메뉴 건너뛰기




Volumn 16, Issue 7, 2012, Pages 729-742

Targeting the liver kinase B1/AMP-activated protein kinase pathway as a therapeutic strategy for hematological malignancies

Author keywords

AMPK; leukemias; LKB1; metformin; translation

Indexed keywords

5 AMINO 4 IMIDAZOLECARBOXAMIDE RIBOSIDE; 6,7 DIHYDRO 4 HYDROXY 3 (2' HYDROXY 1,1' BIPHENYL 4 YL) 6 OXOTHIENO[2,3 B]PYRIDINE 5 CARBONITRILE; ADENOSINE PHOSPHATE; ASPARAGINASE; BCR ABL PROTEIN; BERBERINE; CASPASE; DEXAMETHASONE; DOXORUBICIN; EPIGALLOCATECHIN GALLATE; GALEGINE; HISPIDULIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; IMATINIB; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; METFORMIN; METHOTREXATE; NILOTINIB; ONCOPROTEIN; PHENFORMIN; PIOGLITAZONE; RAPAMYCIN; RAPAMYCIN DERIVATIVE; REACTIVE NITROGEN SPECIES; RESVERATROL; ROSIGLITAZONE; TEMSIROLIMUS; TUMOR SUPPRESSOR PROTEIN; UNINDEXED DRUG; VINCRISTINE;

EID: 84862558416     PISSN: 14728222     EISSN: 17447631     Source Type: Journal    
DOI: 10.1517/14728222.2012.694869     Document Type: Review
Times cited : (38)

References (143)
  • 1
    • 80053035284 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An energy sensor that regulates all aspects of cell function
    • A comprehensive and update review on regulation and function of AMPK
    • Hardie DG. AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. Genes Dev 2011;25:1895-908 A comprehensive and update review on regulation and function of AMPK.
    • (2011) Genes Dev , vol.25 , pp. 1895-1908
    • Hardie, D.G.1
  • 4
    • 79956088595 scopus 로고    scopus 로고
    • The long and winding road to rational treatment of cancer associated with LKB1/AMPK/TSC/mTORC1 signaling
    • van Veelen W, Korsse SE, van de Laar L, Peppelenbosch MP. The long and winding road to rational treatment of cancer associated with LKB1/AMPK/TSC/mTORC1 signaling. Oncogene 2011;30:2289-303
    • (2011) Oncogene , vol.30 , pp. 2289-2303
    • Van Veelen, W.1    Korsse, S.E.2    Van De Laar, L.3    Peppelenbosch, M.P.4
  • 6
    • 64549113040 scopus 로고    scopus 로고
    • Somatic LKB1 mutations promote cervical cancer progression
    • Wingo SN, Gallardo TD, Akbay EA, et al. Somatic LKB1 mutations promote cervical cancer progression. PLoS ONE 2009;4:e5137
    • (2009) PLoS ONE , vol.4
    • Wingo, S.N.1    Gallardo, T.D.2    Akbay, E.A.3
  • 7
    • 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, 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
  • 10
    • 0012889321 scopus 로고    scopus 로고
    • Acadesine activates AMPK and induces apoptosis in B-cell chronic lymphocytic leukemia cells but not in T lymphocytes
    • DOI 10.1182/blood-2002-07-2339
    • Campas C, Lopez JM, Santidrian AF, et al. Acadesine activates AMPK and induces apoptosis in B-cell chronic lymphocytic leukemia cells but not in T lymphocytes. Blood 2003;101:3674-80 The first paper demonstrating AMPK activation by AICAR in a preclinical setting of a hematological disorder. (Pubitemid 36857958)
    • (2003) Blood , vol.101 , Issue.9 , pp. 3674-3680
    • Campas, C.1    Lopez, J.M.2    Santidrian, A.F.3    Barragan, M.4    Bellosillo, B.5    Colomer, D.6    Gil, J.7
  • 11
    • 34548653197 scopus 로고    scopus 로고
    • Activation of adenosine monophosphate activated protein kinase inhibits growth of multiple myeloma cells
    • DOI 10.1016/j.yexcr.2007.06.020, PII S0014482707002790
    • Baumann P, Mandl-Weber S, Emmerich B, et al. Activation of adenosine monophosphate activated protein kinase inhibits growth of multiple myeloma cells. Exp Cell Res 2007;313:3592-603 First paper highlighting AMPK as a possible therapeutic target in MM. (Pubitemid 47404540)
    • (2007) Experimental Cell Research , vol.313 , Issue.16 , pp. 3592-3603
    • Baumann, P.1    Mandl-Weber, S.2    Emmerich, B.3    Straka, C.4    Schmidmaier, R.5
  • 12
    • 64849110053 scopus 로고    scopus 로고
    • Stabilization and activation of p53 downregulates mTOR signaling through AMPK in mantle cell lymphoma
    • Evidence of the existence of p53/AMPK/mTORC1 signaling in MLC
    • Drakos E, Atsaves V, Li J, et al. Stabilization and activation of p53 downregulates mTOR signaling through AMPK in mantle cell lymphoma. Leukemia 2009;23:784-90 Evidence of the existence of p53/AMPK/mTORC1 signaling in MLC.
    • (2009) Leukemia , vol.23 , pp. 784-790
    • Drakos, E.1    Atsaves, V.2    Li, J.3
  • 13
    • 76249124608 scopus 로고    scopus 로고
    • Resveratrol promotes autophagic cell death in chronic myelogenous leukemia cells via JNK-mediated p62/ SQSTM1 expression and AMPK activation
    • Puissant A, Robert G, Fenouille N, et al. Resveratrol promotes autophagic cell death in chronic myelogenous leukemia cells via JNK-mediated p62/ SQSTM1 expression and AMPK activation. Cancer Res 2010;70:1042-52
    • (2010) Cancer Res , vol.70 , pp. 1042-1052
    • Puissant, A.1    Robert, G.2    Fenouille, N.3
  • 14
    • 78549283186 scopus 로고    scopus 로고
    • The LKB1/AMPK signaling pathway has tumor suppressor activity in acute myeloid leukemia through the repression of mTOR-dependent oncogenic mRNA translation
    • An extremely comprehensive paper on AMPK/mTORC1-dependent control of translation in AML cells
    • Green AS, Chapuis N, Maciel TT, et al. The LKB1/AMPK signaling pathway has tumor suppressor activity in acute myeloid leukemia through the repression of mTOR-dependent oncogenic mRNA translation. Blood 2010;116:4262-73 An extremely comprehensive paper on AMPK/mTORC1-dependent control of translation in AML cells.
    • (2010) Blood , vol.116 , pp. 4262-4273
    • Green, A.S.1    Chapuis, N.2    Maciel, T.T.3
  • 15
    • 84856757946 scopus 로고    scopus 로고
    • AMP-dependent kinase/mammalian target of rapamycin complex 1 signaling in T-cell acute lymphoblastic leukemia: Therapeutic implications
    • Grimaldi C, Chiarini F, Tabellini G, et al. AMP-dependent kinase/mammalian target of rapamycin complex 1 signaling in T-cell acute lymphoblastic leukemia: therapeutic implications. Leukemia 2010;26:91-100
    • (2010) Leukemia , vol.26 , pp. 91-100
    • Grimaldi, C.1    Chiarini, F.2    Tabellini, G.3
  • 16
    • 84862908818 scopus 로고    scopus 로고
    • AMPK and mTOR in cellular energy homeostasis and drug targets
    • An update review on AMPK/mTOR signaling as a novel drug target
    • Inoki K, Kim J, Guan KL. AMPK and mTOR in cellular energy homeostasis and drug targets. Annu Rev Pharmacol Toxicol 2012;52:381-400 An update review on AMPK/mTOR signaling as a novel drug target.
    • (2012) Annu Rev Pharmacol Toxicol , vol.52 , pp. 381-400
    • Inoki, K.1    Kim, J.2    Guan, K.L.3
  • 17
    • 34648828532 scopus 로고    scopus 로고
    • AMP-activated/SNF1 protein kinases: Conserved guardians of cellular energy
    • DOI 10.1038/nrm2249, PII NRM2249
    • Hardie DG. AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy. Nat Rev Mol Cell Biol 2007;8:774-85 (Pubitemid 47462132)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 774-785
    • Hardie, D.G.1
  • 19
    • 0033230853 scopus 로고    scopus 로고
    • AMP deamination and purine exchange in human skeletal muscle during and after intense exercise
    • DOI 10.1111/j.1469-7793.1999.00909.x
    • Hellsten Y, Richter EA, Kiens B, Bangsbo J. AMP deamination and purine exchange in human skeletal muscle during and after intense exercise. J Physiol 1999;520:909-20 (Pubitemid 29533045)
    • (1999) Journal of Physiology , vol.520 , Issue.3 , pp. 909-920
    • Hellsten, Y.1    Richter, E.A.2    Kiens, B.3    Bangsbo, J.4
  • 20
    • 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, et al. 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;270:27186-91
    • (1995) J Biol Chem , vol.270 , pp. 27186-27191
    • Hawley, S.A.1    Selbert, M.A.2    Goldstein, E.G.3
  • 21
    • 79954517977 scopus 로고    scopus 로고
    • Structure of mammalian AMPK and its regulation by ADP
    • Xiao B, Sanders MJ, Underwood E, et al. Structure of mammalian AMPK and its regulation by ADP. Nature 2011;472:230-3
    • (2011) Nature , vol.472 , pp. 230-233
    • Xiao, B.1    Sanders, M.J.2    Underwood, E.3
  • 22
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase
    • DOI 10.1016/j.cmet.2005.05.009, PII S155041310500166X
    • Hawley SA, Pan DA, Mustard KJ, et al. Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. Cell Metab 2005;2:9-19 (Pubitemid 43239821)
    • (2005) Cell Metabolism , vol.2 , Issue.1 , pp. 9-19
    • Hawley, S.A.1    Pan, D.A.2    Mustard, K.J.3    Ross, L.4    Bain, J.5    Edelman, A.M.6    Frenguelli, B.G.7    Hardie, D.G.8
  • 24
    • 33748747706 scopus 로고    scopus 로고
    • Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro
    • DOI 10.1074/jbc.M604399200
    • 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;281:25336-43 (Pubitemid 44401921)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.35 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.-P.2    Carlson, M.3
  • 26
    • 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;10:1247-55
    • (2000) Curr Biol , vol.10 , pp. 1247-1255
    • Marsin, A.S.1    Bertrand, L.2    Rider, M.H.3
  • 27
    • 0025192341 scopus 로고
    • Location and fuction of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase
    • DOI 10.1111/j.1432-1033.1990.tb15293.x
    • Davies SP, Sim AT, Hardie DG. Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase. Eur J Biochem 1990;187:183-90 (Pubitemid 20040376)
    • (1990) European Journal of Biochemistry , vol.187 , Issue.1 , pp. 183-190
    • Davies, S.P.1    Sim, A.T.R.2    Hardie, D.G.3
  • 28
    • 0036863086 scopus 로고    scopus 로고
    • Regulation of mammalian acetyl-CoA carboxylase
    • DOI 10.1042/BST0301059
    • Munday MR. Regulation of mammalian acetyl-CoA carboxylase. Biochem Soc Trans 2002;30:1059-64 (Pubitemid 36002406)
    • (2002) Biochemical Society Transactions , vol.30 , Issue.6 , pp. 1059-1064
    • Munday, M.R.1
  • 29
    • 50949087166 scopus 로고    scopus 로고
    • Malonyl-CoA, a key signaling molecule in mammalian cells
    • Saggerson D. Malonyl-CoA, a key signaling molecule in mammalian cells. Annu Rev Nutr 2008;28:253-72
    • (2008) Annu Rev Nutr , vol.28 , pp. 253-272
    • Saggerson, D.1
  • 30
    • 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
    • DOI 10.1111/j.1432-1033.1989.tb15186.x
    • 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;186:129-36 (Pubitemid 20015135)
    • (1989) European Journal of Biochemistry , vol.186 , Issue.1-2 , pp. 129-136
    • Carling, D.1    Clarke, P.R.2    Zammit, V.A.3    Hardie, D.G.4
  • 31
    • 27144506185 scopus 로고    scopus 로고
    • The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism
    • Koo SH, Flechner L, Qi L, et al. The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism. Nature 2005;437:1109-11
    • (2005) Nature , vol.437 , pp. 1109-1111
    • Koo, S.H.1    Flechner, L.2    Qi, L.3
  • 33
    • 38749110036 scopus 로고    scopus 로고
    • Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators
    • DOI 10.1042/BJ20071114
    • Chen S, Murphy J, Toth R, et al. Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators. Biochem J 2008;409:449-59 (Pubitemid 351184963)
    • (2008) Biochemical Journal , vol.409 , Issue.2 , pp. 449-459
    • Chen, S.1    Murphy, J.2    Toth, R.3    Campbell, D.G.4    Morrice, N.A.5    Mackintosh, C.6
  • 35
    • 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, et al. Class IIa histone deacetylases are hormone-activated regulators of FOXO and mammalian glucose homeostasis. Cell 2011;145:607-21
    • (2011) Cell , vol.145 , pp. 607-621
    • Mihaylova, M.M.1    Vasquez, D.S.2    Ravnskjaer, K.3
  • 36
    • 42449161465 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5
    • McGee SL, van Denderen BJ, Howlett KF, et al. AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5. Diabetes 2008;57:860-7
    • (2008) Diabetes , vol.57 , pp. 860-867
    • McGee, S.L.1    Van Denderen, B.J.2    Howlett, K.F.3
  • 37
    • 65349122785 scopus 로고    scopus 로고
    • Inhibition of contraction-stimulated AMP-activated protein kinase inhibits contraction-stimulated increases in PAS-TBC1D1 and glucose transport without altering PAS-AS160 in rat skeletal muscle
    • Funai K, Cartee GD. Inhibition of contraction-stimulated AMP-activated protein kinase inhibits contraction-stimulated increases in PAS-TBC1D1 and glucose transport without altering PAS-AS160 in rat skeletal muscle. Diabetes 2009;58:1096-104
    • (2009) Diabetes , vol.58 , pp. 1096-1104
    • Funai, K.1    Cartee, G.D.2
  • 38
    • 79251507286 scopus 로고    scopus 로고
    • Metformin induces Rab4 through AMPK and modulates GLUT4 translocation in skeletal muscle cells
    • Lee JO, Lee SK, Jung JH, et al. Metformin induces Rab4 through AMPK and modulates GLUT4 translocation in skeletal muscle cells. J Cell Physiol 2011;226:974-81
    • (2011) J Cell Physiol , vol.226 , pp. 974-981
    • Lee, J.O.1    Lee, S.K.2    Jung, J.H.3
  • 39
    • 46749125376 scopus 로고    scopus 로고
    • Transcriptional control of mitochondrial biogenesis: The central role of PGC-1alpha
    • DOI 10.1093/cvr/cvn098
    • Ventura-Clapier R, Garnier A, Veksler V. Transcriptional control of mitochondrial biogenesis: the central role of PGC-1alpha. Cardiovasc Res 2008;79:208-17 (Pubitemid 351951611)
    • (2008) Cardiovascular Research , vol.79 , Issue.2 , pp. 208-217
    • Ventura-Clapier, R.1    Garnier, A.2    Veksler, V.3
  • 40
    • 77249156847 scopus 로고    scopus 로고
    • Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle
    • Canto C, Jiang LQ, Deshmukh AS, et al. Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle. Cell Metab 2010;11:213-19
    • (2010) Cell Metab , vol.11 , pp. 213-219
    • Canto, C.1    Jiang, L.Q.2    Deshmukh, A.S.3
  • 42
    • 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;13:132-41
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 43
    • 77951221542 scopus 로고    scopus 로고
    • The role of the Atg1/ULK1 complex in autophagy regulation
    • Mizushima N. The role of the Atg1/ULK1 complex in autophagy regulation. Curr Opin Cell Biol 2011;22:132-9
    • (2011) Curr Opin Cell Biol , vol.22 , pp. 132-139
    • Mizushima, N.1
  • 44
    • 78650510609 scopus 로고    scopus 로고
    • MTOR: From growth signal integration to cancer, diabetes and ageing
    • Zoncu R, Efeyan A, Sabatini DM. mTOR: from growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol 2011;12:21-35
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 46
    • 34548693675 scopus 로고    scopus 로고
    • S6k
    • DOI 10.1016/j.febslet.2007.08.045, PII S0014579307009222
    • Hornberger TA, Sukhija KB, Wang XR, Chien S. mTOR is the rapamycin-sensitive kinase that confers mechanically-induced phosphorylation of the hydrophobic motif site Thr(389) in p70(S6k). FEBS Lett 2007;581:4562-6 (Pubitemid 47418781)
    • (2007) FEBS Letters , vol.581 , Issue.24 , pp. 4562-4566
    • Hornberger, T.A.1    Sukhija, K.B.2    Wang, X.-R.3    Chien, S.4
  • 47
    • 69249084037 scopus 로고    scopus 로고
    • Mechanism of PDK1-catalyzed Thr- 229 phosphorylation of the S6K1 protein kinase
    • Keshwani MM, Gao X, Harris TK. Mechanism of PDK1-catalyzed Thr- 229 phosphorylation of the S6K1 protein kinase. J Biol Chem 2009;284:22611-24
    • (2009) J Biol Chem , vol.284 , pp. 22611-22624
    • Keshwani, M.M.1    Gao, X.2    Harris, T.K.3
  • 48
    • 79953149505 scopus 로고    scopus 로고
    • Regulation of ribosomal protein S6 phosphorylation by casein kinase 1 and protein phosphatase 1
    • Hutchinson JA, Shanware NP, Chang H, Tibbetts RS. Regulation of ribosomal protein S6 phosphorylation by casein kinase 1 and protein phosphatase 1. J Biol Chem 2011;286:8688-96
    • (2011) J Biol Chem , vol.286 , pp. 8688-8696
    • Hutchinson, J.A.1    Shanware, N.P.2    Chang, H.3    Tibbetts, R.S.4
  • 49
    • 66349138290 scopus 로고    scopus 로고
    • Interferon-dependent engagement of eukaryotic initiation factor 4B via S6 kinase (S6K) and ribosomal protein S6K-mediated signals
    • Kroczynska B, Kaur S, Katsoulidis E, et al. Interferon-dependent engagement of eukaryotic initiation factor 4B via S6 kinase (S6K) and ribosomal protein S6K-mediated signals. Mol Cell Biol 2009;29:2865-75
    • (2009) Mol Cell Biol , vol.29 , pp. 2865-2875
    • Kroczynska, B.1    Kaur, S.2    Katsoulidis, E.3
  • 50
    • 40449091284 scopus 로고    scopus 로고
    • Translation inhibitor Pdcd4 is targeted for degradation during tumor promotion
    • DOI 10.1158/0008-5472.CAN-07-1719
    • Schmid T, Jansen AP, Baker AR, et al. Translation inhibitor Pdcd4 is targeted for degradation during tumor promotion. Cancer Res 2008;68:1254-60 (Pubitemid 351346830)
    • (2008) Cancer Research , vol.68 , Issue.5 , pp. 1254-1260
    • Schmid, T.1    Jansen, A.P.2    Baker, A.R.3    Hegamyer, G.4    Hagan, J.P.5    Colburn, N.H.6
  • 51
    • 84859361694 scopus 로고    scopus 로고
    • TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR
    • Fiesel FC, Weber SS, Supper J, et al. TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR. Nucleic Acids Res 2012;40:2668-82
    • (2012) Nucleic Acids Res , vol.40 , pp. 2668-2682
    • Fiesel, F.C.1    Weber, S.S.2    Supper, J.3
  • 53
    • 79955637310 scopus 로고    scopus 로고
    • The biological and therapeutic relevance of mRNA translation in cancer
    • Blagden SP, Willis AE. The biological and therapeutic relevance of mRNA translation in cancer. Nat Rev Clin Oncol 2011;8:280-91
    • (2011) Nat Rev Clin Oncol , vol.8 , pp. 280-291
    • Blagden, S.P.1    Willis, A.E.2
  • 54
    • 83655212693 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4F: A vulnerability of tumor cells
    • Lee T, Pelletier J. Eukaryotic initiation factor 4F: a vulnerability of tumor cells. Future Med Chem 2012;4:19-31
    • (2012) Future Med Chem , vol.4 , pp. 19-31
    • Lee, T.1    Pelletier, J.2
  • 55
    • 79960271775 scopus 로고    scopus 로고
    • Targeting the translational apparatus to improve leukemia therapy: Roles of the PI3K/PTEN/Akt/mTOR pathway
    • Martelli AM, Evangelisti C, Chappell W, et al. Targeting the translational apparatus to improve leukemia therapy: roles of the PI3K/PTEN/Akt/mTOR pathway. Leukemia 2011;25:1064-79
    • (2011) Leukemia , vol.25 , pp. 1064-1079
    • Martelli, A.M.1    Evangelisti, C.2    Chappell, W.3
  • 56
    • 74849095946 scopus 로고    scopus 로고
    • Targeting translation in acute myeloid leukemia: A new paradigm for therapy?
    • Tamburini J, Green AS, Chapuis N, et al. Targeting translation in acute myeloid leukemia: a new paradigm for therapy? Cell Cycle 2009;8:3893-9
    • (2009) Cell Cycle , vol.8 , pp. 3893-3899
    • Tamburini, J.1    Green, A.S.2    Chapuis, N.3
  • 57
    • 53549113031 scopus 로고    scopus 로고
    • The role of TOR in autophagy regulation from yeast to plants and mammals
    • Diaz-Troya S, Perez-Perez ME, Florencio FJ, Crespo JL. The role of TOR in autophagy regulation from yeast to plants and mammals. Autophagy 2008;4:851-65
    • (2008) Autophagy , vol.4 , pp. 851-865
    • Diaz-Troya, S.1    Perez-Perez, M.E.2    Florencio, F.J.3    Crespo, J.L.4
  • 58
    • 84856800302 scopus 로고    scopus 로고
    • Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: Cross talk, shortcuts, and feedbacks
    • Alers S, Loffler AS, Wesselborg S, Stork B. Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks. Mol Cell Biol 2012;32:2-11
    • (2012) Mol Cell Biol , vol.32 , pp. 2-11
    • Alers, S.1    Loffler, A.S.2    Wesselborg, S.3    Stork, B.4
  • 59
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/Akt pathway
    • Manning BD, Tee AR, Logsdon MN, et al. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/Akt pathway. Mol Cell 2002;10:151-62
    • (2002) Mol Cell , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3
  • 60
    • 34047095297 scopus 로고    scopus 로고
    • The Two TORCs and Akt
    • DOI 10.1016/j.devcel.2007.03.020, PII S1534580707001207
    • Bhaskar PT, Hay N. The two TORCs and Akt. Dev Cell 2007;12:487-502 (Pubitemid 46523652)
    • (2007) Developmental Cell , vol.12 , Issue.4 , pp. 487-502
    • Bhaskar, P.T.1    Hay, N.2
  • 61
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
    • DOI 10.1016/S0092-8674(03)00929-2
    • Inoki K, Zhu T, Guan KL. TSC2 mediates cellular energy response to control cell growth and survival. Cell 2003;115:577-90 (Pubitemid 37506046)
    • (2003) Cell , vol.115 , Issue.5 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.-L.3
  • 62
    • 79952281400 scopus 로고    scopus 로고
    • Inactivation of Rheb by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1
    • Zheng M, Wang YH, Wu XN, et al. Inactivation of Rheb by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1. Nat Cell Biol 2011;13:263-72
    • (2011) Nat Cell Biol , vol.13 , pp. 263-272
    • Zheng, M.1    Wang, Y.H.2    Wu, X.N.3
  • 63
    • 79955389182 scopus 로고    scopus 로고
    • Cell-type-dependent regulation of mTORC1 by REDD1 and the tumor suppressors TSC1/TSC2 and LKB1 in response to hypoxia
    • Wolff NC, Vega-Rubin-de-Celis S, Xie XJ, et al. Cell-type-dependent regulation of mTORC1 by REDD1 and the tumor suppressors TSC1/TSC2 and LKB1 in response to hypoxia. Mol Cell Biol 2011;31:1870-84
    • (2011) Mol Cell Biol , vol.31 , pp. 1870-1884
    • Wolff, N.C.1    Vega-Rubin-de-Celis, S.2    Xie, X.J.3
  • 64
    • 77955287742 scopus 로고    scopus 로고
    • Metformin, independent of AMPK, inhibits mTORC1 in a rag GTPase-dependent manner
    • Kalender A, Selvaraj A, Kim SY, et al. Metformin, independent of AMPK, inhibits mTORC1 in a rag GTPase-dependent manner. Cell Metab 2010;11:390-401
    • (2010) Cell Metab , vol.11 , pp. 390-401
    • Kalender, A.1    Selvaraj, A.2    Kim, S.Y.3
  • 66
    • 3042818799 scopus 로고    scopus 로고
    • Regulation of the TSC pathway by LKB1: Evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome
    • DOI 10.1101/gad.1199104
    • Corradetti MN, Inoki K, Bardeesy N, et al. Regulation of the TSC pathway by LKB1: evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome. Genes Dev 2004;18:1533-8 (Pubitemid 38868905)
    • (2004) Genes and Development , vol.18 , Issue.13 , pp. 1533-1538
    • Corradetti, M.N.1    Inoki, K.2    Bardeesy, N.3    DePinho, R.A.4    Guan, K.-L.5
  • 69
    • 72149093508 scopus 로고    scopus 로고
    • Cardiac-specific deletion of LKB1 leads to hypertrophy and dysfunction
    • Ikeda Y, Sato K, Pimentel DR, et al. Cardiac-specific deletion of LKB1 leads to hypertrophy and dysfunction. J Biol Chem 2009;284:35839-49
    • (2009) J Biol Chem , vol.284 , pp. 35839-35849
    • Ikeda, Y.1    Sato, K.2    Pimentel, D.R.3
  • 70
    • 67749111502 scopus 로고    scopus 로고
    • The LKB1-AMPK pathway: Metabolism and growth control in tumour suppression
    • Shackelford DB, Shaw RJ. The LKB1-AMPK pathway: metabolism and growth control in tumour suppression. Nat Rev Cancer 2009;9:563-75
    • (2009) Nat Rev Cancer , vol.9 , pp. 563-575
    • Shackelford, D.B.1    Shaw, R.J.2
  • 71
    • 80054084051 scopus 로고    scopus 로고
    • Pharmacological management of type 2 diabetes mellitus: An update
    • El-Kaissi S, Sherbeeni S. Pharmacological management of type 2 diabetes mellitus: an update. Curr Diabetes Rev 2011;7:392-405
    • (2011) Curr Diabetes Rev , vol.7 , pp. 392-405
    • El-Kaissi, S.1    Sherbeeni, S.2
  • 72
    • 73349087844 scopus 로고    scopus 로고
    • LKB1 and mammalian target of rapamycin as predictive factors for the anticancer efficacy of metformin
    • Memmott RM, Dennis PA. LKB1 and mammalian target of rapamycin as predictive factors for the anticancer efficacy of metformin. J Clin Oncol 2009;27:e226
    • (2009) J Clin Oncol , vol.27
    • Memmott, R.M.1    Dennis, P.A.2
  • 73
    • 36348950449 scopus 로고    scopus 로고
    • Metformin inhibits mammalian target of rapamycin-dependent translation initiation in breast cancer cells
    • DOI 10.1158/0008-5472.CAN-07-2310
    • Dowling RJ, Zakikhani M, Fantus IG, et al. Metformin inhibits mammalian target of rapamycin-dependent translation initiation in breast cancer cells. Cancer Res 2007;67:10804-12 (Pubitemid 350145909)
    • (2007) Cancer Research , vol.67 , Issue.22 , pp. 10804-10812
    • Dowling, R.J.O.1    Zakikhani, M.2    Fantus, I.G.3    Pollak, M.4    Sonenberg, N.5
  • 74
    • 77956410464 scopus 로고    scopus 로고
    • Use of cells expressing gamma subunit variants to identify diverse mechanisms of AMPK activation
    • Hawley SA, Ross FA, Chevtzoff C, et al. Use of cells expressing gamma subunit variants to identify diverse mechanisms of AMPK activation. Cell Metab 2010;11:554-65
    • (2010) Cell Metab , vol.11 , pp. 554-565
    • Hawley, S.A.1    Ross, F.A.2    Chevtzoff, C.3
  • 75
    • 48649085816 scopus 로고    scopus 로고
    • Regulation of TORC1 by Rag GTPases in nutrient response
    • Kim E, Goraksha-Hicks P, Li L, et al. Regulation of TORC1 by Rag GTPases in nutrient response. Nat Cell Biol 2008;10:935-45
    • (2008) Nat Cell Biol , vol.10 , pp. 935-945
    • Kim, E.1    Goraksha-Hicks, P.2    Li, L.3
  • 78
    • 0035124186 scopus 로고    scopus 로고
    • New oral therapies for type 2 diabetes mellitus: The glitazones or insulin sensitizers
    • DOI 10.1146/annurev.med.52.1.239
    • Mudaliar S, Henry RR. New oral therapies for type 2 diabetes mellitus: the glitazones or insulin sensitizers. Annu Rev Med 2001;52:239-57 (Pubitemid 32195323)
    • (2001) Annual Review of Medicine , vol.52 , pp. 239-257
    • Mudaliar, S.1    Henry, R.R.2
  • 79
    • 0037067666 scopus 로고    scopus 로고
    • The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways
    • DOI 10.1074/jbc.M202489200
    • 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;277:25226-32 (Pubitemid 34951829)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25226-25232
    • Fryer, L.G.D.1    Parbu-Patel, A.2    Carling, D.3
  • 80
    • 33644978143 scopus 로고    scopus 로고
    • Rosiglitazone suppresses human lung carcinoma cell growth through PPARgamma-dependent and PPARgamma-independent signal pathways
    • Han S, Roman J. Rosiglitazone suppresses human lung carcinoma cell growth through PPARgamma-dependent and PPARgamma-independent signal pathways. Mol Cancer Ther 2006;5:430-7
    • (2006) Mol Cancer Ther , vol.5 , pp. 430-437
    • Han, S.1    Roman, J.2
  • 82
    • 77954667427 scopus 로고    scopus 로고
    • Different effects of thiazolidinediones on cardiovascular risk in patients with type 2 diabetes mellitus: Pioglitazone versus rosiglitazone
    • Simo R, Rodriguez A, Caveda E. Different effects of thiazolidinediones on cardiovascular risk in patients with type 2 diabetes mellitus: pioglitazone versus rosiglitazone. Curr Drug Saf 2010;5:234-44
    • (2010) Curr Drug Saf , vol.5 , pp. 234-244
    • Simo, R.1    Rodriguez, A.2    Caveda, E.3
  • 83
    • 0028073143 scopus 로고
    • Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase
    • DOI 10.1016/0014-5793(94)01006-4
    • Sullivan JE, Brocklehurst KJ, Marley AE, et al. Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase. FEBS Lett 1994;353:33-6 (Pubitemid 24312538)
    • (1994) FEBS Letters , vol.353 , Issue.1 , pp. 33-36
    • Sullivan, J.E.1
  • 84
    • 85047689953 scopus 로고
    • 5-Aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells?
    • Corton JM, Gillespie JG, Hawley SA, Hardie DG. 5-aminoimidazole-4- carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells? Eur J Biochem 1995;229:558-65
    • (1995) Eur J Biochem , vol.229 , pp. 558-565
    • Corton, J.M.1    Gillespie, J.G.2    Hawley, S.A.3    Hardie, D.G.4
  • 87
    • 48449084609 scopus 로고    scopus 로고
    • Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: A mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action
    • Turner N, Li JY, Gosby A, et al. Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: a mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action. Diabetes 2008;57:1414-18
    • (2008) Diabetes , vol.57 , pp. 1414-1418
    • Turner, N.1    Li, J.Y.2    Gosby, A.3
  • 90
    • 33746592505 scopus 로고    scopus 로고
    • Increased cancer-related mortality for patients with type 2 diabetes who use sulfonylureas or insulin: Response to Farooki and Schneider [15]
    • DOI 10.2337/dc06-0997
    • Bowker SL, Majumdar SR, Veugelers P, Johnson JA. Increased cancer-related mortality for patients with type 2 diabetes who use sulfonylureas or insulin: response to Farooki and Schneider. Diabetes Care 2006;29:1990-1 (Pubitemid 44156679)
    • (2006) Diabetes Care , vol.29 , Issue.8 , pp. 1990-1991
    • Bowker, S.L.1    Majumdar, S.R.2    Veugelers, P.3    Johnson, J.A.4
  • 91
    • 53749089278 scopus 로고    scopus 로고
    • Antidiabetic medication and prostate cancer risk: A population-based case-control study
    • Murtola TJ, Tammela TL, Lahtela J, Auvinen A. Antidiabetic medication and prostate cancer risk: a population-based case-control study. Am J Epidemiol 2008;168:925-31
    • (2008) Am J Epidemiol , vol.168 , pp. 925-931
    • Murtola, T.J.1    Tammela, T.L.2    Lahtela, J.3    Auvinen, A.4
  • 92
    • 69549097703 scopus 로고    scopus 로고
    • New users of metformin are at low risk of incident cancer: A cohort studyamong people with type 2 diabetes
    • Libby G, Donnelly LA, Donnan PT, et al. New users of metformin are at low risk of incident cancer: a cohort studyamong people with type 2 diabetes. Diabetes Care 2009;32:1620-5
    • (2009) Diabetes Care , vol.32 , pp. 1620-1625
    • Libby, G.1    Donnelly, L.A.2    Donnan, P.T.3
  • 93
    • 84858695046 scopus 로고    scopus 로고
    • Cancer risk in diabetic patients treated with metformin: A systematic review and meta-analysis
    • Noto H, Goto A, Tsujimoto T, Noda M. Cancer risk in diabetic patients treated with metformin: a systematic review and meta-analysis. PloS One 2012;7:1-9
    • (2012) PloS One , vol.7 , pp. 1-9
    • Noto, H.1    Goto, A.2    Tsujimoto, T.3    Noda, M.4
  • 94
    • 79959466358 scopus 로고    scopus 로고
    • Minireview: IGF, Insulin, and cancer
    • Gallagher EJ, LeRoith D. Minireview: IGF, Insulin, and cancer. Endocrinology 2011;152:2546-51
    • (2011) Endocrinology , vol.152 , pp. 2546-2551
    • Gallagher, E.J.1    LeRoith, D.2
  • 95
    • 3543072186 scopus 로고    scopus 로고
    • Overweight, obesity and cancer: Epidemiological evidence and proposed mechanisms
    • Calle EE, Kaaks R. Overweight, obesity and cancer: epidemiological evidence and proposed mechanisms. Nat Rev Cancer 2004;4:579-91 (Pubitemid 39025053)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.8 , pp. 579-591
    • Calle, E.E.1    Kaaks, R.2
  • 96
    • 5144234027 scopus 로고    scopus 로고
    • Insulin therapy and colorectal cancer risk among type 2 diabetes mellitus patients
    • DOI 10.1053/j.gastro.2004.07.011, PII S0016508504012363
    • Yang YX, Hennessy S, Lewis JD. Insulin therapy and colorectal cancer risk among type 2 diabetes mellitus patients. Gastroenterology 2004;127:1044-50 (Pubitemid 39345873)
    • (2004) Gastroenterology , vol.127 , Issue.4 , pp. 1044-1050
    • Yang, Y.-X.1    Hennessy, S.2    Lewis, J.D.3
  • 100
    • 70349883650 scopus 로고    scopus 로고
    • Histological evaluation of AMPK signalling in primary breast cancer
    • Hadad SM, Baker L, Quinlan PR, et al. Histological evaluation of AMPK signalling in primary breast cancer. BMC Cancer 2009;9:307
    • (2009) BMC Cancer , vol.9 , pp. 307
    • Hadad, S.M.1    Baker, L.2    Quinlan, P.R.3
  • 102
    • 77950243447 scopus 로고    scopus 로고
    • Drugging the PI3 kinome: From chemical tools to drugs in the clinic
    • Workman P, Clarke PA, Raynaud FI, van Montfort RL. Drugging the PI3 kinome: from chemical tools to drugs in the clinic. Cancer Res 2010;70:2146-57
    • (2010) Cancer Res , vol.70 , pp. 2146-2157
    • Workman, P.1    Clarke, P.A.2    Raynaud, F.I.3    Van Montfort, R.L.4
  • 103
    • 77952116629 scopus 로고    scopus 로고
    • Metformin in cancer therapy: A new perspective for an old antidiabetic drug?
    • Ben Sahra I, Le Marchand-Brustel Y, Tanti JF, Bost F. Metformin in cancer therapy: a new perspective for an old antidiabetic drug? Mol Cancer Ther 2010;9:1092-9
    • (2010) Mol Cancer Ther , vol.9 , pp. 1092-1099
    • Ben Sahra, I.1    Le Marchand-Brustel, Y.2    Tanti, J.F.3    Bost, F.4
  • 105
    • 84857975015 scopus 로고    scopus 로고
    • Metformin: Multi-faceted protection against cancer
    • Del Barco S, Vazquez-Martin A, Cufi S, et al. Metformin: multi-faceted protection against cancer. Oncotarget 2011;2:896-917
    • (2011) Oncotarget , vol.2 , pp. 896-917
    • Del Barco, S.1    Vazquez-Martin, A.2    Cufi, S.3
  • 106
    • 83555164657 scopus 로고    scopus 로고
    • Metformin and neoplasia: Implications and indications
    • Aljada A, Mousa SA. Metformin and neoplasia: implications and indications. Pharmacol Ther 2012;133:108-15
    • (2012) Pharmacol Ther , vol.133 , pp. 108-115
    • Aljada, A.1    Mousa, S.A.2
  • 107
    • 80054108407 scopus 로고    scopus 로고
    • Signal transduction inhibitors in chronic lymphocytic leukemia
    • Ma S, Rosen ST. Signal transduction inhibitors in chronic lymphocytic leukemia. Curr Opin Oncol 2011;23:601-8
    • (2011) Curr Opin Oncol , vol.23 , pp. 601-608
    • Ma, S.1    Rosen, S.T.2
  • 108
    • 77958198168 scopus 로고    scopus 로고
    • AICAR induces apoptosis independently of AMPK and p53 through up-regulation of the BH3-only proteins BIM and NOXA in chronic lymphocytic leukemia cells
    • Santidrian AF, Gonzalez-Girones DM, et al. AICAR induces apoptosis independently of AMPK and p53 through up-regulation of the BH3-only proteins BIM and NOXA in chronic lymphocytic leukemia cells. Blood 2010;116:3023-32
    • (2010) Blood , vol.116 , pp. 3023-3032
    • Santidrian, A.F.1    Gonzalez-Girones, D.M.2
  • 109
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • DOI 10.1038/sj.onc.1210220, PII 1210220
    • Adams JM, Cory S. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 2007;26:1324-37 (Pubitemid 46328466)
    • (2007) Oncogene , vol.26 , Issue.9 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 110
    • 70849113936 scopus 로고    scopus 로고
    • Acadesine kills chronic myelogenous leukemia (CML) cells through PKC-dependent induction of autophagic cell death
    • An example of how AICAR induces AMPK-independent cytotoxic effects in CML cells
    • Robert G, Ben Sahra I, Puissant A, et al. Acadesine kills chronic myelogenous leukemia (CML) cells through PKC-dependent induction of autophagic cell death. PLoS One 2009;4:e7889 An example of how AICAR induces AMPK-independent cytotoxic effects in CML cells.
    • (2009) PLoS One , vol.4
    • Robert, G.1    Ben Sahra, I.2    Puissant, A.3
  • 111
    • 79959250885 scopus 로고    scopus 로고
    • Optimizing the selection of kinase inhibitors for chronic myeloid leukemia patients
    • Hiwase DK, Yeung DT, White DL. Optimizing the selection of kinase inhibitors for chronic myeloid leukemia patients. Expert Rev Hematol 2011;4:285-99
    • (2011) Expert Rev Hematol , vol.4 , pp. 285-299
    • Hiwase, D.K.1    Yeung, D.T.2    White, D.L.3
  • 112
    • 83455225509 scopus 로고    scopus 로고
    • Antileukemic effects of AMPK activators on BCR-ABL-expressing cells
    • Vakana E, Altman JK, Glaser H, et al. Antileukemic effects of AMPK activators on BCR-ABL-expressing cells. Blood 2011;118:6399-402
    • (2011) Blood , vol.118 , pp. 6399-6402
    • Vakana, E.1    Altman, J.K.2    Glaser, H.3
  • 113
    • 77955354069 scopus 로고    scopus 로고
    • AMPK- and p62/SQSTM1-dependent autophagy mediate Resveratrol-induced cell death in chronic myelogenous leukemia
    • Puissant A, Auberger P. AMPK- and p62/SQSTM1-dependent autophagy mediate Resveratrol-induced cell death in chronic myelogenous leukemia. Autophagy 2010;6:655-7
    • (2010) Autophagy , vol.6 , pp. 655-657
    • Puissant, A.1    Auberger, P.2
  • 114
    • 79952078495 scopus 로고    scopus 로고
    • Biology, risk stratification, and therapy of pediatric acute leukemias: An update
    • Pui CH, Carroll WL, Meshinchi S, Arceci RJ. Biology, risk stratification, and therapy of pediatric acute leukemias: an update. J Clin Oncol 2011; 29:551-65
    • (2011) J Clin Oncol , vol.29 , pp. 551-565
    • Pui, C.H.1    Carroll, W.L.2    Meshinchi, S.3    Arceci, R.J.4
  • 115
    • 34547981921 scopus 로고    scopus 로고
    • Cytotoxic effect of 5-aminoimidazole-4-carboxamide- 1-beta-4- ribofuranoside (AICAR) on childhood acute lymphoblastic leukemia (ALL) cells: Implication for targeted therapy
    • First report of AICAR as an activator of AMPK in B-ALL cells
    • Sengupta TK, Leclerc GM, Hsieh-Kinser TT, et al. Cytotoxic effect of 5-aminoimidazole-4-carboxamide- 1-beta-4-ribofuranoside (AICAR) on childhood acute lymphoblastic leukemia (ALL) cells: implication for targeted therapy. Mol Cancer 2007;6:46 First report of AICAR as an activator of AMPK in B-ALL cells.
    • (2007) Mol Cancer , vol.6 , pp. 46
    • Sengupta, T.K.1    Leclerc, G.M.2    Hsieh-Kinser, T.T.3
  • 116
    • 78649348967 scopus 로고    scopus 로고
    • Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress
    • Sengupta S, Peterson TR, Sabatini DM. Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress. Mol Cell 2010;40:310-22
    • (2010) Mol Cell , vol.40 , pp. 310-322
    • Sengupta, S.1    Peterson, T.R.2    Sabatini, D.M.3
  • 117
    • 38049187096 scopus 로고    scopus 로고
    • Mammalian target of rapamycin (mTOR) inhibition activates phosphatidylinositol 3-kinase/Akt by up-regulating insulin-like growth factor-1 receptor signaling in acute myeloid leukemia: Rationale for therapeutic inhibition of both pathways
    • Tamburini J, Chapuis N, Bardet V, et al. Mammalian target of rapamycin (mTOR) inhibition activates phosphatidylinositol 3-kinase/Akt by up-regulating insulin-like growth factor-1 receptor signaling in acute myeloid leukemia: rationale for therapeutic inhibition of both pathways. Blood 2008;111:379-82
    • (2008) Blood , vol.111 , pp. 379-382
    • Tamburini, J.1    Chapuis, N.2    Bardet, V.3
  • 118
    • 77956875005 scopus 로고    scopus 로고
    • AMPK-induced activation of Akt by AICAR is mediated by IGF-1R dependent and independent mechanisms in acute lymphoblastic leukemia
    • Leclerc GM, Leclerc GJ, Fu G, Barredo JC. AMPK-induced activation of Akt by AICAR is mediated by IGF-1R dependent and independent mechanisms in acute lymphoblastic leukemia. J Mol Signal 2010;5:15
    • (2010) J Mol Signal , vol.5 , pp. 15
    • Leclerc, G.M.1    Leclerc, G.J.2    Fu, G.3    Barredo, J.C.4
  • 119
    • 84856756817 scopus 로고    scopus 로고
    • ETV6-RUNX1-positive childhood acute lymphoblastic leukemia: Improved outcome with contemporary therapy
    • Bhojwani D, Pei D, Sandlund JT, et al. ETV6-RUNX1-positive childhood acute lymphoblastic leukemia: improved outcome with contemporary therapy. Leukemia 2012;26:265-70
    • (2012) Leukemia , vol.26 , pp. 265-270
    • Bhojwani, D.1    Pei, D.2    Sandlund, J.T.3
  • 120
    • 79955755022 scopus 로고    scopus 로고
    • AMPK and Akt determine apoptotic cell death following perturbations of one-carbon metabolism by regulating ER stress in acute lymphoblastic leukemia
    • A paper highlighting the cross-talks between AMPK and Akt in B-ALL cells
    • Kuznetsov JN, Leclerc GJ, Leclerc GM, Barredo JC. AMPK and Akt determine apoptotic cell death following perturbations of one-carbon metabolism by regulating ER stress in acute lymphoblastic leukemia. Mol Cancer Ther 2011;10:437-47 A paper highlighting the cross-talks between AMPK and Akt in B-ALL cells.
    • (2011) Mol Cancer Ther , vol.10 , pp. 437-447
    • Kuznetsov, J.N.1    Leclerc, G.J.2    Leclerc, G.M.3    Barredo, J.C.4
  • 121
    • 66449117931 scopus 로고    scopus 로고
    • AMP-activated protein kinase promotes human prostate cancer cell growth and survival
    • Park HU, Suy S, Danner M, et al. AMP-activated protein kinase promotes human prostate cancer cell growth and survival. Mol Cancer Ther 2009;8:733-41
    • (2009) Mol Cancer Ther , vol.8 , pp. 733-741
    • Park, H.U.1    Suy, S.2    Danner, M.3
  • 123
    • 55849138418 scopus 로고    scopus 로고
    • PTEN posttranslational inactivation and hyperactivation of the PI3K/Akt pathway sustain primary T cell leukemia viability
    • Silva A, Yunes JA, Cardoso BA, et al. PTEN posttranslational inactivation and hyperactivation of the PI3K/Akt pathway sustain primary T cell leukemia viability. J Clin Invest 2008;118:3762-74
    • (2008) J Clin Invest , vol.118 , pp. 3762-3774
    • Silva, A.1    Yunes, J.A.2    Cardoso, B.A.3
  • 124
    • 77950518606 scopus 로고    scopus 로고
    • Genome-wide RNA-mediated interference screen identifies miR-19 targets in Notch-induced T-cellacute lymphoblastic leukaemia
    • Mavrakis KJ, Wolfe AL, Oricchio E, et al. Genome-wide RNA-mediated interference screen identifies miR-19 targets in Notch-induced T-cellacute lymphoblastic leukaemia. Nat Cell Biol 2010;12:372-9
    • (2010) Nat Cell Biol , vol.12 , pp. 372-379
    • Mavrakis, K.J.1    Wolfe, A.L.2    Oricchio, E.3
  • 125
    • 13544271135 scopus 로고    scopus 로고
    • Acadesine induces apoptosis in B cells from mantle cell lymphoma and splenic marginal zone lymphoma [4]
    • DOI 10.1038/sj.leu.2403593
    • Campas C, Santidrian AF, Domingo A, Gil J. Acadesine induces apoptosis in B cells from mantle cell lymphoma and splenic marginal zone lymphoma. Leukemia 2005;19:292-4 (Pubitemid 40220598)
    • (2005) Leukemia , vol.19 , Issue.2 , pp. 292-294
    • Campas, C.1    Santidrian, A.F.2    Domingo, A.3    Gil, J.4
  • 126
    • 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;134:451-60
    • (2008) Cell , vol.134 , pp. 451-460
    • Budanov, A.V.1    Karin, M.2
  • 127
    • 0037103193 scopus 로고    scopus 로고
    • Functional interleukin-7 receptors (IL-7Rs) are expressed by marrow stromal cells: Binding of IL-7 increases levels of IL-6 mRNA and secreted protein
    • DOI 10.1182/blood-2002-01-0062
    • Iwata M, Graf L, Awaya N, Torok-Storb B. Functional interleukin-7 receptors (IL-7Rs) are expressed by marrow stromal cells: binding of IL-7 increases levels of IL-6 mRNA and secreted protein. Blood 2002;100:1318-25 (Pubitemid 34864287)
    • (2002) Blood , vol.100 , Issue.4 , pp. 1318-1325
    • Iwata, M.1    Graf, L.2    Awaya, N.3    Torok-Storb, B.4
  • 128
    • 75149126171 scopus 로고    scopus 로고
    • Autophagy augmented by troglitazone is independent of EGFR transactivation and correlated with AMP-activated protein kinase signaling
    • Yan J, Yang H, Wang G, et al. Autophagy augmented by troglitazone is independent of EGFR transactivation and correlated with AMP-activated protein kinase signaling. Autophagy 2010;6:67-73
    • (2010) Autophagy , vol.6 , pp. 67-73
    • Yan, J.1    Yang, H.2    Wang, G.3
  • 129
    • 79960845901 scopus 로고    scopus 로고
    • Evidence for biological effects of metformin in operable breast cancer: A pre-operative, window-of-opportunity, randomized trial
    • Hadad S, Iwamoto T, Jordan L, et al. Evidence for biological effects of metformin in operable breast cancer: a pre-operative, window-of-opportunity, randomized trial. Breast Cancer Res Treat 2011;128:783-94
    • (2011) Breast Cancer Res Treat , vol.128 , pp. 783-794
    • Hadad, S.1    Iwamoto, T.2    Jordan, L.3
  • 130
    • 44849099894 scopus 로고    scopus 로고
    • The antidiabetic drug metformin exerts an antitumoral effect in vitro and in vivo through a decrease of cyclin D1 level
    • An example of AMPK-independent cytotoxicity induced by AICAR in Jurkat T-ALL cells
    • Ben Sahra I, Laurent K, Loubat A, et al. The antidiabetic drug metformin exerts an antitumoral effect in vitro and in vivo through a decrease of cyclin D1 level. Oncogene 2008;27:3576-86 An example of AMPK-independent cytotoxicity induced by AICAR in Jurkat T-ALL cells.
    • (2008) Oncogene , vol.27 , pp. 3576-3586
    • Ben Sahra, I.1    Laurent, K.2    Loubat, A.3
  • 131
    • 78349273297 scopus 로고    scopus 로고
    • Dual inhibition of PI3K and mTORC1/2 signaling by NVP-BEZ235 as a new therapeutic strategy for acute myeloid leukemia
    • Chapuis N, Tamburini J, Green AS, et al. Dual inhibition of PI3K and mTORC1/2 signaling by NVP-BEZ235 as a new therapeutic strategy for acute myeloid leukemia. Clin Cancer Res 2011;16:5424-35
    • (2011) Clin Cancer Res , vol.16 , pp. 5424-5435
    • Chapuis, N.1    Tamburini, J.2    Green, A.S.3
  • 132
    • 79955818156 scopus 로고    scopus 로고
    • Targeted inhibition of mTORC1 and mTORC2 by active-site mTOR inhibitors has cytotoxic effects in T-cell acute lymphoblastic leukemia
    • Evangelisti C, Ricci F, Tazzari P, et al. Targeted inhibition of mTORC1 and mTORC2 by active-site mTOR inhibitors has cytotoxic effects in T-cell acute lymphoblastic leukemia. Leukemia 2011;25:781-91
    • (2011) Leukemia , vol.25 , pp. 781-791
    • Evangelisti, C.1    Ricci, F.2    Tazzari, P.3
  • 133
    • 84862012594 scopus 로고    scopus 로고
    • The dual mTORC1 and mTORC2 inhibitor AZD8055 has anti-tumor activity in acute myeloid leukemia
    • In press; doi 10.1038/leu.2011.339
    • Willems L, Chapuis N, Puissant A, et al. The dual mTORC1 and mTORC2 inhibitor AZD8055 has anti-tumor activity in acute myeloid leukemia. Leukemia 2011;In press; doi 10.1038/leu.2011.339
    • (2011) Leukemia
    • Willems, L.1    Chapuis, N.2    Puissant, A.3
  • 134
    • 23044482013 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of the acetyl-Coa-carboxylase-alpha gene induces growth inhibition and apoptosis of prostate cancer cells
    • DOI 10.1158/0008-5472.CAN-05-0571
    • Brusselmans K, De Schrijver E, Verhoeven G, Swinnen JV. RNA interference-mediated silencing of the acetyl-CoA-carboxylase-alpha gene induces growth inhibition and apoptosis of prostate cancer cells. Cancer Res 2005;65:6719-25 (Pubitemid 41060709)
    • (2005) Cancer Research , vol.65 , Issue.15 , pp. 6719-6725
    • Brusselmans, K.1    De Schrijver, E.2    Verhoeven, G.3    Swinnen, J.V.4
  • 135
    • 33744808464 scopus 로고    scopus 로고
    • Acetyl-CoA carboxylase alpha is essential to breast cancer cell survival
    • DOI 10.1158/0008-5472.CAN-05-1489
    • Chajes V, Cambot M, Moreau K, et al. Acetyl-CoA carboxylase alpha is essential to breast cancer cell survival. Cancer Res 2006;66:5287-94 (Pubitemid 43844953)
    • (2006) Cancer Research , vol.66 , Issue.10 , pp. 5287-5294
    • Chajes, V.1    Cambot, M.2    Moreau, K.3    Lenoir, G.M.4    Joulin, V.5
  • 136
    • 84855885803 scopus 로고    scopus 로고
    • Cell cycle regulation in hematopoietic stem cells
    • Pietras EM, Warr MR, Passegue E. Cell cycle regulation in hematopoietic stem cells. J Cell Biol 2011;195:709-20
    • (2011) J Cell Biol , vol.195 , pp. 709-720
    • Pietras, E.M.1    Warr, M.R.2    Passegue, E.3
  • 137
    • 78649811793 scopus 로고    scopus 로고
    • Lkb1 regulates cell cycle and energy metabolism in haematopoietic stem cells
    • An outstanding report on LKB1-dependent, but AMPK-independent, control of HSC cell cycle
    • Nakada D, Saunders TL, Morrison SJ. Lkb1 regulates cell cycle and energy metabolism in haematopoietic stem cells. Nature 2010;468:653-8 An outstanding report on LKB1-dependent, but AMPK-independent, control of HSC cell cycle.
    • (2010) Nature , vol.468 , pp. 653-658
    • Nakada, D.1    Saunders, T.L.2    Morrison, S.J.3
  • 138
    • 78649851511 scopus 로고    scopus 로고
    • The Lkb1 metabolic sensor maintains haematopoietic stem cell survival
    • An outstanding manuscript on LKB1-dependent, but AMPK-independent, control of HSC survival
    • Gurumurthy S, Xie SZ, Alagesan B, et al. The Lkb1 metabolic sensor maintains haematopoietic stem cell survival. Nature 2010;468:659-63 An outstanding manuscript on LKB1-dependent, but AMPK-independent, control of HSC survival.
    • (2010) Nature , vol.468 , pp. 659-663
    • Gurumurthy, S.1    Xie, S.Z.2    Alagesan, B.3
  • 139
    • 78649874959 scopus 로고    scopus 로고
    • Lkb1 regulates quiescence and metabolic homeostasis of haematopoietic stem cells
    • An outstanding paper on LKB1-dependent, but AMPK-independent, control of HSC quiescence
    • Gan B, Hu J, Jiang S, et al. Lkb1 regulates quiescence and metabolic homeostasis of haematopoietic stem cells. Nature 2010;468:701-4 An outstanding paper on LKB1-dependent, but AMPK-independent, control of HSC quiescence.
    • (2010) Nature , vol.468 , pp. 701-704
    • Gan, B.1    Hu, J.2    Jiang, S.3
  • 140
    • 77954955537 scopus 로고    scopus 로고
    • The emerging role of the phosphatidylinositol 3-kinase/Akt/ mammalian target of rapamycin signaling network in normal myelopoiesis and leukemogenesis
    • Martelli AM, Evangelisti C, Chiarini F, et al. The emerging role of the phosphatidylinositol 3-kinase/Akt/ mammalian target of rapamycin signaling network in normal myelopoiesis and leukemogenesis. Biochim Biophys Acta 2010;1803:991-1002
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 991-1002
    • Martelli, A.M.1    Evangelisti, C.2    Chiarini, F.3
  • 141
    • 58249105984 scopus 로고    scopus 로고
    • Targeting the leukemic stem cell: The Holy Grail of leukemia therapy
    • Misaghian N, Ligresti G, Steelman LS, et al. Targeting the leukemic stem cell: the Holy Grail of leukemia therapy. Leukemia 2009;23:25-42
    • (2009) Leukemia , vol.23 , pp. 25-42
    • Misaghian, N.1    Ligresti, G.2    Steelman, L.S.3
  • 142
    • 77949453508 scopus 로고    scopus 로고
    • Targeted elimination of leukemia stem cells; a new therapeutic approach in hemato-oncology
    • ten Cate B, de Bruyn M, Wei Y, et al. Targeted elimination of leukemia stem cells; a new therapeutic approach in hemato-oncology. Curr Drug Targets 2010;11:95-110
    • (2010) Curr Drug Targets , vol.11 , pp. 95-110
    • Ten Cate, B.1    De Bruyn, M.2    Wei, Y.3
  • 143
    • 70350668791 scopus 로고    scopus 로고
    • The 5'adenosine monophosphate-activated protein kinase: Regulating the ebb and flow of cellular energetics
    • Karagounis LG, Hawley JA. The 5'adenosine monophosphate-activated protein kinase: regulating the ebb and flow of cellular energetics. Int J Biochem Cell Biol 2009;41:2360-3
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 2360-2363
    • Karagounis, L.G.1    Hawley, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.