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Volumn 184, Issue 1-2, 1998, Pages 169-182

Adenylate kinase: Kinetic behavior in intact cells indicates it is integral to multiple cellular processes

Author keywords

18O phosphoryl oxygen exchange; Adenylate kinase; Creatine kinase; Insulin secretion; K(ATP)+ channel; Ligand conduction; Phosphoryl transfer; Regulation of cell energy metabolism

Indexed keywords

ADENINE NUCLEOTIDE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; CREATINE KINASE; INSULIN; ION CHANNEL; POTASSIUM CHANNEL;

EID: 0031680034     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-1-4615-5653-4_13     Document Type: Review
Times cited : (140)

References (68)
  • 3
    • 0026549468 scopus 로고
    • Control of respiration and ATP synthesis in mammalian mitochondria and cells
    • Brown GC: Control of respiration and ATP synthesis in mammalian mitochondria and cells. Biochem J 284: 1-13, 1992
    • (1992) Biochem J , vol.284 , pp. 1-13
    • Brown, G.C.1
  • 4
    • 0024496705 scopus 로고
    • Relation between phosphate metabolites and oxygen consumption of heart in vivo
    • Katz LA, Swain JA, Portman MA, Balaban RS: Relation between phosphate metabolites and oxygen consumption of heart in vivo. Am J Physiol 256: H262-H274, 1989
    • (1989) Am J Physiol , vol.256
    • Katz, L.A.1    Swain, J.A.2    Portman, M.A.3    Balaban, R.S.4
  • 5
    • 0028930129 scopus 로고
    • Adenylate kinase-catalyzed phosphoryl transfer couples ATP utilization with its generation by glycolysis in intact muscle
    • Zeleznikar RJ, Dzeja PP, Goldberg ND: Adenylate kinase-catalyzed phosphoryl transfer couples ATP utilization with its generation by glycolysis in intact muscle. J Biol Chem 270: 7311-7319, 1995
    • (1995) J Biol Chem , vol.270 , pp. 7311-7319
    • Zeleznikar, R.J.1    Dzeja, P.P.2    Goldberg, N.D.3
  • 6
    • 0025216676 scopus 로고
    • + channel activity in intact and permeabilized rat ventricular myocytes
    • + channel activity in intact and permeabilized rat ventricular myocytes. J Physiol 423:91-110, 1990
    • (1990) J Physiol , vol.423 , pp. 91-110
    • Nichols, C.G.1    Lederer, W.J.2
  • 7
    • 8944233359 scopus 로고    scopus 로고
    • Suppression of adenylate kinase catalyzed phosphotransfer precedes and is associated with glucose-induced insulin secretion in intact HIT-T15 cells
    • Olson LK, Schroeder W, Robertson RP, Goldberg ND, Walseth TF: Suppression of adenylate kinase catalyzed phosphotransfer precedes and is associated with glucose-induced insulin secretion in intact HIT-T15 cells. J Biol Chem 271: 16544-16552, 1996
    • (1996) J Biol Chem , vol.271 , pp. 16544-16552
    • Olson, L.K.1    Schroeder, W.2    Robertson, R.P.3    Goldberg, N.D.4    Walseth, T.F.5
  • 9
    • 0029597776 scopus 로고
    • Skeletal muscle - A paradigm for testing principles of bioenergetics
    • Kushmeric MJ: Skeletal muscle - a paradigm for testing principles of bioenergetics. J Bioenerg Biomem 27: 555-569, 1995
    • (1995) J Bioenerg Biomem , vol.27 , pp. 555-569
    • Kushmeric, M.J.1
  • 10
    • 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 HM: Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The 'phosphocreatine circuit' for cellular energy homeostasis. Biochem J 281:21-40, 1992
    • (1992) Biochem J , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 11
    • 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 VA, Khuchua ZA, Vasilyeva EV, Belikova YO, Kuznetsov AV: Metabolic compartmentation and substrate channelling in muscle cells. Role of coupled creatine kinases in in vivo regulation of cellular respiration-a synthesis. Mol Cell Biochem 133/134: 155-192, 1994
    • (1994) Mol Cell Biochem , vol.133-134 , pp. 155-192
    • Saks, V.A.1    Khuchua, Z.A.2    Vasilyeva, E.V.3    Belikova, Y.O.4    Kuznetsov, A.V.5
  • 12
    • 17544373377 scopus 로고    scopus 로고
    • Suppression of creatine kinasecatalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle
    • Dzeja PP, Zeleznikar RJ, Goldberg ND: Suppression of creatine kinasecatalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle. J Biol Chem 271: 12847-12851, 1996
    • (1996) J Biol Chem , vol.271 , pp. 12847-12851
    • Dzeja, P.P.1    Zeleznikar, R.J.2    Goldberg, N.D.3
  • 13
    • 2642693511 scopus 로고
    • Enzyme organization in vivo: Thermodynamickinetic perspectives
    • PA Sere, RW Estabrook (eds). Academic Press, New York
    • Welch GR, DeMoss JA: Enzyme organization in vivo: Thermodynamickinetic perspectives. In: PA Sere, RW Estabrook (eds). Microenvironments and Metabolic Compartmentation. Academic Press, New York, 1978, pp 323-344
    • (1978) Microenvironments and Metabolic Compartmentation , pp. 323-344
    • Welch, G.R.1    DeMoss, J.A.2
  • 14
    • 0026406806 scopus 로고
    • Biochemical topology: From vectorial metabolism to morphogenesis
    • Harold FM: Biochemical topology: from vectorial metabolism to morphogenesis. Biosc Rep 11: 347-385, 1991
    • (1991) Biosc Rep , vol.11 , pp. 347-385
    • Harold, F.M.1
  • 15
    • 0027366579 scopus 로고
    • The cell-bag of enzymes or network of channels?
    • Mathews CK: The cell-bag of enzymes or network of channels? J Bacteriol 175: 6377-6381, 1993
    • (1993) J Bacteriol , vol.175 , pp. 6377-6381
    • Mathews, C.K.1
  • 16
    • 0023902409 scopus 로고
    • Regulation of cyclic GMP metabolism in toad photoreceptors. Definition of the metabolic events subserving photoexcited and attenuated states
    • Dawis SM, Graeff RM, Heyman RA, Walseth TF, Goldberg ND: Regulation of cyclic GMP metabolism in toad photoreceptors. Definition of the metabolic events subserving photoexcited and attenuated states. J Biol Chem 263: 8771-8785, 1988
    • (1988) J Biol Chem , vol.263 , pp. 8771-8785
    • Dawis, S.M.1    Graeff, R.M.2    Heyman, R.A.3    Walseth, T.F.4    Goldberg, N.D.5
  • 17
    • 0025191301 scopus 로고
    • Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle
    • Zeleznikar RJ, Heyman RA, Graeff RM, Walseth TF, Dawis SM, Butz EA, Goldberg ND: Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle. J Biol Chem 265:300-311, 1990
    • (1990) J Biol Chem , vol.265 , pp. 300-311
    • Zeleznikar, R.J.1    Heyman, R.A.2    Graeff, R.M.3    Walseth, T.F.4    Dawis, S.M.5    Butz, E.A.6    Goldberg, N.D.7
  • 18
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shuttle
    • Bessman SP, Carpenter CL: The creatine-creatine phosphate energy shuttle. Annu Rev Biochem 54: 831-862, 1985
    • (1985) Annu Rev Biochem , vol.54 , pp. 831-862
    • Bessman, S.P.1    Carpenter, C.L.2
  • 19
    • 0021999606 scopus 로고
    • The effect of adenylate kinase activity on the rate and efficiency of energy transport from mitochondria to hexokinase
    • Dzeja P, Kalvenas A, ToleikisA, PraskeviciusA: The effect of adenylate kinase activity on the rate and efficiency of energy transport from mitochondria to hexokinase. Biochem Int 10:259-265, 1985
    • (1985) Biochem Int , vol.10 , pp. 259-265
    • Dzeja, P.1    Kalvenas, A.2    ToleikisA3    PraskeviciusA4
  • 20
    • 0024535905 scopus 로고
    • Adenylate kinase activity in ejaculated bovine sperm flagella
    • Schoff PK, Cheetham J, Lardy HA: Adenylate kinase activity in ejaculated bovine sperm flagella. J Biol Chem 264:6086-6091, 1989
    • (1989) J Biol Chem , vol.264 , pp. 6086-6091
    • Schoff, P.K.1    Cheetham, J.2    Lardy, H.A.3
  • 21
    • 0026517684 scopus 로고
    • The role of adenylate kinase in dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space
    • Gellerich FN: The role of adenylate kinase in dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space. FEBS Lett 297: 55-58, 1992
    • (1992) FEBS Lett , vol.297 , pp. 55-58
    • Gellerich, F.N.1
  • 23
    • 0026406805 scopus 로고
    • Foundations of vectorial metabolism and osmochemistry
    • Mitchell P: Foundations of vectorial metabolism and osmochemistry. Biosci Rep 11: 297-346, 1991
    • (1991) Biosci Rep , vol.11 , pp. 297-346
    • Mitchell, P.1
  • 24
    • 0001542971 scopus 로고
    • The role of myokinase in transphosphorylations. 1. the enzymatic phosphorylation of hexoses by adenyl pyrophosphate
    • Colowick SP, Kalckar HM: The role of myokinase in transphosphorylations. 1. The enzymatic phosphorylation of hexoses by adenyl pyrophosphate. J Biol Chem 148: 117-126, 1943
    • (1943) J Biol Chem , vol.148 , pp. 117-126
    • Colowick, S.P.1    Kalckar, H.M.2
  • 25
    • 70349640265 scopus 로고
    • Adenylate kinase
    • PD Boyer (ed). Academic Press, New York
    • Noda LH: Adenylate kinase. In: PD Boyer (ed). The Enzymes, 3rd ed, vol 8. Academic Press, New York, 1973, pp 279-305
    • (1973) The Enzymes, 3rd Ed , vol.8 , pp. 279-305
    • Noda, L.H.1
  • 26
    • 0014353859 scopus 로고
    • The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers
    • Atkinson DE: The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers. Biochemistry 7: 4030-4034, 1968
    • (1968) Biochemistry , vol.7 , pp. 4030-4034
    • Atkinson, D.E.1
  • 27
    • 0027716645 scopus 로고
    • Meaning of energetic parameters
    • Kammermeier H: Meaning of energetic parameters. Basic Res Cardiol 88: 380-384, 1993
    • (1993) Basic Res Cardiol , vol.88 , pp. 380-384
    • Kammermeier, H.1
  • 28
    • 0013820392 scopus 로고
    • On the mechanism of muscular contraction
    • Davies RE: On the mechanism of muscular contraction. Essays Biochem 1: 29-55, 1965
    • (1965) Essays Biochem , vol.1 , pp. 29-55
    • Davies, R.E.1
  • 29
    • 0015053709 scopus 로고
    • Relationship of ATP: AMP phosphotransferase isozymes to tissue respiration
    • Criss WE: Relationship of ATP: AMP phosphotransferase isozymes to tissue respiration. Arch Biochem Biophys 144: 138-142, 1971
    • (1971) Arch Biochem Biophys , vol.144 , pp. 138-142
    • Criss, W.E.1
  • 30
    • 0027418855 scopus 로고
    • Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isoenzymes
    • Tanabe T, Yamada M, Noma T, Kajii T, Nakazawa A: Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isoenzymes. J Biochem 113: 200-207, 1993
    • (1993) J Biochem , vol.113 , pp. 200-207
    • Tanabe, T.1    Yamada, M.2    Noma, T.3    Kajii, T.4    Nakazawa, A.5
  • 31
    • 0028030901 scopus 로고
    • Interaction of creatine kinase and adenylate kinase systems in muscle cells
    • Savabi F: Interaction of creatine kinase and adenylate kinase systems in muscle cells. Mol Cell Biochem 133/134: 145-152, 1994
    • (1994) Mol Cell Biochem , vol.133-134 , pp. 145-152
    • Savabi, F.1
  • 34
    • 0022298736 scopus 로고
    • Theoretical support for the heart phosphocreatine energy transport shuttle based on the intracellular diffusion limited mobility of ADP
    • Jacobus WE: Theoretical support for the heart phosphocreatine energy transport shuttle based on the intracellular diffusion limited mobility of ADP. Biochem Biophys Res Commun 133: 1035-1041, 1985
    • (1985) Biochem Biophys Res Commun , vol.133 , pp. 1035-1041
    • Jacobus, W.E.1
  • 36
    • 0026778659 scopus 로고
    • Product inhibition of the actomyosin subfragment-1 ATPase in skeletal, cardiac, and smooth muscle
    • Drew JS, Harwalkar VA, Stein LA: Product inhibition of the actomyosin subfragment-1 ATPase in skeletal, cardiac, and smooth muscle. Circ Res 71: 1067-1077, 1992
    • (1992) Circ Res , vol.71 , pp. 1067-1077
    • Drew, J.S.1    Harwalkar, V.A.2    Stein, L.A.3
  • 37
    • 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, Oechner U, Magdolen V: Yeast adenylate kinase is active simultaneously in mitochondria and cytoplasm and is required for non-fermentative growth. Eur J Biochem 178:451-457, 1988
    • (1988) Eur J Biochem , vol.178 , pp. 451-457
    • Bandlow, W.1    Strobel, G.2    Zoglowek, C.3    Oechner, U.4    Magdolen, V.5
  • 38
    • 0027178212 scopus 로고
    • ATP binding to cytochromec diminishes electron flow in the mitochondrial respiratory pathway
    • Craig DB, Wallace CJ: ATP binding to cytochromec diminishes electron flow in the mitochondrial respiratory pathway. Prot Sci 2: 966-976, 1993
    • (1993) Prot Sci , vol.2 , pp. 966-976
    • Craig, D.B.1    Wallace, C.J.2
  • 41
    • 0001236342 scopus 로고
    • Cation dynamics and diffusion in lithium orthosilicate: Two-dimensional lithium-6 NMR
    • Xu Z, Stebbins JF: Cation dynamics and diffusion in lithium orthosilicate: two-dimensional lithium-6 NMR. Science 270: 1332-1334, 1995
    • (1995) Science , vol.270 , pp. 1332-1334
    • Xu, Z.1    Stebbins, J.F.2
  • 42
    • 0345613372 scopus 로고
    • Molecular mechanisms for proton transport in membranes
    • Nagle JF, Morowitz HJ: Molecular mechanisms for proton transport in membranes. Proc Natl Acad Sci USA 75:289-302, 1978
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 289-302
    • Nagle, J.F.1    Morowitz, H.J.2
  • 43
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Sere P: Complexes of sequential metabolic enzymes. Ann Rev Biochem 56: 89-124, 1987
    • (1987) Ann Rev Biochem , vol.56 , pp. 89-124
    • Sere, P.1
  • 44
    • 0026778172 scopus 로고
    • In situ compartmentation of creatine kinase in intact sarcomeric muscle: The actomyosin overlap zone as a molecular sieve
    • Wegmann G, Zanolla E, Eppenberger HM, Wallimann T: In situ compartmentation of creatine kinase in intact sarcomeric muscle: The actomyosin overlap zone as a molecular sieve. J Muscle Res Cell Motil 13: 420-435, 1992
    • (1992) J Muscle Res Cell Motil , vol.13 , pp. 420-435
    • Wegmann, G.1    Zanolla, E.2    Eppenberger, H.M.3    Wallimann, T.4
  • 45
    • 0023353449 scopus 로고
    • Analysis of compartmentation of ATP in skeletal and cardiac muscle using P nuclear magnetic resonance saturation transfer
    • Zahler R, Bittl JA, Ingwall J: Analysis of compartmentation of ATP in skeletal and cardiac muscle using P nuclear magnetic resonance saturation transfer. Biophys J 51: 883-893, 1987
    • (1987) Biophys J , vol.51 , pp. 883-893
    • Zahler, R.1    Bittl, J.A.2    Ingwall, J.3
  • 46
    • 0026037225 scopus 로고
    • Whole-organ enzymology of creatine kinase system in heart
    • Ingwal JS: Whole-organ enzymology of creatine kinase system in heart. Biochem Soc Trans 19: 1006-1010, 1991
    • (1991) Biochem Soc Trans , vol.19 , pp. 1006-1010
    • Ingwal, J.S.1
  • 47
    • 0018422127 scopus 로고
    • 31P NMR studies of the intact human red blood cell
    • 31P NMR studies of the intact human red blood cell. Biochim Biophys Acta 586: 189-195, 1979
    • (1979) Biochim Biophys Acta , vol.586 , pp. 189-195
    • Gupta, R.K.1
  • 49
    • 0029665566 scopus 로고    scopus 로고
    • P-31-NMR-measured creatine reaction flux inmuscle-a caveat
    • WallimannT: P-31-NMR-measured creatine reaction flux inmuscle-a caveat. J Muscle Res Cell Mot 17: 177-181, 1996
    • (1996) J Muscle Res Cell Mot , vol.17 , pp. 177-181
    • WallimannT1
  • 50
    • 0001877146 scopus 로고
    • An allosteric enzyme model with positive feedback applied to glycolytic oscillations
    • Goldbeter A, Nicolis G: An allosteric enzyme model with positive feedback applied to glycolytic oscillations. Progr Theor Biol 4: 65-160, 1976
    • (1976) Progr Theor Biol , vol.4 , pp. 65-160
    • Goldbeter, A.1    Nicolis, G.2
  • 52
    • 0025300438 scopus 로고
    • Properties and functions of ATP-sensitive K-channels
    • Ashcroft SJH, Ashcroft FM: Properties and functions of ATP-sensitive K-channels. Cell Signal 2: 197-214, 1990
    • (1990) Cell Signal , vol.2 , pp. 197-214
    • Ashcroft, S.J.H.1    Ashcroft, F.M.2
  • 53
    • 0029164287 scopus 로고
    • The ABC of channel regulation
    • Higgins CF: The ABC of channel regulation. Cell 82:693-696, 1995
    • (1995) Cell , vol.82 , pp. 693-696
    • Higgins, C.F.1
  • 54
    • 0029995952 scopus 로고    scopus 로고
    • + channels: Generating excitement in pancreatic beta-cells
    • + channels: Generating excitement in pancreatic beta-cells. Diabetes 45: 845-853, 1996
    • (1996) Diabetes , vol.45 , pp. 845-853
    • Dukes, I.D.1    Philipson, L.H.2
  • 55
    • 0028822992 scopus 로고
    • Structural and functional similarities between the nucleotide-binding domains of CFTR and GTP-binding proteins
    • Carson MR, Welsh MJ: Structural and functional similarities between the nucleotide-binding domains of CFTR and GTP-binding proteins. Biophys J 69: 2443-2448, 1995
    • (1995) Biophys J , vol.69 , pp. 2443-2448
    • Carson, M.R.1    Welsh, M.J.2
  • 56
    • 0018168846 scopus 로고
    • Adenosine triphosphatases of rat pancreatic islets: Comparison with those of rat kidney
    • Levin SR, Kasson BG, Driessen JF: Adenosine triphosphatases of rat pancreatic islets: comparison with those of rat kidney. J Clin Invest 62: 692-701, 1978
    • (1978) J Clin Invest , vol.62 , pp. 692-701
    • Levin, S.R.1    Kasson, B.G.2    Driessen, J.F.3
  • 58
    • 0017435456 scopus 로고
    • The role of compartmentation in the control of glycolysis
    • Ottaway JH, Mowbray J: The role of compartmentation in the control of glycolysis. Curr Top Cell Regul 12: 107-208, 1977
    • (1977) Curr Top Cell Regul , vol.12 , pp. 107-208
    • Ottaway, J.H.1    Mowbray, J.2
  • 59
    • 0022536461 scopus 로고
    • Intracellular localization of ATP: AMP phosphotransferase in Escherchia coli
    • Watanabe K, Fukumoto H, Isoi K: Intracellular localization of ATP: AMP phosphotransferase in Escherchia coli. Biochem Biophys Res Commun 134: 527-531, 1986
    • (1986) Biochem Biophys Res Commun , vol.134 , pp. 527-531
    • Watanabe, K.1    Fukumoto, H.2    Isoi, K.3
  • 60
    • 0024418297 scopus 로고
    • Rat brain synaptosomal ATP: AMP-phosphotransferase activity
    • Nagy AK, Shuster TA, Delgado-Escueta AV: Rat brain synaptosomal ATP: AMP-phosphotransferase activity. J Neurochem 53: 1166-1172, 1989
    • (1989) J Neurochem , vol.53 , pp. 1166-1172
    • Nagy, A.K.1    Shuster, T.A.2    Delgado-Escueta, A.V.3
  • 61
    • 0027340688 scopus 로고
    • ATP channel by ADP and diazoxide requires nucleotide hydrolysis in mouse pancreatic β-cells
    • ATP channel by ADP and diazoxide requires nucleotide hydrolysis in mouse pancreatic β-cells. J Physiol 463: 349-365, 1993
    • (1993) J Physiol , vol.463 , pp. 349-365
    • Larsson, O.1    Ammala, C.2    Bokvist, K.3    Fredholm, B.4    Rorsman, P.5
  • 62
    • 0028785948 scopus 로고
    • +-activated channel present in rat cortical neurones
    • +-activated channel present in rat cortical neurones. J Physiol 488:319-337, 1995
    • (1995) J Physiol , vol.488 , pp. 319-337
    • Lee, K.1    Rowe, I.C.M.2    Ashford, M.W.3
  • 63
    • 0026437322 scopus 로고
    • Control of CFTR chloride conductance by ATP levels through non-hydrolytic binding
    • Quinton PM, Reddy MM: Control of CFTR chloride conductance by ATP levels through non-hydrolytic binding. Nature 360: 79-81, 1992
    • (1992) Nature , vol.360 , pp. 79-81
    • Quinton, P.M.1    Reddy, M.M.2
  • 64
    • 0028835463 scopus 로고
    • Isolation and characterization of adenylate kinase (ADK) mutations in Salmonella typhimurium which block the ability of glycine betaine to function as an osmoprotectant
    • Gutierrez JA, Csonka LN: Isolation and characterization of adenylate kinase (ADK) mutations in Salmonella typhimurium which block the ability of glycine betaine to function as an osmoprotectant. J Bacteriol 177: 390-400, 1995
    • (1995) J Bacteriol , vol.177 , pp. 390-400
    • Gutierrez, J.A.1    Csonka, L.N.2
  • 65
    • 33646299823 scopus 로고    scopus 로고
    • Creatine phosphate turnover in skeletal muscles of M-CK, ScCKmit and MCK/ ScCKmit deficient mice
    • Dzeja P, Noronha L, Zeleznikar R, Wieringa B, Goldberg N: Creatine phosphate turnover in skeletal muscles of M-CK, ScCKmit and MCK/ ScCKmit deficient mice. FASEB J 10: LB114, 1996
    • (1996) FASEB J , vol.10
    • Dzeja, P.1    Noronha, L.2    Zeleznikar, R.3    Wieringa, B.4    Goldberg, N.5
  • 66
    • 0025971079 scopus 로고
    • Modulation of hexokinase association with mitochondria analyzed with quantitative three-dimensional cofocal microscopy
    • Lynch RM, Fogarty KE, Fay FS: Modulation of hexokinase association with mitochondria analyzed with quantitative three-dimensional cofocal microscopy. J Cell Biol 112: 385-395, 1991
    • (1991) J Cell Biol , vol.112 , pp. 385-395
    • Lynch, R.M.1    Fogarty, K.E.2    Fay, F.S.3
  • 68
    • 0028781629 scopus 로고
    • i → ATP flux in lamb myocardium in vivo
    • i → ATP flux in lamb myocardium in vivo. Biochim Biophys Acta 1185: 221-227, 1994
    • (1994) Biochim Biophys Acta , vol.1185 , pp. 221-227
    • Portman, M.A.1


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