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Volumn 15, Issue 1, 2014, Pages 32-52

Targeting the LKB1 tumor suppressor

Author keywords

AMP activated protein kinase (AMPK); LKB1 (serine threonine kinase 11, STK11); Mutations; Targeting therapeutics; Tumor suppression

Indexed keywords

5 (3 FLUOROPHENYL) N (3 PIPERIDINYL) 3 UREIDO 2 THIOPHENECARBOXAMIDE; 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; 6,7 DIHYDRO 4 HYDROXY 3 (2' HYDROXY 1,1' BIPHENYL 4 YL) 6 OXOTHIENO[2,3 B]PYRIDINE 5 CARBONITRILE; CELECOXIB; CHECKPOINT KINASE 1; CYCLOOXYGENASE 2 INHIBITOR; DASATINIB; EVEROLIMUS; HEAT SHOCK PROTEIN 90 INHIBITOR; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; MAMMALIAN TARGET OF RAPAMYCIN INHIBITOR; METFORMIN; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 2; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; NOVOBIOCIN; PHENFORMIN; PROTEIN KINASE LKB1; PROTEIN P53; RAPAMYCIN; RIDAFOROLIMUS; SALICYLIC ACID; TANESPIMYCIN; TEMSIROLIMUS; UNCLASSIFIED DRUG; K RAS PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; NONSTEROID ANTIINFLAMMATORY AGENT; PROTEINASE ACTIVATED RECEPTOR 1; STAT3 PROTEIN; STRESS ACTIVATED PROTEIN KINASE; VEMURAFENIB;

EID: 84892963416     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/1389450114666140106095811     Document Type: Review
Times cited : (51)

References (262)
  • 1
    • 0032495530 scopus 로고    scopus 로고
    • A serine/threonine kinase gene defective in Peutz-Jeghers syndrome
    • Hemminki A, Markie D, Tomlinson I, et al. A serine/threonine kinase gene defective in Peutz-Jeghers syndrome. Nature 1998; 391: 184-87.
    • (1998) Nature , vol.391 , pp. 184-187
    • Hemminki, A.1    Markie, D.2    Tomlinson, I.3
  • 2
    • 0031012344 scopus 로고    scopus 로고
    • Localization of a susceptibility locus for Peutz-Jeghers syndrome to 19p using comparative genomic hybridization and targeted linkage analysis
    • Hemminki A, Tomlinson I, Markie D, et al. Localization of a susceptibility locus for Peutz-Jeghers syndrome to 19p using comparative genomic hybridization and targeted linkage analysis. Nat Genet 1997; 15: 87-90.
    • (1997) Nat Genet , vol.15 , pp. 87-90
    • Hemminki, A.1    Tomlinson, I.2    Markie, D.3
  • 4
    • 37149042642 scopus 로고    scopus 로고
    • A role for LKB1 gene in human cancer beyond the Peutz-Jeghers syndrome
    • Sanchez-Cespedes M. A role for LKB1 gene in human cancer beyond the Peutz-Jeghers syndrome. Oncogene 2007; 26: 7825-32.
    • (2007) Oncogene , vol.26 , pp. 7825-7832
    • Sanchez-Cespedes, M.1
  • 5
    • 0031974516 scopus 로고    scopus 로고
    • Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase
    • Jenne DE, Reimann H, Nezu J, et al. Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase. Nat Genet 1998; 18: 38-43.
    • (1998) Nat Genet , vol.18 , pp. 38-43
    • Jenne, D.E.1    Reimann, H.2    Nezu, J.3
  • 6
    • 0038614742 scopus 로고    scopus 로고
    • Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD
    • Baas AF, Boudeau J, Sapkota GP, et al. Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD. EMBO J 2003; 22: 3062-72.
    • (2003) EMBO J , vol.22 , pp. 3062-3072
    • Baas, A.F.1    Boudeau, J.2    Sapkota, G.P.3
  • 7
    • 1842581909 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network
    • Brajenovic M, Joberty G, Küster B, Bouwmeester T, Drewes G. Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network. J Biol Chem 2004; 279: 12804-11.
    • (2004) J Biol Chem , vol.279 , pp. 12804-12811
    • Brajenovic, M.1    Joberty, G.2    Küster, B.3    Bouwmeester, T.4    Drewes, G.5
  • 8
    • 0141753981 scopus 로고    scopus 로고
    • MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm
    • Boudeau J, Baas AF, Deak M, et al. MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm. EMBO J 2003; 22: 5102-14.
    • (2003) EMBO J , vol.22 , pp. 5102-5114
    • Boudeau, J.1    Baas, A.F.2    Deak, M.3
  • 9
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade
    • Hawley SA, Boudeau J, Reid JL, et al. Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β 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
    • 10744230065 scopus 로고    scopus 로고
    • LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
    • Woods A, Johnstone SR, Dickerson K, et al. LKB1 is the upstream kinase in the AMP-activated protein kinase cascade. Curr Biol 2003; 13: 2004-08.
    • (2003) Curr Biol , vol.13 , pp. 2004-2008
    • Woods, A.1    Johnstone, S.R.2    Dickerson, K.3
  • 11
    • 1542618348 scopus 로고    scopus 로고
    • The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress
    • Shaw RJ, Kosmatka M, Bardeesy N, et al. The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress. Proc Natl Acad Sci U S A 2004; 101: 3329-35.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 3329-3335
    • Shaw, R.J.1    Kosmatka, M.2    Bardeesy, N.3
  • 12
    • 12144287284 scopus 로고    scopus 로고
    • LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1
    • Lizcano JM, Göransson O, Toth R, et al. LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1. EMBO J 2004; 23: 833-43.
    • (2004) EMBO J , vol.23 , pp. 833-843
    • Lizcano, J.M.1    Göransson, O.2    Toth, R.3
  • 13
    • 84876320551 scopus 로고    scopus 로고
    • LKB1 and AMPK and the cancermetabolism link-ten years after
    • Hardie DG, Alessi DR. LKB1 and AMPK and the cancermetabolism link-ten years after. BMC Biol 2013; 11: 36.
    • (2013) BMC Biol , vol.11 , pp. 36
    • Hardie, D.G.1    Alessi, D.R.2
  • 14
    • 34547926839 scopus 로고    scopus 로고
    • LKB1 modulates lung cancer differentiation and metastasis
    • Ji H, Ramsey MR, Hayes DN, Fan C, et al. LKB1 modulates lung cancer differentiation and metastasis. Nature 2007; 448: 807-10.
    • (2007) Nature , vol.448 , pp. 807-810
    • Ji, H.1    Ramsey, M.R.2    Hayes, D.N.3    Fan, C.4
  • 15
    • 33746905916 scopus 로고    scopus 로고
    • LKB1 mutation in large cell carcinoma of the lung
    • Zhong D, Guo L, de Aguirre I, et al. LKB1 mutation in large cell carcinoma of the lung. Lung Cancer 2006; 53: 285-94.
    • (2006) Lung Cancer , vol.53 , pp. 285-294
    • Zhong, D.1    Guo, L.2    de Aguirre, I.3
  • 16
    • 77249121152 scopus 로고    scopus 로고
    • Homozygous deletion of the STK11/LKB1 locus and the generation of novel fusion transcripts in cervical cancer cells
    • McCabe MT, Powell DR, Zhou W, Vertino PM. Homozygous deletion of the STK11/LKB1 locus and the generation of novel fusion transcripts in cervical cancer cells. Cancer Genet Cytogenet 2010; 197: 130-41.
    • (2010) Cancer Genet Cytogenet , vol.197 , pp. 130-141
    • McCabe, M.T.1    Powell, D.R.2    Zhou, W.3    Vertino, P.M.4
  • 17
    • 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
  • 18
    • 84856215097 scopus 로고    scopus 로고
    • Altered LKB1/CREB-regulated transcription co-activator (CRTC) signaling axis promotes esophageal cancer cell migration and invasion
    • Gu Y, Lin S, Li JL, et al. Altered LKB1/CREB-regulated transcription co-activator (CRTC) signaling axis promotes esophageal cancer cell migration and invasion. Oncogene 2012; 31: 469-79.
    • (2012) Oncogene , vol.31 , pp. 469-479
    • Gu, Y.1    Lin, S.2    Li, J.L.3
  • 19
    • 0037068461 scopus 로고    scopus 로고
    • Loss of the Lkb1 tumour suppressor provokes intestinal polyposis but resistance to transformation
    • Bardeesy N, Sinha M, Hezel AF, et al. Loss of the Lkb1 tumour suppressor provokes intestinal polyposis but resistance to transformation. Nature 2002; 419: 162-7.
    • (2002) Nature , vol.419 , pp. 162-167
    • Bardeesy, N.1    Sinha, M.2    Hezel, A.F.3
  • 20
    • 0036645286 scopus 로고    scopus 로고
    • Inactivation of LKB1/STK11 is a common event in adenocarcinomas of the lung
    • Sanchez-Cespedes M, Parrella P, Esteller M, et al. Inactivation of LKB1/STK11 is a common event in adenocarcinomas of the lung. Cancer Res 2002; 62: 3659-62.
    • (2002) Cancer Res , vol.62 , pp. 3659-3662
    • Sanchez-Cespedes, M.1    Parrella, P.2    Esteller, M.3
  • 21
    • 78049515002 scopus 로고    scopus 로고
    • Lung adenocarcinoma from East Asian never-smokers is a disease largely defined by targetable oncogenic mutant kinases
    • Sun Y, Ren Y, Fang Z, et al. Lung adenocarcinoma from East Asian never-smokers is a disease largely defined by targetable oncogenic mutant kinases. J Clin Oncol 2010; 28: 4616-20.
    • (2010) J Clin Oncol , vol.28 , pp. 4616-4620
    • Sun, Y.1    Ren, Y.2    Fang, Z.3
  • 22
    • 77949469320 scopus 로고    scopus 로고
    • Lkb1 inactivation is sufficient to drive endometrial cancers that are aggressive yet highly responsive to mTOR inhibitor monotherapy
    • Contreras CM, Akbay EA, Gallardo TD, et al. Lkb1 inactivation is sufficient to drive endometrial cancers that are aggressive yet highly responsive to mTOR inhibitor monotherapy. Dis Model Mech 2010; 3: 181-93.
    • (2010) Dis Model Mech , vol.3 , pp. 181-193
    • Contreras, C.M.1    Akbay, E.A.2    Gallardo, T.D.3
  • 23
    • 38849193504 scopus 로고    scopus 로고
    • Loss of Lkb1 provokes highly invasive endometrial adenocarcinomas
    • Contreras CM, Gurumurthy S, Haynie JM, et al. Loss of Lkb1 provokes highly invasive endometrial adenocarcinomas. Cancer Res 2008; 68: 759-66.
    • (2008) Cancer Res , vol.68 , pp. 759-766
    • Contreras, C.M.1    Gurumurthy, S.2    Haynie, J.M.3
  • 24
    • 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
  • 25
    • 0035980097 scopus 로고    scopus 로고
    • LKB1 associates with Brg1 and is necessary for Brg1-induced growth arrest
    • Marignani PA, Kanai F, Carpenter CL. LKB1 associates with Brg1 and is necessary for Brg1-induced growth arrest. J Biol Chem 2001; 276: 32415-8.
    • (2001) J Biol Chem , vol.276 , pp. 32415-32418
    • Marignani, P.A.1    Kanai, F.2    Carpenter, C.L.3
  • 26
    • 1542777034 scopus 로고    scopus 로고
    • Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD
    • Baas AF, Kuipers J, van der Wel NN, et al. Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD. Cell 2004; 116: 457-66.
    • (2004) Cell , vol.116 , pp. 457-466
    • Baas, A.F.1    Kuipers, J.2    van der Wel, N.N.3
  • 27
    • 33846521353 scopus 로고    scopus 로고
    • Regulation of epithelial tight junction assembly and disassembly by AMP-activated protein kinase
    • Zheng B, Cantley LC. Regulation of epithelial tight junction assembly and disassembly by AMP-activated protein kinase. Proc Natl Acad Sci U S A 2007; 104: 819-22.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 819-822
    • Zheng, B.1    Cantley, L.C.2
  • 28
    • 0034964446 scopus 로고    scopus 로고
    • The Peutz-Jegher gene product LKB1 is a mediator of p53-dependent cell death
    • Karuman P, Gozani O, Odze RD, et al. The Peutz-Jegher gene product LKB1 is a mediator of p53-dependent cell death. Mol Cell 2001; 7: 1307-19.
    • (2001) Mol Cell , vol.7 , pp. 1307-1319
    • Karuman, P.1    Gozani, O.2    Odze, R.D.3
  • 29
    • 78649874959 scopus 로고    scopus 로고
    • Lkb1 regulates quiescence and metabolic homeostasis of haematopoietic stem cells
    • Gan B, Hu J, Jiang S, et al. Lkb1 regulates quiescence and metabolic homeostasis of haematopoietic stem cells. Nature 2010; 468: 701-4.
    • (2010) Nature , vol.468 , pp. 701-704
    • Gan, B.1    Hu, J.2    Jiang, S.3
  • 30
    • 78649851511 scopus 로고    scopus 로고
    • The Lkb1 metabolic sensor maintains haematopoietic stem cell survival
    • Gurumurthy S, Xie SZ, Alagesan B, et al. The Lkb1 metabolic sensor maintains haematopoietic stem cell survival. Nature 2010; 468: 659-63.
    • (2010) Nature , vol.468 , pp. 659-663
    • Gurumurthy, S.1    Xie, S.Z.2    Alagesan, B.3
  • 31
    • 78649811793 scopus 로고    scopus 로고
    • Lkb1 regulates cell cycle and energy metabolism in haematopoietic stem cells
    • Nakada D, Saunders TL, Morrison SJ. Lkb1 regulates cell cycle and energy metabolism in haematopoietic stem cells. Nature 2010; 468: 653-8.
    • (2010) Nature , vol.468 , pp. 653-658
    • Nakada, D.1    Saunders, T.L.2    Morrison, S.J.3
  • 32
    • 33847072201 scopus 로고    scopus 로고
    • AMP-activated protein kinase as a drug target
    • Hardie DG. AMP-activated protein kinase as a drug target. Annu Rev Pharmacol Toxicol 2007; 47: 185-210.
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 185-210
    • Hardie, D.G.1
  • 33
    • 80053035284 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An energy sensor that regulates all aspects of cell function
    • Hardie DG. AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. Genes Dev 2011; 25: 1895-908.
    • (2011) Genes Dev , vol.25 , pp. 1895-1908
    • Hardie, D.G.1
  • 34
    • 56049112796 scopus 로고    scopus 로고
    • Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes
    • Scott JW, van Denderen BJ, Jorgensen SB, et al. Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes. Chem Biol 2008; 15: 1220-30.
    • (2008) Chem Biol , vol.15 , pp. 1220-1230
    • Scott, J.W.1    van Denderen, B.J.2    Jorgensen, S.B.3
  • 35
    • 34848850156 scopus 로고    scopus 로고
    • An AMPK-FOXO pathway mediates longevity induced by a novel method of dietary restriction in C. elegans
    • Greer EL, Dowlatshahi D, Banko MR, et al. An AMPK-FOXO pathway mediates longevity induced by a novel method of dietary restriction in C. elegans. Curr Biol 2007; 17: 1646-56.
    • (2007) Curr Biol , vol.17 , pp. 1646-1656
    • Greer, E.L.1    Dowlatshahi, D.2    Banko, M.R.3
  • 36
    • 33745840203 scopus 로고    scopus 로고
    • 5'-AMP-activated protein kinase (AMPK) is induced by low-oxygen and glucose deprivation conditions found in solid-tumor microenvironments
    • Laderoute KR, Amin K, Calaoagan JM, et al. 5'-AMP-activated protein kinase (AMPK) is induced by low-oxygen and glucose deprivation conditions found in solid-tumor microenvironments. Mol Cell Biol 2006; 26: 5336-47.
    • (2006) Mol Cell Biol , vol.26 , pp. 5336-5347
    • Laderoute, K.R.1    Amin, K.2    Calaoagan, J.M.3
  • 37
    • 77956401999 scopus 로고    scopus 로고
    • Metformin and other biguanides in oncology: Advancing the research agenda
    • Pollak M. Metformin and other biguanides in oncology: advancing the research agenda. Cancer Prev Res (Phila) 2010; 3: 1060-5.
    • (2010) Cancer Prev Res (Phila) , vol.3 , pp. 1060-1065
    • Pollak, M.1
  • 38
    • 28844433635 scopus 로고    scopus 로고
    • The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin
    • Shaw RJ, Lamia KA, Vasquez D, et al. The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin. Science 2005; 310: 1642-6.
    • (2005) Science , vol.310 , pp. 1642-1646
    • Shaw, R.J.1    Lamia, K.A.2    Vasquez, D.3
  • 39
    • 84862908818 scopus 로고    scopus 로고
    • AMPK and mTOR in cellular energy homeostasis and drug targets
    • Inoki K, Kim J, Guan KL. AMPK and mTOR in cellular energy homeostasis and drug targets. Annu Rev Pharmacol Toxicol 2012; 52: 381-400.
    • (2012) Annu Rev Pharmacol Toxicol , vol.52 , pp. 381-400
    • Inoki, K.1    Kim, J.2    Guan, K.L.3
  • 40
    • 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
  • 41
    • 80052511813 scopus 로고    scopus 로고
    • The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
    • Mihaylova MM, Shaw RJ. The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. Nat Cell Biol 2011; 13: 1016-23.
    • (2011) Nat Cell Biol , vol.13 , pp. 1016-1023
    • Mihaylova, M.M.1    Shaw, R.J.2
  • 42
    • 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, et al. Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy. Science 2011; 331: 456-61.
    • (2011) Science , vol.331 , pp. 456-461
    • Egan, D.F.1    Shackelford, D.B.2    Mihaylova, M.M.3
  • 43
    • 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: 104-12.
    • (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
  • 44
    • 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, et al. AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice. Cell Metab 2011; 13: 376-88.
    • (2011) Cell Metab , vol.13 , pp. 376-388
    • Li, Y.1    Xu, S.2    Mihaylova, M.M.3
  • 45
    • 33749349202 scopus 로고    scopus 로고
    • Polyphenols stimulate AMP-activated protein kinase, lower lipids, and inhibit accelerated atherosclerosis in diabetic LDL receptor-deficient mice
    • Zang M, Xu S, Maitland-Toolan KA, et al. Polyphenols stimulate AMP-activated protein kinase, lower lipids, and inhibit accelerated atherosclerosis in diabetic LDL receptor-deficient mice. Diabetes 2006; 55: 2180-91.
    • (2006) Diabetes , vol.55 , pp. 2180-2191
    • Zang, M.1    Xu, S.2    Maitland-Toolan, K.A.3
  • 46
    • 9144271181 scopus 로고    scopus 로고
    • AMP-activated protein kinase is required for the lipid-lowering effect of metformin in insulinresistant human HepG2 cells
    • Zang M, Zuccollo A, Hou X, et al. AMP-activated protein kinase is required for the lipid-lowering effect of metformin in insulinresistant human HepG2 cells. J Biol Chem 2004; 279: 47898-905.
    • (2004) J Biol Chem , vol.279 , pp. 47898-47905
    • Zang, M.1    Zuccollo, A.2    Hou, X.3
  • 47
    • 79251556232 scopus 로고    scopus 로고
    • Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-β peptide degradation
    • Vingtdeux V, Chandakkar P, Zhao H, d'Abramo C, Davies P, Marambaud P. Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-β peptide degradation. FASEB J 2011; 25: 219-31.
    • (2011) FASEB J , vol.25 , pp. 219-231
    • Vingtdeux, V.1    Chandakkar, P.2    Zhao, H.3    d'Abramo, C.4    Davies, P.5    Marambaud, P.6
  • 48
    • 3042818799 scopus 로고    scopus 로고
    • Regulation of the TSC pathway by LKB1: Evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome
    • Corradetti MN, Inoki K, Bardeesy N, DePinho RA, Guan KL. 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.
    • (2004) Genes Dev , vol.18 , pp. 1533-1538
    • Corradetti, M.N.1    Inoki, K.2    Bardeesy, N.3    DePinho, R.A.4    Guan, K.L.5
  • 49
    • 33748153690 scopus 로고    scopus 로고
    • TSC2 integrates Wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth
    • Inoki K, Ouyang H, Zhu T, et al. TSC2 integrates Wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth. Cell 2006; 126: 955-68.
    • (2006) Cell , vol.126 , pp. 955-968
    • Inoki, K.1    Ouyang, H.2    Zhu, T.3
  • 50
    • 84859778293 scopus 로고    scopus 로고
    • mTOR signaling in growth control and disease
    • Laplante M, Sabatini DM. mTOR signaling in growth control and disease. Cell 2012; 149: 274-93.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 52
    • 67650480092 scopus 로고    scopus 로고
    • mTOR and HIF-1alpha-mediated tumor metabolism in an LKB1 mouse model of Peutz-Jeghers syndrome
    • Shackelford DB, Vasquez DS, Corbeil J, et al. mTOR and HIF-1alpha-mediated tumor metabolism in an LKB1 mouse model of Peutz-Jeghers syndrome. Proc Natl Acad Sci USA 2009; 106: 11137-42.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11137-11142
    • Shackelford, D.B.1    Vasquez, D.S.2    Corbeil, J.3
  • 53
    • 84872159532 scopus 로고    scopus 로고
    • AMPK is a negative regulator of the Warburg effect and suppresses tumor growth In vivo
    • Faubert B, Boily G, Izreig S, et al. AMPK is a negative regulator of the Warburg effect and suppresses tumor growth In vivo. Cell Metab 2013; 17: 113-24.
    • (2013) Cell Metab , vol.17 , pp. 113-124
    • Faubert, B.1    Boily, G.2    Izreig, S.3
  • 54
    • 39749102904 scopus 로고    scopus 로고
    • Suppression of Peutz-Jeghers polyposis by targeting mammalian target of rapamycin signaling
    • Wei C, Amos CI, Zhang N, et al. Suppression of Peutz-Jeghers polyposis by targeting mammalian target of rapamycin signaling. Clin Cancer Res 2008; 14: 1167-71.
    • (2008) Clin Cancer Res , vol.14 , pp. 1167-1171
    • Wei, C.1    Amos, C.I.2    Zhang, N.3
  • 55
    • 84863763440 scopus 로고    scopus 로고
    • AMPK regulates NADPH homeostasis to promote tumor cell survival during energy stress
    • Jeon SM, Chandel NS, Hay N. AMPK regulates NADPH homeostasis to promote tumor cell survival during energy stress. Nature 2012; 485: 661-5.
    • (2012) Nature , vol.485 , pp. 661-665
    • Jeon, S.M.1    Chandel, N.S.2    Hay, N.3
  • 56
    • 84877851087 scopus 로고    scopus 로고
    • AMPK: A contextual oncogene or tumor suppressor?
    • Liang J, Mills GB. AMPK: a contextual oncogene or tumor suppressor? Cancer Res 2013; 73: 2929-35.
    • (2013) Cancer Res , vol.73 , pp. 2929-2935
    • Liang, J.1    Mills, G.B.2
  • 57
    • 84876936567 scopus 로고    scopus 로고
    • AMPK activation by oncogenesis is required to maintain cancer cell proliferation in astrocytic tumors
    • Ríos M, Foretz M, Viollet B, et al. AMPK activation by oncogenesis is required to maintain cancer cell proliferation in astrocytic tumors. Cancer Res 2013; 73: 2628-38.
    • (2013) Cancer Res , vol.73 , pp. 2628-2638
    • Ríos, M.1    Foretz, M.2    Viollet, B.3
  • 58
    • 26444610333 scopus 로고    scopus 로고
    • LKB1 interacts with and phosphorylates PTEN: A functional link between two proteins involved in cancer predisposing syndromes
    • Mehenni H, Lin-Marq N, Buchet-Poyau K, et al. LKB1 interacts with and phosphorylates PTEN: a functional link between two proteins involved in cancer predisposing syndromes. Hum Mol Genet 2005; 14: 2209-19.
    • (2005) Hum Mol Genet , vol.14 , pp. 2209-2219
    • Mehenni, H.1    Lin-Marq, N.2    Buchet-Poyau, K.3
  • 59
    • 0037125996 scopus 로고    scopus 로고
    • Induction of cyclooxygenase-2 in a mouse model of Peutz-Jeghers polyposis
    • Rossi DJ, Ylikorkala A, Korsisaari N, et al. Induction of cyclooxygenase-2 in a mouse model of Peutz-Jeghers polyposis. Proc Natl Acad Sci USA 2002; 99: 12327-32.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12327-12332
    • Rossi, D.J.1    Ylikorkala, A.2    Korsisaari, N.3
  • 60
    • 35548952703 scopus 로고    scopus 로고
    • Suppression of oncogenic properties of c-Myc by LKB1-controlled epithelial organization
    • Partanen JI, Nieminen AI, Mäkelä TP, Klefstrom J. Suppression of oncogenic properties of c-Myc by LKB1-controlled epithelial organization. Proc Natl Acad Sci USA 2007; 104: 14694-9.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14694-14699
    • Partanen, J.I.1    Nieminen, A.I.2    Mäkelä, T.P.3    Klefstrom, J.4
  • 61
    • 0037096833 scopus 로고    scopus 로고
    • Growth arrest by the LKB1 tumor suppressor: Induction of p21(WAF1/CIP1)
    • Tiainen M, Vaahtomeri K, Ylikorkala A, Makela TP. Growth arrest by the LKB1 tumor suppressor: induction of p21(WAF1/CIP1). Hum Mol Genet 2002; 11: 1497-504.
    • (2002) Hum Mol Genet , vol.11 , pp. 1497-1504
    • Tiainen, M.1    Vaahtomeri, K.2    Ylikorkala, A.3    Makela, T.P.4
  • 63
    • 34250793435 scopus 로고    scopus 로고
    • LKB1 catalytically deficient mutants enhance cyclin D1 expression
    • Scott KD, Nath-Sain S, Agnew MD, Marignani PA. LKB1 catalytically deficient mutants enhance cyclin D1 expression. Cancer Res 2007; 67: 5622-7.
    • (2007) Cancer Res , vol.67 , pp. 5622-5627
    • Scott, K.D.1    Nath-Sain, S.2    Agnew, M.D.3    Marignani, P.A.4
  • 64
    • 34250827107 scopus 로고    scopus 로고
    • Energy-dependent regulation of cell structure by AMP-activated protein kinase
    • Lee JH, Koh H, Kim M, et al. Energy-dependent regulation of cell structure by AMP-activated protein kinase. Nature 2007; 447: 1017-20.
    • (2007) Nature , vol.447 , pp. 1017-1020
    • Lee, J.H.1    Koh, H.2    Kim, M.3
  • 65
    • 34247478454 scopus 로고    scopus 로고
    • LKB1/STRAD promotes axon initiation during neuronal polarization
    • Shelly M, Cancedda L, Heilshorn S, Sumbre G, Poo MM. LKB1/STRAD promotes axon initiation during neuronal polarization. Cell 2007; 129: 565-77.
    • (2007) Cell , vol.129 , pp. 565-577
    • Shelly, M.1    Cancedda, L.2    Heilshorn, S.3    Sumbre, G.4    Poo, M.M.5
  • 66
    • 34247511497 scopus 로고    scopus 로고
    • LKB1 and SAD kinases define a pathway required for the polarization of cortical neurons
    • Barnes AP, Lilley BN, Pan YA, et al. LKB1 and SAD kinases define a pathway required for the polarization of cortical neurons. Cell 2007; 129: 549-63.
    • (2007) Cell , vol.129 , pp. 549-563
    • Barnes, A.P.1    Lilley, B.N.2    Pan, Y.A.3
  • 67
    • 3042649049 scopus 로고    scopus 로고
    • LKB1 kinase: Master and commander of metabolism and polarity
    • Spicer J, Ashworth A. LKB1 kinase: master and commander of metabolism and polarity. Curr Biol 2004; 14: R383-5.
    • (2004) Curr Biol , vol.14 , pp. 383-385
    • Spicer, J.1    Ashworth, A.2
  • 68
    • 77956906920 scopus 로고    scopus 로고
    • Regulation of bile canalicular network formation and maintenance by AMP-activated protein kinase and LKB1
    • Fu D, Wakabayashi Y, Ido Y, Lippincott-Schwartz J, Arias IM. Regulation of bile canalicular network formation and maintenance by AMP-activated protein kinase and LKB1. J Cell Sci 2010; 123: 3294-302.
    • (2010) J Cell Sci , vol.123 , pp. 3294-3302
    • Fu, D.1    Wakabayashi, Y.2    Ido, Y.3    Lippincott-Schwartz, J.4    Arias, I.M.5
  • 69
    • 33751204464 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates the assembly of epithelial tight junctions
    • Zhang L, Li J, Young LH, Caplan MJ. AMP-activated protein kinase regulates the assembly of epithelial tight junctions. Proc Natl Acad Sci USA 2006; 103: 17272-7.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17272-17277
    • Zhang, L.1    Li, J.2    Young, L.H.3    Caplan, M.J.4
  • 70
    • 64549137929 scopus 로고    scopus 로고
    • Mst4 and Ezrin induce brush borders downstream of the Lkb1/Strad/Mo25 polarization complex
    • ten Klooster JP, Jansen M, Yuan J, et al. Mst4 and Ezrin induce brush borders downstream of the Lkb1/Strad/Mo25 polarization complex. Dev Cell 2009; 16: 551-62.
    • (2009) Dev Cell , vol.16 , pp. 551-562
    • ten Klooster, J.P.1    Jansen, M.2    Yuan, J.3
  • 71
    • 84864869731 scopus 로고    scopus 로고
    • Rap2A links intestinal cell polarity to brush border formation
    • Gloerich M, ten Klooster JP, Vliem MJ, et al. Rap2A links intestinal cell polarity to brush border formation. Nat Cell Biol 2012; 14: 793-801.
    • (2012) Nat Cell Biol , vol.14 , pp. 793-801
    • Gloerich, M.1    ten Klooster, J.P.2    Vliem, M.J.3
  • 72
    • 78149259013 scopus 로고    scopus 로고
    • Primary cilia regulate mTORC1 activity and cell size through Lkb1
    • Boehlke C, Kotsis F, Patel V, et al. Primary cilia regulate mTORC1 activity and cell size through Lkb1. Nat Cell Biol 2010; 12: 1115-22.
    • (2010) Nat Cell Biol , vol.12 , pp. 1115-1122
    • Boehlke, C.1    Kotsis, F.2    Patel, V.3
  • 74
    • 84655169623 scopus 로고    scopus 로고
    • Epithelial cell polarity, stem cells and cancer
    • Martin-Belmonte F, Perez-Moreno M. Epithelial cell polarity, stem cells and cancer. Nat Rev Cancer 2011; 12: 23-38.
    • (2011) Nat Rev Cancer , vol.12 , pp. 23-38
    • Martin-Belmonte, F.1    Perez-Moreno, M.2
  • 75
    • 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: 25336-43.
    • (2006) J Biol Chem , vol.281 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.P.2    Carlson, M.3
  • 76
    • 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: 29060-6.
    • (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
  • 78
    • 76449101125 scopus 로고    scopus 로고
    • Differential requirements for STRAD in LKB1-dependent functions in C. elegans
    • Narbonne P, Hyenne V, Li S, Labbé JC, Roy R. Differential requirements for STRAD in LKB1-dependent functions in C. elegans. Development 2010; 137: 661-70.
    • (2010) Development , vol.137 , pp. 661-670
    • Narbonne, P.1    Hyenne, V.2    Li, S.3    Labbé, J.C.4    Roy, R.5
  • 79
    • 77957879994 scopus 로고    scopus 로고
    • Lymphocytes accelerate epithelial tight junction assembly: Role of AMP-activated protein kinase (AMPK)
    • Tang XX, Chen H, Yu S, Zhang L, Caplan MJ, Chan HC. Lymphocytes accelerate epithelial tight junction assembly: role of AMP-activated protein kinase (AMPK). PLoS One 2010; 5: e12343.
    • (2010) PLoS One , vol.5
    • Tang, X.X.1    Chen, H.2    Yu, S.3    Zhang, L.4    Caplan, M.J.5    Chan, H.C.6
  • 80
    • 35748943872 scopus 로고    scopus 로고
    • Dialogue between LKB1 and AMPK: A hot topic at the cellular pole
    • Forcet C, Billaud M. Dialogue between LKB1 and AMPK: a hot topic at the cellular pole. Sci STKE 2007; 2007(404): pe51.
    • (2007) Sci STKE , vol.2007 , Issue.404
    • Forcet, C.1    Billaud, M.2
  • 81
    • 19944413010 scopus 로고    scopus 로고
    • Genome-wide survey of protein kinases required for cell cycle progression
    • Bettencourt-Dias M, Giet R, Sinka R, et al. Genome-wide survey of protein kinases required for cell cycle progression. Nature 2004; 432: 980-7.
    • (2004) Nature , vol.432 , pp. 980-987
    • Bettencourt-Dias, M.1    Giet, R.2    Sinka, R.3
  • 82
    • 84864009034 scopus 로고    scopus 로고
    • The LKB1 tumor suppressor controls spindle orientation and localization of activated AMPK in mitotic epithelial cells
    • Wei C, Bhattaram VK, Igwe JC, Fleming E, Tirnauer JS. The LKB1 tumor suppressor controls spindle orientation and localization of activated AMPK in mitotic epithelial cells. PLoS One 2012; 7: e41118.
    • (2012) PLoS One , vol.7
    • Wei, C.1    Bhattaram, V.K.2    Igwe, J.C.3    Fleming, E.4    Tirnauer, J.S.5
  • 83
    • 84355161919 scopus 로고    scopus 로고
    • Chemical genetic screen for AMPKα2 substrates uncovers a network of proteins involved in mitosis
    • Banko MR, Allen JJ, Schaffer BE, et al. Chemical genetic screen for AMPKα2 substrates uncovers a network of proteins involved in mitosis. Mol Cell 2011; 44: 878-92.
    • (2011) Mol Cell , vol.44 , pp. 878-892
    • Banko, M.R.1    Allen, J.J.2    Schaffer, B.E.3
  • 85
    • 10944257674 scopus 로고    scopus 로고
    • Crosslinks and crosstalk: Human cancer syndromes and DNA repair defects
    • Risinger MA, Groden J. Crosslinks and crosstalk: human cancer syndromes and DNA repair defects. Cancer Cell 2004; 6: 539-45.
    • (2004) Cancer Cell , vol.6 , pp. 539-545
    • Risinger, M.A.1    Groden, J.2
  • 86
    • 36749022214 scopus 로고    scopus 로고
    • The DNA damage response: Ten years after
    • Harper JW, Elledge SJ. The DNA damage response: ten years after. Mol Cell 2007; 28: 739-45.
    • (2007) Mol Cell , vol.28 , pp. 739-745
    • Harper, J.W.1    Elledge, S.J.2
  • 87
    • 34249947699 scopus 로고    scopus 로고
    • ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage
    • Matsuoka S, Ballif BA, Smogorzewska A, et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science 2007; 316: 1160-6.
    • (2007) Science , vol.316 , pp. 1160-1166
    • Matsuoka, S.1    Ballif, B.A.2    Smogorzewska, A.3
  • 88
    • 17644362355 scopus 로고    scopus 로고
    • DNA damage-induced association of ATM with its target proteins requires a protein interaction domain in the N terminus of ATM
    • Fernandes N, Sun Y, Chen S, et al. DNA damage-induced association of ATM with its target proteins requires a protein interaction domain in the N terminus of ATM. J Biol Chem 2005; 280: 15158-64.
    • (2005) J Biol Chem , vol.280 , pp. 15158-15164
    • Fernandes, N.1    Sun, Y.2    Chen, S.3
  • 89
    • 0036901639 scopus 로고    scopus 로고
    • Ionizing radiation induces ataxia telangiectasia mutated kinase (ATM)-mediated phosphorylation of LKB1/STK11 at Thr-366
    • Sapkota GP, Deak M, Kieloch A, et al. Ionizing radiation induces ataxia telangiectasia mutated kinase (ATM)-mediated phosphorylation of LKB1/STK11 at Thr-366. Biochem J 2002; 368(Pt 2): 507-16.
    • (2002) Biochem J , vol.368 , Issue.PART 2 , pp. 507-516
    • Sapkota, G.P.1    Deak, M.2    Kieloch, A.3
  • 91
    • 77749233738 scopus 로고    scopus 로고
    • ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS
    • Alexander A, Cai SL, Kim J, et al. ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS. Proc Natl Acad Sci USA 2010; 107: 4153-8.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4153-4158
    • Alexander, A.1    Cai, S.L.2    Kim, J.3
  • 92
    • 84862119127 scopus 로고    scopus 로고
    • LKB1/STK11 inactivation leads to expansion of a prometastatic tumor subpopulation in melanoma
    • Liu W, Monahan KB, Pfefferle AD, et al. LKB1/STK11 inactivation leads to expansion of a prometastatic tumor subpopulation in melanoma. Cancer Cell 2012; 21: 751-64.
    • (2012) Cancer Cell , vol.21 , pp. 751-764
    • Liu, W.1    Monahan, K.B.2    Pfefferle, A.D.3
  • 93
    • 79251614530 scopus 로고    scopus 로고
    • Lkb1 and Pten synergise to suppress mTOR-mediated tumorigenesis and epithelialmesenchymal transition in the mouse bladder
    • Shorning BY, Griffiths D, Clarke AR. Lkb1 and Pten synergise to suppress mTOR-mediated tumorigenesis and epithelialmesenchymal transition in the mouse bladder. PLoS One 2011; 6: e16209.
    • (2011) PLoS One , vol.6
    • Shorning, B.Y.1    Griffiths, D.2    Clarke, A.R.3
  • 94
    • 77957021496 scopus 로고    scopus 로고
    • Involvement of LKB1 in epithelial-mesenchymal transition (EMT) of human lung cancer cells
    • Roy BC, Kohno T, Iwakawa R, et al. Involvement of LKB1 in epithelial-mesenchymal transition (EMT) of human lung cancer cells. Lung Cancer 2010; 70: 136-45.
    • (2010) Lung Cancer , vol.70 , pp. 136-145
    • Roy, B.C.1    Kohno, T.2    Iwakawa, R.3
  • 95
    • 70349565231 scopus 로고    scopus 로고
    • SIK1 couples LKB1 to p53-dependent anoikis and suppresses metastasis
    • Cheng H, Liu P, Wang ZC, et al. SIK1 couples LKB1 to p53-dependent anoikis and suppresses metastasis. Sci Signal 2009; 2: ra35.
    • (2009) Sci Signal , vol.2
    • Cheng, H.1    Liu, P.2    Wang, Z.C.3
  • 96
    • 84857043185 scopus 로고    scopus 로고
    • The AMPK stress response pathway mediates anoikis resistance through inhibition of mTOR and suppression of protein synthesis
    • Ng TL, Leprivier G, Robertson MD, et al. The AMPK stress response pathway mediates anoikis resistance through inhibition of mTOR and suppression of protein synthesis. Cell Death Differ 2012; 19: 501-10.
    • (2012) Cell Death Differ , vol.19 , pp. 501-510
    • Ng, T.L.1    Leprivier, G.2    Robertson, M.D.3
  • 97
    • 78650488264 scopus 로고    scopus 로고
    • LKB1 inhibits lung cancer progression through lysyl oxidase and extracellular matrix remodeling
    • Gao Y, Xiao Q, Ma H, et al. LKB1 inhibits lung cancer progression through lysyl oxidase and extracellular matrix remodeling. Proc Natl Acad Sci USA 2010; 107: 18892-7.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18892-18897
    • Gao, Y.1    Xiao, Q.2    Ma, H.3
  • 99
    • 34848861463 scopus 로고    scopus 로고
    • The energy sensor AMPactivated protein kinase directly regulates the mammalian FOXO3 transcription factor
    • Greer EL, Oskoui PR, Banko MR, et al. The energy sensor AMPactivated protein kinase directly regulates the mammalian FOXO3 transcription factor. J Biol Chem 2007; 282: 30107-19.
    • (2007) J Biol Chem , vol.282 , pp. 30107-30119
    • Greer, E.L.1    Oskoui, P.R.2    Banko, M.R.3
  • 100
    • 33646376411 scopus 로고    scopus 로고
    • Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells
    • Yilmaz OH, Valdez R, Theisen BK, et al. Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells. Nature 2006; 441: 475-82.
    • (2006) Nature , vol.441 , pp. 475-482
    • Yilmaz, O.H.1    Valdez, R.2    Theisen, B.K.3
  • 101
    • 78650866793 scopus 로고    scopus 로고
    • The tumor suppressor LKB1 emerges as a critical factor in hematopoietic stem cell biology
    • Krock B, Skuli N, Simon MC. The tumor suppressor LKB1 emerges as a critical factor in hematopoietic stem cell biology. Cell Metab 2011; 13: 8-10.
    • (2011) Cell Metab , vol.13 , pp. 8-10
    • Krock, B.1    Skuli, N.2    Simon, M.C.3
  • 102
    • 84859496182 scopus 로고    scopus 로고
    • LKB1 controls the pluripotent state of human embryonic stem cells
    • Lai D, Chen Y, Wang F, Jiang L, Wei C. LKB1 controls the pluripotent state of human embryonic stem cells. Cell Reprogram 2012; 14: 164-70.
    • (2012) Cell Reprogram , vol.14 , pp. 164-170
    • Lai, D.1    Chen, Y.2    Wang, F.3    Jiang, L.4    Wei, C.5
  • 103
    • 33744828352 scopus 로고    scopus 로고
    • Exonic STK11 deletions are not a rare cause of Peutz-Jeghers syndrome
    • Hearle NC, Rudd MF, Lim W, et al. Exonic STK11 deletions are not a rare cause of Peutz-Jeghers syndrome. J Med Genet 2006; 43: e15.
    • (2006) J Med Genet , vol.43
    • Hearle, N.C.1    Rudd, M.F.2    Lim, W.3
  • 104
    • 33745966059 scopus 로고    scopus 로고
    • LKB1 exonic and whole gene deletions are a common cause of Peutz-Jeghers syndrome
    • Volikos E, Robinson J, Aittomaki K, et al. LKB1 exonic and whole gene deletions are a common cause of Peutz-Jeghers syndrome. J Med Genet 2006; 43: e18.
    • (2006) J Med Genet , vol.43
    • Volikos, E.1    Robinson, J.2    Aittomaki, K.3
  • 105
    • 0034464147 scopus 로고    scopus 로고
    • Very high risk of cancer in familial Peutz-Jeghers syndrome
    • Giardiello FM, Brensinger JD, Tersmette AC, et al. Very high risk of cancer in familial Peutz-Jeghers syndrome. Gastroenterology 2000; 119: 1447-53.
    • (2000) Gastroenterology , vol.119 , pp. 1447-1453
    • Giardiello, F.M.1    Brensinger, J.D.2    Tersmette, A.C.3
  • 106
    • 33744782567 scopus 로고    scopus 로고
    • Frequency and spectrum of cancers in the Peutz-Jeghers syndrome
    • Hearle N, Schumacher V, Menko FH, et al. Frequency and spectrum of cancers in the Peutz-Jeghers syndrome. Clin Cancer Res 2006; 12: 3209-15.
    • (2006) Clin Cancer Res , vol.12 , pp. 3209-3215
    • Hearle, N.1    Schumacher, V.2    Menko, F.H.3
  • 107
    • 34748845413 scopus 로고    scopus 로고
    • Prevalence and specificity of LKB1 genetic alterations in lung cancers
    • Matsumoto S, Iwakawa R, Takahashi K, et al. Prevalence and specificity of LKB1 genetic alterations in lung cancers. Oncogene 2007; 26: 5911-8.
    • (2007) Oncogene , vol.26 , pp. 5911-5918
    • Matsumoto, S.1    Iwakawa, R.2    Takahashi, K.3
  • 108
    • 44649104448 scopus 로고    scopus 로고
    • Targeting AMPK: A new therapeutic opportunity in breast cancer
    • Hadad SM, Fleming S, Thompson AM. Targeting AMPK: a new therapeutic opportunity in breast cancer. Crit Rev Oncol Hematol 2008; 67: 1-7.
    • (2008) Crit Rev Oncol Hematol , vol.67 , pp. 1-7
    • Hadad, S.M.1    Fleming, S.2    Thompson, A.M.3
  • 109
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000; 100: 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 110
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell 2011; 144: 646-74.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 111
    • 84862742039 scopus 로고    scopus 로고
    • Targeted therapy for patients with chronic myeloid leukemia: Clinical trial experience and challenges in intertrial comparisons
    • Tiu R, Kalaycio M. Targeted therapy for patients with chronic myeloid leukemia: clinical trial experience and challenges in intertrial comparisons. Leuk Lymphoma 2012; 53: 1263-72.
    • (2012) Leuk Lymphoma , vol.53 , pp. 1263-1272
    • Tiu, R.1    Kalaycio, M.2
  • 113
    • 84856693441 scopus 로고    scopus 로고
    • Mutant p53 protein, master regulator of human malignancies: A report on the Fifth Mutant p53 Workshop
    • Blandino G, Deppert W, Hainaut P, et al. Mutant p53 protein, master regulator of human malignancies: a report on the Fifth Mutant p53 Workshop. Cell Death Differ 2012; 19: 180-3.
    • (2012) Cell Death Differ , vol.19 , pp. 180-183
    • Blandino, G.1    Deppert, W.2    Hainaut, P.3
  • 115
    • 0036949663 scopus 로고    scopus 로고
    • Mutant p53-dependent growth suppression distinguishes PRIMA-1 from known anticancer drugs: A statistical analysis of information in the National Cancer Institute database
    • Bykov VJ, Issaeva N, Selivanova G, Wiman KG. Mutant p53-dependent growth suppression distinguishes PRIMA-1 from known anticancer drugs: a statistical analysis of information in the National Cancer Institute database. Carcinogenesis 2002; 23: 2011-8.
    • (2002) Carcinogenesis , vol.23 , pp. 2011-2018
    • Bykov, V.J.1    Issaeva, N.2    Selivanova, G.3    Wiman, K.G.4
  • 116
    • 65449144050 scopus 로고    scopus 로고
    • PRIMA-1 reactivates mutant p53 by covalent binding to the core domain
    • Lambert JM, Gorzov P, Veprintsev DB, et al. PRIMA-1 reactivates mutant p53 by covalent binding to the core domain. Cancer Cell 2009; 15: 376-88.
    • (2009) Cancer Cell , vol.15 , pp. 376-388
    • Lambert, J.M.1    Gorzov, P.2    Veprintsev, D.B.3
  • 117
    • 84876976694 scopus 로고    scopus 로고
    • Targeting triple negative breast cancer: Is p53 the answer?
    • Turner N, Moretti E, Siclari O, et al. Targeting triple negative breast cancer: is p53 the answer? Cancer Treat Rev 2013; 39: 541-50.
    • (2013) Cancer Treat Rev , vol.39 , pp. 541-550
    • Turner, N.1    Moretti, E.2    Siclari, O.3
  • 118
    • 84856753045 scopus 로고    scopus 로고
    • The genetic basis for cancer treatment decisions
    • Dancey JE, Bedard PL, Onetto N, Hudson TJ. The genetic basis for cancer treatment decisions. Cell 2012; 148: 409-20.
    • (2012) Cell , vol.148 , pp. 409-420
    • Dancey, J.E.1    Bedard, P.L.2    Onetto, N.3    Hudson, T.J.4
  • 119
    • 84880352272 scopus 로고    scopus 로고
    • Myc and mTOR converge on a common node in protein synthesis control that confers synthetic lethality in Myc-driven cancers
    • Pourdehnad M, Truitt ML, Siddiqi IN, Ducker GS, Shokat KM, Ruggero D. Myc and mTOR converge on a common node in protein synthesis control that confers synthetic lethality in Myc-driven cancers. Proc Natl Acad Sci USA 2013; 110: 11988-93.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 11988-11993
    • Pourdehnad, M.1    Truitt, M.L.2    Siddiqi, I.N.3    Ducker, G.S.4    Shokat, K.M.5    Ruggero, D.6
  • 120
    • 84880163379 scopus 로고    scopus 로고
    • Perspective: Combined forces
    • Sawyers CL. Perspective: combined forces. Nature 2013; 498: S7.
    • (2013) Nature , vol.498
    • Sawyers, C.L.1
  • 121
    • 65849278908 scopus 로고    scopus 로고
    • Finding and drugging the vulnerabilities of RASdependent cancers
    • Sawyers CL. Finding and drugging the vulnerabilities of RASdependent cancers. Cell 2009; 137: 796-8.
    • (2009) Cell , vol.137 , pp. 796-798
    • Sawyers, C.L.1
  • 122
    • 76449110054 scopus 로고    scopus 로고
    • Synthetic lethality: A framework for the development of wiser cancer therapeutics
    • Kaelin WG Jr. Synthetic lethality: a framework for the development of wiser cancer therapeutics. Genome Med 2009; 1: 99.
    • (2009) Genome Med , vol.1 , pp. 99
    • Kaelin Jr., W.G.1
  • 123
    • 84872387485 scopus 로고    scopus 로고
    • Synthetic lethal interaction of combined BCL-XL and MEK inhibition promotes tumor regressions in KRAS mutant cancer models
    • Corcoran RB, Cheng KA, Hata AN, et al. Synthetic lethal interaction of combined BCL-XL and MEK inhibition promotes tumor regressions in KRAS mutant cancer models. Cancer Cell 2013; 23: 121-8.
    • (2013) Cancer Cell , vol.23 , pp. 121-128
    • Corcoran, R.B.1    Cheng, K.A.2    Hata, A.N.3
  • 124
    • 65849111219 scopus 로고    scopus 로고
    • Synthetic lethal interaction between oncogenic KRAS dependency and STK33 suppression in human cancer cells
    • Scholl C, Fröhling S, Dunn IF, et al. Synthetic lethal interaction between oncogenic KRAS dependency and STK33 suppression in human cancer cells. Cell 2009; 137: 821-34.
    • (2009) Cell , vol.137 , pp. 821-834
    • Scholl, C.1    Fröhling, S.2    Dunn, I.F.3
  • 125
    • 66149091940 scopus 로고    scopus 로고
    • A genome-wide RNAi screen identifies multiple synthetic lethal interactions with the Ras oncogene
    • Luo J, Emanuele MJ, Li D, et al. A genome-wide RNAi screen identifies multiple synthetic lethal interactions with the Ras oncogene. Cell 2009; 137: 835-48.
    • (2009) Cell , vol.137 , pp. 835-848
    • Luo, J.1    Emanuele, M.J.2    Li, D.3
  • 126
    • 79251564088 scopus 로고    scopus 로고
    • A review of PARP inhibitors: From bench to bedside
    • Underhill C, Toulmonde M, Bonnefoi H. A review of PARP inhibitors: from bench to bedside. Ann Oncol 2011; 22: 268-79.
    • (2011) Ann Oncol , vol.22 , pp. 268-279
    • Underhill, C.1    Toulmonde, M.2    Bonnefoi, H.3
  • 127
    • 69549145898 scopus 로고    scopus 로고
    • The potential role and application of PARP inhibitors in cancer treatment
    • Chalmers AJ. The potential role and application of PARP inhibitors in cancer treatment. Br Med Bull 2009; 89: 23-40.
    • (2009) Br Med Bull , vol.89 , pp. 23-40
    • Chalmers, A.J.1
  • 129
    • 17244375049 scopus 로고    scopus 로고
    • Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase
    • Bryant HE, Schultz N, Thomas HD, et al. Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase. Nature 2005; 434: 913-7.
    • (2005) Nature , vol.434 , pp. 913-917
    • Bryant, H.E.1    Schultz, N.2    Thomas, H.D.3
  • 130
    • 17244373777 scopus 로고    scopus 로고
    • Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy
    • Farmer H, McCabe N, Lord CJ, et al. Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy. Nature 2005; 434: 917-21.
    • (2005) Nature , vol.434 , pp. 917-921
    • Farmer, H.1    McCabe, N.2    Lord, C.J.3
  • 131
    • 77954032829 scopus 로고    scopus 로고
    • Poly(ADP)-ribose polymerase inhibition: Frequent durable responses in BRCA carrier ovarian cancer correlating with platinum-free interval
    • Fong PC, Yap TA, Boss DS, et al. Poly(ADP)-ribose polymerase inhibition: frequent durable responses in BRCA carrier ovarian cancer correlating with platinum-free interval. J Clin Oncol 2010; 28: 2512-9.
    • (2010) J Clin Oncol , vol.28 , pp. 2512-2519
    • Fong, P.C.1    Yap, T.A.2    Boss, D.S.3
  • 132
    • 84954358647 scopus 로고    scopus 로고
    • A highthroughput RNA interference screen for DNA repair determinants of PARP inhibitor sensitivity
    • Lord CJ, McDonald S, Swift S, Turner NC, Ashworth A. A highthroughput RNA interference screen for DNA repair determinants of PARP inhibitor sensitivity. DNA Repair (Amst) 2008; 7: 2010-9.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 2010-2019
    • Lord, C.J.1    McDonald, S.2    Swift, S.3    Turner, N.C.4    Ashworth, A.5
  • 133
    • 43249085571 scopus 로고    scopus 로고
    • A synthetic lethal siRNA screen identifying genes mediating sensitivity to a PARP inhibitor
    • Turner NC, Lord CJ, Iorns E, et al. A synthetic lethal siRNA screen identifying genes mediating sensitivity to a PARP inhibitor. EMBO J 2008; 27: 1368-77.
    • (2008) EMBO J , vol.27 , pp. 1368-1377
    • Turner, N.C.1    Lord, C.J.2    Iorns, E.3
  • 134
    • 77149157867 scopus 로고    scopus 로고
    • Synthetic lethal targeting of PTEN mutant cells with PARP inhibitors
    • Mendes-Pereira AM, Martin SA, Brough R, et al. Synthetic lethal targeting of PTEN mutant cells with PARP inhibitors. EMBO Mol Med 2009; 1: 315-22.
    • (2009) EMBO Mol Med , vol.1 , pp. 315-322
    • Mendes-Pereira, A.M.1    Martin, S.A.2    Brough, R.3
  • 135
    • 77954358148 scopus 로고    scopus 로고
    • PTEN loss compromises homologous recombination repair in astrocytes: Implications for glioblastoma therapy with temozolomide or poly(ADP-ribose) polymerase inhibitors
    • McEllin B, Camacho CV, Mukherjee B, et al. PTEN loss compromises homologous recombination repair in astrocytes: implications for glioblastoma therapy with temozolomide or poly(ADP-ribose) polymerase inhibitors. Cancer Res 2010; 70: 5457-64.
    • (2010) Cancer Res , vol.70 , pp. 5457-5464
    • McEllin, B.1    Camacho, C.V.2    Mukherjee, B.3
  • 136
    • 2342658475 scopus 로고    scopus 로고
    • New targeted therapies in breast cancer
    • Kaklamani V, O'Regan RM. New targeted therapies in breast cancer. Semin Oncol 2004; 31: S20-5.
    • (2004) Semin Oncol , vol.31 , pp. 20-25
    • Kaklamani, V.1    O'Regan, R.M.2
  • 137
    • 56749160290 scopus 로고    scopus 로고
    • Clinically applicable models to characterize BRCA1 and BRCA2 variants of uncertain significance
    • Spearman AD, Sweet K, Zhou XP, McLennan J, Couch FJ, Toland AE. Clinically applicable models to characterize BRCA1 and BRCA2 variants of uncertain significance. J Clin Oncol 2008; 26: 5393-400.
    • (2008) J Clin Oncol , vol.26 , pp. 5393-5400
    • Spearman, A.D.1    Sweet, K.2    Zhou, X.P.3    McLennan, J.4    Couch, F.J.5    Toland, A.E.6
  • 138
    • 33748065304 scopus 로고    scopus 로고
    • Deficiency in the repair of DNA damage by homologous recombination and sensitivity to poly(ADP-ribose) polymerase inhibition
    • McCabe N, Turner NC, Lord CJ, et al. Deficiency in the repair of DNA damage by homologous recombination and sensitivity to poly(ADP-ribose) polymerase inhibition. Cancer Res 2006; 66: 8109-15.
    • (2006) Cancer Res , vol.66 , pp. 8109-8115
    • McCabe, N.1    Turner, N.C.2    Lord, C.J.3
  • 140
    • 33748118458 scopus 로고    scopus 로고
    • Neither LKB1 nor AMPK are the direct targets of metformin
    • Hardie DG. Neither LKB1 nor AMPK are the direct targets of metformin. Gastroenterology 2006; 131: 973.
    • (2006) Gastroenterology , vol.131 , pp. 973
    • Hardie, D.G.1
  • 141
    • 77950191479 scopus 로고    scopus 로고
    • Targeting cancer cell metabolism: The combination of metformin and 2-deoxyglucose induces p53-dependent apoptosis in prostate cancer cells
    • Ben Sahra I, Laurent K, Giuliano S, et al. Targeting cancer cell metabolism: the combination of metformin and 2-deoxyglucose induces p53-dependent apoptosis in prostate cancer cells. Cancer Res 2010; 70: 2465-75.
    • (2010) Cancer Res , vol.70 , pp. 2465-2475
    • Ben Sahra, I.1    Laurent, K.2    Giuliano, S.3
  • 142
    • 20844449238 scopus 로고    scopus 로고
    • AMP-activated protein kinase induces a p53-dependent metabolic checkpoint
    • Jones RG, Plas DR, Kubek S, et al. AMP-activated protein kinase induces a p53-dependent metabolic checkpoint. Mol Cell 2005; 18: 283-93.
    • (2005) Mol Cell , vol.18 , pp. 283-293
    • Jones, R.G.1    Plas, D.R.2    Kubek, S.3
  • 143
    • 3342915617 scopus 로고    scopus 로고
    • AMP-activated protein kinase inhibits angiotensin II-stimulated vascular smooth muscle cell proliferation
    • Nagata D, Takeda R, Sata M, et al. AMP-activated protein kinase inhibits angiotensin II-stimulated vascular smooth muscle cell proliferation. Circulation 2004; 110: 444-51.
    • (2004) Circulation , vol.110 , pp. 444-451
    • Nagata, D.1    Takeda, R.2    Sata, M.3
  • 144
    • 26844527037 scopus 로고    scopus 로고
    • Adenosine monophosphate-activated protein kinase suppresses vascular smooth muscle cell proliferation through the inhibition of cell cycle progression
    • Igata M, Motoshima H, Tsuruzoe K, et al. Adenosine monophosphate-activated protein kinase suppresses vascular smooth muscle cell proliferation through the inhibition of cell cycle progression. Circ Res 2005; 97: 837-44.
    • (2005) Circ Res , vol.97 , pp. 837-844
    • Igata, M.1    Motoshima, H.2    Tsuruzoe, K.3
  • 145
    • 39449120283 scopus 로고    scopus 로고
    • Thromboxane receptor activates the AMP-activated protein kinase in vascular smooth muscle cells via hydrogen peroxide
    • Zhang M, Dong Y, Xu J, et al. Thromboxane receptor activates the AMP-activated protein kinase in vascular smooth muscle cells via hydrogen peroxide. Circ Res 2008; 102: 328-37.
    • (2008) Circ Res , vol.102 , pp. 328-337
    • Zhang, M.1    Dong, Y.2    Xu, J.3
  • 146
    • 84861222690 scopus 로고    scopus 로고
    • The ancient drug salicylate directly activates AMP-activated protein kinase
    • Hawley SA, Fullerton MD, Ross FA, et al. The ancient drug salicylate directly activates AMP-activated protein kinase. Science 2012; 336: 918-22.
    • (2012) Science , vol.336 , pp. 918-922
    • Hawley, S.A.1    Fullerton, M.D.2    Ross, F.A.3
  • 148
    • 84866322945 scopus 로고    scopus 로고
    • Investigating metformin for cancer prevention and treatment: The end of the beginning
    • Pollak MN. Investigating metformin for cancer prevention and treatment: the end of the beginning. Cancer Discov 2012; 2: 778-90.
    • (2012) Cancer Discov , vol.2 , pp. 778-790
    • Pollak, M.N.1
  • 149
    • 33744514139 scopus 로고    scopus 로고
    • Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome
    • Cool B, Zinker B, Chiou W, et al. Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome. Cell Metab 2006; 3: 403-16.
    • (2006) Cell Metab , vol.3 , pp. 403-416
    • Cool, B.1    Zinker, B.2    Chiou, W.3
  • 150
    • 36348978499 scopus 로고    scopus 로고
    • Defining the mechanism of activation of AMP-activated protein kinase by the small molecule A-769662, a member of the thienopyridone family
    • Sanders MJ, Ali ZS, Hegarty BD, Heath R, Snowden MA, Carling D. Defining the mechanism of activation of AMP-activated protein kinase by the small molecule A-769662, a member of the thienopyridone family. J Biol Chem 2007; 282: 32539-48.
    • (2007) J Biol Chem , vol.282 , pp. 32539-32548
    • Sanders, M.J.1    Ali, Z.S.2    Hegarty, B.D.3    Heath, R.4    Snowden, M.A.5    Carling, D.6
  • 151
    • 36348998521 scopus 로고    scopus 로고
    • Mechanism of action of A-769662, a valuable tool for activation of AMP-activated protein kinase
    • Göransson O, McBride A, Hawley SA, et al. Mechanism of action of A-769662, a valuable tool for activation of AMP-activated protein kinase. J Biol Chem 2007; 282: 32549-60.
    • (2007) J Biol Chem , vol.282 , pp. 32549-32560
    • Göransson, O.1    McBride, A.2    Hawley, S.A.3
  • 152
    • 56049112796 scopus 로고    scopus 로고
    • Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes
    • Scott JW, van Denderen BJ, Jorgensen SB, et al. Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes. Chem Biol 2008; 15: 1220-30.
    • (2008) Chem Biol , vol.15 , pp. 1220-1230
    • Scott, J.W.1    van Denderen, B.J.2    Jorgensen, S.B.3
  • 153
    • 70349921265 scopus 로고    scopus 로고
    • A-769662 activates AMPK beta1-containing complexes but induces glucose uptake through a PI3-kinase-dependent pathway in mouse skeletal muscle
    • Treebak JT, Birk JB, Hansen BF, Olsen GS, Wojtaszewski JF. A-769662 activates AMPK beta1-containing complexes but induces glucose uptake through a PI3-kinase-dependent pathway in mouse skeletal muscle. Am J Physiol Cell Physiol 2009; 297: C1041-52.
    • (2009) Am J Physiol Cell Physiol , vol.297 , pp. 1041-1042
    • Treebak, J.T.1    Birk, J.B.2    Hansen, B.F.3    Olsen, G.S.4    Wojtaszewski, J.F.5
  • 154
  • 155
    • 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
  • 157
    • 36348950449 scopus 로고    scopus 로고
    • Metformin inhibits mammalian target of rapamycin-dependent translation initiation in breast cancer cells
    • Dowling RJ, Zakikhani M, Fantus IG, Pollak M, Sonenberg N. Metformin inhibits mammalian target of rapamycin-dependent translation initiation in breast cancer cells. Cancer Res 2007; 67: 10804-12.
    • (2007) Cancer Res , vol.67 , pp. 10804-10812
    • Dowling, R.J.1    Zakikhani, M.2    Fantus, I.G.3    Pollak, M.4    Sonenberg, N.5
  • 158
    • 69249162223 scopus 로고    scopus 로고
    • Metformin disrupts crosstalk between G protein-coupled receptor and insulin receptor signaling systems and inhibits pancreatic cancer growth
    • Kisfalvi K, Eibl G, Sinnett-Smith J, Rozengurt E. Metformin disrupts crosstalk between G protein-coupled receptor and insulin receptor signaling systems and inhibits pancreatic cancer growth. Cancer Res 2009; 69: 6539-45.
    • (2009) Cancer Res , vol.69 , pp. 6539-6545
    • Kisfalvi, K.1    Eibl, G.2    Sinnett-Smith, J.3    Rozengurt, E.4
  • 159
    • 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
    • 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.
    • (2008) Oncogene , vol.27 , pp. 3576-3586
    • Ben Sahra, I.1    Laurent, K.2    Loubat, A.3
  • 160
    • 60749108023 scopus 로고    scopus 로고
    • The antidiabetic drug metformin suppresses HER2 (erbB-2) oncoprotein overexpression via inhibition of the mTOR effector p70S6K1 in human breast carcinoma cells
    • Vazquez-Martin A, Oliveras-Ferraros C, Menendez JA. The antidiabetic drug metformin suppresses HER2 (erbB-2) oncoprotein overexpression via inhibition of the mTOR effector p70S6K1 in human breast carcinoma cells. Cell Cycle 2009; 8: 88-96.
    • (2009) Cell Cycle , vol.8 , pp. 88-96
    • Vazquez-Martin, A.1    Oliveras-Ferraros, C.2    Menendez, J.A.3
  • 161
    • 67650514082 scopus 로고    scopus 로고
    • Metformin induces unique biological and molecular responses in triple negative breast cancer cells
    • Liu B, Fan Z, Edgerton SM, et al. Metformin induces unique biological and molecular responses in triple negative breast cancer cells. Cell Cycle 2009; 8: 2031-40.
    • (2009) Cell Cycle , vol.8 , pp. 2031-2040
    • Liu, B.1    Fan, Z.2    Edgerton, S.M.3
  • 162
    • 24644475793 scopus 로고    scopus 로고
    • Effect of metformin on life span and on the development of spontaneous mammary tumors in HER-2/neu transgenic mice
    • Anisimov VN, Berstein LM, Egormin PA, Piskunova TS, Popovich IG, Zabezhinski MA, et al. Effect of metformin on life span and on the development of spontaneous mammary tumors in HER-2/neu transgenic mice. Exp Gerontol 2005; 40: 685-93.
    • (2005) Exp Gerontol , vol.40 , pp. 685-693
    • Anisimov, V.N.1    Berstein, L.M.2    Egormin, P.A.3    Piskunova, T.S.4    Popovich, I.G.5    Zabezhinski, M.A.6
  • 163
    • 84872529696 scopus 로고    scopus 로고
    • Metformin inhibits the inflammatory response associated with cellular transformation and cancer stem cell growth
    • Hirsch HA, Iliopoulos D, Struhl K. Metformin inhibits the inflammatory response associated with cellular transformation and cancer stem cell growth. Proc Natl Acad Sci USA 2013; 110: 972-7.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 972-977
    • Hirsch, H.A.1    Iliopoulos, D.2    Struhl, K.3
  • 164
    • 83355163333 scopus 로고    scopus 로고
    • Dual inhibition of tumor energy pathway by 2-deoxyglucose and metformin is effective against a broad spectrum of preclinical cancer models
    • Cheong JH, Park ES, Liang J, et al. Dual inhibition of tumor energy pathway by 2-deoxyglucose and metformin is effective against a broad spectrum of preclinical cancer models. Mol Cancer Ther 2011; 10: 2350-62.
    • (2011) Mol Cancer Ther , vol.10 , pp. 2350-2362
    • Cheong, J.H.1    Park, E.S.2    Liang, J.3
  • 165
    • 84865685190 scopus 로고    scopus 로고
    • Metformin impairs the growth of liver kinase B1-intact cervical cancer cells
    • Xiao X, He Q, Lu C, et al. Metformin impairs the growth of liver kinase B1-intact cervical cancer cells. Gynecol Oncol 2012; 127: 249-55.
    • (2012) Gynecol Oncol , vol.127 , pp. 249-255
    • Xiao, X.1    He, Q.2    Lu, C.3
  • 166
    • 33751284806 scopus 로고    scopus 로고
    • Metformin is an AMP kinase-dependent growth inhibitor for breast cancer cells
    • Zakikhani M, Dowling R, Fantus IG, Sonenberg N, Pollak M. Metformin is an AMP kinase-dependent growth inhibitor for breast cancer cells. Cancer Res 2006; 66: 10269-73.
    • (2006) Cancer Res , vol.66 , pp. 10269-10273
    • Zakikhani, M.1    Dowling, R.2    Fantus, I.G.3    Sonenberg, N.4    Pollak, M.5
  • 167
    • 77953653569 scopus 로고    scopus 로고
    • New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion
    • Zagórska A, Deak M, Campbell DG, et al. New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion. Sci Signal 2010; 3: ra25.
    • (2010) Sci Signal , vol.3
    • Zagórska, A.1    Deak, M.2    Campbell, D.G.3
  • 168
    • 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
  • 169
    • 84873707522 scopus 로고    scopus 로고
    • Biguanides suppress hepatic glucagon signalling by decreasing production of cyclic AMP
    • Miller RA, Chu Q, Xie J, Foretz M, Viollet B, Birnbaum MJ. Biguanides suppress hepatic glucagon signalling by decreasing production of cyclic AMP. Nature 2013; 494: 256-60.
    • (2013) Nature , vol.494 , pp. 256-260
    • Miller, R.A.1    Chu, Q.2    Xie, J.3    Foretz, M.4    Viollet, B.5    Birnbaum, M.J.6
  • 170
    • 77954933558 scopus 로고    scopus 로고
    • Metformin inhibits hepatic gluconeogenesis in mice independently of the LKB1/AMPK pathway via a decrease in hepatic energy state
    • Foretz M, Hébrard S, Leclerc J, et al. Metformin inhibits hepatic gluconeogenesis in mice independently of the LKB1/AMPK pathway via a decrease in hepatic energy state. J Clin Invest 2010; 120: 2355-69.
    • (2010) J Clin Invest , vol.120 , pp. 2355-2369
    • Foretz, M.1    Hébrard, S.2    Leclerc, J.3
  • 172
    • 45849105156 scopus 로고    scopus 로고
    • The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • Sancak Y, Peterson TR, Shaul YD, et al. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 2008; 320: 1496-501.
    • (2008) Science , vol.320 , pp. 1496-1501
    • Sancak, Y.1    Peterson, T.R.2    Shaul, Y.D.3
  • 173
    • 79952538201 scopus 로고    scopus 로고
    • Diet and tumor LKB1 expression interact to determine sensitivity to anti-neoplastic effects of metformin In vivo
    • Algire C, Amrein L, Bazile M, David S, Zakikhani M, Pollak M. Diet and tumor LKB1 expression interact to determine sensitivity to anti-neoplastic effects of metformin In vivo. Oncogene 2011; 30: 1174-82.
    • (2011) Oncogene , vol.30 , pp. 1174-1182
    • Algire, C.1    Amrein, L.2    Bazile, M.3    David, S.4    Zakikhani, M.5    Pollak, M.6
  • 174
    • 84873584845 scopus 로고    scopus 로고
    • LKB1 inactivation dictates therapeutic response of non-small cell lung cancer to the metabolism drug phenformin
    • Shackelford DB, Abt E, Gerken L, et al. LKB1 inactivation dictates therapeutic response of non-small cell lung cancer to the metabolism drug phenformin. Cancer Cell 2013; 23: 143-58.
    • (2013) Cancer Cell , vol.23 , pp. 143-158
    • Shackelford, D.B.1    Abt, E.2    Gerken, L.3
  • 175
    • 34247881866 scopus 로고    scopus 로고
    • Interference with energy metabolism by 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside induces HPV suppression in cervical carcinoma cells and apoptosis in the absence of LKB1
    • Nafz J, De-Castro Arce J, Fleig V, Patzelt A, Mazurek S, Rösl F. Interference with energy metabolism by 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside induces HPV suppression in cervical carcinoma cells and apoptosis in the absence of LKB1. Biochem J 2007; 403: 501-10.
    • (2007) Biochem J , vol.403 , pp. 501-510
    • Nafz, J.1    De-Castro Arce, J.2    Fleig, V.3    Patzelt, A.4    Mazurek, S.5    Rösl, F.6
  • 176
    • 84869788946 scopus 로고    scopus 로고
    • Metformin and the risk of cancer: Time-related biases in observational studies
    • Suissa S, Azoulay L. Metformin and the risk of cancer: time-related biases in observational studies. Diabetes Care 2012; 35: 2665-73.
    • (2012) Diabetes Care , vol.35 , pp. 2665-2673
    • Suissa, S.1    Azoulay, L.2
  • 177
    • 84859778293 scopus 로고    scopus 로고
    • mTOR signaling in growth control and disease
    • Laplante M, Sabatini DM. mTOR signaling in growth control and disease. Cell 2012; 149: 274-93.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 178
    • 84884676252 scopus 로고    scopus 로고
    • Nutrient signaling to mTOR and cell growth
    • Jewell JL, Guan KL. Nutrient signaling to mTOR and cell growth. Trends Biochem Sci 2013; 38: 233-42.
    • (2013) Trends Biochem Sci , vol.38 , pp. 233-242
    • Jewell, J.L.1    Guan, K.L.2
  • 179
    • 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
  • 180
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism
    • Hara K, Yonezawa K, Weng QP, Kozlowski MT, Belham C, Avruch J. Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J Biol Chem 1998; 273: 14484-94.
    • (1998) J Biol Chem , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 181
    • 0028899789 scopus 로고
    • Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes
    • Blommaart EF, Luiken JJ, Blommaart PJ, van Woerkom GM, Meijer AJ. Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes. J Biol Chem 1995; 270: 2320-6.
    • (1995) J Biol Chem , vol.270 , pp. 2320-2326
    • Blommaart, E.F.1    Luiken, J.J.2    Blommaart, P.J.3    van Woerkom, G.M.4    Meijer, A.J.5
  • 182
    • 84877965001 scopus 로고    scopus 로고
    • Regulation of mTORC1 and its impact on gene expression at a glance
    • Laplante M, Sabatini DM. Regulation of mTORC1 and its impact on gene expression at a glance. J Cell Sci 2013; 126: 1713-9.
    • (2013) J Cell Sci , vol.126 , pp. 1713-1719
    • Laplante, M.1    Sabatini, D.M.2
  • 183
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 2005; 307: 1098-101.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 184
    • 84883556505 scopus 로고    scopus 로고
    • Targeting the PI3K/AKT/mTOR and Raf/MEK/ERK pathways in the treatment of breast cancer
    • Saini KS, Loi S, de Azambuja E, et al. Targeting the PI3K/AKT/mTOR and Raf/MEK/ERK pathways in the treatment of breast cancer. Cancer Treat Rev 2013; 39: 935-46.
    • (2013) Cancer Treat Rev , vol.39 , pp. 935-946
    • Saini, K.S.1    Loi, S.2    de Azambuja, E.3
  • 185
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • Jacinto E, Loewith R, Schmidt A, et al. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat Cell Biol 2004; 6: 1122-8.
    • (2004) Nat Cell Biol , vol.6 , pp. 1122-1128
    • Jacinto, E.1    Loewith, R.2    Schmidt, A.3
  • 186
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptorindependent pathway that regulates the cytoskeleton
    • Sarbassov DD, Ali SM, Kim DH, et al. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptorindependent pathway that regulates the cytoskeleton. Curr Biol 2004; 14: 1296-302.
    • (2004) Curr Biol , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1    Ali, S.M.2    Kim, D.H.3
  • 187
    • 84859117806 scopus 로고    scopus 로고
    • Rapamycin-induced insulin resistance is mediated by mTORC2 loss and uncoupled from longevity
    • Lamming DW, Ye L, Katajisto P, et al. Rapamycin-induced insulin resistance is mediated by mTORC2 loss and uncoupled from longevity. Science 2012; 335: 1638-43.
    • (2012) Science , vol.335 , pp. 1638-1643
    • Lamming, D.W.1    Ye, L.2    Katajisto, P.3
  • 188
    • 84860217431 scopus 로고    scopus 로고
    • The functions and regulation of the PTEN tumor suppressor
    • Song MS, Salmena L, Pandolfi PP. The functions and regulation of the PTEN tumor suppressor. Nat Rev Mol Cell Biol 2012; 13: 283-96.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 283-296
    • Song, M.S.1    Salmena, L.2    Pandolfi, P.P.3
  • 189
    • 84883787742 scopus 로고    scopus 로고
    • mTOR kinase inhibitors as potential cancer therapeutic drugs
    • Sun SY. mTOR kinase inhibitors as potential cancer therapeutic drugs. Cancer Lett 2013; 340: 1-8.
    • (2013) Cancer Lett , vol.340 , pp. 1-8
    • Sun, S.Y.1
  • 190
    • 84876863294 scopus 로고    scopus 로고
    • Current status and future perspectives of PI3K and mTOR inhibitor as anticancer drugs in breast cancer
    • Zhang X, Li XR, Zhang J. Current status and future perspectives of PI3K and mTOR inhibitor as anticancer drugs in breast cancer. Curr Cancer Drug Targets 2013; 13: 175-87.
    • (2013) Curr Cancer Drug Targets , vol.13 , pp. 175-187
    • Zhang, X.1    Li, X.R.2    Zhang, J.3
  • 191
    • 84881558888 scopus 로고    scopus 로고
    • Differentiating mTOR inhibitors in renal cell carcinoma
    • Pal SK, Quinn DI. Differentiating mTOR inhibitors in renal cell carcinoma. Cancer Treat Rev 2013; 39: 709-19.
    • (2013) Cancer Treat Rev , vol.39 , pp. 709-719
    • Pal, S.K.1    Quinn, D.I.2
  • 192
    • 84872527628 scopus 로고    scopus 로고
    • mTOR is a key modulator of ageing and age-related disease
    • Johnson SC, Rabinovitch PS, Kaeberlein M. mTOR is a key modulator of ageing and age-related disease. Nature 2013; 493: 338-45.
    • (2013) Nature , vol.493 , pp. 338-345
    • Johnson, S.C.1    Rabinovitch, P.S.2    Kaeberlein, M.3
  • 193
    • 38849208347 scopus 로고    scopus 로고
    • Antitumor activity of rapamycin in a Phase I trial for patients with recurrent PTENdeficient glioblastoma
    • Cloughesy TF, Yoshimoto K, Nghiemphu P, et al. Antitumor activity of rapamycin in a Phase I trial for patients with recurrent PTENdeficient glioblastoma. PLoS Med 2008; 5: e8.
    • (2008) PLoS Med , vol.5
    • Cloughesy, T.F.1    Yoshimoto, K.2    Nghiemphu, P.3
  • 194
    • 67749110462 scopus 로고    scopus 로고
    • Oral rapamycin reduces tumour burden and vascularization in Lkb1(+/-) mice
    • Robinson J, Lai C, Martin A, Nye E, Tomlinson I, Silver A. Oral rapamycin reduces tumour burden and vascularization in Lkb1(+/-) mice. J Pathol 2009; 219: 35-40.
    • (2009) J Pathol , vol.219 , pp. 35-40
    • Robinson, J.1    Lai, C.2    Martin, A.3    Nye, E.4    Tomlinson, I.5    Silver, A.6
  • 195
    • 58749097239 scopus 로고    scopus 로고
    • LKB1/KRAS mutant lung cancers constitute a genetic subset of NSCLC with increased sensitivity to MAPK and mTOR signalling inhibition
    • Mahoney CL, Choudhury B, Davies H, et al. LKB1/KRAS mutant lung cancers constitute a genetic subset of NSCLC with increased sensitivity to MAPK and mTOR signalling inhibition. Br J Cancer 2009; 100: 370-5.
    • (2009) Br J Cancer , vol.100 , pp. 370-375
    • Mahoney, C.L.1    Choudhury, B.2    Davies, H.3
  • 196
    • 62749135926 scopus 로고    scopus 로고
    • Chemopreventive efficacy of rapamycin on Peutz-Jeghers syndrome in a mouse model
    • Wei C, Amos CI, Zhang N, Zhu J, Wang X, Frazier ML. Chemopreventive efficacy of rapamycin on Peutz-Jeghers syndrome in a mouse model. Cancer Lett 2009; 277: 149-54.
    • (2009) Cancer Lett , vol.277 , pp. 149-154
    • Wei, C.1    Amos, C.I.2    Zhang, N.3    Zhu, J.4    Wang, X.5    Frazier, M.L.6
  • 197
    • 84867112902 scopus 로고    scopus 로고
    • Altered LKB1/AMPK/TSC1/TSC2/mTOR signaling causes disruption of Sertoli cell polarity and spermatogenesis
    • Tanwar PS, Kaneko-Tarui T, Zhang L, Teixeira JM. Altered LKB1/AMPK/TSC1/TSC2/mTOR signaling causes disruption of Sertoli cell polarity and spermatogenesis. Hum Mol Genet 2012; 21: 4394-405.
    • (2012) Hum Mol Genet , vol.21 , pp. 4394-4405
    • Tanwar, P.S.1    Kaneko-Tarui, T.2    Zhang, L.3    Teixeira, J.M.4
  • 198
    • 84875325305 scopus 로고    scopus 로고
    • Hsp90, an unlikely ally in the war on cancer
    • Barrott JJ, Haystead TA. Hsp90, an unlikely ally in the war on cancer. FEBS J 2013; 280: 1381-96.
    • (2013) FEBS J , vol.280 , pp. 1381-1396
    • Barrott, J.J.1    Haystead, T.A.2
  • 199
    • 84865695733 scopus 로고    scopus 로고
    • Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition
    • Taipale M, Krykbaeva I, Koeva M, et al. Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition. Cell 2012; 150: 987-1001.
    • (2012) Cell , vol.150 , pp. 987-1001
    • Taipale, M.1    Krykbaeva, I.2    Koeva, M.3
  • 201
    • 18444404925 scopus 로고    scopus 로고
    • Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: Implications for cancer therapy
    • Citri A, Alroy I, Lavi S, et al. Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: implications for cancer therapy. EMBO J 2002; 21: 2407-17.
    • (2002) EMBO J , vol.21 , pp. 2407-2417
    • Citri, A.1    Alroy, I.2    Lavi, S.3
  • 202
    • 0033863883 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
    • An WG, Schulte TW, Neckers LM. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ 2000; 11: 355-60.
    • (2000) Cell Growth Differ , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 203
    • 0035877701 scopus 로고    scopus 로고
    • Specific association of a set of molecular chaperones including HSP90 and Cdc37 with MOK, a member of the mitogen-activated protein kinase superfamily
    • Miyata Y, Ikawa Y, Shibuya M, Nishida E. Specific association of a set of molecular chaperones including HSP90 and Cdc37 with MOK, a member of the mitogen-activated protein kinase superfamily. J Biol Chem 2001; 276: 21841-48.
    • (2001) J Biol Chem , vol.276 , pp. 21841-21848
    • Miyata, Y.1    Ikawa, Y.2    Shibuya, M.3    Nishida, E.4
  • 204
    • 84875519144 scopus 로고    scopus 로고
    • Targeting the molecular chaperone heat shock protein 90 (HSP90): Lessons learned and future directions
    • Hong DS, Banerji U, Tavana B, George GC, Aaron J, Kurzrock R. Targeting the molecular chaperone heat shock protein 90 (HSP90): lessons learned and future directions. Cancer Treat Rev 2013; 39: 375-87.
    • (2013) Cancer Treat Rev , vol.39 , pp. 375-387
    • Hong, D.S.1    Banerji, U.2    Tavana, B.3    George, G.C.4    Aaron, J.5    Kurzrock, R.6
  • 205
    • 84857994615 scopus 로고    scopus 로고
    • HSP90 inhibition: Two-pronged exploitation of cancer dependencies
    • Travers J, Sharp S, Workman P. HSP90 inhibition: two-pronged exploitation of cancer dependencies. Drug Discov Today 2012; 17: 242-52.
    • (2012) Drug Discov Today , vol.17 , pp. 242-252
    • Travers, J.1    Sharp, S.2    Workman, P.3
  • 206
    • 84876717451 scopus 로고    scopus 로고
    • Hsp90 inhibitors as anti-cancer agents, from basic discoveries to clinical development
    • Soga S, Akinaga S, Shiotsu Y. Hsp90 inhibitors as anti-cancer agents, from basic discoveries to clinical development. Curr Pharm Des 2013; 19: 366-76.
    • (2013) Curr Pharm Des , vol.19 , pp. 366-376
    • Soga, S.1    Akinaga, S.2    Shiotsu, Y.3
  • 207
    • 61449182121 scopus 로고    scopus 로고
    • Principles of cancer therapy: Oncogene and non-oncogene addiction
    • Luo J, Solimini NL, Elledge SJ. Principles of cancer therapy: oncogene and non-oncogene addiction. Cell 2009; 136: 823-37.
    • (2009) Cell , vol.136 , pp. 823-837
    • Luo, J.1    Solimini, N.L.2    Elledge, S.J.3
  • 208
    • 84863652136 scopus 로고    scopus 로고
    • Circumventing cancer drug resistance in the era of personalized medicine
    • Garraway LA, Janne PA. Circumventing cancer drug resistance in the era of personalized medicine. Cancer Discov 2012; 2: 214-226.
    • (2012) Cancer Discov , vol.2 , pp. 214-226
    • Garraway, L.A.1    Janne, P.A.2
  • 209
    • 44649139884 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibition in lung cancer
    • Shimamura T, Shapiro GI. Heat shock protein 90 inhibition in lung cancer. J Thoracic Oncol 2008; 3: S152-9.
    • (2008) J Thoracic Oncol , vol.3 , pp. 152-159
    • Shimamura, T.1    Shapiro, G.I.2
  • 210
    • 84860533156 scopus 로고    scopus 로고
    • The HSP90 inhibitor XL888 overcomes BRAF inhibitor resistance mediated through diverse mechanisms
    • Paraiso KH, Haarberg HE, Wood E, et al. The HSP90 inhibitor XL888 overcomes BRAF inhibitor resistance mediated through diverse mechanisms. Clin Cancer Res 2012; 18: 2502-14.
    • (2012) Clin Cancer Res , vol.18 , pp. 2502-2514
    • Paraiso, K.H.1    Haarberg, H.E.2    Wood, E.3
  • 211
    • 0037444766 scopus 로고    scopus 로고
    • Heatshock protein 90 and Cdc37 interact with LKB1 and regulate its stability
    • Boudeau J, Deak M, Lawlor MA, Morrice NA, Alessi DR. Heatshock protein 90 and Cdc37 interact with LKB1 and regulate its stability. Biochem J 2003; 370: 849-57.
    • (2003) Biochem J , vol.370 , pp. 849-857
    • Boudeau, J.1    Deak, M.2    Lawlor, M.A.3    Morrice, N.A.4    Alessi, D.R.5
  • 212
    • 0346057795 scopus 로고    scopus 로고
    • Stability of the Peutz-Jeghers syndrome kinase LKB1 requires its binding to the molecular chaperones Hsp90/Cdc37
    • Nony P, Gaude H, Rossel M, Fournier L, Rouault JP, Billaud M. Stability of the Peutz-Jeghers syndrome kinase LKB1 requires its binding to the molecular chaperones Hsp90/Cdc37. Oncogene 2003; 22: 9165-75.
    • (2003) Oncogene , vol.22 , pp. 9165-9175
    • Nony, P.1    Gaude, H.2    Rossel, M.3    Fournier, L.4    Rouault, J.P.5    Billaud, M.6
  • 213
    • 84860407614 scopus 로고    scopus 로고
    • Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1
    • Gaude H, Aznar N, Delay A, et al. Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1. Oncogene 2012; 31: 1582-91.
    • (2012) Oncogene , vol.31 , pp. 1582-1591
    • Gaude, H.1    Aznar, N.2    Delay, A.3
  • 214
    • 84859187259 scopus 로고    scopus 로고
    • Systematic identification of genomic markers of drug sensitivity in cancer cells
    • Garnett MJ, Edelman EJ, Heidorn SJ, et al. Systematic identification of genomic markers of drug sensitivity in cancer cells. Nature 2012; 483: 570-5.
    • (2012) Nature , vol.483 , pp. 570-575
    • Garnett, M.J.1    Edelman, E.J.2    Heidorn, S.J.3
  • 215
    • 77649090075 scopus 로고    scopus 로고
    • Cyclooxygenase-2 and cancer treatment: Understanding the risk should be worth the reward
    • Menter DG, Schilsky RL, DuBois RN. Cyclooxygenase-2 and cancer treatment: understanding the risk should be worth the reward. Clin Cancer Res 2010; 16: 1384-90.
    • (2010) Clin Cancer Res , vol.16 , pp. 1384-1390
    • Menter, D.G.1    Schilsky, R.L.2    DuBois, R.N.3
  • 216
    • 39849093868 scopus 로고    scopus 로고
    • AMP-activated protein kinase is involved in COX-2 expression in response to ultrasound in cultured osteoblasts
    • Hou CH, Tan TW, Tang CH. AMP-activated protein kinase is involved in COX-2 expression in response to ultrasound in cultured osteoblasts. Cell Signal 2008; 20: 978-88.
    • (2008) Cell Signal , vol.20 , pp. 978-988
    • Hou, C.H.1    Tan, T.W.2    Tang, C.H.3
  • 219
    • 56749159779 scopus 로고    scopus 로고
    • UVB irradiation regulates Cox-2 mRNA stability through AMPK and HuR in human keratinocytes
    • Zhang J, Bowden GT. UVB irradiation regulates Cox-2 mRNA stability through AMPK and HuR in human keratinocytes. Mol Carcinog 2008; 47: 974-83.
    • (2008) Mol Carcinog , vol.47 , pp. 974-983
    • Zhang, J.1    Bowden, G.T.2
  • 220
    • 0030606299 scopus 로고    scopus 로고
    • Suppression of intestinal polyposis in Apc 716 knockout mice by inhibition of cyclooxygenase 2 (COX-2)
    • Oshima M, Dinchuk JE, Kargman SL, et al. Suppression of intestinal polyposis in Apc 716 knockout mice by inhibition of cyclooxygenase 2 (COX-2). Cell 1996; 87: 803-9.
    • (1996) Cell , vol.87 , pp. 803-809
    • Oshima, M.1    Dinchuk, J.E.2    Kargman, S.L.3
  • 221
    • 0034796261 scopus 로고    scopus 로고
    • Acceleration of intestinal polyposis through prostaglandin receptor EP2 in Apc 716 knockout mice
    • Sonoshita M, Takaku K, Sasaki N, et al. Acceleration of intestinal polyposis through prostaglandin receptor EP2 in Apc 716 knockout mice. Nat Med 2001; 7: 1048-51.
    • (2001) Nat Med , vol.7 , pp. 1048-1051
    • Sonoshita, M.1    Takaku, K.2    Sasaki, N.3
  • 222
    • 0034098691 scopus 로고    scopus 로고
    • Biology of the adenomatous polyposis coli tumor suppressor
    • Goss KH, Groden J. Biology of the adenomatous polyposis coli tumor suppressor. J Clin Oncol 2000; 18: 1967-79.
    • (2000) J Clin Oncol , vol.18 , pp. 1967-1979
    • Goss, K.H.1    Groden, J.2
  • 223
    • 1542269250 scopus 로고    scopus 로고
    • Simultaneous expression of COX-2 and mPGES-1 in mouse gastrointestinal hamartomas
    • Takeda H, Miyoshi H, Tamai Y, Oshima M, Taketo MM. Simultaneous expression of COX-2 and mPGES-1 in mouse gastrointestinal hamartomas. Br J Cancer 2004; 90: 701-4.
    • (2004) Br J Cancer , vol.90 , pp. 701-704
    • Takeda, H.1    Miyoshi, H.2    Tamai, Y.3    Oshima, M.4    Taketo, M.M.5
  • 224
    • 33845411885 scopus 로고    scopus 로고
    • The LKB1 tumor suppressor kinase in human disease
    • Katajisto P, Vallenius T, Vaahtomeri K, et al. The LKB1 tumor suppressor kinase in human disease. Bioch Biophys 2007; 1775: 63-75.
    • (2007) Bioch Biophys , vol.1775 , pp. 63-75
    • Katajisto, P.1    Vallenius, T.2    Vaahtomeri, K.3
  • 225
    • 0344862109 scopus 로고    scopus 로고
    • Correlation of staining for LKB1 and COX-2 in hamartomatous polyps and carcinomas from patients with Peutz-Jeghers syndrome
    • Wei C, Amos CI, Rashid A, et al. Correlation of staining for LKB1 and COX-2 in hamartomatous polyps and carcinomas from patients with Peutz-Jeghers syndrome. J Histochem Cytochem 2003; 51: 1665-72.
    • (2003) J Histochem Cytochem , vol.51 , pp. 1665-1672
    • Wei, C.1    Amos, C.I.2    Rashid, A.3
  • 226
    • 12444302178 scopus 로고    scopus 로고
    • Cyclooxygenase 2 expression and molecular alterations in Peutz-Jeghers hamartomas and carcinomas
    • De Leng WW, Westerman AM, Weterman MA, et al. Cyclooxygenase 2 expression and molecular alterations in Peutz-Jeghers hamartomas and carcinomas. Clin Cancer Res 2003; 9: 3065-72.
    • (2003) Clin Cancer Res , vol.9 , pp. 3065-3072
    • De Leng, W.W.1    Westerman, A.M.2    Weterman, M.A.3
  • 228
    • 41349114071 scopus 로고    scopus 로고
    • LKB1 signaling in mesenchymal cells required for suppression of gastrointestinal polyposis
    • Katajisto P, Vaahtomeri K, Ekman N, et al. LKB1 signaling in mesenchymal cells required for suppression of gastrointestinal polyposis. Nat Genet 2008; 40: 455-9.
    • (2008) Nat Genet , vol.40 , pp. 455-459
    • Katajisto, P.1    Vaahtomeri, K.2    Ekman, N.3
  • 229
    • 5144232989 scopus 로고    scopus 로고
    • Suppression of Peutz-Jeghers polyposis by inhibition of cyclooxygenase-2
    • Udd L, Katajisto P, Rossi DJ, et al. Suppression of Peutz-Jeghers polyposis by inhibition of cyclooxygenase-2. Gastroenterology 2004; 127: 1030-7.
    • (2004) Gastroenterology , vol.127 , pp. 1030-1037
    • Udd, L.1    Katajisto, P.2    Rossi, D.J.3
  • 230
    • 0041438603 scopus 로고    scopus 로고
    • Cooperation of cyclooxygenase 1 and cyclooxygenase 2 in intestinal polyposis
    • Takeda H, Sonoshita M, Oshima H, et al. Cooperation of cyclooxygenase 1 and cyclooxygenase 2 in intestinal polyposis. Cancer Res 2003; 63: 4872-7.
    • (2003) Cancer Res , vol.63 , pp. 4872-4877
    • Takeda, H.1    Sonoshita, M.2    Oshima, H.3
  • 231
    • 78650746613 scopus 로고    scopus 로고
    • LKB1/PEA3/αNp63 pathway regulates PTGS-2 (COX-2) transcription in lung cancer cells upon cigarette smoke exposure
    • Ratovitski EA. LKB1/PEA3/αNp63 pathway regulates PTGS-2 (COX-2) transcription in lung cancer cells upon cigarette smoke exposure. Oxid Med Cell Longev 2010; 3: 317-24.
    • (2010) Oxid Med Cell Longev , vol.3 , pp. 317-324
    • Ratovitski, E.A.1
  • 232
    • 84879074624 scopus 로고    scopus 로고
    • Liver Kinase B1 Is Required for Thromboxane Receptor-Dependent Nuclear Factor-βB Activation and Inflammatory Responses
    • He J, Zhou Y, Xing J, et al. Liver Kinase B1 Is Required for Thromboxane Receptor-Dependent Nuclear Factor-βB Activation and Inflammatory Responses. Arterioscler Thromb Vasc Biol 2013; 33: 1297-305.
    • (2013) Arterioscler Thromb Vasc Biol , vol.33 , pp. 1297-1305
    • He, J.1    Zhou, Y.2    Xing, J.3
  • 233
    • 82055161852 scopus 로고    scopus 로고
    • Cyclooxygenase as a target for colorectal cancer chemoprevention
    • Moreira L, Castells A. Cyclooxygenase as a target for colorectal cancer chemoprevention. Curr Drug Targets 2011; 12: 1888-94.
    • (2011) Curr Drug Targets , vol.12 , pp. 1888-1894
    • Moreira, L.1    Castells, A.2
  • 234
    • 41349104451 scopus 로고    scopus 로고
    • Chemoprevention of colorectal neoplasia: The potential for personalized medicine
    • Arber N, Levin B. Chemoprevention of colorectal neoplasia: the potential for personalized medicine. Gastroenterology 2008; 134: 1224-37.
    • (2008) Gastroenterology , vol.134 , pp. 1224-1237
    • Arber, N.1    Levin, B.2
  • 235
    • 76849095665 scopus 로고    scopus 로고
    • The role of COX-2 in intestinal inflammation and colorectal cancer
    • Wang D, Dubois RN. The role of COX-2 in intestinal inflammation and colorectal cancer. Oncogene 2010; 29: 781-8.
    • (2010) Oncogene , vol.29 , pp. 781-788
    • Wang, D.1    Dubois, R.N.2
  • 236
    • 66849099322 scopus 로고    scopus 로고
    • Targeted genetic disruption of peroxisome proliferator-activated receptor-delta and colonic tumorigenesis
    • Zuo X, Peng Z, Moussalli MJ, et al. Targeted genetic disruption of peroxisome proliferator-activated receptor-delta and colonic tumorigenesis. J Natl Cancer Inst 2009; 101: 762-767.
    • (2009) J Natl Cancer Inst , vol.101 , pp. 762-767
    • Zuo, X.1    Peng, Z.2    Moussalli, M.J.3
  • 237
    • 0037081194 scopus 로고    scopus 로고
    • Cyclooxygenase 2-and prostaglandin E(2) receptor EP(2)-dependent angiogenesis in Apc(Delta716) mouse intestinal polyps
    • Seno H, Oshima M, Ishikawa TO, et al. Cyclooxygenase 2-and prostaglandin E(2) receptor EP(2)-dependent angiogenesis in Apc(Delta716) mouse intestinal polyps. Cancer Res 2002; 62: 506-11.
    • (2002) Cancer Res , vol.62 , pp. 506-511
    • Seno, H.1    Oshima, M.2    Ishikawa, T.O.3
  • 238
    • 0035903028 scopus 로고    scopus 로고
    • Vascular abnormalities and deregulation of VEGF in Lkb1-deficient mice
    • Ylikorkala A, Rossi DJ, Korsisaari N, et al. Vascular abnormalities and deregulation of VEGF in Lkb1-deficient mice. Science 2001; 293: 1323-6.
    • (2001) Science , vol.293 , pp. 1323-1326
    • Ylikorkala, A.1    Rossi, D.J.2    Korsisaari, N.3
  • 239
    • 84885094670 scopus 로고    scopus 로고
    • N-Methylnitrosourea aggravates gastrointestinal polyposis in Lkb1+/-mice
    • Udd L, Gao Y, Ristimäki AP, Mäkelä TP. N-Methylnitrosourea aggravates gastrointestinal polyposis in Lkb1+/-mice. Carcinogenesis 2013; 34(10): 2409-14.
    • (2013) Carcinogenesis , vol.34 , Issue.10 , pp. 2409-2414
    • Udd, L.1    Gao, Y.2    Ristimäki, A.P.3    Mäkelä, T.P.4
  • 240
    • 17744418769 scopus 로고    scopus 로고
    • The effect of celecoxib, a cyclooxygenase-2 inhibitor, in familial adenomatous polyposis
    • Steinbach G, Lynch PM, Phillips RKS, et al. The effect of celecoxib, a cyclooxygenase-2 inhibitor, in familial adenomatous polyposis. N Engl J Med 2000; 342: 1946-52.
    • (2000) N Engl J Med , vol.342 , pp. 1946-1952
    • Steinbach, G.1    Lynch, P.M.2    Phillips, R.K.S.3
  • 241
    • 0038070069 scopus 로고    scopus 로고
    • Cyclooxygenase-2 expression and effect of celecoxib in gastric adenomas of trefoil factor 1-deficient mice
    • Saukkonen K, Tomasetto C, Narko K, Rio MC, Ristimaki A. Cyclooxygenase-2 expression and effect of celecoxib in gastric adenomas of trefoil factor 1-deficient mice. Cancer Res 2003; 63: 3032-6.
    • (2003) Cancer Res , vol.63 , pp. 3032-3036
    • Saukkonen, K.1    Tomasetto, C.2    Narko, K.3    Rio, M.C.4    Ristimaki, A.5
  • 242
    • 68449084677 scopus 로고    scopus 로고
    • The role of Src in solid tumors
    • Wheeler DL, Iida M, Dunn EF. The role of Src in solid tumors. Oncologist 2009; 14: 667-78.
    • (2009) Oncologist , vol.14 , pp. 667-678
    • Wheeler, D.L.1    Iida, M.2    Dunn, E.F.3
  • 244
    • 84872684334 scopus 로고    scopus 로고
    • Estrogen receptor signaling as a target for novel breast cancer therapeutics
    • Renoir JM, Marsaud V, Lazennec G. Estrogen receptor signaling as a target for novel breast cancer therapeutics. Biochem Pharmacol 2013; 85: 449-65.
    • (2013) Biochem Pharmacol , vol.85 , pp. 449-465
    • Renoir, J.M.1    Marsaud, V.2    Lazennec, G.3
  • 245
    • 77950491674 scopus 로고    scopus 로고
    • Phase I/II study of the Src inhibitor dasatinib in combination with erlotinib in advanced non-small-cell lung cancer
    • Haura EB, Tanvetyanon T, Chiappori A, et al. Phase I/II study of the Src inhibitor dasatinib in combination with erlotinib in advanced non-small-cell lung cancer. J Clin Oncol 2010; 28: 1387-94.
    • (2010) J Clin Oncol , vol.28 , pp. 1387-1394
    • Haura, E.B.1    Tanvetyanon, T.2    Chiappori, A.3
  • 246
    • 54549086723 scopus 로고    scopus 로고
    • Src family kinase oncogenic potential and pathways in prostate cancer as revealed by AZD0530
    • Chang YM, Bai L, Liu S, Yang JC, Kung HJ, Evans CP. Src family kinase oncogenic potential and pathways in prostate cancer as revealed by AZD0530. Oncogene 2008; 27: 6365-75.
    • (2008) Oncogene , vol.27 , pp. 6365-6375
    • Chang, Y.M.1    Bai, L.2    Liu, S.3    Yang, J.C.4    Kung, H.J.5    Evans, C.P.6
  • 247
    • 77953238558 scopus 로고    scopus 로고
    • Integrative genomic and proteomic analyses identify targets for Lkb1-deficient metastatic lung tumors
    • Carretero J, Shimamura T, Rikova K, et al. Integrative genomic and proteomic analyses identify targets for Lkb1-deficient metastatic lung tumors. Cancer Cell 2010; 17: 547-59.
    • (2010) Cancer Cell , vol.17 , pp. 547-559
    • Carretero, J.1    Shimamura, T.2    Rikova, K.3
  • 248
    • 31144459985 scopus 로고    scopus 로고
    • Oncogenic pathway signatures in human cancers as a guide to targeted therapies
    • Bild AH, Yao G, Chang JT, et al. Oncogenic pathway signatures in human cancers as a guide to targeted therapies. Nature 2006; 439: 353-7.
    • (2006) Nature , vol.439 , pp. 353-357
    • Bild, A.H.1    Yao, G.2    Chang, J.T.3
  • 249
    • 57349194139 scopus 로고    scopus 로고
    • Effective use of PI3K and MEK inhibitors to treat mutant Kras G12D and PIK3CA H1047R murine lung cancers
    • Engelman JA, Chen L, Tan X, et al. Effective use of PI3K and MEK inhibitors to treat mutant Kras G12D and PIK3CA H1047R murine lung cancers. Nat Med 2008; 14: 1351-6.
    • (2008) Nat Med , vol.14 , pp. 1351-1356
    • Engelman, J.A.1    Chen, L.2    Tan, X.3
  • 250
    • 77953239772 scopus 로고    scopus 로고
    • LKB1 and Src: Antagonistic regulators of tumor growth and metastasis
    • Slack-Davis J, Dasilva JO, Parsons SJ. LKB1 and Src: antagonistic regulators of tumor growth and metastasis. Cancer Cell 2010; 17: 527-9.
    • (2010) Cancer Cell , vol.17 , pp. 527-529
    • Slack-Davis, J.1    Dasilva, J.O.2    Parsons, S.J.3
  • 251
    • 58649110598 scopus 로고    scopus 로고
    • Oncogenic B-RAF negatively regulates the tumor suppressor LKB1 to promote melanoma cell proliferation
    • Zheng B, Jeong JH, Asara JM, et al. Oncogenic B-RAF negatively regulates the tumor suppressor LKB1 to promote melanoma cell proliferation. Mol Cell 2009; 33: 237-47.
    • (2009) Mol Cell , vol.33 , pp. 237-247
    • Zheng, B.1    Jeong, J.H.2    Asara, J.M.3
  • 252
    • 62849094740 scopus 로고    scopus 로고
    • Uncoupling of the LKB1-AMPKalpha energy sensor pathway by growth factors and oncogenic BRAF
    • Esteve-Puig R, Canals F, Colomé N, Merlino G, Recio JA. Uncoupling of the LKB1-AMPKalpha energy sensor pathway by growth factors and oncogenic BRAF. PLoS One 2009; 4: e4771.
    • (2009) PLoS One , vol.4
    • Esteve-Puig, R.1    Canals, F.2    Colomé, N.3    Merlino, G.4    Recio, J.A.5
  • 253
    • 58749097239 scopus 로고    scopus 로고
    • LKB1/KRAS mutant lung cancers constitute a genetic subset of NSCLC with increased sensitivity to MAPK and mTOR signalling inhibition
    • Mahoney CL, Choudhury B, Davies H, et al. LKB1/KRAS mutant lung cancers constitute a genetic subset of NSCLC with increased sensitivity to MAPK and mTOR signalling inhibition. Br J Cancer 2009; 100: 370-5.
    • (2009) Br J Cancer , vol.100 , pp. 370-375
    • Mahoney, C.L.1    Choudhury, B.2    Davies, H.3
  • 254
    • 84881508779 scopus 로고    scopus 로고
    • Metabolic and Functional Genomic Studies Identify Deoxythymidylate Kinase as a target in LKB1 Mutant Lung Cancer
    • Liu Y, Marks K, Cowley GS, et al. Metabolic and Functional Genomic Studies Identify Deoxythymidylate Kinase as a target in LKB1 Mutant Lung Cancer. Cancer Discov 2013; 3: 870-879.
    • (2013) Cancer Discov , vol.3 , pp. 870-879
    • Liu, Y.1    Marks, K.2    Cowley, G.S.3
  • 255
    • 20244388673 scopus 로고    scopus 로고
    • Inhibition of human Chk1 causes increased initiation of DNA replication, phosphorylation of ATR targets, and DNA breakage
    • Syljuåsen RG, Sørensen CS, Hansen LT, et al. Inhibition of human Chk1 causes increased initiation of DNA replication, phosphorylation of ATR targets, and DNA breakage. Mol Cell Biol 2005; 25: 3553-62.
    • (2005) Mol Cell Biol , vol.25 , pp. 3553-3562
    • Syljuåsen, R.G.1    Sørensen, C.S.2    Hansen, L.T.3
  • 256
    • 79651470785 scopus 로고    scopus 로고
    • Death by releasing the breaks: CHK1 inhibitors as cancer therapeutics
    • Ma CX, Janetka JW, Piwnica-Worms H. Death by releasing the breaks: CHK1 inhibitors as cancer therapeutics. Trends Mol Med 2011; 17: 88-96.
    • (2011) Trends Mol Med , vol.17 , pp. 88-96
    • Ma, C.X.1    Janetka, J.W.2    Piwnica-Worms, H.3
  • 257
    • 65449142073 scopus 로고    scopus 로고
    • CHK1 inhibition as a strategy for targeting Fanconi Anemia (FA) DNA repair pathway deficient tumors
    • Chen CC, Kennedy RD, Sidi S, Look AT, D'Andrea A. CHK1 inhibition as a strategy for targeting Fanconi Anemia (FA) DNA repair pathway deficient tumors. Mol Cancer 2009; 8: 24.
    • (2009) Mol Cancer , vol.8 , pp. 24
    • Chen, C.C.1    Kennedy, R.D.2    Sidi, S.3    Look, A.T.4    D'Andrea, A.5
  • 258
    • 79955686677 scopus 로고    scopus 로고
    • CHK1 inhibitors in combination chemotherapy: Thinking beyond the cell cycle
    • Dent P, Tang Y, Yacoub A, Dai Y, Fisher PB, Grant S. CHK1 inhibitors in combination chemotherapy: thinking beyond the cell cycle. Mol Interv 2011; 11: 133-40.
    • (2011) Mol Interv , vol.11 , pp. 133-140
    • Dent, P.1    Tang, Y.2    Yacoub, A.3    Dai, Y.4    Fisher, P.B.5    Grant, S.6
  • 259
    • 34247481285 scopus 로고    scopus 로고
    • Targeting checkpoint kinase 1 in cancer therapeutics
    • Tse AN, Carvajal R, Schwartz GK. Targeting checkpoint kinase 1 in cancer therapeutics. Clin Cancer Res 2007; 13: 1955-60.
    • (2007) Clin Cancer Res , vol.13 , pp. 1955-1960
    • Tse, A.N.1    Carvajal, R.2    Schwartz, G.K.3
  • 260
    • 0023925454 scopus 로고
    • Interactions between deoxyribonucleotide and DNA synthesis
    • Reichard P. Interactions between deoxyribonucleotide and DNA synthesis. Annu Rev Biochem 1988; 57: 349-74.
    • (1988) Annu Rev Biochem , vol.57 , pp. 349-374
    • Reichard, P.1
  • 261
    • 0031725620 scopus 로고    scopus 로고
    • Thymine metabolism and thymineless death in prokaryotes and eukaryotes
    • Ahmad SI, Kirk SH, Eisenstark A. Thymine metabolism and thymineless death in prokaryotes and eukaryotes. Annu Rev Microbiol 1998; 52: 591-625.
    • (1998) Annu Rev Microbiol , vol.52 , pp. 591-625
    • Ahmad, S.I.1    Kirk, S.H.2    Eisenstark, A.3
  • 262
    • 84862777541 scopus 로고    scopus 로고
    • A murine lung cancer coclinical trial identifies genetic modifiers of therapeutic response
    • Chen Z, Cheng K, Walton Z, et al. A murine lung cancer coclinical trial identifies genetic modifiers of therapeutic response. Nature 2012; 483: 613-7.
    • (2012) Nature , vol.483 , pp. 613-617
    • Chen, Z.1    Cheng, K.2    Walton, Z.3


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