메뉴 건너뛰기




Volumn 12, Issue 7, 1998, Pages 523-529

Phosphotransfer reactions in the regulation of ATP-sensitive K+ channels

Author keywords

Adenylate kinase; Creatine kinase; Glycolysis; K(ATP) channel; Metabolic signaling; Pyruvate kinase

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; POTASSIUM CHANNEL; PYRUVATE KINASE;

EID: 0031918019     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.12.7.523     Document Type: Review
Times cited : (136)

References (72)
  • 1
    • 0025300438 scopus 로고
    • Properties and functions of ATP-sensitive K-channels
    • Ashcroft, S. J. H., and Ashcroft, F. M. (1990) Properties and functions of ATP-sensitive K-channels. Cell Signal. 2, 197-214
    • (1990) Cell Signal. , vol.2 , pp. 197-214
    • Ashcroft, S.J.H.1    Ashcroft, F.M.2
  • 2
    • 0026344826 scopus 로고
    • Adenosine triphosphate-sensitive potassium channels in the cardiovascular system
    • Nichols, C. G., and Lederer, W. J. (1991) Adenosine triphosphate-sensitive potassium channels in the cardiovascular system. Am. J. Physiol. 261, H1675-H1686
    • (1991) Am. J. Physiol. , vol.261
    • Nichols, C.G.1    Lederer, W.J.2
  • 3
    • 0028036988 scopus 로고
    • ATP-sensitive potassium channels: An overview
    • Lazdunski, M. (1994) ATP-sensitive potassium channels: an overview. J. Cardiovasc. Pharmacol. 24, S1-S5
    • (1994) J. Cardiovasc. Pharmacol. , vol.24
    • Lazdunski, M.1
  • 4
    • 0028873314 scopus 로고
    • Cardiac ATPsensitive K+ channels: Regulation by intracellular nucleotides and K+ channel-opening drugs
    • Terzic, A., Jahangir, A., and Kurachi, Y. (1995) Cardiac ATPsensitive K+ channels: Regulation by intracellular nucleotides and K+ channel-opening drugs. Am. J. Physiol. 269, C525-C545
    • (1995) Am. J. Physiol. , vol.269
    • Terzic, A.1    Jahangir, A.2    Kurachi, Y.3
  • 5
    • 0030036875 scopus 로고    scopus 로고
    • Molecular biology of the β-cell ATP-sensitive K+ channel
    • Seino, S., Inagaki, N., Namba, N., and Gonoi, T. (1996) Molecular biology of the β-cell ATP-sensitive K+ channel. Diabetes Rev. 4, 177-190
    • (1996) Diabetes Rev. , vol.4 , pp. 177-190
    • Seino, S.1    Inagaki, N.2    Namba, N.3    Gonoi, T.4
  • 6
    • 0030747393 scopus 로고    scopus 로고
    • The ABCs of ATP-sensitive potassium channels: More pieces of the puzzle
    • Bryan, J., and Aguilar-Bryan, L. (1997) The ABCs of ATP-sensitive potassium channels: more pieces of the puzzle. Curr. Opin. Cell Biol. 9, 553-559
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 553-559
    • Bryan, J.1    Aguilar-Bryan, L.2
  • 7
    • 0027987085 scopus 로고
    • Interactive regulation of the ATP-sensitive potassium channel of cardiac muscle
    • Findlay, I. (1994) Interactive regulation of the ATP-sensitive potassium channel of cardiac muscle. J. Cardiovasc. Pharmacol. 24, S6-S11
    • (1994) J. Cardiovasc. Pharmacol. , vol.24
    • Findlay, I.1
  • 9
    • 0030907755 scopus 로고    scopus 로고
    • The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide
    • Gribble, F. M., Tucker, S. J., and Ashcroft, F. M. (1997) The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide. EMBO J. 16, 1145-1152
    • (1997) EMBO J. , vol.16 , pp. 1145-1152
    • Gribble, F.M.1    Tucker, S.J.2    Ashcroft, F.M.3
  • 12
    • 0029898253 scopus 로고    scopus 로고
    • A family of sulfonylurea re-. ceptors determines the properties of ATP-sensitive K+ channels
    • Inagaki, N., Gonoi, T., Clement, J. P., Wang, C. Z., Aguilar-Bryan, L., Bryan, J., and Seino, S. (1996) A family of sulfonylurea re-. ceptors determines the properties of ATP-sensitive K+ channels. Neuron 16, 1011-1017
    • (1996) Neuron , vol.16 , pp. 1011-1017
    • Inagaki, N.1    Gonoi, T.2    Clement, J.P.3    Wang, C.Z.4    Aguilar-Bryan, L.5    Bryan, J.6    Seino, S.7
  • 15
    • 0030980845 scopus 로고    scopus 로고
    • Subunit stoichiometry of the pancreatic beta-cell ATP-sensitive K+ channel
    • Inagaki, N., Gonoi, T., and Seino, S. (1997) Subunit stoichiometry of the pancreatic beta-cell ATP-sensitive K+ channel. FEBS Lett. 409, 232-236
    • (1997) FEBS Lett. , vol.409 , pp. 232-236
    • Inagaki, N.1    Gonoi, T.2    Seino, S.3
  • 16
    • 0031005755 scopus 로고    scopus 로고
    • Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor
    • Tucker, S. J., Gribble, F. M., Zhao, C., Trapp, S., and Ashcroft, F. M. (1997) Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor. Nature (London) 387, 179-183
    • (1997) Nature (London) , vol.387 , pp. 179-183
    • Tucker, S.J.1    Gribble, F.M.2    Zhao, C.3    Trapp, S.4    Ashcroft, F.M.5
  • 18
    • 0030747115 scopus 로고    scopus 로고
    • Burst kinetics of co-expressed Kir6.2/SUR1 clones: Comparison of recombinant with native ATP-sensitive K+ channel behavior
    • Alekseev, A. E., Kennedy, M. E., Navarro, B., and Terzic, A. (1997) Burst kinetics of co-expressed Kir6.2/SUR1 clones: Comparison of recombinant with native ATP-sensitive K+ channel behavior. J. Membr. Biol. 159, 161-168
    • (1997) J. Membr. Biol. , vol.159 , pp. 161-168
    • Alekseev, A.E.1    Kennedy, M.E.2    Navarro, B.3    Terzic, A.4
  • 19
    • 0031935902 scopus 로고    scopus 로고
    • Evidence for direct physical association between a K+ channel (Kir6.2) and an ABC protein (SUR1) which affects cellular distribution and kinetic behavior of an ATP-sensitive K+ channel
    • In press
    • Lorenz, L., Alekseev, A. E., Krapivinsky, G. B., Carrasco, A. J., Clapham, D. E., and Terzic, A. (1998) Evidence for direct physical association between a K+ channel (Kir6.2) and an ABC protein (SUR1) which affects cellular distribution and kinetic behavior of an ATP-sensitive K+ channel. Mol. Cell. Biol. In press
    • (1998) Mol. Cell. Biol.
    • Lorenz, L.1    Alekseev, A.E.2    Krapivinsky, G.B.3    Carrasco, A.J.4    Clapham, D.E.5    Terzic, A.6
  • 20
    • 0030611865 scopus 로고    scopus 로고
    • 2+-independent ATP binding of the sulfonylurea receptor SUR1
    • 2+-independent ATP binding of the sulfonylurea receptor SUR1. J. Biol. Chem. 272, 22983-22986
    • (1997) J. Biol. Chem. , vol.272 , pp. 22983-22986
    • Ueda, K.1    Inagaki, N.2    Seino, S.3
  • 22
    • 85047680360 scopus 로고
    • Nucleotide regulation of ATP sensitive potassium channels
    • Terzic, A., Tung, R. T., and Kurachi, Y. (1994) Nucleotide regulation of ATP sensitive potassium channels. Cardiovasc. Res. 28, 746-753
    • (1994) Cardiovasc. Res. , vol.28 , pp. 746-753
    • Terzic, A.1    Tung, R.T.2    Kurachi, Y.3
  • 25
    • 0030067124 scopus 로고    scopus 로고
    • A lesson in metabolic regulation inspired by the glucosesensor paradigm
    • Matschinsky, F. M. (1996) A lesson in metabolic regulation inspired by the glucosesensor paradigm. Diabetes 45, 223-241
    • (1996) Diabetes , vol.45 , pp. 223-241
    • Matschinsky, F.M.1
  • 26
    • 0030867470 scopus 로고    scopus 로고
    • Roleof ATP and Pi in the mechanism of insulin secretion in the mouse insulinoma (TC3) cell line
    • Papas, K. K., Long, R. C., Jr., Constantinadis, J., and Sambanis, A. (1997) Roleof ATP and Pi in the mechanism of insulin secretion in the mouse insulinoma (TC3) cell line. Biochem. J. 326, 807-814
    • (1997) Biochem. J. , vol.326 , pp. 807-814
    • Papas, K.K.1    Long Jr., R.C.2    Constantinadis, J.3    Sambanis, A.4
  • 28
    • 0030747295 scopus 로고    scopus 로고
    • Hypoxia-induced inhibition of adenosine kinase potentiates cardiac adenosine release
    • Decking, U. K., Schlieper, G., Kroll, K., and Schrader, J. (1997) Hypoxia-induced inhibition of adenosine kinase potentiates cardiac adenosine release. Circ. Res. 81, 154-164
    • (1997) Circ. Res. , vol.81 , pp. 154-164
    • Decking, U.K.1    Schlieper, G.2    Kroll, K.3    Schrader, J.4
  • 29
    • 0028885706 scopus 로고
    • Possible links between glucose-induced changes in the energy state of pancreatic β-cells and insulin release
    • Detimary, P., Jonas, J. C., and Henquin, J. C. (1995) Possible links between glucose-induced changes in the energy state of pancreatic β-cells and insulin release. J. Clin. Invest. 96, 1738-1745
    • (1995) J. Clin. Invest. , vol.96 , pp. 1738-1745
    • Detimary, P.1    Jonas, J.C.2    Henquin, J.C.3
  • 31
    • 0029833117 scopus 로고    scopus 로고
    • Stable and diffusible pools of nucleotides in pancreatic islet cells
    • Detimary, P., Jonas, J. C., and Henquin, J. C. (1996) Stable and diffusible pools of nucleotides in pancreatic islet cells. Endocrinology 137, 4671-4676
    • (1996) Endocrinology , vol.137 , pp. 4671-4676
    • Detimary, P.1    Jonas, J.C.2    Henquin, J.C.3
  • 33
    • 0018741768 scopus 로고
    • The stimulus-secretion coupling of glucose-induced insulin release. the links between metabolism and cationic events
    • Malaisse, W. J., Hutton, J. C., Kawazu, S., Herchulez, A.,Valverde, J., and Sener, A. (1979) The stimulus-secretion coupling of glucose-induced insulin release. The links between metabolism and cationic events. Diabetologia 16, 331-341
    • (1979) Diabetologia , vol.16 , pp. 331-341
    • Malaisse, W.J.1    Hutton, J.C.2    Kawazu, S.3    Herchulez, A.4    Valverde, J.5    Sener, A.6
  • 34
    • 0023152575 scopus 로고
    • Glucose-induced changes in cytosolic ATP content in pancreatic islets
    • Malaise, W. J., and Sener, A. (1987) Glucose-induced changes in cytosolic ATP content in pancreatic islets. Biochim. Biophys. Acta 927, 190-195
    • (1987) Biochim. Biophys. Acta , vol.927 , pp. 190-195
    • Malaise, W.J.1    Sener, A.2
  • 35
    • 0026333684 scopus 로고
    • The role of ATP and free ADP in metabolic coupling during fuel-stimulated insulin release from islet β-cells in the isolated perfused rat pancreas
    • Ghosh, A., Ronner, P., Cheong, E., Khalid, P., and Matschinsky, F. M. (1991) The role of ATP and free ADP in metabolic coupling during fuel-stimulated insulin release from islet β-cells in the isolated perfused rat pancreas. J. Biol. Chem. 266, 22887-22892
    • (1991) J. Biol. Chem. , vol.266 , pp. 22887-22892
    • Ghosh, A.1    Ronner, P.2    Cheong, E.3    Khalid, P.4    Matschinsky, F.M.5
  • 36
    • 8944233359 scopus 로고    scopus 로고
    • Suppression of adenylate kinase catalyzed phosphotransfer precedes and is associated with glucoseinduced insulin secretion in intact HIT-T15 cells
    • Olson, L. K., Schroeder, W., Robertson, R. P., Goldberg, N. D., and Walseth, T. F. (1996) Suppression of adenylate kinase catalyzed phosphotransfer precedes and is associated with glucoseinduced insulin secretion in intact HIT-T15 cells. J. Biol. Chem. 271, 16544-16552
    • (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
  • 37
    • 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. , vol.133-134 , pp. 155-192
    • Saks, V.A.1    Khuchua, Z.A.2    Vasilyeva, E.V.3    Belikova, O.Y.4    Kuznetsov, A.V.5
  • 38
    • 0028930129 scopus 로고
    • Adenylate kinase-catalyzed phosphoryl transfer couples ATP utiliza- Tion 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 utiliza- tion 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
  • 39
    • 0030595328 scopus 로고    scopus 로고
    • Signal transduction via the multi-step phosphorelay: Not necessarily a road less traveled
    • Appleby, J. L., Parkinson, J. S., and Bourret, R. B. (1996) Signal transduction via the multi-step phosphorelay: not necessarily a road less traveled. Cell 86, 845-848
    • (1996) Cell , vol.86 , pp. 845-848
    • Appleby, J.L.1    Parkinson, J.S.2    Bourret, R.B.3
  • 40
    • 0027715423 scopus 로고
    • Mode-switching of a voltage-gated cation channel is mediated by a protein kinase A-regulated tyrosine phosphatase
    • Wilson, G. F., and Kaczmarek, L. K. (1993) Mode-switching of a voltage-gated cation channel is mediated by a protein kinase A-regulated tyrosine phosphatase. Nature (London) 366, 433-438
    • (1993) Nature (London) , vol.366 , pp. 433-438
    • Wilson, G.F.1    Kaczmarek, L.K.2
  • 42
    • 0024444850 scopus 로고
    • + Channels. Evidence for preferential regulation by glycolysis
    • + Channels. Evidence for preferential regulation by glycolysis. J. Gen. Physiol. 94, 911-935
    • (1989) J. Gen. Physiol. , vol.94 , pp. 911-935
    • Weiss, J.N.1    Lamp, S.T.2
  • 44
    • 0031680034 scopus 로고    scopus 로고
    • Adenylate kinase: Kinetic behavior in intact cells indicates it is integral to multiple cellular processes
    • In press
    • Dzeja, 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. In press
    • (1998) Mol. Cell. Biochem.
    • Dzeja, P.1    Zeleznikar, R.J.2    Goldberg, N.D.3
  • 45
    • 0016216009 scopus 로고
    • Adenylate kinase of porcine heart
    • Kubo, S., and Noda, L. H. (1974) Adenylate kinase of porcine heart. Eur. J. Bioch. 48, 325-331
    • (1974) Eur. J. Bioch. , vol.48 , pp. 325-331
    • Kubo, S.1    Noda, L.H.2
  • 46
    • 0019978430 scopus 로고
    • Informational aspects of Gibbs function output from nucleotide pools and of the adenylate kinase reaction
    • Kremen, A. (1982) Informational aspects of Gibbs function output from nucleotide pools and of the adenylate kinase reaction. J. Theor. Biol. 96, 425-441
    • (1982) J. Theor. Biol. , vol.96 , pp. 425-441
    • Kremen, A.1
  • 47
    • 0023224335 scopus 로고
    • The adenylate kinase reaction acts as a frequency filter towards fluctuations of ATP utilization in the cell
    • Veuthey, A. L., and Stucki, J. (1987) The adenylate kinase reaction acts as a frequency filter towards fluctuations of ATP utilization in the cell. Biophys. Chem. 26, 19-28
    • (1987) Biophys. Chem. , vol.26 , pp. 19-28
    • Veuthey, A.L.1    Stucki, J.2
  • 48
    • 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. 113, 200-207
    • (1993) J. Biochem. , vol.113 , pp. 200-207
    • Tanabe, T.1    Yamada, M.2    Noma, T.3    Kajii, T.4    Nakazawa, A.5
  • 49
    • 17544373377 scopus 로고    scopus 로고
    • Suppression ofcreatine kinase-catalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle
    • Dzeja, P. P., Zeleznikar, R. J., and Goldberg, N. D. (1996) Suppression ofcreatine kinase-catalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle. J. Biol. Chem. 271, 12847-12851
    • (1996) J. Biol. Chem. , vol.271 , pp. 12847-12851
    • Dzeja, P.P.1    Zeleznikar, R.J.2    Goldberg, N.D.3
  • 50
    • 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., Toleikis, A., and Praskevicius, A. (1985) The effect of adenylate kinase activity on the rate and efficiency of energy transport from mitochondria to hexokinase. Biochem. Int. 10, 259-265
    • (1985) Biochem. Int. , vol.10 , pp. 259-265
    • Dzeja, P.1    Kalvenas, A.2    Toleikis, A.3    Praskevicius, A.4
  • 52
    • 2642697625 scopus 로고
    • Changes in adenylate kinase isoenzyme activity in ischemic rabbit heart
    • Vitkevicius, K., and Dzeja, P. (1990) Changes in adenylate kinase isoenzyme activity in ischemic rabbit heart. Byull. Eksp. Biol. Med. 110, 1039-1040
    • (1990) Byull. Eksp. Biol. Med. , vol.110 , pp. 1039-1040
    • Vitkevicius, K.1    Dzeja, P.2
  • 53
    • 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, J. A., and Csonka, L. N. (1995) 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) J. Bacteriol , vol.177 , pp. 390-400
    • Gutierrez, J.A.1    Csonka, L.N.2
  • 54
    • 0030806301 scopus 로고    scopus 로고
    • A recombinant polypeptide model of the second nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator functions as an active ATPase, GTPase and adenylate kinase
    • Randak, C., Neth, P., Auerswald, E. A., Eckerskorn, C., Assfalgmachleidt, J., and Machleidt, W. (1997) A recombinant polypeptide model of the second nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator functions as an active ATPase, GTPase and adenylate kinase. fEBS Lett. 410,180-186
    • (1997) FEBS Lett. , vol.410 , pp. 180-186
    • Randak, C.1    Neth, P.2    Auerswald, E.A.3    Eckerskorn, C.4    Assfalgmachleidt, J.5    Machleidt, W.6
  • 55
    • 0026437322 scopus 로고
    • Control of CFTR chloride conductance by ATP levels through non-hydrolytic binding
    • Quinten, P- M., and Reddy, M. M. (1992) Control of CFTR chloride conductance by ATP levels through non-hydrolytic binding. Nature (London) 360, 79-81
    • (1992) Nature (London) , vol.360 , pp. 79-81
    • Quinten, P.M.1    Reddy, M.M.2
  • 61
    • 0030803791 scopus 로고    scopus 로고
    • Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a trafic ATPase (ABC transporter)
    • Liu, C. E., Liu, P. Q., and Ames, G. F. L. (1997) Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a trafic ATPase (ABC transporter). J. Biol. Chem. 272, 21883-21891
    • (1997) J. Biol. Chem. , vol.272 , pp. 21883-21891
    • Liu, C.E.1    Liu, P.Q.2    Ames, G.F.L.3
  • 62
    • 0026652559 scopus 로고
    • ATP is a coupling modulator of parallel Na,K-ATPase-K-channel activity in the renal proximal tubule
    • Tsuchiya, R., Wang, W., Giebisch, G., and Welling, P. A. (1992) ATP is a coupling modulator of parallel Na,K-ATPase-K-channel activity in the renal proximal tubule. Proc. Natl. Acad. Sci. USA 89, 6418-6422
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6418-6422
    • Tsuchiya, R.1    Wang, W.2    Giebisch, G.3    Welling, P.A.4
  • 64
    • 0028085284 scopus 로고
    • Effects of glucose and fatty acids on myocardial ischemia and arrhythmias
    • Oliver, M. F., and Opie, L. H. (1994) Effects of glucose and fatty acids on myocardial ischemia and arrhythmias. Lancet 343, 155-158
    • (1994) Lancet , vol.343 , pp. 155-158
    • Oliver, M.F.1    Opie, L.H.2
  • 65
    • 0028284749 scopus 로고
    • A critical period in the development of the insulin secretory response to glucose in fetal rat pancreas
    • Bliss, C. R., and Sharp, G. W. (1994) A critical period in the development of the insulin secretory response to glucose in fetal rat pancreas. Life Sci. 55, 423-427
    • (1994) Life Sci. , vol.55 , pp. 423-427
    • Bliss, C.R.1    Sharp, G.W.2
  • 66
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., Sanders, D. A., and McCormick, F. (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature (London) 349, 117-127
    • (1991) Nature (London) , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 67
    • 2642693511 scopus 로고
    • Enzyme organization in vivo: Thermodynamic-kinetic perspectives
    • Sere, P. A., Estabrook, R. W., eds, Academic Press, New York
    • Welch, G. R., and DeMoss, J. A. (1978) Enzyme organization in vivo: thermodynamic-kinetic perspectives. In Microenvironments and Metabolic Compartmentation (Sere, P. A., Estabrook, R. W., eds) pp. 323-344, Academic Press, New York
    • (1978) Microenvironments and Metabolic Compartmentation , pp. 323-344
    • Welch, G.R.1    DeMoss, J.A.2
  • 68
    • 0030046495 scopus 로고    scopus 로고
    • Mitochondria and diabetes: Genetic, biochemical, and clinical implications of the cellular energy circuit
    • Gerbittz, 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
    • Gerbittz, K.-D.1    Gempel, K.2    Brdiczka, D.3
  • 69
    • 0029923582 scopus 로고    scopus 로고
    • The effects of phosphocreatine introduced simultaneously into many cardiac cells
    • Tuganowski, W. (1996) The effects of phosphocreatine introduced simultaneously into many cardiac cells. Pfluegers Arch. Eur. J. Physiol. 431, 652-657
    • (1996) Pfluegers Arch. Eur. J. Physiol. , vol.431 , pp. 652-657
    • Tuganowski, W.1
  • 70
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.