks, V.A., Kuznetsov, A.V., Kupriyanov, V.V., Miceli, M.V. & Jacobus, W.E. 1985. Creatine kinase of rat heart mitochondria. The demonstration of functional coupling to oxidative phosphorylation in an inner membrane-matrix preparation. J Biol Chem 260, 7757–7764.
    • (1985) J Biol Chem , vol.260 , pp. 7757-7764
    • Saks, V.A.1    Kuznetsov, A.V.2    Kupriyanov, V.V.3    Miceli, M.V.4    Jacobus, W.E.5
  • 128
    • 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. 1994. 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 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.4    Kuznetsov, A.V.5
  • 129
    • 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. & Tiivel, T. 1995. 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 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    Tiivel, T.7
  • 130
    • 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. 1996. Metabolic control and metabolic capacity: two aspects of creatine kinase functioning in the cells. Biochim Biophys Acta 1274, 81–88.
    • (1996) Biochim Biophys Acta , vol.1274 , pp. 81-88
    • Saks, V.A.1    Ventura-Clapier, R.2    Aliev, M.K.3
  • 131
    • 7344229928 scopus 로고    scopus 로고
    • Quantitative studies of enzyme-substrate compartmentation, functional coupling and metabolic channelling in muscle cells
    • Saks, V., Dos Santos, P., Gellerich, F.N. & Diolez, P. 1998. Quantitative studies of enzyme-substrate compartmentation, functional coupling and metabolic channelling in muscle cells. Mol Cell Biochem 184, 291–307.
    • (1998) Mol Cell Biochem , vol.184 , pp. 291-307
    • Saks, V.1    Dos Santos, P.2    Gellerich, F.N.3    Diolez, P.4
  • 134
    • 33645897315 scopus 로고    scopus 로고
    • Cardiac system bioenergetics: metabolic basis of the Frank-Starling law
    • Saks, V., Dzeja, P., Schlattner, U., Vendelin, M., Terzic, A. & Wallimann, T. 2006a. Cardiac system bioenergetics: metabolic basis of the Frank-Starling law. J Physiol 571, 253–273.
    • (2006) J Physiol , vol.571 , pp. 253-273
    • Saks, V.1    Dzeja, P.2    Schlattner, U.3    Vendelin, M.4    Terzic, A.5    Wallimann, T.6
  • 135
    • 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. 2006b. Molecular system bioenergetics: regulation of substrate supply in response to heart energy demands. J Physiol 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
  • 136
    • 44649177173 scopus 로고    scopus 로고
    • The creatine kinase isoenzymes in organized metabolic networks and regulation of cellular respiration: a new role for Maxwell's demon
    • In, C. Vial, (ed.), Nova Science Publisher, New York
    • Saks, V., Guerrero, K., Vendelin, M., Engelbrecht, J. & Seppet, E. 2006c. The creatine kinase isoenzymes in organized metabolic networks and regulation of cellular respiration: a new role for Maxwell's demon. In: C. Vial (ed.) Creatine Kinase, pp. 223–267. Nova Science Publisher, New York.
    • (2006) Creatine Kinase , pp. 223-267
    • Saks, V.1    Guerrero, K.2    Vendelin, M.3    Engelbrecht, J.4    Seppet, E.5
  • 137
    • 84900949800 scopus 로고    scopus 로고
    • Mechanisms and modeling of energy transfer between intracellular compartments
    • In, G.E. Gibson, &, G.A. Dienel, (ed.), 3rd edn, Springer Science+Business Media, LLC
    • Saks, V., Vendelin, M., Aliev, M.K., Kekelidze, T. & Engelbrecht, J. 2007a. Mechanisms and modeling of energy transfer between intracellular compartments. In: G.E. Gibson & G.A. Dienel (ed.) Handbook of Neurochemistry and Molecular Neurobiology, 3rd edn, pp. 815–560. Springer Science+Business Media, LLC.
    • (2007) Handbook of Neurochemistry and Molecular Neurobiology , pp. 560-815
    • Saks, V.1    Vendelin, M.2    Aliev, M.K.3    Kekelidze, T.4    Engelbrecht, J.5
  • 138
    • 84889354603 scopus 로고    scopus 로고
    • Integrated and organized cellular energetic systems: theories of cell energetics, compartmentation and metabolic channeling
    • In, V.A. Saks, (ed.), Wiley-VCH, Weinheim, Germany
    • Saks, V.A., Monge, C., Anmann, T. & Dzeja, P.P. 2007b. Integrated and organized cellular energetic systems: theories of cell energetics, compartmentation and metabolic channeling. In: V.A. Saks (ed.) Molecular System Bioenergetics. Energy for Life, pp. 59–109. Wiley-VCH, Weinheim, Germany.
    • (2007) Molecular System Bioenergetics. Energy for Life , pp. 59-109
    • Saks, V.A.1    Monge, C.2    Anmann, T.3    Dzeja, P.P.4
  • 139
    • 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. 2008. Metabolic compartmentation - a system level property of muscle cells: real problems of diffusion in living cells. Int J Mol Sci 9, 751–767.
    • (2008) Int J Mol Sci , vol.9 , pp. 751-767
    • Saks, V.1    Beraud, N.2    Wallimann, T.3
  • 140
    • 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. 2009. Philosophical basis and some historical aspects of systems biology: from Hegel to Noble - applications for bioenergetic research. Int J Mol Sci 10, 1161–1192.
    • (2009) Int J Mol Sci , vol.10 , pp. 1161-1192
    • Saks, V.1    Monge, C.2    Guzun, R.3
  • 143
    • 0032482127 scopus 로고    scopus 로고
    • Impaired cardiac energetics in mice lacking muscle-specific isoenzymes of creatine kinase
    • Saupe, K.W., Spindler, M., Tian, R. & Ingwall, J.S. 1998. Impaired cardiac energetics in mice lacking muscle-specific isoenzymes of creatine kinase. Circ Res 82, 898–907.
    • (1998) Circ Res , vol.82 , pp. 898-907
    • Saupe, K.W.1    Spindler, M.2    Tian, R.3    Ingwall, J.S.4
  • 144
    • 29344468308 scopus 로고    scopus 로고
    • Metabolite channeling: creatine kinase microcompartments
    • In, W.J. Lennarz, &, M.D. Lane, (eds), Academic Press, New York
    • Schlattner, U. & Wallimann, T. 2004. Metabolite channeling: creatine kinase microcompartments. In: W.J. Lennarz & M.D. Lane (eds) Encyclopedia of Biological Chemistry, pp. 646–651. Academic Press, New York.
    • (2004) Encyclopedia of Biological Chemistry , pp. 646-651
    • Schlattner, U.1    Wallimann, T.2
  • 148
    • 84880710379 scopus 로고    scopus 로고
    • Keeping mitochondria in shape: a matter of life and death
    • Scorrano, L. 2013. Keeping mitochondria in shape: a matter of life and death. Eur J Clin Invest 43, 886–893.
    • (2013) Eur J Clin Invest , vol.43 , pp. 886-893
    • Scorrano, L.1
  • 149
    • 0033014826 scopus 로고    scopus 로고
    • Examination of the transverse tubular system in living cardiac rat myocytes by 2-photon microscopy and digital image-processing techniques
    • Soeller, C. & Cannell, M.B. 1999. Examination of the transverse tubular system in living cardiac rat myocytes by 2-photon microscopy and digital image-processing techniques. Circ Res 84, 266–275.
    • (1999) Circ Res , vol.84 , pp. 266-275
    • Soeller, C.1    Cannell, M.B.2
  • 150
    • 64749099928 scopus 로고    scopus 로고
    • Three-dimensional high-resolution imaging of cardiac proteins to construct models of intracellular Ca2+ signalling in rat ventricular myocytes
    • Soeller, C., Jayasinghe, I.D., Li, P., Holden, A.V. & Cannell, M.B. 2009. Three-dimensional high-resolution imaging of cardiac proteins to construct models of intracellular Ca2+ signalling in rat ventricular myocytes. Exp Physiol 94, 496–508.
    • (2009) Exp Physiol , vol.94 , pp. 496-508
    • Soeller, C.1    Jayasinghe, I.D.2    Li, P.3    Holden, A.V.4    Cannell, M.B.5
  • 151
    • 0001249135 scopus 로고
    • The regulation of the energy output of the heart
    • Starling, E.H. & Visscher, M.B. 1927. The regulation of the energy output of the heart. J Physiol 62, 243–261.
    • (1927) J Physiol , vol.62 , pp. 243-261
    • Starling, E.H.1    Visscher, M.B.2
  • 152
    • 76349119210 scopus 로고    scopus 로고
    • Protein S-nitrosylation and cardioprotection
    • Sun, J. & Murphy, E. 2010. Protein S-nitrosylation and cardioprotection. Circ Res 106, 285–296.
    • (2010) Circ Res , vol.106 , pp. 285-296
    • Sun, J.1    Murphy, E.2
  • 153
    • 36348964192 scopus 로고    scopus 로고
    • Preconditioning Results in S-Nitrosylation of Proteins Involved in Regulation of Mitochondrial Energetics and Calcium Transport
    • Sun, J., Morgan, M., Chen, R.F., Steenbergen, C. & Murphy, E. 2007. Preconditioning Results in S-Nitrosylation of Proteins Involved in Regulation of Mitochondrial Energetics and Calcium Transport. Circ Res 101, 1155–1163.
    • (2007) Circ Res , vol.101 , pp. 1155-1163
    • Sun, J.1    Morgan, M.2    Chen, R.F.3    Steenbergen, C.4    Murphy, E.5
  • 154
    • 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, G.T. 1998. Cytoskeletal role in the transition from compensated to decompensated hypertrophy during adult canine left ventricular pressure overloading. Circ Res 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.T.6
  • 155
    • 81155139741 scopus 로고    scopus 로고
    • High efficiency of energy flux controls within mitochondrial interactosome in cardiac intracellular energetic units
    • Tepp, K., Shevchuk, I., Chekulayev, V., Timohhina, N., Kuznetsov, A.V., Guzun, R., Saks, V. & Kaambre, T. 2011. High efficiency of energy flux controls within mitochondrial interactosome in cardiac intracellular energetic units. Biochim Biophys Acta 1807, 1549–1561.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 1549-1561
    • Tepp, K.1    Shevchuk, I.2    Chekulayev, V.3    Timohhina, N.4    Kuznetsov, A.V.5    Guzun, R.6    Saks, V.7    Kaambre, T.8
  • 157
    • 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., Sikk, P., Kaambre, T., Sackett, D. & Saks, V. 2009. Direct measurement of energy fluxes from mitochondria into cytoplasm in permeabilized cardiac cells in situ: some evidence for Mitochondrial Interactosome. J Bioenerg Biomembr 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    Sikk, P.7    Kaambre, T.8    Sackett, D.9    Saks, V.10
  • 158
    • 0037182850 scopus 로고    scopus 로고
    • The nature and transport mechanism of hydrated hydroxide ions in aqueous solution
    • Tuckerman, M.E., Marx, D. & Parrinello, M. 2002. The nature and transport mechanism of hydrated hydroxide ions in aqueous solution. Nature 417, 925–929.
    • (2002) Nature , vol.417 , pp. 925-929
    • Tuckerman, M.E.1    Marx, D.2    Parrinello, M.3
  • 159
    • 0021819865 scopus 로고
    • Relative abilities of phosphagens with different thermodynamic or kinetic properties to help sustain ATP and total adenylate pools in heart during ischemia
    • Turner, D.M. & Walker, J.B. 1985. Relative abilities of phosphagens with different thermodynamic or kinetic properties to help sustain ATP and total adenylate pools in heart during ischemia. Arch Biochem Biophys 238, 642–651.
    • (1985) Arch Biochem Biophys , vol.238 , pp. 642-651
    • Turner, D.M.1    Walker, J.B.2
  • 161
    • 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. 2000. Regulation of mitochondrial respiration in heart cells analyzed by reaction-diffusion model of energy transfer. Am J Physiol Cell Physiol 278, C747–C764.
    • (2000) Am J Physiol Cell Physiol , vol.278 , pp. C747-C764
    • Vendelin, M.1    Kongas, O.2    Saks, V.3
  • 164
    • 0021947598 scopus 로고
    • Localization and function of M-line-bound creatine kinase. M-band model and creatine phosphate shuttle
    • Wallimann, T. & Eppenberger, H.M. 1985. Localization and function of M-line-bound creatine kinase. M-band model and creatine phosphate shuttle. Cell Muscle Motil 6, 239–285.
    • (1985) Cell Muscle Motil , vol.6 , pp. 239-285
    • Wallimann, T.1    Eppenberger, H.M.2
  • 165
    • 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. 1992. 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 281(Pt 1), 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
  • 167
    • 80052800016 scopus 로고    scopus 로고
    • The creatine kinase system and pleiotropic effects of creatine
    • Wallimann, T., Tokarska-Schlattner, M. & Schlattner, U. 2011. The creatine kinase system and pleiotropic effects of creatine. Amino Acids 40, 1271–1296.
    • (2011) Amino Acids , vol.40 , pp. 1271-1296
    • Wallimann, T.1    Tokarska-Schlattner, M.2    Schlattner, U.3
  • 169
    • 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. 2005. ATP flux through creatine kinase in the normal, stressed, and failing human heart. Proc Natl Acad Sci USA 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
  • 170
    • 0018336297 scopus 로고
    • Mitochondrial function in the heart
    • Williamson, J.R. 1979. Mitochondrial function in the heart. Annu Rev Physiol 41, 485–506.
    • (1979) Annu Rev Physiol , vol.41 , pp. 485-506
    • Williamson, J.R.1
  • 171
    • 0017071201 scopus 로고
    • Coordination of citric acid cycle activity with electron transport flux
    • Williamson, J.R., Ford, C., Illingworth, J. & Safer, B. 1976. Coordination of citric acid cycle activity with electron transport flux. Circ Res 38, I39–I51.
    • (1976) Circ Res , vol.38 , pp. I39-I51
    • Williamson, J.R.1    Ford, C.2    Illingworth, J.3    Safer, B.4
  • 172
    • 0028229723 scopus 로고
    • ADP inhibits the sliding velocity of fluorescent actin filaments on cardiac and skeletal myosins
    • Yamashita, H., Sata, M., Sugiura, S., Momomura, S., Serizawa, T. & Iizuka, M. 1994. ADP inhibits the sliding velocity of fluorescent actin filaments on cardiac and skeletal myosins. Circ Res 74, 1027–1033.
    • (1994) Circ Res , vol.74 , pp. 1027-1033
    • Yamashita, H.1    Sata, M.2    Sugiura, S.3    Momomura, S.4    Serizawa, T.5    Iizuka, M.6
  • 173
    • 0028930129 scopus 로고
    • Adenylate kinase-catalyzed phosphoryl transfer couples ATP utilization with its generation by glycolysis in intact muscle
    • Zeleznikar, R.J., Dzeja, P.P. & Goldberg, N.D. 1995. Adenylate kinase-catalyzed phosphoryl transfer couples ATP utilization with its generation by glycolysis in intact muscle. J Biol Chem 270, 7311–7319.
    • (1995) J Biol Chem , vol.270 , pp. 7311-7319
    • Zeleznikar, R.J.1    Dzeja, P.P.2    Goldberg, N.D.3


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