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Volumn 28, Issue 10, 2014, Pages 1602-1615

Minireview: Hey U(PS): Metabolic and proteolytic homeostasis linked via AMPK and the ubiquitin proteasome system

Author keywords

[No Author keywords available]

Indexed keywords

ATROGIN 1; DEUBIQUITINASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; LAFORIN; MALIN; MUSCLE RING FINGER 1 PROTEIN; PROTEASOME; REGULATOR PROTEIN; S PHASE KINASE ASSOCIATED PROTEIN 2; SUMO PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84907676869     PISSN: 08888809     EISSN: 19449917     Source Type: Journal    
DOI: 10.1210/me.2014-1180     Document Type: Article
Times cited : (31)

References (157)
  • 1
    • 0015864346 scopus 로고
    • Modulation of 3-hydroxy-3- methylglutaryl coenzyme A reductase activity with cAMP and wth protein fractions of rat liver cytosol
    • Beg ZH, Allmann DW, Gibson DM. Modulation of 3-hydroxy-3- methylglutaryl coenzyme A reductase activity with cAMP and wth protein fractions of rat liver cytosol. Biochem Biophys Res Commun. 1973;54(4):1362-1369.
    • (1973) Biochem Biophys Res Commun , vol.54 , Issue.4 , pp. 1362-1369
    • Beg, Z.H.1    Allmann, D.W.2    Gibson, D.M.3
  • 2
    • 0015918822 scopus 로고
    • Regulation of hepatic acetyl coenzyme A carboxylase by phosphorylation and dephosphorylation
    • Carlson CA, Kim KH. Regulation of hepatic acetyl coenzyme A carboxylase by phosphorylation and dephosphorylation. J Biol Chem. 1973;248(1):378-380.
    • (1973) J Biol Chem , vol.248 , Issue.1 , pp. 378-380
    • Carlson, C.A.1    Kim, K.H.2
  • 3
    • 0024786438 scopus 로고
    • Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl- CoA reductase kinase activities
    • Carling D, Clarke PR, Zammit VA, Hardie DG. Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl- CoA reductase kinase activities. Eur J Biochem. 1989; 186(1-2):129-136.
    • (1989) Eur J Biochem , vol.186 , Issue.1-2 , pp. 129-136
    • Carling, D.1    Clarke, P.R.2    Zammit, V.A.3    Hardie, D.G.4
  • 4
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: A nutrient and energy sensor that maintains energy homeostasis
    • Hardie DG, Ross FA, Hawley SA. AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nat Rev Mol Cell Biol. 2012;13(4):251-262.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , Issue.4 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 5
    • 84883709817 scopus 로고    scopus 로고
    • AMPK: A target for drugs and natural products with effects on both diabetes and cancer
    • Hardie DG. AMPK: a target for drugs and natural products with effects on both diabetes and cancer. Diabetes. 2013;62(7):2164-2172.
    • (2013) Diabetes , vol.62 , Issue.7 , pp. 2164-2172
    • Hardie, D.G.1
  • 6
    • 84865846785 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulation and biological actions in the heart
    • Zaha VG, Young LH. AMP-activated protein kinase regulation and biological actions in the heart. Circ Res. 2012;111(6):800-814.
    • (2012) Circ Res , vol.111 , Issue.6 , pp. 800-814
    • Zaha, V.G.1    Young, L.H.2
  • 7
    • 64349115078 scopus 로고    scopus 로고
    • AMPK in the brain: Its roles in energy balance and neuroprotection
    • Ronnett GV, Ramamurthy S, Kleman AM, Landree LE, Aja S. AMPK in the brain: its roles in energy balance and neuroprotection. J Neurochem. 2009;109(suppl 1):17-23.
    • (2009) J Neurochem , vol.109 , Issue.1 , pp. 17-23
    • Ronnett, G.V.1    Ramamurthy, S.2    Kleman, A.M.3    Landree, L.E.4    Aja, S.5
  • 8
    • 0032567252 scopus 로고    scopus 로고
    • Functional domains of the α1 catalytic subunit of the AMP-activated protein kinase
    • Crute BE, Seefeld K, Gamble J, Kemp BE, Witters LA. Functional domains of the α1 catalytic subunit of the AMP-activated protein kinase. J Biol Chem. 1998;273(52):35347-35354.
    • (1998) J Biol Chem , vol.273 , Issue.52 , pp. 35347-35354
    • Crute, B.E.1    Seefeld, K.2    Gamble, J.3    Kemp, B.E.4    Witters, L.A.5
  • 9
    • 0032529139 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Greater AMP dependence, and preferential nuclear localization, of complexes containing the α2 isoform
    • Salt I, Celler JW, Hawley SA, et al. AMP-activated protein kinase: greater AMP dependence, and preferential nuclear localization, of complexes containing the α2 isoform. Biochem J. 1998;334(pt 1):177-187.
    • (1998) Biochem J , vol.334 , pp. 177-187
    • Salt, I.1    Celler, J.W.2    Hawley, S.A.3
  • 10
    • 0038814313 scopus 로고    scopus 로고
    • A novel domain in AMPactivated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias
    • Hudson ER, Pan DA, James J, et al. A novel domain in AMPactivated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias. Curr Biol. 2003; 13(10):861-866.
    • (2003) Curr Biol , vol.13 , Issue.10 , pp. 861-866
    • Hudson, E.R.1    Pan, D.A.2    James, J.3
  • 11
    • 0032524622 scopus 로고    scopus 로고
    • Identification of a novel AMP-activated protein kinase β subunit isoform that is highly expressed in skeletal muscle
    • Thornton C, Snowden MA, Carling D. Identification of a novel AMP-activated protein kinase β subunit isoform that is highly expressed in skeletal muscle. J Biol Chem. 1998;273(20):12443-12450.
    • (1998) J Biol Chem , vol.273 , Issue.20 , pp. 12443-12450
    • Thornton, C.1    Snowden, M.A.2    Carling, D.3
  • 12
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • Bateman A. The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem Sci. 1997;22(1):12-13.
    • (1997) Trends Biochem Sci , vol.22 , Issue.1 , pp. 12-13
    • Bateman, A.1
  • 13
    • 85047691317 scopus 로고    scopus 로고
    • CBS domains form energysensing modules whose binding of adenosine ligands is disrupted by disease mutations
    • Scott JW, Hawley SA, Green KA, et al. CBS domains form energysensing modules whose binding of adenosine ligands is disrupted by disease mutations. J Clin Invest. 2004;113(2):274-284.
    • (2004) J Clin Invest , vol.113 , Issue.2 , pp. 274-284
    • Scott, J.W.1    Hawley, S.A.2    Green, K.A.3
  • 14
    • 0034654362 scopus 로고    scopus 로고
    • Characterization of AMP-activated protein kinase -γ subunit isoforms and their role in AMP binding
    • Cheung PC, Salt IP, Davies SP, Hardie DG, Carling D. Characterization of AMP-activated protein kinase γ-subunit isoforms and their role in AMP binding. Biochem J. 2000;346(pt 3):659-669.
    • (2000) Biochem J , vol.346 , pp. 659-669
    • Cheung, P.C.1    Salt, I.P.2    Davies, S.P.3    Hardie, D.G.4    Carling, D.5
  • 15
    • 33749367975 scopus 로고    scopus 로고
    • Activation of AMPK α-and γ-isoform complexes in the intact ischemic rat heart
    • Li J, Coven DL, Miller EJ, Hu X, et al. Activation of AMPK α- and γ-isoform complexes in the intact ischemic rat heart. Am J Physiol Heart Circ Physiol. 2006;291(4):H1927-H1934.
    • (2006) Am J Physiol Heart Circ Physiol , vol.291 , Issue.4 , pp. H1927-H1934
    • Li, J.1    Coven, D.L.2    Miller, E.J.3    Hu, X.4
  • 16
    • 0942265675 scopus 로고    scopus 로고
    • Expression profiling of the γ-subunit isoforms of AMP-activated protein kinase suggests a major role for γ3 in white skeletal muscle
    • Mahlapuu M, Johansson C, Lindgren K, et al. Expression profiling of the γ-subunit isoforms of AMP-activated protein kinase suggests a major role for γ3 in white skeletal muscle. Am J Physiol Endocrinol Metab. 2004;286(2):E194-E200.
    • (2004) Am J Physiol Endocrinol Metab , vol.286 , Issue.2 , pp. E194-E200
    • Mahlapuu, M.1    Johansson, C.2    Lindgren, K.3
  • 17
    • 0022371303 scopus 로고
    • Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5¢-monophosphate
    • Ferrer A, Caelles C, Massot N, Hegardt FG. Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5¢-monophosphate. Biochem Biophys Res Commun. 1985;132(2):497-504.
    • (1985) Biochem Biophys Res Commun , vol.132 , Issue.2 , pp. 497-504
    • Ferrer, A.1    Caelles, C.2    Massot, N.3    Hegardt, F.G.4
  • 18
    • 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 SA, Davison M, Woods A, et al. 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. 1996;271(44): 27879-27887.
    • (1996) J Biol Chem , vol.271 , Issue.44 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3
  • 19
    • 1542618348 scopus 로고    scopus 로고
    • The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress
    • Shaw RJ, Kosmatka M, Bardeesy N, et al. The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress. Proc Natl Acad Sci USA. 2004;101(10):3329-3335.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.10 , pp. 3329-3335
    • Shaw, R.J.1    Kosmatka, M.2    Bardeesy, N.3
  • 20
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinaseβ is an alternative upstream kinase for AMPactivated protein kinase
    • Hawley SA, Pan DA, Mustard KJ, et al. Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMPactivated protein kinase. Cell Metab. 2005;2(1):9-19.
    • (2005) Cell Metab , vol.2 , Issue.1 , pp. 9-19
    • Hawley, S.A.1    Pan, D.A.2    Mustard, K.J.3
  • 21
    • 0028845251 scopus 로고
    • 5¢-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
    • Hawley SA, Selbert MA, Goldstein EG, Edelman AM, Carling D, Hardie DG. 5¢-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. J Biol Chem. 1995;270(45):27186-27191.
    • (1995) J Biol Chem , vol.270 , Issue.45 , 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
  • 22
    • 33748747706 scopus 로고    scopus 로고
    • Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro
    • Momcilovic M, Hong SP, Carlson M. Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro. J Biol Chem. 2006;281(35):25336-25343.
    • (2006) J Biol Chem , vol.281 , Issue.35 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.P.2    Carlson, M.3
  • 23
    • 33751229931 scopus 로고    scopus 로고
    • A pivotal role for endogenous TGFβ-activated kinase-1 in the LKB1/AMP-activated protein kinase energy-sensor pathway
    • Xie M, Zhang D, Dyck JR, et al. A pivotal role for endogenous TGF-β-activated kinase-1 in the LKB1/AMP-activated protein kinase energy-sensor pathway. Proc Natl Acad Sci USA. 2006; 103(46):17378-17383.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.46 , pp. 17378-17383
    • Xie, M.1    Zhang, D.2    Dyck, J.R.3
  • 24
    • 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-2Cα and native bovine protein phosphatase- 2AC
    • Davies SP, Helps NR, Cohen PT, Hardie DG. 5¢-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C a and native bovine protein phosphatase- 2AC. FEBS Lett. 1995;377(3):421-425.
    • (1995) FEBS Lett , vol.377 , Issue.3 , pp. 421-425
    • Davies, S.P.1    Helps, N.R.2    Cohen, P.T.3    Hardie, D.G.4
  • 25
    • 84885168009 scopus 로고    scopus 로고
    • AMP is a true physiological regulator of AMP-activated protein kinase by both allosteric activation and enhancing net phosphorylation
    • Gowans GJ, Hawley SA, Ross FA, Hardie DG. AMP is a true physiological regulator of AMP-activated protein kinase by both allosteric activation and enhancing net phosphorylation. Cell Metab. 2013;18(4):556-566.
    • (2013) Cell Metab , vol.18 , Issue.4 , pp. 556-566
    • Gowans, G.J.1    Hawley, S.A.2    Ross, F.A.3    Hardie, D.G.4
  • 26
    • 2342476366 scopus 로고    scopus 로고
    • High-density lipoprotein and apolipoprotein AI increase endothelialNO synthase activity by protein association and multisite phosphorylation
    • Drew BG, Fidge NH, Gallon-Beaumier G, Kemp BE, Kingwell BA. High-density lipoprotein and apolipoprotein AI increase endothelialNO synthase activity by protein association and multisite phosphorylation. Proc Natl Acad Sci USA. 2004;101(18):6999-7004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.18 , pp. 6999-7004
    • Drew, B.G.1    Fidge, N.H.2    Gallon-Beaumier, G.3    Kemp, B.E.4    Kingwell, B.A.5
  • 27
    • 0037122766 scopus 로고    scopus 로고
    • Leptin stimulates fattyacid oxidation by activating AMP-activated protein kinase
    • Minokoshi Y, Kim YB, Peroni OD, et al. Leptin stimulates fattyacid oxidation by activating AMP-activated protein kinase. Nature. 2002;415(6869):339-343.
    • (2002) Nature , vol.415 , Issue.6869 , pp. 339-343
    • Minokoshi, Y.1    Kim, Y.B.2    Peroni, O.D.3
  • 28
    • 0036851817 scopus 로고    scopus 로고
    • Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMPactivated protein kinase
    • Yamauchi T, Kamon J, Minokoshi Y, et al. Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMPactivated protein kinase. Nat Med. 2002;8(11):1288-1295.
    • (2002) Nat Med , vol.8 , Issue.11 , pp. 1288-1295
    • Yamauchi, T.1    Kamon, J.2    Minokoshi, Y.3
  • 29
    • 33646828975 scopus 로고    scopus 로고
    • Insulin antagonizes ischemia-induced Thr172 phosphorylation of AMP-activated protein kinase α-subunits in heart via hierarchical phosphorylation of Ser485/491
    • Horman S, Vertommen D, Heath R, et al. Insulin antagonizes ischemia-induced Thr172 phosphorylation of AMP-activated protein kinase α-subunits in heart via hierarchical phosphorylation of Ser485/491. J Biol Chem. 2006;281(9):5335-5340.
    • (2006) J Biol Chem , vol.281 , Issue.9 , pp. 5335-5340
    • Horman, S.1    Vertommen, D.2    Heath, R.3
  • 30
    • 34249850161 scopus 로고    scopus 로고
    • The role of AMPK and mTOR in nutrient sensing in pancreatic β-cells
    • Gleason CE, Lu D, Witters LA, Newgard CB, Birnbaum MJ. The role of AMPK and mTOR in nutrient sensing in pancreatic β-cells. J Biol Chem. 2007;282(14):10341-10351.
    • (2007) J Biol Chem , vol.282 , Issue.14 , pp. 10341-10351
    • Gleason, C.E.1    Lu, D.2    Witters, L.A.3    Newgard, C.B.4    Birnbaum, M.J.5
  • 31
    • 33751552452 scopus 로고    scopus 로고
    • Tumor necrosis factor α-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling
    • Steinberg GR, Michell BJ, van Denderen BJ, et al. Tumor necrosis factor α-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling. Cell Metab. 2006;4(6):465-474.
    • (2006) Cell Metab , vol.4 , Issue.6 , pp. 465-474
    • Steinberg, G.R.1    Michell, B.J.2    van Denderen, B.J.3
  • 32
    • 0028073143 scopus 로고
    • Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase
    • Sullivan JE, Brocklehurst KJ, Marley AE, Carey F, Carling D, Beri RK. Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase. FEBS Lett. 1994;353(1):33-36.
    • (1994) FEBS Lett , vol.353 , Issue.1 , 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
  • 33
    • 0034773404 scopus 로고    scopus 로고
    • Role of AMP-activated protein kinase in mechanism of metformin action
    • Zhou G, Myers R, Li Y, et al. Role of AMP-activated protein kinase in mechanism of metformin action. J Clin Invest. 2001; 108(8):1167-1174.
    • (2001) J Clin Invest , vol.108 , Issue.8 , pp. 1167-1174
    • Zhou, G.1    Myers, R.2    Li, Y.3
  • 34
    • 0036324142 scopus 로고    scopus 로고
    • The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism
    • Hawley SA, Gadalla AE, Olsen GS, Hardie DG. The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism. Diabetes. 2002;51(8):2420-2425.
    • (2002) Diabetes , vol.51 , Issue.8 , pp. 2420-2425
    • Hawley, S.A.1    Gadalla, A.E.2    Olsen, G.S.3    Hardie, D.G.4
  • 35
    • 77954933558 scopus 로고    scopus 로고
    • Metformin inhibits hepatic gluconeogenesis in mice independently of the LKB1/AMPK pathway via a decrease in hepatic energy state
    • Foretz M, Hébrard S, Leclerc J, et al. Metformin inhibits hepatic gluconeogenesis in mice independently of the LKB1/AMPK pathway via a decrease in hepatic energy state. J Clin Invest. 2010; 120(7):2355-2369.
    • (2010) J Clin Invest , vol.120 , Issue.7 , pp. 2355-2369
    • Foretz, M.1    Hébrard, S.2    Leclerc, J.3
  • 36
    • 84873707522 scopus 로고    scopus 로고
    • Biguanides suppress hepatic glucagon signalling by decreasing production of cyclic AMP
    • Miller RA, Chu Q, Xie J, Foretz M, Viollet B, Birnbaum MJ. Biguanides suppress hepatic glucagon signalling by decreasing production of cyclic AMP. Nature. 2013;494(7436):256-260.
    • (2013) Nature , vol.494 , Issue.7436 , pp. 256-260
    • Miller, R.A.1    Chu, Q.2    Xie, J.3    Foretz, M.4    Viollet, B.5    Birnbaum, M.J.6
  • 37
    • 0037067666 scopus 로고    scopus 로고
    • The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways
    • Fryer LG, Parbu-Patel A, Carling D. The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways. J Biol Chem. 2002; 277(28):25226-25232.
    • (2002) J Biol Chem , vol.277 , Issue.28 , pp. 25226-25232
    • Fryer, L.G.1    Parbu-Patel, A.2    Carling, D.3
  • 38
    • 33646346627 scopus 로고    scopus 로고
    • Mice lacking adiponectin show decreased hepatic insulin sensitivity and reduced responsiveness to peroxisome proliferator-activated receptor γ agonists
    • Nawrocki AR, Rajala MW, Tomas E, et al. Mice lacking adiponectin show decreased hepatic insulin sensitivity and reduced responsiveness to peroxisome proliferator-activated receptor γ agonists. J Biol Chem. 2006;281(5):2654-2660.
    • (2006) J Biol Chem , vol.281 , Issue.5 , pp. 2654-2660
    • Nawrocki, A.R.1    Rajala, M.W.2    Tomas, E.3
  • 39
    • 67650914230 scopus 로고    scopus 로고
    • AMPK in health and disease
    • Steinberg GR, Kemp BE. AMPK in health and disease. Physiol Rev. 2009;89(3):1025-1078.
    • (2009) Physiol Rev , vol.89 , Issue.3 , pp. 1025-1078
    • Steinberg, G.R.1    Kemp, B.E.2
  • 40
    • 36549040859 scopus 로고    scopus 로고
    • The selectivity of protein kinase inhibitors: A further update
    • Bain J, Plater L, Elliott M, et al. The selectivity of protein kinase inhibitors: a further update. Biochem J. 2007;408(3):297-315.
    • (2007) Biochem J , vol.408 , Issue.3 , pp. 297-315
    • Bain, J.1    Plater, L.2    Elliott, M.3
  • 41
    • 0032881635 scopus 로고    scopus 로고
    • Translocation of myocardial GLUT-4 and increased glucose uptake through activation of AMPK by AICAR
    • Russell RR 3rd, Bergeron R, Shulman GI, Young LH. Translocation of myocardial GLUT-4 and increased glucose uptake through activation of AMPK by AICAR. Am J Physiol. 1999;277(2 pt 2):H643-H649.
    • (1999) Am J Physiol , vol.277 , Issue.2 , pp. H643-H649
    • Russell, R.R.1    Bergeron, R.2    Shulman, G.I.3    Young, L.H.4
  • 42
    • 0037677773 scopus 로고    scopus 로고
    • Contraction-induced fatty acid translocase/CD36 translocation in rat cardiac myocytes is mediated through AMP-activated protein kinase signaling
    • Luiken JJ, Coort SL, Willems J, et al. Contraction-induced fatty acid translocase/CD36 translocation in rat cardiac myocytes is mediated through AMP-activated protein kinase signaling. Diabetes. 2003;52(7):1627-1634.
    • (2003) Diabetes , vol.52 , Issue.7 , pp. 1627-1634
    • Luiken, J.J.1    Coort, S.L.2    Willems, J.3
  • 43
    • 0034687210 scopus 로고    scopus 로고
    • Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia
    • Marsin AS, Bertrand L, Rider MH, et al. Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia. Curr Biol. 2000;10(20):1247-1255.
    • (2000) Curr Biol , vol.10 , Issue.20 , pp. 1247-1255
    • Marsin, A.S.1    Bertrand, L.2    Rider, M.H.3
  • 44
    • 0029093341 scopus 로고
    • High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5¢ -AMP-activated protein kinase inhibition of acetyl-CoA carboxylase
    • Kudo N, Barr AJ, Barr RL, Desai S, Lopaschuk GD. High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5¢ -AMP-activated protein kinase inhibition of acetyl-CoA carboxylase. J Biol Chem. 1995;270(29):17513-17520.
    • (1995) J Biol Chem , vol.270 , Issue.29 , pp. 17513-17520
    • Kudo, N.1    Barr, A.J.2    Barr, R.L.3    Desai, S.4    Lopaschuk, G.D.5
  • 45
    • 0032508564 scopus 로고    scopus 로고
    • Inhibition of hepatocytic autophagy by adenosine, aminoimidazole-4-carboxamide riboside, and N6- mercaptopurine riboside. Evidence for involvement of amp-activated protein kinase
    • Samari HR, Seglen PO. Inhibition of hepatocytic autophagy by adenosine, aminoimidazole-4-carboxamide riboside, and N6- mercaptopurine riboside. Evidence for involvement of amp-activated protein kinase. J Biol Chem. 1998;273(37):23758-23763.
    • (1998) J Biol Chem , vol.273 , Issue.37 , pp. 23758-23763
    • Samari, H.R.1    Seglen, P.O.2
  • 46
    • 0024335432 scopus 로고
    • The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase
    • Carling D, Hardie DG. The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase. Biochim Biophys Acta. 1989;1012(1):81-86.
    • (1989) Biochim Biophys Acta , vol.1012 , Issue.1 , pp. 81-86
    • Carling, D.1    Hardie, D.G.2
  • 47
    • 0029005507 scopus 로고
    • Inhibition of fatty acid and cholesterol synthesis by stimulation of AMPactivated protein kinase
    • Henin N, Vincent MF, Gruber HE, Van den Berghe G. Inhibition of fatty acid and cholesterol synthesis by stimulation of AMPactivated protein kinase. FASEB J. 1995;9(7):541-546.
    • (1995) FASEB J , vol.9 , Issue.7 , pp. 541-546
    • Henin, N.1    Vincent, M.F.2    Gruber, H.E.3    Van den Berghe, G.4
  • 48
    • 0023896220 scopus 로고
    • The low activity of acetyl-CoA carboxylase in basal and glucagon-stimulated hepatocytes is due to phosphorylation by the AMP-activated protein kinase and not cyclic AMPdependent protein kinase
    • Sim AT, Hardie DG. The low activity of acetyl-CoA carboxylase in basal and glucagon-stimulated hepatocytes is due to phosphorylation by the AMP-activated protein kinase and not cyclic AMPdependent protein kinase. FEBS Lett. 1988;233(2):294-298.
    • (1988) FEBS Lett , vol.233 , Issue.2 , pp. 294-298
    • Sim, A.T.1    Hardie, D.G.2
  • 49
    • 0037025356 scopus 로고    scopus 로고
    • AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling
    • Bolster DR, Crozier SJ, Kimball SR, Jefferson LS. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J Biol Chem. 2002;277(27):23977-23980.
    • (2002) J Biol Chem , vol.277 , Issue.27 , pp. 23977-23980
    • Bolster, D.R.1    Crozier, S.J.2    Kimball, S.R.3    Jefferson, L.S.4
  • 50
    • 0037143449 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis
    • Horman S, Browne G, Krause U, et al. Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis. Curr Biol. 2002; 12(16):1419-1423.
    • (2002) Curr Biol , vol.12 , Issue.16 , pp. 1419-1423
    • Horman, S.1    Browne, G.2    Krause, U.3
  • 51
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki K, Zhu T, Guan KL. TSC2 mediates cellular energy response to control cell growth and survival. Cell. 2003;115(5):577-590.
    • (2003) Cell , vol.115 , Issue.5 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 52
    • 84355161919 scopus 로고    scopus 로고
    • Chemical genetic screen for AMPKα2 substrates uncovers a network of proteins involved in mitosis
    • Banko MR, Allen JJ, Schaffer BE, et al. Chemical genetic screen for AMPKα2 substrates uncovers a network of proteins involved in mitosis. Mol Cell. 2011;44(6):878-892.
    • (2011) Mol Cell , vol.44 , Issue.6 , pp. 878-892
    • Banko, M.R.1    Allen, J.J.2    Schaffer, B.E.3
  • 53
    • 80053035284 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An energy sensor that regulates all aspects of cell function
    • Hardie DG. AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. Genes Dev. 2011;25(18): 1895-1908.
    • (2011) Genes Dev , vol.25 , Issue.18 , pp. 1895-1908
    • Hardie, D.G.1
  • 54
    • 84900800420 scopus 로고    scopus 로고
    • AMPK: Regulating energy balance at the cellular and whole body levels
    • Hardie DG, Ashford ML. AMPK: regulating energy balance at the cellular and whole body levels. Physiology (Bethesda). 2014; 29(2):99-107.
    • (2014) Physiology (Bethesda) , vol.29 , Issue.2 , pp. 99-107
    • Hardie, D.G.1    Ashford, M.L.2
  • 55
    • 33745225026 scopus 로고    scopus 로고
    • AMP-activated protein kinase- development of the energy sensor concept
    • Hardie DG, Hawley SA, Scott JW. AMP-activated protein kinase- development of the energy sensor concept. J Physiol. 2006;574(pt 1):7-15.
    • (2006) J Physiol , vol.574 , pp. 7-15
    • Hardie, D.G.1    Hawley, S.A.2    Scott, J.W.3
  • 56
    • 34248194200 scopus 로고    scopus 로고
    • The regulation of AMPK β1, TSC2, and PTEN expression by p53: Stress, cell and tissue specificity, and the role of these gene products in modulating the IGF- 1-AKT-mTOR pathways
    • Feng Z, Hu W, de Stanchina E, et al. The regulation of AMPK β1, TSC2, and PTEN expression by p53: stress, cell and tissue specificity, and the role of these gene products in modulating the IGF- 1-AKT-mTOR pathways. Cancer Res. 2007;67(7):3043-3053.
    • (2007) Cancer Res , vol.67 , Issue.7 , pp. 3043-3053
    • Feng, Z.1    Hu, W.2    de Stanchina, E.3
  • 57
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock KL, Gramm C, Rothstein L, et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 1994; 78(5):761-771.
    • (1994) Cell , vol.78 , Issue.5 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3
  • 59
    • 84874077399 scopus 로고    scopus 로고
    • E3 ubiquitin ligase, WWP1, interacts with AMPKα2 and down-regulates its expression in skeletal muscle C2C12 cells
    • Lee JO, Lee SK, Kim N, et al. E3 ubiquitin ligase, WWP1, interacts with AMPKα2 and down-regulates its expression in skeletal muscle C2C12 cells. J Biol Chem. 2013;288(7):4673-4680.
    • (2013) J Biol Chem , vol.288 , Issue.7 , pp. 4673-4680
    • Lee, J.O.1    Lee, S.K.2    Kim, N.3
  • 60
    • 84860561281 scopus 로고    scopus 로고
    • Loss of AMP-activated protein kinase-α2 impairs the insulin-sensitizing effect of calorie restriction in skeletal muscle
    • Wang P, Zhang RY, Song J, et al. Loss of AMP-activated protein kinase--α2 impairs the insulin-sensitizing effect of calorie restriction in skeletal muscle. Diabetes. 2012;61(5):1051-1061.
    • (2012) Diabetes , vol.61 , Issue.5 , pp. 1051-1061
    • Wang, P.1    Zhang, R.Y.2    Song, J.3
  • 61
    • 44649099112 scopus 로고    scopus 로고
    • Downregulation of AMP-activated protein kinase by Cidea-mediated ubiquitination and degradation in brown adipose tissue
    • Qi J, Gong J, Zhao T, et al. Downregulation of AMP-activated protein kinase by Cidea-mediated ubiquitination and degradation in brown adipose tissue. EMBO J. 2008;27(11):1537-1548.
    • (2008) EMBO J , vol.27 , Issue.11 , pp. 1537-1548
    • Qi, J.1    Gong, J.2    Zhao, T.3
  • 62
    • 84878695660 scopus 로고    scopus 로고
    • Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity
    • S1801-1804
    • Rubio T, Vernia S, Sanz P. Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity. Mol Biol Cell. 2013;24(11):1801-1811, S1801-1804.
    • (2013) Mol Biol Cell , vol.24 , Issue.11 , pp. 1801-1811
    • Rubio, T.1    Vernia, S.2    Sanz, P.3
  • 63
    • 84862778000 scopus 로고    scopus 로고
    • Cidea is an essential transcriptional coactivator regulating mammary gland secretion of milk lipids
    • Wang W, Lv N, Zhang S, et al. Cidea is an essential transcriptional coactivator regulating mammary gland secretion of milk lipids. Nat Med. 2012;18(2):235-243.
    • (2012) Nat Med , vol.18 , Issue.2 , pp. 235-243
    • Wang, W.1    Lv, N.2    Zhang, S.3
  • 64
    • 84860201914 scopus 로고    scopus 로고
    • CIDE proteins and lipid metabolism
    • Xu L, Zhou L, Li P. CIDE proteins and lipid metabolism. Arterioscler Thromb Vasc Biol. 2012;32(5):1094-1098.
    • (2012) Arterioscler Thromb Vasc Biol , vol.32 , Issue.5 , pp. 1094-1098
    • Xu, L.1    Zhou, L.2    Li, P.3
  • 65
    • 0041353552 scopus 로고    scopus 로고
    • Cidea-deficient mice have lean phenotype and are resistant to obesity
    • Zhou Z, Yon Toh S, Chen Z, et al. Cidea-deficient mice have lean phenotype and are resistant to obesity. Nat Genet. 2003;35(1): 49-56.
    • (2003) Nat Genet , vol.35 , Issue.1 , pp. 49-56
    • Zhou, Z.1    Yon Toh, S.2    Chen, Z.3
  • 66
    • 10744223839 scopus 로고    scopus 로고
    • CHIP activates HSF1 and confers protection against apoptosis and cellular stress
    • Dai Q, Zhang C, Wu Y, et al. CHIP activates HSF1 and confers protection against apoptosis and cellular stress. EMBO J. 2003; 22(20):5446-5458.
    • (2003) EMBO J , vol.22 , Issue.20 , pp. 5446-5458
    • Dai, Q.1    Zhang, C.2    Wu, Y.3
  • 67
    • 44949127204 scopus 로고    scopus 로고
    • CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control
    • Min JN, Whaley RA, Sharpless NE, Lockyer P, Portbury AL, Patterson C. CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control. Mol Cell Biol. 2008;28(12):4018-4025.
    • (2008) Mol Cell Biol , vol.28 , Issue.12 , pp. 4018-4025
    • Min, J.N.1    Whaley, R.A.2    Sharpless, N.E.3    Lockyer, P.4    Portbury, A.L.5    Patterson, C.6
  • 69
    • 84860407614 scopus 로고    scopus 로고
    • Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1
    • Gaude H, Aznar N, Delay A, et al. Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1. Oncogene. 2012;31(12):1582-1591.
    • (2012) Oncogene , vol.31 , Issue.12 , pp. 1582-1591
    • Gaude, H.1    Aznar, N.2    Delay, A.3
  • 71
    • 84902147210 scopus 로고    scopus 로고
    • Autosomal recessive cerebellar ataxia of adult onset due to STUB1 mutations
    • Depondt C, Donatello S, Simonis N, et al. Autosomal recessive cerebellar ataxia of adult onset due to STUB1 mutations. Neurology. 2014;82(19):1749-1750.
    • (2014) Neurology , vol.82 , Issue.19 , pp. 1749-1750
    • Depondt, C.1    Donatello, S.2    Simonis, N.3
  • 72
    • 84892971939 scopus 로고    scopus 로고
    • Ataxia and hypogonadism caused by the loss of ubiquitin ligase activity of the U box protein CHIP
    • Shi CH, Schisler JC, Rubel CE, et al. Ataxia and hypogonadism caused by the loss of ubiquitin ligase activity of the U box protein CHIP. Hum Mol Genet. 2014;23(4):1013-1024.
    • (2014) Hum Mol Genet , vol.23 , Issue.4 , pp. 1013-1024
    • Shi, C.H.1    Schisler, J.C.2    Rubel, C.E.3
  • 73
    • 84891602619 scopus 로고    scopus 로고
    • Identification of CHIP as a novel causative gene for autosomal recessive cerebellar ataxia
    • Shi Y, Wang J, Li JD, et al. Identification of CHIP as a novel causative gene for autosomal recessive cerebellar ataxia. PLoS One. 2013;8(12):e81884.
    • (2013) PLoS One , vol.8 , Issue.12
    • Shi, Y.1    Wang, J.2    Li, J.D.3
  • 74
    • 84892750162 scopus 로고    scopus 로고
    • PNPLA6 mutations cause Boucher-Neuhauser and Gordon Holmes syndromes as part of a broad neurodegenerative spectrum
    • Synofzik M, Gonzalez MA, Lourenco CM, et al. PNPLA6 mutations cause Boucher-Neuhauser and Gordon Holmes syndromes as part of a broad neurodegenerative spectrum. Brain. 2014; 137(pt 1):69-77.
    • (2014) Brain , vol.137 , pp. 69-77
    • Synofzik, M.1    Gonzalez, M.A.2    Lourenco, C.M.3
  • 75
    • 68949107216 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) molecular crossroad for metabolic control and survival of neurons
    • Spasic MR, Callaerts P, Norga KK. AMP-activated protein kinase (AMPK) molecular crossroad for metabolic control and survival of neurons. Neuroscientist. 2009;15(4):309-316.
    • (2009) Neuroscientist , vol.15 , Issue.4 , pp. 309-316
    • Spasic, M.R.1    Callaerts, P.2    Norga, K.K.3
  • 77
    • 0242268533 scopus 로고    scopus 로고
    • Insulin signaling in microdomains of the plasma membrane
    • Saltiel AR, Pessin JE. Insulin signaling in microdomains of the plasma membrane. Traffic. 2003;4(11):711-716.
    • (2003) Traffic , vol.4 , Issue.11 , pp. 711-716
    • Saltiel, A.R.1    Pessin, J.E.2
  • 78
    • 85047692840 scopus 로고    scopus 로고
    • C-Cbl-deficient mice havereduced adiposity, higher energy expenditure, and improved peripheral insulin action
    • Molero JC, Jensen TE, Withers PC, et al. c-Cbl-deficient mice havereduced adiposity, higher energy expenditure, and improved peripheral insulin action. J Clin Invest. 2004;114(9):1326-1333.
    • (2004) J Clin Invest , vol.114 , Issue.9 , pp. 1326-1333
    • Molero, J.C.1    Jensen, T.E.2    Withers, P.C.3
  • 79
    • 33845534390 scopus 로고    scopus 로고
    • Genetic ablation of the c-Cbl ubiquitin ligase domain results in increased energy expenditure and improved insulin action
    • Molero JC, Turner N, Thien CB, Langdon WY, James DE, Cooney GJ. Genetic ablation of the c-Cbl ubiquitin ligase domain results in increased energy expenditure and improved insulin action. Diabetes. 2006;55(12):3411-3417.
    • (2006) Diabetes , vol.55 , Issue.12 , pp. 3411-3417
    • Molero, J.C.1    Turner, N.2    Thien, C.B.3    Langdon, W.Y.4    James, D.E.5    Cooney, G.J.6
  • 80
    • 77949350034 scopus 로고    scopus 로고
    • Identification of a primary target of thalidomide teratogenicity
    • Ito T, Ando H, Suzuki T, et al. Identification of a primary target of thalidomide teratogenicity. Science. 2010;327(5971):1345-1350.
    • (2010) Science , vol.327 , Issue.5971 , pp. 1345-1350
    • Ito, T.1    Ando, H.2    Suzuki, T.3
  • 81
    • 79551581810 scopus 로고    scopus 로고
    • Functional modulation of AMP-activated protein kinase by cereblon
    • Lee KM, Jo S, Kim H, Lee J, Park CS. Functional modulation of AMP-activated protein kinase by cereblon. Biochim Biophys Acta. 2011;1813(3):448-455.
    • (2011) Biochim Biophys Acta , vol.1813 , Issue.3 , pp. 448-455
    • Lee, K.M.1    Jo, S.2    Kim, H.3    Lee, J.4    Park, C.S.5
  • 82
    • 33748570421 scopus 로고    scopus 로고
    • Novel RING E3 ubiquitin ligases in breast cancer
    • Burger A, Amemiya Y, Kitching R, Seth AK. Novel RING E3 ubiquitin ligases in breast cancer. Neoplasia. 2006;8(8):689-695.
    • (2006) Neoplasia , vol.8 , Issue.8 , pp. 689-695
    • Burger, A.1    Amemiya, Y.2    Kitching, R.3    Seth, A.K.4
  • 83
    • 84891601317 scopus 로고    scopus 로고
    • Regulation of metformin response by breast cancer associated gene 2
    • Buac D, Kona FR, Seth AK, Dou QP. Regulation of metformin response by breast cancer associated gene 2. Neoplasia. 2013; 15(12):1379-1390.
    • (2013) Neoplasia , vol.15 , Issue.12 , pp. 1379-1390
    • Buac, D.1    Kona, F.R.2    Seth, A.K.3    Dou, Q.P.4
  • 84
    • 42449090346 scopus 로고    scopus 로고
    • Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains
    • Al-Hakim AK, Zagorska A, Chapman L, Deak M, Peggie M, Alessi DR. Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains. Biochem J. 2008;411(2):249-260.
    • (2008) Biochem J , vol.411 , Issue.2 , pp. 249-260
    • Al-Hakim, A.K.1    Zagorska, A.2    Chapman, L.3    Deak, M.4    Peggie, M.5    Alessi, D.R.6
  • 85
    • 84866716158 scopus 로고    scopus 로고
    • APC/C(Cdh1) targets brain-specific kinase 2 (BRSK2) for degradation via the ubiquitin-proteasome pathway
    • Li R, Wan B, Zhou J, et al. APC/C(Cdh1) targets brain-specific kinase 2 (BRSK2) for degradation via the ubiquitin-proteasome pathway. PLoS One. 2012;7(9):e45932.
    • (2012) PLoS One , vol.7 , Issue.9
    • Li, R.1    Wan, B.2    Zhou, J.3
  • 86
    • 84862298972 scopus 로고    scopus 로고
    • Jab1 interacts with brain-specific kinase 2 (BRSK2) and promotes its degradation in the ubiquitinproteasome pathway
    • Zhou J, Wan B, Li R, et al. Jab1 interacts with brain-specific kinase 2 (BRSK2) and promotes its degradation in the ubiquitinproteasome pathway. Biochem Biophys Res Commun. 2012; 422(4):647-652.
    • (2012) Biochem Biophys Res Commun , vol.422 , Issue.4 , pp. 647-652
    • Zhou, J.1    Wan, B.2    Li, R.3
  • 87
    • 0031807249 scopus 로고    scopus 로고
    • Atrophin-1, the DRPLA gene product, interacts with two families ofWWdomain-containing proteins
    • Wood JD, Yuan J, Margolis RL, et al. Atrophin-1, the DRPLA gene product, interacts with two families ofWWdomain-containing proteins. Mol Cell Neurosci. 1998;11(3):149-160.
    • (1998) Mol Cell Neurosci , vol.11 , Issue.3 , pp. 149-160
    • Wood, J.D.1    Yuan, J.2    Margolis, R.L.3
  • 88
    • 84885094614 scopus 로고    scopus 로고
    • The ATP costs and time required to degrade ubiquitinated proteins by the 26 S proteasome
    • Peth A, Nathan JA, Goldberg AL. The ATP costs and time required to degrade ubiquitinated proteins by the 26 S proteasome. J Biol Chem. 2013;288(40):29215-29222.
    • (2013) J Biol Chem , vol.288 , Issue.40 , pp. 29215-29222
    • Peth, A.1    Nathan, J.A.2    Goldberg, A.L.3
  • 89
    • 78650100616 scopus 로고    scopus 로고
    • Ubiquitin: Same molecule, different degradation pathways
    • Clague MJ, Urbé S. Ubiquitin: same molecule, different degradation pathways. Cell. 2010;143(5):682-685.
    • (2010) Cell , vol.143 , Issue.5 , pp. 682-685
    • Clague, M.J.1    Urbé, S.2
  • 90
    • 38449110592 scopus 로고    scopus 로고
    • SNF1/AMPK pathways in yeast
    • Hedbacker K, Carlson M. SNF1/AMPK pathways in yeast. Front Biosci. 2008;13:2408-2420.
    • (2008) Front Biosci , vol.13 , pp. 2408-2420
    • Hedbacker, K.1    Carlson, M.2
  • 91
    • 79960326517 scopus 로고    scopus 로고
    • Ubp8 and SAGA regulate Snf1 AMP kinase activity
    • Wilson MA, Koutelou E, Hirsch C, et al. Ubp8 and SAGA regulate Snf1 AMP kinase activity. Mol Cell Biol. 2011;31(15):3126-3135.
    • (2011) Mol Cell Biol , vol.31 , Issue.15 , pp. 3126-3135
    • Wilson, M.A.1    Koutelou, E.2    Hirsch, C.3
  • 92
    • 30544437191 scopus 로고    scopus 로고
    • 14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK
    • Al-Hakim AK, Goransson O, Deak M, et al. 14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK. J Cell Sci. 2005;118(pt 23):5661-5673.
    • (2005) J Cell Sci , vol.118 , pp. 5661-5673
    • Al-Hakim, A.K.1    Goransson, O.2    Deak, M.3
  • 93
    • 84886409705 scopus 로고    scopus 로고
    • SUMOylation regulates the SNF1 protein kinase
    • Simpson-Lavy KJ, Johnston M. SUMOylation regulates the SNF1 protein kinase. Proc Natl Acad Sci USA. 2013;110(43):17432-17437.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.43 , pp. 17432-17437
    • Simpson-Lavy, K.J.1    Johnston, M.2
  • 94
    • 36348977099 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolytic control of SUMO conjugates
    • Uzunova K, Göttsche K, Miteva M, et al. Ubiquitin-dependent proteolytic control of SUMO conjugates. J Biol Chem. 2007; 282(47):34167-34175.
    • (2007) J Biol Chem , vol.282 , Issue.47 , pp. 34167-34175
    • Uzunova, K.1    Göttsche, K.2    Miteva, M.3
  • 95
    • 68049129864 scopus 로고    scopus 로고
    • In vivo activation of AMP-activated protein kinase attenuates diabetes-enhanced degradation of GTP cyclohydrolase I
    • Wang S, Xu J, Song P, Viollet B, Zou MH. In vivo activation of AMP-activated protein kinase attenuates diabetes-enhanced degradation of GTP cyclohydrolase I. Diabetes. 2009;58(8):1893-1901.
    • (2009) Diabetes , vol.58 , Issue.8 , pp. 1893-1901
    • Wang, S.1    Xu, J.2    Song, P.3    Viollet, B.4    Zou, M.H.5
  • 96
    • 41249091730 scopus 로고    scopus 로고
    • Role of AMP-activated protein kinase in autophagy and proteasome function
    • Viana R, Aguado C, Esteban I, et al. Role of AMP-activated protein kinase in autophagy and proteasome function. Biochem Biophys Res Commun. 2008;369(3):964-968.
    • (2008) Biochem Biophys Res Commun , vol.369 , Issue.3 , pp. 964-968
    • Viana, R.1    Aguado, C.2    Esteban, I.3
  • 97
    • 77950989801 scopus 로고    scopus 로고
    • AMPKα2 deletion causes aberrant expression and activation of NAD(P)H oxidase and consequent endothelial dysfunction in vivo: Role of 26S proteasomes
    • Wang S, Zhang M, Liang B, et al. AMPKα2 deletion causes aberrant expression and activation of NAD(P)H oxidase and consequent endothelial dysfunction in vivo: role of 26S proteasomes. Circ Res. 2010;106(6):1117-1128.
    • (2010) Circ Res , vol.106 , Issue.6 , pp. 1117-1128
    • Wang, S.1    Zhang, M.2    Liang, B.3
  • 98
    • 84860501679 scopus 로고    scopus 로고
    • Regulation of the proteasome by AMPK in endothelial cells: The role of O-GlcNAc transferase (OGT)
    • Xu J, Wang S, Viollet B, Zou MH. Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT). PLoS One. 2012;7(5):e36717.
    • (2012) PLoS One , vol.7 , Issue.5
    • Xu, J.1    Wang, S.2    Viollet, B.3    Zou, M.H.4
  • 99
    • 70350347981 scopus 로고    scopus 로고
    • Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
    • Moreno D, Viana R, Sanz P. Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase. Int J Biochem Cell Biol. 2009;41(12):2431-2439.
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.12 , pp. 2431-2439
    • Moreno, D.1    Viana, R.2    Sanz, P.3
  • 100
    • 81355160428 scopus 로고    scopus 로고
    • AMPKα2 deletion exacerbates neointima formation by upregulating Skp2 in vascular smooth muscle cells
    • Song P, Wang S, He C, Liang B, Viollet B, Zou MH. AMPKα2 deletion exacerbates neointima formation by upregulating Skp2 in vascular smooth muscle cells. Circ Res. 2011;109(11):1230-1239.
    • (2011) Circ Res , vol.109 , Issue.11 , pp. 1230-1239
    • Song, P.1    Wang, S.2    He, C.3    Liang, B.4    Viollet, B.5    Zou, M.H.6
  • 101
    • 84888197890 scopus 로고    scopus 로고
    • Adenosine monophosphateactivated protein kinase-α2 deficiency promotes vascular smooth muscle cell migration via S-phase kinase-associated protein 2 upregulation and E-cadherin downregulation
    • Song P, Zhou Y, Coughlan KA, et al. Adenosine monophosphateactivated protein kinase-α2 deficiency promotes vascular smooth muscle cell migration via S-phase kinase-associated protein 2 upregulation and E-cadherin downregulation. Arterioscler Thromb Vasc Biol. 2013;33(12):2800-2809.
    • (2013) Arterioscler Thromb Vasc Biol , vol.33 , Issue.12 , pp. 2800-2809
    • Song, P.1    Zhou, Y.2    Coughlan, K.A.3
  • 102
    • 0028179669 scopus 로고
    • p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-β and contact inhibition to cell cycle arrest
    • Polyak K, Kato JY, Solomon MJ, et al. p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-β and contact inhibition to cell cycle arrest. Genes Dev. 1994;8(1):9-22.
    • (1994) Genes Dev , vol.8 , Issue.1 , pp. 9-22
    • Polyak, K.1    Kato, J.Y.2    Solomon, M.J.3
  • 103
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano AC, Eytan E, Hershko A, Pagano M. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat Cell Biol. 1999;1(4):193-199.
    • (1999) Nat Cell Biol , vol.1 , Issue.4 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 104
    • 77953035951 scopus 로고    scopus 로고
    • AMPK-mediated phosphorylation of murine p27 at T197 promotes binding of 14-3-3 proteins and increases p27 stability
    • Short JD, Dere R, Houston KD, et al. AMPK-mediated phosphorylation of murine p27 at T197 promotes binding of 14-3-3 proteins and increases p27 stability. Mol Carcinog. 2010;49(5):429-439.
    • (2010) Mol Carcinog , vol.49 , Issue.5 , pp. 429-439
    • Short, J.D.1    Dere, R.2    Houston, K.D.3
  • 105
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine SC, Latres E, Baumhueter S, et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science. 2001; 294(5547):1704-1708.
    • (2001) Science , vol.294 , Issue.5547 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3
  • 106
    • 11244260636 scopus 로고    scopus 로고
    • Muscle ring finger protein-1 inhibits PKC[Î] activation and prevents cardiomyocyte hypertrophy
    • Arya R, Kedar V, Hwang JR, et al. Muscle ring finger protein-1 inhibits PKC[Î] activation and prevents cardiomyocyte hypertrophy. J Cell Biol. 2004;167(6):1147-1159.
    • (2004) J Cell Biol , vol.167 , Issue.6 , pp. 1147-1159
    • Arya, R.1    Kedar, V.2    Hwang, J.R.3
  • 107
    • 9644270401 scopus 로고    scopus 로고
    • Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex
    • Li HH, Kedar V, Zhang C, et al. Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex. J Clin Invest. 2004;114(8): 1058-1071.
    • (2004) J Clin Invest , vol.114 , Issue.8 , pp. 1058-1071
    • Li, H.H.1    Kedar, V.2    Zhang, C.3
  • 108
    • 33947522846 scopus 로고    scopus 로고
    • Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo
    • Willis MS, Ike C, Li L, Wang DZ, Glass DJ, Patterson C. Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo. Circ Res. 2007;100(4):456-459.
    • (2007) Circ Res , vol.100 , Issue.4 , pp. 456-459
    • Willis, M.S.1    Ike, C.2    Li, L.3    Wang, D.Z.4    Glass, D.J.5    Patterson, C.6
  • 109
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes MD, Lecker SH, Jagoe RT, Navon A, Goldberg AL. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc Natl Acad Sci USA. 2001;98(25): 14440-14445.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.25 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 110
    • 34249703500 scopus 로고    scopus 로고
    • AMPactivated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells
    • Krawiec BJ, Nystrom GJ, Frost RA, Jefferson LS, Lang CH. AMPactivated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells. Am J Physiol Endocrinol Metab. 2007;292(6):E1555-E1567.
    • (2007) Am J Physiol Endocrinol Metab , vol.292 , Issue.6 , pp. E1555-E1567
    • Krawiec, B.J.1    Nystrom, G.J.2    Frost, R.A.3    Jefferson, L.S.4    Lang, C.H.5
  • 111
    • 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, Yakabe Y. AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes. Biosci Biotechnol Biochem. 2007;71(7):1650-1656.
    • (2007) Biosci Biotechnol Biochem , vol.71 , Issue.7 , pp. 1650-1656
    • Nakashima, K.1    Yakabe, Y.2
  • 112
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • Sandri M, Sandri C, Gilbert A, et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell. 2004;117(3):399-412.
    • (2004) Cell , vol.117 , Issue.3 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3
  • 113
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • Stitt TN, Drujan D, Clarke BA, et al. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell. 2004; 14(3):395-403.
    • (2004) Mol Cell , vol.14 , Issue.3 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3
  • 114
    • 66049138419 scopus 로고    scopus 로고
    • Rosiglitazone-induced heart remodelling is associated with enhanced turnover of myofibrillar protein and mTOR activation
    • Festuccia WT, Laplante M, Brûlé S, et al. Rosiglitazone-induced heart remodelling is associated with enhanced turnover of myofibrillar protein and mTOR activation. J Mol Cell Cardiol. 2009; 47(1):85-95.
    • (2009) J Mol Cell Cardiol , vol.47 , Issue.1 , pp. 85-95
    • Festuccia, W.T.1    Laplante, M.2    Brûlé, S.3
  • 115
    • 68049100485 scopus 로고    scopus 로고
    • Sepsis and AMPK activation by AICAR differentially regulate FoxO-1, -3 and -4 mRNA in striated muscle
    • Nystrom GJ, Lang CH. Sepsis and AMPK activation by AICAR differentially regulate FoxO-1, -3 and -4 mRNA in striated muscle. Int J Clin Exp Med. 2008;1(1):50-63.
    • (2008) Int J Clin Exp Med , vol.1 , Issue.1 , pp. 50-63
    • Nystrom, G.J.1    Lang, C.H.2
  • 116
    • 80053519193 scopus 로고    scopus 로고
    • Angiotensin II upregulates protein phosphatase 2Cα and inhibits AMP-activated protein kinase signaling and energy balance leading to skeletal muscle wasting
    • Tabony AM, Yoshida T, Galvez S, et al. Angiotensin II upregulates protein phosphatase 2Cα and inhibits AMP-activated protein kinase signaling and energy balance leading to skeletal muscle wasting. Hypertension. 2011;58(4):643-649.
    • (2011) Hypertension , vol.58 , Issue.4 , pp. 643-649
    • Tabony, A.M.1    Yoshida, T.2    Galvez, S.3
  • 117
    • 34848861463 scopus 로고    scopus 로고
    • The energy sensor AMPactivated protein kinase directly regulates the mammalian FOXO3 transcription factor
    • Greer EL, Oskoui PR, Banko MR, et al. The energy sensor AMPactivated protein kinase directly regulates the mammalian FOXO3 transcription factor. J Biol Chem. 2007;282(41):30107-30119.
    • (2007) J Biol Chem , vol.282 , Issue.41 , pp. 30107-30119
    • Greer, E.L.1    Oskoui, P.R.2    Banko, M.R.3
  • 118
    • 70349253984 scopus 로고    scopus 로고
    • AMP-activated protein kinase enhances the expression of muscle-specific ubiquitin ligases despite its activation of IGF-1/Akt signaling in C2C12 myotubes
    • Tong JF, Yan X, Zhu MJ, Du M. AMP-activated protein kinase enhances the expression of muscle-specific ubiquitin ligases despite its activation of IGF-1/Akt signaling in C2C12 myotubes. J Cell Biochem. 2009;108(2):458-468.
    • (2009) J Cell Biochem , vol.108 , Issue.2 , pp. 458-468
    • Tong, J.F.1    Yan, X.2    Zhu, M.J.3    Du, M.4
  • 119
    • 80255131441 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates E3 ligases in rodent heart
    • Baskin KK, Taegtmeyer H. AMP-activated protein kinase regulates E3 ligases in rodent heart. Circ Res. 2011;109(10):1153-1161.
    • (2011) Circ Res , vol.109 , Issue.10 , pp. 1153-1161
    • Baskin, K.K.1    Taegtmeyer, H.2
  • 120
    • 17344362307 scopus 로고    scopus 로고
    • Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy
    • Minassian BA, Lee JR, Herbrick JA, et al. Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat Genet. 1998;20(2):171-174.
    • (1998) Nat Genet , vol.20 , Issue.2 , pp. 171-174
    • Minassian, B.A.1    Lee, J.R.2    Herbrick, J.A.3
  • 121
    • 0141618459 scopus 로고    scopus 로고
    • Mutations in NHLRC1 cause progressive myoclonus epilepsy
    • Chan EM, Young EJ, Ianzano L, et al. Mutations in NHLRC1 cause progressive myoclonus epilepsy. Nat Genet. 2003;35(2): 125-127.
    • (2003) Nat Genet , vol.35 , Issue.2 , pp. 125-127
    • Chan, E.M.1    Young, E.J.2    Ianzano, L.3
  • 123
    • 17644444332 scopus 로고    scopus 로고
    • Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation
    • Fernández-Sánchez ME, Criado-García O, Heath KE, et al. Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. Hum Mol Genet. 2003;12(23): 3161-3171.
    • (2003) Hum Mol Genet , vol.12 , Issue.23 , pp. 3161-3171
    • Fernández-Sánchez, M.E.1    Criado-García, O.2    Heath, K.E.3
  • 124
    • 37649004558 scopus 로고    scopus 로고
    • Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo
    • Tagliabracci VS, Turnbull J, Wang W, et al. Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. Proc Natl Acad Sci USA. 2007;104(49): 19262-19266.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.49 , pp. 19262-19266
    • Tagliabracci, V.S.1    Turnbull, J.2    Wang, W.3
  • 125
    • 0037169553 scopus 로고    scopus 로고
    • A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen
    • Wang J, Stuckey JA, Wishart MJ, Dixon JE. A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen. J Biol Chem. 2002;277(4):2377-2380.
    • (2002) J Biol Chem , vol.277 , Issue.4 , pp. 2377-2380
    • Wang, J.1    Stuckey, J.A.2    Wishart, M.J.3    Dixon, J.E.4
  • 126
    • 80052065377 scopus 로고    scopus 로고
    • Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase
    • Romá-Mateo C, Solaz-Fuster Mdel C, Gimeno-Alcañiz JV, et al. Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase. Biochem J. 2011;439(2):265-275.
    • (2011) Biochem J , vol.439 , Issue.2 , pp. 265-275
    • Romá-Mateo, C.1    Solaz-Fuster Mdel, C.2    Gimeno-Alcañiz, J.V.3
  • 127
    • 39749136257 scopus 로고    scopus 로고
    • Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway
    • Solaz-Fuster MC, Gimeno-Alcañiz JV, Ros S, et al. Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway. Hum Mol Genet. 2008;17(5):667-678.
    • (2008) Hum Mol Genet , vol.17 , Issue.5 , pp. 667-678
    • Solaz-Fuster, M.C.1    Gimeno-Alcañiz, J.V.2    Ros, S.3
  • 128
    • 42949086604 scopus 로고    scopus 로고
    • Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)
    • Worby CA, Gentry MS, Dixon JE. Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG). J Biol Chem. 2008;283(7):4069-4076.
    • (2008) J Biol Chem , vol.283 , Issue.7 , pp. 4069-4076
    • Worby, C.A.1    Gentry, M.S.2    Dixon, J.E.3
  • 129
    • 67649760225 scopus 로고    scopus 로고
    • AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex
    • Vernia S, Solaz-Fuster MC, Gimeno-Alcañiz JV, et al. AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex. J Biol Chem. 2009;284(13):8247-8255.
    • (2009) J Biol Chem , vol.284 , Issue.13 , pp. 8247-8255
    • Vernia, S.1    Solaz-Fuster, M.C.2    Gimeno-Alcañiz, J.V.3
  • 130
    • 77955098709 scopus 로고    scopus 로고
    • The laforinmalin complex, involved in Lafora disease, promotes the incorporation of K63-linked ubiquitin chains into AMP-activated protein kinase β subunits
    • Moreno D, Towler MC, Hardie DG, Knecht E, Sanz P. The laforinmalin complex, involved in Lafora disease, promotes the incorporation of K63-linked ubiquitin chains into AMP-activated protein kinase β subunits. Mol Biol Cell. 2010;21(15):2578-2588.
    • (2010) Mol Biol Cell , vol.21 , Issue.15 , pp. 2578-2588
    • Moreno, D.1    Towler, M.C.2    Hardie, D.G.3    Knecht, E.4    Sanz, P.5
  • 131
    • 79960657101 scopus 로고    scopus 로고
    • Lafora disease E3- ubiquitin ligase malin is related to TRIM32 at both the phylogenetic and functional level
    • Roma-Mateo C, Moreno D, Vernia S, et al. Lafora disease E3- ubiquitin ligase malin is related to TRIM32 at both the phylogenetic and functional level. BMC Evol Biol. 2011;11:225.
    • (2011) BMC Evol Biol , vol.11
    • Roma-Mateo, C.1    Moreno, D.2    Vernia, S.3
  • 132
    • 84866417635 scopus 로고    scopus 로고
    • Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy
    • Cohen S, Zhai B, Gygi SP, Goldberg AL. Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy. J Cell Biol. 2012;198(4):575-589.
    • (2012) J Cell Biol , vol.198 , Issue.4 , pp. 575-589
    • Cohen, S.1    Zhai, B.2    Gygi, S.P.3    Goldberg, A.L.4
  • 133
    • 20844463813 scopus 로고    scopus 로고
    • Insights into Lafora disease: Malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin
    • Gentry MS, Worby CA, Dixon JE. Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc Natl Acad Sci USA. 2005;102(24): 8501-8506.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.24 , pp. 8501-8506
    • Gentry, M.S.1    Worby, C.A.2    Dixon, J.E.3
  • 134
    • 84863011221 scopus 로고    scopus 로고
    • The laforin-malin complex negatively regulates glycogen synthesis by modulating cellular glucose uptake via glucose transporters
    • Singh PK, Singh S, Ganesh S. The laforin-malin complex negatively regulates glycogen synthesis by modulating cellular glucose uptake via glucose transporters. Mol Cell Biol. 2012;32(3):652-663.
    • (2012) Mol Cell Biol , vol.32 , Issue.3 , pp. 652-663
    • Singh, P.K.1    Singh, S.2    Ganesh, S.3
  • 135
    • 67649865826 scopus 로고    scopus 로고
    • AMPK controls epithelial Na(+) channels through Nedd4-2 and causes an epithelial phenotype when mutated
    • Almaça J, Kongsuphol P, Hieke B, et al. AMPK controls epithelial Na(+) channels through Nedd4-2 and causes an epithelial phenotype when mutated. Pflugers Arch. 2009;458(4):713-721.
    • (2009) Pflugers Arch , vol.458 , Issue.4 , pp. 713-721
    • Almaça, J.1    Kongsuphol, P.2    Hieke, B.3
  • 136
    • 33748750919 scopus 로고    scopus 로고
    • AMP-activated kinase inhibits the epithelial Na+ channel through functional regulation of the ubiquitin ligase Nedd4-2
    • Bhalla V, Oyster NM, Fitch AC, et al. AMP-activated kinase inhibits the epithelial Na+ channel through functional regulation of the ubiquitin ligase Nedd4-2. J Biol Chem. 2006;281(36):26159-26169.
    • (2006) J Biol Chem , vol.281 , Issue.36 , pp. 26159-26169
    • Bhalla, V.1    Oyster, N.M.2    Fitch, A.C.3
  • 137
    • 23744492591 scopus 로고    scopus 로고
    • Epithelial sodium channel inhibition by AMP-activated protein kinase in oocytes and polarized renal epithelial cells
    • Carattino MD, Edinger RS, Grieser HJ, et al. Epithelial sodium channel inhibition by AMP-activated protein kinase in oocytes and polarized renal epithelial cells. J Biol Chem. 2005;280(18): 17608-17616.
    • (2005) J Biol Chem , vol.280 , Issue.18 , pp. 17608-17616
    • Carattino, M.D.1    Edinger, R.S.2    Grieser, H.J.3
  • 138
    • 77953105547 scopus 로고    scopus 로고
    • Down-regulation of Na+ -coupled glutamate transporter EAAT3 and EAAT4 by AMP-activated protein kinase
    • Sopjani M, Alesutan I, Dërmaku-Sopjani M, et al. Down-regulation of Na+ -coupled glutamate transporter EAAT3 and EAAT4 by AMP-activated protein kinase. J Neurochem. 2010;113(6): 1426-1435.
    • (2010) J Neurochem , vol.113 , Issue.6 , pp. 1426-1435
    • Sopjani, M.1    Alesutan, I.2    Dërmaku-Sopjani, M.3
  • 139
    • 79251545532 scopus 로고    scopus 로고
    • Inhibition of the heterotetrameric K+ channel KCNQ1/KCNE1 by the AMP-activated protein kinase
    • Alesutan I, Föller M, Sopjani M, et al. Inhibition of the heterotetrameric K+ channel KCNQ1/KCNE1 by the AMP-activated protein kinase. Mol Membr Biol. 2011;28(2):79-89.
    • (2011) Mol Membr Biol , vol.28 , Issue.2 , pp. 79-89
    • Alesutan, I.1    Föller, M.2    Sopjani, M.3
  • 140
    • 79956193992 scopus 로고    scopus 로고
    • Inhibition of Kir2.1 (KCNJ2) by the AMP-activated protein kinase
    • Alesutan I, Munoz C, Sopjani M, et al. Inhibition of Kir2.1 (KCNJ2) by the AMP-activated protein kinase. Biochem Biophys Res Commun. 2011;408(4):505-510.
    • (2011) Biochem Biophys Res Commun , vol.408 , Issue.4 , pp. 505-510
    • Alesutan, I.1    Munoz, C.2    Sopjani, M.3
  • 141
    • 78649979349 scopus 로고    scopus 로고
    • AMP-activated protein kinase inhibits KCNQ1 channels through regulation of the ubiquitin ligase Nedd4-2 in renal epithelial cells
    • Alzamora R, Gong F, Rondanino C, et al. AMP-activated protein kinase inhibits KCNQ1 channels through regulation of the ubiquitin ligase Nedd4-2 in renal epithelial cells. Am J Physiol Renal Physiol. 2010;299(6):F1308-F1319.
    • (2010) Am J Physiol Renal Physiol , vol.299 , Issue.6 , pp. F1308-F1319
    • Alzamora, R.1    Gong, F.2    Rondanino, C.3
  • 142
  • 143
    • 84870368355 scopus 로고    scopus 로고
    • Downregulation of Kv1.5 K channels by the AMP-activated protein kinase
    • Mia S, Munoz C, Pakladok T, et al. Downregulation of Kv1.5 K channels by the AMP-activated protein kinase. Cell Physiol Biochem. 2012;30(4):1039-1050.
    • (2012) Cell Physiol Biochem , vol.30 , Issue.4 , pp. 1039-1050
    • Mia, S.1    Munoz, C.2    Pakladok, T.3
  • 144
    • 84866753209 scopus 로고    scopus 로고
    • Regulation of Orai1/STIM1 by the kinases SGK1 and AMPK
    • Lang F, Eylenstein A, Shumilina E. Regulation of Orai1/STIM1 by the kinases SGK1 and AMPK. Cell Calcium. 2012;52(5):347-354.
    • (2012) Cell Calcium , vol.52 , Issue.5 , pp. 347-354
    • Lang, F.1    Eylenstein, A.2    Shumilina, E.3
  • 145
    • 67650046374 scopus 로고    scopus 로고
    • AMP-activated protein kinase phosphorylation of the R domain inhibits PKA stimulation of CFTR
    • King JD Jr, Fitch AC, Lee JK, et al. AMP-activated protein kinase phosphorylation of the R domain inhibits PKA stimulation of CFTR. Am J Physiol Cell Physiol. 2009;297(1):C94-C101.
    • (2009) Am J Physiol Cell Physiol , vol.297 , Issue.1 , pp. C94-C101
    • King, J.D.1    Fitch, A.C.2    Lee, J.K.3
  • 146
    • 65549152318 scopus 로고    scopus 로고
    • Mechanistic insight into control of CFTR by AMPK
    • Kongsuphol P, Cassidy D, Hieke B, et al. Mechanistic insight into control of CFTR by AMPK. J Biol Chem. 2009;284(9):5645-5653.
    • (2009) J Biol Chem , vol.284 , Issue.9 , pp. 5645-5653
    • Kongsuphol, P.1    Cassidy, D.2    Hieke, B.3
  • 147
    • 60949109291 scopus 로고    scopus 로고
    • Inhibition of the KCa3.1 channels by AMP-activated protein kinase in human airway epithelial cells
    • Klein H, Garneau L, Trinh NT, et al. Inhibition of the KCa3.1 channels by AMP-activated protein kinase in human airway epithelial cells. Am J Physiol Cell Physiol. 2009;296(2):C285-C295.
    • (2009) Am J Physiol Cell Physiol , vol.296 , Issue.2 , pp. C285-C295
    • Klein, H.1    Garneau, L.2    Trinh, N.T.3
  • 148
    • 34247178517 scopus 로고    scopus 로고
    • AMP-activated protein kinase mediates carotid body excitation by hypoxia
    • Wyatt CN, Mustard KJ, Pearson SA, et al. AMP-activated protein kinase mediates carotid body excitation by hypoxia. J Biol Chem. 2007;282(11):8092-8098.
    • (2007) J Biol Chem , vol.282 , Issue.11 , pp. 8092-8098
    • Wyatt, C.N.1    Mustard, K.J.2    Pearson, S.A.3
  • 149
    • 77950195325 scopus 로고    scopus 로고
    • Regulation of Na+ -coupled glucose carrier SGLT1 by AMP-activated protein kinase
    • Sopjani M, Bhavsar SK, Fraser S, Kemp BE, Foller M, Lang F. Regulation of Na+ -coupled glucose carrier SGLT1 by AMP-activated protein kinase. Mol Membr Biol. 2010;27(2-3):137-144.
    • (2010) Mol Membr Biol , vol.27 , Issue.2-3 , pp. 137-144
    • Sopjani, M.1    Bhavsar, S.K.2    Fraser, S.3    Kemp, B.E.4    Foller, M.5    Lang, F.6
  • 151
    • 84901396281 scopus 로고    scopus 로고
    • Regulation of ion channels and transporters by AMPactivated kinase (AMPK)
    • Lang F, Foller M. Regulation of ion channels and transporters by AMPactivated kinase (AMPK). Channels (Austin). 2014;8(1):20-28.
    • (2014) Channels (Austin) , vol.8 , Issue.1 , pp. 20-28
    • Lang, F.1    Foller, M.2
  • 152
    • 79951702955 scopus 로고    scopus 로고
    • Bortezomib as the first proteasome inhibitor anticancer drug: Current status and future perspectives
    • Chen D, Frezza M, Schmitt S, Kanwar J, Dou QP. Bortezomib as the first proteasome inhibitor anticancer drug: current status and future perspectives. Curr Cancer Drug Targets. 2011;11(3):239-253.
    • (2011) Curr Cancer Drug Targets , vol.11 , Issue.3 , pp. 239-253
    • Chen, D.1    Frezza, M.2    Schmitt, S.3    Kanwar, J.4    Dou, Q.P.5
  • 153
    • 79959508832 scopus 로고    scopus 로고
    • Curcumin improves insulin resistance in skeletal muscle of rats
    • Na LX, Zhang YL, Li Y, et al. Curcumin improves insulin resistance in skeletal muscle of rats. Nutr Metab Cardiovasc Dis. 2011; 21(7):526-533.
    • (2011) Nutr Metab Cardiovasc Dis , vol.21 , Issue.7 , pp. 526-533
    • Na, L.X.1    Zhang, Y.L.2    Li, Y.3
  • 154
    • 84855503887 scopus 로고    scopus 로고
    • Curcumin prevents high fat diet induced insulin resistance and obesity via attenuating lipogenesis in liver and inflammatory pathway in adipocytes
    • Shao W, Yu Z, Chiang Y, et al. Curcumin prevents high fat diet induced insulin resistance and obesity via attenuating lipogenesis in liver and inflammatory pathway in adipocytes. PLoS One. 2012;7(1):e28784.
    • (2012) PLoS One , vol.7 , Issue.1
    • Shao, W.1    Yu, Z.2    Chiang, Y.3
  • 155
    • 46349088791 scopus 로고    scopus 로고
    • Dietary curcumin significantly improves obesity-associated inflammation and diabetes in mouse models of diabesity
    • Weisberg SP, Leibel R, Tortoriello DV. Dietary curcumin significantly improves obesity-associated inflammation and diabetes in mouse models of diabesity. Endocrinology. 2008;149(7):3549-3558.
    • (2008) Endocrinology , vol.149 , Issue.7 , pp. 3549-3558
    • Weisberg, S.P.1    Leibel, R.2    Tortoriello, D.V.3
  • 157
    • 13344285343 scopus 로고    scopus 로고
    • Mammalian AMP-activated protein kinase subfamily
    • Stapleton D, Mitchelhill KI, Gao G, et al. Mammalian AMP-activated protein kinase subfamily. J Biol Chem. 1996;271(2):611-614.
    • (1996) J Biol Chem , vol.271 , Issue.2 , pp. 611-614
    • Stapleton, D.1    Mitchelhill, K.I.2    Gao, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.