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Volumn 31, Issue 9, 2010, Pages 1154-1164

Autophagic pathways as new targets for cancer drug development

Author keywords

autophagy; autophagy related gene (ATG), Beclin 1; Bcl 2; cancer; Class III and I PI3K; mTOR; p53

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BECLIN 1; BIM PROTEIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE KINASE; DNA; ELONGATION FACTOR 2 KINASE; GLYCOGEN SYNTHASE KINASE 3ALPHA; GLYCOGEN SYNTHASE KINASE 3BETA; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN INHIBITOR; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PLECKSTRIN; PROTEIN BAD; PROTEIN BCL 2; PROTEIN KINASE B; PROTEIN KINASE LKB1; PROTEIN MDM2; PROTEIN P53; PROTEIN SH2; PROTEIN TYROSINE KINASE; SNARE PROTEIN; STRESS ACTIVATED PROTEIN KINASE 1; TRANSCRIPTION FACTOR FOXO; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TUBERIN; UNINDEXED DRUG;

EID: 77956363593     PISSN: 16714083     EISSN: 17457254     Source Type: Journal    
DOI: 10.1038/aps.2010.118     Document Type: Review
Times cited : (107)

References (120)
  • 1
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451: 1069-1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 2
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008; 132: 27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 5
    • 34347394714 scopus 로고    scopus 로고
    • Targeting autophagy augments the anticancer activity of the histone deacetylase inhibitor SAHA to overcome Bcr-Abl-mediated drug resistance
    • Carew JS, Nawrocki ST, Kahue CN, Zhang H, Yang C, Chung L, et al. Targeting autophagy augments the anticancer activity of the histone deacetylase inhibitor SAHA to overcome Bcr-Abl-mediated drug resistance. Blood 2007; 110: 313-322
    • (2007) Blood , vol.110 , pp. 313-322
    • Carew, J.S.1    Nawrocki, S.T.2    Kahue, C.N.3    Zhang, H.4    Yang, C.5    Chung, L.6
  • 6
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagydefective mutants of Saccharomyces cerevisiae
    • Tsukada M, Ohsumi Y. Isolation and characterization of autophagydefective mutants of Saccharomyces cerevisiae. FEBS Lett 1993; 333:169-174
    • (1993) FEBS Lett , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 7
    • 57649195400 scopus 로고    scopus 로고
    • Autophagy and multivesicular bodies: Two closely related partners
    • Fader CM, Colombo MI. Autophagy and multivesicular bodies: two closely related partners. Cell Death Differ 2009; 16: 70-78
    • (2009) Cell Death Differ , vol.16 , pp. 70-78
    • Fader, C.M.1    Colombo, M.I.2
  • 8
    • 48949098967 scopus 로고    scopus 로고
    • New insights into the mechanisms of macroautophagy in mammalian cells
    • Eskelinen EL. New insights into the mechanisms of macroautophagy in mammalian cells. Int Rev Cell Mol Biol 2008; 266: 207-247
    • (2008) Int Rev Cell Mol Biol , vol.266 , pp. 207-247
    • Eskelinen, E.L.1
  • 9
    • 47149103494 scopus 로고    scopus 로고
    • Toward unraveling membrane biogenesis in mammalian autophagy
    • Yoshimori T, Noda T. Toward unraveling membrane biogenesis in mammalian autophagy. Curr Opin Cell Biol 2008; 20: 401-407
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 401-407
    • Yoshimori, T.1    Noda, T.2
  • 10
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S, Loewith R, Hall MN. TOR signaling in growth and metabolism. Cell 2006; 124: 471-484
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 12
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase y sorting in Saccharomyces cerevisiae
    • Kihara A, Noda T, Ishihara N, Ohsumi Y. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J Cell Biol 2001; 152: 519-530
    • (2001) J Cell Biol , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 13
    • 0028964232 scopus 로고
    • Vesicle-mediated protein transport: Regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeast
    • Stack JH, DeWald DB, Takegawa K, Emr SD. Vesicle-mediated protein transport: regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeast. J Cell Biol 1995; 129: 321-334.
    • (1995) J Cell Biol , vol.129 , pp. 321-334
    • Stack, J.H.1    Dewald, D.B.2    Takegawa, K.3    Emr, S.D.4
  • 14
    • 33745751085 scopus 로고    scopus 로고
    • Autophagic and tumour suppressor activity of a novel Beclin 1-binding protein UVRAG
    • Liang C, Feng P, Ku B, Dotan I, Canaani D, Oh BH, et al. Autophagic and tumour suppressor activity of a novel Beclin 1-binding protein UVRAG. Nat Cell Biol 2006; 8: 688-699
    • (2006) Nat Cell Biol , vol.8 , pp. 688-699
    • Liang, C.1    Feng, P.2    Ku, B.3    Dotan, I.4    Canaani, D.5    Oh, B.H.6
  • 15
    • 34848899280 scopus 로고    scopus 로고
    • Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis
    • Takahashi Y, Coppola D, Matsushita N, Cualing HD, Sun M, Sato Y, et al. Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis. Nat Cell Biol 2007; 9: 1142-1151
    • (2007) Nat Cell Biol , vol.9 , pp. 1142-1151
    • Takahashi, Y.1    Coppola, D.2    Matsushita, N.3    Cualing, H.D.4    Sun, M.5    Sato, Y.6
  • 16
    • 33745086418 scopus 로고    scopus 로고
    • Assortment of phosphatidylinositol 3-kinase complexes-Atg14p directs association of complex i to the pre-autophagosomal structure in Saccharomyces cerevisiae
    • Obara K, Sekito T, Ohsumi Y. Assortment of phosphatidylinositol 3-kinase complexes-Atg14p directs association of complex I to the pre-autophagosomal structure in Saccharomyces cerevisiae. Mol Biol Cell 2006; 17: 1527-1539
    • (2006) Mol Biol Cell , vol.17 , pp. 1527-1539
    • Obara, K.1    Sekito, T.2    Ohsumi, Y.3
  • 17
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • Itakura E, Kishi C, Inoue K, Mizushima N. Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol Biol Cell 2008; 19: 5360-5372
    • (2008) Mol Biol Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 18
    • 0035967888 scopus 로고    scopus 로고
    • Phoxy lipids: Revealing PX domains as phosphoinositide binding modules
    • Wishart MJ, Taylor GS, Dixon JE. Phoxy lipids: Revealing PX domains as phosphoinositide binding modules. Cell 2001; 105: 817-820
    • (2001) Cell , vol.105 , pp. 817-820
    • Wishart, M.J.1    Taylor, G.S.2    Dixon, J.E.3
  • 19
    • 0035871081 scopus 로고    scopus 로고
    • Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins
    • Gillooly DJ, Simonsen A, Stenmark H. Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins. Biochem J 2001; 355: 249-258
    • (2001) Biochem J , vol.355 , pp. 249-258
    • Gillooly, D.J.1    Simonsen, A.2    Stenmark, H.3
  • 20
    • 53049102656 scopus 로고    scopus 로고
    • The Atg18-Atg2 complex is recruited to autophagic membranes via phosphatidylinositol 3-phosphate and exerts an essential function
    • Obara K, Sekito T, Niimi K, Ohsumi Y. The Atg18-Atg2 complex is recruited to autophagic membranes via phosphatidylinositol 3-phosphate and exerts an essential function. J Biol Chem 2008; 283: 23972-23980
    • (2008) J Biol Chem , vol.283 , pp. 23972-23980
    • Obara, K.1    Sekito, T.2    Niimi, K.3    Ohsumi, Y.4
  • 22
    • 0033214582 scopus 로고    scopus 로고
    • Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast
    • Shintani T, Mizushima N, Ogawa Y, Matsuura A, Noda T, Ohsumi Y. Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J 1999; 18: 5234-5241
    • (1999) EMBO J , vol.18 , pp. 5234-5241
    • Shintani, T.1    Mizushima, N.2    Ogawa, Y.3    Matsuura, A.4    Noda, T.5    Ohsumi, Y.6
  • 24
    • 0038325675 scopus 로고    scopus 로고
    • Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate
    • Mizushima N, Kuma A, Kobayashi Y, Yamamoto A, Matsubae M, Takao T, et al. Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate. J Cell Sci 2003; 116: 1679-1688
    • (2003) J Cell Sci , vol.116 , pp. 1679-1688
    • Mizushima, N.1    Kuma, A.2    Kobayashi, Y.3    Yamamoto, A.4    Matsubae, M.5    Takao, T.6
  • 26
    • 0034676037 scopus 로고    scopus 로고
    • The reversible modi?cation regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway
    • Kirisako T, Ichimura Y, Okada H, Kabeya Y, Mizushima N, Yoshimori T, et al. The reversible modi?cation regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway. J Cell Biol 2000; 151: 263-276
    • (2000) J Cell Biol , vol.151 , pp. 263-276
    • Kirisako, T.1    Ichimura, Y.2    Okada, H.3    Kabeya, Y.4    Mizushima, N.5    Yoshimori, T.6
  • 27
    • 0035911162 scopus 로고    scopus 로고
    • Dissection of autophagosome formation using Apg5-de?cient mouse embryonic stem cells
    • Mizushima N, Yamamoto A, Hatano M, Kobayashi Y, Kabeya Y, Suzuki K, et al. Dissection of autophagosome formation using Apg5-de?cient mouse embryonic stem cells. J Cell Biol 2001; 152: 657-668
    • (2001) J Cell Biol , vol.152 , pp. 657-668
    • Mizushima, N.1    Yamamoto, A.2    Hatano, M.3    Kobayashi, Y.4    Kabeya, Y.5    Suzuki, K.6
  • 28
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • Hanada T, Noda NN, Satomi Y, Ichimura Y, Fujioka Y, Takao T, et al. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J Biol Chem 2007; 282: 37298-37302
    • (2007) J Biol Chem , vol.282 , pp. 37298-37302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3    Ichimura, Y.4    Fujioka, Y.5    Takao, T.6
  • 29
    • 33846010776 scopus 로고    scopus 로고
    • Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes
    • Fass E, Shvets E, Degani I, Hirschberg K, Elazar Z. Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes. J Biol Chem 2006; 281: 36303-36316
    • (2006) J Biol Chem , vol.281 , pp. 36303-36316
    • Fass, E.1    Shvets, E.2    Degani, I.3    Hirschberg, K.4    Elazar, Z.5
  • 30
    • 33645120442 scopus 로고    scopus 로고
    • Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes
    • Kochl R, Hu XW, Chan EY, Tooze S.A. Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes. Trafc 2006; 7: 129-145
    • (2006) Trafc , vol.7 , pp. 129-145
    • Kochl, R.1    Hu, X.W.2    Chan, E.Y.3    Tooze, S.A.4
  • 31
    • 70349969648 scopus 로고    scopus 로고
    • Apoptosis and autophagy: Targeting autophagy signaling in cancer cells -Trick or treats?
    • Elisabeth A C, Pietri P, Marja J. Apoptosis and autophagy: Targeting autophagy signaling in cancer cells -trick or treats? FEBS J 2009; 276: 6084-6096.
    • (2009) FEBS J , vol.276 , pp. 6084-6096
    • Elisabeth, A.C.1    Pietri, P.2    Marja, J.3
  • 32
    • 46449120732 scopus 로고    scopus 로고
    • Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic traf?cking
    • Liang C, Lee JS, Inn KS, Gack MU, Li Q, Roberts EA, et al. Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic traf?cking. Nat Cell Biol 2008; 10: 776-787
    • (2008) Nat Cell Biol , vol.10 , pp. 776-787
    • Liang, C.1    Lee, J.S.2    Inn, K.S.3    Gack, M.U.4    Li, Q.5    Roberts, E.A.6
  • 34
    • 9144240441 scopus 로고    scopus 로고
    • Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene
    • Qu X, Yu J, Bhagat G, Furuya N, Hibshoosh H, Troxel A, et al. Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene. J Clin Invest 2003; 112: 1809-1820
    • (2003) J Clin Invest , vol.112 , pp. 1809-1820
    • Qu, X.1    Yu, J.2    Bhagat, G.3    Furuya, N.4    Hibshoosh, H.5    Troxel, A.6
  • 35
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsuffcient tumor suppressor
    • Yue Z, Jin S, Yang C, Levine AJ, Heintz N. Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsuffcient tumor suppressor. Proc Natl Acad Sci USA 2003; 100: 15077-15082
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15077-15082
    • Yue, Z.1    Jin, S.2    Yang, C.3    Levine, A.J.4    Heintz, N.5
  • 36
    • 0344142468 scopus 로고    scopus 로고
    • Cloning and genomic organization of beclin 1, a candidate tumor suppressor gene on chromosome 17q21
    • Aita VM, Liang XH, Murty VV, Pincus DL, Yu W, Cayanis E, et al. Cloning and genomic organization of beclin 1, a candidate tumor suppressor gene on chromosome 17q21. Genomics 1999; 59: 59-65.
    • (1999) Genomics , vol.59 , pp. 59-65
    • Aita, V.M.1    Liang, X.H.2    Murty, V.V.3    Pincus, D.L.4    Yu, W.5    Cayanis, E.6
  • 37
    • 39049194057 scopus 로고    scopus 로고
    • The evolutionarily conserved domain of Beclin 1 is required for Vps34 binding, autophagy and tumor-suppressor function
    • Furuya N, Yu J, By?eld M, Pattingre S, Levine B. The evolutionarily conserved domain of Beclin 1 is required for Vps34 binding, autophagy and tumor-suppressor function. Autophagy 2005; 1: 46-52.
    • (2005) Autophagy , vol.1 , pp. 46-52
    • Furuya, N.1    Yu, J.2    Byeld, M.3    Pattingre, S.4    Levine, B.5
  • 38
    • 1242296021 scopus 로고    scopus 로고
    • Manipulation of nonsense mediated decay identi?es gene mutations in colon cancer cells with microsatellite instability
    • Ionov Y, Nowak N, Perucho M, Markowitz S, Cowell JK. Manipulation of nonsense mediated decay identi?es gene mutations in colon cancer cells with microsatellite instability. Oncogene 2004; 23: 639-645
    • (2004) Oncogene , vol.23 , pp. 639-645
    • Ionov, Y.1    Nowak, N.2    Perucho, M.3    Markowitz, S.4    Cowell, J.K.5
  • 41
    • 50449094644 scopus 로고    scopus 로고
    • Decreased expression of Bax-interacting factor-1 (Bif-1) in invasive urinary bladder and gallbladder cancers
    • Kim SY, Oh YL, Kim KM, Jeong EG, Kim MS, Yoo NJ, et al. Decreased expression of Bax-interacting factor-1 (Bif-1) in invasive urinary bladder and gallbladder cancers. Pathology 2008; 40: 553-557.
    • (2008) Pathology , vol.40 , pp. 553-557
    • Kim, S.Y.1    Oh, Y.L.2    Kim, K.M.3    Jeong, E.G.4    Kim, M.S.5    Yoo, N.J.6
  • 42
    • 33747592333 scopus 로고    scopus 로고
    • Decreased expression of tumor suppressor Bax-interacting factor-1 (Bif-1), a Bax activator, in gastric carcinomas
    • Lee JW, Jeong EG, Soung YH, Nam SW, Lee JY, Yoo NJ, et al. Decreased expression of tumor suppressor Bax-interacting factor-1 (Bif-1), a Bax activator, in gastric carcinomas. Pathology 2006; 38: 312-315.
    • (2006) Pathology , vol.38 , pp. 312-315
    • Lee, J.W.1    Jeong, E.G.2    Soung, Y.H.3    Nam, S.W.4    Lee, J.Y.5    Yoo, N.J.6
  • 43
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • Green DR, Evan GI. A matter of life and death. Cancer Cell 2002; 1: 19-30.
    • (2002) Cancer Cell , vol.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 44
    • 0034520466 scopus 로고    scopus 로고
    • Bcl-2 down-regulation causes autophagy in a caspase-independent manner in human leukemic HL60 cells
    • Saeki K, Yuo A, Okuma E, Yazaki Y, Susin SA, Kroemer G, et al. Bcl-2 down-regulation causes autophagy in a caspase-independent manner in human leukemic HL60 cells. Cell Death Differ 2000; 7: 1263-1269
    • (2000) Cell Death Differ , vol.7 , pp. 1263-1269
    • Saeki, K.1    Yuo, A.2    Okuma, E.3    Yazaki, Y.4    Susin, S.A.5    Kroemer, G.6
  • 45
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • Pattingre S, Tassa A, Qu X, Garuti R, Liang XH, Mizushima N, et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 2005; 122: 927-939
    • (2005) Cell , vol.122 , pp. 927-939
    • Pattingre, S.1    Tassa, A.2    Qu, X.3    Garuti, R.4    Liang, X.H.5    Mizushima, N.6
  • 46
    • 34248998801 scopus 로고    scopus 로고
    • Functional and physical interaction between Bcl-xL and a BH3-like domain in Beclin-1
    • Maiuri MC, Le Toumelin G, Criollo A, Rain JC, Gautier F, Juin P, et al. Functional and physical interaction between Bcl-xL and a BH3-like domain in Beclin-1. EMBO J 2007; 26: 2527-2539
    • (2007) EMBO J , vol.26 , pp. 2527-2539
    • Maiuri, M.C.1    Le Toumelin, G.2    Criollo, A.3    Rain, J.C.4    Gautier, F.5    Juin, P.6
  • 47
    • 34249037565 scopus 로고    scopus 로고
    • Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein
    • Oberstein A, Jeffrey PD, Shi Y. Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein. J Biol Chem 2007; 282: 13123-13132
    • (2007) J Biol Chem , vol.282 , pp. 13123-13132
    • Oberstein, A.1    Jeffrey, P.D.2    Shi, Y.3
  • 48
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy
    • Wei Y, Pattingre S, Sinha S, Bassik M, Levine B. JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Mol Cell 2008; 30: 678-688
    • (2008) Mol Cell , vol.30 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3    Bassik, M.4    Levine, B.5
  • 49
  • 50
    • 67650270918 scopus 로고    scopus 로고
    • Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-xL
    • Zalckvar E, Berissi H, Eisenstein M, Kimchi A. Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-xL. Autophagy 2009; 5: 720-722
    • (2009) Autophagy , vol.5 , pp. 720-722
    • Zalckvar, E.1    Berissi, H.2    Eisenstein, M.3    Kimchi, A.4
  • 51
    • 34250894388 scopus 로고    scopus 로고
    • BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-xL
    • Maiuri MC, Criollo A, Tasdemir E, Vicencio JM, Tajeddine N, Hickman JA, et al. BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-xL. Autophagy 2007; 3: 374-376
    • (2007) Autophagy , vol.3 , pp. 374-376
    • Maiuri, M.C.1    Criollo, A.2    Tasdemir, E.3    Vicencio, J.M.4    Tajeddine, N.5    Hickman, J.A.6
  • 52
    • 0035190026 scopus 로고    scopus 로고
    • Cellular function of phosphoinositide 3-kinases: Implications for development, homeostasis, and cancer
    • Katso R, Okkenhaug K, Ahmadi K, White S, Timms J, Waterfield MD. Cellular function of phosphoinositide 3-kinases: implications for development, homeostasis, and cancer. Annu Rev Cell Dev Biol 2001; 17: 615-675
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 615-675
    • Katso, R.1    Okkenhaug, K.2    Ahmadi, K.3    White, S.4    Timms, J.5    Waterfield, M.D.6
  • 53
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman JA, Luo J, Cantley LC. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat Rev Genet 2006; 7: 606-619
    • (2006) Nat Rev Genet , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 55
    • 0032514801 scopus 로고    scopus 로고
    • Regulation of the p85/p110? phosphatidylinositol 3′-kinase. Distinct roles for the N-terminal and C-terminal SH2 domains
    • Yu J, Wjasow C, Backer JM. Regulation of the p85/p110? phosphatidylinositol 3′-kinase. Distinct roles for the N-terminal and C-terminal SH2 domains. J Biol Chem 1998; 273: 30199-30203
    • (1998) J Biol Chem , vol.273 , pp. 30199-30203
    • Yu, J.1    Wjasow, C.2    Backer, J.M.3
  • 56
    • 0035929650 scopus 로고    scopus 로고
    • The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway
    • Arico S, Petiot A, Bauvy C, Dubbelhuis PF, Meijer AJ, Codogno P, et al. The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway. J Biol Chem 2001; 276: 35243-35246
    • (2001) J Biol Chem , vol.276 , pp. 35243-35246
    • Arico, S.1    Petiot, A.2    Bauvy, C.3    Dubbelhuis, P.F.4    Meijer, A.J.5    Codogno, P.6
  • 57
    • 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: 1098-1101
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 58
    • 0142227019 scopus 로고    scopus 로고
    • Targeting the PI3K-Akt pathway in human cancer: Rationale and promise
    • Luo J, Manning BD, Cantley LC. Targeting the PI3K-Akt pathway in human cancer: rationale and promise. Cancer Cell 2003; 4: 257-262
    • (2003) Cancer Cell , vol.4 , pp. 257-262
    • Luo, J.1    Manning, B.D.2    Cantley, L.C.3
  • 59
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley LC. The phosphoinositide 3-kinase pathway. Science 2002; 296: 1655-1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 60
    • 33745307617 scopus 로고    scopus 로고
    • Ras PI(3)K and mTOR signaling controls tumor cell growth
    • Shaw RJ, Cantley LC. Ras, PI(3)K and mTOR signaling controls tumor cell growth. Nature 2006; 441: 424-430
    • (2006) Nature , vol.441 , pp. 424-430
    • Shaw, R.J.1    Cantley, L.C.2
  • 61
    • 28844448182 scopus 로고    scopus 로고
    • Oncogenic PI3K deregulates transcription and translation
    • Bader AG, Kang S, Zhao L, Vogt PK. Oncogenic PI3K deregulates transcription and translation. Nat Rev Cancer 2005; 5: 921-929
    • (2005) Nat Rev Cancer , vol.5 , pp. 921-929
    • Bader, A.G.1    Kang, S.2    Zhao, L.3    Vogt, P.K.4
  • 62
    • 0035736487 scopus 로고    scopus 로고
    • HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation
    • Zhou BP, Liao Y, Xia W, Zou Y, Spohn B, Hung MC. HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation. Nat Cell Biol 2001; 3: 973-982
    • (2001) Nat Cell Biol , vol.3 , pp. 973-982
    • Zhou, B.P.1    Liao, Y.2    Xia, W.3    Zou, Y.4    Spohn, B.5    Hung, M.C.6
  • 63
    • 0038540963 scopus 로고    scopus 로고
    • United at last: The tuberous sclerosis complex gene products connect the phosphoinositide 3-kinase/Akt pathway to mammalian target of rapamycin (mTOR) signalling
    • Manning BD, Cantley LC. United at last: the tuberous sclerosis complex gene products connect the phosphoinositide 3-kinase/Akt pathway to mammalian target of rapamycin (mTOR) signalling. Biochem Soc Trans 2003; 31: 573-578
    • (2003) Biochem Soc Trans , vol.31 , pp. 573-578
    • Manning, B.D.1    Cantley, L.C.2
  • 64
    • 25444524850 scopus 로고    scopus 로고
    • Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
    • Hahn-Windgassen A, Nogueira V, Chen CC, Skeen JE, Sonenberg N, Hay N. Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity. J Biol Chem 2005; 280:32081-32089
    • (2005) J Biol Chem , vol.280 , pp. 32081-32089
    • Hahn-Windgassen, A.1    Nogueira, V.2    Chen, C.C.3    Skeen, J.E.4    Sonenberg, N.5    Hay, N.6
  • 65
    • 67749122122 scopus 로고    scopus 로고
    • Targeting PI3K signalling in cancer: Opportunities, challenges and limitations
    • Engelman JA. Targeting PI3K signalling in cancer: opportunities, challenges and limitations. Nat Rev Cancer 2009; 9: 550-562.
    • (2009) Nat Rev Cancer , vol.9 , pp. 550-562
    • Engelman, J.A.1
  • 66
    • 35348822482 scopus 로고    scopus 로고
    • Coactivation of receptor tyrosine kinases affects the response of tumor cells to targeted therapies
    • Stommel JM, Kimmelman AC, Ying H, Nabioullin R, Ponugoti AH, Wiedemeyer R, et al. Coactivation of receptor tyrosine kinases affects the response of tumor cells to targeted therapies. Science 2007; 318: 287-290
    • (2007) Science , vol.318 , pp. 287-290
    • Stommel, J.M.1    Kimmelman, A.C.2    Ying, H.3    Nabioullin, R.4    Ponugoti, A.H.5    Wiedemeyer, R.6
  • 67
    • 34249075147 scopus 로고    scopus 로고
    • MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling
    • Engelman JA, Zejnullahu K, Mitsudomi T, Song Y, Hyland C, Park JO, et al. MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling. Science 2007; 316: 1039-1043
    • (2007) Science , vol.316 , pp. 1039-1043
    • Engelman, J.A.1    Zejnullahu, K.2    Mitsudomi, T.3    Song, Y.4    Hyland, C.5    Park, J.O.6
  • 68
    • 46749156706 scopus 로고    scopus 로고
    • Acquired resistance to EGFR tyrosine kinase inhibitors in cancer cells is mediated by loss of IGF-binding proteins
    • Guix M, Faber AC, Wang SE, Olivares MG, Song Y, Qu S, et al. Acquired resistance to EGFR tyrosine kinase inhibitors in cancer cells is mediated by loss of IGF-binding proteins. J Clin Invest 2008; 118: 2609-2619
    • (2008) J Clin Invest , vol.118 , pp. 2609-2619
    • Guix, M.1    Faber, A.C.2    Wang, S.E.3    Olivares, M.G.4    Song, Y.5    Qu, S.6
  • 69
    • 13944284494 scopus 로고    scopus 로고
    • Oncogenic mutations of PIK3CA in human cancers
    • Samuels Y, Velculescu VE. Oncogenic mutations of PIK3CA in human cancers. Cell Cycle 2004; 3: 1221-1224.
    • (2004) Cell Cycle , vol.3 , pp. 1221-1224
    • Samuels, Y.1    Velculescu, V.E.2
  • 70
  • 72
    • 33646706052 scopus 로고    scopus 로고
    • Oncogenic PI3K and its role in cancer
    • Samuels Y, Ericson K. Oncogenic PI3K and its role in cancer. Curr Opin Oncol 2006; 18: 77-82.
    • (2006) Curr Opin Oncol , vol.18 , pp. 77-82
    • Samuels, Y.1    Ericson, K.2
  • 73
    • 0033056764 scopus 로고    scopus 로고
    • The molecular perspective: The ras oncogene
    • Goodsell DS. The molecular perspective: the ras oncogene. Oncologist 1999; 4: 263-264
    • (1999) Oncologist , vol.4 , pp. 263-264
    • Goodsell, D.S.1
  • 74
    • 0030936323 scopus 로고    scopus 로고
    • PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer
    • Li J, Yen C, Liaw D, Podsypanina K, Bose S, Wang SI, et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 1997; 275: 1943-1947.
    • (1997) Science , vol.275 , pp. 1943-1947
    • Li, J.1    Yen, C.2    Liaw, D.3    Podsypanina, K.4    Bose, S.5    Wang, S.I.6
  • 75
    • 2342545519 scopus 로고    scopus 로고
    • Target of rapamycin (TOR): An integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression
    • Fingar DC, Blenis J. Target of rapamycin (TOR): An integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression. Oncogene 2004; 23: 3151-3171
    • (2004) Oncogene , vol.23 , pp. 3151-3171
    • Fingar, D.C.1    Blenis, J.2
  • 76
    • 0036753494 scopus 로고    scopus 로고
    • Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control
    • Loewith R, Jacinto E, Wullschleger S, Lorberg A, Crespo JL, Bonenfant D, et al. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol Cell 2002; 10: 457-468
    • (2002) Mol Cell , vol.10 , pp. 457-468
    • Loewith, R.1    Jacinto, E.2    Wullschleger, S.3    Lorberg, A.4    Crespo, J.L.5    Bonenfant, D.6
  • 77
    • 0036342294 scopus 로고    scopus 로고
    • Identication of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase-akt pathway
    • Manning BD, Tee AR, Logsdon MN, Blenis J, Cantley LC. Identication of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase-akt pathway. Mol Cell 2002; 10: 151-162
    • (2002) Mol Cell , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3    Blenis, J.4    Cantley, L.C.5
  • 78
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signaling
    • Inoki K, Li Y, Zhu T, Wu J, Guan K L. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signaling. Nat Cell Biol 2002; 4: 648-657
    • (2002) Nat Cell Biol , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 79
    • 17444431201 scopus 로고    scopus 로고
    • Pandol PP Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis
    • Ma L, Chen Z, Erdjument-Bromage H, Tempst P, Pandol PP. Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis. Cell 2005; 121: 179-193
    • (2005) Cell , vol.121 , pp. 179-193
    • Ma, L.1    Chen, Z.2    Erdjument-Bromage, H.3    Tempst, P.4
  • 80
    • 4544384577 scopus 로고    scopus 로고
    • Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase
    • Roux PP, Ballif BA, Anjum R, Gygi SP, Blenis J. Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase. Proc Natl Acad Sci USA 2004; 101: 13489-13494
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13489-13494
    • Roux, P.P.1    Ballif, B.A.2    Anjum, R.3    Gygi, S.P.4    Blenis, J.5
  • 81
    • 58649084625 scopus 로고    scopus 로고
    • Peptide combinatorial libraries identify TSC2 as a death-associated protein kinase (DAPK) death domain-binding protein and reveal a stimulatory role for DAPK in mTORC1 signaling
    • Stevens C, Lin Y, Harrison B, Burch L, Ridgway RA, Sansom O, et al. Peptide combinatorial libraries identify TSC2 as a death-associated protein kinase (DAPK) death domain-binding protein and reveal a stimulatory role for DAPK in mTORC1 signaling. J Biol Chem 2009; 284: 334-344
    • (2009) J Biol Chem , vol.284 , pp. 334-344
    • Stevens, C.1    Lin, Y.2    Harrison, B.3    Burch, L.4    Ridgway, R.A.5    Sansom, O.6
  • 82
    • 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: 1533-1538
    • (2004) Genes Dev , vol.18 , pp. 1533-1538
    • Corradetti, M.N.1    Inoki, K.2    Bardeesy, N.3    Depinho, R.A.4    Guan, K.L.5
  • 85
    • 48449101433 scopus 로고    scopus 로고
    • P53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling
    • Budanov AV, Karin M. p53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling. Cell 2008; 134: 451-460
    • (2008) Cell , vol.134 , pp. 451-460
    • Budanov, A.V.1    Karin, M.2
  • 86
    • 0032127805 scopus 로고    scopus 로고
    • Human ULK1, a novel serine/threonine kinase related to UNC-51 kinase of Caenorhabditis elegans: CDNA cloning, expression, and chromosomal assignment
    • Kuroyanagi H, Yan J, Seki N, Yamanouchi Y, Suzuki Y, Takano T, et al. Human ULK1, a novel serine/threonine kinase related to UNC-51 kinase of Caenorhabditis elegans: cDNA cloning, expression, and chromosomal assignment. Genomics 1998; 51: 76-85.
    • (1998) Genomics , vol.51 , pp. 76-85
    • Kuroyanagi, H.1    Yan, J.2    Seki, N.3    Yamanouchi, Y.4    Suzuki, Y.5    Takano, T.6
  • 87
    • 0033592671 scopus 로고    scopus 로고
    • Mouse ULK2, a novel member of the UNC-51-like protein kinases: Unique features of functional domains
    • Yan J, Kuroyanagi H, Tomemori T, Okazaki N, Asato K, Matsuda Y, et al. Mouse ULK2, a novel member of the UNC-51-like protein kinases: unique features of functional domains. Oncogene 1999; 18: 5850-5859
    • (1999) Oncogene , vol.18 , pp. 5850-5859
    • Yan, J.1    Kuroyanagi, H.2    Tomemori, T.3    Okazaki, N.4    Asato, K.5    Matsuda, Y.6
  • 88
    • 34548482499 scopus 로고    scopus 로고
    • SiRNA screening of the kinome identi?es ULK1 as a multidomain modulator of autophagy
    • Chan EY, Kir S, Tooze S.A. siRNA screening of the kinome identi?es ULK1 as a multidomain modulator of autophagy. J Biol Chem 2007; 282: 25464-25474
    • (2007) J Biol Chem , vol.282 , pp. 25464-25474
    • Chan, E.Y.1    Kir, S.2    Tooze, S.A.3
  • 89
    • 43149090064 scopus 로고    scopus 로고
    • FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells
    • Hara T, Takamura A, Kishi C, Iemura S, Natsume T, Guan JL, et al. FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells. J Cell Biol 2008; 181: 497-510.
    • (2008) J Cell Biol , vol.181 , pp. 497-510
    • Hara, T.1    Takamura, A.2    Kishi, C.3    Iemura, S.4    Natsume, T.5    Guan, J.L.6
  • 90
    • 58149473473 scopus 로고    scopus 로고
    • Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism
    • Chan EY, Longatti A, McKnight NC, Tooze S.A. Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism. Mol Cell Biol 2009; 29: 157-171
    • (2009) Mol Cell Biol , vol.29 , pp. 157-171
    • Chan, E.Y.1    Longatti, A.2    McKnight, N.C.3    Tooze, S.A.4
  • 91
    • 65249119430 scopus 로고    scopus 로고
    • Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy
    • Hosokawa N, Hara T, Kaizuka T, Kishi C, Takamura A, Miura Y, et al. Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy. Mol Biol Cell 2009; 20: 1981-1991
    • (2009) Mol Biol Cell , vol.20 , pp. 1981-1991
    • Hosokawa, N.1    Hara, T.2    Kaizuka, T.3    Kishi, C.4    Takamura, A.5    Miura, Y.6
  • 92
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • Jung CH, Jun CB, Ro SH, Kim YM, Otto NM, Cao J, et al. ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol Biol Cell 2009; 20: 1992-2003.
    • (2009) Mol Biol Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3    Kim, Y.M.4    Otto, N.M.5    Cao, J.6
  • 93
    • 66449083078 scopus 로고    scopus 로고
    • ULK1.ATG13. FIP200 complex mediates mTOR signaling and is essential for autophagy
    • Ganley IG, Lam du H, Wang J, Ding X, Chen S, Lang X. ULK1.ATG13. FIP200 complex mediates mTOR signaling and is essential for autophagy. J Biol Chem 2009; 284: 12297-12305
    • (2009) J Biol Chem , vol.284 , pp. 12297-12305
    • Ganley, I.G.1    Lam Du, H.2    Wang, J.3    Ding, X.4    Chen, S.5    Lang, X.6
  • 94
    • 33846514235 scopus 로고    scopus 로고
    • Hierarchy of Atg proteins in pre-autophagosomal structure organization
    • Suzuki K, Kubota Y, Sekito T, Ohsumi Y. Hierarchy of Atg proteins in pre-autophagosomal structure organization. Genes Cells 2007; 12: 209-218
    • (2007) Genes Cells , vol.12 , pp. 209-218
    • Suzuki, K.1    Kubota, Y.2    Sekito, T.3    Ohsumi, Y.4
  • 95
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras AC, Raught B, Sonenberg N. Regulation of translation initiation by FRAP/mTOR. Genes Dev 2001; 15: 807-826
    • (2001) Genes Dev , vol.15 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 96
    • 65549132539 scopus 로고    scopus 로고
    • Silencing of elongation factor-2 kinase potentiates the effect of 2-deoxy-D-glucose against human glioma cells through blunting of autophagy
    • Wu H, Zhu H, Liu DX, Niu TK, Ren X, Patel R, et al. Silencing of elongation factor-2 kinase potentiates the effect of 2-deoxy-D-glucose against human glioma cells through blunting of autophagy. Cancer Res 2009; 69: 2453-2460.
    • (2009) Cancer Res , vol.69 , pp. 2453-2460
    • Wu, H.1    Zhu, H.2    Liu, D.X.3    Niu, T.K.4    Ren, X.5    Patel, R.6
  • 97
    • 0035859956 scopus 로고    scopus 로고
    • P70S6 kinase signals cell survival as well as growth, inactivating the proapoptotic molecule BAD
    • Harada H, Andersen JS, Mann M, Terada N, Korsmeyer SJ. p70S6 kinase signals cell survival as well as growth, inactivating the proapoptotic molecule BAD. Proc Natl Acad Sci USA 2001; 98: 9666-9670
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9666-9670
    • Harada, H.1    Andersen, J.S.2    Mann, M.3    Terada, N.4    Korsmeyer, S.J.5
  • 98
    • 33745885329 scopus 로고    scopus 로고
    • DRAM, a p53-induced modulator of autophagy, is critical for apoptosis
    • Crighton D, Wilkinson S, OPrey J, Syed N, Smith P, Harrison PR, et al. DRAM, a p53-induced modulator of autophagy, is critical for apoptosis. Cell 2006; 126: 121-134
    • (2006) Cell , vol.126 , pp. 121-134
    • Crighton, D.1    Wilkinson, S.2    Oprey, J.3    Syed, N.4    Smith, P.5    Harrison, P.R.6
  • 101
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • Kroemer G, Jaattela M. Lysosomes and autophagy in cell death control. Nat Rev Cancer 2005; 5: 886-897
    • (2005) Nat Rev Cancer , vol.5 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 102
    • 2442482810 scopus 로고    scopus 로고
    • Autophagy as a cell death and tumor suppressor mechanism
    • Gozuacik D, Kimchi A. Autophagy as a cell death and tumor suppressor mechanism. Oncogene 2004; 23: 2891-2906
    • (2004) Oncogene , vol.23 , pp. 2891-2906
    • Gozuacik, D.1    Kimchi, A.2
  • 103
    • 25444440875 scopus 로고    scopus 로고
    • The role of autophagy in cancer development and response to therapy
    • Kondo Y, Kanzawa T, Sawaya R, Kondo S. The role of autophagy in cancer development and response to therapy. Nat Rev Cancer 2005; 5: 726734.
    • (2005) Nat Rev Cancer , vol.5 , pp. 726-734
    • Kondo, Y.1    Kanzawa, T.2    Sawaya, R.3    Kondo, S.4
  • 104
    • 77953721135 scopus 로고    scopus 로고
    • Autophagy and autophagic cell death
    • Gewirtz DA, Holt SE, and Grant S (Eds) NJ: Humana Press
    • Djavaheri-Mergny M, Botti J, Codogno P. Autophagy and autophagic cell death. In: Gewirtz DA, Holt SE, and Grant S (Eds). Apoptosis, Senescence, and Cancer. NJ: Humana Press; 2007. p 93-107.
    • (2007) Apoptosis, Senescence, and Cancer , pp. 93-107
    • Djavaheri-Mergny, M.1    Botti, J.2    Codogno, P.3
  • 105
    • 33947417275 scopus 로고    scopus 로고
    • Crosstalk between Bak/Bax and mTOR signaling regulates radiation-induced autophagy
    • Moretti L, Attia A, Kim KW, Lu B. Crosstalk between Bak/Bax and mTOR signaling regulates radiation-induced autophagy. Autophagy 2007; 3: 142-144.
    • (2007) Autophagy , vol.3 , pp. 142-144
    • Moretti, L.1    Attia, A.2    Kim, K.W.3    Lu, B.4
  • 107
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 30-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P. Distinct classes of phosphatidylinositol 30-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem 2000; 275: 992-998
    • (2000) J Biol Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 108
    • 17144427728 scopus 로고    scopus 로고
    • Synergistic augmentation of rapamycin-induced autophagy in malignant glioma cells by phosphatidylinositol 3-kinase/protein kinase B inhibitors
    • Takeuchi H, KondoY, Fujiwara K, Kanzawa T, Aoki H, Mills GB, et al. Synergistic augmentation of rapamycin-induced autophagy in malignant glioma cells by phosphatidylinositol 3-kinase/protein kinase B inhibitors. Cancer Res 2005; 65: 3336-3346
    • (2005) Cancer Res , vol.65 , pp. 3336-3346
    • Takeuchi, H.1    Kondoy Fujiwara, K.2    Kanzawa, T.3    Aoki, H.4    Mills, G.B.5
  • 110
    • 77953699668 scopus 로고    scopus 로고
    • Targeting the prodeath and prosurvival functions of autophagy as novel therapeutic strategies in cancer
    • Dalby KN, Tekedereli I, Lopez-Berestein G, Ozpolat B. Targeting the prodeath and prosurvival functions of autophagy as novel therapeutic strategies in cancer. Autophagy 2010; 6: 322-329.
    • (2010) Autophagy , vol.6 , pp. 322-329
    • Dalby, K.N.1    Tekedereli, I.2    Lopez-Berestein, G.3    Ozpolat, B.4
  • 111
    • 60349085032 scopus 로고    scopus 로고
    • Autophagy inhibits reactive oxygen species-mediated apoptosis via activating p38-nuclear factor-kappa B survival pathways in oridonin-treated murine fibrosarcoma L929 cells
    • Cheng Y, Qiu F, Ye YC, Guo ZM, Tashiro S, Onodera S, et al. Autophagy inhibits reactive oxygen species-mediated apoptosis via activating p38-nuclear factor-kappa B survival pathways in oridonin-treated murine fibrosarcoma L929 cells, FEBS J 2009; 276: 1291-1306.
    • (2009) FEBS J , vol.276 , pp. 1291-1306
    • Cheng, Y.1    Qiu, F.2    Ye, Y.C.3    Guo, Z.M.4    Tashiro, S.5    Onodera, S.6
  • 112
    • 77956362469 scopus 로고    scopus 로고
    • Cytoprotective Effect of the Elongation Factor-2 Kinase-Mediated Autophagy in Breast Cancer Cells Subjected to Growth Factor Inhibition
    • Cheng Y, Li H, Ren X, Niu T, Hait WN, Yang J. Cytoprotective Effect of the Elongation Factor-2 Kinase-Mediated Autophagy in Breast Cancer Cells Subjected to Growth Factor Inhibition. PLoS One 2010; 5: e9715.
    • (2010) PLoS One , vol.5
    • Cheng, Y.1    Li, H.2    Ren, X.3    Niu, T.4    Hait, W.N.5    Yang, J.6
  • 114
    • 33847258674 scopus 로고    scopus 로고
    • Discovery and development of SAHA as an anticancer agent
    • Marks PA. Discovery and development of SAHA as an anticancer agent. Oncogene 2007; 26: 1351-1356
    • (2007) Oncogene , vol.26 , pp. 1351-1356
    • Marks, P.A.1
  • 115
    • 48249090836 scopus 로고    scopus 로고
    • Therapeutic activity of mTOR-inhibitors in mantle cell lymphoma: Clues but no clear answers
    • Younes A. Therapeutic activity of mTOR-inhibitors in mantle cell lymphoma: clues but no clear answers. Autophagy 2008; 4: 707-709
    • (2008) Autophagy , vol.4 , pp. 707-709
    • Younes, A.1
  • 116
    • 48249090416 scopus 로고    scopus 로고
    • Autophagy upregulation by inhibitors of caspase-3 and mTOR enhances radiotherapy in a mouse model of lung cancer
    • Kim KW, Hwang M, Moretti L, Jaboin JJ, Cha YI, Lu B. Autophagy upregulation by inhibitors of caspase-3 and mTOR enhances radiotherapy in a mouse model of lung cancer. Autophagy 2008; 4: 659-668.
    • (2008) Autophagy , vol.4 , pp. 659-668
    • Kim, K.W.1    Hwang, M.2    Moretti, L.3    Jaboin, J.J.4    Cha, Y.I.5    Lu, B.6
  • 118
    • 13944256602 scopus 로고    scopus 로고
    • Arsenic trioxide induces autophagic cell death in malignant glioma cells by upregulation of mitochondrial cell death protein BNIP3
    • Kanzawa T, Zhang L, Xiao L, Germano IM, Kondo Y, Kondo S. Arsenic trioxide induces autophagic cell death in malignant glioma cells by upregulation of mitochondrial cell death protein BNIP3. Oncogene 2005; 24: 980-991
    • (2005) Oncogene , vol.24 , pp. 980-991
    • Kanzawa, T.1    Zhang, L.2    Xiao, L.3    Germano, I.M.4    Kondo, Y.5    Kondo, S.6
  • 119
    • 58749105634 scopus 로고    scopus 로고
    • Polygonatum cyrtonema lectin induces apoptosis and autophagy in human melanoma A375 cells through a mitochondria-mediated ROS-p38-p53 pathway
    • Liu B, Cheng Y, Zhang B, Bian HJ, Bao JK. Polygonatum cyrtonema lectin induces apoptosis and autophagy in human melanoma A375 cells through a mitochondria-mediated ROS-p38-p53 pathway. Cancer Lett 2009; 275: 54-60.
    • (2009) Cancer Lett , vol.275 , pp. 54-60
    • Liu, B.1    Cheng, Y.2    Zhang, B.3    Bian, H.J.4    Bao, J.K.5
  • 120
    • 61649114199 scopus 로고    scopus 로고
    • Molecular mechanisms of Polygonatum cyrtonema Lectin-induced apoptosis and autophagy in cancer cells
    • Liu B, Cheng Y, Bian HJ, Bao JK. Molecular mechanisms of Polygonatum cyrtonema Lectin-induced apoptosis and autophagy in cancer cells. Autophagy 2009; 5: 253-255
    • (2009) Autophagy , vol.5 , pp. 253-255
    • Liu, B.1    Cheng, Y.2    Bian, H.J.3    Bao, J.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.