메뉴 건너뛰기




Volumn 127, Issue 6, 2004, Pages 1798-1808

The role of AMP-activated protein kinase in the action of ethanol in the liver

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINO 4 IMIDAZOLECARBOXAMIDE RIBOSIDE; ACETYL COENZYME A CARBOXYLASE; ALCOHOL; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; METFORMIN; PALMITIC ACID; STEROL REGULATORY ELEMENT BINDING PROTEIN 1;

EID: 9644290860     PISSN: 00165085     EISSN: None     Source Type: Journal    
DOI: 10.1053/j.gastro.2004.09.049     Document Type: Article
Times cited : (406)

References (54)
  • 1
    • 0001513966 scopus 로고    scopus 로고
    • Obesity increases sensitivity to endotoxin liver injury: Implications for the pathogenesis of steatohepatitis
    • S.Q. Yang, H.Z. Lin, M.D. Lane, M. Clemens, A.M. Diehl Obesity increases sensitivity to endotoxin liver injury implications for the pathogenesis of steatohepatitis Proc Natl Acad Sci U S A 94 1997 2557 2562
    • (1997) Proc Natl Acad Sci U S a , vol.94 , pp. 2557-2562
    • Yang, S.Q.1    Lin, H.Z.2    Lane, M.D.3    Clemens, M.4    Diehl, A.M.5
  • 2
    • 0034890078 scopus 로고    scopus 로고
    • Fatty liver vulnerability to endotoxin-induced damage despite NF-κB induction and inhibited caspase 3 activation
    • S. Yang, H. Lin, A.M. Diehl Fatty liver vulnerability to endotoxin-induced damage despite NF-κB induction and inhibited caspase 3 activation Am J Physiol Gastrointest Liver Physiol 281 2001 G382 G392
    • (2001) Am J Physiol Gastrointest Liver Physiol , vol.281
    • Yang, S.1    Lin, H.2    Diehl, A.M.3
  • 3
    • 0034970161 scopus 로고    scopus 로고
    • Nonalcoholic fatty liver disease: Implications for alcoholic liver disease pathogenesis
    • A.M. Diehl Nonalcoholic fatty liver disease implications for alcoholic liver disease pathogenesis Alcohol Clin Exp Res 25 2001 8S 14S
    • (2001) Alcohol Clin Exp Res , vol.25
    • Diehl, A.M.1
  • 5
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • D.G. Hardie, D. Carling, M. Carlson The AMP-activated/SNF1 protein kinase subfamily metabolic sensors of the eukaryotic cell? Annu Rev Biochem 67 1998 821 855
    • (1998) Annu Rev Biochem , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 6
    • 0032792665 scopus 로고    scopus 로고
    • AMP-activated protein kinase, a metabolic master switch: Possible roles in type 2 diabetes
    • W.W. Winder, D.G. Hardie AMP-activated protein kinase, a metabolic master switch possible roles in type 2 diabetes Am J Physiol 277 1999 E1 E10
    • (1999) Am J Physiol , vol.277
    • Winder, W.W.1    Hardie, D.G.2
  • 7
    • 0035970805 scopus 로고    scopus 로고
    • Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2
    • L. Abu-Elheiga, M.M. Matzuk, K.A. Abo-Hashema, S.J. Wakil Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2 Science 291 2001 2613 2616
    • (2001) Science , vol.291 , pp. 2613-2616
    • Abu-Elheiga, L.1    Matzuk, M.M.2    Abo-Hashema, K.A.3    Wakil, S.J.4
  • 9
    • 0142181286 scopus 로고    scopus 로고
    • Malonyl-CoA and AMP-activated protein kinase: An expanding partnership
    • A.K. Saha, N.B. Ruderman Malonyl-CoA and AMP-activated protein kinase an expanding partnership Mol Cell Biochem 253 2003 65 70
    • (2003) Mol Cell Biochem , vol.253 , pp. 65-70
    • Saha, A.K.1    Ruderman, N.B.2
  • 10
    • 0036324142 scopus 로고    scopus 로고
    • The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism
    • S.A. Hawley, A.E. Gadalla, G.S. Olsen, D.G. Hardie The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism Diabetes 51 2002 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
  • 11
    • 0037067666 scopus 로고    scopus 로고
    • The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways
    • L.G. Fryer, A. Parbu-Patel, D. Carling The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways J Biol Chem 277 2002 25226 25232
    • (2002) J Biol Chem , vol.277 , pp. 25226-25232
    • Fryer, L.G.1    Parbu-Patel, A.2    Carling, D.3
  • 12
  • 15
    • 0036251153 scopus 로고    scopus 로고
    • SREBPs: Activators of the complete program of cholesterol and fatty acid synthesis in the liver
    • J.D. Horton, J.L. Goldstein, M.S. Brown SREBPs activators of the complete program of cholesterol and fatty acid synthesis in the liver J Clin Invest 109 2002 1125 1131
    • (2002) J Clin Invest , vol.109 , pp. 1125-1131
    • Horton, J.D.1    Goldstein, J.L.2    Brown, M.S.3
  • 16
    • 0033570119 scopus 로고    scopus 로고
    • Increased levels of nuclear SREBP-1c associated with fatty livers in two mouse models of diabetes mellitus
    • I. Shimomura, Y. Bashmakov, J.D. Horton Increased levels of nuclear SREBP-1c associated with fatty livers in two mouse models of diabetes mellitus J Biol Chem 274 1999 30028 30032
    • (1999) J Biol Chem , vol.274 , pp. 30028-30032
    • Shimomura, I.1    Bashmakov, Y.2    Horton, J.D.3
  • 17
    • 0029797604 scopus 로고    scopus 로고
    • Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a
    • H. Shimano, J.D. Horton, R.E. Hammer, I. Shimomura, M.S. Brown, J.L. Goldstein Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a J Clin Invest 98 1996 1575 1584
    • (1996) J Clin Invest , vol.98 , pp. 1575-1584
    • Shimano, H.1    Horton, J.D.2    Hammer, R.E.3    Shimomura, I.4    Brown, M.S.5    Goldstein, J.L.6
  • 18
    • 0037047284 scopus 로고    scopus 로고
    • Ethanol induces fatty acid synthesis pathways by activation of sterol regulatory element-binding protein (SREBP)
    • M. You, M. Fischer, M.A. Deeg, D.W. Crabb Ethanol induces fatty acid synthesis pathways by activation of sterol regulatory element-binding protein (SREBP) J Biol Chem 277 2002 29342 29347
    • (2002) J Biol Chem , vol.277 , pp. 29342-29347
    • You, M.1    Fischer, M.2    Deeg, M.A.3    Crabb, D.W.4
  • 19
    • 0037960128 scopus 로고    scopus 로고
    • Betaine decreases hyperhomocysteinemia, endoplasmic reticulum stress, and liver injury in alcohol-fed mice
    • C. Ji, N. Kaplowitz Betaine decreases hyperhomocysteinemia, endoplasmic reticulum stress, and liver injury in alcohol-fed mice Gastroenterology 124 2003 1488 1499
    • (2003) Gastroenterology , vol.124 , pp. 1488-1499
    • Ji, C.1    Kaplowitz, N.2
  • 20
    • 0037370152 scopus 로고    scopus 로고
    • Acetaldehyde impairs mitochondrial glutathione transport in HepG2 cells through endoplasmic reticulum stress
    • J.M. Lluis, A. Colell, C. Garcia-Ruiz, N. Kaplowitz, J.C. Fernandez-Checa Acetaldehyde impairs mitochondrial glutathione transport in HepG2 cells through endoplasmic reticulum stress Gastroenterology 124 2003 708 724
    • (2003) Gastroenterology , vol.124 , pp. 708-724
    • Lluis, J.M.1    Colell, A.2    Garcia-Ruiz, C.3    Kaplowitz, N.4    Fernandez-Checa, J.C.5
  • 23
    • 0023280274 scopus 로고
    • A method for increasing the sensitivity of chloramphenicol acetyltransferase assays in extracts of transfected cultured cells
    • D.W. Crabb, J.E. Dixon A method for increasing the sensitivity of chloramphenicol acetyltransferase assays in extracts of transfected cultured cells Anal Biochem 163 1987 88 92
    • (1987) Anal Biochem , vol.163 , pp. 88-92
    • Crabb, D.W.1    Dixon, J.E.2
  • 24
    • 0023266056 scopus 로고
    • Isolated rat hepatocyte couplets in short-term culture: Structural characteristics and plasma membrane reorganization
    • A. Gautam, O.C. Ng, J.L. Boyer Isolated rat hepatocyte couplets in short-term culture structural characteristics and plasma membrane reorganization Hepatology 7 1987 216 223
    • (1987) Hepatology , vol.7 , pp. 216-223
    • Gautam, A.1    Ng, O.C.2    Boyer, J.L.3
  • 25
    • 0024839973 scopus 로고
    • Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay
    • S.P. Davies, D. Carling, D.G. Hardie Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay Eur J Biochem 186 1989 123 128
    • (1989) Eur J Biochem , vol.186 , pp. 123-128
    • Davies, S.P.1    Carling, D.2    Hardie, D.G.3
  • 26
    • 0018356140 scopus 로고
    • Mitochondrial and peroxisomal fatty acid oxidation in liver homogenates and isolated hepatocytes from control and clofibrate-treated rats
    • G.P. Mannaerts, L.J. Debeer, J. Thomas, P.J. De Schepper Mitochondrial and peroxisomal fatty acid oxidation in liver homogenates and isolated hepatocytes from control and clofibrate-treated rats J Biol Chem 254 1979 4585 4595
    • (1979) J Biol Chem , vol.254 , pp. 4585-4595
    • Mannaerts, G.P.1    Debeer, L.J.2    Thomas, J.3    De Schepper, P.J.4
  • 27
    • 0032897276 scopus 로고    scopus 로고
    • High-level expression of rat class I alcohol dehydrogenase is sufficient for ethanol-induced fat accumulation in transduced HeLa cells
    • A. Galli, D. Price, D. Crabb High-level expression of rat class I alcohol dehydrogenase is sufficient for ethanol-induced fat accumulation in transduced HeLa cells Hepatology 29 1999 1164 1170
    • (1999) Hepatology , vol.29 , pp. 1164-1170
    • Galli, A.1    Price, D.2    Crabb, D.3
  • 28
    • 0042847330 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor α (PPARα) agonist treatment reverses PPARalpha dysfunction and abnormalities in hepatic lipid metabolism in ethanol-fed mice
    • M. Fischer, M. You, M. Matsumoto, D.W. Crabb Peroxisome proliferator-activated receptor α (PPARα) agonist treatment reverses PPARalpha dysfunction and abnormalities in hepatic lipid metabolism in ethanol-fed mice J Biol Chem 278 2003 27997 28004
    • (2003) J Biol Chem , vol.278 , pp. 27997-28004
    • Fischer, M.1    You, M.2    Matsumoto, M.3    Crabb, D.W.4
  • 29
    • 0013869851 scopus 로고
    • Role of dietary, adipose, and endogenously synthesized fatty acids in the pathogenesis of the alcoholic fatty liver
    • C.S. Lieber, N. Spritz, L.M. DeCarli Role of dietary, adipose, and endogenously synthesized fatty acids in the pathogenesis of the alcoholic fatty liver J Clin Invest 45 1966 51 62
    • (1966) J Clin Invest , vol.45 , pp. 51-62
    • Lieber, C.S.1    Spritz, N.2    Decarli, L.M.3
  • 30
    • 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
    • S.A. Hawley, M. Davison, A. Woods, S.P. Davies, R.K. Beri, D. Carling, D.G. Hardie 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 1996 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
  • 31
    • 0026782061 scopus 로고
    • Insulin activation of acetyl-CoA carboxylase accompanied by inhibition of the 5′-AMP-activated protein kinase
    • L.A. Witters, B.E. Kemp Insulin activation of acetyl-CoA carboxylase accompanied by inhibition of the 5′-AMP-activated protein kinase J Biol Chem 267 1992 2864 2867
    • (1992) J Biol Chem , vol.267 , pp. 2864-2867
    • Witters, L.A.1    Kemp, B.E.2
  • 32
    • 0024210550 scopus 로고
    • Determination of short-chain coenzyme a compounds by reversed-phase high-performance liquid chromatography
    • M.T. King, P.D. Reiss, N.W. Cornell Determination of short-chain coenzyme A compounds by reversed-phase high-performance liquid chromatography Methods Enzymol 166 1988 70 79
    • (1988) Methods Enzymol , vol.166 , pp. 70-79
    • King, M.T.1    Reiss, P.D.2    Cornell, N.W.3
  • 33
    • 0031007065 scopus 로고    scopus 로고
    • The AMP-activated protein kinase--fuel gauge of the mammalian cell?
    • D.G. Hardie, D. Carling The AMP-activated protein kinase--fuel gauge of the mammalian cell? Eur J Biochem 246 1997 259 273
    • (1997) Eur J Biochem , vol.246 , pp. 259-273
    • Hardie, D.G.1    Carling, D.2
  • 34
    • 0035808410 scopus 로고    scopus 로고
    • The transcriptional and DNA binding activity of peroxisome proliferator-activated receptor alpha is inhibited by ethanol metabolism. a novel mechanism for the development of ethanol-induced fatty liver
    • A. Galli, J. Pinaire, M. Fischer, R. Dorris, D.W. Crabb The transcriptional and DNA binding activity of peroxisome proliferator-activated receptor alpha is inhibited by ethanol metabolism. A novel mechanism for the development of ethanol-induced fatty liver J Biol Chem 5 276 2001 68 75
    • (2001) J Biol Chem , vol.5 , Issue.276 , pp. 68-75
    • Galli, A.1    Pinaire, J.2    Fischer, M.3    Dorris, R.4    Crabb, D.W.5
  • 35
    • 0029616379 scopus 로고
    • Hormonal and chemical influences on the expression of class 2 aldehyde dehydrogenases in rat H4IIEC3 and human HuH7 hepatoma cells
    • D.W. Crabb, M.J. Stewart, Q. Xiao Hormonal and chemical influences on the expression of class 2 aldehyde dehydrogenases in rat H4IIEC3 and human HuH7 hepatoma cells Alcohol Clin Exp Res 19 1995 1414 1419
    • (1995) Alcohol Clin Exp Res , vol.19 , pp. 1414-1419
    • Crabb, D.W.1    Stewart, M.J.2    Xiao, Q.3
  • 36
    • 0032567252 scopus 로고    scopus 로고
    • Functional domains of the α1 catalytic subunit of the AMP-activated protein kinase
    • B.E. Crute, K. Seefeld, J. Gamble, B.E. Kemp, L.A. Witters Functional domains of the α1 catalytic subunit of the AMP-activated protein kinase J Biol Chem 273 1998 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
  • 37
    • 0033815967 scopus 로고    scopus 로고
    • Characterization of the role of AMP-activated protein kinase in the regulation of glucose-activated gene expression using constitutively active and dominant negative forms of the kinase
    • A. Woods, D. Azzout-Marniche, M. Foretz, S.C. Stein, P. Lemarchand, P. Ferre, F. Foufelle, D. Carling Characterization of the role of AMP-activated protein kinase in the regulation of glucose-activated gene expression using constitutively active and dominant negative forms of the kinase Mol Cell Biol 20 2000 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
  • 38
    • 0034141355 scopus 로고    scopus 로고
    • The regulation of AMP-activated protein kinase by phosphorylation
    • S.C. Stein, A. Woods, N.A. Jones, M.D. Davison, D. Carling The regulation of AMP-activated protein kinase by phosphorylation Biochem J 345 2000 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
  • 39
    • 0023774506 scopus 로고
    • Short-term inhibition of carnitine palmitoyltransferase I activity in rat hepatocytes incubated with ethanol
    • M. Guzman, M.J. Geelen Short-term inhibition of carnitine palmitoyltransferase I activity in rat hepatocytes incubated with ethanol Biochem Biophys Res Commun 154 1988 682 687
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 682-687
    • Guzman, M.1    Geelen, M.J.2
  • 40
    • 0023601680 scopus 로고
    • Ethanol feeding to rats reversibly decreases hepatic carnitine palmitoyltransferase activity and increases enzyme sensitivity to malonyl-CoA
    • M. Guzman, J. Castro, A. Maquedano Ethanol feeding to rats reversibly decreases hepatic carnitine palmitoyltransferase activity and increases enzyme sensitivity to malonyl-CoA Biochem Biophys Res Commun 149 1987 443 448
    • (1987) Biochem Biophys Res Commun , vol.149 , pp. 443-448
    • Guzman, M.1    Castro, J.2    Maquedano, A.3
  • 41
    • 0024267601 scopus 로고
    • Effects of ethanol feeding on the activity and regulation of hepatic carnitine palmitoyltransferase I
    • M. Guzman, M.J. Geelen Effects of ethanol feeding on the activity and regulation of hepatic carnitine palmitoyltransferase I Arch Biochem Biophys 267 1988 580 588
    • (1988) Arch Biochem Biophys , vol.267 , pp. 580-588
    • Guzman, M.1    Geelen, M.J.2
  • 42
    • 1642546212 scopus 로고    scopus 로고
    • Over-expression of sterol regulatory element binding protein-1c in rat pancreatic islets induces lipogenesis and decreases glucose-stimulated insulin release: Modulation by 5-aminoimidazole-4-carboxamide ribonucleoside
    • F. Diraison, L. Parton, P. Ferre, F. Foufelle, C.P. Briscoe, I. Leclerc, G.A. Rutter Over-expression of sterol regulatory element binding protein-1c in rat pancreatic islets induces lipogenesis and decreases glucose-stimulated insulin release modulation by 5-aminoimidazole-4-carboxamide ribonucleoside Biochem J 378 2004 769 778
    • (2004) Biochem J , vol.378 , pp. 769-778
    • Diraison, F.1    Parton, L.2    Ferre, P.3    Foufelle, F.4    Briscoe, C.P.5    Leclerc, I.6    Rutter, G.A.7
  • 43
    • 0141905919 scopus 로고    scopus 로고
    • Roles of 5′-AMP-activated protein kinase (AMPK) in mammalian glucose homoeostasis
    • G.A. Rutter, X. Da Silva, G.I. Leclerc Roles of 5′-AMP-activated protein kinase (AMPK) in mammalian glucose homoeostasis Biochem J 75 2003 1 16
    • (2003) Biochem J , vol.75 , pp. 1-16
    • Rutter, G.A.1    Da Silva, X.2    Leclerc, G.I.3
  • 44
    • 0037453007 scopus 로고    scopus 로고
    • Liver-specific mRNA for Insig-2 down-regulated by insulin: Implications for fatty acid synthesis
    • D. Yabe, R. Komuro, G. Liang, J.L. Goldstein, M.S. Brown Liver-specific mRNA for Insig-2 down-regulated by insulin implications for fatty acid synthesis Proc Natl Acad Sci U S A 100 2003 3155 3160
    • (2003) Proc Natl Acad Sci U S a , vol.100 , pp. 3155-3160
    • Yabe, D.1    Komuro, R.2    Liang, G.3    Goldstein, J.L.4    Brown, M.S.5
  • 45
    • 0033599028 scopus 로고    scopus 로고
    • Transport-dependent proteolysis of SREBP: Relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
    • R.A. DeBose-Boyd, M.S. Brown, W.P. Li, A. Nohturfft, J.L. Goldstein, P.J. Espenshade Transport-dependent proteolysis of SREBP relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi Cell 99 1999 703 712
    • (1999) Cell , vol.99 , pp. 703-712
    • Debose-Boyd, R.A.1    Brown, M.S.2    Li, W.P.3    Nohturfft, A.4    Goldstein, J.L.5    Espenshade, P.J.6
  • 47
    • 0027162774 scopus 로고
    • Acetate-induced changes of adenine nucleotide levels in rat liver
    • M.M. Zydowo, R.T. Smolenski, J. Swierczynski Acetate-induced changes of adenine nucleotide levels in rat liver Metabolism 42 1993 644 648
    • (1993) Metabolism , vol.42 , pp. 644-648
    • Zydowo, M.M.1    Smolenski, R.T.2    Swierczynski, J.3
  • 48
    • 0018369512 scopus 로고
    • Effect of acute and chronic ethanol administration on the content of coenzymes linked to energy transfer in the liver of rats fed standard or low-protein diet
    • H. Kono, J.C. Bode, G.A. Martini Effect of acute and chronic ethanol administration on the content of coenzymes linked to energy transfer in the liver of rats fed standard or low-protein diet Gastroenterol Jpn 14 1979 226 232
    • (1979) Gastroenterol Jpn , vol.14 , pp. 226-232
    • Kono, H.1    Bode, J.C.2    Martini, G.A.3
  • 50
    • 0041302377 scopus 로고    scopus 로고
    • The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice
    • A. Xu, Y. Wang, H. Keshaw, L.Y. Xu, K.S. Lam, G.J. Cooper The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice J Clin Invest 112 2003 91 100
    • (2003) J Clin Invest , vol.112 , pp. 91-100
    • Xu, A.1    Wang, Y.2    Keshaw, H.3    Xu, L.Y.4    Lam, K.S.5    Cooper, G.J.6
  • 52
    • 0037329494 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins
    • T. Leff AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins Biochem Soc Trans 31 2003 224 227
    • (2003) Biochem Soc Trans , vol.31 , pp. 224-227
    • Leff, T.1
  • 53
    • 0032529139 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Greater AMP dependence, and preferential nuclear localization, of complexes containing the α2 isoform
    • I. Salt, J.W. Celler, S.A. Hawley, A. Prescott, A. Woods, D. Carling, D.G. Hardie AMP-activated protein kinase greater AMP dependence, and preferential nuclear localization, of complexes containing the α2 isoform Biochem J 334 1998 177 187
    • (1998) Biochem J , vol.334 , pp. 177-187
    • Salt, I.1    Celler, J.W.2    Hawley, S.A.3    Prescott, A.4    Woods, A.5    Carling, D.6    Hardie, D.G.7
  • 54
    • 0032878549 scopus 로고    scopus 로고
    • The regulation of acetyl-CoA carboxylase--a potential target for the action of hypolipidemic agents
    • M.R. Munday, C.J. Hemingway The regulation of acetyl-CoA carboxylase--a potential target for the action of hypolipidemic agents Adv Enzyme Regul 39 1999 205 234
    • (1999) Adv Enzyme Regul , vol.39 , pp. 205-234
    • Munday, M.R.1    Hemingway, C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.