메뉴 건너뛰기




Volumn , Issue , 2007, Pages 303-338

Signaling by AMP-activated Protein Kinase

Author keywords

Energy transfer networks; Mammalian AMPK; Metabolic feedback regulation; Modeling cellular energetics; Molecular system bioenergetics; Sensing cellular energy stress situations; Signaling by AMP activated protein kinase; Signaling of cellular energy stress situations

Indexed keywords


EID: 58149398449     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527621095.ch9     Document Type: Chapter
Times cited : (6)

References (174)
  • 1
    • 33745225026 scopus 로고    scopus 로고
    • AMP-activated protein kinase-development of the energy sensor concept
    • Hardie, D. G., Hawley, S. A., Scott, J. W. (2006) AMP-activated protein kinase-development of the energy sensor concept. J. Physiol. 574 7-15.
    • (2006) J. Physiol. , vol.574 , pp. 7-15
    • Hardie, D.G.1    Hawley, S.A.2    Scott, J.W.3
  • 4
    • 33645738458 scopus 로고    scopus 로고
    • Complexity of the TOR signaling network
    • Inoki, K., Guan, K. L. (2006) Complexity of the TOR signaling network. Trends Cell Biol. 16 206-212.
    • (2006) Trends Cell Biol. , vol.16 , pp. 206-212
    • Inoki, K.1    Guan, K.L.2
  • 5
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger, S., Loewith, R., Hall, M. N. (2006) TOR signaling in growth and metabolism. Cell 124 471-484.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 7
    • 0037328989 scopus 로고    scopus 로고
    • A molecular approach to the concerted action of kinases involved in energy homoeostasis
    • Neumann, D., Schlattner, U., 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
  • 8
    • 33644943620 scopus 로고    scopus 로고
    • AMPK: a key sensor of fuel and energy status in skeletal muscle
    • Hardie, D. G., Sakamoto, K. (2006) AMPK: a key sensor of fuel and energy status in skeletal muscle. Physiology 21 48-60.
    • (2006) Physiology , vol.21 , pp. 48-60
    • Hardie, D.G.1    Sakamoto, K.2
  • 9
    • 0014353859 scopus 로고
    • The energy charge of the adenylate pool as a regulatory parameter.Interaction with feedback modifiers
    • Atkinson, D. E. (1968) The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers. Biochemistry 7 4030-4034.
    • (1968) Biochemistry , vol.7 , pp. 4030-4034
    • Atkinson, D.E.1
  • 10
    • 0035542970 scopus 로고    scopus 로고
    • AMP-activated protein kinase: the energy charge hypothesis revisited
    • Hardie, D. G., Hawley, S. A. (2001) AMP-activated protein kinase: the energy charge hypothesis revisited. Bioessays 23 1112-1119.
    • (2001) Bioessays , vol.23 , pp. 1112-1119
    • Hardie, D.G.1    Hawley, S.A.2
  • 11
    • 0034687243 scopus 로고    scopus 로고
    • Metabolic control: a new solution to an old problem
    • Hardie, D. G. (2000) Metabolic control: a new solution to an old problem. Curr. Biol. 10, R757-759.
    • (2000) Curr. Biol. , vol.10
    • Hardie, D.G.1
  • 12
    • 20844451123 scopus 로고    scopus 로고
    • AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism
    • Kahn, B. B., Alquier, T., Carling, D., Hardie, D. G. (2005) AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab. 1 15-25.
    • (2005) Cell Metab. , vol.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4
  • 13
    • 18044389727 scopus 로고    scopus 로고
    • AMPactivated protein kinase and the metabolic syndrome
    • Fryer, L. G., Carling, D. (2005) AMPactivated protein kinase and the metabolic syndrome. Biochem. Soc. Trans. 33 362-366.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 362-366
    • Fryer, L.G.1    Carling, D.2
  • 14
    • 30944448596 scopus 로고    scopus 로고
    • Chutes and Ladders: the search for protein kinases that act on AMPK
    • Witters, L. A., Kemp, B. E., Means, A. R. (2006) Chutes and Ladders: the search for protein kinases that act on AMPK. Trends Biochem. Sci. 31 13-16.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 13-16
    • Witters, L.A.1    Kemp, B.E.2    Means, A.R.3
  • 15
    • 23844454317 scopus 로고    scopus 로고
    • Emerging role of AMP-activated protein kinase in coupling membrane transport to cellular metabolism
    • Hallows, K. R. (2005) Emerging role of AMP-activated protein kinase in coupling membrane transport to cellular metabolism. Curr. Opin. Nephrol. Hypertens. 14 464-471.
    • (2005) Curr. Opin. Nephrol. Hypertens. , vol.14 , pp. 464-471
    • Hallows, K.R.1
  • 16
    • 33847072201 scopus 로고    scopus 로고
    • AMP-Activated Protein Kinase as a Drug Target
    • Hardie, D. G. (2007) AMP-Activated Protein Kinase as a Drug Target. Annu. Rev. Pharmacol. Toxicol. 47 185-210.
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 185-210
    • Hardie, D.G.1
  • 18
    • 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, 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. 281 21-40.
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 19
    • 0028017704 scopus 로고
    • Creatine kinase in non-muscle tissues and cells
    • Wallimann, T., Hemmer, W. (1994) Creatine kinase in non-muscle tissues and cells. Mol. Cell. Biochem. 133-134, 193-220.
    • (1994) Mol. Cell. Biochem. , vol.133-134 , pp. 193-220
    • Wallimann, T.1    Hemmer, W.2
  • 20
    • 27244445183 scopus 로고    scopus 로고
    • Dynamics of nucleotide metabolism as a supporter of life phenomena
    • Noma, T. (2005) Dynamics of nucleotide metabolism as a supporter of life phenomena. J. Med. Invest. 52 127-136.
    • (2005) J. Med. Invest. , vol.52 , pp. 127-136
    • Noma, T.1
  • 21
    • 34047271438 scopus 로고    scopus 로고
    • A sea urchin sperm flagellar adenylate kinase with triplicated catalytic domains
    • Kinukawa, M., Nomura, M., Vacquier, V. D. (2007) A sea urchin sperm flagellar adenylate kinase with triplicated catalytic domains. J. Biol. Chem. 282 2947-2955.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2947-2955
    • Kinukawa, M.1    Nomura, M.2    Vacquier, V.D.3
  • 22
    • 0029665566 scopus 로고    scopus 로고
    • 31P-NMRmeasured creatine kinase reaction flux in muscle: a caveat! J
    • Wallimann, T. (1996) 31P-NMRmeasured creatine kinase reaction flux in muscle: a caveat! J. Muscle Res. Cell Motil. 17 177-181.
    • (1996) Muscle Res. Cell Motil. , vol.17 , pp. 177-181
    • Wallimann, T.1
  • 23
    • 0242654423 scopus 로고
    • Studies on actin.III. G-F transformation of actin and muscular contraction (experiments in vivo).
    • Martonosi, A., Gouvea, M. A., Gergely, J. (1960) Studies on actin.III. G-F transformation of actin and muscular contraction (experiments in vivo). J. Biol. Chem. 235 1707-1710.
    • (1960) J. Biol. Chem. , vol.235 , pp. 1707-1710
    • Martonosi, A.1    Gouvea, M.A.2    Gergely, J.3
  • 24
    • 19644373804 scopus 로고    scopus 로고
    • 31P-NMR observation of free ADP during fatiguing, repetitive contractions of murine skeletal muscle lacking AK1
    • Hancock, C. R., Brault, J. J., Wiseman, R. W., Terjung, R. L., Meyer, R. A. (2005) 31P-NMR observation of free ADP during fatiguing, repetitive contractions of murine skeletal muscle lacking AK1. Am. J. Physiol. 288, C1298-1304.
    • (2005) Am. J. Physiol. , vol.288
    • Hancock, C.R.1    Brault, J.J.2    Wiseman, R.W.3    Terjung, R.L.4    Meyer, R.A.5
  • 25
    • 33646374461 scopus 로고    scopus 로고
    • Contraction-mediated phosphorylation of AMPK is lower in skeletal muscle of adenylate kinasedeficient mice
    • Hancock, C. R., Janssen, E., Terjung, R. L. (2006) Contraction-mediated phosphorylation of AMPK is lower in skeletal muscle of adenylate kinasedeficient mice. J. Appl. Physiol. 100 406-413.
    • (2006) J. Appl. Physiol. , vol.100 , pp. 406-413
    • Hancock, C.R.1    Janssen, E.2    Terjung, R.L.3
  • 26
    • 0036750019 scopus 로고    scopus 로고
    • Is creatine kinase a target for AMP-activated protein kinase in the heart? J
    • Ingwall, J. S. (2002) Is creatine kinase a target for AMP-activated protein kinase in the heart? J. Mol. Cell. Cardiol. 34 1111-1120.
    • (2002) Mol. Cell. Cardiol. , vol.34 , pp. 1111-1120
    • Ingwall, J.S.1
  • 27
    • 0033230853 scopus 로고    scopus 로고
    • AMP deamination and purine exchange in human skeletal muscle during and after intense exercise
    • Hellsten, Y., Richter, E. A., Kiens, B., Bangsbo, J. (1999) AMP deamination and purine exchange in human skeletal muscle during and after intense exercise. J. Physiol. 520 909-920.
    • (1999) J. Physiol. , vol.520 , pp. 909-920
    • Hellsten, Y.1    Richter, E.A.2    Kiens, B.3    Bangsbo, J.4
  • 29
    • 0016246840 scopus 로고
    • Calculated equilibria of phosphocreatine and adenosine phosphates during utilization of high energy phosphate by muscle
    • McGilvery, R. W., Murray, T. W. (1974) Calculated equilibria of phosphocreatine and adenosine phosphates during utilization of high energy phosphate by muscle. J. Biol. Chem. 249 5845-5850.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5845-5850
    • McGilvery, R.W.1    Murray, T.W.2
  • 30
    • 0024308609 scopus 로고
    • Subcellular compartmentation of creatine kinase isoenzymes, regulation of CK and octameric structure of mitochondrial CK: important aspects of the phosphoryl-creatine circuit
    • Wallimann, T., Schnyder, T., Schlegel, J., Wyss, M., Wegmann, G., Rossi, A. M., Hemmer, W., Eppenberger, H. M., Quest, A. F. (1989) Subcellular compartmentation of creatine kinase isoenzymes, regulation of CK and octameric structure of mitochondrial CK: important aspects of the phosphoryl-creatine circuit. Prog. Clin. Biol. Res. 315 159-176.
    • (1989) Prog. Clin. Biol. Res. , vol.315 , pp. 159-176
    • Wallimann, T.1    Schnyder, T.2    Schlegel, J.3    Wyss, M.4    Wegmann, G.5    Rossi, A.M.6    Hemmer, W.7    Eppenberger, H.M.8    Quest, A.F.9
  • 31
    • 17544373377 scopus 로고    scopus 로고
    • Suppression of creatine kinase-catalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle
    • Dzeja, P. P., Zeleznikar, R. J., Goldberg, N. D. (1996) Suppression of creatine 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
  • 32
    • 29344468308 scopus 로고    scopus 로고
    • Metabolite channeling: creatine kinase microcompartments, in Encyclopedia of Biological Chemistry
    • Lennarz, W. J., Lane, M. D., Eds., Academic Press, New York, USA
    • Schlattner, U., Wallimann, T. (2004) Metabolite channeling: creatine kinase microcompartments, in Encyclopedia of Biological Chemistry (Lennarz, W. J., Lane, M. D., Eds.) pp 646-651, Academic Press, New York, USA.
    • (2004) , pp. 646-651
    • Schlattner, U.1    Wallimann, T.2
  • 34
    • 0020334290 scopus 로고
    • A 31P-NMR saturation transfer study of the regulation of creatine kinase in the rat heart
    • Matthews, P. M., Bland, J. L., Gadian, D. G., Radda, G. K. (1982) A 31P-NMR saturation transfer study of the regulation of creatine kinase in the rat heart. Biochim. Biophys. Acta 721 312-320.
    • (1982) Biochim. Biophys. Acta , vol.721 , pp. 312-320
    • Matthews, P.M.1    Bland, J.L.2    Gadian, D.G.3    Radda, G.K.4
  • 35
    • 0026698727 scopus 로고
    • Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism
    • Wyss, M., Smeitink, J., Wevers, R. A., Wallimann, T. (1992) Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism. Biochim. Biophys. Acta 1102 119-166.
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 119-166
    • Wyss, M.1    Smeitink, J.2    Wevers, R.A.3    Wallimann, T.4
  • 36
    • 0037379434 scopus 로고    scopus 로고
    • Isolation, characterization and nucleotide sequence of the muscle isoforms of creatine kinase from the Antarctic teleost Chaenocephalus aceratus
    • Winnard, P., Cashon, R. E., Sidell, B. D., Vayda, M. E. (2003) Isolation, characterization and nucleotide sequence of the muscle isoforms of creatine kinase from the Antarctic teleost Chaenocephalus aceratus. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 134 651-667.
    • (2003) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.134 , pp. 651-667
    • Winnard, P.1    Cashon, R.E.2    Sidell, B.D.3    Vayda, M.E.4
  • 37
    • 0000398122 scopus 로고    scopus 로고
    • An iso-random Bi Bi mechanism for adenylate kinase
    • Sheng, X. R., Li, X., Pan, X. M. (1999) An iso-random Bi Bi mechanism for adenylate kinase. J. Biol. Chem. 274 22238-22242.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22238-22242
    • Sheng, X.R.1    Li, X.2    Pan, X.M.3
  • 38
    • 0035955468 scopus 로고    scopus 로고
    • Cysteine-25 of adenylate kinase reacts with dithiothreitol to form an adduct upon aging of the enzyme
    • Li, X., Han, Y., Pan, X. M. (2001) Cysteine-25 of adenylate kinase reacts with dithiothreitol to form an adduct upon aging of the enzyme. FEBS Lett. 507 169-173.
    • (2001) FEBS Lett. , vol.507 , pp. 169-173
    • Li, X.1    Han, Y.2    Pan, X.M.3
  • 39
    • 0842323771 scopus 로고    scopus 로고
    • Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice
    • Dzeja, P. P., Terzic, A., Wieringa, B. (2004) Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice. Mol. Cell. Biochem. 256-257, 13-27.
    • (2004) Mol. Cell. Biochem. , vol.256-257 , pp. 13-27
    • Dzeja, P.P.1    Terzic, A.2    Wieringa, B.3
  • 40
    • 33845949733 scopus 로고    scopus 로고
    • Dissecting the role of 50-AMP for allosteric stimulation, activation and deactivation of AMP-activated protein kinase
    • Suter, M., Riek, U., Tuerk, R., Schlattner, U., Wallimann, T., Neumann, D. (2006) Dissecting the role of 50-AMP for allosteric stimulation, activation and deactivation of AMP-activated protein kinase. J. Biol. Chem. 281 32207-32216.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32207-32216
    • Suter, M.1    Riek, U.2    Tuerk, R.3    Schlattner, U.4    Wallimann, T.5    Neumann, D.6
  • 41
    • 0031935635 scopus 로고    scopus 로고
    • Molecular and kinetic alterations of muscle AMP deaminase during chronic creatine depletion
    • Rush, J. W., Tullson, P. C., Terjung, R. L. (1998) Molecular and kinetic alterations of muscle AMP deaminase during chronic creatine depletion. Am. J. Physiol. 274, C465-471.
    • (1998) Am. J. Physiol. , vol.274
    • Rush, J.W.1    Tullson, P.C.2    Terjung, R.L.3
  • 42
    • 0028948536 scopus 로고
    • Oxidative modulation and inactivation of rabbit cardiac adenylate deaminase
    • Janero, D. R., Yarwood, C. (1995) Oxidative modulation and inactivation of rabbit cardiac adenylate deaminase. Biochem. J. 306 421-427.
    • (1995) Biochem. J. , vol.306 , pp. 421-427
    • Janero, D.R.1    Yarwood, C.2
  • 43
    • 0037058977 scopus 로고    scopus 로고
    • AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation
    • Zong, H., Ren, J. M., Young, L. H., Pypaert, M., Mu, J., Birnbaum, M. J., Shulman, G. I. (2002) AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation. Proc. Natl. Acad. Sci. USA 99 15983-15987.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15983-15987
    • Zong, H.1    Ren, J.M.2    Young, L.H.3    Pypaert, M.4    Mu, J.5    Birnbaum, M.J.6    Shulman, G.I.7
  • 44
    • 0023784260 scopus 로고
    • The pigeon heart 50-nucleotidase responsible for ischaemia-induced adenosine formation
    • Newby, A. C. (1988) The pigeon heart 50-nucleotidase responsible for ischaemia-induced adenosine formation. Biochem. J. 253 123-130.
    • (1988) Biochem. J. , vol.253 , pp. 123-130
    • Newby, A.C.1
  • 46
    • 0037329494 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins
    • Leff, T. (2003) AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins. Biochem. Soc. Trans. 31 224-227.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 224-227
    • Leff, T.1
  • 47
    • 33845335159 scopus 로고    scopus 로고
    • Molecular system bioenergetics: regulation of substrate supply in response to heart energy demands
    • Saks, V., Favier, R., Guzun, R., Schlattner, U., Wallimann, T. (2006) Molecular system bioenergetics: regulation of substrate supply in response to heart energy demands. J. Physiol. 577 769-777.
    • (2006) J. Physiol. , vol.577 , pp. 769-777
    • Saks, V.1    Favier, R.2    Guzun, R.3    Schlattner, U.4    Wallimann, T.5
  • 48
    • 33745204925 scopus 로고    scopus 로고
    • AMPK alterations in cardiac physiology and pathology: enemy or ally? J
    • Dyck, J. R., Lopaschuk, G. D. (2006) AMPK alterations in cardiac physiology and pathology: enemy or ally? J. Physiol. 574 95-112.
    • (2006) Physiol. , vol.574 , pp. 95-112
    • Dyck, J.R.1    Lopaschuk, G.D.2
  • 49
    • 33745196745 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase in the liver: a new strategy for the management of metabolic hepatic disorders
    • Viollet, B., Foretz, M., Guigas, B., Horman, S., Dentin, R., Bertrand, L., Hue, L., Andreelli, F. (2006) Activation of AMP-activated protein kinase in the liver: a new strategy for the management of metabolic hepatic disorders. J. Physiol. 574 41-53.
    • (2006) J. Physiol. , vol.574 , pp. 41-53
    • Viollet, B.1    Foretz, M.2    Guigas, B.3    Horman, S.4    Dentin, R.5    Bertrand, L.6    Hue, L.7    Andreelli, F.8
  • 50
    • 12144250304 scopus 로고    scopus 로고
    • Creatine feeding increases GLUT4 expression in rat skeletal muscle
    • Ju, J. S., Smith, J. L., Oppelt, P. J., Fisher, J. S. (2005) Creatine feeding increases GLUT4 expression in rat skeletal muscle. Am. J. Physiol. 288, E347-352.
    • (2005) Am. J. Physiol. , vol.288
    • Ju, J.S.1    Smith, J.L.2    Oppelt, P.J.3    Fisher, J.S.4
  • 51
    • 33846012164 scopus 로고    scopus 로고
    • Role of {alpha}2-AMPK in basal, trainingand AICAR-induced GLUT4, hexokinase II and mitochondrial protein expression in mouse muscle
    • Jorgensen, S. B., Treebak, J. T., Viollet, B., Schjerling, P., Vaulont, S., Wojtaszewski, J. F., Richter, E. A. (2007) Role of {alpha}2-AMPK in basal, trainingand AICAR-induced GLUT4, hexokinase II and mitochondrial protein expression in mouse muscle. Am. J. Physiol. 292, E331-339.
    • (2007) Am. J. Physiol. , vol.292
    • Jorgensen, S.B.1    Treebak, J.T.2    Viollet, B.3    Schjerling, P.4    Vaulont, S.5    Wojtaszewski, J.F.6    Richter, E.A.7
  • 52
    • 1642387890 scopus 로고    scopus 로고
    • Creatine supplementation increases glucose oxidation and AMPK phosphorylation and reduces lactate production in L6 rat skeletal muscle cells
    • Ceddia, R. B., Sweeney, G. (2004) Creatine supplementation increases glucose oxidation and AMPK phosphorylation and reduces lactate production in L6 rat skeletal muscle cells. J. Physiol. 555 409-421.
    • (2004) J. Physiol. , vol.555 , pp. 409-421
    • Ceddia, R.B.1    Sweeney, G.2
  • 54
    • 0032536774 scopus 로고    scopus 로고
    • Dual regulation of the AMPactivated protein kinase provides a novel mechanism for the control of creatine kinase in skeletal muscle
    • Ponticos, M., Lu, Q. L., Morgan, J. E., Hardie, D. G., Partridge, T. A., Carling, D. (1998) Dual regulation of the AMPactivated protein kinase provides a novel mechanism for the control of creatine kinase in skeletal muscle. EMBO J. 17 1688-1699.
    • (1998) EMBO J. , vol.17 , pp. 1688-1699
    • Ponticos, M.1    Lu, Q.L.2    Morgan, J.E.3    Hardie, D.G.4    Partridge, T.A.5    Carling, D.6
  • 55
    • 33646091533 scopus 로고    scopus 로고
    • Evidence against regulation of AMP-activated protein kinase and LKB1/STRAD/MO25 activity by creatine phosphate
    • Taylor, E. B., Ellingson, W. J., Lamb, J. D., Chesser, D. G., Compton, C. L., Winder, W. W. (2006) Evidence against regulation of AMP-activated protein kinase and LKB1/STRAD/MO25 activity by creatine phosphate. Am. J. Physiol. 290, E661-669.
    • (2006) Am. J. Physiol. , vol.290
    • Taylor, E.B.1    Ellingson, W.J.2    Lamb, J.D.3    Chesser, D.G.4    Compton, C.L.5    Winder, W.W.6
  • 56
    • 15444368657 scopus 로고    scopus 로고
    • AMP kinase expression and activity in human skeletal muscle: effects of immobilization, retraining, and creatine supplementation
    • Eijnde, B. O., Derave, W., Wojtaszewski, J. F., Richter, E. A., Hespel, P. (2005) AMP kinase expression and activity in human skeletal muscle: effects of immobilization, retraining, and creatine supplementation. J. Appl. Physiol. 98 1228-1233.
    • (2005) J. Appl. Physiol. , vol.98 , pp. 1228-1233
    • Eijnde, B.O.1    Derave, W.2    Wojtaszewski, J.F.3    Richter, E.A.4    Hespel, P.5
  • 57
    • 0038199737 scopus 로고    scopus 로고
    • Management of cellular energy by the AMP-activated protein kinase system
    • Hardie, D. G., Scott, J. W., Pan, D. A., Hudson, E. R. (2003) Management of cellular energy by the AMP-activated protein kinase system. FEBS Lett. 546 113-120.
    • (2003) FEBS Lett. , vol.546 , pp. 113-120
    • Hardie, D.G.1    Scott, J.W.2    Pan, D.A.3    Hudson, E.R.4
  • 58
    • 0029561919 scopus 로고
    • 50-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C alpha and native bovine protein phosphatase-2AC.
    • Davies, S. P., Helps, N. R., Cohen, P. T., Hardie, D. G. (1995) 50-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C alpha and native bovine protein phosphatase-2AC. FEBS Lett. 377 421-425.
    • (1995) FEBS Lett. , vol.377 , pp. 421-425
    • Davies, S.P.1    Helps, N.R.2    Cohen, P.T.3    Hardie, D.G.4
  • 59
    • 33751032385 scopus 로고    scopus 로고
    • Calcium microdomains: Organization and function
    • Berridge, M. J. (2006) Calcium microdomains: Organization and function. Cell Calcium 40 405-412.
    • (2006) Cell Calcium , vol.40 , pp. 405-412
    • Berridge, M.J.1
  • 61
    • 0031007065 scopus 로고    scopus 로고
    • The AMP-activated protein kinase-fuel gauge of the mammalian cell? Eur
    • Hardie, D. G., Carling, D. (1997) The AMP-activated protein kinase-fuel gauge of the mammalian cell? Eur. J. Biochem. 246 259-273.
    • (1997) J. Biochem. , vol.246 , pp. 259-273
    • Hardie, D.G.1    Carling, D.2
  • 62
    • 33747202449 scopus 로고    scopus 로고
    • Restricted diffusion of a freely diffusible second messenger: mechanisms underlying compartmentalized cAMP signalling
    • Zaccolo, M., Di Benedetto, G., Lissandron, V., Mancuso, L., Terrin, A., Zamparo, I. (2006) Restricted diffusion of a freely diffusible second messenger: mechanisms underlying compartmentalized cAMP signalling. Biochem. Soc. Trans. 34 495-497.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 495-497
    • Zaccolo, M.1    Di Benedetto, G.2    Lissandron, V.3    Mancuso, L.4    Terrin, A.5    Zamparo, I.6
  • 63
    • 0024786438 scopus 로고
    • Purification and characterization of the AMP-activated protein kinas. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl-CoA reductase kinase activities.
    • Carling, D., Clarke, P. R., Zammit, V. A., Hardie, D. G. (1989) Purification and characterization of the AMP-activated protein kinas. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl-CoA reductase kinase activities.. Eur. J. Biochem. 186 129-136.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 129-136
    • Carling, D.1    Clarke, P.R.2    Zammit, V.A.3    Hardie, D.G.4
  • 64
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Annu
    • Hardie, D. G., Carling, D., Carlson, M. (1998) The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67 821-855.
    • (1998) Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 66
    • 0344081177 scopus 로고    scopus 로고
    • Minireview: the AMP-activated protein kinase cascade: the key sensor of cellular energy status
    • Hardie, D. G. (2003) Minireview: the AMP-activated protein kinase cascade: the key sensor of cellular energy status. Endocrinology 144 5179-5183.
    • (2003) Endocrinology , vol.144 , pp. 5179-5183
    • Hardie, D.G.1
  • 67
    • 33748744959 scopus 로고    scopus 로고
    • Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity
    • Elbing, K., Rubenstein, E. M., McCartney, R. R., Schmidt, M. C. (2006) Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity. J. Biol. Chem. 281 26170-26180.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26170-26180
    • Elbing, K.1    Rubenstein, E.M.2    McCartney, R.R.3    Schmidt, M.C.4
  • 68
    • 0347318052 scopus 로고    scopus 로고
    • The AMP-activated protein kinase cascade-a unifying system for energy control
    • Carling, D. (2004) The AMP-activated protein kinase cascade-a unifying system for energy control. Trends Biochem. Sci. 29 18-24.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 18-24
    • Carling, D.1
  • 69
    • 27144548462 scopus 로고    scopus 로고
    • Crystal structure of the protein kinase domain of yeast AMPactivated protein kinase Snf1
    • Rudolph, M. J., Amodeo, G. A., Bai, Y., Tong, L. (2005) Crystal structure of the protein kinase domain of yeast AMPactivated protein kinase Snf1. Biochem. Biophys. Res. Commun. 337 1224-1228.
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1224-1228
    • Rudolph, M.J.1    Amodeo, G.A.2    Bai, Y.3    Tong, L.4
  • 70
    • 0032567252 scopus 로고    scopus 로고
    • Functional domains of the alpha1 catalytic subunit of the AMP-activated protein kinase
    • Crute, B. E., Seefeld, K., Gamble, J., Kemp, B. E., Witters, L. A. (1998) Functional domains of the alpha1 catalytic subunit of the AMP-activated protein kinase. J. Biol. Chem. 273 35347-35354.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35347-35354
    • Crute, B.E.1    Seefeld, K.2    Gamble, J.3    Kemp, B.E.4    Witters, L.A.5
  • 71
    • 33846945033 scopus 로고    scopus 로고
    • Conserved alpha helix acts as autoinhibitory sequence in AMPactivated protein kinase alpha subunits
    • Pang, T., Xiong, B., Li, J. Y., Qiu, B. Y., Jin, G. Z., Shen, J. K., Li, J. (2007) Conserved alpha helix acts as autoinhibitory sequence in AMPactivated protein kinase alpha subunits. J. Biol. Chem. 282 495-506.
    • (2007) J. Biol. Chem. , vol.282 , pp. 495-506
    • Pang, T.1    Xiong, B.2    Li, J.Y.3    Qiu, B.Y.4    Jin, G.Z.5    Shen, J.K.6    Li, J.7
  • 72
    • 0038814313 scopus 로고    scopus 로고
    • A Novel Domain in AMPActivated Protein Kinase Causes Glycogen Storage Bodies Similar to Those Seen in Hereditary Cardiac Arrhythmias
    • Hudson, E. R., Pan, D. A., James, J., Lucocq, J. M., Hawley, S. A., Green, K. A., Baba, O., Terashima, T., Hardie, D. G. (2003) A Novel Domain in AMPActivated Protein Kinase Causes Glycogen Storage Bodies Similar to Those Seen in Hereditary Cardiac Arrhythmias. Curr. Biol. 13 861-866.
    • (2003) Curr. Biol. , vol.13 , pp. 861-866
    • Hudson, E.R.1    Pan, D.A.2    James, J.3    Lucocq, J.M.4    Hawley, S.A.5    Green, K.A.6    Baba, O.7    Terashima, T.8    Hardie, D.G.9
  • 76
    • 1342332128 scopus 로고    scopus 로고
    • Bateman domains and adenosine derivatives form a binding contract
    • Kemp, B. E. (2004) Bateman domains and adenosine derivatives form a binding contract. J. Clin. Invest. 113 182-184.
    • (2004) J. Clin. Invest. , vol.113 , pp. 182-184
    • Kemp, B.E.1
  • 78
    • 0035910109 scopus 로고    scopus 로고
    • Novel PRKAG2 mutation responsible for the genetic syndrome of ventricular preexcitation and conduction system disease with childhood onset and absence of cardiac hypertrophy
    • Gollob, M. H., Seger, J. J., Gollob, T. N., Tapscott, T., Gonzales, O., Bachinski, L., Roberts, R. (2001) Novel PRKAG2 mutation responsible for the genetic syndrome of ventricular preexcitation and conduction system disease with childhood onset and absence of cardiac hypertrophy. Circulation 104 3030-3033.
    • (2001) Circulation , vol.104 , pp. 3030-3033
    • Gollob, M.H.1    Seger, J.J.2    Gollob, T.N.3    Tapscott, T.4    Gonzales, O.5    Bachinski, L.6    Roberts, R.7
  • 80
    • 0035872209 scopus 로고    scopus 로고
    • Mutations in the gamma(2) subunit of AMP-activated protein kinase cause familial hypertrophic cardiomyopathy: evidence for the central role of energy compromise in disease pathogenesis
    • Blair, E., Redwood, C., Ashrafian, H., Oliveira, M., Broxholme, J., Kerr, B., Salmon, A., Ostman-Smith, I., Watkins, H. (2001) Mutations in the gamma(2) subunit of AMP-activated protein kinase cause familial hypertrophic cardiomyopathy: evidence for the central role of energy compromise in disease pathogenesis. Hum. Mol. Genet. 10 1215-1220.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1215-1220
    • Blair, E.1    Redwood, C.2    Ashrafian, H.3    Oliveira, M.4    Broxholme, J.5    Kerr, B.6    Salmon, A.7    Ostman-Smith, I.8    Watkins, H.9
  • 81
    • 34047161436 scopus 로고    scopus 로고
    • Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase
    • Townley, R., Shapiro, L. (2007) Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase. Science 315 1726-1729.
    • (2007) Science , vol.315 , pp. 1726-1729
    • Townley, R.1    Shapiro, L.2
  • 83
    • 14544271907 scopus 로고    scopus 로고
    • AMP-activated protein kinase: balancing the scales
    • Carling, D. (2005) AMP-activated protein kinase: balancing the scales. Biochimie 87 87-91.
    • (2005) Biochimie , vol.87 , pp. 87-91
    • Carling, D.1
  • 84
    • 18944396765 scopus 로고    scopus 로고
    • Fatal congenital heart glycogenosis caused by a recurrent activating R531Q mutation in the gamma 2-subunit of AMP-activated protein kinase (PRKAG2), not by phosphorylase kinase deficiency
    • Burwinkel, B., Scott, J. W., Buhrer, C., van Landeghem, F. K., Cox, G. F., Wilson, C. J., Grahame Hardie, D., Kilimann, M. W. (2005) Fatal congenital heart glycogenosis caused by a recurrent activating R531Q mutation in the gamma 2-subunit of AMP-activated protein kinase (PRKAG2), not by phosphorylase kinase deficiency. Am. J. Hum. Genet. 76 1034-1049.
    • (2005) Am. J. Hum. Genet. , vol.76 , pp. 1034-1049
    • Burwinkel, B.1    Scott, J.W.2    Buhrer, C.3    Van Landeghem, F.K.4    Cox, G.F.5    Wilson, C.J.6    Grahame, H.D.7    Kilimann, M.W.8
  • 87
    • 33846955046 scopus 로고    scopus 로고
    • Regulation of AMP-activated protein kinase by a pseudosubstrate sequence on the gamma subunit
    • Scott, J. W., Ross, F. A., Liu, J. K. D., Hardie, D. G. (2007) Regulation of AMP-activated protein kinase by a pseudosubstrate sequence on the gamma subunit. EMBO J. 26 806-815.
    • (2007) EMBO J. , vol.26 , pp. 806-815
    • Scott, J.W.1    Ross, F.A.2    Liu, J.K.D.3    Hardie, D.G.4
  • 88
    • 0028845251 scopus 로고
    • 50-AMP activates the AMP-activated protein kinase cascade, and Ca2{thorn}/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
    • Hawley, S. A., Selbert, M. A., Goldstein, E. G., Edelman, A. M., Carling, D., Hardie, D. G. (1995) 50-AMP activates the AMP-activated protein kinase cascade, and Ca2{thorn}/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. J. Biol. Chem. 270 27186-27191.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27186-27191
    • Hawley, S.A.1    Selbert, M.A.2    Goldstein, E.G.3    Edelman, A.M.4    Carling, D.5    Hardie, D.G.6
  • 89
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade
    • Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Makela, T. P., Alessi, D. R., Hardie, D. G. (2003) Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J. Biol. 2, 28.
    • (2003) J. Biol. , vol.2 , pp. 28
    • Hawley, S.A.1    Boudeau, J.2    Reid, J.L.3    Mustard, K.J.4    Udd, L.5    Makela, T.P.6    Alessi, D.R.7    Hardie, D.G.8
  • 90
    • 34147152841 scopus 로고    scopus 로고
    • Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
    • Sanders, M. J., Grondin, P. O., Hegarty, B. D., Snowden, M. A., Carling, D. (2006) Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade. Biochem. J. 403 139-148.
    • (2006) Biochem. J. , vol.403 , pp. 139-148
    • Sanders, M.J.1    Grondin, P.O.2    Hegarty, B.D.3    Snowden, M.A.4    Carling, D.5
  • 92
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase
    • Hawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., Hardie, D. G. (1996) Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J. Biol. Chem. 271 27879-27887.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3    Davies, S.P.4    Beri, R.K.5    Carling, D.6    Hardie, D.G.7
  • 93
    • 0034141355 scopus 로고    scopus 로고
    • The regulation of AMP-activated protein kinase by phosphorylation
    • Stein, S. C., Woods, A., Jones, N. A., Davison, M. D., Carling, D. (2000) The regulation of AMP-activated protein kinase by phosphorylation. Biochem. J. 345 437-443.
    • (2000) Biochem. J. , vol.345 , pp. 437-443
    • Stein, S.C.1    Woods, A.2    Jones, N.A.3    Davison, M.D.4    Carling, D.5
  • 94
    • 1542618348 scopus 로고    scopus 로고
    • The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress
    • Shaw, R. J., Kosmatka, M., Bardeesy, N., Hurley, R. L., Witters, L. A., DePinho, R. A., Cantley, L. C. (2004) The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress. Proc. Natl. Acad. Sci. U.S.A. 101 3329-3335.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 3329-3335
    • Shaw, R.J.1    Kosmatka, M.2    Bardeesy, N.3    Hurley, R.L.4    Witters, L.A.5    DePinho, R.A.6    Cantley, L.C.7
  • 96
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase
    • Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G., Hardie, D. G. (2005) Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. Cell Metab. 2 9-19.
    • (2005) Cell Metab. , vol.2 , pp. 9-19
    • Hawley, S.A.1    Pan, D.A.2    Mustard, K.J.3    Ross, L.4    Bain, J.5    Edelman, A.M.6    Frenguelli, B.G.7    Hardie, D.G.8
  • 97
    • 23044437445 scopus 로고    scopus 로고
    • Ca2{thorn}/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells
    • Woods, A., Dickerson, K., Heath, R., Hong, S. P., Momcilovic, M., Johnstone, S. R., Carlson, M., Carling, D. (2005) Ca2{thorn}/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells. Cell Metab. 2 21-33.
    • (2005) Cell Metab. , vol.2 , pp. 21-33
    • Woods, A.1    Dickerson, K.2    Heath, R.3    Hong, S.P.4    Momcilovic, M.5    Johnstone, S.R.6    Carlson, M.7    Carling, D.8
  • 98
    • 23844471263 scopus 로고    scopus 로고
    • The Ca2{thorn}/ calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases
    • Hurley, R. L., Anderson, K. A., Franzone, J. M., Kemp, B. E., Means, A. R., Witters, L. A. (2005) The Ca2{thorn}/ calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases. J. Biol. Chem. 280 29060-29066.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29060-29066
    • Hurley, R.L.1    Anderson, K.A.2    Franzone, J.M.3    Kemp, B.E.4    Means, A.R.5    Witters, L.A.6
  • 99
    • 0037524354 scopus 로고    scopus 로고
    • LKB1, a protein kinase regulating cell proliferation and polarity
    • Boudeau, J., Sapkota, G., Alessi, D. R. (2003) LKB1, a protein kinase regulating cell proliferation and polarity. FEBS Lett. 546 159-165.
    • (2003) FEBS Lett. , vol.546 , pp. 159-165
    • Boudeau, J.1    Sapkota, G.2    Alessi, D.R.3
  • 100
    • 33745213627 scopus 로고    scopus 로고
    • AMPK and cell proliferation-AMPK as a therapeutic target for atherosclerosis and cancer
    • Motoshima, H., Goldstein, B. J., Igata, M., Araki, E. (2006) AMPK and cell proliferation-AMPK as a therapeutic target for atherosclerosis and cancer. J. Physiol. 574 63-71.
    • (2006) J. Physiol. , vol.574 , pp. 63-71
    • Motoshima, H.1    Goldstein, B.J.2    Igata, M.3    Araki, E.4
  • 101
    • 14244251499 scopus 로고    scopus 로고
    • Identification of the sucrose non-fermenting related kinase SNRK, as a novel LKB1 substrate
    • Jaleel, M., McBride, A., Lizcano, J. M., Deak, M., Toth, R., Morrice, N. A., Alessi, D. R. (2005) Identification of the sucrose non-fermenting related kinase SNRK, as a novel LKB1 substrate. FEBS Lett. 579 1417-1423.
    • (2005) FEBS Lett. , vol.579 , pp. 1417-1423
    • Jaleel, M.1    McBride, A.2    Lizcano, J.M.3    Deak, M.4    Toth, R.5    Morrice, N.A.6    Alessi, D.R.7
  • 103
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K., Zhu, T., Guan, K. L. (2003) TSC2 mediates cellular energy response to control cell growth and survival. Cell 115 577-590.
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 104
    • 0141753981 scopus 로고    scopus 로고
    • MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm
    • Boudeau, J., Baas, A. F., Deak, M., Morrice, N. A., Kieloch, A., Schutkowski, M., Prescott, A. R., Clevers, H. C., Alessi, D. R. (2003) MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm. EMBO J. 22 5102-5114.
    • (2003) EMBO J. , vol.22 , pp. 5102-5114
    • Boudeau, J.1    Baas, A.F.2    Deak, M.3    Morrice, N.A.4    Kieloch, A.5    Schutkowski, M.6    Prescott, A.R.7    Clevers, H.C.8    Alessi, D.R.9
  • 106
    • 20044370885 scopus 로고    scopus 로고
    • Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction
    • Sakamoto, K., McCarthy, A., Smith, D., Green, K. A., Grahame Hardie, D., Ashworth, A., Alessi, D. R. (2005) Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction. EMBO J. 24 1810-1820.
    • (2005) EMBO J. , vol.24 , pp. 1810-1820
    • Sakamoto, K.1    McCarthy, A.2    Smith, D.3    Green, K.A.4    Grahame, H.D.5    Ashworth, A.6    Alessi, D.R.7
  • 108
    • 0035028435 scopus 로고    scopus 로고
    • Ca(2{thorn})/CaM-dependent kinases: from activation to function
    • Hook, S. S., Means, A. R. (2001) Ca(2{thorn})/CaM-dependent kinases: from activation to function. Annu. Rev. Pharmacol. Toxicol. 41 471-505.
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 471-505
    • Hook, S.S.1    Means, A.R.2
  • 109
    • 0033137329 scopus 로고    scopus 로고
    • The Cacalmodulin-dependent protein kinase cascade
    • Soderling, T. R. (1999) The Cacalmodulin-dependent protein kinase cascade. Trends Biochem. Sci. 24 232-236.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 232-236
    • Soderling, T.R.1
  • 110
    • 0035830935 scopus 로고    scopus 로고
    • Cellular signaling through multifunctional Ca2{thorn}/calmodulindependent protein kinase II
    • Soderling, T. R., Chang, B., Brickey, D. (2001) Cellular signaling through multifunctional Ca2{thorn}/calmodulindependent protein kinase II. J. Biol. Chem. 276 3719-3722.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3719-3722
    • Soderling, T.R.1    Chang, B.2    Brickey, D.3
  • 111
    • 0035413609 scopus 로고    scopus 로고
    • Structure and regulation of calcium/ calmodulin-dependent protein kinases
    • Soderling, T. R., Stull, J. T. (2001) Structure and regulation of calcium/ calmodulin-dependent protein kinases. Chem. Rev. 101 2341-2352.
    • (2001) Chem. Rev. , vol.101 , pp. 2341-2352
    • Soderling, T.R.1    Stull, J.T.2
  • 112
    • 0242524520 scopus 로고    scopus 로고
    • Loss of Ca2{thorn}/calmodulin kinase kinase beta affects the formation of some, but not all, types of hippocampus-dependent long-term memory
    • Peters, M., Mizuno, K., Ris, L., Angelo, M., Godaux, E., Giese, K. P. (2003) Loss of Ca2{thorn}/calmodulin kinase kinase beta affects the formation of some, but not all, types of hippocampus-dependent long-term memory. J. Neurosci. 23 9752-9760.
    • (2003) J. Neurosci. , vol.23 , pp. 9752-9760
    • Peters, M.1    Mizuno, K.2    Ris, L.3    Angelo, M.4    Godaux, E.5    Giese, K.P.6
  • 114
    • 3843071026 scopus 로고    scopus 로고
    • Regulation and function of the calcium/ calmodulin-dependent protein kinase IV/protein serine/threonine phosphatase 2A signaling complex
    • Anderson, K. A., Noeldner, P. K., Reece, K., Wadzinski, B. E., Means, A. R. (2004) Regulation and function of the calcium/ calmodulin-dependent protein kinase IV/protein serine/threonine phosphatase 2A signaling complex. J. Biol. Chem. 279 31708-31716.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31708-31716
    • Anderson, K.A.1    Noeldner, P.K.2    Reece, K.3    Wadzinski, B.E.4    Means, A.R.5
  • 115
    • 33746979242 scopus 로고    scopus 로고
    • Thrombin activates AMP-activated protein kinase in endothelial cells via a pathway involving Ca2{thorn}/calmodulin-dependent protein kinase kinase beta
    • Stahmann, N., Woods, A., Carling, D., Heller, R. (2006) Thrombin activates AMP-activated protein kinase in endothelial cells via a pathway involving Ca2{thorn}/calmodulin-dependent protein kinase kinase beta. Mol. Cell. Biol. 26 5933-5945.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5933-5945
    • Stahmann, N.1    Woods, A.2    Carling, D.3    Heller, R.4
  • 116
    • 33745823168 scopus 로고    scopus 로고
    • Regulation of the energy sensor AMP-activated protein kinase by antigen receptor and Ca2{thorn} in T lymphocytes
    • Tamas, P., Hawley, S. A., Clarke, R. G., Mustard, K. J., Green, K., Hardie, D. G., Cantrell, D. A. (2006) Regulation of the energy sensor AMP-activated protein kinase by antigen receptor and Ca2{thorn} in T lymphocytes. J. Exp. Med. 203 1665-1670.
    • (2006) J. Exp. Med. , vol.203 , pp. 1665-1670
    • Tamas, P.1    Hawley, S.A.2    Clarke, R.G.3    Mustard, K.J.4    Green, K.5    Hardie, D.G.6    Cantrell, D.A.7
  • 117
    • 33748747706 scopus 로고    scopus 로고
    • Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro
    • Momcilovic, M., Hong, S. P., Carlson, M. (2006) Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro. J. Biol. Chem. 281 25336-25343.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.P.2    Carlson, M.3
  • 119
    • 33646828975 scopus 로고    scopus 로고
    • Insulin antagonizes ischemia-induced Thr172 phosphorylation of AMP-activated protein kinase alpha-subunits in heart via hierarchical phosphorylation of Ser485/491
    • Horman, S., Vertommen, D., Heath, R., Neumann, D., Mouton, V., Woods, A., Schlattner, U., Wallimann, T., Carling, D., Hue, L., Rider, M. H. (2006) Insulin antagonizes ischemia-induced Thr172 phosphorylation of AMP-activated protein kinase alpha-subunits in heart via hierarchical phosphorylation of Ser485/491. J. Biol. Chem. 281 5335-5340.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5335-5340
    • Horman, S.1    Vertommen, D.2    Heath, R.3    Neumann, D.4    Mouton, V.5    Woods, A.6    Schlattner, U.7    Wallimann, T.8    Carling, D.9    Hue, L.10    Rider, M.H.11
  • 120
    • 0141925771 scopus 로고    scopus 로고
    • Akt activity negatively regulates phosphorylation of AMP-activated protein kinase in the heart
    • Kovacic, S., Soltys, C. L., Barr, A. J., Shiojima, I., Walsh, K., Dyck, J. R. (2003) Akt activity negatively regulates phosphorylation of AMP-activated protein kinase in the heart. J. Biol. Chem. 278 39422-39427.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39422-39427
    • Kovacic, S.1    Soltys, C.L.2    Barr, A.J.3    Shiojima, I.4    Walsh, K.5    Dyck, J.R.6
  • 121
    • 33845972272 scopus 로고    scopus 로고
    • Regulation of AMP-activated protein kinase by multisite phosphorylation in response to agents that elevate cellular cAMP
    • Hurley, R. L., Barre, L. K., Wood, S. D., Anderson, K. A., Kemp, B. E., Means, A. R., Witters, L. A. (2006) Regulation of AMP-activated protein kinase by multisite phosphorylation in response to agents that elevate cellular cAMP. J. Biol. Chem. 281 36662-36672.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36662-36672
    • Hurley, R.L.1    Barre, L.K.2    Wood, S.D.3    Anderson, K.A.4    Kemp, B.E.5    Means, A.R.6    Witters, L.A.7
  • 122
    • 0034141636 scopus 로고    scopus 로고
    • LKB1, a novel serine/threonine protein kinase and potential tumour suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA) and prenylated in vivo
    • Collins, S. P., Reoma, J. L., Gamm, D. M., Uhler, M. D. (2000) LKB1, a novel serine/threonine protein kinase and potential tumour suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA) and prenylated in vivo. Biochem. J. 345 673-680.
    • (2000) Biochem. J. , vol.345 , pp. 673-680
    • Collins, S.P.1    Reoma, J.L.2    Gamm, D.M.3    Uhler, M.D.4
  • 124
    • 0025915269 scopus 로고
    • Evidence that AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMPactivated protein kinase. A sensitive mechanism to protect the cell against ATP depletion.
    • Moore, F., Weekes, J., Hardie, D. G. (1991) Evidence that AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMPactivated protein kinase. A sensitive mechanism to protect the cell against ATP depletion. . Eur. J. Biochem. 199 691-697.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 691-697
    • Moore, F.1    Weekes, J.2    Hardie, D.G.3
  • 125
    • 11144283125 scopus 로고    scopus 로고
    • Role of PP2C in cardiac lipid accumulation in obese rodents and its prevention by troglitazone
    • Wang, M. Y., Unger, R. H. (2005) Role of PP2C in cardiac lipid accumulation in obese rodents and its prevention by troglitazone. Am. J. Physiol. 288, E216-221.
    • (2005) Am. J. Physiol. , vol.288
    • Wang, M.Y.1    Unger, R.H.2
  • 127
    • 0028942747 scopus 로고
    • Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I
    • Dale, S., Wilson, W. A., Edelman, A. M., Hardie, D. G. (1995) Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Lett. 361 191-195.
    • (1995) FEBS Lett. , vol.361 , pp. 191-195
    • Dale, S.1    Wilson, W.A.2    Edelman, A.M.3    Hardie, D.G.4
  • 128
    • 0036290846 scopus 로고    scopus 로고
    • Protein kinase substrate recognition studied using the recombinant catalytic domain of AMPactivated protein kinase and a model substrate
    • Scott, J. W., Norman, D. G., Hawley, S. A., Kontogiannis, L., Hardie, D. G. (2002) Protein kinase substrate recognition studied using the recombinant catalytic domain of AMPactivated protein kinase and a model substrate. J. Mol. Biol. 317 309-323.
    • (2002) J. Mol. Biol. , vol.317 , pp. 309-323
    • Scott, J.W.1    Norman, D.G.2    Hawley, S.A.3    Kontogiannis, L.4    Hardie, D.G.5
  • 129
    • 0018337894 scopus 로고
    • Phosphorylation-dephosphorylation of enzymes
    • Krebs, E. G., Beavo, J. A. (1979) Phosphorylation-dephosphorylation of enzymes. Annu. Rev. Biochem. 48 923-959.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 923-959
    • Krebs, E.G.1    Beavo, J.A.2
  • 131
    • 0033815967 scopus 로고    scopus 로고
    • Characterization of the role of AMPactivated protein kinase in the regulation of glucose-activated gene expression using constitutively active and dominant negative forms of the kinase
    • Woods, A., Azzout-Marniche, D., Foretz, M., Stein, S. C., Lemarchand, P., Ferre, P., Foufelle, F., Carling, D. (2000) Characterization of the role of AMPactivated protein kinase in the regulation of glucose-activated gene expression using constitutively active and dominant negative forms of the kinase. Mol. Cell. Biol. 20 6704-6711.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6704-6711
    • Woods, A.1    Azzout-Marniche, D.2    Foretz, M.3    Stein, S.C.4    Lemarchand, P.5    Ferre, P.6    Foufelle, F.7    Carling, D.8
  • 133
    • 0345832116 scopus 로고    scopus 로고
    • Knockout of the alpha2 but not alpha1 50-AMP-activated protein kinase isoform abolishes 5-aminoimidazole-4-carboxamide-1-beta-4-ribofuranosidebut not contractioninduced glucose uptake in skeletal muscle
    • Jorgensen, S. B., Viollet, B., Andreelli, F., Frosig, C., Birk, J. B., Schjerling, P., Vaulont, S., Richter, E. A., Wojtaszewski, J. F. (2004) Knockout of the alpha2 but not alpha1 50-AMP-activated protein kinase isoform abolishes 5-aminoimidazole-4-carboxamide-1-beta-4-ribofuranosidebut not contractioninduced glucose uptake in skeletal muscle. J. Biol. Chem. 279 1070-1079.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1070-1079
    • Jorgensen, S.B.1    Viollet, B.2    Andreelli, F.3    Frosig, C.4    Birk, J.B.5    Schjerling, P.6    Vaulont, S.7    Richter, E.A.8    Wojtaszewski, J.F.9
  • 134
    • 10944237677 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiration by nitric oxide rapidly stimulates cytoprotective GLUT3-mediated glucose uptake through 50-AMP-activated protein kinase
    • Cidad, P., Almeida, A., Bolanos, J. P. (2004) Inhibition of mitochondrial respiration by nitric oxide rapidly stimulates cytoprotective GLUT3-mediated glucose uptake through 50-AMP-activated protein kinase. Biochem. J. 384 629-636.
    • (2004) Biochem. J. , vol.384 , pp. 629-636
    • Cidad, P.1    Almeida, A.2    Bolanos, J.P.3
  • 135
    • 0038043252 scopus 로고    scopus 로고
    • Adipose-specific expression, phosphorylation of Ser794 in insulin receptor substrate-1, and activation in diabetic animals of salt-inducible kinase-2
    • Horike, N., Takemori, H., Katoh, Y., Doi, J., Min, L., Asano, T., Sun, X. J., Yamamoto, H., Kasayama, S., Muraoka, M., Nonaka, Y., Okamoto, M. (2003) Adipose-specific expression, phosphorylation of Ser794 in insulin receptor substrate-1, and activation in diabetic animals of salt-inducible kinase-2. J. Biol. Chem. 278 18440-18447.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18440-18447
    • Horike, N.1    Takemori, H.2    Katoh, Y.3    Doi, J.4    Min, L.5    Asano, T.6    Sun, X.J.7    Yamamoto, H.8    Kasayama, S.9    Muraoka, M.10    Nonaka, Y.11    Okamoto, M.12
  • 138
    • 2942729619 scopus 로고    scopus 로고
    • LKB1 tumor suppressor protein: PARtaker in cell polarity
    • Baas, A. F., Smit, L., Clevers, H. (2004) LKB1 tumor suppressor protein: PARtaker in cell polarity. Trends Cell Biol. 14 312-319.
    • (2004) Trends Cell Biol. , vol.14 , pp. 312-319
    • Baas, A.F.1    Smit, L.2    Clevers, H.3
  • 139
    • 20444399500 scopus 로고    scopus 로고
    • Regulation of SNARK activity in response to cellular stresses
    • Lefebvre, D. L., Rosen, C. F. (2005) Regulation of SNARK activity in response to cellular stresses. Biochim. Biophys. Acta 1724 71-85.
    • (2005) Biochim. Biophys. Acta , vol.1724 , pp. 71-85
    • Lefebvre, D.L.1    Rosen, C.F.2
  • 140
    • 17144474893 scopus 로고    scopus 로고
    • Activity of LKB1 and AMPK-related kinases in skeletal muscle: effects of contraction, phenformin, and AICAR
    • Sakamoto, K., Goransson, O., Hardie, D. G., Alessi, D. R. (2004) Activity of LKB1 and AMPK-related kinases in skeletal muscle: effects of contraction, phenformin, and AICAR. Am. J. Physiol. 287, E310-317.
    • (2004) Am. J. Physiol. , vol.287
    • Sakamoto, K.1    Goransson, O.2    Hardie, D.G.3    Alessi, D.R.4
  • 142
    • 85047689953 scopus 로고
    • 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells?
    • Corton, J. M., Gillespie, J. G., Hawley, S. A., Hardie, D. G. (1995) 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells?. Eur. J. Biochem. 229 558-565.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 558-565
    • Corton, J.M.1    Gillespie, J.G.2    Hawley, S.A.3    Hardie, D.G.4
  • 143
    • 0028073143 scopus 로고
    • Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase
    • Sullivan, J. E., Brocklehurst, K. J., Marley, A. E., Carey, F., Carling, D., Beri, R. K. (1994) Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase. FEBS Lett. 353 33-36.
    • (1994) FEBS Lett. , vol.353 , pp. 33-36
    • Sullivan, J.E.1    Brocklehurst, K.J.2    Marley, A.E.3    Carey, F.4    Carling, D.5    Beri, R.K.6
  • 145
    • 2642614548 scopus 로고    scopus 로고
    • Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro
    • Anthonsen, M. W., Ronnstrand, L., Wernstedt, C., Degerman, E., Holm, C. (1998) Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro. J. Biol. Chem. 273 215-221.
    • (1998) J. Biol. Chem. , vol.273 , pp. 215-221
    • Anthonsen, M.W.1    Ronnstrand, L.2    Wernstedt, C.3    Degerman, E.4    Holm, C.5
  • 147
    • 4344618856 scopus 로고    scopus 로고
    • 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis
    • Rider, M. H., Bertrand, L., Vertommen, D., Michels, P. A., Rousseau, G. G., Hue, L. (2004) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis. Biochem. J. 381 561-579.
    • (2004) Biochem. J. , vol.381 , pp. 561-579
    • Rider, M.H.1    Bertrand, L.2    Vertommen, D.3    Michels, P.A.4    Rousseau, G.G.5    Hue, L.6
  • 149
    • 0033542476 scopus 로고    scopus 로고
    • Activation of nitric oxide synthase in endothelial cells by Aktdependent phosphorylation
    • Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., Zeiher, A. M. (1999) Activation of nitric oxide synthase in endothelial cells by Aktdependent phosphorylation. Nature 399 601-605.
    • (1999) Nature , vol.399 , pp. 601-605
    • Dimmeler, S.1    Fleming, I.2    Fisslthaler, B.3    Hermann, C.4    Busse, R.5    Zeiher, A.M.6
  • 150
    • 0037677096 scopus 로고    scopus 로고
    • Insulinstimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation
    • Sano, H., Kane, S., Sano, E., Miinea, C. P., Asara, J. M., Lane, W. S., Garner, C. W., Lienhard, G. E. (2003) Insulinstimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation. J. Biol. Chem. 278 14599-14602.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14599-14602
    • Sano, H.1    Kane, S.2    Sano, E.3    Miinea, C.P.4    Asara, J.M.5    Lane, W.S.6    Garner, C.W.7    Lienhard, G.E.8
  • 153
    • 0142149149 scopus 로고    scopus 로고
    • Myocardial ischemia and increased heart work modulate the phosphorylation state of eukaryotic elongation factor-2
    • Horman, S., Beauloye, C., Vertommen, D., Vanoverschelde, J. L., Hue, L., Rider, M. H. (2003) Myocardial ischemia and increased heart work modulate the phosphorylation state of eukaryotic elongation factor-2. J. Biol. Chem 278 41970-41976.
    • (2003) J. Biol. Chem , vol.278 , pp. 41970-41976
    • Horman, S.1    Beauloye, C.2    Vertommen, D.3    Vanoverschelde, J.L.4    Hue, L.5    Rider, M.H.6
  • 154
    • 0037025356 scopus 로고    scopus 로고
    • AMPactivated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling
    • Bolster, D. R., Crozier, S. J., Kimball, S. R., Jefferson, L. S. (2002) AMPactivated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J. Biol. Chem. 277 23977-23980.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23977-23980
    • Bolster, D.R.1    Crozier, S.J.2    Kimball, S.R.3    Jefferson, L.S.4
  • 155
    • 0037143449 scopus 로고    scopus 로고
    • Activation of AMPactivated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis
    • Horman, S., Browne, G. J., Krause, U., Patel, J. V., Vertommen, D., Bertrand, L., Lavoinne, A., Hue, L., Proud, C. G., Rider, M. H. (2002) Activation of AMPactivated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis. Curr. Biol. 12 1419-1423.
    • (2002) Curr. Biol. , vol.12 , pp. 1419-1423
    • Horman, S.1    Browne, G.J.2    Krause, U.3    Patel, J.V.4    Vertommen, D.5    Bertrand, L.6    Lavoinne, A.7    Hue, L.8    Proud, C.G.9    Rider, M.H.10
  • 156
    • 0036364274 scopus 로고    scopus 로고
    • Control of p70 ribosomal protein S6 kinase and acetylCoA carboxylase activity by AMP-activated protein kinase and protein phosphatases in isolated rat hepatocytes
    • Krause, U., Bertrand, L., Hue, L. (2002) Control of p70 ribosomal protein S6 kinase and acetylCoA carboxylase activity by AMP-activated protein kinase and protein phosphatases in isolated rat hepatocytes. Eur. J. Biochem. 269 3751-3759.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3751-3759
    • Krause, U.1    Bertrand, L.2    Hue, L.3
  • 157
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki, K., Li, Y., Zhu, T., Wu, J., Guan, K. L. (2002) TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 4 648-657.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 158
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and aminoacid deficiency on protein translation
    • Nave, B. T., Ouwens, M., Withers, D. J., Alessi, D. R., Shepherd, P. R. (1999) Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and aminoacid deficiency on protein translation. Biochem. J. 344 427-431.
    • (1999) Biochem. J. , vol.344 , pp. 427-431
    • Nave, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 159
    • 1942469564 scopus 로고    scopus 로고
    • Thr2446 is a novel mammalian target of rapamycin (mTOR) phosphorylation site regulated by nutrient status
    • Cheng, S. W., Fryer, L. G., Carling, D., Shepherd, P. R. (2004) Thr2446 is a novel mammalian target of rapamycin (mTOR) phosphorylation site regulated by nutrient status. J. Biol. Chem. 279 15719-15722.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15719-15722
    • Cheng, S.W.1    Fryer, L.G.2    Carling, D.3    Shepherd, P.R.4
  • 160
    • 0037067666 scopus 로고    scopus 로고
    • The Anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways
    • Fryer, L. G., Parbu-Patel, A., Carling, D. (2002) The Anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways. J. Biol. Chem. 277 25226-25232.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25226-25232
    • Fryer, L.G.1    Parbu-Patel, A.2    Carling, D.3
  • 163
    • 33745213627 scopus 로고    scopus 로고
    • AMPK and cell proliferation-AMPK as a therapeutic target for atherosclerosis and cancer
    • Motoshima, H., Goldstein, B. J., Igata, M., Araki, E. (2006) AMPK and cell proliferation-AMPK as a therapeutic target for atherosclerosis and cancer. J. Physiol. 574 63-71.
    • (2006) J. Physiol. , vol.574 , pp. 63-71
    • Motoshima, H.1    Goldstein, B.J.2    Igata, M.3    Araki, E.4
  • 164
    • 0023789884 scopus 로고
    • Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase
    • Munday, M. R., Campbell, D. G., Carling, D., Hardie, D. G. (1988) Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase. Eur. J. Biochem. 175 331-338.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 331-338
    • Munday, M.R.1    Campbell, D.G.2    Carling, D.3    Hardie, D.G.4
  • 166
    • 0029665214 scopus 로고    scopus 로고
    • Analysis of the specificity of the AMP-activated protein kinase by sitedirected mutagenesis of bacterially expressed 3-hydroxy 3-methylglutaryl-CoA reductase, using a single primer variant of the unique-site-elimination method
    • Ching, Y. P., Davies, S. P., Hardie, D. G. (1996) Analysis of the specificity of the AMP-activated protein kinase by sitedirected mutagenesis of bacterially expressed 3-hydroxy 3-methylglutaryl-CoA reductase, using a single primer variant of the unique-site-elimination method. Eur. J. Biochem. 237 800-808.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 800-808
    • Ching, Y.P.1    Davies, S.P.2    Hardie, D.G.3
  • 167
    • 0024335432 scopus 로고
    • The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase
    • Carling, D., Hardie, D. G. (1989) The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase. Biochim. Biophys. Acta 1012 81-86.
    • (1989) Biochim. Biophys. Acta , vol.1012 , pp. 81-86
    • Carling, D.1    Hardie, D.G.2
  • 168
    • 0037163076 scopus 로고    scopus 로고
    • The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase
    • Marsin, A.-S., Bouzin, C., Bertrand, L., Hue, L. (2002) The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase. J. Biol. Chem. 277 30778-30783.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30778-30783
    • Marsin, A.-S.1    Bouzin, C.2    Bertrand, L.3    Hue, L.4
  • 169
    • 0037040185 scopus 로고    scopus 로고
    • Mechanism for fatty acid ''sparing'' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMPactivated protein kinase
    • Kawaguchi, T., Osatomi, K., Yamashita, H., Kabashima, T., Uyeda, K. (2002) Mechanism for fatty acid ''sparing'' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMPactivated protein kinase. J. Biol. Chem. 277 3829-3835.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3829-3835
    • Kawaguchi, T.1    Osatomi, K.2    Yamashita, H.3    Kabashima, T.4    Uyeda, K.5
  • 170
    • 0042847434 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates HNF4alpha transcriptional activity by inhibiting dimer formation and decreasing protein stability
    • Hong, Y. H., Varanasi, U. S., Yang, W., Leff, T. (2003) AMP-activated protein kinase regulates HNF4alpha transcriptional activity by inhibiting dimer formation and decreasing protein stability. J. Biol. Chem. 278 27495-27501.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27495-27501
    • Hong, Y.H.1    Varanasi, U.S.2    Yang, W.3    Leff, T.4
  • 171
    • 0035914324 scopus 로고    scopus 로고
    • Regulation of transcription by AMP-activated protein kinase: phosphorylation of p300 blocks its interaction with nuclear receptors
    • Yang, W., Hong, Y. H., Shen, X. Q., Frankowski, C., Camp, H. S., Leff, T. (2001) Regulation of transcription by AMP-activated protein kinase: phosphorylation of p300 blocks its interaction with nuclear receptors. J. Biol. Chem. 276 38341-38344.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38341-38344
    • Yang, W.1    Hong, Y.H.2    Shen, X.Q.3    Frankowski, C.4    Camp, H.S.5    Leff, T.6
  • 172
    • 1642328617 scopus 로고    scopus 로고
    • Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398
    • Browne, G. J., Finn, S. G., Proud, C. G. (2004) Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398. J. Biol. Chem. 279 12220-12231.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12220-12231
    • Browne, G.J.1    Finn, S.G.2    Proud, C.G.3
  • 173
    • 0035861644 scopus 로고    scopus 로고
    • 50-AMPactivated protein kinase phosphorylates IRS-1 on Ser-789 in mouse C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside
    • Jakobsen, S. N., Hardie, D. G., Morrice, N., Tornqvist, H. E. (2001) 50-AMPactivated protein kinase phosphorylates IRS-1 on Ser-789 in mouse C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside. J. Biol. Chem. 276 46912-46916.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46912-46916
    • Jakobsen, S.N.1    Hardie, D.G.2    Morrice, N.3    Tornqvist, H.E.4
  • 174
    • 0031052020 scopus 로고    scopus 로고
    • Identification of Raf-1 Ser621 kinase activity from NIH 3T3 cells as AMPactivated protein kinase
    • Sprenkle, A. B., Davies, S. P., Carling, D., Hardie, D. G., Sturgill, T. W. (1997) Identification of Raf-1 Ser621 kinase activity from NIH 3T3 cells as AMPactivated protein kinase. FEBS Lett. 403 254-258.
    • (1997) FEBS Lett. , vol.403 , pp. 254-258
    • Sprenkle, A.B.1    Davies, S.P.2    Carling, D.3    Hardie, D.G.4    Sturgill, T.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.