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Volumn 48, Issue 7, 2016, Pages

Regulation and function of AMPK in physiology and diseases

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE;

EID: 84990918092     PISSN: 12263613     EISSN: 20926413     Source Type: Journal    
DOI: 10.1038/EMM.2016.81     Document Type: Review
Times cited : (815)

References (144)
  • 1
    • 0028068882 scopus 로고
    • Purification of the AMP-activated protein kinase on ATP-gamma-sepharose and analysis of its subunit structure
    • Davies SP, Hawley SA, Woods A, Carling D, Haystead TA, Hardie DG. Purification of the AMP-activated protein kinase on ATP-gamma-sepharose and analysis of its subunit structure. Eur J Biochem 1994; 223: 351–357.
    • (1994) Eur J Biochem , vol.223 , pp. 351-357
    • Davies, S.P.1    Hawley, S.A.2    Woods, A.3    Carling, D.4    Haystead, T.A.5    Hardie, D.G.6
  • 2
    • 84958774989 scopus 로고    scopus 로고
    • Evolving lessons on the complex role of AMPK in normal physiology and cancer
    • Dasgupta B, Chhipa RR. Evolving lessons on the complex role of AMPK in normal physiology and cancer. Trends Pharmacol Sci 2016; 37: 192–206.
    • (2016) Trends Pharmacol Sci , vol.37 , pp. 192-206
    • Dasgupta, B.1    Chhipa, R.R.2
  • 3
    • 84955464040 scopus 로고    scopus 로고
    • Differential regulation by AMP and ADP of AMPK complexes containing different gamma subunit isoforms
    • Ross FA, Jensen TE, Hardie DG. Differential regulation by AMP and ADP of AMPK complexes containing different gamma subunit isoforms. Biochem J 2016; 473: 189–199.
    • (2016) Biochem J , vol.473 , pp. 189-199
    • Ross, F.A.1    Jensen, T.E.2    Hardie, D.G.3
  • 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: 251–262.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 6
    • 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 SA, Boudeau J, Reid JL, Mustard KJ, Udd L, Makela TP et al. 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 2003; 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
  • 8
    • 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, Hurley RL, Witters LA, DePinho RA 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: 3329–3335.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3329-3335
    • Shaw, R.J.1    Kosmatka, M.2    Bardeesy, N.3    Hurley, R.L.4    Witters, L.A.5    Depinho, R.A.6
  • 9
    • 23044437445 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells
    • Woods A, Dickerson K, Heath R, Hong SP, Momcilovic M, Johnstone SR et al. Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells. Cell Metab 2005; 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
  • 10
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase
    • Hawley SA, Pan DA, Mustard KJ, Ross L, Bain J, Edelman AM et al. Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. Cell Metab 2005; 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
  • 11
    • 23844471263 scopus 로고    scopus 로고
    • The Ca2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases
    • Hurley RL, Anderson KA, Franzone JM, Kemp BE, Means AR, Witters LA. The Ca2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases. J Biol Chem 2005; 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
  • 12
    • 0029561919 scopus 로고
    • 5′-AMP inhibits depho-sphorylation, 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 SP, Helps NR, Cohen PT, Hardie DG. 5′-AMP inhibits depho-sphorylation, 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 1995; 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
  • 13
    • 78650606464 scopus 로고    scopus 로고
    • Beta-subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK)
    • Oakhill JS, Chen ZP, Scott JW, Steel R, Castelli LA, Ling N et al. Beta-subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK). Proc Natl Acad Sci USA 2010; 107: 19237–19241.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19237-19241
    • Oakhill, J.S.1    Chen, Z.P.2    Scott, J.W.3    Steel, R.4    Castelli, L.A.5    Ling, N.6
  • 14
    • 57849090443 scopus 로고    scopus 로고
    • The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor
    • McBride A, Ghilagaber S, Nikolaev A, Hardie DG. The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor. Cell Metab 2009; 9: 23–34.
    • (2009) Cell Metab , vol.9 , pp. 23-34
    • McBride, A.1    Ghilagaber, S.2    Nikolaev, A.3    Hardie, D.G.4
  • 15
    • 33751229931 scopus 로고    scopus 로고
    • A pivotal role for endogenous TGF-beta-activated kinase-1 in the LKB1/AMP-activated protein kinase energy-sensor pathway
    • Xie M, Zhang D, Dyck JR, Li Y, Zhang H, Morishima M et al. A pivotal role for endogenous TGF-beta-activated kinase-1 in the LKB1/AMP-activated protein kinase energy-sensor pathway. Proc Natl Acad Sci USA 2006; 103: 17378–17383.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17378-17383
    • Xie, M.1    Zhang, D.2    Dyck, J.R.3    Li, Y.4    Zhang, H.5    Morishima, M.6
  • 16
    • 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: 25336–25343.
    • (2006) J Biol Chem , vol.281 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.P.2    Carlson, M.3
  • 17
    • 84897534723 scopus 로고    scopus 로고
    • Phosphorylation by Akt within the ST loop of AMPK-alpha1 down-regulates its activation in tumour cells
    • Hawley SA, Ross FA, Gowans GJ, Tibarewal P, Leslie NR, Hardie DG. Phosphorylation by Akt within the ST loop of AMPK-alpha1 down-regulates its activation in tumour cells. Biochem J 2014; 459: 275–287.
    • (2014) Biochem J , vol.459 , pp. 275-287
    • Hawley, S.A.1    Ross, F.A.2    Gowans, G.J.3    Tibarewal, P.4    Leslie, N.R.5    Hardie, D.G.6
  • 19
    • 84863535512 scopus 로고    scopus 로고
    • p70S6 kinase phosphorylates AMPK on serine 491 to mediate leptin's effect on food intake
    • Dagon Y, Hur E, Zheng B, Wellenstein K, Cantley LC, Kahn BB. p70S6 kinase phosphorylates AMPK on serine 491 to mediate leptin's effect on food intake. Cell Metab 2012; 16: 104–112.
    • (2012) Cell Metab , vol.16 , pp. 104-112
    • Dagon, Y.1    Hur, E.2    Zheng, B.3    Wellenstein, K.4    Cantley, L.C.5    Kahn, B.B.6
  • 20
    • 84973389963 scopus 로고    scopus 로고
    • PKD1 inhibits AMPKalpha2 through phosphorylation of serine 491 and impairs insulin signaling in skeletal muscle cells
    • Coughlan KA, Valentine RJ, Sudit BS, Allen K, Dagon Y, Kahn BB et al. PKD1 inhibits AMPKalpha2 through phosphorylation of serine 491 and impairs insulin signaling in skeletal muscle cells. J Biol Chem 2016; 291: 5664–5675.
    • (2016) J Biol Chem , vol.291 , pp. 5664-5675
    • Coughlan, K.A.1    Valentine, R.J.2    Sudit, B.S.3    Allen, K.4    Dagon, Y.5    Kahn, B.B.6
  • 21
    • 75049085233 scopus 로고    scopus 로고
    • PKA phosphorylates and inactivates AMPKalpha to promote efficient lipolysis
    • Djouder N, Tuerk RD, Suter M, Salvioni P, Thali RF, Scholz R et al. PKA phosphorylates and inactivates AMPKalpha to promote efficient lipolysis. EMBO J 2010; 29: 469–481.
    • (2010) EMBO J , vol.29 , pp. 469-481
    • Djouder, N.1    Tuerk, R.D.2    Suter, M.3    Salvioni, P.4    Thali, R.F.5    Scholz, R.6
  • 22
    • 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, Zhao J, Lam P, Ye J et al. Downregulation of AMP-activated protein kinase by Cidea-mediated ubiquitination and degradation in brown adipose tissue. EMBO J 2008; 27: 1537–1548.
    • (2008) EMBO J , vol.27 , pp. 1537-1548
    • Qi, J.1    Gong, J.2    Zhao, T.3    Zhao, J.4    Lam, P.5    Ye, J.6
  • 24
    • 84874077399 scopus 로고    scopus 로고
    • E3 ubiquitin ligase, WWP1, interacts with AMPKalpha2 and down-regulates its expression in skeletal muscle C2C12 cells
    • Lee JO, Lee SK, Kim N, Kim JH, You GY, Moon JW et al. E3 ubiquitin ligase, WWP1, interacts with AMPKalpha2 and down-regulates its expression in skeletal muscle C2C12 cells. J Biol Chem 2013; 288: 4673–4680.
    • (2013) J Biol Chem , vol.288 , pp. 4673-4680
    • Lee, J.O.1    Lee, S.K.2    Kim, N.3    Kim, J.H.4    You, G.Y.5    Moon, J.W.6
  • 26
    • 84878695660 scopus 로고    scopus 로고
    • Sumoylation of AMPKbeta2 subunit enhances AMP-activated protein kinase activity
    • Rubio T, Vernia S, Sanz P. Sumoylation of AMPKbeta2 subunit enhances AMP-activated protein kinase activity. Mol Biol Cell 2013; 24: 1801–1811.
    • (2013) Mol Biol Cell , vol.24 , pp. 1801-1811
    • Rubio, T.1    Vernia, S.2    Sanz, P.3
  • 27
    • 84923927635 scopus 로고    scopus 로고
    • The double-edged sword of AMPK signaling in cancer and its therapeutic implications
    • Jeon SM, Hay N. The double-edged sword of AMPK signaling in cancer and its therapeutic implications. Arch Pharm Res 2015; 38: 346–357.
    • (2015) Arch Pharm Res , vol.38 , pp. 346-357
    • Jeon, S.M.1    Hay, N.2
  • 28
    • 84862849835 scopus 로고    scopus 로고
    • Redox implications of AMPK-mediated signal transduction beyond energetic clues
    • Cardaci S, Filomeni G, Ciriolo MR. Redox implications of AMPK-mediated signal transduction beyond energetic clues. J Cell Sci 2012; 125: 2115–2125.
    • (2012) J Cell Sci , vol.125 , pp. 2115-2125
    • Cardaci, S.1    Filomeni, G.2    Ciriolo, M.R.3
  • 29
    • 77958501463 scopus 로고    scopus 로고
    • Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase
    • Zmijewski JW, Banerjee S, Bae H, Friggeri A, Lazarowski ER, Abraham E. Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase. J Biol Chem 2010; 285: 33154–33164.
    • (2010) J Biol Chem , vol.285 , pp. 33154-33164
    • Zmijewski, J.W.1    Banerjee, S.2    Bae, H.3    Friggeri, A.4    Lazarowski, E.R.5    Abraham, E.6
  • 30
    • 84893432818 scopus 로고    scopus 로고
    • A redox-dependent mechanism for regulation of AMPK activation by Thioredoxin1 during energy starvation
    • Shao D, Oka S, Liu T, Zhai P, Ago T, Sciarretta S et al. A redox-dependent mechanism for regulation of AMPK activation by Thioredoxin1 during energy starvation. Cell Metab 2014; 19: 232–245.
    • (2014) Cell Metab , vol.19 , pp. 232-245
    • Shao, D.1    Oka, S.2    Liu, T.3    Zhai, P.4    Ago, T.5    Sciarretta, S.6
  • 31
    • 33750293584 scopus 로고    scopus 로고
    • Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling
    • Baba M, Hong SB, Sharma N, Warren MB, Nickerson ML, Iwamatsu A et al. Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling. Proc Natl Acad Sci USA 2006; 103: 15552–15557.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15552-15557
    • Baba, M.1    Hong, S.B.2    Sharma, N.3    Warren, M.B.4    Nickerson, M.L.5    Iwamatsu, A.6
  • 33
    • 84902201289 scopus 로고    scopus 로고
    • The tumor suppressor folliculin regulates AMPK-dependent metabolic transformation
    • Yan M, Gingras MC, Dunlop EA, Nouet Y, Dupuy F, Jalali Z et al. The tumor suppressor folliculin regulates AMPK-dependent metabolic transformation. J Clin Invest 2014; 124: 2640–2650.
    • (2014) J Clin Invest , vol.124 , pp. 2640-2650
    • Yan, M.1    Gingras, M.C.2    Dunlop, E.A.3    Nouet, Y.4    Dupuy, F.5    Jalali, Z.6
  • 34
    • 48449101433 scopus 로고    scopus 로고
    • p53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling
    • Budanov AV, Karin M. p53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling. Cell 2008; 134: 451–460.
    • (2008) Cell , vol.134 , pp. 451-460
    • Budanov, A.V.1    Karin, M.2
  • 35
    • 84885142437 scopus 로고    scopus 로고
    • AMP as a low-energy charge signal autonomously initiates assembly of AXIN–AMPK– LKB1 complex for AMPK activation
    • Zhang YL, Guo H, Zhang CS, Lin SY, Yin Z, Peng Y et al. AMP as a low-energy charge signal autonomously initiates assembly of AXIN–AMPK– LKB1 complex for AMPK activation. Cell Metab 2013; 18: 546–555.
    • (2013) Cell Metab , vol.18 , pp. 546-555
    • Zhang, Y.L.1    Guo, H.2    Zhang, C.S.3    Lin, S.Y.4    Yin, Z.5    Peng, Y.6
  • 36
    • 84939426946 scopus 로고    scopus 로고
    • Myristoylation confers noncanonical AMPK functions in autophagy selectivity and mitochondrial surveillance
    • Liang J, Xu ZX, Ding Z, Lu Y, Yu Q, Werle KD et al. Myristoylation confers noncanonical AMPK functions in autophagy selectivity and mitochondrial surveillance. Nat Commun 2015; 6: 7926.
    • (2015) Nat Commun , vol.6
    • Liang, J.1    Xu, Z.X.2    Ding, Z.3    Lu, Y.4    Yu, Q.5    Werle, K.D.6
  • 37
    • 34250182374 scopus 로고    scopus 로고
    • Leptin stimulates fatty acid oxidation and peroxisome proliferator-activated receptor alpha gene expression in mouse C2C12 myoblasts by changing the subcellular localization of the alpha2 form of AMP-activated protein kinase
    • Suzuki A, Okamoto S, Lee S, Saito K, Shiuchi T, Minokoshi Y. Leptin stimulates fatty acid oxidation and peroxisome proliferator-activated receptor alpha gene expression in mouse C2C12 myoblasts by changing the subcellular localization of the alpha2 form of AMP-activated protein kinase. Mol Cell Biol 2007; 27: 4317–4327.
    • (2007) Mol Cell Biol , vol.27 , pp. 4317-4327
    • Suzuki, A.1    Okamoto, S.2    Lee, S.3    Saito, K.4    Shiuchi, T.5    Minokoshi, Y.6
  • 38
    • 0033054706 scopus 로고    scopus 로고
    • Cellular distribution and developmental expression of AMP-activated protein kinase isoforms in mouse central nervous system
    • Turnley AM, Stapleton D, Mann RJ, Witters LA, Kemp BE, Bartlett PF. Cellular distribution and developmental expression of AMP-activated protein kinase isoforms in mouse central nervous system. J. Neurochem 1999; 72: 1707–1716.
    • (1999) J. Neurochem , vol.72 , pp. 1707-1716
    • Turnley, A.M.1    Stapleton, D.2    Mann, R.J.3    Witters, L.A.4    Kemp, B.E.5    Bartlett, P.F.6
  • 39
    • 39449096289 scopus 로고    scopus 로고
    • Phosphorylation of LKB1 at serine 428 by protein kinase C-zeta is required for metformin-enhanced activation of the AMP-activated protein kinase in endothelial cells
    • Xie Z, Dong Y, Scholz R, Neumann D, Zou MH. Phosphorylation of LKB1 at serine 428 by protein kinase C-zeta is required for metformin-enhanced activation of the AMP-activated protein kinase in endothelial cells. Circulation 2008; 117: 952–962.
    • (2008) Circulation , vol.117 , pp. 952-962
    • Xie, Z.1    Dong, Y.2    Scholz, R.3    Neumann, D.4    Zou, M.H.5
  • 40
    • 33646573080 scopus 로고    scopus 로고
    • Activation of protein kinase C zeta by peroxynitrite regulates LKB1-dependent AMP-activated protein kinase in cultured endothelial cells
    • Xie Z, Dong Y, Zhang M, Cui MZ, Cohen RA, Riek U et al. Activation of protein kinase C zeta by peroxynitrite regulates LKB1-dependent AMP-activated protein kinase in cultured endothelial cells. J Biol Chem 2006; 281: 6366–6375.
    • (2006) J Biol Chem , vol.281 , pp. 6366-6375
    • Xie, Z.1    Dong, Y.2    Zhang, M.3    Cui, M.Z.4    Cohen, R.A.5    Riek, U.6
  • 41
    • 84878759308 scopus 로고    scopus 로고
    • Phosphorylation of serine 399 in LKB1 protein short form by protein kinase Czeta is required for its nucleocytoplasmic transport and consequent AMP-activated protein kinase (AMPK) activation
    • Zhu H, Moriasi CM, Zhang M, Zhao Y, Zou MH. Phosphorylation of serine 399 in LKB1 protein short form by protein kinase Czeta is required for its nucleocytoplasmic transport and consequent AMP-activated protein kinase (AMPK) activation. J Biol Chem 2013; 288: 16495–16505.
    • (2013) J Biol Chem , vol.288 , pp. 16495-16505
    • Zhu, H.1    Moriasi, C.M.2    Zhang, M.3    Zhao, Y.4    Zou, M.H.5
  • 42
    • 67650083087 scopus 로고    scopus 로고
    • Identification of the serine 307 of LKB1 as a novel phosphorylation site essential for its nucleocytoplasmic transport and endothelial cell angiogenesis
    • Xie Z, Dong Y, Zhang J, Scholz R, Neumann D, Zou MH. Identification of the serine 307 of LKB1 as a novel phosphorylation site essential for its nucleocytoplasmic transport and endothelial cell angiogenesis. Mol Cell Biol 2009; 29: 3582–3596.
    • (2009) Mol Cell Biol , vol.29 , pp. 3582-3596
    • Xie, Z.1    Dong, Y.2    Zhang, J.3    Scholz, R.4    Neumann, D.5    Zou, M.H.6
  • 43
    • 75149117805 scopus 로고    scopus 로고
    • Fyn-dependent regulation of energy expenditure and body weight is mediated by tyrosine phosphorylation of LKB1
    • Yamada E, Pessin JE, Kurland IJ, Schwartz GJ, Bastie CC. Fyn-dependent regulation of energy expenditure and body weight is mediated by tyrosine phosphorylation of LKB1. Cell Metab 2010; 11: 113–124.
    • (2010) Cell Metab , vol.11 , pp. 113-124
    • Yamada, E.1    Pessin, J.E.2    Kurland, I.J.3    Schwartz, G.J.4    Bastie, C.C.5
  • 44
    • 55549096745 scopus 로고    scopus 로고
    • SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation
    • Lan F, Cacicedo JM, Ruderman N, Ido Y. SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation. J Biol Chem 2008; 283: 27628–27635.
    • (2008) J Biol Chem , vol.283 , pp. 27628-27635
    • Lan, F.1    Cacicedo, J.M.2    Ruderman, N.3    Ido, Y.4
  • 45
    • 84938552420 scopus 로고    scopus 로고
    • A critical SUMO1 modification of LKB1 regulates AMPK activity during energy stress
    • Ritho J, Arold ST, Yeh ET. A critical SUMO1 modification of LKB1 regulates AMPK activity during energy stress. Cell Rep 2015; 12: 734–742.
    • (2015) Cell Rep , vol.12 , pp. 734-742
    • Ritho, J.1    Arold, S.T.2    Yeh, E.T.3
  • 46
    • 84925272879 scopus 로고    scopus 로고
    • Skp2-dependent ubiquitination and activation of LKB1 is essential for cancer cell survival under energy stress
    • Lee SW, Li CF, Jin G, Cai Z, Han F, Chan CH et al. Skp2-dependent ubiquitination and activation of LKB1 is essential for cancer cell survival under energy stress. Mol Cell 2015; 57: 1022–1033.
    • (2015) Mol Cell , vol.57 , pp. 1022-1033
    • Lee, S.W.1    Li, C.F.2    Jin, G.3    Cai, Z.4    Han, F.5    Chan, C.H.6
  • 47
    • 84871326334 scopus 로고    scopus 로고
    • Post-translational modification of serine/threonine kinase LKB1 via adduction of the reactive lipid species 4-hydroxy-trans-2-nonenal (HNE) at lysine residue 97 directly inhibits kinase activity
    • Calamaras TD, Lee C, Lan F, Ido Y, Siwik DA, Colucci WS. Post-translational modification of serine/threonine kinase LKB1 via adduction of the reactive lipid species 4-hydroxy-trans-2-nonenal (HNE) at lysine residue 97 directly inhibits kinase activity. J Biol Chem 2012; 287: 42400–42406.
    • (2012) J Biol Chem , vol.287 , pp. 42400-42406
    • Calamaras, T.D.1    Lee, C.2    Lan, F.3    Ido, Y.4    Siwik, D.A.5    Colucci, W.S.6
  • 48
    • 33646372991 scopus 로고    scopus 로고
    • Reactive lipid species from cyclooxygenase-2 inactivate tumor suppressor LKB1/STK11: Cyclopente-none prostaglandins and 4-hydroxy-2-nonenal covalently modify and inhibit the AMP-kinase kinase that modulates cellular energy homeostasis and protein translation
    • Wagner TM, Mullally JE, Fitzpatrick FA. Reactive lipid species from cyclooxygenase-2 inactivate tumor suppressor LKB1/STK11: cyclopente-none prostaglandins and 4-hydroxy-2-nonenal covalently modify and inhibit the AMP-kinase kinase that modulates cellular energy homeostasis and protein translation. J Biol Chem 2006; 281: 2598–2604.
    • (2006) J Biol Chem , vol.281 , pp. 2598-2604
    • Wagner, T.M.1    Mullally, J.E.2    Fitzpatrick, F.A.3
  • 49
    • 79953755370 scopus 로고    scopus 로고
    • AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice
    • Li Y, Xu S, Mihaylova MM, Zheng B, Hou X, Jiang B et al. AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice. Cell Metab 2011; 13: 376–388.
    • (2011) Cell Metab , vol.13 , pp. 376-388
    • Li, Y.1    Xu, S.2    Mihaylova, M.M.3    Zheng, B.4    Hou, X.5    Jiang, B.6
  • 50
    • 0036864358 scopus 로고    scopus 로고
    • Regulation of fatty acid synthesis and oxidation by the AMP-activated protein kinase
    • Hardie DG, Pan DA. Regulation of fatty acid synthesis and oxidation by the AMP-activated protein kinase. Biochem Soc Trans 2002; 30: 1064–1070.
    • (2002) Biochem Soc Trans , vol.30 , pp. 1064-1070
    • Hardie, D.G.1    Pan, D.A.2
  • 51
    • 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 DM, Seefeld K, Witters LA, Coleman RA. 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 1999; 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
  • 52
    • 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: 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
  • 53
    • 60549115574 scopus 로고    scopus 로고
    • Crucial role for LKB1 to AMPKalpha2 axis in the regulation of CD36-mediated long-chain fatty acid uptake into cardiomyocytes
    • Habets DD, Coumans WA, El Hasnaoui M, Zarrinpashneh E, Bertrand L, Viollet B et al. Crucial role for LKB1 to AMPKalpha2 axis in the regulation of CD36-mediated long-chain fatty acid uptake into cardiomyocytes. Biochim Biophys Acta 2009; 1791: 212–219.
    • (2009) Biochim Biophys Acta , vol.1791 , pp. 212-219
    • Habets, D.D.1    Coumans, W.A.2    El Hasnaoui, M.3    Zarrinpashneh, E.4    Bertrand, L.5    Viollet, B.6
  • 54
    • 0025330929 scopus 로고
    • Identification and role of the basal phosphorylation site on hormone-sensitive lipase
    • Garton AJ, Yeaman SJ. Identification and role of the basal phosphorylation site on hormone-sensitive lipase. Eur J Biochem 1990; 191: 245–250.
    • (1990) Eur J Biochem , vol.191 , pp. 245-250
    • Garton, A.J.1    Yeaman, S.J.2
  • 55
    • 21644455008 scopus 로고    scopus 로고
    • Anti-lipolytic action of AMP-activated protein kinase in rodent adipocytes
    • Daval M, Diot-Dupuy F, Bazin R, Hainault I, Viollet B, Vaulont S et al. Anti-lipolytic action of AMP-activated protein kinase in rodent adipocytes. J Biol Chem 2005; 280: 25250–25257.
    • (2005) J Biol Chem , vol.280 , pp. 25250-25257
    • Daval, M.1    Diot-Dupuy, F.2    Bazin, R.3    Hainault, I.4    Viollet, B.5    Vaulont, S.6
  • 56
    • 44349161745 scopus 로고    scopus 로고
    • Discovery of TBC1D1 as an insulin-, AICAR-, and contraction-stimulated signaling nexus in mouse skeletal muscle
    • Taylor EB, An D, Kramer HF, Yu H, Fujii NL, Roeckl KS et al. Discovery of TBC1D1 as an insulin-, AICAR-, and contraction-stimulated signaling nexus in mouse skeletal muscle. J Biol Chem 2008; 283: 9787–9796.
    • (2008) J Biol Chem , vol.283 , pp. 9787-9796
    • Taylor, E.B.1    An, D.2    Kramer, H.F.3    Yu, H.4    Fujii, N.L.5    Roeckl, K.S.6
  • 57
    • 84875813063 scopus 로고    scopus 로고
    • AMPK-dependent degradation of TXNIP upon energy stress leads to enhanced glucose uptake via GLUT1
    • Wu N, Zheng B, Shaywitz A, Dagon Y, Tower C, Bellinger G et al. AMPK-dependent degradation of TXNIP upon energy stress leads to enhanced glucose uptake via GLUT1. Mol Cell 2013; 49: 1167–1175.
    • (2013) Mol Cell , vol.49 , pp. 1167-1175
    • Wu, N.1    Zheng, B.2    Shaywitz, A.3    Dagon, Y.4    Tower, C.5    Bellinger, G.6
  • 60
    • 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, Deprez J, Beauloye C, Vincent MF 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: 1247–1255.
    • (2000) Curr Biol , vol.10 , pp. 1247-1255
    • Marsin, A.S.1    Bertrand, L.2    Rider, M.H.3    Deprez, J.4    Beauloye, C.5    Vincent, M.F.6
  • 61
    • 0037163076 scopus 로고    scopus 로고
    • The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase
    • Marsin AS, Bouzin C, Bertrand L, Hue L. The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase. J Biol Chem 2002; 277: 30778–30783.
    • (2002) J Biol Chem , vol.277 , pp. 30778-30783
    • Marsin, A.S.1    Bouzin, C.2    Bertrand, L.3    Hue, L.4
  • 62
    • 79952395789 scopus 로고    scopus 로고
    • Molecular mechanism by which AMP-activated protein kinase activation promotes glycogen accumulation in muscle
    • Hunter RW, Treebak JT, Wojtaszewski JFP, Sakamoto K. Molecular mechanism by which AMP-activated protein kinase activation promotes glycogen accumulation in muscle. Diabetes 2011; 60: 766–774.
    • (2011) Diabetes , vol.60 , pp. 766-774
    • Hunter, R.W.1    Treebak, J.T.2    Wojtaszewski, J.F.P.3    Sakamoto, K.4
  • 63
    • 27144506185 scopus 로고    scopus 로고
    • The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism
    • Koo SH, Flechner L, Qi L, Zhang X, Screaton RA, Jeffries S et al. The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism. Nature 2005; 437: 1109–1111.
    • (2005) Nature , vol.437 , pp. 1109-1111
    • Koo, S.H.1    Flechner, L.2    Qi, L.3    Zhang, X.4    Screaton, R.A.5    Jeffries, S.6
  • 64
    • 0035406121 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor-4alpha involved in type 1 maturity-onset diabetes of the young is a novel target of AMP-activated protein kinase
    • Leclerc I, Lenzner C, Gourdon L, Vaulont S, Kahn A, Viollet B. Hepatocyte nuclear factor-4alpha involved in type 1 maturity-onset diabetes of the young is a novel target of AMP-activated protein kinase. Diabetes 2001; 50: 1515–1521.
    • (2001) Diabetes , vol.50 , pp. 1515-1521
    • Leclerc, I.1    Lenzner, C.2    Gourdon, L.3    Vaulont, S.4    Kahn, A.5    Viollet, B.6
  • 65
    • 79955815135 scopus 로고    scopus 로고
    • Class IIa histone deacetylases are hormone-activated regulators of FOXO and mammalian glucose homeostasis
    • Mihaylova MM, Vasquez DS, Ravnskjaer K, Denechaud PD, Yu RT, Alvarez JG et al. Class IIa histone deacetylases are hormone-activated regulators of FOXO and mammalian glucose homeostasis. Cell 2011; 145: 607–621.
    • (2011) Cell , vol.145 , pp. 607-621
    • Mihaylova, M.M.1    Vasquez, D.S.2    Ravnskjaer, K.3    Denechaud, P.D.4    Yu, R.T.5    Alvarez, J.G.6
  • 66
    • 70449584566 scopus 로고    scopus 로고
    • AMP-activated protein kinase adapts rRNA synthesis to cellular energy supply
    • Hoppe S, Bierhoff H, Cado I, Weber A, Tiebe M, Grummt I et al. AMP-activated protein kinase adapts rRNA synthesis to cellular energy supply. Proc Natl Acad Sci USA 2009; 106: 17781–17786.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 17781-17786
    • Hoppe, S.1    Bierhoff, H.2    Cado, I.3    Weber, A.4    Tiebe, M.5    Grummt, I.6
  • 67
    • 84878271546 scopus 로고    scopus 로고
    • The eEF2 kinase confers resistance to nutrient deprivation by blocking translation elongation
    • Leprivier G, Remke M, Rotblat B, Dubuc A, Mateo AR, Kool M et al. The eEF2 kinase confers resistance to nutrient deprivation by blocking translation elongation. Cell 2013; 153: 1064–1079.
    • (2013) Cell , vol.153 , pp. 1064-1079
    • Leprivier, G.1    Remke, M.2    Rotblat, B.3    Dubuc, A.4    Mateo, A.R.5    Kool, M.6
  • 69
    • 79955419135 scopus 로고    scopus 로고
    • Up-regulation of AMP-activated protein kinase in cancer cell lines is mediated through c-Src activation
    • Mizrachy-Schwartz S, Cohen N, Klein S, Kravchenko-Balasha N, Levitzki A. Up-regulation of AMP-activated protein kinase in cancer cell lines is mediated through c-Src activation. J Biol Chem 2011; 286: 15268–15277.
    • (2011) J Biol Chem , vol.286 , pp. 15268-15277
    • Mizrachy-Schwartz, S.1    Cohen, N.2    Klein, S.3    Kravchenko-Balasha, N.4    Levitzki, A.5
  • 70
    • 79251587803 scopus 로고    scopus 로고
    • Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy
    • Egan DF, Shackelford DB, Mihaylova MM, Gelino S, Kohnz RA, Mair W et al. Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy. Science 2011; 331: 456–461.
    • (2011) Science , vol.331 , pp. 456-461
    • Egan, D.F.1    Shackelford, D.B.2    Mihaylova, M.M.3    Gelino, S.4    Kohnz, R.A.5    Mair, W.6
  • 71
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim J, Kundu M, Viollet B, Guan KL. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol 2011; 13: 132–141.
    • (2011) Nat. Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 72
    • 80053163909 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) beta1beta2 muscle null mice reveal an essential role for AMPK in maintaining mitochondrial content and glucose uptake during exercise
    • O'Neill HM, Maarbjerg SJ, Crane JD, Jeppesen J, Jorgensen SB, Schertzer JD et al. AMP-activated protein kinase (AMPK) beta1beta2 muscle null mice reveal an essential role for AMPK in maintaining mitochondrial content and glucose uptake during exercise. Proc Natl Acad Sci USA 2011; 108: 16092–16097.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 16092-16097
    • O'neill, H.M.1    Maarbjerg, S.J.2    Crane, J.D.3    Jeppesen, J.4    Jorgensen, S.B.5    Schertzer, J.D.6
  • 74
    • 24144463983 scopus 로고    scopus 로고
    • Metabolic control through the PGC-1 family of transcription coactivators
    • Lin J, Handschin C, Spiegelman BM. Metabolic control through the PGC-1 family of transcription coactivators. Cell Metab 2005; 1: 361–370.
    • (2005) Cell Metab , vol.1 , pp. 361-370
    • Lin, J.1    Handschin, C.2    Spiegelman, B.M.3
  • 75
    • 34547545892 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha
    • Jager S, Handschin C, St-Pierre J, Spiegelman BM. AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha. Proc Natl Acad Sci USA 2007; 104: 12017–12022.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12017-12022
    • Jager, S.1    Handschin, C.2    St-Pierre, J.3    Spiegelman, B.M.4
  • 76
    • 43049121395 scopus 로고    scopus 로고
    • Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt
    • Fulco M, Cen Y, Zhao P, Hoffman EP, McBurney MW, Sauve AA et al. Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt. Dev Cell 2008; 14: 661–673.
    • (2008) Dev Cell , vol.14 , pp. 661-673
    • Fulco, M.1    Cen, Y.2    Zhao, P.3    Hoffman, E.P.4    McBurney, M.W.5    Sauve, A.A.6
  • 77
    • 67349276169 scopus 로고    scopus 로고
    • AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
    • Canto C, Gerhart-Hines Z, Feige JN, Lagouge M, Noriega L, Milne JC et al. AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 2009; 458: 1056–1060.
    • (2009) Nature , vol.458 , pp. 1056-1060
    • Canto, C.1    Gerhart-Hines, Z.2    Feige, J.N.3    Lagouge, M.4    Noriega, L.5    Milne, J.C.6
  • 78
    • 85018222039 scopus 로고    scopus 로고
    • AMPK maintains energy homeostasis and survival in cancer cells via regulating p38/PGC-1α-mediated mitochondrial biogenesis
    • Chaube B, Malvi P, Singh SV, Mohammad N, Viollet B, Bhat MK. AMPK maintains energy homeostasis and survival in cancer cells via regulating p38/PGC-1α-mediated mitochondrial biogenesis. Cell Death Discov 2015; 1: 15063.
    • (2015) Cell Death Discov , vol.1
    • Chaube, B.1    Malvi, P.2    Singh, S.V.3    Mohammad, N.4    Viollet, B.5    Bhat, M.K.6
  • 79
    • 34848861463 scopus 로고    scopus 로고
    • The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor
    • Greer EL, Oskoui PR, Banko MR, Maniar JM, Gygi MP, Gygi SP et al. The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor. J Biol Chem 2007; 282: 30107–30119.
    • (2007) J Biol Chem , vol.282 , pp. 30107-30119
    • Greer, E.L.1    Oskoui, P.R.2    Banko, M.R.3    Maniar, J.M.4    Gygi, M.P.5    Gygi, S.P.6
  • 80
    • 70349633673 scopus 로고    scopus 로고
    • Activation of the AMPK–FOXO3 pathway reduces fatty acid-induced increase in intracellular reactive oxygen species by upregulating thioredoxin
    • Li XN, Song J, Zhang L, LeMaire SA, Hou X, Zhang C et al. Activation of the AMPK–FOXO3 pathway reduces fatty acid-induced increase in intracellular reactive oxygen species by upregulating thioredoxin. Diabetes 2009; 58: 2246–2257.
    • (2009) Diabetes , vol.58 , pp. 2246-2257
    • Li, X.N.1    Song, J.2    Zhang, L.3    Lemaire, S.A.4    Hou, X.5    Zhang, C.6
  • 82
    • 85056570121 scopus 로고    scopus 로고
    • AMPK signalling regulates Nrf2 localization and activity via sirtuins in a monocytic cell line
    • Naveira LN, Mercado N, Ito K. AMPK signalling regulates Nrf2 localization and activity via sirtuins in a monocytic cell line. Eur Respir J 2011; 38: Suppl 55.
    • (2011) Eur Respir J , vol.38
    • Naveira, L.N.1    Mercado, N.2    Ito, K.3
  • 83
    • 84863763440 scopus 로고    scopus 로고
    • AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress
    • Jeon S-M, Chandel NS, Hay N. AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress. Nature 2012; 485: 661–665.
    • (2012) Nature , vol.485 , pp. 661-665
    • Jeon, S.-M.1    Chandel, N.S.2    Hay, N.3
  • 85
    • 84930641237 scopus 로고    scopus 로고
    • Nutrient excess and AMPK downregulation in incubated skeletal muscle and muscle of glucose infused rats
    • Coughlan KA, Balon TW, Valentine RJ, Petrocelli R, Schultz V, Brandon A et al. Nutrient excess and AMPK downregulation in incubated skeletal muscle and muscle of glucose infused rats. PLoS ONE 2015; 10: e0127388.
    • (2015) Plos ONE , vol.10
    • Coughlan, K.A.1    Balon, T.W.2    Valentine, R.J.3    Petrocelli, R.4    Schultz, V.5    Brandon, A.6
  • 86
    • 0038015693 scopus 로고    scopus 로고
    • Glucose autoregulates its uptake in skeletal muscle: Involvement of AMP-activated protein kinase
    • Itani SI, Saha AK, Kurowski TG, Coffin HR, Tornheim K, Ruderman NB. Glucose autoregulates its uptake in skeletal muscle: involvement of AMP-activated protein kinase. Diabetes 2003; 52: 1635–1640.
    • (2003) Diabetes , vol.52 , pp. 1635-1640
    • Itani, S.I.1    Saha, A.K.2    Kurowski, T.G.3    Coffin, H.R.4    Tornheim, K.5    Ruderman, N.B.6
  • 87
    • 33645092172 scopus 로고    scopus 로고
    • Increased malonyl-CoA and diacylglycerol content and reduced AMPK activity accompany insulin resistance induced by glucose infusion in muscle and liver of rats
    • Kraegen EW, Saha AK, Preston E, Wilks D, Hoy AJ, Cooney GJ et al. Increased malonyl-CoA and diacylglycerol content and reduced AMPK activity accompany insulin resistance induced by glucose infusion in muscle and liver of rats. Am J Physiol Endocrinol Metab 2006; 290: E471–E479.
    • (2006) Am J Physiol Endocrinol Metab , vol.290 , pp. E471-E479
    • Kraegen, E.W.1    Saha, A.K.2    Preston, E.3    Wilks, D.4    Hoy, A.J.5    Cooney, G.J.6
  • 88
    • 77957567397 scopus 로고    scopus 로고
    • Downregulation of AMPK accompanies leucine-and glucose-induced increases in protein synthesis and insulin resistance in rat skeletal muscle
    • Saha AK, Xu XJ, Lawson E, Deoliveira R, Brandon AE, Kraegen EW et al. Downregulation of AMPK accompanies leucine-and glucose-induced increases in protein synthesis and insulin resistance in rat skeletal muscle. Diabetes 2010; 59: 2426–2434.
    • (2010) Diabetes , vol.59 , pp. 2426-2434
    • Saha, A.K.1    Xu, X.J.2    Lawson, E.3    Deoliveira, R.4    Brandon, A.E.5    Kraegen, E.W.6
  • 89
    • 34247241597 scopus 로고    scopus 로고
    • Leucine stimulates mammalian target of rapamycin signaling in C2C12 myoblasts in part through inhibition of adenosine monophosphate-activated protein kinase
    • Du M, Shen QW, Zhu MJ, Ford SP. Leucine stimulates mammalian target of rapamycin signaling in C2C12 myoblasts in part through inhibition of adenosine monophosphate-activated protein kinase. J Anim Sci 2007; 85: 919–927.
    • (2007) J Anim Sci , vol.85 , pp. 919-927
    • Du, M.1    Shen, Q.W.2    Zhu, M.J.3    Ford, S.P.4
  • 90
    • 80055115885 scopus 로고    scopus 로고
    • Insulin resistance due to nutrient excess: Is it a consequence of AMPK downregulation?
    • Saha AK, Xu XJ, Balon TW, Brandon A, Kraegen EW, Ruderman NB. Insulin resistance due to nutrient excess: is it a consequence of AMPK downregulation? Cell Cycle 2011; 10: 3447–3451.
    • (2011) Cell Cycle , vol.10 , pp. 3447-3451
    • Saha, A.K.1    Xu, X.J.2    Balon, T.W.3    Brandon, A.4    Kraegen, E.W.5    Ruderman, N.B.6
  • 91
    • 34248199965 scopus 로고    scopus 로고
    • Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase
    • Wu Y, Song P, Xu J, Zhang M, Zou MH. Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase. J Biol Chem 2007; 282: 9777–9788.
    • (2007) J Biol Chem , vol.282 , pp. 9777-9788
    • Wu, Y.1    Song, P.2    Xu, J.3    Zhang, M.4    Zou, M.H.5
  • 92
    • 84907809393 scopus 로고    scopus 로고
    • Insulin inhibits AMPK activity and phosphorylates AMPK Ser(4)(8)(5)/(4)(9)(1) through Akt in hepatocytes, myotubes and incubated rat skeletal muscle
    • Valentine RJ, Coughlan KA, Ruderman NB, Saha AK. Insulin inhibits AMPK activity and phosphorylates AMPK Ser(4)(8)(5)/(4)(9)(1) through Akt in hepatocytes, myotubes and incubated rat skeletal muscle. Arch Biochem Biophys 2014; 562: 62–69.
    • (2014) Arch Biochem Biophys , vol.562 , pp. 62-69
    • Valentine, R.J.1    Coughlan, K.A.2    Ruderman, N.B.3    Saha, A.K.4
  • 93
    • 0037122766 scopus 로고    scopus 로고
    • Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
    • Minokoshi Y, Kim Y-B, Peroni OD, Fryer LGD, Muller C, Carling D et al. Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. Nature 2002; 415: 339–343.
    • (2002) Nature , vol.415 , pp. 339-343
    • Minokoshi, Y.1    Kim, Y.-B.2    Peroni, O.D.3    Fryer, L.G.D.4    Muller, C.5    Carling, D.6
  • 94
    • 33748742812 scopus 로고    scopus 로고
    • The suppressor of cytokine signaling 3 inhibits leptin activation of AMP-kinase in cultured skeletal muscle of obese humans
    • Steinberg GR, McAinch AJ, Chen MB, O'Brien PE, Dixon JB, Cameron-Smith D et al. The suppressor of cytokine signaling 3 inhibits leptin activation of AMP-kinase in cultured skeletal muscle of obese humans. J Clin Endocrinol Metab 2006; 91: 3592–3597.
    • (2006) J Clin Endocrinol Metab , vol.91 , pp. 3592-3597
    • Steinberg, G.R.1    McAinch, A.J.2    Chen, M.B.3    O'brien, P.E.4    Dixon, J.B.5    Cameron-Smith, D.6
  • 95
    • 33646570554 scopus 로고    scopus 로고
    • CNTF reverses obesity-induced insulin resistance by activating skeletal muscle AMPK
    • Watt MJ, Dzamko N, Thomas WG, Rose-John S, Ernst M, Carling D et al. CNTF reverses obesity-induced insulin resistance by activating skeletal muscle AMPK. Nat Med 2006; 12: 541–548.
    • (2006) Nat Med , vol.12 , pp. 541-548
    • Watt, M.J.1    Dzamko, N.2    Thomas, W.G.3    Rose-John, S.4    Ernst, M.5    Carling, D.6
  • 96
    • 33746037555 scopus 로고    scopus 로고
    • Ciliary neurotrophic factor suppresses hypothalamic AMP-kinase signaling in leptin-resistant obese mice
    • Steinberg GR, Watt MJ, Fam BC, Proietto J, Andrikopoulos S, Allen AM et al. Ciliary neurotrophic factor suppresses hypothalamic AMP-kinase signaling in leptin-resistant obese mice. Endocrinology 2006; 147: 3906–3914.
    • (2006) Endocrinology , vol.147 , pp. 3906-3914
    • Steinberg, G.R.1    Watt, M.J.2    Fam, B.C.3    Proietto, J.4    Andrikopoulos, S.5    Allen, A.M.6
  • 98
    • 0036851817 scopus 로고    scopus 로고
    • Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase
    • Yamauchi T, Kamon J, Minokoshi Y, Ito Y, Waki H, Uchida S et al. Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nat Med 2002; 8: 1288–1295.
    • (2002) Nat Med , vol.8 , pp. 1288-1295
    • Yamauchi, T.1    Kamon, J.2    Minokoshi, Y.3    Ito, Y.4    Waki, H.5    Uchida, S.6
  • 100
    • 3242720519 scopus 로고    scopus 로고
    • Circulating adiponectin levels increase in rats on caloric restriction: The potential for insulin sensitization
    • Zhu M, Miura J, Lu LX, Bernier M, DeCabo R, Lane MA et al. Circulating adiponectin levels increase in rats on caloric restriction: the potential for insulin sensitization. Exp Gerontol 2004; 39: 1049–1059.
    • (2004) Exp Gerontol , vol.39 , pp. 1049-1059
    • Zhu, M.1    Miura, J.2    Lu, L.X.3    Bernier, M.4    Decabo, R.5    Lane, M.A.6
  • 101
    • 81755172024 scopus 로고    scopus 로고
    • Central mechanisms involved in the orexigenic actions of ghrelin
    • Andrews ZB. Central mechanisms involved in the orexigenic actions of ghrelin. Peptides 2011; 32: 2248–2255.
    • (2011) Peptides , vol.32 , pp. 2248-2255
    • Andrews, Z.B.1
  • 103
    • 21644453934 scopus 로고    scopus 로고
    • Cannabinoids and ghrelin have both central and peripheral metabolic and cardiac effects via AMP-activated protein kinase
    • Kola B, Hubina E, Tucci SA, Kirkham TC, Garcia EA, Mitchell SE et al. Cannabinoids and ghrelin have both central and peripheral metabolic and cardiac effects via AMP-activated protein kinase. J Biol Chem 2005; 280: 25196–25201.
    • (2005) J Biol Chem , vol.280 , pp. 25196-25201
    • Kola, B.1    Hubina, E.2    Tucci, S.A.3    Kirkham, T.C.4    Garcia, E.A.5    Mitchell, S.E.6
  • 104
    • 84861558069 scopus 로고    scopus 로고
    • Profound hypoglycemia in starved, ghrelin-deficient mice is caused by decreased gluconeogenesis and reversed by lactate or fatty acids
    • Li RL, Sherbet DP, Elsbernd BL, Goldstein JL, Brown MS, Zhao TJ. Profound hypoglycemia in starved, ghrelin-deficient mice is caused by decreased gluconeogenesis and reversed by lactate or fatty acids. J Biol Chem 2012; 287: 17942–17950.
    • (2012) J Biol Chem , vol.287 , pp. 17942-17950
    • Li, R.L.1    Sherbet, D.P.2    Elsbernd, B.L.3    Goldstein, J.L.4    Brown, M.S.5    Zhao, T.J.6
  • 105
  • 106
    • 84872576236 scopus 로고    scopus 로고
    • Metabolism of inflammation limited by AMPK and pseudo-starvation
    • O'Neill LA, Hardie DG. Metabolism of inflammation limited by AMPK and pseudo-starvation. Nature 2013; 493: 346–355.
    • (2013) Nature , vol.493 , pp. 346-355
    • O'neill, L.A.1    Hardie, D.G.2
  • 107
    • 78650964142 scopus 로고    scopus 로고
    • Decreased AMP-activated protein kinase activity is associated with increased inflammation in visceral adipose tissue and with whole-body insulin resistance in morbidly obese humans
    • Gauthier MS, O'Brien EL, Bigornia S, Mott M, Cacicedo JM, Xu XJ et al. Decreased AMP-activated protein kinase activity is associated with increased inflammation in visceral adipose tissue and with whole-body insulin resistance in morbidly obese humans. Biochem Biophys Res Commun 2011; 404: 382–387.
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 382-387
    • Gauthier, M.S.1    O'brien, E.L.2    Bigornia, S.3    Mott, M.4    Cacicedo, J.M.5    Xu, X.J.6
  • 108
    • 33751552452 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling
    • Steinberg GR, Michell BJ, van Denderen BJ, Watt MJ, Carey AL, Fam BC et al. Tumor necrosis factor alpha-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling. Cell Metab 2006; 4: 465–474.
    • (2006) Cell Metab , vol.4 , pp. 465-474
    • Steinberg, G.R.1    Michell, B.J.2    van Denderen, B.J.3    Watt, M.J.4    Carey, A.L.5    Fam, B.C.6
  • 109
    • 70350560556 scopus 로고    scopus 로고
    • Nutrient stress activates inflammation and reduces glucose metabolism by suppressing AMP-activated protein kinase in the heart
    • Ko HJ, Zhang Z, Jung DY, Jun JY, Ma Z, Jones KE et al. Nutrient stress activates inflammation and reduces glucose metabolism by suppressing AMP-activated protein kinase in the heart. Diabetes 2009; 58: 2536–2546.
    • (2009) Diabetes , vol.58 , pp. 2536-2546
    • Ko, H.J.1    Zhang, Z.2    Jung, D.Y.3    Jun, J.Y.4    Ma, Z.5    Jones, K.E.6
  • 110
    • 77953517927 scopus 로고    scopus 로고
    • Macrophage alpha1 AMP-activated protein kinase (alpha1AMPK) antagonizes fatty acid-induced inflammation through SIRT1
    • Yang Z, Kahn BB, Shi H, Xue BZ. Macrophage alpha1 AMP-activated protein kinase (alpha1AMPK) antagonizes fatty acid-induced inflammation through SIRT1. J Biol Chem 2010; 285: 19051–19059.
    • (2010) J Biol Chem , vol.285
    • Yang, Z.1    Kahn, B.B.2    Shi, H.3    Xue, B.Z.4
  • 111
    • 84901271982 scopus 로고    scopus 로고
    • Human resistin promotes neutrophil proinflammatory activation and neutrophil extracellular trap formation and increases severity of acute lung injury
    • Jiang S, Park DW, Tadie JM, Gregoire M, Deshane J, Pittet JF et al. Human resistin promotes neutrophil proinflammatory activation and neutrophil extracellular trap formation and increases severity of acute lung injury. J Immunol 2014; 192: 4795–4803.
    • (2014) J Immunol , vol.192 , pp. 4795-4803
    • Jiang, S.1    Park, D.W.2    Tadie, J.M.3    Gregoire, M.4    Deshane, J.5    Pittet, J.F.6
  • 112
    • 79952411393 scopus 로고    scopus 로고
    • Inflammatory induction of human resistin causes insulin resistance in endotoxemic mice
    • Park HK, Qatanani M, Briggs ER, Ahima RS, Lazar MA. Inflammatory induction of human resistin causes insulin resistance in endotoxemic mice. Diabetes 2011; 60: 775–783.
    • (2011) Diabetes , vol.60 , pp. 775-783
    • Park, H.K.1    Qatanani, M.2    Briggs, E.R.3    Ahima, R.S.4    Lazar, M.A.5
  • 113
    • 71749096431 scopus 로고    scopus 로고
    • Resistin is stored in neutrophil granules being released upon challenge with inflammatory stimuli
    • Bostrom EA, Tarkowski A, Bokarewa M. Resistin is stored in neutrophil granules being released upon challenge with inflammatory stimuli. Biochim Biophys Acta 2009; 1793: 1894–1900.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1894-1900
    • Bostrom, E.A.1    Tarkowski, A.2    Bokarewa, M.3
  • 114
    • 70349570571 scopus 로고    scopus 로고
    • Resistin induces insulin resistance by both AMPK-dependent and AMPK-independent mechanisms in HepG2 cells
    • Luo Z, Zhang Y, Li F, He J, Ding H, Yan L et al. Resistin induces insulin resistance by both AMPK-dependent and AMPK-independent mechanisms in HepG2 cells. Endocrine 2009; 36: 60–69.
    • (2009) Endocrine , vol.36 , pp. 60-69
    • Luo, Z.1    Zhang, Y.2    Li, F.3    He, J.4    Ding, H.5    Yan, L.6
  • 115
    • 84861694184 scopus 로고    scopus 로고
    • A novel pro-inflammatory mechanism of action of resistin in human endothelial cells: Up-regulation of SOCS3 expression through STAT3 activation
    • Pirvulescu M, Manduteanu I, Gan AM, Stan D, Simion V, Butoi E et al. A novel pro-inflammatory mechanism of action of resistin in human endothelial cells: up-regulation of SOCS3 expression through STAT3 activation. Biochem Biophys Res Commun 2012; 422: 321–326.
    • (2012) Biochem Biophys Res Commun , vol.422 , pp. 321-326
    • Pirvulescu, M.1    Manduteanu, I.2    Gan, A.M.3    Stan, D.4    Simion, V.5    Butoi, E.6
  • 116
    • 58849115949 scopus 로고    scopus 로고
    • Adenosine 5'-monophosphate-activated protein kinase promotes macrophage polarization to an anti-inflammatory functional phenotype
    • Sag D, Carling D, Stout RD, Suttles J. Adenosine 5'-monophosphate-activated protein kinase promotes macrophage polarization to an anti-inflammatory functional phenotype. J Immunol 2008; 181: 8633–8641.
    • (2008) J Immunol , vol.181 , pp. 8633-8641
    • Sag, D.1    Carling, D.2    Stout, R.D.3    Suttles, J.4
  • 117
    • 79959956336 scopus 로고    scopus 로고
    • AMP-activated protein kinase inhibits NF-kappaB signaling and inflammation: Impact on healthspan and lifespan
    • Salminen A, Hyttinen JM, Kaarniranta K. AMP-activated protein kinase inhibits NF-kappaB signaling and inflammation: impact on healthspan and lifespan. J Mol Med (Berl.) 2011; 89: 667–676.
    • (2011) J Mol Med (Berl.) , vol.89 , pp. 667-676
    • Salminen, A.1    Hyttinen, J.M.2    Kaarniranta, K.3
  • 118
    • 84055190798 scopus 로고    scopus 로고
    • Hematopoietic AMPK beta1 reduces mouse adipose tissue macro-phage inflammation and insulin resistance in obesity
    • Galic S, Fullerton MD, Schertzer JD, Sikkema S, Marcinko K, Walkley CR et al. Hematopoietic AMPK beta1 reduces mouse adipose tissue macro-phage inflammation and insulin resistance in obesity. J Clin Invest 2011; 121: 4903–4915.
    • (2011) J Clin Invest , vol.121 , pp. 4903-4915
    • Galic, S.1    Fullerton, M.D.2    Schertzer, J.D.3    Sikkema, S.4    Marcinko, K.5    Walkley, C.R.6
  • 120
    • 84874993428 scopus 로고    scopus 로고
    • AMPK and exercise: Glucose uptake and insulin sensitivity
    • O'Neill HM. AMPK and exercise: glucose uptake and insulin sensitivity. Diabetes Metab J 2013; 37: 1–21.
    • (2013) Diabetes Metab J , vol.37 , pp. 1-21
    • O'neill, H.M.1
  • 121
    • 84855182851 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) controls the aging process via an integrated signaling network
    • Salminen A, Kaarniranta K. AMP-activated protein kinase (AMPK) controls the aging process via an integrated signaling network. Ageing Res Rev 2012; 11: 230–241.
    • (2012) Ageing Res Rev , vol.11 , pp. 230-241
    • Salminen, A.1    Kaarniranta, K.2
  • 122
    • 40949123149 scopus 로고    scopus 로고
    • Activation of innate immunity system during aging: NF-kB signaling is the molecular culprit of inflamm-aging
    • Salminen A, Huuskonen J, Ojala J, Kauppinen A, Kaarniranta K, Suuronen T. Activation of innate immunity system during aging: NF-kB signaling is the molecular culprit of inflamm-aging. Ageing Res Rev 2008; 7: 83–105.
    • (2008) Ageing Res Rev , vol.7 , pp. 83-105
    • Salminen, A.1    Huuskonen, J.2    Ojala, J.3    Kauppinen, A.4    Kaarniranta, K.5    Suuronen, T.6
  • 123
    • 84903691827 scopus 로고    scopus 로고
    • Role of diacylglycerol activation of PKCtheta in lipid-induced muscle insulin resistance in humans
    • Szendroedi J, Yoshimura T, Phielix E, Koliaki C, Marcucci M, Zhang D et al. Role of diacylglycerol activation of PKCtheta in lipid-induced muscle insulin resistance in humans. Proc Natl Acad Sci USA 2014; 111: 9597–9602.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 9597-9602
    • Szendroedi, J.1    Yoshimura, T.2    Phielix, E.3    Koliaki, C.4    Marcucci, M.5    Zhang, D.6
  • 124
    • 78651376861 scopus 로고    scopus 로고
    • Protein kinase C isoforms: Mediators of reactive lipid metabolites in the development of insulin resistance
    • Turban S, Hajduch E. Protein kinase C isoforms: mediators of reactive lipid metabolites in the development of insulin resistance. FEBS Lett 2011; 585: 269–274.
    • (2011) FEBS Lett , vol.585 , pp. 269-274
    • Turban, S.1    Hajduch, E.2
  • 125
    • 84891785508 scopus 로고    scopus 로고
    • TOR-centric view on insulin resistance and diabetic complications: Perspective for endocrinologists and gerontologists
    • Blagosklonny MV. TOR-centric view on insulin resistance and diabetic complications: perspective for endocrinologists and gerontologists. Cell Death Dis 2013; 4: e964.
    • (2013) Cell Death Dis , vol.4 , pp. e964
    • Blagosklonny, M.V.1
  • 126
    • 84927173996 scopus 로고    scopus 로고
    • Branched-chain amino acids in metabolic signalling and insulin resistance
    • Lynch CJ, Adams SH. Branched-chain amino acids in metabolic signalling and insulin resistance. Nat Rev Endocrinol 2014; 10: 723–736.
    • (2014) Nat Rev Endocrinol , vol.10 , pp. 723-736
    • Lynch, C.J.1    Adams, S.H.2
  • 128
    • 79952003715 scopus 로고    scopus 로고
    • FFA-induced adipocyte inflammation and insulin resistance: Involvement of ER stress and IKKβ pathways
    • Jiao P, Ma J, Feng B, Zhang H, Alan-Diehl J, Eugene-Chin Y et al. FFA-induced adipocyte inflammation and insulin resistance: involvement of ER stress and IKKβ pathways. Obesity 2011; 19: 483–491.
    • (2011) Obesity , vol.19 , pp. 483-491
    • Jiao, P.1    Ma, J.2    Feng, B.3    Zhang, H.4    Alan-Diehl, J.5    Eugene-Chin, Y.6
  • 129
    • 84869184022 scopus 로고    scopus 로고
    • Obesity-induced endoplasmic reticulum stress causes chronic inflammation in adipose tissue
    • Kawasaki N, Asada R, Saito A, Kanemoto S, Imaizumi K. Obesity-induced endoplasmic reticulum stress causes chronic inflammation in adipose tissue. Sci Rep 2012; 2: 799.
    • (2012) Sci Rep , vol.2
    • Kawasaki, N.1    Asada, R.2    Saito, A.3    Kanemoto, S.4    Imaizumi, K.5
  • 130
    • 84893455835 scopus 로고    scopus 로고
    • The dark face of AMPK as an essential tumor promoter
    • Jeon SM, Hay N. The dark face of AMPK as an essential tumor promoter. Cell Logist 2012; 2: 197–202.
    • (2012) Cell Logist , vol.2 , pp. 197-202
    • Jeon, S.M.1    Hay, N.2
  • 131
    • 84875740314 scopus 로고    scopus 로고
    • Integrative analysis of complex cancer genomics and clinical profiles using the cBioPortal
    • Gao J, Aksoy BA, Dogrusoz U, Dresdner G, Gross B, Sumer SO et al. Integrative analysis of complex cancer genomics and clinical profiles using the cBioPortal. Sci Signal 2013; 6: pl1.
    • (2013) Sci Signal , vol.6 , pp. pl1
    • Gao, J.1    Aksoy, B.A.2    Dogrusoz, U.3    Dresdner, G.4    Gross, B.5    Sumer, S.O.6
  • 132
    • 84866002291 scopus 로고    scopus 로고
    • The cBio cancer genomics portal: An open platform for exploring multidimen-sional cancer genomics data
    • Cerami E, Gao J, Dogrusoz U, Gross BE, Sumer SO, Aksoy BA et al. The cBio cancer genomics portal: an open platform for exploring multidimen-sional cancer genomics data. Cancer Discov 2012; 2: 401–404.
    • (2012) Cancer Discov , vol.2 , pp. 401-404
    • Cerami, E.1    Gao, J.2    Dogrusoz, U.3    Gross, B.E.4    Sumer, S.O.5    Aksoy, B.A.6
  • 133
    • 0027196120 scopus 로고
    • Mechanisms of multistep carcinogenesis and carcinogen risk assessment
    • Barrett JC. Mechanisms of multistep carcinogenesis and carcinogen risk assessment. Environ. Health Perspect 1993; 100: 9–20.
    • (1993) Environ. Health Perspect , vol.100 , pp. 9-20
    • Barrett, J.C.1
  • 134
    • 84961858396 scopus 로고    scopus 로고
    • STK11/LKB1 deficiency promotes neutrophil recruitment and proinflam-matory cytokine production to suppress T-cell activity in the lung tumor microenvironment
    • Koyama S, Akbay EA, Li YY, Aref AR, Skoulidis F, Herter-Sprie GS et al. STK11/LKB1 deficiency promotes neutrophil recruitment and proinflam-matory cytokine production to suppress T-cell activity in the lung tumor microenvironment. Cancer Res 2016; 76: 999–1008.
    • (2016) Cancer Res , vol.76 , pp. 999-1008
    • Koyama, S.1    Akbay, E.A.2    Li, Y.Y.3    Aref, A.R.4    Skoulidis, F.5    Herter-Sprie, G.S.6
  • 135
    • 84861142867 scopus 로고    scopus 로고
    • AMPKalpha modulation in cancer progression: Multilayer integrative analysis of the whole transcriptome in Asian gastric cancer
    • Kim YH, Liang H, Liu X, Lee JS, Cho JY, Cheong JH et al. AMPKalpha modulation in cancer progression: multilayer integrative analysis of the whole transcriptome in Asian gastric cancer. Cancer Res 2012; 72: 2512–2521.
    • (2012) Cancer Res , vol.72 , pp. 2512-2521
    • Kim, Y.H.1    Liang, H.2    Liu, X.3    Lee, J.S.4    Cho, J.Y.5    Cheong, J.H.6
  • 136
    • 0037068461 scopus 로고    scopus 로고
    • Loss of the Lkb1 tumour suppressor provokes intestinal polyposis but resistance to transformation
    • Bardeesy N, Sinha M, Hezel AF, Signoretti S, Hathaway NA, Sharpless NE et al. Loss of the Lkb1 tumour suppressor provokes intestinal polyposis but resistance to transformation. Nature 2002; 419: 162–167.
    • (2002) Nature , vol.419 , pp. 162-167
    • Bardeesy, N.1    Sinha, M.2    Hezel, A.F.3    Signoretti, S.4    Hathaway, N.A.5    Sharpless, N.E.6
  • 137
    • 84938794719 scopus 로고    scopus 로고
    • Co-occurring genomic alterations define major subsets of KRAS-mutant lung adenocarcinoma with distinct biology, immune profiles, and therapeutic vulnerabilities
    • Skoulidis F, Byers LA, Diao L, Papadimitrakopoulou VA, Tong P, Izzo J et al. Co-occurring genomic alterations define major subsets of KRAS-mutant lung adenocarcinoma with distinct biology, immune profiles, and therapeutic vulnerabilities. Cancer Discov 2015; 5: 860–877.
    • (2015) Cancer Discov , vol.5 , pp. 860-877
    • Skoulidis, F.1    Byers, L.A.2    Diao, L.3    Papadimitrakopoulou, V.A.4    Tong, P.5    Izzo, J.6
  • 140
    • 79955662435 scopus 로고    scopus 로고
    • Stimulation of human whole-body energy expenditure by salsalate is fueled by higher lipid oxidation under fasting conditions and by higher oxidative glucose disposal under insulin-stimulated conditions
    • Meex RC, Phielix E, Moonen-Kornips E, Schrauwen P, Hesselink MK. Stimulation of human whole-body energy expenditure by salsalate is fueled by higher lipid oxidation under fasting conditions and by higher oxidative glucose disposal under insulin-stimulated conditions. J Clin Endocrinol Metab 2011; 96: 1415–1423.
    • (2011) J Clin Endocrinol Metab , vol.96 , pp. 1415-1423
    • Meex, R.C.1    Phielix, E.2    Moonen-Kornips, E.3    Schrauwen, P.4    Hesselink, M.K.5
  • 141
    • 65349152488 scopus 로고    scopus 로고
    • Aspirin and non-steroidal anti-inflammatory drugs for cancer prevention: An international consensus statement
    • Cuzick J, Otto F, Baron JA, Brown PH, Burn J, Greenwald P et al. Aspirin and non-steroidal anti-inflammatory drugs for cancer prevention: an international consensus statement. Lancet Oncol 2009; 10: 501–507.
    • (2009) Lancet Oncol , vol.10 , pp. 501-507
    • Cuzick, J.1    Otto, F.2    Baron, J.A.3    Brown, P.H.4    Burn, J.5    Greenwald, P.6
  • 142
    • 84942115958 scopus 로고    scopus 로고
    • Metformin and inflammation: Its potential beyond glucose-lowering effect
    • Saisho Y. Metformin and inflammation: its potential beyond glucose-lowering effect. Endocr Metab Immune Disord Drug Targets 2015; 15: 196–205.
    • (2015) Endocr Metab Immune Disord Drug Targets , vol.15 , pp. 196-205
    • Saisho, Y.1


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