메뉴 건너뛰기




Volumn 1797, Issue 6-7, 2010, Pages 678-697

Structure-function relationships in feedback regulation of energy fluxes in vivo in health and disease: Mitochondrial Interactosome

Author keywords

Creatine kinase; Energy metabolism; Mitochondria; Permeabilized cell; Respiration; Systems biology; Tubulin

Indexed keywords

ADENINE NUCLEOTIDE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CALCIUM ION; CREATINE; CREATINE KINASE; CREATINE PHOSPHATE; CYTOSKELETON PROTEIN; HEXOKINASE; LACTIC ACID; MITOCHONDRIAL ENZYME; TUBULIN; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 77953811727     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.01.011     Document Type: Review
Times cited : (97)

References (204)
  • 1
    • 84889281594 scopus 로고    scopus 로고
    • Integration of adenylate kinase and glycolytic and glycogenolytic circuits in cellular energetics
    • Wiley-VCH, Weinheim, GmbH, Germany, V. Saks (Ed.)
    • Dzeja P., Chung S., Terzic A. Integration of adenylate kinase and glycolytic and glycogenolytic circuits in cellular energetics. Molecular System Bioenergetics. Energy for Life 2007, 195-264. Wiley-VCH, Weinheim, GmbH, Germany. V. Saks (Ed.).
    • (2007) Molecular System Bioenergetics. Energy for Life , pp. 195-264
    • Dzeja, P.1    Chung, S.2    Terzic, A.3
  • 2
    • 33751383273 scopus 로고    scopus 로고
    • Skeletal muscle energetics with PNMR: personal views and historic perspectives
    • Chance B., Im J., Nioka S., Kushmerick M. Skeletal muscle energetics with PNMR: personal views and historic perspectives. NMR Biomed. 2006, 19:904-926.
    • (2006) NMR Biomed. , vol.19 , pp. 904-926
    • Chance, B.1    Im, J.2    Nioka, S.3    Kushmerick, M.4
  • 3
    • 0026732710 scopus 로고
    • Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi
    • Kushmerick M.J., Moerland T.S., Wiseman R.W. Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:7521-7525.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 7521-7525
    • Kushmerick, M.J.1    Moerland, T.S.2    Wiseman, R.W.3
  • 5
    • 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
  • 6
    • 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
  • 11
    • 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
  • 12
    • 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. Energetic crosstalk between organelles: architectural integration of energy production and utilization. Circ. Res. 2001, 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
  • 16
    • 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
  • 17
    • 0036872241 scopus 로고    scopus 로고
    • Desmin cytoskeleton: a potential regulator of muscle mitochondrial behaviour and function
    • Capetenaki Y. Desmin cytoskeleton: a potential regulator of muscle mitochondrial behaviour and function. Trends Cardiovasc. Med. 2002, 12:339-348.
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 339-348
    • Capetenaki, Y.1
  • 20
    • 0034683573 scopus 로고    scopus 로고
    • Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function
    • Milner D.J., Mavroidis M., Weisleder N., Capetanaki Y. Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function. J. Cell Biol. 2000, 150:1283-1298.
    • (2000) J. Cell Biol. , vol.150 , pp. 1283-1298
    • Milner, D.J.1    Mavroidis, M.2    Weisleder, N.3    Capetanaki, Y.4
  • 21
    • 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
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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. 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    Saks, V.7
  • 28
    • 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
  • 29
    • 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
  • 30
    • 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
  • 33
    • 0033834262 scopus 로고    scopus 로고
    • A metabolic control analysis of kinetic controls in ATP free energy metabolism in contracting skeletal muscle
    • Jeneson J.A., Westerhoff H.V., Kushmerick M.J. A metabolic control analysis of kinetic controls in ATP free energy metabolism in contracting skeletal muscle. Am. J. Physiol. Cell Physiol. 2000, 279:C813-C832.
    • (2000) Am. J. Physiol. Cell Physiol. , vol.279
    • Jeneson, J.A.1    Westerhoff, H.V.2    Kushmerick, M.J.3
  • 34
    • 34548742394 scopus 로고    scopus 로고
    • Adenine nucleotide-creatine-phosphate module in myocardial metabolic system explains fast phase of dynamic regulation of oxidative phosphorylation
    • Van Beek J.H. Adenine nucleotide-creatine-phosphate module in myocardial metabolic system explains fast phase of dynamic regulation of oxidative phosphorylation. Am. J. Physiol. Cell Physiol. 2007, 293:C815-C829.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Van Beek, J.H.1
  • 35
    • 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
  • 36
    • 0011017415 scopus 로고    scopus 로고
    • Kluwer Academic Publishers, Dordrecht-Boston-London
    • Ingwall J.S. ATP and the Heart 2002, 1-244. Kluwer Academic Publishers, Dordrecht-Boston-London.
    • (2002) ATP and the Heart , pp. 1-244
    • Ingwall, J.S.1
  • 37
    • 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:I39-I51.
    • (1976) Circ. Res. , vol.38
    • Williamson, J.R.1    Ford, C.2    Illingworth, J.3    Safer, B.4
  • 38
    • 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
  • 40
    • 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
  • 42
    • 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(Pt 1):21-40.
    • (1992) Biochem. J. , vol.281 , Issue.PART 1 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 43
    • 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
  • 44
    • 67349244350 scopus 로고    scopus 로고
    • Domestication of the cardiac mitochondrion for energy conversion
    • Balaban R.S. Domestication of the cardiac mitochondrion for energy conversion. J. Mol. Cell. Cardiol. 2009, 46:832-841.
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 832-841
    • Balaban, R.S.1
  • 45
    • 44749088596 scopus 로고    scopus 로고
    • Mitochondrial Ca2+ and the heart
    • Dedkova E.N., Blatter L.A. Mitochondrial Ca2+ and the heart. Cell Calcium 2008, 44:77-91.
    • (2008) Cell Calcium , vol.44 , pp. 77-91
    • Dedkova, E.N.1    Blatter, L.A.2
  • 46
    • 67349155990 scopus 로고    scopus 로고
    • Morphological dynamics of mitochondria - a special emphasis on cardiac muscle cells
    • Hom J., Sheu S.S. Morphological dynamics of mitochondria - a special emphasis on cardiac muscle cells. J. Mol. Cell. Cardiol. 2009, 48:811-820.
    • (2009) J. Mol. Cell. Cardiol. , vol.48 , pp. 811-820
    • Hom, J.1    Sheu, S.S.2
  • 47
    • 48149106709 scopus 로고    scopus 로고
    • Physiological heart activation by adrenaline involves parallel activation of ATP usage and supply
    • Korzeniewski B., Deschodt-Arsac V., Calmettes G., Franconi J.M., Diolez P. Physiological heart activation by adrenaline involves parallel activation of ATP usage and supply. Biochem. J. 2008, 413:343-347.
    • (2008) Biochem. J. , vol.413 , pp. 343-347
    • Korzeniewski, B.1    Deschodt-Arsac, V.2    Calmettes, G.3    Franconi, J.M.4    Diolez, P.5
  • 48
    • 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, 41:1272-32.
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 1272-32
    • Liu, T.1    O'Rourke, B.2
  • 49
    • 0034959184 scopus 로고    scopus 로고
    • Simulation of cardiac work transitions, in vitro: effects of simultaneous Ca2+ and ATPase additions on isolated porcine heart mitochondria
    • Territo P.R., French S.A., Balaban R.S. Simulation of cardiac work transitions, in vitro: effects of simultaneous Ca2+ and ATPase additions on isolated porcine heart mitochondria. Cell Calcium 2001, 30:19-27.
    • (2001) Cell Calcium , vol.30 , pp. 19-27
    • Territo, P.R.1    French, S.A.2    Balaban, R.S.3
  • 50
    • 0035996962 scopus 로고    scopus 로고
    • Simultaneous measurements of mitochondrial NADH and Ca(2+) during increased work in intact rat heart trabeculae
    • Brandes R., Bers D.M. Simultaneous measurements of mitochondrial NADH and Ca(2+) during increased work in intact rat heart trabeculae. Biophys. J. 2002, 83:587-604.
    • (2002) Biophys. J. , vol.83 , pp. 587-604
    • Brandes, R.1    Bers, D.M.2
  • 53
    • 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
  • 55
    • 15544390385 scopus 로고    scopus 로고
    • Calcium, thin filaments, and the integrative biology of cardiac contractility
    • Kobayashi T., Solaro R.J. Calcium, thin filaments, and the integrative biology of cardiac contractility. Annu. Rev. Physiol. 2005, 67:39-67.
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 39-67
    • Kobayashi, T.1    Solaro, R.J.2
  • 56
    • 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
  • 60
    • 0024496705 scopus 로고
    • Relation between phosphate metabolites and oxygen consumption of heart in vivo
    • Katz L.A., Swain J.A., Portman M.A., Balaban R.S. Relation between phosphate metabolites and oxygen consumption of heart in vivo. Am. J. Physiol. 1989, 256:H265-H274.
    • (1989) Am. J. Physiol. , vol.256
    • Katz, L.A.1    Swain, J.A.2    Portman, M.A.3    Balaban, R.S.4
  • 61
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers D.M. Cardiac excitation-contraction coupling. Nature 2002, 415:198-205.
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 62
    • 0041534404 scopus 로고    scopus 로고
    • Ca(2+) signalling in mitochondria: mechanism and role in physiology and pathology
    • Brini M. Ca(2+) signalling in mitochondria: mechanism and role in physiology and pathology. Cell Calcium 2003, 34:399-405.
    • (2003) Cell Calcium , vol.34 , pp. 399-405
    • Brini, M.1
  • 63
    • 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
  • 64
    • 0038035753 scopus 로고    scopus 로고
    • The heart
    • Lippincott-Raven Publishers, Philadelphia
    • Opie L. The heart. Physiology, from Cell to Circulation 1998, 43-63. Lippincott-Raven Publishers, Philadelphia.
    • (1998) Physiology, from Cell to Circulation , pp. 43-63
    • Opie, L.1
  • 66
    • 41149109075 scopus 로고    scopus 로고
    • Prologue: mind over molecule: activating biological demons
    • Noble D. Prologue: mind over molecule: activating biological demons. Ann. N. Y. Acad. Sci. 2008, 1123:xi-xix.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1123
    • Noble, D.1
  • 67
    • 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
  • 68
    • 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
  • 69
    • 0842280576 scopus 로고    scopus 로고
    • Studies of mitochondrial respiration in muscle cells in situ: use and misuse of experimental evidence in mathematical modelling
    • Seppet E.K., Eimre M., Andrienko T., Kaambre T., Sikk P., Kuznetsov A.V., Saks V. Studies of mitochondrial respiration in muscle cells in situ: use and misuse of experimental evidence in mathematical modelling. Mol. Cell. Biochem. 2004, 256-257:219-227.
    • (2004) Mol. Cell. Biochem. , pp. 219-227
    • Seppet, E.K.1    Eimre, M.2    Andrienko, T.3    Kaambre, T.4    Sikk, P.5    Kuznetsov, A.V.6    Saks, V.7
  • 70
    • 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
  • 71
    • 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
  • 73
    • 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. 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    Kuznetsov, A.V.7    Pison, C.8    Saks, V.9
  • 75
    • 0015860346 scopus 로고
    • Creatine kinase of rat heart mitochondria. Coupling of creatine phosphorylation to electron transport
    • Jacobus W.E., Lehninger A.L. Creatine kinase of rat heart mitochondria. Coupling of creatine phosphorylation to electron transport. J. Biol. Chem. 1973, 248:4803-4810.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4803-4810
    • Jacobus, W.E.1    Lehninger, A.L.2
  • 76
    • 0016720206 scopus 로고
    • Studies of energy transport in heart cells. Mitochondrial isoenzyme of creatine phosphokinase: kinetic properties and regulatory action of Mg2+ ions
    • Saks V.A., Chernousova G.B., Gukovsky D.E., Smirnov V.N., Chazov E.I. Studies of energy transport in heart cells. Mitochondrial isoenzyme of creatine phosphokinase: kinetic properties and regulatory action of Mg2+ ions. Eur. J. Biochem. 1975, 57:273-290.
    • (1975) Eur. J. Biochem. , vol.57 , pp. 273-290
    • Saks, V.A.1    Chernousova, G.B.2    Gukovsky, D.E.3    Smirnov, V.N.4    Chazov, E.I.5
  • 77
    • 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
  • 78
    • 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
  • 79
    • 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
  • 80
    • 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
    • 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, vol. 5:815-860. Springer Science and Business Media, New York-Boston, USA.
    • (2007) Handbook of Neurochemistry and Molecular Neurobiology , vol.vol. 5 , pp. 815-860
    • Saks, V.A.1    Vendelin, M.2    Aliev, M.K.3    Kekelidze, T.4    Engelbrecht, J.5
  • 82
    • 0034962004 scopus 로고    scopus 로고
    • Effect of endurance training on oxidative and antioxidative function in human permeabilized muscle fibres
    • Walsh B., Tonkonogi M., Sahlin K. Effect of endurance training on oxidative and antioxidative function in human permeabilized muscle fibres. Pflugers Arch. 2001, 442:420-425.
    • (2001) Pflugers Arch. , vol.442 , pp. 420-425
    • Walsh, B.1    Tonkonogi, M.2    Sahlin, K.3
  • 85
    • 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., Braguer D. 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    Braguer, D.7
  • 86
    • 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
  • 88
    • 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. 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    Vendelin, M.7    Saks, V.A.8
  • 89
    • 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. 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    Sikk, P.7    Kaambre, T.8    Sackett, D.9    Saks, V.10
  • 90
    • 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., Wallimann T., Aliev M., Vendelin M. 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    Wallimann, T.7    Aliev, M.8    Vendelin, M.9
  • 91
    • 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. Transport ATPases into the year 2008: a brief overview related to types, structures, functions and roles in health and disease. J. Bioenerg. Biomembr. 2007, 39:349-355.
    • (2007) J. Bioenerg. Biomembr. , vol.39 , pp. 349-355
    • Pedersen, P.L.1
  • 92
    • 35448964610 scopus 로고    scopus 로고
    • Warburg, me and hexokinase 2: multiple discoveries of key molecular events underlying one of cancers' most common phenotypes, the "Warburg effect", i.e., elevated glycolysis in the presence of oxygen
    • Pedersen P.L. Warburg, me and hexokinase 2: multiple discoveries of key molecular events underlying one of cancers' most common phenotypes, the "Warburg effect", i.e., elevated glycolysis in the presence of oxygen. J. Bioenerg. Biomembr. 2007, 39:211-222.
    • (2007) J. Bioenerg. Biomembr. , vol.39 , pp. 211-222
    • Pedersen, P.L.1
  • 93
    • 0034532649 scopus 로고    scopus 로고
    • ATP synthases in the year 2000: evolving views about the structures of these remarkable enzyme complexes
    • Pedersen P.L., Ko Y.H., Hong S. ATP synthases in the year 2000: evolving views about the structures of these remarkable enzyme complexes. J. Bioenerg. Biomembr. 2000, 32:325-332.
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 325-332
    • Pedersen, P.L.1    Ko, Y.H.2    Hong, S.3
  • 94
    • 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
  • 95
    • 0030583580 scopus 로고    scopus 로고
    • Is there the creatine kinase equilibrium in working heart cells?
    • Saks V.A., Aliev M.K. Is there the creatine kinase equilibrium in working heart cells?. Biochem. Biophys. Res. Commun. 1996, 227:360-367.
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 360-367
    • Saks, V.A.1    Aliev, M.K.2
  • 97
    • 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
  • 98
    • 34247373746 scopus 로고    scopus 로고
    • Kinetics of integrated electron transfer in the mitochondrial respiratory chain: random collisions vs. solid state electron channeling
    • Lenaz G., Genova M.L. Kinetics of integrated electron transfer in the mitochondrial respiratory chain: random collisions vs. solid state electron channeling. Am. J. Physiol. Cell Physiol. 2007, 292:C1221-C1239.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Lenaz, G.1    Genova, M.L.2
  • 99
    • 56349087328 scopus 로고    scopus 로고
    • Supramolecular organization of protein complexes in the mitochondrial inner membrane
    • Vonck J., Schafer E. Supramolecular organization of protein complexes in the mitochondrial inner membrane. Biochim. Biophys. Acta 2009, 1793:117-124.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 117-124
    • Vonck, J.1    Schafer, E.2
  • 100
    • 0018391707 scopus 로고
    • Compartmentation and communication in living systems. Ligand conduction: a general catalytic principle in chemical, osmotic and chemiosmotic reaction systems.
    • Mitchell P. Compartmentation and communication in living systems. Ligand conduction: a general catalytic principle 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
  • 101
    • 24044554855 scopus 로고    scopus 로고
    • Foundations of vectorial metabolism and osmochemistry
    • discussion 434-385.
    • Mitchell P.D. Foundations of vectorial metabolism and osmochemistry. Biosci. Rep. 2004, 24:386-434. discussion 434-385.
    • (2004) Biosci. Rep. , vol.24 , pp. 386-434
    • Mitchell, P.D.1
  • 102
    • 0038037716 scopus 로고    scopus 로고
    • Phosphotransfer networks and cellular energetics
    • Dzeja P.P., Terzic A. Phosphotransfer networks and cellular energetics. J. Exp. Biol. 2003, 206:2039-2047.
    • (2003) J. Exp. Biol. , vol.206 , pp. 2039-2047
    • Dzeja, P.P.1    Terzic, A.2
  • 103
    • 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. Adenylate kinase-catalyzed phosphoryl transfer couples ATP utilization with its generation by glycolysis in intact muscle. J. Biol. Chem. 1995, 270:7311-7319.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7311-7319
    • Zeleznikar, R.J.1    Dzeja, P.P.2    Goldberg, N.D.3
  • 104
    • 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
  • 106
    • 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
  • 108
    • 67149104150 scopus 로고    scopus 로고
    • System analysis of cardiac energetics-excitation-contraction coupling: integration of mitochondrial respiration, phosphotransfer pathways, metabolic pacing and substrate supply in the heart
    • Wiley-VCH, Weinheim, GmbH, Germany, V. Saks (Ed.)
    • Saks V.A., Dzeja P., Guzun R., Aliev M.K., Vendelin M., Terzic A., Wallimann T. System analysis of cardiac energetics-excitation-contraction coupling: integration of mitochondrial respiration, phosphotransfer pathways, metabolic pacing and substrate supply in the heart. Molecular System Bioenergetics. Energy for Life 2007, 367-405. Wiley-VCH, Weinheim, GmbH, Germany. V. Saks (Ed.).
    • (2007) Molecular System Bioenergetics. Energy for Life , pp. 367-405
    • Saks, V.A.1    Dzeja, P.2    Guzun, R.3    Aliev, M.K.4    Vendelin, M.5    Terzic, A.6    Wallimann, T.7
  • 109
    • 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
  • 110
    • 58549102952 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiration by inorganic phosphate; comparing permeabilized muscle fibers and isolated mitochondria prepared from type-1 and type-2 rat skeletal muscle
    • Scheibye-Knudsen M., Quistorff B. Regulation of mitochondrial respiration by inorganic phosphate; comparing permeabilized muscle fibers and isolated mitochondria prepared from type-1 and type-2 rat skeletal muscle. Eur. J. Appl. Physiol. 2009, 105:279-287.
    • (2009) Eur. J. Appl. Physiol. , vol.105 , pp. 279-287
    • Scheibye-Knudsen, M.1    Quistorff, B.2
  • 111
    • 0141531999 scopus 로고    scopus 로고
    • Metabolic network control of oxidative phosphorylation: multiple roles of inorganic phosphate
    • Bose S., French S., Evans F.J., Joubert F., Balaban R.S. Metabolic network control of oxidative phosphorylation: multiple roles of inorganic phosphate. J. Biol. Chem. 2003, 278:39155-39165.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39155-39165
    • Bose, S.1    French, S.2    Evans, F.J.3    Joubert, F.4    Balaban, R.S.5
  • 112
    • 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
  • 114
    • 0022543113 scopus 로고
    • Mitochondrial creatine kinase activity alterations in skeletal muscle during long-distance running
    • Apple F.S., Rogers M.A. Mitochondrial creatine kinase activity alterations in skeletal muscle during long-distance running. J. Appl. Physiol. 1986, 61:482-485.
    • (1986) J. Appl. Physiol. , vol.61 , pp. 482-485
    • Apple, F.S.1    Rogers, M.A.2
  • 115
    • 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
  • 117
    • 0001221508 scopus 로고
    • On respiratory impairment in cancer cells
    • Warburg O. On respiratory impairment in cancer cells. Science 1956, 124:269-270.
    • (1956) Science , vol.124 , pp. 269-270
    • Warburg, O.1
  • 120
    • 44649182288 scopus 로고    scopus 로고
    • Mitochondrial medicine: the central role of cellular energetic depression and mitochondria in cell pathophysiology
    • Wiley-VCH, Weinheim, GmbH, Germany, V. Saks (Ed.)
    • Seppet E., Gizatullina Z., Trumbeckaite, Zierz S., Striggow F., Gellerich F. Mitochondrial medicine: the central role of cellular energetic depression and mitochondria in cell pathophysiology. Molecular System Bioenergetics. Energy for Life 2007, 479-521. Wiley-VCH, Weinheim, GmbH, Germany. V. Saks (Ed.).
    • (2007) Molecular System Bioenergetics. Energy for Life , pp. 479-521
    • Seppet, E.1    Gizatullina, Z.2    Trumbeckaite3    Zierz, S.4    Striggow, F.5    Gellerich, F.6
  • 121
    • 60249083822 scopus 로고    scopus 로고
    • Hexokinase-2 bound to mitochondria: cancer's stygian link to the "Warburg effect" and a pivotal target for effective therapy
    • Mathupala S.P., Ko Y.H., Pedersen P.L. Hexokinase-2 bound to mitochondria: cancer's stygian link to the "Warburg effect" and a pivotal target for effective therapy. Semin. Cancer Biol. 2009, 19:17-24.
    • (2009) Semin. Cancer Biol. , vol.19 , pp. 17-24
    • Mathupala, S.P.1    Ko, Y.H.2    Pedersen, P.L.3
  • 123
    • 0019815655 scopus 로고
    • Energy metabolism of tumor cells. Requirement for a form of hexokinase with a propensity for mitochondrial binding
    • Bustamante E., Morris H.P., Pedersen P.L. Energy metabolism of tumor cells. Requirement for a form of hexokinase with a propensity for mitochondrial binding. J. Biol. Chem. 1981, 256:8699-8704.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8699-8704
    • Bustamante, E.1    Morris, H.P.2    Pedersen, P.L.3
  • 124
    • 0042575733 scopus 로고
    • High aerobic glycolysis of rat hepatoma cells in culture: role of mitochondrial hexokinase
    • Bustamante E., Pedersen P.L. High aerobic glycolysis of rat hepatoma cells in culture: role of mitochondrial hexokinase. Proc. Natl. Acad. Sci. U. S. A. 1977, 74:3735-3739.
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 3735-3739
    • Bustamante, E.1    Pedersen, P.L.2
  • 125
    • 0037056002 scopus 로고    scopus 로고
    • Mitochondrial bound type II hexokinase: a key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention
    • Pedersen P.L., Mathupala S., Rempel A., Geschwind J.F., Ko Y.H. Mitochondrial bound type II hexokinase: a key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention. Biochim. Biophys. Acta 2002, 1555:14-20.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 14-20
    • Pedersen, P.L.1    Mathupala, S.2    Rempel, A.3    Geschwind, J.F.4    Ko, Y.H.5
  • 126
    • 33746924468 scopus 로고    scopus 로고
    • Hexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria
    • Mathupala S.P., Ko Y.H., Pedersen P.L. Hexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria. Oncogene 2006, 25:4777-4786.
    • (2006) Oncogene , vol.25 , pp. 4777-4786
    • Mathupala, S.P.1    Ko, Y.H.2    Pedersen, P.L.3
  • 127
    • 0038714272 scopus 로고    scopus 로고
    • Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function
    • Wilson J.E. Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function. J. Exp. Biol. 2003, 206:2049-2057.
    • (2003) J. Exp. Biol. , vol.206 , pp. 2049-2057
    • Wilson, J.E.1
  • 129
    • 38849119213 scopus 로고    scopus 로고
    • Calcium and cell death: the mitochondrial connection
    • Bernardi P., Rasola A. Calcium and cell death: the mitochondrial connection. Subcell. Biochem. 2007, 45:481-506.
    • (2007) Subcell. Biochem. , vol.45 , pp. 481-506
    • Bernardi, P.1    Rasola, A.2
  • 130
    • 46349097952 scopus 로고    scopus 로고
    • Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore
    • Leung A.W., Halestrap A.P. Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore. Biochim. Biophys. Acta 2008, 1777:946-952.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 946-952
    • Leung, A.W.1    Halestrap, A.P.2
  • 131
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens J.F. Mitochondrial formation of reactive oxygen species. J. Physiol. 2003, 552:335-344.
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 132
    • 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., Oliveira M.F., Galina A. 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    Oliveira, M.F.7    Galina, A.8
  • 133
    • 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
  • 135
    • 0033935979 scopus 로고    scopus 로고
    • Creatine and creatinine metabolism
    • Wyss M., Kaddurah-Daouk R. Creatine and creatinine metabolism. Physiol. Rev. 2000, 80:1107-1213.
    • (2000) Physiol. Rev. , vol.80 , pp. 1107-1213
    • Wyss, M.1    Kaddurah-Daouk, R.2
  • 137
    • 84889354603 scopus 로고    scopus 로고
    • Integrated and organized cellular energetic systems: theories of cell energetics, compartmentation and metabolic channeling
    • Wiley-VCH, Weinheim, GmbH, 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, Weinheim, GmbH, 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
  • 138
    • 67650867606 scopus 로고    scopus 로고
    • Principles of mathematical modeling and in silico studies of integrated systems of cellular energetics
    • Wiley-VCH, Weinheim, GmbH, Germany, V. Saks (Ed.)
    • Vendelin M., Saks V., Engelbrecht J. Principles of mathematical modeling and in silico studies of integrated systems of cellular energetics. Molecular System Bioenergetics. Energy for Life 2007, 407-433. Wiley-VCH, Weinheim, GmbH, Germany. V. Saks (Ed.).
    • (2007) Molecular System Bioenergetics. Energy for Life , pp. 407-433
    • Vendelin, M.1    Saks, V.2    Engelbrecht, J.3
  • 140
    • 33646340668 scopus 로고    scopus 로고
    • The creatine kinase/creatine connection to Alzheimer's disease: CK-inactivation, APP-CK complexes and focal creatine deposits
    • Burklen T.S., Schlattner U., Homayouni R., Gough K., Rak M., Szeghalmi A., Wallimann T. The creatine kinase/creatine connection to Alzheimer's disease: CK-inactivation, APP-CK complexes and focal creatine deposits. J. Biomed. Biotechnol. 2006, 2006:35936.
    • (2006) J. Biomed. Biotechnol. , vol.2006 , pp. 35936
    • Burklen, T.S.1    Schlattner, U.2    Homayouni, R.3    Gough, K.4    Rak, M.5    Szeghalmi, A.6    Wallimann, T.7
  • 141
    • 65249129156 scopus 로고    scopus 로고
    • Creatine and its potential therapeutic value for targeting cellular energy impairment in neurodegenerative diseases
    • Adhihetty P.J., Beal M.F. Creatine and its potential therapeutic value for targeting cellular energy impairment in neurodegenerative diseases. Neuromol. Med. 2008, 10:275-290.
    • (2008) Neuromol. Med. , vol.10 , pp. 275-290
    • Adhihetty, P.J.1    Beal, M.F.2
  • 142
    • 45249095633 scopus 로고    scopus 로고
    • Phosphocreatine as an energy source for actin cytoskeletal rearrangements during myoblast fusion
    • O'Connor R.S., Steeds C.M., Wiseman R.W., Pavlath G.K. Phosphocreatine as an energy source for actin cytoskeletal rearrangements during myoblast fusion. J. Physiol. 2008, 586:2841-2853.
    • (2008) J. Physiol. , vol.586 , pp. 2841-2853
    • O'Connor, R.S.1    Steeds, C.M.2    Wiseman, R.W.3    Pavlath, G.K.4
  • 144
    • 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
  • 145
  • 146
    • 0025087657 scopus 로고
    • Regulation of systolic force and control of free energy of ATP-hydrolysis in hypoxic hearts
    • Kammermeier H., Roeb E., Jungling E., Meyer B. Regulation of systolic force and control of free energy of ATP-hydrolysis in hypoxic hearts. J. Mol. Cell. Cardiol. 1990, 22:707-713.
    • (1990) J. Mol. Cell. Cardiol. , vol.22 , pp. 707-713
    • Kammermeier, H.1    Roeb, E.2    Jungling, E.3    Meyer, B.4
  • 147
    • 0025141834 scopus 로고
    • Mechanism of ischemic contracture in ferret hearts: relative roles of [Ca2+]i elevation and ATP depletion
    • Koretsune Y., Marban E. Mechanism of ischemic contracture in ferret hearts: relative roles of [Ca2+]i elevation and ATP depletion. Am. J. Physiol. 1990, 258:H9-H16.
    • (1990) Am. J. Physiol. , vol.258
    • Koretsune, Y.1    Marban, E.2
  • 149
    • 59449085388 scopus 로고    scopus 로고
    • Energy metabolism in heart failure and remodelling
    • Ingwall J.S. Energy metabolism in heart failure and remodelling. Cardiovasc. Res. 2009, 81:412-419.
    • (2009) Cardiovasc. Res. , vol.81 , pp. 412-419
    • Ingwall, J.S.1
  • 150
    • 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
  • 151
    • 23644449906 scopus 로고    scopus 로고
    • The fall in creatine levels and creatine kinase isozyme changes in the failing heart are reversible: complex post-transcriptional regulation of the components of the CK system
    • Shen W., Spindler M., Higgins M.A., Jin N., Gill R.M., Bloem L.J., Ryan T.P., Ingwall J.S. The fall in creatine levels and creatine kinase isozyme changes in the failing heart are reversible: complex post-transcriptional regulation of the components of the CK system. J. Mol. Cell. Cardiol. 2005, 39:537-544.
    • (2005) J. Mol. Cell. Cardiol. , vol.39 , pp. 537-544
    • Shen, W.1    Spindler, M.2    Higgins, M.A.3    Jin, N.4    Gill, R.M.5    Bloem, L.J.6    Ryan, T.P.7    Ingwall, J.S.8
  • 152
    • 4444286823 scopus 로고    scopus 로고
    • Transgenesis and cardiac energetics: new insights into cardiac metabolism
    • Ingwall J.S. Transgenesis and cardiac energetics: new insights into cardiac metabolism. J. Mol. Cell. Cardiol. 2004, 37:613-623.
    • (2004) J. Mol. Cell. Cardiol. , vol.37 , pp. 613-623
    • Ingwall, J.S.1
  • 153
    • 0030008105 scopus 로고    scopus 로고
    • Energetic basis for reduced contractile reserve in isolated rat hearts
    • Tian R., Ingwall J.S. Energetic basis for reduced contractile reserve in isolated rat hearts. Am. J. Physiol. 1996, 270:H1207-H1216.
    • (1996) Am. J. Physiol. , vol.270
    • Tian, R.1    Ingwall, J.S.2
  • 154
    • 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. U. S. A. 2005, 102:808-813.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 808-813
    • Weiss, R.G.1    Gerstenblith, G.2    Bottomley, P.A.3
  • 155
    • 33748370968 scopus 로고    scopus 로고
    • Heart failure: a model of cardiac and skeletal muscle energetic failure
    • Mettauer B., Zoll J., Garnier A., Ventura-Clapier R. Heart failure: a model of cardiac and skeletal muscle energetic failure. Pflugers Arch. 2006, 452:653-666.
    • (2006) Pflugers Arch. , vol.452 , pp. 653-666
    • Mettauer, B.1    Zoll, J.2    Garnier, A.3    Ventura-Clapier, R.4
  • 157
    • 0034633813 scopus 로고    scopus 로고
    • Heart failure affects mitochondrial but not myofibrillar intrinsic properties of skeletal muscle
    • De Sousa E., Veksler V., Bigard X., Mateo P., Ventura-Clapier R. Heart failure affects mitochondrial but not myofibrillar intrinsic properties of skeletal muscle. Circulation 2000, 102:1847-1853.
    • (2000) Circulation , vol.102 , pp. 1847-1853
    • De Sousa, E.1    Veksler, V.2    Bigard, X.3    Mateo, P.4    Ventura-Clapier, R.5
  • 158
    • 35548995604 scopus 로고    scopus 로고
    • Creatine: endogenous metabolite, dietary, and therapeutic supplement
    • Brosnan J.T., Brosnan M.E. Creatine: endogenous metabolite, dietary, and therapeutic supplement. Annu. Rev. Nutr. 2007, 27:241-261.
    • (2007) Annu. Rev. Nutr. , vol.27 , pp. 241-261
    • Brosnan, J.T.1    Brosnan, M.E.2
  • 160
    • 44949166981 scopus 로고    scopus 로고
    • Introduction-creatine: cheap ergogenic supplement with great potential for health and disease
    • Wallimann T. Introduction-creatine: cheap ergogenic supplement with great potential for health and disease. Subcell. Biochem. 2007, 46:1-16.
    • (2007) Subcell. Biochem. , vol.46 , pp. 1-16
    • Wallimann, T.1
  • 163
    • 17544373377 scopus 로고    scopus 로고
    • Suppression of creatine kinase-catalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle
    • Dzeja P.P., Zeleznikar R.J., Goldberg N.D. Suppression of creatine kinase-catalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle. J. Biol. Chem. 1996, 271:12847-12851.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12847-12851
    • Dzeja, P.P.1    Zeleznikar, R.J.2    Goldberg, N.D.3
  • 164
    • 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
  • 166
  • 171
    • 0001838147 scopus 로고
    • The mechanism of the reaction catalysed by adenosine triphosphate-creatine phosphotransferase
    • Morrison J.F., James E. The mechanism of the reaction catalysed by adenosine triphosphate-creatine phosphotransferase. Biochem. J. 1965, 97:37-52.
    • (1965) Biochem. J. , vol.97 , pp. 37-52
    • Morrison, J.F.1    James, E.2
  • 173
    • 0023679888 scopus 로고
    • Reduction of ventricular arrhythmias by phosphocreatine (Neoton) in patients with acute myocardial infarction
    • Ruda M., Samarenko M.B., Afonskaya N.I., Saks V.A. Reduction of ventricular arrhythmias by phosphocreatine (Neoton) in patients with acute myocardial infarction. Am. Heart J. 1988, 116:393-397.
    • (1988) Am. Heart J. , vol.116 , pp. 393-397
    • Ruda, M.1    Samarenko, M.B.2    Afonskaya, N.I.3    Saks, V.A.4
  • 174
    • 0021339774 scopus 로고
    • Creatine phosphate: an additive myocardial protective and antiarrhythmic agent in cardioplegia
    • Robinson L.A., Braimbridge M.V., Hearse D.J. Creatine phosphate: an additive myocardial protective and antiarrhythmic agent in cardioplegia. J. Thorac Cardiovasc. Surg. 1984, 87:190-200.
    • (1984) J. Thorac Cardiovasc. Surg. , vol.87 , pp. 190-200
    • Robinson, L.A.1    Braimbridge, M.V.2    Hearse, D.J.3
  • 176
    • 0027304843 scopus 로고
    • Phosphocreatine: molecular and cellular aspects of the mechanism of cardioprotective action
    • Saks V., Strumia E. Phosphocreatine: molecular and cellular aspects of the mechanism of cardioprotective action. Curr. Theaurapeut. Res. 1993, 53:565-598.
    • (1993) Curr. Theaurapeut. Res. , vol.53 , pp. 565-598
    • Saks, V.1    Strumia, E.2
  • 177
    • 34247385040 scopus 로고    scopus 로고
    • MR, spectroscopy in heart failure-clinical and experimental findings
    • Ten Hove M., Neubauer S. MR, spectroscopy in heart failure-clinical and experimental findings. Heart Fail. Rev. 2007, 12:48-57.
    • (2007) Heart Fail. Rev. , vol.12 , pp. 48-57
    • Ten Hove, M.1    Neubauer, S.2
  • 178
    • 47349100745 scopus 로고    scopus 로고
    • The application of NMR spectroscopy for the study of heart failure
    • ten Hove M., Neubauer S. The application of NMR spectroscopy for the study of heart failure. Curr. Pharm. Des. 2008, 14:1787-1797.
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 1787-1797
    • Ten Hove, M.1    Neubauer, S.2
  • 179
    • 44949138383 scopus 로고    scopus 로고
    • Resolution of creatine and phosphocreatine 1H signals in isolated human skeletal muscle using HR-MAS 1H NMR
    • Chen J.H., Wu Y.V., DeCarolis P., O'Connor R., Somberg C.J., Singer S. Resolution of creatine and phosphocreatine 1H signals in isolated human skeletal muscle using HR-MAS 1H NMR. Magn. Reson. Med. 2008, 59:1221-1224.
    • (2008) Magn. Reson. Med. , vol.59 , pp. 1221-1224
    • Chen, J.H.1    Wu, Y.V.2    DeCarolis, P.3    O'Connor, R.4    Somberg, C.J.5    Singer, S.6
  • 180
    • 34848924909 scopus 로고    scopus 로고
    • Absolute quantification of phosphorus metabolite concentrations in human muscle in vivo by 31P MRS: a quantitative review
    • Kemp G.J., Meyerspeer M., Moser E. Absolute quantification of phosphorus metabolite concentrations in human muscle in vivo by 31P MRS: a quantitative review. NMR Biomed. 2007, 20:555-565.
    • (2007) NMR Biomed. , vol.20 , pp. 555-565
    • Kemp, G.J.1    Meyerspeer, M.2    Moser, E.3
  • 181
    • 45249093481 scopus 로고    scopus 로고
    • The phosphocreatine-creatine kinase system helps to shape muscle cells and keep them healthy and alive
    • Saks V. The phosphocreatine-creatine kinase system helps to shape muscle cells and keep them healthy and alive. J. Physiol. 2008, 586:2817-2818.
    • (2008) J. Physiol. , vol.586 , pp. 2817-2818
    • Saks, V.1
  • 183
  • 185
    • 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
  • 186
    • 17244378347 scopus 로고    scopus 로고
    • Thermodynamics of stoichiometric biochemical networks in living systems far from equilibrium
    • Qian H., Beard D.A. Thermodynamics of stoichiometric biochemical networks in living systems far from equilibrium. Biophys. Chem. 2005, 114:213-220.
    • (2005) Biophys. Chem. , vol.114 , pp. 213-220
    • Qian, H.1    Beard, D.A.2
  • 187
    • 0037315604 scopus 로고    scopus 로고
    • Stoichiometric network theory for nonequilibrium biochemical systems
    • Qian H., Beard D.A., Liang S.D. Stoichiometric network theory for nonequilibrium biochemical systems. Eur. J. Biochem. 2003, 270:415-421.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 415-421
    • Qian, H.1    Beard, D.A.2    Liang, S.D.3
  • 188
    • 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
  • 191
    • 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. 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    Tiivel, T.7
  • 192
    • 0028940661 scopus 로고
    • Correlation between degree of rupture of outer mitochondrial membrane and changes of kinetics of regulation of respiration by ADP in permeabilized heart and liver cells
    • Saks V., Belikova Y., Vasilyeva E., Kuznetsov A., Fontaine E., Keriel C., Leverve X. Correlation between degree of rupture of outer mitochondrial membrane and changes of kinetics of regulation of respiration by ADP in permeabilized heart and liver cells. Biochem. Biophys. Res. Commun. 1995, 208:919-926.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 919-926
    • Saks, V.1    Belikova, Y.2    Vasilyeva, E.3    Kuznetsov, A.4    Fontaine, E.5    Keriel, C.6    Leverve, X.7
  • 193
    • 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., Perov N.A. 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    Perov, N.A.7
  • 194
    • 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
  • 197
    • 0035371774 scopus 로고    scopus 로고
    • What controls the outer mitochondrial membrane permeability for ADP: facts for and against the role of oncotic pressure
    • Liobikas J., Kopustinskiene D.M., Toleikis A. What controls the outer mitochondrial membrane permeability for ADP: facts for and against the role of oncotic pressure. Biochim. Biophys. Acta 2001, 1505:220-225.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 220-225
    • Liobikas, J.1    Kopustinskiene, D.M.2    Toleikis, A.3
  • 199
    • 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. Cytoplasmic cellular structures control permeability of outer mitochondrial membrane for ADP and oxidative phosphorylation in rat liver cells. Biochem. Biophys. Res. Commun. 1995, 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
  • 200
    • 0029147509 scopus 로고
    • Muscle creatine kinase-deficient mice. II. Cardiac and skeletal muscles exhibit tissue-specific adaptation of the mitochondrial function
    • Veksler V.I., Kuznetsov A.V., Anflous K., Mateo P., van Deursen J., Wieringa B., Ventura-Clapier R. Muscle creatine kinase-deficient mice. II. Cardiac and skeletal muscles exhibit tissue-specific adaptation of the mitochondrial function. J. Biol. Chem. 1995, 270:19921-19929.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19921-19929
    • Veksler, V.I.1    Kuznetsov, A.V.2    Anflous, K.3    Mateo, P.4    van Deursen, J.5    Wieringa, B.6    Ventura-Clapier, R.7
  • 202
    • 77950874950 scopus 로고    scopus 로고
    • Compartmentation of ATP in cardiomyocytes and mitochondria. Kinetic studies and direct measurements
    • 241a (Boston, USA)
    • Monge C., Grichine A., Rostovtseva T., Sackett P., Saks V. Compartmentation of ATP in cardiomyocytes and mitochondria. Kinetic studies and direct measurements. Biophys. J. 2009, 93(6). 241a (Boston, USA).
    • (2009) Biophys. J. , vol.93 , Issue.6
    • Monge, C.1    Grichine, A.2    Rostovtseva, T.3    Sackett, P.4    Saks, V.5
  • 204
    • 74549187999 scopus 로고    scopus 로고
    • Intracellular diffusion restrictions in isolated cardiomyocytes from rainbow trout
    • Sokolova N., Vendelin M., Birkedal R. Intracellular diffusion restrictions in isolated cardiomyocytes from rainbow trout. BMC Cell Biol. 2009, 10.1186/1471-2121-10-90.
    • (2009) BMC Cell Biol.
    • Sokolova, N.1    Vendelin, M.2    Birkedal, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.