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Volumn 50, Issue 13, 2011, Pages 2515-2529

Intrinsic protein kinase activity in mitochondrial oxidative phosphorylation complexes

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPHOSPHORYLATION; BN-PAGE; CLASSICAL EXAMPLE; CREATINE KINASE; GEL ELECTROPHORESIS; KINASE ACTIVITY; LOW CONCENTRATIONS; METABOLIC CONTROL; MITOCHONDRIAL COMPLEX; MITOCHONDRIAL OXIDATIVE PHOSPHORYLATION; MITOCHONDRIAL PROTEIN; OXIDATIVE PHOSPHORYLATION; P-PROTEIN; PHOSPHATASE ACTIVITY; PROTEIN KINASE; PROTEIN PHOSPHORYLATION; PYRUVATES; SODIUM DODECYL SULFATE; TARGET PROTEINS; WESTERN BLOTS;

EID: 79953178934     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101434x     Document Type: Article
Times cited : (28)

References (55)
  • 1
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • DOI 10.1016/S0092-8674(03)00116-8
    • Newmeyer, D. D. and Ferguson-Miller, S. (2003) Mitochondria: Releasing power for life and unleashing the machineries of death Cell 112 (4) 481-490 (Pubitemid 36263081)
    • (2003) Cell , vol.112 , Issue.4 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 2
    • 30944449043 scopus 로고    scopus 로고
    • Mitochondrial modulation: Reversible phosphorylation takes center stage?
    • DOI 10.1016/j.tibs.2005.11.005, PII S096800040500335X
    • Pagliarini, D. J. and Dixon, J. E. (2006) Mitochondrial modulation: Reversible phosphorylation takes center stage? Trends Biochem. Sci. 31 (1) 26-34 (Pubitemid 43117540)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.1 , pp. 26-34
    • Pagliarini, D.J.1    Dixon, J.E.2
  • 4
    • 0037431026 scopus 로고    scopus 로고
    • Identification of 14 new phosphoproteins involved in important plant mitochondrial processes
    • DOI 10.1016/S0014-5793(03)00250-3
    • Bykova, N. V., Egsgaard, H., and Moller, I. M. (2003) Identification of 14 new phosphoproteins involved in important plant mitochondrial processes FEBS Lett. 540 (1-3) 141-146 (Pubitemid 36398046)
    • (2003) FEBS Letters , vol.540 , Issue.1-3 , pp. 141-146
    • Bykova, N.V.1    Egsgaard, H.2    Moller, I.M.3
  • 7
    • 33748752151 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity
    • DOI 10.1074/jbc.M603536200
    • Schieke, S. M., Phillips, D., McCoy, J. P., Jr., Aponte, A. M., Shen, R. F., Balaban, R. S., and Finkel, T. (2006) The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity J. Biol. Chem. 281 (37) 27643-27652 (Pubitemid 44401789)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.37 , pp. 27643-27652
    • Schieke, S.M.1    Phillips, D.2    McCoy Jr., J.P.3    Aponte, A.M.4    Shen, R.-F.5    Balaban, R.S.6    Finkel, T.7
  • 8
    • 0038034950 scopus 로고    scopus 로고
    • Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye
    • DOI 10.1074/jbc.C300189200
    • Schulenberg, B., Aggeler, R., Beechem, J. M., Capaldi, R. A., and Patton, W. F. (2003) Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye J. Biol. Chem. 278 (29) 27251-27255 (Pubitemid 36876882)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 27251-27255
    • Schulenberg, B.1    Aggeler, R.2    Beechem, J.M.3    Capaldi, R.A.4    Patton, W.F.5
  • 9
    • 0034705703 scopus 로고    scopus 로고
    • Protein phosphorylation/dephosphorylation in the inner membrane of potato tuber mitochondria
    • DOI 10.1016/S0014-5793(00)01680-X, PII S001457930001680X
    • Struglics, A., Fredlund, K. M., Konstantinov, Y. M., Allen, J. F., and Moller, I. M. (2000) Protein phosphorylation/dephosphorylation in the inner membrane of potato tuber mitochondria FEBS Lett. 475 (3) 213-217 (Pubitemid 30408456)
    • (2000) FEBS Letters , vol.475 , Issue.3 , pp. 213-217
    • Struglics, A.1    Fredlund, K.M.2    Konstantinov, Y.M.3    Allen, J.F.4    Moller, I.M.5
  • 12
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • DOI 10.1016/S0092-8674(00)81382-3
    • Zha, J., Harada, H., Yang, E., Jockel, J., and Korsmeyer, S. J. (1996) Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) Cell 87 (4) 619-628 (Pubitemid 26386936)
    • (1996) Cell , vol.87 , Issue.4 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 13
    • 0030769818 scopus 로고    scopus 로고
    • Studies on the regulation of the mitochondrial α-ketoacid dehydrogenase complexes and their kinases
    • DOI 10.1016/S0065-2571(96)00009-X, PII S006525719600009X
    • Harris, R. A., Hawes, J. W., Popov, K. M., Zhao, Y., Shimomura, Y., Sato, J., Jaskiewicz, J., and Hurley, T. D. (1997) Studies on the regulation of the mitochondrial α-ketoacid dehydrogenase complexes and their kinases Adv. Enzyme Regul. 37, 271-293 (Pubitemid 27371564)
    • (1997) Advances in Enzyme Regulation , vol.37 , pp. 271-293
    • Harris, R.A.1    Hawes, J.W.2    Popov, K.M.3    Zhao, Y.4    Shimomura, Y.5    Sato, J.6    Jaskiewicz, J.7    Hurley, T.D.8
  • 17
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H. and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form Anal. Biochem. 199 (2) 223-231
    • (1991) Anal. Biochem. , vol.199 , Issue.2 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 19
    • 0141557578 scopus 로고    scopus 로고
    • Structural characterization of native mouse zona pellucida proteins using mass spectrometry
    • DOI 10.1074/jbc.M304026200
    • Boja, E. S., Hoodbhoy, T., Fales, H. M., and Dean, J. (2003) Structural characterization of native mouse zona pellucida proteins using mass spectrometry J. Biol. Chem. 278 (36) 34189-34202 (Pubitemid 37553261)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.36 , pp. 34189-34202
    • Boja, E.S.1    Hoodbhoy, T.2    Fales, H.M.3    Deanll, J.4
  • 20
    • 0036566190 scopus 로고    scopus 로고
    • Mutation of conserved active-site threonine residues in creatine kinase affects autophosphorylation and enzyme kinetics
    • DOI 10.1042/0264-6021:3630785
    • Stolz, M., Hornemann, T., Schlattner, U., and Wallimann, T. (2002) Mutation of conserved active-site threonine residues in creatine kinase affects autophosphorylation and enzyme kinetics Biochem. J. 363 (Part 3) 785-792 (Pubitemid 34526400)
    • (2002) Biochemical Journal , vol.363 , Issue.3 , pp. 785-792
    • Stolz, M.1    Hornemann, T.2    Schlattner, U.3    Wallimann, T.4
  • 21
    • 34547138661 scopus 로고    scopus 로고
    • High resolution clear native electrophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes
    • DOI 10.1074/mcp.M700076-MCP200
    • Wittig, I., Karas, M., and Schagger, H. (2007) High resolution clear native electrophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes Mol. Cell. Proteomics 6 (7) 1215-1225 (Pubitemid 47099231)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.7 , pp. 1215-1225
    • Wittig, I.1    Karas, M.2    Schagger, H.3
  • 22
    • 42249088081 scopus 로고    scopus 로고
    • How to analyze protein complexes by 2D blue native SDS-PAGE
    • DOI 10.1002/pmic.200700205
    • Reisinger, V. and Eichacker, L. A. (2007) How to analyze protein complexes by 2D blue native SDS-PAGE Proteomics 7 (Suppl. 1) 6-16 (Pubitemid 351547765)
    • (2007) Proteomics - Practical Proteomics , vol.2 , Issue.1 , pp. 6-16
    • Reisinger, V.1    Eichacker, L.A.2
  • 23
    • 0033820841 scopus 로고    scopus 로고
    • Separation of intact pyruvate dehydrogenase complex using blue native agarose gel electrophoresis
    • Henderson, N. S., Nijtmans, L. G., Lindsay, J. G., Lamantea, E., Zeviani, M., and Holt, I. J. (2000) Separation of intact pyruvate dehydrogenase complex using blue native agarose gel electrophoresis Electrophoresis 21 (14) 2925-2931
    • (2000) Electrophoresis , vol.21 , Issue.14 , pp. 2925-2931
    • Henderson, N.S.1    Nijtmans, L.G.2    Lindsay, J.G.3    Lamantea, E.4    Zeviani, M.5    Holt, I.J.6
  • 25
    • 70350710639 scopus 로고    scopus 로고
    • Succinyl-CoA synthetase is a phosphate target for the activation of mitochondrial metabolism
    • Phillips, D., Aponte, A. M., French, S. A., Chess, D. J., and Balaban, R. S. (2009) Succinyl-CoA synthetase is a phosphate target for the activation of mitochondrial metabolism Biochemistry 48 (30) 7140-7149
    • (2009) Biochemistry , vol.48 , Issue.30 , pp. 7140-7149
    • Phillips, D.1    Aponte, A.M.2    French, S.A.3    Chess, D.J.4    Balaban, R.S.5
  • 27
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • DOI 10.1038/341125a0
    • Ostermann, J., Horwich, A. L., Neupert, W., and Hartl, F. U. (1989) Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis Nature 341 (6238) 125-130 (Pubitemid 19222773)
    • (1989) Nature , vol.341 , Issue.6238 , pp. 125-130
    • Ostermann, J.1    Horwich, A.L.2    Neupert, W.3    Hartl, F.-U.4
  • 28
    • 0029101502 scopus 로고
    • Autophosphorylation of creatine kinase: Characterization and identification of a specifically phosphorylated peptide
    • Hemmer, W., Furter-Graves, E. M., Frank, G., Wallimann, T., and Furter, R. (1995) Autophosphorylation of creatine kinase: Characterization and identification of a specifically phosphorylated peptide Biochim. Biophys. Acta 1251 (2) 81-90
    • (1995) Biochim. Biophys. Acta , vol.1251 , Issue.2 , pp. 81-90
    • Hemmer, W.1    Furter-Graves, E.M.2    Frank, G.3    Wallimann, T.4    Furter, R.5
  • 29
    • 0024996554 scopus 로고
    • Phosphorylation of chicken brain-type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo
    • DOI 10.1016/0014-5793(90)81215-A
    • Quest, A. F., Soldati, T., Hemmer, W., Perriard, J. C., Eppenberger, H. M., and Wallimann, T. (1990) Phosphorylation of chicken brain-type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo FEBS Lett. 269 (2) 457-464 (Pubitemid 20273847)
    • (1990) FEBS Letters , vol.269 , Issue.2 , pp. 457-464
    • Quest, A.F.G.1    Soldati, T.2    Hemmer, W.3    Perriard, J.-C.4    Eppenberger, H.M.5    Wallimann, T.6
  • 30
    • 0033614790 scopus 로고    scopus 로고
    • ATP nucleotidylation of creatine kinase
    • David, S. S. and Haley, B. E. (1999) ATP nucleotidylation of creatine kinase Biochemistry 38 (26) 8492-8500
    • (1999) Biochemistry , vol.38 , Issue.26 , pp. 8492-8500
    • David, S.S.1    Haley, B.E.2
  • 31
    • 0030848050 scopus 로고    scopus 로고
    • Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome-c oxidase
    • Arnold, S. and Kadenbach, B. (1997) Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome-c oxidase Eur. J. Biochem. 249 (1) 350-354 (Pubitemid 27432632)
    • (1997) European Journal of Biochemistry , vol.249 , Issue.1 , pp. 350-354
    • Arnold, S.1    Kadenbach, B.2
  • 32
    • 0033033002 scopus 로고    scopus 로고
    • The intramitochondrial ATP/ADP-ratio controls cytochrome c oxidase activity allosterically
    • DOI 10.1016/S0014-5793(98)01694-9, PII S0014579398016949
    • Arnold, S. and Kadenbach, B. (1999) The intramitochondrial ATP/ADP-ratio controls cytochrome c oxidase activity allosterically FEBS Lett. 443 (2) 105-108 (Pubitemid 29078611)
    • (1999) FEBS Letters , vol.443 , Issue.2 , pp. 105-108
    • Arnold, S.1    Kadenbach, B.2
  • 34
    • 0033965893 scopus 로고    scopus 로고
    • The allosteric ATP-inhibition of cytochrome c oxidase activity is reversibly switched on by cAMP-dependent phosphorylation
    • DOI 10.1016/S0014-5793(99)01773-1, PII S0014579399017731
    • Bender, E. and Kadenbach, B. (2000) The allosteric ATP-inhibition of cytochrome c oxidase activity is reversibly switched on by cAMP-dependent phosphorylation FEBS Lett. 466 (1) 130-134 (Pubitemid 30050698)
    • (2000) FEBS Letters , vol.466 , Issue.1 , pp. 130-134
    • Bender, E.1    Kadenbach, B.2
  • 36
    • 37549066690 scopus 로고    scopus 로고
    • Structures of the human pyruvate dehydrogenase complex cores: A highly conserved catalytic center with flexible N-terminal domains
    • Yu, X., Hiromasa, Y., Tsen, H., Stoops, J. K., Roche, T. E., and Zhou, Z. H. (2008) Structures of the human pyruvate dehydrogenase complex cores: A highly conserved catalytic center with flexible N-terminal domains Structure 16 (1) 104-114
    • (2008) Structure , vol.16 , Issue.1 , pp. 104-114
    • Yu, X.1    Hiromasa, Y.2    Tsen, H.3    Stoops, J.K.4    Roche, T.E.5    Zhou, Z.H.6
  • 37
    • 0037048701 scopus 로고    scopus 로고
    • 2-fold lower than that of complex III in human mitochondria
    • 2-fold lower than that of complex III in human mitochondria FEBS Lett. 529 (2-3) 173-178
    • (2002) FEBS Lett. , vol.529 , Issue.2-3 , pp. 173-178
    • Murray, J.1    Gilkerson, R.2    Capaldi, R.A.3
  • 38
    • 77954927294 scopus 로고    scopus 로고
    • Stoichiometry of STAT3 and mitochondrial proteins: Implications for the regulation of oxidative phosphorylation by protein-protein interactions
    • Phillips, D., Reilley, M. J., Aponte, A. M., Wang, G., Boja, E., Gucek, M., and Balaban, R. S. (2010) Stoichiometry of STAT3 and mitochondrial proteins: Implications for the regulation of oxidative phosphorylation by protein-protein interactions J. Biol. Chem. 285 (31) 23532-23536
    • (2010) J. Biol. Chem. , vol.285 , Issue.31 , pp. 23532-23536
    • Phillips, D.1    Reilley, M.J.2    Aponte, A.M.3    Wang, G.4    Boja, E.5    Gucek, M.6    Balaban, R.S.7
  • 40
    • 4444305698 scopus 로고    scopus 로고
    • Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry
    • DOI 10.1002/elps.200406007
    • Schulenberg, B., Goodman, T. N., Aggeler, R., Capaldi, R. A., and Patton, W. F. (2004) Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry Electrophoresis 25 (15) 2526-2532 (Pubitemid 39193662)
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2526-2532
    • Schulenberg, B.1    Goodman, T.N.2    Aggeler, R.3    Capaldi, R.A.4    Patton, W.F.5
  • 41
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning, G., Whyte, D. B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002) The protein kinase complement of the human genome Science 298 (5600) 1912-1934 (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 42
    • 0036040203 scopus 로고    scopus 로고
    • Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces
    • DOI 10.1007/s00253-002-1045-1
    • Umeyama, T., Lee, P. C., and Horinouchi, S. (2002) Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces Appl. Microbiol. Biotechnol. 59 (4-5) 419-425 (Pubitemid 35002175)
    • (2002) Applied Microbiology and Biotechnology , vol.59 , Issue.4-5 , pp. 419-425
    • Umeyama, T.1    Lee, P.-C.2    Horinouchi, S.3
  • 43
    • 0031722706 scopus 로고    scopus 로고
    • Novel families of putative protein kinases in bacteria and archaea: Evolution of the 'eukaryotic' protein kinase superfamily
    • Leonard, C. J., Aravind, L., and Koonin, E. V. (1998) Novel families of putative protein kinases in bacteria and archaea: Evolution of the "eukaryotic" protein kinase superfamily Genome Res. 8 (10) 1038-1047 (Pubitemid 28532492)
    • (1998) Genome Research , vol.8 , Issue.10 , pp. 1038-1047
    • Leonard, C.J.1    Aravind, L.2    Koonin, E.V.3
  • 45
    • 29144466723 scopus 로고    scopus 로고
    • Branched-chain 6-ketoacid dehydrogenase kinase: A mammalian enzyme with histidine kinase activity
    • Lasker, M. V., Thai, P., Besant, P. G., Bui, C. D., Naidu, S., and Turck, C. W. (2002) Branched-chain 6-ketoacid dehydrogenase kinase: A mammalian enzyme with histidine kinase activity J. Biomol. Tech. 13 (4) 238-245
    • (2002) J. Biomol. Tech. , vol.13 , Issue.4 , pp. 238-245
    • Lasker, M.V.1    Thai, P.2    Besant, P.G.3    Bui, C.D.4    Naidu, S.5    Turck, C.W.6
  • 46
    • 66149112136 scopus 로고    scopus 로고
    • Reversible phosphorylation of histidine residues in proteins from vertebrates
    • Klumpp, S. and Krieglstein, J. (2009) Reversible phosphorylation of histidine residues in proteins from vertebrates Sci. Signal. 2 (61) e13
    • (2009) Sci. Signal. , vol.2 , Issue.61 , pp. 13
    • Klumpp, S.1    Krieglstein, J.2
  • 47
    • 0029154302 scopus 로고
    • Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium
    • Morera, S., Chiadmi, M., LeBras, G., Lascu, I., and Janin, J. (1995) Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium Biochemistry 34 (35) 11062-11070
    • (1995) Biochemistry , vol.34 , Issue.35 , pp. 11062-11070
    • Morera, S.1    Chiadmi, M.2    Lebras, G.3    Lascu, I.4    Janin, J.5
  • 48
    • 32344445336 scopus 로고    scopus 로고
    • Autophosphorylation of Arabidopsis nucleoside diphosphate kinase 2 occurs only on its active histidine residue
    • DOI 10.1021/bi051868a
    • Shen, Y., Kim, J. I., and Song, P. S. (2006) Autophosphorylation of Arabidopsis nucleoside diphosphate kinase 2 occurs only on its active histidine residue Biochemistry 45 (6) 1946-1949 (Pubitemid 43222138)
    • (2006) Biochemistry , vol.45 , Issue.6 , pp. 1946-1949
    • Shen, Y.1    Kim, J.-I.2    Song, P.-S.3
  • 49
    • 33845643217 scopus 로고    scopus 로고
    • Autophosphorylation of Solanum chacoense cytosolic nucleoside diphosphate kinase on Ser117
    • DOI 10.1093/jxb/erl175
    • Dorion, S., Dumas, F., and Rivoal, J. (2006) Autophosphorylation of Solanum chacoense cytosolic nucleoside diphosphate kinase on Ser117 J. Exp. Bot. 57 (15) 4079-4088 (Pubitemid 44950408)
    • (2006) Journal of Experimental Botany , vol.57 , Issue.15 , pp. 4079-4088
    • Dorion, S.1    Dumas, F.2    Rivoal, J.3
  • 50
    • 50549214640 scopus 로고
    • Metabolic function of phosphohistidine
    • Pressman, B. C. (1964) Metabolic function of phosphohistidine Biochem. Biophys. Res. Commun. 15 (4) 556-561
    • (1964) Biochem. Biophys. Res. Commun. , vol.15 , Issue.4 , pp. 556-561
    • Pressman, B.C.1
  • 51
    • 4243918385 scopus 로고
    • The formation of bound phosphohistidine from adenosine triphosphate-P32 in mitochondria
    • Peter, J. B. and Boyer, P. D. (1963) The formation of bound phosphohistidine from adenosine triphosphate-P32 in mitochondria J. Biol. Chem. 238, 1180-1182
    • (1963) J. Biol. Chem. , vol.238 , pp. 1180-1182
    • Peter, J.B.1    Boyer, P.D.2
  • 52
    • 0006190955 scopus 로고
    • Characteristics of bound phosphohistidine labeling in mitochondria
    • Lindberg, O., Duffy, J. J., Norman, A. W., and Boyer, P. D. (1965) Characteristics of bound phosphohistidine labeling in mitochondria J. Biol. Chem. 240, 2850-2854
    • (1965) J. Biol. Chem. , vol.240 , pp. 2850-2854
    • Lindberg, O.1    Duffy, J.J.2    Norman, A.W.3    Boyer, P.D.4
  • 53
    • 0017306759 scopus 로고
    • Regulation of pyruvate dehydrogenase in rat heart. Mechanism of regulation of proportions of dephosphorylated and phosphorylated enzyme by oxidation of fatty acids and ketone bodies and of effects of diabetes: Role of coenzyme A, acetyl-coenzyme A and reduced and oxidized nicotinamide-adenine dinucleotide
    • Kerbey, A. L., Randle, P. J., Cooper, R. H., Whitehouse, S., Pask, H. T., and Denton, R. M. (1976) Regulation of pyruvate dehydrogenase in rat heart. Mechanism of regulation of proportions of dephosphorylated and phosphorylated enzyme by oxidation of fatty acids and ketone bodies and of effects of diabetes: Role of coenzyme A, acetyl-coenzyme A and reduced and oxidized nicotinamide-adenine dinucleotide Biochem. J. 154 (2) 327-348
    • (1976) Biochem. J. , vol.154 , Issue.2 , pp. 327-348
    • Kerbey, A.L.1    Randle, P.J.2    Cooper, R.H.3    Whitehouse, S.4    Pask, H.T.5    Denton, R.M.6
  • 54
    • 0023828808 scopus 로고
    • Mono(ADP-ribosylation) in rat liver mitochondria
    • Frei, B. and Richter, C. (1988) Mono(ADP-ribosylation) in rat liver mitochondria Biochemistry 27 (2) 529-535 (Pubitemid 18043502)
    • (1988) Biochemistry , vol.27 , Issue.2 , pp. 529-535
    • Frei, B.1    Richter, C.2
  • 55
    • 27744501798 scopus 로고    scopus 로고
    • Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms
    • DOI 10.1074/jbc.M508660200
    • Berger, F., Lau, C., Dahlmann, M., and Ziegler, M. (2005) Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms J. Biol. Chem. 280 (43) 36334-36341 (Pubitemid 41633907)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.43 , pp. 36334-36341
    • Berger, F.1    Lau, C.2    Dahlmann, M.3    Ziegler, M.4


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