메뉴 건너뛰기




Volumn 206, Issue 12, 2003, Pages 2039-2047

Phosphotransfer networks and cellular energetics

Author keywords

Adenylate kinase; Carbonic anhydrase; Creatine kinase; Energy; Glycolysis; Homeostasis; Metabolism; Mitochondria

Indexed keywords

ADENOSINE TRIPHOSPHATE; PHOSPHOTRANSFERASE;

EID: 0038037716     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: 10.1242/jeb.00426     Document Type: Review
Times cited : (407)

References (92)
  • 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. and 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
  • 2
    • 0033746173 scopus 로고    scopus 로고
    • CNS energy metabolism as related to function
    • Ames, A., III (2000). CNS energy metabolism as related to function. Brain Res. Brain Res. Rev. 34, 42-68.
    • (2000) Brain Res. Brain Res. Rev. , vol.34 , pp. 42-68
    • Ames A. III1
  • 3
    • 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
  • 4
    • 0024262838 scopus 로고
    • Yeast adenylate kinase is active simultaneously in mitochondria and cytoplasm and is required for non-fermentative growth
    • Bandlow, W., Strobel, G., Zoglowek, C., Oechsner, U. and Magdolen, V. (1988). Yeast adenylate kinase is active simultaneously in mitochondria and cytoplasm and is required for non-fermentative growth. Eur. J. Biochem. 178, 451-457.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 451-457
    • Bandlow, W.1    Strobel, G.2    Zoglowek, C.3    Oechsner, U.4    Magdolen, V.5
  • 5
    • 0026714957 scopus 로고
    • The effects of dNTP pool imbalances on frameshift fidelity during DNA replication
    • Bebenek, K., Roberts, J. D. and Kunkel, T. A. (1992). The effects of dNTP pool imbalances on frameshift fidelity during DNA replication. J. Biol. Chem. 267, 3589-3596.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3589-3596
    • Bebenek, K.1    Roberts, J.D.2    Kunkel, T.A.3
  • 7
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shuttle
    • Bessman, S. P. and 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
  • 8
    • 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., Lechene, P. and 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    Lechene, P.4    Veksler, V.5
  • 10
    • 0033592709 scopus 로고    scopus 로고
    • wt p53 dependent expression of a membrane-associated isoform of adenylate kinase
    • Collavin, L., Lazarevic, D., Utrera, R., Marzinotto, S., Monte, M. and Schneider, C. (1999). wt p53 dependent expression of a membrane-associated isoform of adenylate kinase. Oncogene 18, 5879-5888.
    • (1999) Oncogene , vol.18 , pp. 5879-5888
    • Collavin, L.1    Lazarevic, D.2    Utrera, R.3    Marzinotto, S.4    Monte, M.5    Schneider, C.6
  • 11
    • 0034890250 scopus 로고    scopus 로고
    • Changes in glycolytic network and mitochondrial design in creatine kinase-deficient muscles
    • de Groof, A. J., Oerlemans, F. T., Jost, C. R. and Wieringa, B. (2001). Changes in glycolytic network and mitochondrial design in creatine kinase-deficient muscles. Muscle Nerve 24, 1188-1196.
    • (2001) Muscle Nerve , vol.24 , pp. 1188-1196
    • De Groof, A.J.1    Oerlemans, F.T.2    Jost, C.R.3    Wieringa, B.4
  • 13
    • 0037162481 scopus 로고    scopus 로고
    • Energetic communication between mitochondria and nucleus directed by catalyzed phosphotransfer
    • Dzeja, P. P., Bortolon, R., Perez-Terzic, C., Holmuhamedov, E. L. and Terzic, A. (2002). Energetic communication between mitochondria and nucleus directed by catalyzed phosphotransfer. Proc. Natl. Acad. Sci. USA 99, 10156-10161.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10156-10161
    • Dzeja, P.P.1    Bortolon, R.2    Perez-Terzic, C.3    Holmuhamedov, E.L.4    Terzic, A.5
  • 14
    • 0033402758 scopus 로고    scopus 로고
    • Reduced activity of enzymes coupling ATP-generating with ATP-consuming processes in the failing myocardium
    • Dzeja, P. P., Pucar, D., Redfield, M. M., Burnett, J. C. and Terzic, A. (1999a). Reduced activity of enzymes coupling ATP-generating with ATP-consuming processes in the failing myocardium. Mol. Cell. Biochem. 201, 33-40.
    • (1999) Mol. Cell. Biochem. , vol.201 , pp. 33-40
    • Dzeja, P.P.1    Pucar, D.2    Redfield, M.M.3    Burnett, J.C.4    Terzic, A.5
  • 17
    • 0038036209 scopus 로고    scopus 로고
    • Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice
    • in press
    • Dzeja, P. P., Terzic, A. and Wieringa, B. (2003). Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice. Mol. Cell. Biochem. (in press).
    • (2003) Mol. Cell. Biochem.
    • Dzeja, P.P.1    Terzic, A.2    Wieringa, B.3
  • 18
    • 0033612362 scopus 로고    scopus 로고
    • Adenylate kinase catalyzed phosphotransfer in the myocardium: Increased contribution in heart failure
    • Dzeja, P. P., Vitkevicius, K. T., Redfield, M. M., Burnett, J. C. and Terzic, A. (1999b). Adenylate kinase catalyzed phosphotransfer in the myocardium: Increased contribution in heart failure. Circ. Res. 84, 1137-1143.
    • (1999) Circ. Res. , vol.84 , pp. 1137-1143
    • Dzeja, P.P.1    Vitkevicius, K.T.2    Redfield, M.M.3    Burnett, J.C.4    Terzic, A.5
  • 19
    • 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. and Goldberg, N. D. (1998). Adenylate kinase: kinetic behavior in intact cells indicates it is integral to multiple cellular processes. Mol. Cell. Biochem. 84, 169-182.
    • (1998) Mol. Cell. Biochem. , vol.84 , pp. 169-182
    • Dzeja, P.P.1    Zeleznikar, R.J.2    Goldberg, N.D.3
  • 21
    • 0030046495 scopus 로고    scopus 로고
    • Mitochondria and diabetes, Genetic, biochemical, and clinical implications of the cellular energy circuit
    • Gerbitz, K. D., Gempel, K. and Brdiczka, D. (1996). Mitochondria and diabetes. Genetic, biochemical, and clinical implications of the cellular energy circuit. Diabetes 45, 113-126.
    • (1996) Diabetes , vol.45 , pp. 113-126
    • Gerbitz, K.D.1    Gempel, K.2    Brdiczka, D.3
  • 22
    • 0001877146 scopus 로고
    • An allosteric enzyme model with positive feedback applied to glycolytic oscillations
    • Goldbeter, A. and 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
  • 24
    • 0026406806 scopus 로고
    • Biochemical topology: From vectorial metabolism to morphogenesis
    • Harold, F. M. (1991). Biochemical topology: from vectorial metabolism to morphogenesis. Biosci. Rep. 11, 347-385.
    • (1991) Biosci. Rep. , vol.11 , pp. 347-385
    • Harold, F.M.1
  • 25
    • 0037470151 scopus 로고    scopus 로고
    • Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gβ subunits. Specific activation of Gsα by an NDPK B Gβγ complex in H10 cells
    • Hippe, H. J., Lutz, S., Cuello, F., Knorr, K., Vogt, A., Jakobs, K. H., Wieland, T. and Niroomand, F. (2003). Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gβ subunits. Specific activation of Gsα by an NDPK B Gβγ complex in H10 cells. J. Biol. Chem. 278, 7227-7233.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7227-7233
    • Hippe, H.J.1    Lutz, S.2    Cuello, F.3    Knorr, K.4    Vogt, A.5    Jakobs, K.H.6    Wieland, T.7    Niroomand, F.8
  • 27
    • 0033607168 scopus 로고    scopus 로고
    • The metabolic implications of intracellular circulation
    • Hochachka, P. W. (1999). The metabolic implications of intracellular circulation. Proc. Natl. Acad. Sci. USA 96, 12233-12239.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12233-12239
    • Hochachka, P.W.1
  • 28
    • 0002185678 scopus 로고    scopus 로고
    • The pattern and mechanism of mitochondrial transport in axons
    • Hollenbeck, P. J. (1996). The pattern and mechanism of mitochondrial transport in axons. Front. Biosci. 1, D91-D102.
    • (1996) Front. Biosci. , vol.1
    • Hollenbeck, P.J.1
  • 29
    • 0026037225 scopus 로고
    • Whole-organ enzymology of the creatine kinase system in heart
    • Ingwall, J. S. (1991). Whole-organ enzymology of the creatine kinase system in heart. Biochem. Soc. Trans. 19, 1006-1010.
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 1006-1010
    • Ingwall, J.S.1
  • 31
    • 0021894478 scopus 로고
    • Respiratory control and the integration of heart high-energy phosphate metabolism by mitochondrial creatine kinase
    • Jacobus, W. E. (1985). Respiratory control and the integration of heart high-energy phosphate metabolism by mitochondrial creatine kinase. Annu. Rev. Physiol. 47, 707-725.
    • (1985) Annu. Rev. Physiol. , vol.47 , pp. 707-725
    • Jacobus, W.E.1
  • 33
    • 0034609791 scopus 로고    scopus 로고
    • The large-scale organization of metabolic networks
    • Jeong, H., Tombor, B., Albert, R., Oltvai, Z. N. and Barabasi, A. L. (2000). The large-scale organization of metabolic networks. Nature 407, 651-654.
    • (2000) Nature , vol.407 , pp. 651-654
    • Jeong, H.1    Tombor, B.2    Albert, R.3    Oltvai, Z.N.4    Barabasi, A.L.5
  • 34
    • 0036460110 scopus 로고    scopus 로고
    • Creatine kinase B-driven energy transfer in the brain is important for habituation and spatial learning behaviour, mossy fibre field size and determination of seizure susceptibility
    • Jost, C. R., Van Der Zee, C. E., in't Zandt, H. J., Oerlemans, F., Verheij, M., Streijger, F., Fransen, J., Heerschap, A., Cools, A. R. and Wieringa, B. (2002). Creatine kinase B-driven energy transfer in the brain is important for habituation and spatial learning behaviour, mossy fibre field size and determination of seizure susceptibility. Eur. J. Neurosci. 15, 1692-1706.
    • (2002) Eur. J. Neurosci. , vol.15 , pp. 1692-1706
    • Jost, C.R.1    Van Der Zee, C.E.2    In't Zandt, H.J.3    Oerlemans, F.4    Verheij, M.5    Streijger, F.6    Fransen, J.7    Heerschap, A.8    Cools, A.R.9    Wieringa, B.10
  • 35
    • 0037165834 scopus 로고    scopus 로고
    • 31P NMR detection of subcellular creatine kinase fluxes in the perfused rat heart: Contractility modifies energy transfer pathways
    • 31P NMR detection of subcellular creatine kinase fluxes in the perfused rat heart: contractility modifies energy transfer pathways. J. Biol. Chem. 277, 18469-18476.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18469-18476
    • Joubert, F.1    Mazet, J.L.2    Mateo, P.3    Hoerter, J.A.4
  • 36
    • 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. and 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
  • 37
    • 0030875755 scopus 로고    scopus 로고
    • Myocardial cell energetics
    • Kammermeier, H. (1997). Myocardial cell energetics. Adv. Exp. Biol. 430, 89-96.
    • (1997) Adv. Exp. Biol. , vol.430 , pp. 89-96
    • Kammermeier, H.1
  • 38
    • 0035577280 scopus 로고    scopus 로고
    • Altered brain phosphocreatine and ATP regulation when mitochondrial creatine kinase is absent
    • Kekelidze, T., Khait, I., Togliatti, A., Benzecry, J. M., Wieringa, B. and Holtzman, D. (2001). Altered brain phosphocreatine and ATP regulation when mitochondrial creatine kinase is absent. J. Neurosci. Res. 66, 866-872.
    • (2001) J. Neurosci. Res. , vol.66 , pp. 866-872
    • Kekelidze, T.1    Khait, I.2    Togliatti, A.3    Benzecry, J.M.4    Wieringa, B.5    Holtzman, D.6
  • 41
    • 0030601312 scopus 로고    scopus 로고
    • Nuclear localization of nucleoside diphosphate kinase type B (nm23-H2) in cultured cells
    • Kraeft, S. K., Traincart, F., Mesnildrey, S., Bourdais, J., Veron, M. and Chen, L. B. (1996). Nuclear localization of nucleoside diphosphate kinase type B (nm23-H2) in cultured cells. Exp. Cell Res. 227, 63-69.
    • (1996) Exp. Cell Res. , vol.227 , pp. 63-69
    • Kraeft, S.K.1    Traincart, F.2    Mesnildrey, S.3    Bourdais, J.4    Veron, M.5    Chen, L.B.6
  • 42
    • 0029597776 scopus 로고
    • Skeletal muscle: A paradigm for testing principles of bioenergetics
    • Kushmerick, M. J. (1995). Skeletal muscle: a paradigm for testing principles of bioenergetics. J. Bioenerg. Biomembr. 27, 555-569.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 555-569
    • Kushmerick, M.J.1
  • 44
    • 0037115642 scopus 로고    scopus 로고
    • Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2
    • Lange, S., Auerbach, D., McLoughlin, P., Perriard, E., Schafer, B. W., Perriard, J. C. and Ehler, E. (2002). Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2. J. Cell Sci. 115, 4925-4936.
    • (2002) J. Cell Sci. , vol.115 , pp. 4925-4936
    • Lange, S.1    Auerbach, D.2    McLoughlin, P.3    Perriard, E.4    Schafer, B.W.5    Perriard, J.C.6    Ehler, E.7
  • 45
    • 0030779954 scopus 로고    scopus 로고
    • Experimental evidence for dynamic compartmentation of ADP at the mitochondrial periphery: Coupling of mitochondrial adenylate kinase and mitochondrial hexokinase with oxidative phosphorylation under conditions mimicking the intracellular colloid osmotic pressure
    • Laterveer, F. D., Nicolay, K. and Gellerich, F. N. (1997). Experimental evidence for dynamic compartmentation of ADP at the mitochondrial periphery: coupling of mitochondrial adenylate kinase and mitochondrial hexokinase with oxidative phosphorylation under conditions mimicking the intracellular colloid osmotic pressure. Mol. Cell. Biochem. 174, 43-51.
    • (1997) Mol. Cell. Biochem. , vol.174 , pp. 43-51
    • Laterveer, F.D.1    Nicolay, K.2    Gellerich, F.N.3
  • 46
    • 0029903967 scopus 로고    scopus 로고
    • Use of the forcevelocity test to determine the optimal braking force for a sprint exercise on a friction-loaded cycle ergometer
    • Linossier, M. T., Dormois, D., Fouquet, R., Geyssant, A. and Denis, C. (1996). Use of the forcevelocity test to determine the optimal braking force for a sprint exercise on a friction-loaded cycle ergometer. Eur. J. Appl. Physiol. Occup. Physiol. 74, 420-427.
    • (1996) Eur. J. Appl. Physiol. Occup. Physiol. , vol.74 , pp. 420-427
    • Linossier, M.T.1    Dormois, D.2    Fouquet, R.3    Geyssant, A.4    Denis, C.5
  • 47
    • 0002720053 scopus 로고
    • Metabolic generation and utilization of phosphate bond energy
    • Lipmann, F. (1941). Metabolic generation and utilization of phosphate bond energy. Adv. Enzymol. 1, 99-162.
    • (1941) Adv. Enzymol. , vol.1 , pp. 99-162
    • Lipmann, F.1
  • 48
    • 0034710947 scopus 로고    scopus 로고
    • Creatine kinase, an ATP-generating enzyme, is required for thrombin receptor signaling to the cytoskeleton
    • Mahajan, V. B., Pai, K. S., Lau, A. and Cunningham, D. D. (2000). Creatine kinase, an ATP-generating enzyme, is required for thrombin receptor signaling to the cytoskeleton. Proc. Natl. Acad. Sci. USA 97, 12062-12067.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12062-12067
    • Mahajan, V.B.1    Pai, K.S.2    Lau, A.3    Cunningham, D.D.4
  • 49
    • 0030046478 scopus 로고    scopus 로고
    • Traveling NADH and proton waves during oscillatory glycolysis in vitro
    • Mair, T. and Muller, 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    Muller, S.C.2
  • 51
    • 0027759947 scopus 로고
    • Cellular and subcellular compartmentation of creatine kinase in brain
    • Manos, P. and Bryan, G. K. (1993). Cellular and subcellular compartmentation of creatine kinase in brain. Dev. Neurosci. 15, 271-279.
    • (1993) Dev. Neurosci. , vol.15 , pp. 271-279
    • Manos, P.1    Bryan, G.K.2
  • 52
    • 0023193842 scopus 로고
    • Glycolysis - New concepts in an old pathway
    • Masters, C. J., Reid, S. and Don, M. (1987). Glycolysis - new concepts in an old pathway. Mol. Cell. Biochem. 76, 3-14.
    • (1987) Mol. Cell. Biochem. , vol.76 , pp. 3-14
    • Masters, C.J.1    Reid, S.2    Don, M.3
  • 53
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj, I. W. and Englmeier, L. (1998). Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67, 265-306.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 54
    • 0021436518 scopus 로고
    • A simple analysis of the 'phosphocreatine shuttle'
    • Meyer, R. A., Sweeney, H. L. and Kushmeric, M. J. (1984). A simple analysis of the 'phosphocreatine shuttle'. Am. J. Physiol. 246, C365-C377.
    • (1984) Am. J. Physiol. , vol.246
    • Meyer, R.A.1    Sweeney, H.L.2    Kushmeric, M.J.3
  • 55
    • 0018391707 scopus 로고
    • Compartmentation and communication in living systems. Ligand conduction: A general catalytic principle in chemical, osmotic and chemiosmotic reaction systems
    • Mitchell, P. (1979). Compartmentation and communication in living systems. Ligand conduction: a general catalytic principle in chemical, osmotic and chemiosmotic reaction systems. Eur. J. Biochem. 95, 1-20.
    • (1979) Eur. J. Biochem. , vol.95 , pp. 1-20
    • Mitchell, P.1
  • 56
    • 0014949474 scopus 로고
    • Regulation problems in the energy metabolism of the myocardium (germ)
    • Nagle, S. (1970). Regulation problems in the energy metabolism of the myocardium (germ). Klin. Wochenschr. 48, 1075-1089.
    • (1970) Klin. Wochenschr. , vol.48 , pp. 1075-1089
    • Nagle, S.1
  • 58
    • 0037328989 scopus 로고    scopus 로고
    • A molecular approach to the concerted action of kinases involved in energy homoeostasis
    • Neumann, D., Schlattner, U. and Wallimann, T. (2003). A molecular approach to the concerted action of kinases involved in energy homoeostasis. Biochem. Soc. Trans. 31, 169-174.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 169-174
    • Neumann, D.1    Schlattner, U.2    Wallimann, T.3
  • 59
    • 70349640265 scopus 로고
    • Adenylate kinase
    • ed. P. D. Boyer. New York: Academic Press
    • Noda, L. H. (1973). Adenylate kinase. In The Enzymes, 3rd edition, vol. 8 (ed. P. D. Boyer), pp. 279-305. New York: Academic Press.
    • (1973) The Enzymes, 3rd Edition , vol.8 , pp. 279-305
    • Noda, L.H.1
  • 60
    • 0028037717 scopus 로고
    • Oscillations of membrane current and excitability driven by metabolic oscillations in heart cells
    • O'Rourke, B., Ramza, B. M. and Marban, E. (1994). Oscillations of membrane current and excitability driven by metabolic oscillations in heart cells. Science 265, 962-966.
    • (1994) Science , vol.265 , pp. 962-966
    • O'Rourke, B.1    Ramza, B.M.2    Marban, E.3
  • 61
    • 0017435456 scopus 로고
    • The role of compartmentation in the control of glycolysis
    • Ottaway, J. H. and Mowbray, J. (1977). The role of compartmentation in the control of glycolysis. Curr. Top. Cell. Reg. 12, 107-208.
    • (1977) Curr. Top. Cell. Reg. , vol.12 , pp. 107-208
    • Ottaway, J.H.1    Mowbray, J.2
  • 62
    • 0031041578 scopus 로고    scopus 로고
    • Enhanced catalytic activity of hexokinase by work-induced mitochondrial binding in fast-twitch muscle of rat
    • Parra, J., Brdiczka, D., Cusso, R. and Pette, D. (1997). Enhanced catalytic activity of hexokinase by work-induced mitochondrial binding in fast-twitch muscle of rat. FEBS Lett. 403, 279-282.
    • (1997) FEBS Lett. , vol.403 , pp. 279-282
    • Parra, J.1    Brdiczka, D.2    Cusso, R.3    Pette, D.4
  • 63
    • 0037282545 scopus 로고    scopus 로고
    • Lithium detaches hexokinase from mitochondria and inhibits proliferation of B16 melanoma cells
    • Penso, J. and Beitner, R. (2003). Lithium detaches hexokinase from mitochondria and inhibits proliferation of B16 melanoma cells. Mol. Genet. Metab. 78, 74-78.
    • (2003) Mol. Genet. Metab. , vol.78 , pp. 74-78
    • Penso, J.1    Beitner, R.2
  • 65
    • 0004258824 scopus 로고
    • Englewood Cliffs: Prentice-Hall
    • Peusner, L. (1974). Concepts in Bioenergetics. pp. 67-85. Englewood Cliffs: Prentice-Hall.
    • (1974) Concepts in Bioenergetics , pp. 67-85
    • Peusner, L.1
  • 66
    • 0028781629 scopus 로고
    • Measurement of unidirectional P(i)→ATP flux in lamb myocardium in vivo
    • Portman, M. A. (1994). Measurement of unidirectional P(i)→ATP flux in lamb myocardium in vivo. Biochim. Biophys. Acta 1185, 221-227.
    • (1994) Biochim. Biophys. Acta , vol.1185 , pp. 221-227
    • Portman, M.A.1
  • 69
    • 0026466339 scopus 로고
    • Nucleoside diphosphokinase: A functional link between intermediary metabolism and nucleic acid synthesis
    • Ray, N. B. and Mathews, C. K. (1992). Nucleoside diphosphokinase: a functional link between intermediary metabolism and nucleic acid synthesis. Curr. Top. Cell. Regul. 33, 343-357.
    • (1992) Curr. Top. Cell. Regul. , vol.33 , pp. 343-357
    • Ray, N.B.1    Mathews, C.K.2
  • 73
    • 0028017703 scopus 로고
    • Metabolic compartmentation and substrate channeling in muscle cells. Role of coupled creatine kinases in in vivo regulation of cellular respiration - A synthesis
    • Saks, V. A., Khuchua, Z. A., Vasilyeva, E. V., Belikova, O. Y. and Kuznetsov, A. V. (1994). Metabolic compartmentation and substrate channeling 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. , pp. 133-134
    • Saks, V.A.1    Khuchua, Z.A.2    Vasilyeva, E.V.3    Belikova, O.Y.4    Kuznetsov, A.V.5
  • 74
    • 0032482127 scopus 로고    scopus 로고
    • Impaired cardiac energetics in mice lacking muscle-specific isoenzymes of creatine kinase
    • Saupe, K. W., Spindler, M., Tian, R. and 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
  • 76
    • 0036073201 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase is critically necessary for normal myocardial high-energy phosphate metabolism
    • Spindler, M., Niebler, R., Remkes, H., Horn, M., Lanz, T. and Neubauer, S. (2002). Mitochondrial creatine kinase is critically necessary for normal myocardial high-energy phosphate metabolism. Am. J. Physiol. 283, H680-H687.
    • (2002) Am. J. Physiol. , vol.283
    • Spindler, M.1    Niebler, R.2    Remkes, H.3    Horn, M.4    Lanz, T.5    Neubauer, S.6
  • 78
    • 0033119723 scopus 로고    scopus 로고
    • A novel role for carbonic anhydrase: Cytoplasmic pH gradient dissipation in mouse small intestinal enterocytes
    • Stewart, A. K., Boyd, C. A. and Vaughan-Jones, R. D. (1999). A novel role for carbonic anhydrase: cytoplasmic pH gradient dissipation in mouse small intestinal enterocytes. J. Physiol. 516, 209-217.
    • (1999) J. Physiol. , vol.516 , pp. 209-217
    • Stewart, A.K.1    Boyd, C.A.2    Vaughan-Jones, R.D.3
  • 79
    • 0031134045 scopus 로고    scopus 로고
    • Carbonic anhydrase and the heart
    • Swenson, E. R. (1997). Carbonic anhydrase and the heart. Cardiologia 42, 453-462.
    • (1997) Cardiologia , vol.42 , pp. 453-462
    • Swenson, E.R.1
  • 80
    • 0034352161 scopus 로고    scopus 로고
    • Genetics of energetics: Transcriptional responses in cardiac metabolism
    • Taegtmeyer, H. (2000). Genetics of energetics: transcriptional responses in cardiac metabolism. Ann. Biomed. Eng. 28, 871-876.
    • (2000) Ann. Biomed. Eng. , vol.28 , pp. 871-876
    • Taegtmeyer, H.1
  • 81
    • 0027418855 scopus 로고
    • Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes
    • Tanabe, T., Yamada, M., Noma, T., Kajii, T. and Nakazawa, A. (1993). Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes. J. Biochem. (Tokyo) 113, 200-207.
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 200-207
    • Tanabe, T.1    Yamada, M.2    Noma, T.3    Kajii, T.4    Nakazawa, A.5
  • 83
    • 0037182850 scopus 로고    scopus 로고
    • The nature and transport mechanism of hydrated hydroxide ions in aqueous solution
    • Tuckerman, M. E., Marx, D. and 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
  • 85
    • 0033561360 scopus 로고    scopus 로고
    • Identification of a novel human adenylate kinase, cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein
    • Van Rompay, A. R., Johansson, M. and Karlsson, A. (1999). Identification of a novel human adenylate kinase, cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein. Eur. J. Biochem. 261, 509-517.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 509-517
    • Van Rompay, A.R.1    Johansson, M.2    Karlsson, A.3
  • 86
    • 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. and 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. 28, 21-40.
    • (1992) Biochem. J. , vol.28 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 87
    • 0026778172 scopus 로고
    • In situ compartmentation of creatine kinase in intact sarcomeric muscle: The acto-myosin overlap zone as a molecular sieve
    • Wegmann, G., Zanolla, E., Eppenberger, H. M. and Wallimann, T. (1992). In situ compartmentation of creatine kinase in intact sarcomeric muscle: the acto-myosin overlap zone as a molecular sieve. J. Muscle Res. Cell. Motil. 13, 420-435.
    • (1992) J. Muscle Res. Cell. Motil. , vol.13 , pp. 420-435
    • Wegmann, G.1    Zanolla, E.2    Eppenberger, H.M.3    Wallimann, T.4
  • 88
    • 0023615778 scopus 로고
    • + channels in isolated guinea pig cardiac myocytes
    • + channels in isolated guinea pig cardiac myocytes. Science 238, 67-69.
    • (1987) Science , vol.238 , pp. 67-69
    • Weiss, J.N.1    Lamp, S.T.2
  • 89
    • 0029924575 scopus 로고    scopus 로고
    • The enzymatic basis of information processing in the living cell
    • Welch, G. R. (1996). The enzymatic basis of information processing in the living cell. Biosystems 38, 147-153.
    • (1996) Biosystems , vol.38 , pp. 147-153
    • Welch, G.R.1
  • 90
    • 0031450906 scopus 로고    scopus 로고
    • Structure, catalysis and supramolecular assembly of adenylate kinase from maize
    • Wild, K., Grafmuller, R., Wagner, E. and Schulz, G. E. (1997). Structure, catalysis and supramolecular assembly of adenylate kinase from maize. Eur. J. Biochem. 250, 326-331.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 326-331
    • Wild, K.1    Grafmuller, R.2    Wagner, E.3    Schulz, G.E.4
  • 91
    • 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. and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.