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Volumn 39, Issue 1, 2011, Pages 1-13

AMP-activated protein kinase: A cellular energy sensor with a key role in metabolic disorders and in cancer

Author keywords

AMP activated protein kinase (AMPK); Cancer; Cell metabolism; Energy balance; Mitochondrion; Type 2 diabetes

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; GLYCOGEN PHOSPHORYLASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; METFORMIN; NUTRACEUTICAL;

EID: 79551487613     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0390001     Document Type: Conference Paper
Times cited : (145)

References (146)
  • 1
    • 0027178341 scopus 로고
    • Molecular analysis of the essential gene for adenylate kinase from the fission yeast Schizosaccharomyces pombe
    • Konrad, M. (1993) Molecular analysis of the essential gene for adenylate kinase from the fission yeast Schizosaccharomyces pombe. J. Biol. Chem. 268, 11326-11334
    • (1993) J. Biol. Chem. , vol.268 , pp. 11326-11334
    • Konrad, M.1
  • 2
    • 0035542970 scopus 로고    scopus 로고
    • AMP-activated protein kinase: The energy charge hypothesis revisited
    • Hardie, D.G. and 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
  • 3
    • 0001057329 scopus 로고
    • The action of nucleotides in the disruptive phosphorylation of glycogen
    • Cori, G.T., Colowick, S.P. and Cori, C.F. (1938) The action of nucleotides in the disruptive phosphorylation of glycogen. J. Biol. Chem. 123, 381-389
    • (1938) J. Biol. Chem. , vol.123 , pp. 381-389
    • Cori, G.T.1    Colowick, S.P.2    Cori, C.F.3
  • 4
    • 0000345889 scopus 로고
    • Studies on heart phosphofructokinase: Purification, inhibition and activation
    • Mansour, T.E. (1963) Studies on heart phosphofructokinase: purification, inhibition and activation. J. Biol. Chem. 238, 2285-2292
    • (1963) J. Biol. Chem. , vol.238 , pp. 2285-2292
    • Mansour, T.E.1
  • 5
    • 84883833752 scopus 로고
    • Adenylate as a metabolic regulator: Effect on yeast phosphofructokinase kinetics
    • Ramaiah, A., Hathaway, J.A. and Atkinson, D.E. (1964) Adenylate as a metabolic regulator: effect on yeast phosphofructokinase kinetics. J. Biol. Chem. 239, 3619-3622
    • (1964) J. Biol. Chem. , vol.239 , pp. 3619-3622
    • Ramaiah, A.1    Hathaway, J.A.2    Atkinson, D.E.3
  • 8
    • 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. and 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
  • 9
    • 0015918822 scopus 로고
    • Regulation of hepatic acetyl coenzyme A carboxylase by phosphorylation and dephosphorylation
    • Carlson, C.A. and Kim, K.H. (1973) Regulation of hepatic acetyl coenzyme A carboxylase by phosphorylation and dephosphorylation. J. Biol. Chem. 248, 378-380
    • (1973) J. Biol. Chem. , vol.248 , pp. 378-380
    • Carlson, C.A.1    Kim, K.H.2
  • 10
    • 0015864346 scopus 로고
    • Modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity with cAMP and with protein fractions of rat liver cytosol
    • Beg, Z.H., Allmann, D.W. and Gibson, D.M. (1973) Modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity with cAMP and with protein fractions of rat liver cytosol. Biochem. Biophys. Res. Commun. 54, 1362-1369
    • (1973) Biochem. Biophys. Res. Commun. , vol.54 , pp. 1362-1369
    • Beg, Z.H.1    Allmann, D.W.2    Gibson, D.M.3
  • 11
    • 0018963044 scopus 로고
    • Regulation of rat liver acetyl-CoA carboxylase: Regulation of phosphorylation and inactivation of acetyl-CoA carboxylase by the adenylate energy charge
    • Yeh, L.A., Lee, K.H. and Kim, K.H. (1980) Regulation of rat liver acetyl-CoA carboxylase: regulation of phosphorylation and inactivation of acetyl-CoA carboxylase by the adenylate energy charge. J. Biol. Chem. 255, 2308-2314
    • (1980) J. Biol. Chem. , vol.255 , pp. 2308-2314
    • Yeh, L.A.1    Lee, K.H.2    Kim, K.H.3
  • 12
    • 0017847168 scopus 로고
    • Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme a reductase and its inactivating enzyme: Evidence for regulation by phosphorylation-dephosphorylation
    • Ingebritsen, T.S., Lee, H., Parker, R.A. and Gibson, D.M. (1978) Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme A reductase and its inactivating enzyme: evidence for regulation by phosphorylation-dephosphorylation. Biochem. Biophys. Res. Commun. 81, 1268-1277
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 1268-1277
    • Ingebritsen, T.S.1    Lee, H.2    Parker, R.A.3    Gibson, D.M.4
  • 13
    • 0022371303 scopus 로고
    • Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme a reductase kinase by adenosine 5′-monophosphate
    • Ferrer, A., Caelles, C., Massot, N. and Hegardt, F.G. (1985) Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5′-monophosphate. Biochem. Biophys. Res. Commun. 132, 497-504
    • (1985) Biochem. Biophys. Res. Commun. , vol.132 , pp. 497-504
    • Ferrer, A.1    Caelles, C.2    Massot, N.3    Hegardt, F.G.4
  • 14
    • 0023642627 scopus 로고
    • A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis
    • Carling, D., Zammit, V.A. and Hardie, D.G. (1987) A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis. FEBS Lett. 223, 217-222
    • (1987) FEBS Lett. , vol.223 , pp. 217-222
    • Carling, D.1    Zammit, V.A.2    Hardie, D.G.3
  • 15
    • 0023896220 scopus 로고
    • The low activity of acetyl-CoA carboxylase in basal and glucagon-stimulated hepatocytes is due to phosphorylation by the AMP-activated protein kinase and not cyclic AMP-dependent protein kinase
    • Sim, A.T.R. and Hardie, D.G. (1988) The low activity of acetyl-CoA carboxylase in basal and glucagon-stimulated hepatocytes is due to phosphorylation by the AMP-activated protein kinase and not cyclic AMP-dependent protein kinase. FEBS Lett. 233, 294-298
    • (1988) FEBS Lett. , vol.233 , pp. 294-298
    • Sim, A.T.R.1    Hardie, D.G.2
  • 16
    • 0025310576 scopus 로고
    • Regulation of HMG-CoA reductase: Identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver
    • Clarke, P.R. and Hardie, D.G. (1990) Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver. EMBO J. 9, 2439-2446
    • (1990) EMBO J. , vol.9 , pp. 2439-2446
    • Clarke, P.R.1    Hardie, D.G.2
  • 17
    • 0024546378 scopus 로고
    • The AMP-activated protein kinase: A multisubstrate regulator of lipid metabolism
    • Hardie, D.G., Carling, D. and Sim, A.T.R. (1989) The AMP-activated protein kinase: a multisubstrate regulator of lipid metabolism. Trends Biochem. Sci. 14, 20-23
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 20-23
    • Hardie, D.G.1    Carling, D.2    Sim, A.T.R.3
  • 18
    • 34648828532 scopus 로고    scopus 로고
    • AMP-activated/SNF1 protein kinases: Conserved guardians of cellular energy
    • Hardie, D.G. (2007) AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy. Nat. Rev. Mol. Cell Biol. 8, 774-785
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 774-785
    • Hardie, D.G.1
  • 19
    • 0028070457 scopus 로고
    • Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo
    • Woods, A., Munday, M.R., Scott, J., Yang, X., Carlson, M. and Carling, D. (1994) Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo. J. Biol. Chem. 269, 19509-19515
    • (1994) J. Biol. Chem. , vol.269 , pp. 19509-19515
    • Woods, A.1    Munday, M.R.2    Scott, J.3    Yang, X.4    Carlson, M.5    Carling, D.6
  • 20
    • 67649484365 scopus 로고    scopus 로고
    • Structural insight into the autoinhibition mechanism of AMP-activated protein kinase
    • Chen, L., Jiao, Z.H., Zheng, L.S., Zhang, Y.Y., Xie, S.T., Wang, Z.X. and Wu, J.W. (2009) Structural insight into the autoinhibition mechanism of AMP-activated protein kinase. Nature 459, 1146-1149
    • (2009) Nature , vol.459 , pp. 1146-1149
    • Chen, L.1    Jiao, Z.H.2    Zheng, L.S.3    Zhang, Y.Y.4    Xie, S.T.5    Wang, Z.X.6    Wu, J.W.7
  • 22
    • 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 and activates AMP-activated protein kinase
    • Hawley, S.A., Davison, M., Woods, A., Davies, S.P., Beri, R.K., Carling, D. and 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 and activates 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
  • 23
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L.N., Noble, M.E.M. and Owen, D.J. (1996) Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 24
    • 0027979626 scopus 로고
    • Activation of rat liver AMP-activated protein kinase by the upstream kinase kinase in a purified, reconstituted system: Effects of AMP and AMP analogues
    • Weekes, J., Hawley, S.A., Corton, J., Shugar, D. and Hardie, D.G. (1994) Activation of rat liver AMP-activated protein kinase by the upstream kinase kinase in a purified, reconstituted system: effects of AMP and AMP analogues. Eur. J. Biochem. 219, 751-757
    • (1994) Eur. J. Biochem. , vol.219 , pp. 751-757
    • Weekes, J.1    Hawley, S.A.2    Corton, J.3    Shugar, D.4    Hardie, D.G.5
  • 26
    • 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. and Carling, D. (2007) Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade. Biochem. J. 403, 139-148
    • (2007) 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
  • 27
    • 0038814313 scopus 로고    scopus 로고
    • A novel domain in AMP-activated 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. and Hardie, D.G. (2003) A novel domain in AMP-activated 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
  • 29
    • 26444608572 scopus 로고    scopus 로고
    • Structural basis for glycogen recognition by AMP-activated protein kinase
    • DOI 10.1016/j.str.2005.07.008, PII S0969212605002674
    • Polekhina, G., Gupta, A., van Denderen, B.J., Feil, S.C., Kemp, B.E., Stapleton, D. and Parker, M.W. (2005) Structural basis for glycogen recognition by AMP-activated protein kinase. Structure 13, 1453-1462 (Pubitemid 41427585)
    • (2005) Structure , vol.13 , Issue.10 , pp. 1453-1462
    • Polekhina, G.1    Gupta, A.2    Van Denderen, B.J.W.3    Feil, S.C.4    Kemp, B.E.5    Stapleton, D.6    Parker, M.W.7
  • 30
    • 70349896067 scopus 로고    scopus 로고
    • Association of AMP-activated protein kinase subunits with glycogen particles as revealed in situ by immunoelectron microscopy
    • Bendayan, M., Londono, I., Kemp, B.E., Hardie, G.D., Ruderman, N. and Prentki, M. (2009) Association of AMP-activated protein kinase subunits with glycogen particles as revealed in situ by immunoelectron microscopy. J. Histochem. Cytochem. 57, 963-971
    • (2009) J. Histochem. Cytochem. , vol.57 , pp. 963-971
    • Bendayan, M.1    Londono, I.2    Kemp, B.E.3    Hardie, G.D.4    Ruderman, N.5    Prentki, M.6
  • 31
    • 57849090443 scopus 로고    scopus 로고
    • The glycogen-binding domain on AMP-activated protein kinase is a regulatory domain that allows the kinase to act as a sensor of glycogen structure
    • McBride, A., Ghilagaber, S., Nikolaev, A. and Hardie, D.G. (2009) The glycogen-binding domain on AMP-activated protein kinase is a regulatory domain that allows the kinase to act as a sensor of glycogen structure. Cell Metab. 9, 23-34
    • (2009) Cell Metab. , vol.9 , pp. 23-34
    • McBride, A.1    Ghilagaber, S.2    Nikolaev, A.3    Hardie, D.G.4
  • 32
    • 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
  • 33
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • Bateman, A. (1997) The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem. Sci. 22, 12-13
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 12-13
    • Bateman, A.1
  • 36
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • Hardie, D.G., Carling, D. and Carlson, M. (1998) The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67, 821-855
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 37
    • 10644282295 scopus 로고    scopus 로고
    • The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to lifespan in C. elegans
    • DOI 10.1101/gad.1255404
    • Apfeld, J., O'Connor, G., McDonagh, T., Distefano, P.S. and Curtis, R. (2004) The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to lifespan in C. elegans. Genes Dev. 18, 3004-3009 (Pubitemid 39658169)
    • (2004) Genes and Development , vol.18 , Issue.24 , pp. 3004-3009
    • Apfeld, J.1    O'Connor, G.2    McDonagh, T.3    DiStefano, P.S.4    Curtis, R.5
  • 38
    • 33645090940 scopus 로고    scopus 로고
    • Inhibition of germline proliferation during C. elegans dauer development requires PTEN, LKB1 and AMPK signalling
    • Narbonne, P. and Roy, R. (2006) Inhibition of germline proliferation during C. elegans dauer development requires PTEN, LKB1 and AMPK signalling. Development 133, 611-619
    • (2006) Development , vol.133 , pp. 611-619
    • Narbonne, P.1    Roy, R.2
  • 39
    • 2442611708 scopus 로고    scopus 로고
    • Snf1-related protein kinase 1 is needed for growth in a normal day-night light cycle
    • DOI 10.1038/sj.emboj.7600182
    • Thelander, M., Olsson, T. and Ronne, H. (2004) Snf1-related protein kinase 1 is needed for growth in a normal day-night light cycle. EMBO J. 23, 1900-1910 (Pubitemid 38649652)
    • (2004) EMBO Journal , vol.23 , Issue.8 , pp. 1900-1910
    • Thelander, M.1    Olsson, T.2    Ronne, H.3
  • 40
    • 33846290287 scopus 로고    scopus 로고
    • SNF1/AMPK/SnRK1 kinases, global regulators at the heart of energy control?
    • Polge, C. and Thomas, M. (2007) SNF1/AMPK/SnRK1 kinases, global regulators at the heart of energy control? Trends Plant Sci. 12, 20-28
    • (2007) Trends Plant Sci. , vol.12 , pp. 20-28
    • Polge, C.1    Thomas, M.2
  • 42
    • 0038583957 scopus 로고    scopus 로고
    • Yeast Pak1 kinase associates with and activates Snf1
    • Nath, N., McCartney, R.R. and Schmidt, M.C. (2003) Yeast Pak1 kinase associates with and activates Snf1. Mol. Cell. Biol. 23, 3909-3917
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3909-3917
    • Nath, N.1    McCartney, R.R.2    Schmidt, M.C.3
  • 44
    • 0041305909 scopus 로고    scopus 로고
    • Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases
    • Hong, S.P., Leiper, F.C., Woods, A., Carling, D. and Carlson, M. (2003) Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases. Proc. Natl. Acad. Sci. U.S.A. 100, 8839-8843
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 8839-8843
    • Hong, S.P.1    Leiper, F.C.2    Woods, A.3    Carling, D.4    Carlson, M.5
  • 45
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β 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. and Hardie, D.G. (2003) Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β 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
  • 50
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-β 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. and Hardie, D.G. (2005) Calmodulin-dependent protein kinase kinase-β 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
  • 56
    • 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. and 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
  • 58
    • 0031425839 scopus 로고    scopus 로고
    • AICAR decreases malonyl-CoA and increases fatty acid oxidation in skeletal muscle of the rat
    • Merrill, G.M., Kurth, E., Hardie, D.G. and Winder, W.W. (1997) AICAR decreases malonyl-CoA and increases fatty acid oxidation in skeletal muscle of the rat. Am. J. Physiol. 273, E1107-E1112
    • (1997) Am. J. Physiol. , vol.273
    • Merrill, G.M.1    Kurth, E.2    Hardie, D.G.3    Winder, W.W.4
  • 59
    • 0032765396 scopus 로고    scopus 로고
    • 5′ AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle
    • Kurth-Kraczek, E.J., Hirshman, M.F., Goodyear, L.J. and Winder, W.W. (1999) 5′ AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle. Diabetes 48, 1667-1671
    • (1999) Diabetes , vol.48 , pp. 1667-1671
    • Kurth-Kraczek, E.J.1    Hirshman, M.F.2    Goodyear, L.J.3    Winder, W.W.4
  • 62
    • 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. and Shulman, G.I. (2002) AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation. Proc. Natl. Acad. Sci. U.S.A. 99, 15983-15987
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 63
    • 34547545892 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
    • Jager, S., Handschin, C., St-Pierre, J. and Spiegelman, B.M. (2007) AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α. Proc. Natl. Acad. Sci. U.S.A. 104, 12017-12022
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12017-12022
    • Jager, S.1    Handschin, C.2    St-Pierre, J.3    Spiegelman, B.M.4
  • 65
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
    • DOI 10.1016/S0092-8674(03)00929-2
    • Inoki, K., Zhu, T. and Guan, K.L. (2003) TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577-590 (Pubitemid 37506046)
    • (2003) Cell , vol.115 , Issue.5 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.-L.3
  • 67
    • 0029978799 scopus 로고    scopus 로고
    • Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise
    • Winder, W.W. and Hardie, D.G. (1996) Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise. Am. J. Physiol. 270, E299-E304
    • (1996) Am. J. Physiol. , vol.270
    • Winder, W.W.1    Hardie, D.G.2
  • 68
    • 0028406897 scopus 로고
    • Role of the AMP-activated protein kinase in the cellular stress response
    • Corton, J.M., Gillespie, J.G. and Hardie, D.G. (1994) Role of the AMP-activated protein kinase in the cellular stress response. Curr. Biol. 4, 315-324
    • (1994) Curr. Biol. , vol.4 , pp. 315-324
    • Corton, J.M.1    Gillespie, J.G.2    Hardie, D.G.3
  • 69
    • 0032213768 scopus 로고    scopus 로고
    • AMP-activated protein kinase is activated by low glucose in cell lines derived from pancreatic β cells, and may regulate insulin release
    • Salt, I.P., Johnson, G., Ashcroft, S.J. H. and Hardie, D.G. (1998) AMP-activated protein kinase is activated by low glucose in cell lines derived from pancreatic β cells, and may regulate insulin release. Biochem. J. 335, 533-539
    • (1998) Biochem. J. , vol.335 , pp. 533-539
    • Salt, I.P.1    Johnson, G.2    Ashcroft, S.J.H.3    Hardie, D.G.4
  • 70
    • 0029093341 scopus 로고
    • High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5′-AMP-activated protein kinase inhibition of acetyl-CoA carboxylase
    • Kudo, N., Barr, A.J., Barr, R.L., Desai, S. and Lopaschuk, G.D. (1995) High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5′-AMP-activated protein kinase inhibition of acetyl-CoA carboxylase. J. Biol. Chem. 270, 17513-17520
    • (1995) J. Biol. Chem. , vol.270 , pp. 17513-17520
    • Kudo, N.1    Barr, A.J.2    Barr, R.L.3    Desai, S.4    Lopaschuk, G.D.5
  • 71
    • 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., Hardie, D.G., Ashworth, A. and 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    Hardie, D.G.5    Ashworth, A.6    Alessi, D.R.7
  • 72
    • 33644943620 scopus 로고    scopus 로고
    • AMPK: A key sensor of fuel and energy status in skeletal muscle
    • Hardie, D.G. and 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
  • 76
    • 40749132626 scopus 로고    scopus 로고
    • Key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
    • McCrimmon, R.J., Shaw, M., Fan, X., Cheng, H., Ding, Y., Vella, M.C., Zhou, L., McNay, E.C. and Sherwin, R.S. (2008) Key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia. Diabetes 57, 444-450
    • (2008) Diabetes , vol.57 , pp. 444-450
    • McCrimmon, R.J.1    Shaw, M.2    Fan, X.3    Cheng, H.4    Ding, Y.5    Vella, M.C.6    Zhou, L.7    McNay, E.C.8    Sherwin, R.S.9
  • 77
    • 29244463866 scopus 로고    scopus 로고
    • Does AMP-activated protein kinase couple inhibition of mitochondrial oxidative phosphorylation by hypoxia to calcium signaling in O2-sensing cells?
    • Evans, A.M., Mustard, K.J., Wyatt, C.N., Peers, C., Dipp, M., Kumar, P., Kinnear, N.P. and Hardie, D.G. (2005) Does AMP-activated protein kinase couple inhibition of mitochondrial oxidative phosphorylation by hypoxia to calcium signaling in O2-sensing cells? J. Biol. Chem. 280, 41504-41511
    • (2005) J. Biol. Chem. , vol.280 , pp. 41504-41511
    • Evans, A.M.1    Mustard, K.J.2    Wyatt, C.N.3    Peers, C.4    Dipp, M.5    Kumar, P.6    Kinnear, N.P.7    Hardie, D.G.8
  • 81
    • 0037122766 scopus 로고    scopus 로고
    • Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
    • Minokoshi, Y., Kim, Y.B., Peroni, O.D., Fryer, L.G., Muller, C., Carling, D. and Kahn, B.B. (2002) Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. Nature 415, 339-343
    • (2002) Nature , vol.415 , pp. 339-343
    • Minokoshi, Y.1    Kim, Y.B.2    Peroni, O.D.3    Fryer, L.G.4    Muller, C.5    Carling, D.6    Kahn, B.B.7
  • 85
    • 0036851817 scopus 로고    scopus 로고
    • Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase
    • Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K. et al. (2002) Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nat. Med. 6, 1288-1295
    • (2002) Nat. Med. , vol.6 , pp. 1288-1295
    • Yamauchi, T.1    Kamon, J.2    Minokoshi, Y.3    Ito, Y.4    Waki, H.5    Uchida, S.6    Yamashita, S.7    Noda, M.8    Kita, S.9    Ueki, K.10
  • 86
    • 18844432308 scopus 로고    scopus 로고
    • Adiponectin and adiponectin receptors
    • Kadowaki, T. and Yamauchi, T. (2005) Adiponectin and adiponectin receptors. Endocr. Rev. 26, 439-451
    • (2005) Endocr. Rev. , vol.26 , pp. 439-451
    • Kadowaki, T.1    Yamauchi, T.2
  • 87
    • 33750859187 scopus 로고    scopus 로고
    • Interleukin-6 increases insulin-stimulated glucose disposal in humans and glucose uptake and fatty acid oxidation in vitro via AMP-activated protein kinase
    • Carey, A.L., Steinberg, G.R., Macaulay, S.L., Thomas, W.G., Holmes, A.G., Ramm, G., Prelovsek, O., Hohnen-Behrens, C., Watt, M.J., James, D.E. et al. (2006) Interleukin-6 increases insulin-stimulated glucose disposal in humans and glucose uptake and fatty acid oxidation in vitro via AMP-activated protein kinase. Diabetes 55, 2688-2697
    • (2006) Diabetes , vol.55 , pp. 2688-2697
    • Carey, A.L.1    Steinberg, G.R.2    Macaulay, S.L.3    Thomas, W.G.4    Holmes, A.G.5    Ramm, G.6    Prelovsek, O.7    Hohnen-Behrens, C.8    Watt, M.J.9    James, D.E.10
  • 88
    • 33746037555 scopus 로고    scopus 로고
    • Ciliary neurotrophic factor suppresses hypothalamic AMP-kinase signaling in leptin-resistant obese mice
    • DOI 10.1210/en.2005-1587
    • Steinberg, G.R., Watt, M.J., Fam, B.C., Proietto, J., Andrikopoulos, S., Allen, A.M., Febbraio, M.A. and Kemp, B.E. (2006) Ciliary neurotrophic factor suppresses hypothalamic AMP-kinase signaling in leptin-resistant obese mice. Endocrinology 147, 3906-3914 (Pubitemid 44079396)
    • (2006) Endocrinology , vol.147 , Issue.8 , pp. 3906-3914
    • Steinberg, G.R.1    Watt, M.J.2    Fam, B.C.3    Proietto, J.4    Andrikopoulos, S.5    Allen, A.M.6    Febbraio, M.A.7    Kemp, B.E.8
  • 90
    • 38749137749 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor stimulates AMP-activated protein kinase in the ischaemic heart
    • DOI 10.1038/nature06504, PII NATURE06504
    • Miller, E.J., Li, J., Leng, L., McDonald, C., Atsumi, T., Bucala, R. and Young, L.H. (2008) Macrophage migration inhibitory factor stimulates AMP-activated protein kinase in the ischaemic heart. Nature 451, 578-582 (Pubitemid 351186266)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 578-582
    • Miller, E.J.1    Li, J.2    Leng, L.3    McDonald, C.4    Atsumi, T.5    Bucala, R.6    Young, L.H.7
  • 92
    • 0032792665 scopus 로고    scopus 로고
    • The AMP-activated protein kinase, a metabolic master switch: Possible roles in Type 2 diabetes
    • Winder, W.W. and Hardie, D.G. (1999) The AMP-activated protein kinase, a metabolic master switch: possible roles in Type 2 diabetes. Am. J. Physiol. 277, E1-E10
    • (1999) Am. J. Physiol. , vol.277
    • Winder, W.W.1    Hardie, D.G.2
  • 93
    • 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. and 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
  • 95
    • 0035155821 scopus 로고    scopus 로고
    • Chronic treatment with 5-aminoimidazole-4-carboxamide-1-β-d- ribofuranoside increases insulin-stimulated glucose uptake and GLUT4 translocation in rat skeletal muscles in a fiber type-specific manner
    • Buhl, E.S., Jessen, N., Schmitz, O., Pedersen, S.B., Pedersen, O., Holman, G.D. and Lund, S. (2001) Chronic treatment with 5-aminoimidazole-4- carboxamide-1-β-d-ribofuranoside increases insulin-stimulated glucose uptake and GLUT4 translocation in rat skeletal muscles in a fiber type-specific manner. Diabetes 50, 12-17
    • (2001) Diabetes , vol.50 , pp. 12-17
    • Buhl, E.S.1    Jessen, N.2    Schmitz, O.3    Pedersen, S.B.4    Pedersen, O.5    Holman, G.D.6    Lund, S.7
  • 96
    • 0035029874 scopus 로고    scopus 로고
    • Effect of 5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside infusion on in vivo glucose and lipid metabolism in lean and obese Zucker rats
    • Bergeron, R., Previs, S.F., Cline, G.W., Perret, P., Russell, R.R., 3rd, Young, L.H. and Shulman, G.I. (2001) Effect of 5-aminoimidazole-4-carboxamide-1- β-d-ribofuranoside infusion on in vivo glucose and lipid metabolism in lean and obese Zucker rats. Diabetes 50, 1076-1082
    • (2001) Diabetes , vol.50 , pp. 1076-1082
    • Bergeron, R.1    Previs, S.F.2    Cline, G.W.3    Perret, P.4    Russell III, R.R.5    Young, L.H.6    Shulman, G.I.7
  • 97
    • 0036788292 scopus 로고    scopus 로고
    • AICAR administration causes an apparent enhancement of muscle and liver insulin action in insulin-resistant high-fat-fed rats
    • Iglesias, M.A., Ye, J.M., Frangioudakis, G., Saha, A.K., Tomas, E., Ruderman, N.B., Cooney, G.J. and Kraegen, E.W. (2002) AICAR administration causes an apparent enhancement of muscle and liver insulin action in insulin-resistant high-fat-fed rats. Diabetes 51, 2886-2894
    • (2002) Diabetes , vol.51 , pp. 2886-2894
    • Iglesias, M.A.1    Ye, J.M.2    Frangioudakis, G.3    Saha, A.K.4    Tomas, E.5    Ruderman, N.B.6    Cooney, G.J.7    Kraegen, E.W.8
  • 99
    • 0037067666 scopus 로고    scopus 로고
    • The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct pathways
    • Fryer, L.G., Parbu-Patel, A. and Carling, D. (2002) The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct 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
  • 100
    • 0036324142 scopus 로고    scopus 로고
    • The anti-diabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism
    • Hawley, S.A., Gadalla, A.E., Olsen, G.S. and Hardie, D.G. (2002) The anti-diabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism. Diabetes 51, 2420-2425
    • (2002) Diabetes , vol.51 , pp. 2420-2425
    • Hawley, S.A.1    Gadalla, A.E.2    Olsen, G.S.3    Hardie, D.G.4
  • 101
    • 28844433635 scopus 로고    scopus 로고
    • Medicine: The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin
    • DOI 10.1126/science.1120781
    • Shaw, R.J., Lamia, K.A., Vasquez, D., Koo, S.H., Bardeesy, N., Depinho, R.A., Montminy, M. and Cantley, L.C. (2005) The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin. Science 310, 1642-1646 (Pubitemid 41780780)
    • (2005) Science , vol.310 , Issue.5754 , pp. 1642-1646
    • Shaw, R.J.1    Lamia, K.A.2    Vasquez, D.3    Koo, S.-H.4    Bardeesy, N.5    DePinho, R.A.6    Montminy, M.7    Cantley, L.C.8
  • 103
    • 0029016829 scopus 로고
    • An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor γ (PPARγ )
    • Lehmann, J.M., Moore, L.B., Smith-Oliver, T.A., Wilkison, W.O., Willson, T.M. and Kliewer, S.A. (1995) An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor γ (PPARγ ). J. Biol. Chem. 270, 12953-12956
    • (1995) J. Biol. Chem. , vol.270 , pp. 12953-12956
    • Lehmann, J.M.1    Moore, L.B.2    Smith-Oliver, T.A.3    Wilkison, W.O.4    Willson, T.M.5    Kliewer, S.A.6
  • 106
    • 27744455616 scopus 로고    scopus 로고
    • Genistein, EGCG, and capsaicin inhibit adipocyte differentiation process via activating AMP-activated protein kinase
    • Hwang, J.T., Park, I.J., Shin, J.I., Lee, Y.K., Lee, S.K., Baik, H.W., Ha, J. and Park, O.J. (2005) Genistein, EGCG, and capsaicin inhibit adipocyte differentiation process via activating AMP-activated protein kinase. Biochem. Biophys. Res. Commun. 338, 694-699
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 694-699
    • Hwang, J.T.1    Park, I.J.2    Shin, J.I.3    Lee, Y.K.4    Lee, S.K.5    Baik, H.W.6    Ha, J.7    Park, O.J.8
  • 107
    • 48949115243 scopus 로고    scopus 로고
    • The anti-obesity effect of quercetin is mediated by the AMPK and MAPK signaling pathways
    • Ahn, J., Lee, H., Kim, S., Park, J. and Ha, T. (2008) The anti-obesity effect of quercetin is mediated by the AMPK and MAPK signaling pathways. Biochem. Biophys. Res. Commun. 373, 545-549
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 545-549
    • Ahn, J.1    Lee, H.2    Kim, S.3    Park, J.4    Ha, T.5
  • 108
    • 33749336146 scopus 로고    scopus 로고
    • Berberine, a natural plant product, activates AMP-activated protein kinase with beneficial metabolic effects in diabetic and insulin-resistant states
    • Lee, Y.S., Kim, W.S., Kim, K.H., Yoon, M.J., Cho, H.J., Shen, Y., Ye, J.M., Lee, C.H., Oh, W.K., Kim, C.T. et al. (2006) Berberine, a natural plant product, activates AMP-activated protein kinase with beneficial metabolic effects in diabetic and insulin-resistant states. Diabetes 55, 2256-2264
    • (2006) Diabetes , vol.55 , pp. 2256-2264
    • Lee, Y.S.1    Kim, W.S.2    Kim, K.H.3    Yoon, M.J.4    Cho, H.J.5    Shen, Y.6    Ye, J.M.7    Lee, C.H.8    Oh, W.K.9    Kim, C.T.10
  • 109
    • 0034659785 scopus 로고    scopus 로고
    • Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain
    • Owen, M.R., Doran, E. and Halestrap, A.P. (2000) Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain. Biochem. J. 348, 607-614
    • (2000) Biochem. J. , vol.348 , pp. 607-614
    • Owen, M.R.1    Doran, E.2    Halestrap, A.P.3
  • 110
    • 0034614420 scopus 로고    scopus 로고
    • Dimethylbiguanide inhibits cell respiration via an indirect effect targeted on the respiratory chain complex I
    • El-Mir, M.Y., Nogueira, V., Fontaine, E., Averet, N., Rigoulet, M. and Leverve, X. (2000) Dimethylbiguanide inhibits cell respiration via an indirect effect targeted on the respiratory chain complex I. J. Biol. Chem. 275, 223-228
    • (2000) J. Biol. Chem. , vol.275 , pp. 223-228
    • El-Mir, M.Y.1    Nogueira, V.2    Fontaine, E.3    Averet, N.4    Rigoulet, M.5    Leverve, X.6
  • 112
    • 48449084609 scopus 로고    scopus 로고
    • Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: A mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action
    • Turner, N., Li, J.Y., Gosby, A., To, S.W., Cheng, Z., Miyoshi, H., Taketo, M.M., Cooney, G.J., Kraegen, E.W., James, D.E. et al. (2008) Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: a mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action. Diabetes 57, 1414-1418
    • (2008) Diabetes , vol.57 , pp. 1414-1418
    • Turner, N.1    Li, J.Y.2    Gosby, A.3    To, S.W.4    Cheng, Z.5    Miyoshi, H.6    Taketo, M.M.7    Cooney, G.J.8    Kraegen, E.W.9    James, D.E.10
  • 113
    • 35348865444 scopus 로고    scopus 로고
    • Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols
    • Gledhill, J.R., Montgomery, M.G., Leslie, A.G. and Walker, J.E. (2007) Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols. Proc. Natl. Acad. Sci. U.S.A. 104, 13632-13637
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 13632-13637
    • Gledhill, J.R.1    Montgomery, M.G.2    Leslie, A.G.3    Walker, J.E.4
  • 115
    • 33744514139 scopus 로고    scopus 로고
    • Identification and characterization of a small molecule AMPK activator that treats key components of Type 2 diabetes and the metabolic syndrome
    • Cool, B., Zinker, B., Chiou, W., Kifle, L., Cao, N., Perham, M., Dickinson, R., Adler, A., Gagne, G., Iyengar, R. et al. (2006) Identification and characterization of a small molecule AMPK activator that treats key components of Type 2 diabetes and the metabolic syndrome. Cell Metab. 3, 403-416
    • (2006) Cell Metab. , vol.3 , pp. 403-416
    • Cool, B.1    Zinker, B.2    Chiou, W.3    Kifle, L.4    Cao, N.5    Perham, M.6    Dickinson, R.7    Adler, A.8    Gagne, G.9    Iyengar, R.10
  • 117
    • 36348978499 scopus 로고    scopus 로고
    • Defining the mechanism of activation of AMP-activated protein kinase by the small molecule a-769662, a member of the thienopyridone family
    • Sanders, M.J., Ali, Z.S., Hegarty, B.D., Heath, R., Snowden, M.A. and Carling, D. (2007) Defining the mechanism of activation of AMP-activated protein kinase by the small molecule A-769662, a member of the thienopyridone family. J. Biol. Chem. 282, 32539-32548
    • (2007) J. Biol. Chem. , vol.282 , pp. 32539-32548
    • Sanders, M.J.1    Ali, Z.S.2    Hegarty, B.D.3    Heath, R.4    Snowden, M.A.5    Carling, D.6
  • 119
    • 0035138620 scopus 로고    scopus 로고
    • Method for the quantitative extraction of resveratrol and piceid isomers in grape berry skins: Effect of powdery mildew on the stilbene content
    • Romero-Perez, A.I., Lamuela-Raventos, R.M., Andres-Lacueva, C. and de La Torre-Boronat, M.C. (2001) Method for the quantitative extraction of resveratrol and piceid isomers in grape berry skins: effect of powdery mildew on the stilbene content. J. Agric. Food Chem. 49, 210-215
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 210-215
    • Romero-Perez, A.I.1    Lamuela-Raventos, R.M.2    Andres-Lacueva, C.3    De La Torre-Boronat, M.C.4
  • 121
    • 0035929359 scopus 로고    scopus 로고
    • Cell cycle regulation via p53 phosphorylation by a 5′-AMP activated protein kinase activator, 5-aminoimidazole-4-carboxamide-1-β-d- ribofuranoside, in a human hepatocellular carcinoma cell line
    • Imamura, K., Ogura, T., Kishimoto, A., Kaminishi, M. and Esumi, H. (2001) Cell cycle regulation via p53 phosphorylation by a 5′-AMP activated protein kinase activator, 5-aminoimidazole-4-carboxamide-1-β-d- ribofuranoside, in a human hepatocellular carcinoma cell line. Biochem. Biophys. Res. Commun. 287, 562-567
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 562-567
    • Imamura, K.1    Ogura, T.2    Kishimoto, A.3    Kaminishi, M.4    Esumi, H.5
  • 122
    • 0343550889 scopus 로고
    • Über die airkung von blausäureäthylester (äthylcarbylamin) auf die Pasteursche reaktion
    • Warburg, O. (1926) Über die airkung von blausäureä thylester (äthylcarbylamin) auf die Pasteursche reaktion. Biochem. Z. 172, 432-441
    • (1926) Biochem. Z. , vol.172 , pp. 432-441
    • Warburg, O.1
  • 123
    • 0033949848 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle
    • Winder, W.W., Holmes, B.F., Rubink, D.S., Jensen, E.B., Chen, M. and Holloszy, J.O. (2000) Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle. J. Appl. Physiol. 88, 2219-2226
    • (2000) J. Appl. Physiol. , vol.88 , pp. 2219-2226
    • Winder, W.W.1    Holmes, B.F.2    Rubink, D.S.3    Jensen, E.B.4    Chen, M.5    Holloszy, J.O.6
  • 126
    • 33645766204 scopus 로고    scopus 로고
    • Increased cancer-related mortality for patients with type 2 diabetes who use sulfonylureas or insulin
    • Bowker, S.L., Majumdar, S.R., Veugelers, P. and Johnson, J.A. (2006) Increased cancer-related mortality for patients with Type 2 diabetes who use sulfonylureas or insulin. Diabetes Care 29, 254-258 (Pubitemid 44106500)
    • (2006) Diabetes Care , vol.29 , Issue.2 , pp. 254-258
    • Bowker, S.L.1    Majumdar, S.R.2    Veugelers, P.3    Johnson, J.A.4
  • 128
    • 70349658548 scopus 로고    scopus 로고
    • A cohort study of the risk of cancer associated with Type 2 diabetes
    • Ogunleye, A.A., Ogston, S.A., Morris, A.D. and Evans, J.M. (2009) A cohort study of the risk of cancer associated with Type 2 diabetes. Br. J. Cancer 101, 1199-1201
    • (2009) Br. J. Cancer , vol.101 , pp. 1199-1201
    • Ogunleye, A.A.1    Ogston, S.A.2    Morris, A.D.3    Evans, J.M.4
  • 129
    • 68449094325 scopus 로고    scopus 로고
    • The influence of glucose-lowering therapies on cancer risk in Type 2 diabetes
    • Currie, C.J., Poole, C.D. and Gale, E.A. (2009) The influence of glucose-lowering therapies on cancer risk in Type 2 diabetes. Diabetologia 52, 1766-1777
    • (2009) Diabetologia , vol.52 , pp. 1766-1777
    • Currie, C.J.1    Poole, C.D.2    Gale, E.A.3
  • 133
    • 70350583054 scopus 로고    scopus 로고
    • Metformin use and prostate cancer in Caucasian men: Results from a population-based case-control study
    • Wright, J.L. and Stanford, J.L. (2009) Metformin use and prostate cancer in Caucasian men: results from a population-based case-control study. Cancer Causes Control 20, 1617-1622
    • (2009) Cancer Causes Control , vol.20 , pp. 1617-1622
    • Wright, J.L.1    Stanford, J.L.2
  • 144
    • 58649110598 scopus 로고    scopus 로고
    • Oncogenic B-RAF negatively regulates the tumor suppressor LKB1 to promote melanoma cell proliferation
    • Zheng, B., Jeong, J.H., Asara, J.M., Yuan, Y.Y., Granter, S.R., Chin, L. and Cantley, L.C. (2009) Oncogenic B-RAF negatively regulates the tumor suppressor LKB1 to promote melanoma cell proliferation. Mol. Cell 33, 237-247
    • (2009) Mol. Cell , vol.33 , pp. 237-247
    • Zheng, B.1    Jeong, J.H.2    Asara, J.M.3    Yuan, Y.Y.4    Granter, S.R.5    Chin, L.6    Cantley, L.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.