메뉴 건너뛰기




Volumn , Issue , 2009, Pages 195-216

Amp-activated protein kinase in muscle growth, fat deposition, and meat quality

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85013295659     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (4)

References (214)
  • 2
    • 0029041316 scopus 로고
    • Human acetyl-CoA carboxylase — characterization, molecular-cloning, and evidence for 2 isoforms
    • Abuelheiga, L., A. Jayakumar, A. Baldini, S.S. Chirala, and S.J. Wakil. 1995. Human acetyl-CoA carboxylase — characterization, molecular-cloning, and evidence for 2 isoforms. Proc. Natl. Acad. Sci. U.S.A. 92:4011-4015.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 4011-4015
    • Abuelheiga, L.1    Jayakumar, A.2    Baldini, A.3    Chirala, S.S.4    Wakil, S.J.5
  • 4
    • 0033610891 scopus 로고    scopus 로고
    • Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta
    • Anderson, K.A., RL. Means, Q.H. Huang, B.E. Kemp, E.G. Goldstein, M.A. Selbert, A.M. Edelman, R.T. Fremeau, and A.R. Means. 1998. Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta. J. Biol. Chem. 273:31880-31889.
    • (1998) J. Biol. Chem , vol.273 , pp. 31880-31889
    • Anderson, K.A.1    Means, R.L.2    Huang, Q.H.3    Kemp, B.E.4    Goldstein, E.G.5    Selbert, M.A.6    Edelman, A.M.7    Fremeau, R.T.8    Means, A.R.9
  • 5
    • 0037328991 scopus 로고    scopus 로고
    • Identification and characterization of AMPK gamma 3 mutations in the pig
    • Andersson, L. 2003. Identification and characterization of AMPK gamma 3 mutations in the pig. Biochem. Soc. Trans. 31:232-235.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 232-235
    • Andersson, L.1
  • 9
    • 0037407012 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: A paradigm for myocardial energy depletion
    • Ashrafian, H., C. Redwood, E. Blair, and H. Watkins. 2003. Hypertrophic cardiomyopathy: a paradigm for myocardial energy depletion. Trends Genet. 19:263-268.
    • (2003) Trends Genet , vol.19 , pp. 263-268
    • Ashrafian, H.1    Redwood, C.2    Blair, E.3    Watkins, H.4
  • 12
    • 0015864346 scopus 로고
    • Modulation of 3-hydroxy-3-methylglutaryl Coenzyme A reductase-activity with cAMP and with protein fractions of rat-liver cytosol. Biochem. Biophys. Res
    • Beg, Z.H., D.W. Allmann, and D.M. Gibson. 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) Commun , vol.54 , pp. 1362-1369
    • Beg, Z.H.1    Allmann, D.W.2    Gibson, D.M.3
  • 16
    • 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., S.G. Finn, and C.G. Proud. 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
  • 17
    • 0036438894 scopus 로고    scopus 로고
    • Regulation of peptide-chain elongation in mammalian cells
    • Browne, G.J. and C.G. Proud. 2002. Regulation of peptide-chain elongation in mammalian cells. Eur. J. Biochem. 269:5360-5368.
    • (2002) Eur. J. Biochem , vol.269 , pp. 5360-5368
    • Browne, G.J.1    Proud, C.G.2
  • 18
    • 1642355123 scopus 로고    scopus 로고
    • A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin. Mol. Cell
    • Browne, G.J. and C.G. Proud. 2004. A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin. Mol. Cell. Biol. 24:2986-2997.
    • (2004) Biol , vol.24 , pp. 2986-2997
    • Browne, G.J.1    Proud, C.G.2
  • 20
    • 33646252347 scopus 로고    scopus 로고
    • Comparison of prenatal muscle tissue expression profiles of two pig breeds differing in muscle characteristics
    • Cagnazzo, M., M.F. te Pas, J. Priem, A.A. de Wit, M.H. Pool, R. Davoli, and V. Russo. 2006. Comparison of prenatal muscle tissue expression profiles of two pig breeds differing in muscle characteristics. J. Anim. Sci. 84:1-10.
    • (2006) J. Anim. Sci , vol.84 , pp. 1-10
    • Cagnazzo, M.1    Te Pas, M.F.2    Priem, J.3    De Wit, A.A.4    Pool, M.H.5    Davoli, R.6    Russo, V.7
  • 21
    • 0025003542 scopus 로고
    • Functional properties of phosphorylated elongation factor-II
    • Carlberg, U., A. Nilsson, and O. Nygard. 1990. Functional properties of phosphorylated elongation factor-II. Eur. J. Biochem. 191:639-645.
    • (1990) Eur. J. Biochem , vol.191 , pp. 639-645
    • Carlberg, U.1    Nilsson, A.2    Nygard, O.3
  • 22
    • 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
  • 23
    • 0024786438 scopus 로고
    • Purification and characterization of the AMPactivated protein kinase — copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl-CoA reductase kinase activities
    • Carling, D., P.R. Clarke, V.A. Zammit, and D.G. Hardie. 1989. Purification and characterization of the AMPactivated protein kinase — 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
  • 24
    • 0023642627 scopus 로고
    • A common bicyclic protein-kinase cascade inactivates the regulatory enzymes of fatty-acid and cholesterol-biosynthesis
    • Carling, D., V.A. Zammit, and D.G. Hardie. 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
  • 25
    • 0015918822 scopus 로고
    • Regulation of hepatic acetyl coenzyme-A carboxylase by phosphorylation and dephosphorylation
    • Carlson, C.A. and K. Kim. 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.2
  • 26
    • 33748809566 scopus 로고    scopus 로고
    • Growth performance, carcass composition, quality, and enhancement treatment of fresh pork identified through deoxyribonucleic acid markerassisted selection for the Rendement Napole gene
    • Carr, C.C., J.B. Morgan, E.P. Berg, S.D. Carter, and F.K. Ray. 2006. Growth performance, carcass composition, quality, and enhancement treatment of fresh pork identified through deoxyribonucleic acid markerassisted selection for the Rendement Napole gene. J. Anim. Sci. 84:910-917.
    • (2006) J. Anim. Sci , vol.84 , pp. 910-917
    • Carr, C.C.1    Morgan, J.B.2    Berg, E.P.3    Carter, S.D.4    Ray, F.K.5
  • 27
    • 0023279818 scopus 로고
    • Characterization of mitochondrial-uncoupling protein in bovine fetus and newborn calf
    • Casteilla, L., C. Forest, J. Robelin, D. Ricquier, A. Lombet, and G. Ailhaud. 1987. Characterization of mitochondrial-uncoupling protein in bovine fetus and newborn calf. Am. J. Physiol. 252:E627-636.
    • (1987) Am. J. Physiol , vol.252 , pp. E627-E636
    • Casteilla, L.1    Forest, C.2    Robelin, J.3    Ricquier, D.4    Lombet, A.5    Ailhaud, G.6
  • 28
    • 1942469564 scopus 로고    scopus 로고
    • Thr2446 is a novel mammalian target of rapamycin (MTOR) phosphorylation site regulated by nutrient status
    • Cheng, S.W., L.G. Fryer, D. Carling, and P.R. Shepherd. 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
  • 29
    • 33750519660 scopus 로고    scopus 로고
    • Berberine-stimulated glucose uptake in L6 myotubes involves both AMPK and p38 MAPK
    • Cheng, Z., T. Pang, M. Gu, A.H. Gao, C.M. Xie, J.Y. Li, F.J. Nan, and J. Li. 2006. Berberine-stimulated glucose uptake in L6 myotubes involves both AMPK and p38 MAPK. Biochim. Biophys. Acta 1760:1682-1689.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1682-1689
    • Cheng, Z.1    Pang, T.2    Gu, M.3    Gao, A.H.4    Xie, C.M.5    Li, J.Y.6    Nan, F.J.7    Li, J.8
  • 30
    • 0034654362 scopus 로고    scopus 로고
    • Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding
    • Cheung, P.C.F., I.P. Salt, S.P. Davies, D.G. Hardie, and D. Carling. 2000. Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding. Biochem. J. 346:659-669.
    • (2000) Biochem. J , vol.346 , pp. 659-669
    • Cheung, P.C.F.1    Salt, I.P.2    Davies, S.P.3    Hardie, D.G.4    Carling, D.5
  • 31
    • 21844468767 scopus 로고    scopus 로고
    • Phosphorylation of mammalian target of rapamycin (MTOR) at Ser-2448 is mediated by p70S6 kinase
    • Chiang, G.G. and R.T. Abraham. 2005. Phosphorylation of mammalian target of rapamycin (mTOR) at Ser-2448 is mediated by p70S6 kinase. J. Biol. Chem. 280:25485-25490.
    • (2005) J. Biol. Chem , vol.280 , pp. 25485-25490
    • Chiang, G.G.1    Abraham, R.T.2
  • 32
    • 3042818799 scopus 로고    scopus 로고
    • Regulation of the TSC pathway by LKB1: Evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome
    • Corradetti, M.N., K. Inoki, N. Bardeesy, R.A. DePinho, and K.L. Guan. 2004. Regulation of the TSC pathway by LKB1: evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome. Genes Dev. 18:1533-1538.
    • (2004) Genes Dev , vol.18 , pp. 1533-1538
    • Corradetti, M.N.1    Inoki, K.2    Bardeesy, N.3    Depinho, R.A.4    Guan, K.L.5
  • 33
    • 85047689953 scopus 로고
    • 5-Aminoimidazole-4-carboxamide ribonucleoside — a specific method for activating AMP-activated protein-kinase in intact-cells
    • Corton, J.M., J.G. Gillespie, S.A. Hawley, and D.G. Hardie. 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
  • 34
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross, D.A., D.R. Alessi, P. Cohen, M. Andjelkovich, and B.A. Hemmings. 1995. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378:785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 35
    • 0032567252 scopus 로고    scopus 로고
    • Functional domains of the alpha1 catalytic subunit of the AMP-activated protein kinase
    • Crute, B.E., K. Seefeld, J. Gamble, B.E. Kemp, and L.A. Witters. 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
  • 36
    • 29244434833 scopus 로고    scopus 로고
    • AMPK activation regulates apoptosis, adipogenesis, and lipolysis by eIF2 alpha in adipocytes
    • Dagon, Y., Y. Avraham, and E.M. Berry. 2006. AMPK activation regulates apoptosis, adipogenesis, and lipolysis by eIF2 alpha in adipocytes. Biochem. Biophys. Res. Commun. 340:43-47.
    • (2006) Biochem. Biophys. Res. Commun , vol.340 , pp. 43-47
    • Dagon, Y.1    Avraham, Y.2    Berry, E.M.3
  • 37
    • 0037185021 scopus 로고    scopus 로고
    • Functional analysis of mutations in the gamma 2 subunit of AMP-activated protein kinase associated with cardiac hypertrophy and Wolff-Parkinson-White syndrome
    • Daniel, T. and D. Carling. 2002. Functional analysis of mutations in the gamma 2 subunit of AMP-activated protein kinase associated with cardiac hypertrophy and Wolff-Parkinson-White syndrome. J. Biol. Chem. 277:51017-51024.
    • (2002) J. Biol. Chem , vol.277 , pp. 51017-51024
    • Daniel, T.1    Carling, D.2
  • 39
    • 0029561919 scopus 로고
    • 5′-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., N.R. Helps, P.T. Cohen, and D.G. Hardie. 1995. 5′-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
  • 40
    • 0025192341 scopus 로고
    • Location and function of 3 sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein-kinase
    • Davies, S.P., A.T.R. Sim, and D.G. Hardie. 1990. Location and function of 3 sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein-kinase. Eur. J. Biochem. 187:183-190.
    • (1990) Eur. J. Biochem , vol.187 , pp. 183-190
    • Davies, S.P.1    Sim, A.T.R.2    Hardie, D.G.3
  • 41
    • 17144427672 scopus 로고    scopus 로고
    • Role of alpha-adrenoceptor signaling and AMP-activated protein kinase in glycolysis of postmortem skeletal muscle
    • Du, M., Q.W. Shen, and M.J. Zhu. 2005. Role of alpha-adrenoceptor signaling and AMP-activated protein kinase in glycolysis of postmortem skeletal muscle. J. Agric. Food Chem. 53:3235-3239.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 3235-3239
    • Du, M.1    Shen, Q.W.2    Zhu, M.J.3
  • 42
    • 0000260620 scopus 로고    scopus 로고
    • Comparison of non-carriers and heterozygous carriers of the RN(−) allele for carcass composition, muscle distribution and technological meat quality in Hampshire-sired pigs
    • Enfalt, A.C., K. Lundstrom, I. Hansson, S. Johansen, and P.E. Nystrom. 1997c. Comparison of non-carriers and heterozygous carriers of the RN(−) allele for carcass composition, muscle distribution and technological meat quality in Hampshire-sired pigs. Livestock Production Sci. 47:221-229.
    • (1997) Livestock Production Sci , vol.47 , pp. 221-229
    • Enfalt, A.C.1    Lundstrom, K.2    Hansson, I.3    Johansen, S.4    Nystrom, P.E.5
  • 43
    • 0027456330 scopus 로고
    • Glycogen hyperaccumulation in white muscle-fibers of RN− carrier pigs — a biochemical and ultrastructural study
    • Estrade, M., X. Vignon, E. Rock, and G. Monin. 1993. Glycogen hyperaccumulation in white muscle-fibers of RN− carrier pigs — a biochemical and ultrastructural study. Compar. Biochem. and Physiol. B -Biochem. Mol. Biol. 104:321-326.
    • (1993) Compar. Biochem. and Physiol. B -Biochem. Mol. Biol , vol.104 , pp. 321-326
    • Estrade, M.1    Vignon, X.2    Rock, E.3    Monin, G.4
  • 44
  • 45
    • 0022371303 scopus 로고
    • Activation of rat-liver cytosolic 3-hydroxy-3-methylglutaryl Coenzyme A reductase kinase by adenosine 5′-monophosphate
    • Ferrer, A., C. Caelles, N. Massot, and F.G. Hegardt. 1985. Activation of rat-liver cytosolic 3-hydroxy-3-methylglutaryl Coenzyme A reductase kinase by adenosine 5′-monophosphate. Biochem. Biophysical. Res. Commun. 132:497-504.
    • (1985) Biochem. Biophysical. Res. Commun , vol.132 , pp. 497-504
    • Ferrer, A.1    Caelles, C.2    Massot, N.3    Hegardt, F.G.4
  • 46
    • 29244445804 scopus 로고    scopus 로고
    • Adipogenesis: Cellular and molecular aspects
    • Feve, B. 2005. Adipogenesis: cellular and molecular aspects. Best Pract. Res. Clin. Endocrinol. Metab. 19:483-499.
    • (2005) Best Pract. Res. Clin. Endocrinol. Metab , vol.19 , pp. 483-499
    • Feve, B.1
  • 47
    • 0032511053 scopus 로고    scopus 로고
    • AMP-activated protein kinase inhibits the glucose-activated expression of fatty acid synthase gene in rat hepatocytes
    • Foretz, M., D. Carling, C. Guichard, P. Ferre, and F. Foufelle. 1998. AMP-activated protein kinase inhibits the glucose-activated expression of fatty acid synthase gene in rat hepatocytes. J. Biol. Chem. 273:14767-14771.
    • (1998) J. Biol. Chem , vol.273 , pp. 14767-14771
    • Foretz, M.1    Carling, D.2    Guichard, C.3    Ferre, P.4    Foufelle, F.5
  • 48
    • 0032831661 scopus 로고    scopus 로고
    • Alteration of glycogen and glucose metabolism in ischaemic and post-ischaemic working rat hearts by adenosine A(1) receptor stimulation
    • Fraser, H., G.D. Lopaschuk, and A.S. Clanachan. 1999. Alteration of glycogen and glucose metabolism in ischaemic and post-ischaemic working rat hearts by adenosine A(1) receptor stimulation. Br. J. Pharmacol. 128:197-205.
    • (1999) Br. J. Pharmacol , vol.128 , pp. 197-205
    • Fraser, H.1    Lopaschuk, G.D.2    Clanachan, A.S.3
  • 49
    • 0037067666 scopus 로고    scopus 로고
    • The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways
    • Fryer, L.G., A. Parbu-Patel, and D. Carling. 2002a. 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
  • 50
    • 0036535031 scopus 로고    scopus 로고
    • Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells
    • Fryer, L.G.D., F. Foufelle, K. Barnes, S.A. Baldwin, A. Woods, and D. Carling. 2002b. Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells. Biochem. J. 363:167-174.
    • (2002) Biochem. J , vol.363 , pp. 167-174
    • Fryer, L.G.D.1    Foufelle, F.2    Barnes, K.3    Baldwin, S.A.4    Woods, A.5    Carling, D.6
  • 51
    • 33748612432 scopus 로고    scopus 로고
    • AICAR inhibits adipocyte differentiation in 3T3L1 and restores metabolic alterations in diet-induced obesity mice model
    • Giri, S., R. Rattan, E. Haq, M. Khan, R. Yasmin, J.S. Won, L. Key, A.K. Singh, and I. Singh. 2006a. AICAR inhibits adipocyte differentiation in 3T3L1 and restores metabolic alterations in diet-induced obesity mice model. Nutr. Metab. 3:31-51.
    • (2006) Nutr. Metab , vol.3 , pp. 31-51
    • Giri, S.1    Rattan, R.2    Haq, E.3    Khan, M.4    Yasmin, R.5    Won, J.S.6    Key, L.7    Singh, A.K.8    Singh, I.9
  • 52
    • 23944456384 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy and atrophy signaling pathways
    • Glass, D.J. 2005. Skeletal muscle hypertrophy and atrophy signaling pathways. Int. J. Biochem. Cell Biol. 37:1974-1984.
    • (2005) Int. J. Biochem. Cell Biol , vol.37 , pp. 1974-1984
    • Glass, D.J.1
  • 53
    • 27144511493 scopus 로고    scopus 로고
    • Ontogeny and nutritional programming of adiposity in sheep: Potential role of glucocorticoid action and uncoupling protein-2
    • Gnanalingham, M.G., A. Mostyn, M.E. Symonds, and T. Stephenson. 2005. Ontogeny and nutritional programming of adiposity in sheep: potential role of glucocorticoid action and uncoupling protein-2. Am. J. Physiol. Regul. Integr. Comp. Physiol. 289:R1407-1415.
    • (2005) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.289 , pp. R1407-R1415
    • Gnanalingham, M.G.1    Mostyn, A.2    Symonds, M.E.3    Stephenson, T.4
  • 55
    • 0029745782 scopus 로고    scopus 로고
    • Effects of exercise and insulin on mitogen-activated protein kinase signaling pathways in rat skeletal muscle
    • Goodyear, L.J., P.Y. Chang, D.J. Sherwood, S.D. Dufresne, and D.E. Moller. 1996. Effects of exercise and insulin on mitogen-activated protein kinase signaling pathways in rat skeletal muscle. Am. J. Physiol.271:E403-E408.
    • (1996) Am. J. Physiol , vol.271 , pp. E403-E408
    • Goodyear, L.J.1    Chang, P.Y.2    Sherwood, D.J.3    Dufresne, S.D.4    Moller, D.E.5
  • 57
    • 0034805751 scopus 로고    scopus 로고
    • The effects of AICAR on adipocyte differentiation of 3T3-L1 cells
    • Habinowski, S.A. and L.A. Witters. 2001a. The effects of AICAR on adipocyte differentiation of 3T3-L1 cells. Biochem. Biophys. Res. Commun. 286:852-856.
    • (2001) Biochem. Biophys. Res. Commun , vol.286 , pp. 852-856
    • Habinowski, S.A.1    Witters, L.A.2
  • 58
    • 0347363479 scopus 로고    scopus 로고
    • Inhibition of MAP/ERK kinase prevents IGF-I-induced hypertrophy in rat muscles
    • Haddad, F. and G.R. Adams. 2004. Inhibition of MAP/ERK kinase prevents IGF-I-induced hypertrophy in rat muscles. J. Appl. Physiol. 96:203-210.
    • (2004) J. Appl. Physiol , vol.96 , pp. 203-210
    • Haddad, F.1    Adams, G.R.2
  • 59
    • 2942518272 scopus 로고    scopus 로고
    • Differential regulation of the phosphoinositide 3-kinase and MAP kinase pathways by hepatocyte growth factor vs. Insulin-like growth factor-I in myogenic cells
    • Halevy, O. and L.C. Cantley. 2004. Differential regulation of the phosphoinositide 3-kinase and MAP kinase pathways by hepatocyte growth factor vs. insulin-like growth factor-I in myogenic cells. Exp. Cell Res. 297:224-234.
    • (2004) Exp. Cell Res , vol.297 , pp. 224-234
    • Halevy, O.1    Cantley, L.C.2
  • 60
    • 2342503862 scopus 로고    scopus 로고
    • Relationships between longissimus glycolytic potential and swine growth performance, carcass traits, and pork quality
    • Hamilton, D.N., K.D. Miller, M. Ellis, F.K. McKeith, and E.R. Wilson. 2003. Relationships between longissimus glycolytic potential and swine growth performance, carcass traits, and pork quality. J. Anim. Sci. 81:2206-2212.
    • (2003) J. Anim. Sci , vol.81 , pp. 2206-2212
    • Hamilton, D.N.1    Miller, K.D.2    Ellis, M.3    McKeith, F.K.4    Wilson, E.R.5
  • 61
    • 34047107157 scopus 로고    scopus 로고
    • Biochemistry. Balancing cellular energy
    • Hardie, D.G. 2007. Biochemistry. Balancing cellular energy. Science 315:1671-1672.
    • (2007) Science , vol.315 , pp. 1671-1672
    • Hardie, D.G.1
  • 62
    • 0031007065 scopus 로고    scopus 로고
    • The AMP-activated protein kinase — fuel gauge of the mammalian cell
    • Hardie, D.G., and D. Carling. 1997. The AMP-activated protein kinase — fuel gauge of the mammalian cell? Eur. J. BioChem. 246:259-273.
    • (1997) Eur. J. Biochem , vol.246 , pp. 259-273
    • Hardie, D.G.1    Carling, D.2
  • 63
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • Hardie, D.G., D. Carling, and M. Carlson. 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
  • 64
    • 0024546378 scopus 로고
    • The AMP-activated protein-kinase — a multisubstrate regulator of lipid metabolism
    • Hardie, D.G., D. Carling, and A.T.R. Sim. 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
  • 65
    • 0035542970 scopus 로고    scopus 로고
    • AMP-activated protein kinase: The energy charge hypothesis revisited
    • Hardie, D.G. and S.A. Hawley. 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
  • 66
    • 33745225026 scopus 로고    scopus 로고
    • AMP-activated protein kinase — development of the energy sensor concept
    • Hardie, D.G., S.A. Hawley, and J. Scott. 2006. AMP-activated protein kinase — development of the energy sensor concept. J. Physiol. -London 574:7-15.
    • (2006) J. Physiol. -London , vol.574 , pp. 7-15
    • Hardie, D.G.1    Hawley, S.A.2    Scott, J.3
  • 67
    • 0033560109 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An ultrasensitive system for monitoring cellular energy charge
    • Hardie, D.G., I.P. Salt, S.A. Hawley, and S.P. Davies. 1999. AMP-activated protein kinase: an ultrasensitive system for monitoring cellular energy charge. Biochem. J. 338: 717-722.
    • (1999) Biochem. J , vol.338 , pp. 717-722
    • Hardie, D.G.1    Salt, I.P.2    Hawley, S.A.3    Davies, S.P.4
  • 68
    • 0038199737 scopus 로고    scopus 로고
    • Management of cellular energy by the AMPactivated protein kinase system
    • Hardie, D.G., J.W. Scott, D.A. Pan, and E.R. Hudson. 2003. Management of cellular energy by the AMPactivated 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
  • 69
    • 0037205315 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta: A novel regulator of cardiac hypertrophy and development
    • Hardt, S.E. and J. Sadoshima. 2002. Glycogen synthase kinase-3beta: a novel regulator of cardiac hypertrophy and development. Circulation Res. 90:1055-1063.
    • (2002) Circulation Res , vol.90 , pp. 1055-1063
    • Hardt, S.E.1    Sadoshima, J.2
  • 70
    • 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., J. Boudeau, J.L. Reid, K.J. Mustard, L. Udd, T.P. Makela, D.R. Alessi, and D.G. Hardie. 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
  • 71
    • 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., M. Davison, A. Woods, S.P. Davies, R.K. Beri, D. Carling, and D.G. Hardie. 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
  • 72
    • 0036324142 scopus 로고    scopus 로고
    • The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism
    • Hawley, S.A., A.E. Gadalla, G.S. Olsen, and D.G. Hardie. 2002. The antidiabetic 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
  • 73
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase
    • Hawley, S.A., D.A. Pan, K.J. Mustard, L. Ross, J. Bain, A.M. Edelman, B.G. Frenguelli, and D.G. Hardie. 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
  • 74
    • 0028845251 scopus 로고
    • 5′-AMP activates the AMP-activated protein kinase cascade and Ca2+/calmodulin activates the calmodulin-dependent protein kinase-I cascade, via 3 independent mechanisms
    • Hawley, S.A., M.A. Selbert, E.G. Goldstein, A.M. Edelman, D. Carling, and D.G. Hardie. 1995. 5′-AMP activates the AMP-activated protein kinase cascade and Ca2+/calmodulin activates the calmodulin-dependent protein kinase-I cascade, via 3 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
  • 75
    • 0034070567 scopus 로고    scopus 로고
    • Metabolic stress and altered glucose transport — activation of AMP-activated protein kinase as a unifying coupling mechanism
    • Hayashi, T., M.F. Hirshman, N. Fujii, S.A. Habinowski, L.A. Witters, and L.J. Goodyear. 2000. Metabolic stress and altered glucose transport — activation of AMP-activated protein kinase as a unifying coupling mechanism. Diabetes 49:527-531.
    • (2000) Diabetes , vol.49 , pp. 527-531
    • Hayashi, T.1    Hirshman, M.F.2    Fujii, N.3    Habinowski, S.A.4    Witters, L.A.5    Goodyear, L.J.6
  • 76
    • 0031849916 scopus 로고    scopus 로고
    • Evidence for 5′AMPactivated protein kinase mediation of the effect of muscle contraction on glucose transport
    • Hayashi, T., M.F. Hirshman, E.J. Kurth, W.W. Winder, and L.J. Goodyear. 1998. Evidence for 5′AMPactivated protein kinase mediation of the effect of muscle contraction on glucose transport. Diabetes 47:1369-1373.
    • (1998) Diabetes , vol.47 , pp. 1369-1373
    • Hayashi, T.1    Hirshman, M.F.2    Kurth, E.J.3    Winder, W.W.4    Goodyear, L.J.5
  • 77
    • 0029005507 scopus 로고
    • Inhibition of fatty-acid and cholesterolsynthesis by stimulation of AMP-activated protein-kinase
    • Henin, N., M.F. Vincent, H.E. Gruber, and G. Vandenberghe. 1995. Inhibition of fatty-acid and cholesterolsynthesis by stimulation of AMP-activated protein-kinase. FASEB J. 9:541-546.
    • (1995) FASEB J , vol.9 , pp. 541-546
    • Henin, N.1    Vincent, M.F.2    Gruber, H.E.3    Vandenberghe, G.4
  • 78
    • 0032704115 scopus 로고    scopus 로고
    • Chronic activation of 5′-AMP-activated protein kinase increases GLUT-4, hexokinase, and glycogen in muscle
    • Holmes, B.F., E.J. Kurth-Kraczek, and W.W. Winder. 1999. Chronic activation of 5′-AMP-activated protein kinase increases GLUT-4, hexokinase, and glycogen in muscle. J. Appl. Physiol. 87:1990-1995.
    • (1999) J. Appl. Physiol , vol.87 , pp. 1990-1995
    • Holmes, B.F.1    Kurth-Kraczek, E.J.2    Winder, W.W.3
  • 79
    • 23844471263 scopus 로고    scopus 로고
    • The Ca2+/ calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases
    • Hurley, R.L., K.A. Anderson, J.M. Franzone, B.E. Kemp, A.R. Means, and L.A. Witters. 2005. The Ca2+/ 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
  • 80
    • 27744455616 scopus 로고    scopus 로고
    • Genistein, EGCG, and capsaicin inhibit adipocyte differentiation process via activating AMP-activated protein kinase
    • Hwang, J.T., I.J. Park, J.I. Shin, Y.K. Lee, S.K. Lee, H.W. Baik, J. Ha, and O.J. Park. 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
  • 81
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K., T. Zhu, and K.L. Guan. 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
  • 82
    • 0025279174 scopus 로고
    • Immunological analysis of acetyl-CoA carboxylase mass, tissue distribution and subunit composition
    • Iverson, A.J., A. Bianchi, A.C. Nordlund, and L.A. Witters. 1990. Immunological analysis of acetyl-CoA carboxylase mass, tissue distribution and subunit composition. Biochem. J. 269:365-371.
    • (1990) Biochem. J , vol.269 , pp. 365-371
    • Iverson, A.J.1    Bianchi, A.2    Nordlund, A.C.3    Witters, L.A.4
  • 83
    • 0035861644 scopus 로고    scopus 로고
    • 5′-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in mouse C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside
    • Jakobsen, S.N., D.G. Hardie, N. Morrice, and H.E. Tornqvist. 2001. 5′-AMP-activated 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
  • 86
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L.N., M.E. Noble, and D.J. Owen. 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.2    Owen, D.J.3
  • 88
    • 14244256097 scopus 로고    scopus 로고
    • Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: Possible involvement in obesity-linked insulin resistance
    • Khamzina, L., A. Veilleux, S. Bergeron, and A. Marette. 2005. Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: possible involvement in obesity-linked insulin resistance. Endocrinology 146:1473-1481.
    • (2005) Endocrinology , vol.146 , pp. 1473-1481
    • Khamzina, L.1    Veilleux, A.2    Bergeron, S.3    Marette, A.4
  • 90
    • 0032581393 scopus 로고    scopus 로고
    • Evidence that acetyl-CoA carboxylase isoforms play different biological roles in H9c2 cardiomyocyte
    • Kim, J.M., M. Yoon, I. Kang, S.S. Kim, and J. Ha. 1998. Evidence that acetyl-CoA carboxylase isoforms play different biological roles in H9c2 cardiomyocyte. Biochem. Biophys. Res. Commun. 248:490-496.
    • (1998) Biochem. Biophys. Res. Commun , vol.248 , pp. 490-496
    • Kim, J.M.1    Yoon, M.2    Kang, I.3    Kim, S.S.4    Ha, J.5
  • 91
    • 21344442127 scopus 로고    scopus 로고
    • Hypoxia inhibits adipocyte differentiation in a HDAC-independent manner
    • Kim, K.H., M.J. Song, J. Chung, H. Park, and J.B. Kim. 2005. Hypoxia inhibits adipocyte differentiation in a HDAC-independent manner. Biochem. Biophys. Res. Commun. 333:1178-1184.
    • (2005) Biochem. Biophys. Res. Commun , vol.333 , pp. 1178-1184
    • Kim, K.H.1    Song, M.J.2    Chung, J.3    Park, H.4    Kim, J.B.5
  • 94
    • 34249703500 scopus 로고    scopus 로고
    • AMP-activated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells
    • Krawiec, B.J., G.J. Nystrom, R.A. Frost, L.S. Jefferson, and C.H. Lang. 2007. AMP-activated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells. Am. J. Physiol. Endocrinol. Metab. 292:E1555-E1567.
    • (2007) Am. J. Physiol. Endocrinol. Metab , vol.292 , pp. E1555-E1567
    • Krawiec, B.J.1    Nystrom, G.J.2    Frost, R.A.3    Jefferson, L.S.4    Lang, C.H.5
  • 95
    • 0032765396 scopus 로고    scopus 로고
    • 5′ AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle
    • Kurth-Kraczek, E.J., M.F. Hirshman, L.J. Goodyear, and W.W. Winder. 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
  • 96
    • 1942530258 scopus 로고    scopus 로고
    • Genetic variability of muscle glycolytic potential in pigs
    • Larzul, C., P. Le Roy, G. Monin, and P. Sellier. 1998. Genetic variability of muscle glycolytic potential in pigs. Productions Animales 11:183-197.
    • (1998) Productions Animales , vol.11 , pp. 183-197
    • Larzul, C.1    Le Roy, P.2    Monin, G.3    Sellier, P.4
  • 97
    • 13244298415 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway
    • Latres, E., A.R. Amini, A.A. Amini, J. Griffiths, F.J. Martin, Y. Wei, H. C. Lin, G.D. Yancopoulos, and D.J. Glass. 2005. Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J. Biol. Chem. 280:2737-2744.
    • (2005) J. Biol. Chem , vol.280 , pp. 2737-2744
    • Latres, E.1    Amini, A.R.2    Amini, A.A.3    Griffiths, J.4    Martin, F.J.5    Wei, Y.6    Lin, H.C.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 98
    • 0034060763 scopus 로고    scopus 로고
    • Comparison between the three porcine RN genotypes for growth, carcass composition and meat quality traits
    • Le Roy, P., J.M. Elsen, J.C. Caritez, A. Talmant, H. Juin, P. Sellier, and G. Monin. 2000. Comparison between the three porcine RN genotypes for growth, carcass composition and meat quality traits. Genet. Select. Evolut. 32:165-186.
    • (2000) Genet. Select. Evolut , vol.32 , pp. 165-186
    • Le Roy, P.1    Elsen, J.M.2    Caritez, J.C.3    Talmant, A.4    Juin, H.5    Sellier, P.6    Monin, G.7
  • 99
    • 0039255434 scopus 로고    scopus 로고
    • Pig meat quality. Influence of rearing factors on skeletal muscle traits
    • Lebret, B., L. Fefaucheur, and J. Mourot. 1999a. Pig meat quality. Influence of rearing factors on skeletal muscle traits. Productions Animales 12:11-28.
    • (1999) Productions Animales , vol.12 , pp. 11-28
    • Lebret, B.1    Fefaucheur, L.2    Mourot, J.3
  • 100
    • 0033146508 scopus 로고    scopus 로고
    • Influence of the three RN genotypes on chemical composition, enzyme activities, and myofiber characteristics of porcine skeletal muscle
    • Lebret, B., P. Le Roy, G. Monin, L. Lefaucheur, J.C. Caritez, A. Talmant, J.M. Elsen, and P. Sellier. 1999b. Influence of the three RN genotypes on chemical composition, enzyme activities, and myofiber characteristics of porcine skeletal muscle. J. Anim. Sci. 77:1482-1489.
    • (1999) J. Anim. Sci , vol.77 , pp. 1482-1489
    • Lebret, B.1    Le Roy, P.2    Monin, G.3    Lefaucheur, L.4    Caritez, J.C.5    Talmant, A.6    Elsen, J.M.7    Sellier, P.8
  • 101
    • 0032541083 scopus 로고    scopus 로고
    • The 5′-AMP-activated protein kinase inhibits the transcriptional stimulation by glucose in liver cells, acting through the glucose response complex
    • Leclerc, I., A. Kahn, and B. Doiron. 1998. The 5′-AMP-activated protein kinase inhibits the transcriptional stimulation by glucose in liver cells, acting through the glucose response complex. FEBS Lett. 431:180-184.
    • (1998) FEBS Lett , vol.431 , pp. 180-184
    • Leclerc, I.1    Kahn, A.2    Doiron, B.3
  • 107
    • 0034074153 scopus 로고    scopus 로고
    • 5-Aminoimidazole-4-carboxamide riboside mimics the effects of insulin on the expression of the 2 key gluconeogenic genes PEPCK and glucose-6-phosphatase
    • Lochhead, P.A., I.P. Salt, K.S. Walker, D.G. Hardie, and C. Sutherland. 2000. 5-Aminoimidazole-4-carboxamide riboside mimics the effects of insulin on the expression of the 2 key gluconeogenic genes PEPCK and glucose-6-phosphatase. Diabetes 49:896-903.
    • (2000) Diabetes , vol.49 , pp. 896-903
    • Lochhead, P.A.1    Salt, I.P.2    Walker, K.S.3    Hardie, D.G.4    Sutherland, C.5
  • 108
    • 33845872600 scopus 로고    scopus 로고
    • Ontogenic loss of brown adipose tissue sensitivity to beta-adrenergic stimulation in the ovine
    • Lomax, M.A., F. Sadiq, G. Karamanlidis, A. Karamitri, P. Trayhurn, and D.G. Hazlerigg. 2007. Ontogenic loss of brown adipose tissue sensitivity to beta-adrenergic stimulation in the ovine. Endocrinology 148:461-468.
    • (2007) Endocrinology , vol.148 , pp. 461-468
    • Lomax, M.A.1    Sadiq, F.2    Karamanlidis, G.3    Karamitri, A.4    Trayhurn, P.5    Hazlerigg, D.G.6
  • 112
    • 0031043030 scopus 로고    scopus 로고
    • The mitochondrial carnitine palmitoyltransferase system — from concept to molecular analysis
    • McGarry, J.D. and N.F. Brown. 1997. The mitochondrial carnitine palmitoyltransferase system — from concept to molecular analysis. Eur. J. Biochem. 244:1-14.
    • (1997) Eur. J. Biochem , vol.244 , pp. 1-14
    • McGarry, J.D.1    Brown, N.F.2
  • 113
    • 1642398604 scopus 로고    scopus 로고
    • Continuous myofiber remodeling in uninjured extraocular myofibers: Myonuclear turnover and evidence for apoptosis
    • McLoon, L.K., J. Rowe, J. Wirtschafter, and K.M. McCormick. 2004. Continuous myofiber remodeling in uninjured extraocular myofibers: myonuclear turnover and evidence for apoptosis. Muscle Nerve 29:707-715.
    • (2004) Muscle Nerve , vol.29 , pp. 707-715
    • McLoon, L.K.1    Rowe, J.2    Wirtschafter, J.3    McCormick, K.M.4
  • 114
    • 0036712741 scopus 로고    scopus 로고
    • TSC1-TSC2: A complex tale of PKB-mediated S6K regulation
    • McManus, E.J. and D.R. Alessi. 2002. TSC1-TSC2: a complex tale of PKB-mediated S6K regulation. Nat. Cell Biol. 4:E214-216.
    • (2002) Nat. Cell Biol , vol.4 , pp. E214-E216
    • McManus, E.J.1    Alessi, D.R.2
  • 115
    • 0037093526 scopus 로고    scopus 로고
    • Only the large soluble form of preadipocyte factor-1 (Pref-1), but not the small soluble and membrane forms, inhibits adipocyte differentiation: Role of alternative splicing
    • Mei, B., L. Zhao, L. Chen, and H.S. Sul. 2002. Only the large soluble form of preadipocyte factor-1 (Pref-1), but not the small soluble and membrane forms, inhibits adipocyte differentiation: role of alternative splicing. Biochem. J. 364:137-144.
    • (2002) Biochem. J , vol.364 , pp. 137-144
    • Mei, B.1    Zhao, L.2    Chen, L.3    Sul, H.S.4
  • 116
    • 3843136144 scopus 로고    scopus 로고
    • Treatment of cultured myotubes with the calcium ionophore A23187 increases proteasome activity via a CaMK II-caspase-calpain-dependent mechanism
    • Menconi, M.J., W. Wei, H. Yang, C.J. Wray, and P.O. Hasselgren. 2004. Treatment of cultured myotubes with the calcium ionophore A23187 increases proteasome activity via a CaMK II-caspase-calpain-dependent mechanism. Surgery 136:135-142.
    • (2004) Surgery , vol.136 , pp. 135-142
    • Menconi, M.J.1    Wei, W.2    Yang, H.3    Wray, C.J.4    Hasselgren, P.O.5
  • 117
    • 0031425839 scopus 로고    scopus 로고
    • AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle
    • Merrill, G.F., E.J. Kurth, D.G. Hardie, and W.W. Winder. 1997. AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle. Am. J. Physiol. -Endocrinol. Metab. 36:E1107-E1112.
    • (1997) Am. J. Physiol. -Endocrinol. Metab , vol.36 , pp. E1107-E1112
    • Merrill, G.F.1    Kurth, E.J.2    Hardie, D.G.3    Winder, W.W.4
  • 120
    • 0034221610 scopus 로고    scopus 로고
    • Frequency of the Rendement Napole RN− allele in a population of American Hampshire pigs
    • Miller, K.D., M. Ellis, F.K. McKeith, B.S. Bidner, and D.J. Meisinger. 2000. Frequency of the Rendement Napole RN− allele in a population of American Hampshire pigs. J. Anim. Sci. 78:1811-1815.
    • (2000) J. Anim. Sci , vol.78 , pp. 1811-1815
    • Miller, K.D.1    Ellis, M.2    McKeith, F.K.3    Bidner, B.S.4    Meisinger, D.J.5
  • 122
    • 0037122766 scopus 로고    scopus 로고
    • Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
    • Minokoshi, Y., Y.B. Kim, O.D. Peroni, L.G. Fryer, C. Muller, D. Carling, and B.B. Kahn. 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
  • 123
    • 0038543072 scopus 로고    scopus 로고
    • Rendement Napole gene effects and a comparison of glycolytic potential and DNA genotyping for classification of Rendement Napole status in Hampshire-sired pigs
    • Moeller, S.J., T.J. Baas, T.D. Leeds, R.S. Emnett, and K.M. Irvin. 2003. Rendement Napole gene effects and a comparison of glycolytic potential and DNA genotyping for classification of Rendement Napole status in Hampshire-sired pigs. J. Anim. Sci. 81:402-410.
    • (2003) J. Anim. Sci , vol.81 , pp. 402-410
    • Moeller, S.J.1    Baas, T.J.2    Leeds, T.D.3    Emnett, R.S.4    Irvin, K.M.5
  • 124
    • 33748747706 scopus 로고    scopus 로고
    • Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro
    • Momcilovic, M., S.P. Hong, and M. Carlson. 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
  • 125
    • 0004472278 scopus 로고
    • Pork of low technological quality with a normal rate of muscle pH fall in the immediate post-mortem period: The case of the Hampshire breed
    • Monin, G. and P. Sellier. 1985. Pork of low technological quality with a normal rate of muscle pH fall in the immediate post-mortem period: the case of the Hampshire breed. Meat Sci. 13:49-63.
    • (1985) Meat Sci , vol.13 , pp. 49-63
    • Monin, G.1    Sellier, P.2
  • 126
    • 0035947235 scopus 로고    scopus 로고
    • A role for AMP-activated protein kinase in contraction-and hypoxia-regulated glucose transport in skeletal muscle
    • Mu, J., J.T. Brozinick, O. Valladares, M. Bucan, and M.J. Birnbaum. 2001. A role for AMP-activated protein kinase in contraction-and hypoxia-regulated glucose transport in skeletal muscle. Mol. Cell 7:1085-1094.
    • (2001) Mol. Cell , vol.7 , pp. 1085-1094
    • Mu, J.1    Brozinick, J.T.2    Valladares, O.3    Bucan, M.4    Birnbaum, M.J.5
  • 127
    • 33846425019 scopus 로고    scopus 로고
    • Increased maternal nutrition stimulates peroxisome proliferator activated receptor-γ (PPARγ), adiponectin and leptin mRNA expression in adipose tissue before birth
    • Muhlhausler, B.S., J.A. Duffield, and I.C. McMillen. 2007. Increased maternal nutrition stimulates peroxisome proliferator activated receptor-γ (PPARγ), adiponectin and leptin mRNA expression in adipose tissue before birth. Endocrinology 148:878-885.
    • (2007) Endocrinology , vol.148 , pp. 878-885
    • Muhlhausler, B.S.1    Duffield, J.A.2    McMillen, I.C.3
  • 128
    • 0023789884 scopus 로고
    • Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase
    • Munday, M.R., D.G. Campbell, D. Carling, and D.G. Hardie. 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
  • 129
    • 0033559856 scopus 로고    scopus 로고
    • AMP-activated kinase reciprocally regulates triacylglycerol synthesis and fatty acid oxidation in liver and muscle: Evidence that sn-glycerol-3-phosphate acyltransferase is a novel target
    • Muoio, D.M., K. Seefeld, L.A. Witters, and R.A. Coleman. 1999. AMP-activated kinase reciprocally regulates triacylglycerol synthesis and fatty acid oxidation in liver and muscle: evidence that sn-glycerol-3-phosphate acyltransferase is a novel target. Biochem. J. 338:783-791.
    • (1999) Biochem. J , vol.338 , pp. 783-791
    • Muoio, D.M.1    Seefeld, K.2    Witters, L.A.3    Coleman, R.A.4
  • 133
    • 34548450714 scopus 로고    scopus 로고
    • AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes
    • Nakashima, K. and Y. Yakabe. 2007. AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes. Biosci. Biotechnol. Biochem. 71:1650-1656.
    • (2007) Biosci. Biotechnol. Biochem , vol.71 , pp. 1650-1656
    • Nakashima, K.1    Yakabe, Y.2
  • 134
    • 0141569397 scopus 로고    scopus 로고
    • Mutation analysis of AMP-activated protein kinase subunits in inherited cardiomyopathies: Implications for kinase function and disease pathogenesis
    • Oliveira, S.M., J. Ehtisham, C.S. Redwood, I. Ostman-Smith, E.M. Blair, and H. Watkins. 2003. Mutation analysis of AMP-activated protein kinase subunits in inherited cardiomyopathies: implications for kinase function and disease pathogenesis. J. Mol. Cell Cardiol. 35:1251-1255.
    • (2003) J. Mol. Cell Cardiol , vol.35 , pp. 1251-1255
    • Oliveira, S.M.1    Ehtisham, J.2    Redwood, C.S.3    Ostman-Smith, I.4    Blair, E.M.5    Watkins, H.6
  • 135
    • 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., E. Doran, and A.P. Halestrap. 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
  • 136
    • 0035836770 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/Akt/mTOR pathway mediates and PTEN antagonizes tumor necrosis factor inhibition of insulin signaling through insulin receptor substrate-1
    • Ozes, O.N., H. Akca, L.D. Mayo, J.A. Gustin, T. Maehama, J.E. Dixon, and D.B. Donner. 2001. A phosphatidylinositol 3-kinase/Akt/mTOR pathway mediates and PTEN antagonizes tumor necrosis factor inhibition of insulin signaling through insulin receptor substrate-1. Proc. Natl. Acad. Sci. U.S.A. 98:4640-4645.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4640-4645
    • Ozes, O.N.1    Akca, H.2    Mayo, L.D.3    Gustin, J.A.4    Maehama, T.5    Dixon, J.E.6    Donner, D.B.7
  • 137
    • 0034773628 scopus 로고    scopus 로고
    • Molecular aspects of lipoic acid in the prevention of diabetes complications
    • Packer, L., K. Kraemer, and G. Rimbach. 2001. Molecular aspects of lipoic acid in the prevention of diabetes complications. Nutrition 17:888-895.
    • (2001) Nutrition , vol.17 , pp. 888-895
    • Packer, L.1    Kraemer, K.2    Rimbach, G.3
  • 138
    • 24144459843 scopus 로고    scopus 로고
    • Regulation of fatty acid uptake and metabolism in L6 skeletal muscle cells by resistin
    • Palanivel, R. and G. Sweeney. 2005. Regulation of fatty acid uptake and metabolism in L6 skeletal muscle cells by resistin. FEBS Lett. 579:5049-5054.
    • (2005) FEBS Lett , vol.579 , pp. 5049-5054
    • Palanivel, R.1    Sweeney, G.2
  • 139
    • 0036136897 scopus 로고    scopus 로고
    • Role of translation initiation factor 2B in control of cell survival by the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3beta signaling pathway. Mol
    • Pap, M. and G.M. Cooper. 2002. Role of translation initiation factor 2B in control of cell survival by the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3beta signaling pathway. Mol. Cell Biol. 22:578-586.
    • (2002) Cell Biol , vol.22 , pp. 578-586
    • Pap, M.1    Cooper, G.M.2
  • 140
    • 0037031840 scopus 로고    scopus 로고
    • Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise
    • Park, H., V.K. Kaushik, S. Constant, M. Prentki, E. Przybytkowski, N.B. Ruderman, and A.K. Saha. 2002. Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise. J. Biol. Chem. 277:32571-32577.
    • (2002) J. Biol. Chem , vol.277 , pp. 32571-32577
    • Park, H.1    Kaushik, V.K.2    Constant, S.3    Prentki, M.4    Przybytkowski, E.5    Ruderman, N.B.6    Saha, A.K.7
  • 141
    • 23944521632 scopus 로고    scopus 로고
    • Skeletal myocyte hypertrophy requires mTOR kinase activity and S6K1
    • Park, I.H., E. Erbay, P. Nuzzi, and J. Chen. 2005. Skeletal myocyte hypertrophy requires mTOR kinase activity and S6K1. Exp. Cell Res. 309:211-219.
    • (2005) Exp. Cell Res , vol.309 , pp. 211-219
    • Park, I.H.1    Erbay, E.2    Nuzzi, P.3    Chen, J.4
  • 142
    • 33947602679 scopus 로고    scopus 로고
    • Differential modulation of AMPK signaling pathways by low or high levels of exogenous reactive oxygen species in colon cancer cells
    • Park, I.J., J.T. Hwang, Y.M. Kim, J. Ha, and O.J. Park. 2006. Differential modulation of AMPK signaling pathways by low or high levels of exogenous reactive oxygen species in colon cancer cells. Ann. N.Y. Acad. Sci. 1091:102-109.
    • (2006) Ann. N.Y. Acad. Sci , vol.1091 , pp. 102-109
    • Park, I.J.1    Hwang, J.T.2    Kim, Y.M.3    Ha, J.4    Park, O.J.5
  • 143
    • 0031892271 scopus 로고    scopus 로고
    • TNF-alpha and insulin resistance: Summary and future prospects
    • Peraldi, P. and B. Spiegelman. 1998. TNF-alpha and insulin resistance: summary and future prospects. Mol. Cell Biochem. 182:169-175.
    • (1998) Mol. Cell Biochem , vol.182 , pp. 169-175
    • Peraldi, P.1    Spiegelman, B.2
  • 144
    • 33748792852 scopus 로고    scopus 로고
    • A comparison of thiazolidinedione-induced adipogenesis and myogenesis in stromal-vascular cells from subcutaneous adipose tissue or semitendinosus muscle of postnatal pigs
    • Poulos, S.P. and G.J. Hausman. 2006. A comparison of thiazolidinedione-induced adipogenesis and myogenesis in stromal-vascular cells from subcutaneous adipose tissue or semitendinosus muscle of postnatal pigs. J. Anim. Sci. 84:1076-1082.
    • (2006) J. Anim. Sci , vol.84 , pp. 1076-1082
    • Poulos, S.P.1    Hausman, G.J.2
  • 145
    • 0037135547 scopus 로고    scopus 로고
    • In vivo phosphorylation of insulin receptor substrate 1 at serine 789 by a novel serine kinase in insulin-resistant rodents
    • Qiao, L.Y., R. Zhande, T.L. Jetton, G. Zhou, and X.J. Sun. 2002. In vivo phosphorylation of insulin receptor substrate 1 at serine 789 by a novel serine kinase in insulin-resistant rodents. J. Biol. Chem. 277:26530-26539.
    • (2002) J. Biol. Chem , vol.277 , pp. 26530-26539
    • Qiao, L.Y.1    Zhande, R.2    Jetton, T.L.3    Zhou, G.4    Sun, X.J.5
  • 146
    • 33746256783 scopus 로고    scopus 로고
    • Ca2+-calmodulin-dependent protein kinase expression and signalling in skeletal muscle during exercise
    • Rose, A.J., B. Kiens, and E.A. Richter. 2006. Ca2+-calmodulin-dependent protein kinase expression and signalling in skeletal muscle during exercise. J. Physiol. -London 574:889-903.
    • (2006) J. Physiol. -London , vol.574 , pp. 889-903
    • Rose, A.J.1    Kiens, B.2    Richter, E.A.3
  • 147
    • 0032881635 scopus 로고    scopus 로고
    • Translocation of myocardial GLUT-4 and increased glucose uptake through activation of AMPK by AICAR
    • Russell, R.R., R. Bergeron, G.I. Shulman, and L.H. Young. 1999. Translocation of myocardial GLUT-4 and increased glucose uptake through activation of AMPK by AICAR. Am. J. Physiol. -Heart Circulat. Physiol. 277:H643-H649.
    • (1999) Am. J. Physiol. -Heart Circulat. Physiol , vol.277 , pp. H643-H649
    • Russell, R.R.1    Bergeron, R.2    Shulman, G.I.3    Young, L.H.4
  • 148
    • 0021824214 scopus 로고
    • 5-Amino-4-imidazolecarboxamide riboside (Z-riboside) metabolism in eukaryotic cells
    • Sabina, R.L., D. Patterson, and E.W. Holmes. 1985. 5-Amino-4-imidazolecarboxamide riboside (Z-riboside) metabolism in eukaryotic cells. J. Biol. Chem. 260:6107-6114.
    • (1985) J. Biol. Chem , vol.260 , pp. 6107-6114
    • Sabina, R.L.1    Patterson, D.2    Holmes, E.W.3
  • 149
    • 17144474893 scopus 로고    scopus 로고
    • Activity of LKB1 and AMPK-related kinases in skeletal muscle: Effects of contraction, phenformin, and AICAR
    • Sakamoto, K., O. Goransson, D.G. Hardie, and D.R. Alessi. 2004. Activity of LKB1 and AMPK-related kinases in skeletal muscle: effects of contraction, phenformin, and AICAR. Am. J. Physiol. -Endocrinol. Metab. 287:E310-E317.
    • (2004) Am. J. Physiol. -Endocrinol. Metab , vol.287 , pp. E310-E317
    • Sakamoto, K.1    Goransson, O.2    Hardie, D.G.3    Alessi, D.R.4
  • 150
    • 20044370885 scopus 로고    scopus 로고
    • Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction
    • Sakamoto, K., A. McCarthy, D. Smith, K.A. Green, D.G. Hardie, A. Ashworth, and D.R. Alessi. 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
  • 153
    • 34147152841 scopus 로고    scopus 로고
    • Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
    • Sanders, M.J., P.O. Grondin, B.D. Hegarty, M.A. Snowden, and D. Carling. 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
  • 154
    • 4043085036 scopus 로고    scopus 로고
    • Adenovirusmediated chronic “hyper-resistinemia” leads to in vivo insulin resistance in normal rats
    • Satoh, H., M.T.A. Nguyen, P.D.G. Miles, T. Imamura, I. Usui, and J.M. Olefsky. 2004. Adenovirusmediated chronic “hyper-resistinemia” leads to in vivo insulin resistance in normal rats. J. Clin. Invest. 114:224-231.
    • (2004) J. Clin. Invest , vol.114 , pp. 224-231
    • Satoh, H.1    Nguyen, M.T.A.2    Miles, P.D.G.3    Imamura, T.4    Usui, I.5    Olefsky, J.M.6
  • 155
    • 0345830423 scopus 로고    scopus 로고
    • Calcineurin signaling and NFAT activation in cardiovascular and skeletal muscle development
    • Schulz, R.A. and K.E. Yutzey. 2004. Calcineurin signaling and NFAT activation in cardiovascular and skeletal muscle development. Dev. Biol. 266:1-16.
    • (2004) Dev. Biol , vol.266 , pp. 1-16
    • Schulz, R.A.1    Yutzey, K.E.2
  • 157
    • 33745307617 scopus 로고    scopus 로고
    • Ras, PI(3)K and mTOR signalling controls tumour cell growth
    • Shaw, R.J. and L.C. Cantley. 2006. Ras, PI(3)K and mTOR signalling controls tumour cell growth. Nature 441:424-430.
    • (2006) Nature , vol.441 , pp. 424-430
    • Shaw, R.J.1    Cantley, L.C.2
  • 158
  • 160
    • 27144455796 scopus 로고    scopus 로고
    • Role of AMP-activated protein kinase in the glycolysis of postmortem muscle
    • Shen, Q.W. and M. Du. 2005. Role of AMP-activated protein kinase in the glycolysis of postmortem muscle. J. Sci. Food Agric. 85:2401-2406.
    • (2005) J. Sci. Food Agric , vol.85 , pp. 2401-2406
    • Shen, Q.W.1    Du, M.2
  • 161
    • 33746133584 scopus 로고    scopus 로고
    • Fitness and fatness: The debate continues for AMP activated protein kinase in heart function
    • Shen, Q.W., M. Du, and J. Ren. 2006a. Fitness and fatness: the debate continues for AMP activated protein kinase in heart function. Curr. Cardiol. Rev. 2:117-123.
    • (2006) Curr. Cardiol. Rev , vol.2 , pp. 117-123
    • Shen, Q.W.1    Du, M.2    Ren, J.3
  • 163
    • 33746902695 scopus 로고    scopus 로고
    • Early post-mortem AMP-activated protein kinase (AMPK) activation leads to phosphofructokinase-2 and -1 (PFK-2 and PFK-1) phosphorylation and the development of pale, soft, and exudative (PSE) conditions in porcine longissimus muscle
    • Shen, Q.W., W.J. Means, K.R. Underwood, S.A. Thompson, M. J. Zhu, R. J. McCormick, S. P. Ford, M. Ellis, and M. Du. 2006c. Early post-mortem AMP-activated protein kinase (AMPK) activation leads to phosphofructokinase-2 and -1 (PFK-2 and PFK-1) phosphorylation and the development of pale, soft, and exudative (PSE) conditions in porcine longissimus muscle. J. Agric. Food Chem. 54:5583-5589.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 5583-5589
    • Shen, Q.W.1    Means, W.J.2    Underwood, K.R.3    Thompson, S.A.4    Zhu, M.J.5    McCormick, R.J.6    Ford, S.P.7    Ellis, M.8    Du, M.9
  • 164
    • 34247218013 scopus 로고    scopus 로고
    • The halothane gene, energy metabolism, adenosine monophosphate-activated protein kinase, and glycolysis in postmortem pig longissimus dorsi muscle
    • Shen, Q.W., K.R. Underwood, W.J. Means, R.J. McCormick, and M. Du. 2007a. The halothane gene, energy metabolism, adenosine monophosphate-activated protein kinase, and glycolysis in postmortem pig longissimus dorsi muscle. J. Anim. Sci. 85:1054-1061.
    • (2007) J. Anim. Sci , vol.85 , pp. 1054-1061
    • Shen, Q.W.1    Underwood, K.R.2    Means, W.J.3    McCormick, R.J.4    Du, M.5
  • 165
    • 35048853951 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase kinase is involved in AMP-activated protein kinase activation by alpha-lipoic acid in C2C12 myotubes
    • Shen, Q.W., M.J. Zhu, J. Tong, J. Ren, and M. Du. 2007b. Ca2+/calmodulin-dependent protein kinase kinase is involved in AMP-activated protein kinase activation by alpha-lipoic acid in C2C12 myotubes. Am. J. Physiol. Cell Physiol. 293:C1395-1403.
    • (2007) Am. J. Physiol. Cell Physiol , vol.293 , pp. C1395-C1403
    • Shen, Q.W.1    Zhu, M.J.2    Tong, J.3    Ren, J.4    Du, M.5
  • 166
    • 33746902695 scopus 로고    scopus 로고
    • Early post-mortem AMP-activated protein kinase (AMPK) activation leads to phosphofructokinase-2 and-1 (PFK-2 and PFK-1) phosphorylation and the development of pale, soft, and exudative (PSE) conditions in porcine longissimus muscle
    • Shen, Q.W., W.J. Means, K.R. Underwood, S.A. Thompson, M.J. Zhu, R.J. McCormick, S.P. Ford, M. Ellis, and M. Du. 2006d. Early post-mortem AMP-activated protein kinase (AMPK) activation leads to phosphofructokinase-2 and-1 (PFK-2 and PFK-1) phosphorylation and the development of pale, soft, and exudative (PSE) conditions in porcine longissimus muscle. J. Agric. Food Chem. 54:5583-5589.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 5583-5589
    • Shen, Q.W.1    Means, W.J.2    Underwood, K.R.3    Thompson, S.A.4    Zhu, M.J.5    McCormick, R.J.6    Ford, S.P.7    Ellis, M.8    Du, M.9
  • 169
    • 18944402728 scopus 로고    scopus 로고
    • Insulin-like growth factor I-mediated skeletal muscle hypertrophy is characterized by increased mTOR-p70S6K signaling without increased Akt phosphorylation
    • Song, Y.H., M. Godard, Y. Li, S.R. Richmond, N. Rosenthal, and P. Delafontaine. 2005. Insulin-like growth factor I-mediated skeletal muscle hypertrophy is characterized by increased mTOR-p70S6K signaling without increased Akt phosphorylation. J. Investig. Med. 53:135-142.
    • (2005) J. Investig. Med , vol.53 , pp. 135-142
    • Song, Y.H.1    Godard, M.2    Li, Y.3    Richmond, S.R.4    Rosenthal, N.5    Delafontaine, P.6
  • 170
  • 171
    • 0032523194 scopus 로고    scopus 로고
    • Diastolic dysfunction and altered energetics in the alphaMHC403/+ mouse model of familial hypertrophic cardiomyopathy
    • Spindler, M., K.W. Saupe, M.E. Christe, H.L. Sweeney, C.E. Seidman, J.G. Seidman, and J.S. Ingwall. 1998. Diastolic dysfunction and altered energetics in the alphaMHC403/+ mouse model of familial hypertrophic cardiomyopathy. J. Clin. Invest. 101:1775-1783.
    • (1998) J. Clin. Invest , vol.101 , pp. 1775-1783
    • Spindler, M.1    Saupe, K.W.2    Christe, M.E.3    Sweeney, H.L.4    Seidman, C.E.5    Seidman, J.G.6    Ingwall, J.S.7
  • 175
    • 0034141355 scopus 로고    scopus 로고
    • The regulation of AMP-activated protein kinase by phosphorylation
    • Stein, S.C., A. Woods, N.A. Jones, M.D. Davison, and D. Carling. 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
  • 178
    • 0037370773 scopus 로고    scopus 로고
    • AMPK expression and phosphorylation are increased in rodent muscle after chronic leptin treatment
    • Steinberg, G.R., J.W. E. Rush, and D.J. Dyck. 2003. AMPK expression and phosphorylation are increased in rodent muscle after chronic leptin treatment. Am. J. Physiol. -Endocrinol. Metab. 284:E648-E654.
    • (2003) Am. J. Physiol. -Endocrinol. Metab , vol.284 , pp. E648-E654
    • Steinberg, G.R.1    Rush, J.W.E.2    Dyck, D.J.3
  • 179
    • 15244340082 scopus 로고    scopus 로고
    • Insulinlike growth factor 1 inhibits extracellular signal-regulated kinase to promote neuronal survival via the phosphatidylinositol 3-kinase/protein kinase A/c-Raf pathway
    • Subramaniam, S., N. Shahani, J. Strelau, C. Laliberte, R. Brandt, D. Kaplan, and K. Unsicker. 2005. Insulinlike growth factor 1 inhibits extracellular signal-regulated kinase to promote neuronal survival via the phosphatidylinositol 3-kinase/protein kinase A/c-Raf pathway. J. Neurosci. 25:2838-2852.
    • (2005) J. Neurosci , vol.25 , pp. 2838-2852
    • Subramaniam, S.1    Shahani, N.2    Strelau, J.3    Laliberte, C.4    Brandt, R.5    Kaplan, D.6    Unsicker, K.7
  • 180
    • 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., K.J. Brocklehurst, A.E. Marley, F. Carey, D. Carling, and R.K. Beri. 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
  • 181
    • 0032524622 scopus 로고    scopus 로고
    • Identification of a novel AMP-activated protein kinase beta subunit isoform that is highly expressed in skeletal muscle
    • Thornton, C., M.A. Snowden, and D. Carling. 1998. Identification of a novel AMP-activated protein kinase beta subunit isoform that is highly expressed in skeletal muscle. J. Biol. Chem. 273:12443-12450.
    • (1998) J. Biol. Chem , vol.273 , pp. 12443-12450
    • Thornton, C.1    Snowden, M.A.2    Carling, D.3
  • 182
    • 0035797839 scopus 로고    scopus 로고
    • Increased adenosine monophosphate-activated protein kinase activity in rat hearts with pressure-overload hypertrophy
    • Tian, R., N. Musi, J. D’Agostino, M.F. Hirshman, and L.J. Goodyear. 2001. Increased adenosine monophosphate-activated protein kinase activity in rat hearts with pressure-overload hypertrophy. Circulation 104:1664-1669.
    • (2001) Circulation , vol.104 , pp. 1664-1669
    • Tian, R.1    Musi, N.2    D’Agostino, J.3    Hirshman, M.F.4    Goodyear, L.J.5
  • 183
    • 0037059013 scopus 로고    scopus 로고
    • Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: Acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation
    • Tomas, E., T.S. Tsao, A.K. Saha, H.E. Murrey, C. Zhang, S.I. Itani, H.F. Lodish, and N.B. Ruderman. 2002. Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation. Proc. Natl. Acad. Sci. U.S.A. 99:16309-16313.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16309-16313
    • Tomas, E.1    Tsao, T.S.2    Saha, A.K.3    Murrey, H.E.4    Zhang, C.5    Itani, S.I.6    Lodish, H.F.7    Ruderman, N.B.8
  • 184
    • 45549084432 scopus 로고    scopus 로고
    • AMP-activated protein kinase and adipogenesis in sheep fetal skeletal muscle and 3T3-L1 cells
    • Tong, J., M.J. Zhu, K.R. Underwood, B.W. Hess, S.P. Ford, and M. Du. 2008. AMP-activated protein kinase and adipogenesis in sheep fetal skeletal muscle and 3T3-L1 cells. J. Anim. Sci. 86:1296-1305.
    • (2008) J. Anim. Sci , vol.86 , pp. 1296-1305
    • Tong, J.1    Zhu, M.J.2    Underwood, K.R.3    Hess, B.W.4    Ford, S.P.5    Du, M.6
  • 186
    • 40849130910 scopus 로고    scopus 로고
    • AMP-activated protein kinase is negatively associated with intramuscular fat content in longissimus dorsi muscle of beef cattle
    • Underwood, K.R., W.J. Means, M.J. Zhu, S.P. Ford, B.W. Hess, and M. Du. 2008. AMP-activated protein kinase is negatively associated with intramuscular fat content in longissimus dorsi muscle of beef cattle. Meat Sci. 79:394-402.
    • (2008) Meat Sci , vol.79 , pp. 394-402
    • Underwood, K.R.1    Means, W.J.2    Zhu, M.J.3    Ford, S.P.4    Hess, B.W.5    Du, M.6
  • 187
    • 0033227064 scopus 로고    scopus 로고
    • Glycolytic potential of red, soft, exudative pork longissimus muscle
    • van Laack, R.L. and R.G. Kauffman. 1999. Glycolytic potential of red, soft, exudative pork longissimus muscle. J. Animal Sci. 77:2971-2973.
    • (1999) J. Animal Sci , vol.77 , pp. 2971-2973
    • Van Laack, R.L.1    Kauffman, R.G.2
  • 188
    • 33644864086 scopus 로고    scopus 로고
    • IGF-I stimulates protein synthesis in skeletal muscle through multiple signaling pathways during sepsis
    • Vary, T.C. 2006. IGF-I stimulates protein synthesis in skeletal muscle through multiple signaling pathways during sepsis. Am. J. Physiol. Regul. Integr. Comp. Physiol. 290:R313-321.
    • (2006) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.290 , pp. R313-R321
    • Vary, T.C.1
  • 189
    • 0036838861 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor eIF2Bepsilon in skeletal muscle during sepsis
    • Vary, T.C., G. Deiter, and S.R. Kimball. 2002. Phosphorylation of eukaryotic initiation factor eIF2Bepsilon in skeletal muscle during sepsis. Am. J. Physiol. Endocrinol. Metab. 283:E1032-1039.
    • (2002) Am. J. Physiol. Endocrinol. Metab , vol.283 , pp. E1032-E1039
    • Vary, T.C.1    Deiter, G.2    Kimball, S.R.3
  • 190
  • 191
    • 33747619854 scopus 로고    scopus 로고
    • Insulin resistance accelerates muscle protein degradation: Activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling
    • Wang, X., Z. Hu, J. Hu, J. Du, and W.E. Mitch. 2006. Insulin resistance accelerates muscle protein degradation: activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling. Endocrinology 147:4160-4168.
    • (2006) Endocrinology , vol.147 , pp. 4160-4168
    • Wang, X.1    Hu, Z.2    Hu, J.3    Du, J.4    Mitch, W.E.5
  • 193
    • 0032792665 scopus 로고    scopus 로고
    • AMP-activated protein kinase, a metabolic master switch: Possible roles in type 2 diabetes
    • Winder, W.W., and D.G. Hardie. 1999. 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 , pp. EE1-E10
    • Winder, W.W.1    Hardie, D.G.2
  • 194
    • 0033949848 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle
    • Winder, W.W., B.F. Holmes, D.S. Rubink, E.B. Jensen, M. Chen, and J.O. Holloszy. 2000a. 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
  • 195
    • 85057440763 scopus 로고    scopus 로고
    • Chronic chemical activation of AMP-activated protein kinase increases mitochondrial enzymes and GLUT4 in skeletal muscle of resting rats
    • Winder, W.W., B.F. Holmes, D.S. Rubink, E.B. Jensen, M. Chen, and J.O. Holloszy. 2000b. Chronic chemical activation of AMP-activated protein kinase increases mitochondrial enzymes and GLUT4 in skeletal muscle of resting rats. Diabetes 49:A10.
    • (2000) Diabetes , vol.49 , pp. 10
    • Winder, W.W.1    Holmes, B.F.2    Rubink, D.S.3    Jensen, E.B.4    Chen, M.5    Holloszy, J.O.6
  • 197
    • 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
    • Woods, A., D. Azzout-Marniche, M. Foretz, S.C. Stein, P. Lemarchand, P. Ferre, F. Foufelle, and D. Carling. 2000. 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. 20:6704-6711.
    • (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
  • 198
    • 23044437445 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells
    • Woods, A., K. Dickerson, R. Heath, S.P. Hong, M. Momcilovic, S.R. Johnstone, M. Carlson, and D. Carling. 2005. Ca2+/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
  • 200
    • 0030592623 scopus 로고    scopus 로고
    • The alpha1 and alpha2 isoforms of the AMPactivated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro
    • Woods, A., I. Salt, J. Scott, D.G. Hardie, and D. Carling. 1996. The alpha1 and alpha2 isoforms of the AMPactivated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro. FEBS Lett. 397:347-351.
    • (1996) FEBS Lett , vol.397 , pp. 347-351
    • Woods, A.1    Salt, I.2    Scott, J.3    Hardie, D.G.4    Carling, D.5
  • 201
    • 0043210478 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis
    • Woods, A., D. Vertommen, D. Neumann, R. Turk, J. Bayliss, U. Schlattner, T. Wallimann, D. Carlling, and M.H. Rider. 2003b. Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis. J. Biol. Chem. 278:28434-28442.
    • (2003) J. Biol. Chem , vol.278 , pp. 28434-28442
    • Woods, A.1    Vertommen, D.2    Neumann, D.3    Turk, R.4    Bayliss, J.5    Schlattner, U.6    Wallimann, T.7    Carlling, D.8    Rider, M.H.9
  • 202
    • 0037983775 scopus 로고    scopus 로고
    • Involvement of AMPactivated protein kinase in glucose uptake stimulated by the globular domain of adiponectin in primary rat adipocytes
    • Wu, X.D., H. Motoshima, K. Mahadev, T.J. Stalker, R. Scalia, and B.J. Goldstein. 2003. Involvement of AMPactivated protein kinase in glucose uptake stimulated by the globular domain of adiponectin in primary rat adipocytes. Diabetes 52:1355-1363.
    • (2003) Diabetes , vol.52 , pp. 1355-1363
    • Wu, X.D.1    Motoshima, H.2    Mahadev, K.3    Stalker, T.J.4    Scalia, R.5    Goldstein, B.J.6
  • 203
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger, S., R. Loewith, and M.N. Hall. 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
  • 206
    • 0035914324 scopus 로고    scopus 로고
    • Regulation of transcription by AMP-activated protein kinase — phosphorylation of p300 blocks its interaction with nuclear receptors
    • Yang, W.B., Y.H. Hong, X.Q. Shen, C. Frankowski, H.S. Camp, and T. Leff. 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.B.1    Hong, Y.H.2    Shen, X.Q.3    Frankowski, C.4    Camp, H.S.5    Leff, T.6
  • 207
    • 33750578279 scopus 로고    scopus 로고
    • Adiponectin increases fatty acid oxidation in skeletal muscle cells by sequential activation of AMP-activated protein kinase, p38 mitogenactivated protein kinase, and peroxisome proliferator-activated receptor alpha
    • Yoon, M.J., G.Y. Lee, J.J. Chung, Y.H. Ahn, S.H. Hong, and J.B. Kim. 2006. Adiponectin increases fatty acid oxidation in skeletal muscle cells by sequential activation of AMP-activated protein kinase, p38 mitogenactivated protein kinase, and peroxisome proliferator-activated receptor alpha. Diabetes 55:2562-2570.
    • (2006) Diabetes , vol.55 , pp. 2562-2570
    • Yoon, M.J.1    Lee, G.Y.2    Chung, J.J.3    Ahn, Y.H.4    Hong, S.H.5    Kim, J.B.6
  • 208
    • 0031028222 scopus 로고    scopus 로고
    • Lowflow ischemia leads to translocation of canine heart GLUT-4 and GLUT-1 glucose transporters to the sarcolemma in vivo
    • Young, L.H., Y. Renfu, R. Russell, X.Y. Hu, M. Caplan, J.M. Ren, G.I. Shulman, and A.J. Sinusas. 1997. Lowflow ischemia leads to translocation of canine heart GLUT-4 and GLUT-1 glucose transporters to the sarcolemma in vivo. Circulation 95:415-422.
    • (1997) Circulation , vol.95 , pp. 415-422
    • Young, L.H.1    Renfu, Y.2    Russell, R.3    Hu, X.Y.4    Caplan, M.5    Ren, J.M.6    Shulman, G.I.7    Sinusas, A.J.8
  • 209
  • 212
    • 43749110487 scopus 로고    scopus 로고
    • AMP-activated protein kinase signalling pathways are down regulated and skeletal muscle development impaired in fetuses of obese, overnourished sheep
    • Zhu, M., B. Han, J. Tong, C. Ma, J.W. Kimzey, K.R. Underwood, Y. Xiao, B.W. Hess, S.P. Ford, P.W. Nathanielsz, and M. Du. 2008. AMP-activated protein kinase signalling pathways are down regulated and skeletal muscle development impaired in fetuses of obese, overnourished sheep. J. Physiol. 586:2651-2664.
    • (2008) J. Physiol , vol.586 , pp. 2651-2664
    • Zhu, M.1    Han, B.2    Tong, J.3    Ma, C.4    Kimzey, J.W.5    Underwood, K.R.6    Xiao, Y.7    Hess, B.W.8    Ford, S.P.9    Nathanielsz, P.W.10    Du, M.11
  • 213
    • 0032702870 scopus 로고    scopus 로고
    • Alpha-Lipoic acid in the treatment of diabetic polyneuropathy in Germany: Current evidence from clinical trials. Exper. Clin. Endocrinol
    • Ziegler, D., M. Reljanovic, H. Mehnert, and F.A. Gries. 1999. alpha-Lipoic acid in the treatment of diabetic polyneuropathy in Germany: current evidence from clinical trials. Exper. Clin. Endocrinol. Diabetes 107:421-430.
    • (1999) Diabetes , vol.107 , pp. 421-430
    • Ziegler, D.1    Reljanovic, M.2    Mehnert, H.3    Gries, F.A.4
  • 214
    • 0031028636 scopus 로고    scopus 로고
    • Effects of treatment with the antioxidant alpha-lipoic acid on cardiac autonomic neuropathy in NIDDM patients — a 4-month randomized controlled multicenter trial (DEKAN study)
    • Ziegler, D., H. Schatz, F. Conrad, F.A. Gries, H. Ulrich, and G. Reichel. 1997. Effects of treatment with the antioxidant alpha-lipoic acid on cardiac autonomic neuropathy in NIDDM patients — a 4-month randomized controlled multicenter trial (DEKAN study). Diabetes Care 20:369-373.
    • (1997) Diabetes Care , vol.20 , pp. 369-373
    • Ziegler, D.1    Schatz, H.2    Conrad, F.3    Gries, F.A.4    Ulrich, H.5    Reichel, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.