메뉴 건너뛰기




Volumn 1080, Issue , 2006, Pages 140-153

Maintenance of the metabolic homeostasis of the heart: Developing a systems analysis approach

Author keywords

Complex I; ED FRAP; Modeling; NADH; Oxidative phosphorylation; Phosphoproteome; Protein phosphorylation; Proteome

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CYTOCHROME; PHOSPHORUS 32; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 33845608482     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1196/annals.1380.013     Document Type: Conference Paper
Times cited : (32)

References (51)
  • 1
    • 0005015485 scopus 로고
    • Relation between work and labile phosphate content in the isolated dog heart
    • WOLLENBERGER, A. 1957. Relation between work and labile phosphate content in the isolated dog heart. Circ. Res. 5(2): 175-178.
    • (1957) Circ. Res. , vol.5 , Issue.2 , pp. 175-178
    • Wollenberger, A.1
  • 2
    • 0014508414 scopus 로고
    • High-energy phosphate concentrations in dog myocardium during stress
    • BOERTH, R.C., J.W. COVELL, S.C. SEAGREN, et al. 1969. High-energy phosphate concentrations in dog myocardium during stress. Am. J. Physiol. 216: 1103-1106.
    • (1969) Am. J. Physiol. , vol.216 , pp. 1103-1106
    • Boerth, R.C.1    Covell, J.W.2    Seagren, S.C.3
  • 3
    • 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., R.M. DENTON, P.J. ENGLAND & P.J. RANDLE. 1972. The effects of increased heart work on the tricarboxylate cycle and its interactions with glycolysis in the perfused rat heart. Biochem. J. 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
  • 4
    • 0022505605 scopus 로고
    • Relation between work and phosphate metabolite in the in vivo paced mammalian heart
    • BALABAN, R.S., H.L. KANTOR, L.A. KATZ, et al. 1986. Relation between work and phosphate metabolite in the in vivo paced mammalian heart. Science 232: 1121-1123.
    • (1986) Science , vol.232 , pp. 1121-1123
    • Balaban, R.S.1    Kantor, H.L.2    Katz, L.A.3
  • 5
    • 0024496705 scopus 로고
    • Relation between phosphate metabolites and oxygen consumption of heart in vivo
    • KATZ, L.A., J.A. SWAIN, M.A. PORTMAN, et al. 1989. Relation between phosphate metabolites and oxygen consumption of heart in vivo. Am. J. Physiol. 256: H265-H274.
    • (1989) Am. J. Physiol. , vol.256
    • Katz, L.A.1    Swain, J.A.2    Portman, M.A.3
  • 6
    • 0025248717 scopus 로고
    • Phosphorus-31 nuclear magnetic resonance analysis of transient changes of canine myocardial metabolism in vivo
    • HEINEMAN, F.W., & R.S. BALABAN. 1990. Phosphorus-31 nuclear magnetic resonance analysis of transient changes of canine myocardial metabolism in vivo. J. Clin. Invest. 85: 843-852.
    • (1990) J. Clin. Invest. , vol.85 , pp. 843-852
    • Heineman, F.W.1    Balaban, R.S.2
  • 7
    • 0022555739 scopus 로고
    • 31P-NMR studies of respiratory regulation in the intact myocardium
    • FROM, A.H.L., M.A. PETEIN, S.P. MICHURSKI, et al. 1986. 31P-NMR studies of respiratory regulation in the intact myocardium. FEBS Lett. 206: 257-261.
    • (1986) FEBS Lett. , vol.206 , pp. 257-261
    • From, A.H.L.1    Petein, M.A.2    Michurski, S.P.3
  • 8
    • 0025084933 scopus 로고
    • Transmural high energy phosphate distribution and response to alterations in workload in the normal canine myocardium as studied with spatially localized 31P NMR spectroscopy
    • ROBITAILLE, P.M., H. MERKLE, B. LEW, et al. 1990. Transmural high energy phosphate distribution and response to alterations in workload in the normal canine myocardium as studied with spatially localized 31P NMR spectroscopy. Mag. Res. Med. 16: 91-116.
    • (1990) Mag. Res. Med. , vol.16 , pp. 91-116
    • Robitaille, P.M.1    Merkle, H.2    Lew, B.3
  • 9
    • 0025358020 scopus 로고
    • Absence of pH changes during altered work in the in vivo sheep heart: A 31P NMR investigation
    • DETRE, J.A., A.P. KORETSKY, D.S. WILLIAMS, et al. 1990. Absence of pH changes during altered work in the in vivo sheep heart: a 31P NMR investigation. J. Mol. Cell. Cardiol. 22: 543-553.
    • (1990) J. Mol. Cell. Cardiol. , vol.22 , pp. 543-553
    • Detre, J.A.1    Koretsky, A.P.2    Williams, D.S.3
  • 10
    • 0026874321 scopus 로고
    • Metabolic response of the human heart to inotropic stimulation: In vivo phosphorus-31 studies of normal and cardiomyopathic myocardium
    • SCHAEFER, S., G.G. SCHWARTZ, et al. 1992. Metabolic response of the human heart to inotropic stimulation: in vivo phosphorus-31 studies of normal and cardiomyopathic myocardium. Mag. Res. Med. 25: 260-272.
    • (1992) Mag. Res. Med. , vol.25 , pp. 260-272
    • Schaefer, S.1    Schwartz, G.G.2
  • 11
    • 0026491712 scopus 로고
    • Evidence that mitochondrial phosphate is visible in 31P NMR spectra of isolated, perfused rat hearts
    • GARLICK, P.B., S. SOBOLL & G.R. BULLOCK. 1992. Evidence that mitochondrial phosphate is visible in 31P NMR spectra of isolated, perfused rat hearts. NMR Biomed. 5: 29-36.
    • (1992) NMR Biomed. , vol.5 , pp. 29-36
    • Garlick, P.B.1    Soboll, S.2    Bullock, G.R.3
  • 12
    • 0005255768 scopus 로고
    • Fluorescence measurements of mitochondrial pyridine nucleotide in aerobiosis and anaerobiosis
    • CHANCE, B. & B. THORELL. 1959. Fluorescence measurements of mitochondrial pyridine nucleotide in aerobiosis and anaerobiosis. Nature 184: 931-934.
    • (1959) Nature , vol.184 , pp. 931-934
    • Chance, B.1    Thorell, B.2
  • 13
    • 0000214973 scopus 로고
    • Properties and kinetics of reduced pyridine nucleotide fluorescence of the isolated and in vivo rat heart
    • CHANCE, B., J.R. WILLIAMSON, D. FAMIESON, et al. 1965. Properties and kinetics of reduced pyridine nucleotide fluorescence of the isolated and in vivo rat heart. Biochemische Zeitschrift 341: 357-377.
    • (1965) Biochemische Zeitschrift , vol.341 , pp. 357-377
    • Chance, B.1    Williamson, J.R.2    Famieson, D.3
  • 14
    • 78651031094 scopus 로고
    • The respiratory chain and oxidative phosphorylation
    • CHANCE, B. & C.M. WILLIAMS. 1956. The respiratory chain and oxidative phosphorylation. Adv. Enzymol. 17: 65-134.
    • (1956) Adv. Enzymol. , vol.17 , pp. 65-134
    • Chance, B.1    Williams, C.M.2
  • 15
    • 0027413210 scopus 로고    scopus 로고
    • Effects of afterload and heart rate on NAD(P)H redox state in the isolated rabbit heart
    • HEINEMAN, F.W. & R.S. BALABAN. Effects of afterload and heart rate on NAD(P)H redox state in the isolated rabbit heart. Am. J. Physiol. 264: H433-H440.
    • Am. J. Physiol. , vol.264
    • Heineman, F.W.1    Balaban, R.S.2
  • 16
    • 0027254547 scopus 로고
    • Effect of cardiac work on electrical potential gradient across mitochondrial membrane in perfused rat hearts
    • WAN, B., C. DOUMEN, J. DUSZYNSKI, et al. 1993. Effect of cardiac work on electrical potential gradient across mitochondrial membrane in perfused rat hearts. Am. J. Physiol. 265: 453-460.
    • (1993) Am. J. Physiol. , vol.265 , pp. 453-460
    • Wan, B.1    Doumen, C.2    Duszynski, J.3
  • 17
    • 0029112917 scopus 로고
    • Respiratory control in heart muscle during fatty acid oxidation. Energy state or substrate-level regulation by Ca2+?
    • VUORINEN, K.H., A. LA-RAMI, Y. YAN, et al. 1995. Respiratory control in heart muscle during fatty acid oxidation. Energy state or substrate-level regulation by Ca2+? J. Mol. Cell. Cardiol. 27: 1581-1591.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 1581-1591
    • Vuorinen, K.H.1    La-Rami, A.2    Yan, Y.3
  • 18
    • 0029130118 scopus 로고
    • Increase of cardiac work is associated with decrease of mitochondrial NADH
    • ASHRUF, J.F., J.M. COREMANS, H.A. BRUINING, et al. 1995. Increase of cardiac work is associated with decrease of mitochondrial NADH. Am. J. Physiol. 269: H856-H862.
    • (1995) Am. J. Physiol. , vol.269
    • Ashruf, J.F.1    Coremans, J.M.2    Bruining, H.A.3
  • 19
    • 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(10): 1259-1271.
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , Issue.10 , pp. 1259-1271
    • Balaban, R.S.1
  • 20
    • 0842302328 scopus 로고    scopus 로고
    • Regulation of cellular respiration in myoglobin-deficient mouse heart
    • LIIMATTA, E.V., A. GODECKE, J. SCHRADER & I.E. HASSINEN. 2004. Regulation of cellular respiration in myoglobin-deficient mouse heart. Mol. Cell. Biochem. 256-257: 201-208.
    • (2004) Mol. Cell. Biochem. , vol.256-257 , pp. 201-208
    • Liimatta, E.V.1    Godecke, A.2    Schrader, J.3    Hassinen, I.E.4
  • 21
    • 33750884657 scopus 로고    scopus 로고
    • Maximum oxidative phosphorylation capacity of the mammalian heart
    • MOOTHA, V.K., A.E. ARAI & R.S. BALABAN. 1997. Maximum oxidative phosphorylation capacity of the mammalian heart. Am. J. Physiol. 272: H769-H775.
    • (1997) Am. J. Physiol. , vol.272
    • Mootha, V.K.1    Arai, A.E.2    Balaban, R.S.3
  • 22
    • 0027320183 scopus 로고
    • Microprobe analysis of TC-MIMBI in heart cells: Calculation of mitochondrial membrane potential
    • BACKUS, M., D. PIWNICA-WORMS, D. HOCKETT, et al. 1993. Microprobe analysis of TC-MIMBI in heart cells: calculation of mitochondrial membrane potential. Am. J. Physiol. 265: C178-C187.
    • (1993) Am. J. Physiol. , vol.265
    • Backus, M.1    Piwnica-Worms, D.2    Hockett, D.3
  • 23
    • 0032859610 scopus 로고    scopus 로고
    • Myocardial oxygenation in vivo: Optical spectroscopy of cytoplasmic myoglobin and mitochondrial cytochromes
    • ARAI, A.E., C.E. KASSERRA, P.R. TERRITO, et al. 1999. Myocardial oxygenation in vivo: optical spectroscopy of cytoplasmic myoglobin and mitochondrial cytochromes. Am. J. Physiol. 277: H683-H697.
    • (1999) Am. J. Physiol. , vol.277
    • Arai, A.E.1    Kasserra, C.E.2    Territo, P.R.3
  • 24
    • 0017691722 scopus 로고
    • Control of mitochondrial respiration: A quantitative evaluation of the roles of cytochrome c and oxygen
    • WILSON, D.F., C.S. OWEN & A. HOLIAN. 1977. Control of mitochondrial respiration: a quantitative evaluation of the roles of cytochrome c and oxygen. Arch. Biochem. Biophys. 182: 749-762.
    • (1977) Arch. Biochem. Biophys. , vol.182 , pp. 749-762
    • Wilson, D.F.1    Owen, C.S.2    Holian, A.3
  • 25
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • MCCORMACK, J.G., A.P. HALESTRAP & R.M. DENTON. 1990. Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol. Rev. 70: 391-425.
    • (1990) Physiol. Rev. , vol.70 , pp. 391-425
    • Mccormack, J.G.1    Halestrap, A.P.2    Denton, R.M.3
  • 26
    • 0034052542 scopus 로고    scopus 로고
    • Ca(2+) activation of heart mitochondrial oxidative phosphorylation: Role of F0/F1ATPase
    • TERRITO, P.R., V.K. MOOTHA, S.A. FRENCH & R.S. BALABAN. 2000. Ca(2+) activation of heart mitochondrial oxidative phosphorylation: role of F0/F1ATPase. Am. J. Physiol. 278: C423-C435.
    • (2000) Am. J. Physiol. , vol.278
    • Territo, P.R.1    Mootha, V.K.2    French, S.A.3    Balaban, R.S.4
  • 27
    • 0025831812 scopus 로고
    • Effects of B-hydroxybutyrate on oxidative metabolism and phosphorylation potential in canine heart in vivo
    • KIM, D.K., F.W. HEINEMAN & R.S. BALABAN. 1991. Effects of B-hydroxybutyrate on oxidative metabolism and phosphorylation potential in canine heart in vivo. Am. J. Physiol. 260: H1767-H1773.
    • (1991) Am. J. Physiol. , vol.260
    • Kim, D.K.1    Heineman, F.W.2    Balaban, R.S.3
  • 28
    • 0028651917 scopus 로고
    • The relationship between phosphorylation potential and redox state in the isolated working rabbit heart
    • LAUGHLIN, M.R. & F.W. HEINEMAN. 1994. The relationship between phosphorylation potential and redox state in the isolated working rabbit heart. J. Mol. Cell. Cardiol. 26: 1525-1536.
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 1525-1536
    • Laughlin, M.R.1    Heineman, F.W.2
  • 29
    • 0028878311 scopus 로고
    • Effect of substrate on mitochondrial NADH, cytosolic redox state, and phosphorylated compounds in isolated hearts
    • SCHOLZ, T.D., M.R. LAUGHLIN, R.S. BALABAN, et al. 1995. Effect of substrate on mitochondrial NADH, cytosolic redox state, and phosphorylated compounds in isolated hearts. Am. J. Physiol. 268: H82-H91.
    • (1995) Am. J. Physiol. , vol.268
    • Scholz, T.D.1    Laughlin, M.R.2    Balaban, R.S.3
  • 30
    • 0006283971 scopus 로고
    • Transmural bioenergetic responses of normal myocardium to high workstates
    • ZHANG, J., D.J. DUNCKER, Y. XU, et al. 1995. Transmural bioenergetic responses of normal myocardium to high workstates. Am. J. Physiol. 268: H1891-H1911.
    • (1995) Am. J. Physiol. , vol.268
    • Zhang, J.1    Duncker, D.J.2    Xu, Y.3
  • 31
    • 0033622118 scopus 로고    scopus 로고
    • In vivo (31)P-NMR diffusion spectroscopy of ATP and phosphocreatine in rat skeletal muscle
    • DE GRAAF, R.A., K.A. VAN & K. NICOLAY. 2000. In vivo (31)P-NMR diffusion spectroscopy of ATP and phosphocreatine in rat skeletal muscle. Biophys. J. 78: 1657-1664.
    • (2000) Biophys. J. , vol.78 , pp. 1657-1664
    • De Graaf, R.A.1    Van, K.A.2    Nicolay, K.3
  • 32
    • 0014665355 scopus 로고
    • Ionic mobility in muscle cells
    • KUSHMERICK, M.J. & R.J. PODOLSKY. 1969. Ionic mobility in muscle cells. Science 166: 1297-1298.
    • (1969) Science , vol.166 , pp. 1297-1298
    • Kushmerick, M.J.1    Podolsky, R.J.2
  • 33
    • 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
  • 34
    • 0019471878 scopus 로고
    • Transport of energy in muscle: The phosphorylcreatine shuttle
    • BESSMAN, S.P. & P.J. GEIGER. 1981. Transport of energy in muscle: the phosphorylcreatine shuttle. Science 211: 448-452.
    • (1981) Science , vol.211 , pp. 448-452
    • Bessman, S.P.1    Geiger, P.J.2
  • 35
  • 36
    • 0014008650 scopus 로고
    • The possible role of the mitochondrial bound creatine kinase in regulation of mitochondrial respiration
    • BESSMAN, S.P. & A. FONYO. 1966. The possible role of the mitochondrial bound creatine kinase in regulation of mitochondrial respiration Biochem. Biophys. Res. Commun. 22: 597-602.
    • (1966) Biochem. Biophys. Res. Commun. , vol.22 , pp. 597-602
    • Bessman, S.P.1    Fonyo, A.2
  • 37
    • 0032406769 scopus 로고    scopus 로고
    • Some new aspects of creatine kinase (CK): Compartmentation, structure, function and regulation for cellular and mitochondrial bioenergetics and physiology
    • WALLIMANN, T., M. DOLDER, U. SCHLATTNER, et al. 1998. Some new aspects of creatine kinase (CK): compartmentation, structure, function and regulation for cellular and mitochondrial bioenergetics and physiology. Biofactors 8: 229-234.
    • (1998) Biofactors , vol.8 , pp. 229-234
    • Wallimann, T.1    Dolder, M.2    Schlattner, U.3
  • 38
    • 0034043681 scopus 로고    scopus 로고
    • Role of the creatine/phosphocreatine system in the regulation of mitochondrial respiration
    • SAKS, V.A., O. KONGAS, M. VENDELIN & L. KAY. 2000. Role of the creatine/phosphocreatine system in the regulation of mitochondrial respiration. Acta Physiol. Scand. 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
  • 39
    • 0027199664 scopus 로고
    • Quantitative analysis of the 'phosphocreatine shuttle': I. A probability approach to the description of phosphocreatine production in the coupled creatine kinase-ATP/ADP translocase-oxidative phosphorylation reactions in heart mitochondria
    • ALIEV, M.K. & V.A. SAKS. 1993. Quantitative analysis of the 'phosphocreatine shuttle': I. A probability approach to the description of phosphocreatine production in the coupled creatine kinase-ATP/ADP translocase-oxidative phosphorylation reactions in heart mitochondria. Biochim. Biophys. Acta 1143: 291-300.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 291-300
    • Aliev, M.K.1    Saks, V.A.2
  • 40
    • 0035795177 scopus 로고    scopus 로고
    • Functional complexes of mitochondria with Ca,MgATPases of myofibrils and sarcoplasmic reticulum in muscle cells
    • SEPPET, E.K., T. KAAMBRE, P. SIKK, et al. 2001. Functional complexes of mitochondria with Ca,MgATPases of myofibrils and sarcoplasmic reticulum in muscle cells. Biochim. Biophys. Acta 1504: 379-395.
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 379-395
    • Seppet, E.K.1    Kaambre, T.2    Sikk, P.3
  • 41
    • 0035920253 scopus 로고    scopus 로고
    • Energetic crosstalk between organelles: Architectural integration of energy production and utilization
    • KAASIK, A., V. VEKSLER, E. BOEHM, et al. 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
  • 42
    • 17444399932 scopus 로고    scopus 로고
    • Skeletal muscle NAD(P)H two-photon fluorescence microscopy in vivo: Topology and optical inner filters
    • ROTHSTEIN, E.C., S. CARROLL, C.A. COMBS, et al. 2005. Skeletal muscle NAD(P)H two-photon fluorescence microscopy in vivo: topology and optical inner filters. Biophys. J. 88: 2165-2176.
    • (2005) Biophys. J. , vol.88 , pp. 2165-2176
    • Rothstein, E.C.1    Carroll, S.2    Combs, C.A.3
  • 43
    • 0026662512 scopus 로고
    • Systems analysis of the tricarboxylic acid cycle in Dictyostelium discoideum. I. The basis for model construction
    • WRIGHT, B.E., M.H. BUTLER & K.R. ALBE. 1992. Systems analysis of the tricarboxylic acid cycle in Dictyostelium discoideum. I. The basis for model construction. J. Biol. Chem. 267: 3101-3105.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3101-3105
    • Wright, B.E.1    Butler, M.H.2    Albe, K.R.3
  • 44
    • 0033857139 scopus 로고    scopus 로고
    • Can yeast glycolysis be understood in terms of in vitro kinetics of the constituent enzymes? Testing biochemistry
    • TEUSINK, B., J. PASSARGE, C.A. REIJENGA, et al. 2000. Can yeast glycolysis be understood in terms of in vitro kinetics of the constituent enzymes? Testing biochemistry. Eur. J. Biochem. 267: 5313-5329.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5313-5329
    • Teusink, B.1    Passarge, J.2    Reijenga, C.A.3
  • 45
    • 0023647476 scopus 로고
    • Changes in pyridine nucleotide levels alter oxygen consumption and extramitochondrial phosphates in isolated mitochondria: A 31P NMR and fluorescence study
    • KORETSKY, A.P. & R.S. BALABAN. 1987. Changes in pyridine nucleotide levels alter oxygen consumption and extramitochondrial phosphates in isolated mitochondria: A 31P NMR and fluorescence study. Biochim. Biophys. 893: 398-408.
    • (1987) Biochim. Biophys. , vol.893 , pp. 398-408
    • Koretsky, A.P.1    Balaban, R.S.2
  • 46
    • 0346688697 scopus 로고    scopus 로고
    • NADH enzyme-dependent fluorescence recovery after photobleaching (ED-FRAP): Applications to enzyme and mitochondrial reaction kinetics, in vitro
    • JOUBERT, F., H.M. FALES, H. WEN, et al. 2004. NADH enzyme-dependent fluorescence recovery after photobleaching (ED-FRAP): applications to enzyme and mitochondrial reaction kinetics, in vitro. Biophys. J. 86: 629-645.
    • (2004) Biophys. J. , vol.86 , pp. 629-645
    • Joubert, F.1    Fales, H.M.2    Wen, H.3
  • 47
    • 14044276977 scopus 로고    scopus 로고
    • Distribution of mitochondrial NADH fluorescence lifetimes: Steady-state kinetics of matrix NADH interactions
    • BLINOVA, K., S. CARROLL, S. BOSE, et al. 2005. Distribution of mitochondrial NADH fluorescence lifetimes: steady-state kinetics of matrix NADH interactions. Biochemistry 44: 2585-2594.
    • (2005) Biochemistry , vol.44 , pp. 2585-2594
    • Blinova, K.1    Carroll, S.2    Bose, S.3
  • 48
    • 0029190248 scopus 로고
    • A new family of protein kinases - The mitochondrial protein kinases
    • HARRIS, R.A., K.M. POPOV, Y. ZHAO, et al. 1995. A new family of protein kinases - the mitochondrial protein kinases. Adv. Enzyme Regul. 35: 147-162.
    • (1995) Adv. Enzyme Regul. , vol.35 , pp. 147-162
    • Harris, R.A.1    Popov, K.M.2    Zhao, Y.3
  • 49
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • NEWMEYER, D.D. & S. FERGUSON-MILLER. 2003. Mitochondria: releasing power for life and unleashing the machineries of death. Cell. 112: 481-490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 50
    • 0038034950 scopus 로고    scopus 로고
    • Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye
    • SCHULENBERG, B., R. AGGELER, et al. 2003. Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J. Biol. Chem. 278: 27251-27255.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27251-27255
    • Schulenberg, B.1    Aggeler, R.2
  • 51
    • 33644546383 scopus 로고    scopus 로고
    • Mitochondrial matrix phosphoproteome: Effect of extra mitochondrial calcium
    • HOPPER, R.K., S. CARROLL, A.M. APONTE, et al. 2006. Mitochondrial matrix phosphoproteome: effect of extra mitochondrial calcium. Biochemistry 45: 2524-2536.
    • (2006) Biochemistry , vol.45 , pp. 2524-2536
    • Hopper, R.K.1    Carroll, S.2    Aponte, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.