메뉴 건너뛰기




Volumn 39, Issue 2, 2016, Pages 98-106

Metabolic, autophagic, and mitophagic activities in cancer initiation and progression

Author keywords

Autophagy; Cancer; Mitochondria; Mitophagy; Oxidative stress; Reactive species

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR; ADAPTOR PROTEIN; AUTOPHAGY PROTEIN 5; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; KELCH LIKE ECH ASSOCIATED PROTEIN 1; MAMMALIAN TARGET OF RAPAMYCIN; PARKIN; PROTEIN BNIP3; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR NRF2;

EID: 84978286860     PISSN: 23194170     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bj.2015.10.002     Document Type: Review
Times cited : (24)

References (168)
  • 1
    • 0025883342 scopus 로고
    • Nitric oxide: physiology, pathophysiology, and pharmacology
    • [1] Moncada, S., Palmer, R.M., Higgs, E.A., Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol Rev 43 (1991), 109–142.
    • (1991) Pharmacol Rev , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 2
    • 0028349156 scopus 로고
    • Nitric oxide synthases in mammals
    • [2] Knowles, R.G., Moncada, S., Nitric oxide synthases in mammals. Biochem J 298 (1994), 249–258.
    • (1994) Biochem J , vol.298 , pp. 249-258
    • Knowles, R.G.1    Moncada, S.2
  • 3
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • [3] Pacher, P., Beckman, J.S., Liaudet, L., Nitric oxide and peroxynitrite in health and disease. Physiol Rev 87 (2007), 315–424.
    • (2007) Physiol Rev , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 4
    • 77953752629 scopus 로고    scopus 로고
    • What part of NO don't you understand? Some answers to the cardinal questions in nitric oxide biology
    • [4] Hill, B.G., Dranka, B.P., Bailey, S.M., Lancaster, J.R. Jr., Darley-Usmar, V.M., What part of NO don't you understand? Some answers to the cardinal questions in nitric oxide biology. J Biol Chem 285 (2010), 19699–19704.
    • (2010) J Biol Chem , vol.285 , pp. 19699-19704
    • Hill, B.G.1    Dranka, B.P.2    Bailey, S.M.3    Lancaster, J.R.4    Darley-Usmar, V.M.5
  • 6
    • 84878776025 scopus 로고    scopus 로고
    • Teaching the basics of redox biology to medical and graduate students: oxidants, antioxidants and disease mechanisms
    • [6] Kalyanaraman, B., Teaching the basics of redox biology to medical and graduate students: oxidants, antioxidants and disease mechanisms. Redox Biol 8:1 (2013), 244–257.
    • (2013) Redox Biol , vol.8 , Issue.1 , pp. 244-257
    • Kalyanaraman, B.1
  • 7
    • 84897019491 scopus 로고    scopus 로고
    • Nox enzymes and new thinking on reactive oxygen: a double-edged sword revisited
    • [7] Lambeth, J.D., Neish, A.S., Nox enzymes and new thinking on reactive oxygen: a double-edged sword revisited. Annu Rev Pathol 9 (2014), 119–145.
    • (2014) Annu Rev Pathol , vol.9 , pp. 119-145
    • Lambeth, J.D.1    Neish, A.S.2
  • 9
    • 0034873185 scopus 로고    scopus 로고
    • Reactive oxygen species as intracellular messengers during cell growth and differentiation
    • [9] Sauer, H., Wartenberg, M., Hescheler, J., Reactive oxygen species as intracellular messengers during cell growth and differentiation. Cell Physiol Biochem 11 (2001), 173–186.
    • (2001) Cell Physiol Biochem , vol.11 , pp. 173-186
    • Sauer, H.1    Wartenberg, M.2    Hescheler, J.3
  • 10
    • 0346731072 scopus 로고    scopus 로고
    • Nitric oxide and cell signaling: modulation of redox tone and protein modification
    • [10] Landar, A., Darley-Usmar, V.M., Nitric oxide and cell signaling: modulation of redox tone and protein modification. Amino Acids 2 (2003), 313–321.
    • (2003) Amino Acids , vol.2 , pp. 313-321
    • Landar, A.1    Darley-Usmar, V.M.2
  • 12
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • [12] Circu, M.L., Aw, T.Y., Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic Biol Med 48 (2010), 749–762.
    • (2010) Free Radic Biol Med , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 13
    • 84857833776 scopus 로고    scopus 로고
    • Cell signalling by reactive lipid species: new concepts and molecular mechanisms
    • [13] Higdon, A., Diers, A.R., Oh, J.Y., Landar, A., Darley-Usmar, V.M., Cell signalling by reactive lipid species: new concepts and molecular mechanisms. Biochem J 442 (2012), 453–464.
    • (2012) Biochem J , vol.442 , pp. 453-464
    • Higdon, A.1    Diers, A.R.2    Oh, J.Y.3    Landar, A.4    Darley-Usmar, V.M.5
  • 15
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • [15] Finkel, T., Holbrook, N.J., Oxidants, oxidative stress and the biology of ageing. Nature 408 (2000), 239–247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 17
    • 84908153270 scopus 로고    scopus 로고
    • Targeting antioxidants for cancer therapy
    • [17] Glasauer, A., Chandel, N.S., Targeting antioxidants for cancer therapy. Biochem Pharmacol 92 (2014), 90–101.
    • (2014) Biochem Pharmacol , vol.92 , pp. 90-101
    • Glasauer, A.1    Chandel, N.S.2
  • 18
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: a history of macroautophagy
    • [18] Yang, Z., Klionsky, D.J., Eaten alive: a history of macroautophagy. Nat Cell Biol 12 (2010), 814–822.
    • (2010) Nat Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 19
    • 79251577061 scopus 로고    scopus 로고
    • The regulation of autophagy – unanswered questions
    • [19] Chen, Y., Klionsky, D.J., The regulation of autophagy – unanswered questions. J Cell Sci 124 (2011), 161–170.
    • (2011) J Cell Sci , vol.124 , pp. 161-170
    • Chen, Y.1    Klionsky, D.J.2
  • 20
    • 79952319773 scopus 로고    scopus 로고
    • Mitochondria removal by autophagy
    • [20] Wang, K., Klionsky, D.J., Mitochondria removal by autophagy. Autophagy 7 (2011), 297–300.
    • (2011) Autophagy , vol.7 , pp. 297-300
    • Wang, K.1    Klionsky, D.J.2
  • 21
    • 84891747382 scopus 로고    scopus 로고
    • The machinery of macroautophagy
    • [21] Feng, Y., He, D., Yao, Z., Klionsky, D.J., The machinery of macroautophagy. Cell Res 24 (2014), 24–41.
    • (2014) Cell Res , vol.24 , pp. 24-41
    • Feng, Y.1    He, D.2    Yao, Z.3    Klionsky, D.J.4
  • 22
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • [22] Rubinsztein, D.C., Codogno, P., Levine, B., Autophagy modulation as a potential therapeutic target for diverse diseases. Nat Rev Drug Discov 11 (2012), 709–730.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3
  • 23
    • 84861526009 scopus 로고    scopus 로고
    • Deconvoluting the context-dependent role for autophagy in cancer
    • [23] White, E., Deconvoluting the context-dependent role for autophagy in cancer. Nat Rev Cancer 12 (2012), 401–410.
    • (2012) Nat Rev Cancer , vol.12 , pp. 401-410
    • White, E.1
  • 24
    • 84555195856 scopus 로고    scopus 로고
    • Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling
    • [24] Lee, J., Giordano, S., Zhang, J., Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling. Biochem J 441 (2012), 523–540.
    • (2012) Biochem J , vol.441 , pp. 523-540
    • Lee, J.1    Giordano, S.2    Zhang, J.3
  • 25
    • 84869388804 scopus 로고    scopus 로고
    • Integration of cellular bioenergetics with mitochondrial quality control and autophagy
    • [25] Hill, B.G., Benavides, G.A., Lancaster, J.R. Jr., Ballinger, S., Dell'Italia, L., Jianhua, Z., et al. Integration of cellular bioenergetics with mitochondrial quality control and autophagy. Biol Chem 393 (2012), 1485–1512.
    • (2012) Biol Chem , vol.393 , pp. 1485-1512
    • Hill, B.G.1    Benavides, G.A.2    Lancaster, J.R.3    Ballinger, S.4    Dell'Italia, L.5    Jianhua, Z.6
  • 26
    • 84877628647 scopus 로고    scopus 로고
    • Autophagy in human health and disease
    • [26] Choi, A.M., Ryter, S.W., Levine, B., Autophagy in human health and disease. N Engl J Med 368 (2013), 1845–1846.
    • (2013) N Engl J Med , vol.368 , pp. 1845-1846
    • Choi, A.M.1    Ryter, S.W.2    Levine, B.3
  • 27
    • 84875892111 scopus 로고    scopus 로고
    • Autophagy as a stress-response and quality-control mechanism: implications for cell injury and human disease
    • [27] Murrow, L., Debnath, J., Autophagy as a stress-response and quality-control mechanism: implications for cell injury and human disease. Annu Rev Pathol 8 (2013), 105–137.
    • (2013) Annu Rev Pathol , vol.8 , pp. 105-137
    • Murrow, L.1    Debnath, J.2
  • 28
    • 84892163616 scopus 로고    scopus 로고
    • Autophagy as an essential cellular antioxidant pathway in neurodegenerative disease
    • [28] Giordano, S., Darley-Usmar, V., Zhang, J., Autophagy as an essential cellular antioxidant pathway in neurodegenerative disease. Redox Biol 2 (2013), 82–90.
    • (2013) Redox Biol , vol.2 , pp. 82-90
    • Giordano, S.1    Darley-Usmar, V.2    Zhang, J.3
  • 29
    • 84879475204 scopus 로고    scopus 로고
    • Autophagy and mitophagy in cellular damage control
    • [29] Zhang, J., Autophagy and mitophagy in cellular damage control. Redox Biol 1 (2013), 19–23.
    • (2013) Redox Biol , vol.1 , pp. 19-23
    • Zhang, J.1
  • 30
    • 84879047011 scopus 로고    scopus 로고
    • Cellular metabolic and autophagic pathways: traffic control by redox signaling
    • [30] Dodson, M., Darley-Usmar, V., Zhang, J., Cellular metabolic and autophagic pathways: traffic control by redox signaling. Free Radic Biol Med 63 (2013), 207–221.
    • (2013) Free Radic Biol Med , vol.63 , pp. 207-221
    • Dodson, M.1    Darley-Usmar, V.2    Zhang, J.3
  • 31
    • 84898785937 scopus 로고    scopus 로고
    • Redox regulation of antioxidants, autophagy, and the response to stress: implications for electrophile therapeutics
    • [31] Levonen, A.L., Hill, B.G., Kansanen, E., Zhang, J., Darley-Usmar, V.M., Redox regulation of antioxidants, autophagy, and the response to stress: implications for electrophile therapeutics. Free Radic Biol Med 71 (2014), 196–207.
    • (2014) Free Radic Biol Med , vol.71 , pp. 196-207
    • Levonen, A.L.1    Hill, B.G.2    Kansanen, E.3    Zhang, J.4    Darley-Usmar, V.M.5
  • 34
    • 0027247805 scopus 로고
    • Oxidants in cigarette smoke. Radicals, hydrogen peroxide, peroxynitrate, and peroxynitrite
    • [34] Pryor, W.A., Stone, K., Oxidants in cigarette smoke. Radicals, hydrogen peroxide, peroxynitrate, and peroxynitrite. Ann N Y Acad Sci 686 (1993), 12–27.
    • (1993) Ann N Y Acad Sci , vol.686 , pp. 12-27
    • Pryor, W.A.1    Stone, K.2
  • 35
    • 0027940508 scopus 로고
    • Molecular mechanisms of damage by excess nitrogen oxides: nitration of tyrosine by gas-phase cigarette smoke
    • [35] Eiserich, J.P., Vossen, V., O'Neill, C.A., Halliwell, B., Cross, C.E., van der Vliet, A., Molecular mechanisms of damage by excess nitrogen oxides: nitration of tyrosine by gas-phase cigarette smoke. FEBS Lett 353 (1994), 53–56.
    • (1994) FEBS Lett , vol.353 , pp. 53-56
    • Eiserich, J.P.1    Vossen, V.2    O'Neill, C.A.3    Halliwell, B.4    Cross, C.E.5    van der Vliet, A.6
  • 36
    • 0029886786 scopus 로고    scopus 로고
    • Cancer risk and oxidative DNA damage in man
    • [36] Loft, S., Poulsen, H.E., Cancer risk and oxidative DNA damage in man. J Mol Med Berl 74 (1996), 297–312.
    • (1996) J Mol Med Berl , vol.74 , pp. 297-312
    • Loft, S.1    Poulsen, H.E.2
  • 37
    • 8444234762 scopus 로고    scopus 로고
    • Tobacco smoking and cancer: a brief review of recent epidemiological evidence
    • [37] Sasco, A.J., Secretan, M.B., Straif, K., Tobacco smoking and cancer: a brief review of recent epidemiological evidence. Lung Cancer 45 (2004), S3–S9.
    • (2004) Lung Cancer , vol.45 , pp. S3-S9
    • Sasco, A.J.1    Secretan, M.B.2    Straif, K.3
  • 38
    • 0030980641 scopus 로고    scopus 로고
    • Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts
    • [38] Irani, K., Xia, Y., Zweier, J.L., Sollott, S.J., Der, C.J., Fearon, E.R., et al. Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts. Science 275 (1997), 1649–1652.
    • (1997) Science , vol.275 , pp. 1649-1652
    • Irani, K.1    Xia, Y.2    Zweier, J.L.3    Sollott, S.J.4    Der, C.J.5    Fearon, E.R.6
  • 39
  • 40
    • 0036285034 scopus 로고    scopus 로고
    • c-Myc can induce DNA damage, increase reactive oxygen species, and mitigate p53 function: a mechanism for oncogene-induced genetic instability
    • [40] Vafa, O., Wade, M., Kern, S., Beeche, M., Pandita, T.K., Hampton, G.M., et al. c-Myc can induce DNA damage, increase reactive oxygen species, and mitigate p53 function: a mechanism for oncogene-induced genetic instability. Mol Cell 9 (2002), 1031–1044.
    • (2002) Mol Cell , vol.9 , pp. 1031-1044
    • Vafa, O.1    Wade, M.2    Kern, S.3    Beeche, M.4    Pandita, T.K.5    Hampton, G.M.6
  • 41
    • 77952737658 scopus 로고    scopus 로고
    • Mitochondrial metabolism and ROS generation are essential for Kras-mediated tumorigenicity
    • [41] Weinberg, F., Hamanaka, R., Wheaton, W.W., Weinberg, S., Joseph, J., Lopez, M., et al. Mitochondrial metabolism and ROS generation are essential for Kras-mediated tumorigenicity. Proc Natl Acad Sci USA 107 (2010), 8788–8793.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 8788-8793
    • Weinberg, F.1    Hamanaka, R.2    Wheaton, W.W.3    Weinberg, S.4    Joseph, J.5    Lopez, M.6
  • 42
    • 79959969874 scopus 로고    scopus 로고
    • Glioma stem cell proliferation and tumor growth are promoted by nitric oxide synthase-2
    • [42] Eyler, C.E., Wu, Q., Yan, K., MacSwords, J.M., Chandler-Militello, D., Misuraca, K.L., et al. Glioma stem cell proliferation and tumor growth are promoted by nitric oxide synthase-2. Cell 146 (2011), 53–66.
    • (2011) Cell , vol.146 , pp. 53-66
    • Eyler, C.E.1    Wu, Q.2    Yan, K.3    MacSwords, J.M.4    Chandler-Militello, D.5    Misuraca, K.L.6
  • 43
    • 75349091751 scopus 로고    scopus 로고
    • Perivascular nitric oxide activates notch signaling and promotes stem-like character in PDGF-induced glioma cells
    • [43] Charles, N., Ozawa, T., Squatrito, M., Bleau, A.M., Brennan, C.W., Hambardzumyan, D., et al. Perivascular nitric oxide activates notch signaling and promotes stem-like character in PDGF-induced glioma cells. Cell Stem Cell 6 (2010), 141–152.
    • (2010) Cell Stem Cell , vol.6 , pp. 141-152
    • Charles, N.1    Ozawa, T.2    Squatrito, M.3    Bleau, A.M.4    Brennan, C.W.5    Hambardzumyan, D.6
  • 45
    • 78049426509 scopus 로고    scopus 로고
    • Increased NOS2 predicts poor survival in estrogen receptor-negative breast cancer patients
    • [45] Glynn, S.A., Boersma, B.J., Dorsey, T.H., Yi, M., Yfantis, H.G., Ridnour, L.A., et al. Increased NOS2 predicts poor survival in estrogen receptor-negative breast cancer patients. J Clin Invest 120 (2010), 3843–3854.
    • (2010) J Clin Invest , vol.120 , pp. 3843-3854
    • Glynn, S.A.1    Boersma, B.J.2    Dorsey, T.H.3    Yi, M.4    Yfantis, H.G.5    Ridnour, L.A.6
  • 46
    • 84937523330 scopus 로고    scopus 로고
    • High nitric oxide production, secondary to inducible nitric oxide synthase expression, is essential for regulation of the tumour-initiating properties of colon cancer stem cells
    • [46] Puglisi, M.A., Cenciarelli, C., Tesori, V., Cappellari, M., Martini, M., Di Francesco, A.M., et al. High nitric oxide production, secondary to inducible nitric oxide synthase expression, is essential for regulation of the tumour-initiating properties of colon cancer stem cells. J Pathol 236 (2015), 479–490.
    • (2015) J Pathol , vol.236 , pp. 479-490
    • Puglisi, M.A.1    Cenciarelli, C.2    Tesori, V.3    Cappellari, M.4    Martini, M.5    Di Francesco, A.M.6
  • 48
    • 84861973567 scopus 로고    scopus 로고
    • Tumor suppression in the absence of p53-mediated cell-cycle arrest, apoptosis, and senescence
    • [48] Li, T., Kon, N., Jiang, L., Tan, M., Ludwig, T., Zhao, Y., et al. Tumor suppression in the absence of p53-mediated cell-cycle arrest, apoptosis, and senescence. Cell 149 (2012), 1269–1283.
    • (2012) Cell , vol.149 , pp. 1269-1283
    • Li, T.1    Kon, N.2    Jiang, L.3    Tan, M.4    Ludwig, T.5    Zhao, Y.6
  • 49
    • 0035853157 scopus 로고    scopus 로고
    • Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice
    • [49] Ramos-Gomez, M., Kwak, M.K., Dolan, P.M., Itoh, K., Yamamoto, M., Talalay, P., et al. Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice. Proc Natl Acad Sci USA 98 (2001), 3410–3415.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3410-3415
    • Ramos-Gomez, M.1    Kwak, M.K.2    Dolan, P.M.3    Itoh, K.4    Yamamoto, M.5    Talalay, P.6
  • 50
    • 4644328941 scopus 로고    scopus 로고
    • Nrf2 is essential for the chemopreventive efficacy of oltipraz against urinary bladder carcinogenesis
    • [50] Iida, K., Itoh, K., Kumagai, Y., Oyasu, R., Hattori, K., Kawai, K., et al. Nrf2 is essential for the chemopreventive efficacy of oltipraz against urinary bladder carcinogenesis. Cancer Res 64 (2004), 6424–6431.
    • (2004) Cancer Res , vol.64 , pp. 6424-6431
    • Iida, K.1    Itoh, K.2    Kumagai, Y.3    Oyasu, R.4    Hattori, K.5    Kawai, K.6
  • 51
    • 33748089664 scopus 로고    scopus 로고
    • Inhibition of 7,12-dimethylbenz(a)anthracene-induced skin tumorigenesis in C57BL/6 mice by sulforaphane is mediated by nuclear factor E2-related factor 2
    • [51] Xu, C., Huang, M.T., Shen, G., Yuan, X., Lin, W., Khor, T.O., et al. Inhibition of 7,12-dimethylbenz(a)anthracene-induced skin tumorigenesis in C57BL/6 mice by sulforaphane is mediated by nuclear factor E2-related factor 2. Cancer Res 66 (2006), 8293–8296.
    • (2006) Cancer Res , vol.66 , pp. 8293-8296
    • Xu, C.1    Huang, M.T.2    Shen, G.3    Yuan, X.4    Lin, W.5    Khor, T.O.6
  • 52
    • 33644537902 scopus 로고    scopus 로고
    • Potent protection against aflatoxin-induced tumorigenesis through induction of Nrf2-regulated pathways by the triterpenoid 1-[2-cyano-3-,12-dioxooleana-1,9(11)-dien-28-oyl]imidazole
    • [52] Yates, M.S., Kwak, M.K., Egner, P.A., Groopman, J.D., Bodreddigari, S., Sutter, T.R., et al. Potent protection against aflatoxin-induced tumorigenesis through induction of Nrf2-regulated pathways by the triterpenoid 1-[2-cyano-3-,12-dioxooleana-1,9(11)-dien-28-oyl]imidazole. Cancer Res 66 (2006), 2488–2494.
    • (2006) Cancer Res , vol.66 , pp. 2488-2494
    • Yates, M.S.1    Kwak, M.K.2    Egner, P.A.3    Groopman, J.D.4    Bodreddigari, S.5    Sutter, T.R.6
  • 53
    • 84890441806 scopus 로고    scopus 로고
    • Nrf2 knockout enhances intestinal tumorigenesis in Apc(min/+) mice due to attenuation of anti-oxidative stress pathway while potentiates inflammation
    • [53] Cheung, K.L., Lee, J.H., Khor, T.O., Wu, T.Y., Li, G.X., Chan, J., et al. Nrf2 knockout enhances intestinal tumorigenesis in Apc(min/+) mice due to attenuation of anti-oxidative stress pathway while potentiates inflammation. Mol Carcinog 53 (2014), 77–84.
    • (2014) Mol Carcinog , vol.53 , pp. 77-84
    • Cheung, K.L.1    Lee, J.H.2    Khor, T.O.3    Wu, T.Y.4    Li, G.X.5    Chan, J.6
  • 54
    • 56249086316 scopus 로고    scopus 로고
    • Increased susceptibility of Nrf2 knockout mice to colitis-associated colorectal cancer
    • [54] Khor, T.O., Huang, M.T., Prawan, A., Liu, Y., Hao, X., Yu, S., et al. Increased susceptibility of Nrf2 knockout mice to colitis-associated colorectal cancer. Cancer Prev Res (Phila) 1 (2008), 187–191.
    • (2008) Cancer Prev Res (Phila) , vol.1 , pp. 187-191
    • Khor, T.O.1    Huang, M.T.2    Prawan, A.3    Liu, Y.4    Hao, X.5    Yu, S.6
  • 56
    • 84864348569 scopus 로고    scopus 로고
    • NRF2 and cancer: the good, the bad and the importance of context
    • [56] Sporn, M.B., Liby, K.T., NRF2 and cancer: the good, the bad and the importance of context. Nat Rev Cancer 12 (2012), 564–571.
    • (2012) Nat Rev Cancer , vol.12 , pp. 564-571
    • Sporn, M.B.1    Liby, K.T.2
  • 57
    • 79960060305 scopus 로고    scopus 로고
    • Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis
    • [57] DeNicola, G.M., Karreth, F.A., Humpton, T.J., Gopinathan, A., Wei, C., Frese, K., et al. Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis. Nature 475 (2011), 106–109.
    • (2011) Nature , vol.475 , pp. 106-109
    • DeNicola, G.M.1    Karreth, F.A.2    Humpton, T.J.3    Gopinathan, A.4    Wei, C.5    Frese, K.6
  • 58
    • 51649130168 scopus 로고    scopus 로고
    • Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy
    • [58] Shibata, T., Ohta, T., Tong, K.I., Kokubu, A., Odogawa, R., Tsuta, K., et al. Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy. Proc Natl Acad Sci USA 105 (2008), 13568–13573.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13568-13573
    • Shibata, T.1    Ohta, T.2    Tong, K.I.3    Kokubu, A.4    Odogawa, R.5    Tsuta, K.6
  • 59
    • 76649089973 scopus 로고    scopus 로고
    • Loss of Kelch-like ECH-associated protein 1 function in prostate cancer cells causes chemoresistance and radioresistance and promotes tumor growth
    • [59] Zhang, P., Singh, A., Yegnasubramanian, S., Esopi, D., Kombairaju, P., Bodas, M., et al. Loss of Kelch-like ECH-associated protein 1 function in prostate cancer cells causes chemoresistance and radioresistance and promotes tumor growth. Mol Cancer Ther 9 (2010), 336–346.
    • (2010) Mol Cancer Ther , vol.9 , pp. 336-346
    • Zhang, P.1    Singh, A.2    Yegnasubramanian, S.3    Esopi, D.4    Kombairaju, P.5    Bodas, M.6
  • 60
    • 80054772589 scopus 로고    scopus 로고
    • An antioxidant response phenotype shared between hereditary and sporadic type 2 papillary renal cell carcinoma
    • [60] Ooi, A., Wong, J.C., Petillo, D., Roossien, D., Perrier-Trudova, V., Whitten, D., et al. An antioxidant response phenotype shared between hereditary and sporadic type 2 papillary renal cell carcinoma. Cancer Cell 20 (2011), 511–523.
    • (2011) Cancer Cell , vol.20 , pp. 511-523
    • Ooi, A.1    Wong, J.C.2    Petillo, D.3    Roossien, D.4    Perrier-Trudova, V.5    Whitten, D.6
  • 61
    • 80054767730 scopus 로고    scopus 로고
    • Renal cyst formation in Fh1-deficient mice is independent of the Hif/Phd pathway: roles for fumarate in KEAP1 succination and Nrf2 signaling
    • [61] Adam, J., Hatipoglu, E., O'Flaherty, L., Ternette, N., Sahgal, N., Lockstone, H., et al. Renal cyst formation in Fh1-deficient mice is independent of the Hif/Phd pathway: roles for fumarate in KEAP1 succination and Nrf2 signaling. Cancer Cell 20 (2011), 524–537.
    • (2011) Cancer Cell , vol.20 , pp. 524-537
    • Adam, J.1    Hatipoglu, E.2    O'Flaherty, L.3    Ternette, N.4    Sahgal, N.5    Lockstone, H.6
  • 62
    • 84878785993 scopus 로고    scopus 로고
    • The Keap1-Nrf2 pathway: mechanisms of activation and dysregulation in cancer
    • [62] Kansanen, E., Kuosmanen, S.M., Leinonen, H., Levonen, A.L., The Keap1-Nrf2 pathway: mechanisms of activation and dysregulation in cancer. Redox Biol 1 (2013), 45–49.
    • (2013) Redox Biol , vol.1 , pp. 45-49
    • Kansanen, E.1    Kuosmanen, S.M.2    Leinonen, H.3    Levonen, A.L.4
  • 63
    • 84880048347 scopus 로고    scopus 로고
    • Nrf2 prevents initiation but accelerates progression through the Kras signaling pathway during lung carcinogenesis
    • [63] Satoh, H., Moriguchi, T., Takai, J., Ebina, M., Yamamoto, M., Nrf2 prevents initiation but accelerates progression through the Kras signaling pathway during lung carcinogenesis. Cancer Res 73 (2013), 4158–4168.
    • (2013) Cancer Res , vol.73 , pp. 4158-4168
    • Satoh, H.1    Moriguchi, T.2    Takai, J.3    Ebina, M.4    Yamamoto, M.5
  • 64
  • 65
    • 3543072186 scopus 로고    scopus 로고
    • Overweight, obesity and cancer: epidemiological evidence and proposed mechanisms
    • [65] Calle, E.E., Kaaks, R., Overweight, obesity and cancer: epidemiological evidence and proposed mechanisms. Nat Rev Cancer 4 (2004), 579–591.
    • (2004) Nat Rev Cancer , vol.4 , pp. 579-591
    • Calle, E.E.1    Kaaks, R.2
  • 66
    • 0037464510 scopus 로고    scopus 로고
    • Overweight, obesity, and mortality from cancer in a prospectively studied cohort of U.S. adults
    • [66] Calle, E.E., Rodriguez, C., Walker-Thurmond, K., Thun, M.J., Overweight, obesity, and mortality from cancer in a prospectively studied cohort of U.S. adults. N Engl J Med 348 (2003), 1625–1638.
    • (2003) N Engl J Med , vol.348 , pp. 1625-1638
    • Calle, E.E.1    Rodriguez, C.2    Walker-Thurmond, K.3    Thun, M.J.4
  • 67
    • 85006768050 scopus 로고
    • The metabolism of tumors in the body
    • [67] Warburg, O., Wind, F., Negelein, E., The metabolism of tumors in the body. J Gen Physiol 8 (1927), 519–530.
    • (1927) J Gen Physiol , vol.8 , pp. 519-530
    • Warburg, O.1    Wind, F.2    Negelein, E.3
  • 69
    • 0036717382 scopus 로고    scopus 로고
    • Molecular imaging of cancer with positron emission tomography
    • [69] Gambhir, S.S., Molecular imaging of cancer with positron emission tomography. Nat Rev Cancer 2 (2002), 683–693.
    • (2002) Nat Rev Cancer , vol.2 , pp. 683-693
    • Gambhir, S.S.1
  • 70
    • 34250712408 scopus 로고    scopus 로고
    • Tumor-specific positron emission tomography imaging in patients: [18F] fluorodeoxyglucose and beyond
    • [70] Mankoff, D.A., Eary, J.F., Link, J.M., Muzi, M., Rajendran, J.G., Spence, A.M., et al. Tumor-specific positron emission tomography imaging in patients: [18F] fluorodeoxyglucose and beyond. Clin Cancer Res 13 (2007), 3460–3469.
    • (2007) Clin Cancer Res , vol.13 , pp. 3460-3469
    • Mankoff, D.A.1    Eary, J.F.2    Link, J.M.3    Muzi, M.4    Rajendran, J.G.5    Spence, A.M.6
  • 71
    • 84884893986 scopus 로고    scopus 로고
    • Brain tumor initiating cells adapt to restricted nutrition through preferential glucose uptake
    • [71] Flavahan, W.A., Wu, Q., Hitomi, M., Rahim, N., Kim, Y., Sloan, A.E., et al. Brain tumor initiating cells adapt to restricted nutrition through preferential glucose uptake. Nat Neurosci 16 (2013), 1373–1382.
    • (2013) Nat Neurosci , vol.16 , pp. 1373-1382
    • Flavahan, W.A.1    Wu, Q.2    Hitomi, M.3    Rahim, N.4    Kim, Y.5    Sloan, A.E.6
  • 72
    • 23044500915 scopus 로고    scopus 로고
    • Pyruvate kinase type M2 and its role in tumor growth and spreading
    • [72] Mazurek, S., Boschek, C.B., Hugo, F., Eigenbrodt, E., Pyruvate kinase type M2 and its role in tumor growth and spreading. Semin Cancer Biol 15 (2005), 300–308.
    • (2005) Semin Cancer Biol , vol.15 , pp. 300-308
    • Mazurek, S.1    Boschek, C.B.2    Hugo, F.3    Eigenbrodt, E.4
  • 73
    • 40749163248 scopus 로고    scopus 로고
    • The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
    • [73] Christofk, H.R., Vander Heiden, M.G., Harris, M.H., Ramanathan, A., Gerszten, R.E., Wei, R., et al. The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature 452 (2008), 230–233.
    • (2008) Nature , vol.452 , pp. 230-233
    • Christofk, H.R.1    Vander Heiden, M.G.2    Harris, M.H.3    Ramanathan, A.4    Gerszten, R.E.5    Wei, R.6
  • 74
    • 79958103961 scopus 로고    scopus 로고
    • Pyruvate kinase type M2: a key regulator of the metabolic budget system in tumor cells
    • [74] Mazurek, S., Pyruvate kinase type M2: a key regulator of the metabolic budget system in tumor cells. Int J Biochem Cell Biol 43 (2011), 969–980.
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 969-980
    • Mazurek, S.1
  • 75
    • 84866842363 scopus 로고    scopus 로고
    • Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis
    • [75] Anastasiou, D., Yu, Y., Israelsen, W.J., Jiang, J.K., Boxer, M.B., Hong, B.S., et al. Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis. Nat Chem Biol 8 (2012), 839–847.
    • (2012) Nat Chem Biol , vol.8 , pp. 839-847
    • Anastasiou, D.1    Yu, Y.2    Israelsen, W.J.3    Jiang, J.K.4    Boxer, M.B.5    Hong, B.S.6
  • 76
    • 84905097406 scopus 로고    scopus 로고
    • Pyruvate kinase M2 and cancer: an updated assessment
    • [76] Iqbal, M.A., Gupta, V., Gopinath, P., Mazurek, S., Bamezai, R.N., Pyruvate kinase M2 and cancer: an updated assessment. FEBS Lett 588 (2014), 2685–2692.
    • (2014) FEBS Lett , vol.588 , pp. 2685-2692
    • Iqbal, M.A.1    Gupta, V.2    Gopinath, P.3    Mazurek, S.4    Bamezai, R.N.5
  • 77
    • 33344456073 scopus 로고    scopus 로고
    • Expression of transketolase TKTL1 predicts colon and urothelial cancer patient survival: Warburg effect reinterpreted
    • [77] Langbein, S., Zerilli, M., Zur Hausen, A., Staiger, W., Rensch-Boschert, K., Lukan, N., et al. Expression of transketolase TKTL1 predicts colon and urothelial cancer patient survival: Warburg effect reinterpreted. Br J Cancer 94 (2006), 578–585.
    • (2006) Br J Cancer , vol.94 , pp. 578-585
    • Langbein, S.1    Zerilli, M.2    Zur Hausen, A.3    Staiger, W.4    Rensch-Boschert, K.5    Lukan, N.6
  • 78
    • 34249942508 scopus 로고    scopus 로고
    • Transketolase protein TKTL1 overexpression: a potential biomarker and therapeutic target in breast cancer
    • [78] Földi, M., Stickeler, E., Bau, L., Kretz, O., Watermann, D., Gitsch, G., et al. Transketolase protein TKTL1 overexpression: a potential biomarker and therapeutic target in breast cancer. Oncol Rep 17 (2007), 841–845.
    • (2007) Oncol Rep , vol.17 , pp. 841-845
    • Földi, M.1    Stickeler, E.2    Bau, L.3    Kretz, O.4    Watermann, D.5    Gitsch, G.6
  • 79
    • 37449034854 scopus 로고    scopus 로고
    • Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis
    • [79] DeBerardinis, R.J., Mancuso, A., Daikhin, E., Nissim, I., Yudkoff, M., Wehrli, S., et al. Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis. Proc Natl Acad Sci USA 104 (2007), 19345–19350.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19345-19350
    • DeBerardinis, R.J.1    Mancuso, A.2    Daikhin, E.3    Nissim, I.4    Yudkoff, M.5    Wehrli, S.6
  • 80
    • 70350217425 scopus 로고    scopus 로고
    • Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling
    • [80] Yang, C., Sudderth, J., Dang, T., Bachoo, R.M., McDonald, J.G., DeBerardinis, R.J., Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling. Cancer Res 69 (2009), 7986–7993.
    • (2009) Cancer Res , vol.69 , pp. 7986-7993
    • Yang, C.1    Sudderth, J.2    Dang, T.3    Bachoo, R.M.4    McDonald, J.G.5    DeBerardinis, R.J.6
  • 81
    • 84858120137 scopus 로고    scopus 로고
    • Targeting the lactate transporter MCT1 in endothelial cells inhibits lactate-induced HIF-1 activation and tumor angiogenesis
    • [81] Sonveaux, P., Copetti, T., De Saedeleer, C.J., Végran, F., Verrax, J., Kennedy, K.M., et al. Targeting the lactate transporter MCT1 in endothelial cells inhibits lactate-induced HIF-1 activation and tumor angiogenesis. PLoS One, 7, 2012, e33418.
    • (2012) PLoS One , vol.7 , pp. e33418
    • Sonveaux, P.1    Copetti, T.2    De Saedeleer, C.J.3    Végran, F.4    Verrax, J.5    Kennedy, K.M.6
  • 82
    • 0029908016 scopus 로고    scopus 로고
    • Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation
    • [82] Kohn, A.D., Summers, S.A., Birnbaum, M.J., Roth, R.A., Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J Biol Chem 271 (1996), 31372–31378.
    • (1996) J Biol Chem , vol.271 , pp. 31372-31378
    • Kohn, A.D.1    Summers, S.A.2    Birnbaum, M.J.3    Roth, R.A.4
  • 83
    • 0032571257 scopus 로고    scopus 로고
    • Insulin increases the association of Akt-2 with Glut4-containing vesicles
    • [83] Calera, M.R., Martinez, C., Liu, H., Jack, A.K., Birnbaum, M.J., Pilch, P.F., Insulin increases the association of Akt-2 with Glut4-containing vesicles. J Biol Chem 273 (1998), 7201–7204.
    • (1998) J Biol Chem , vol.273 , pp. 7201-7204
    • Calera, M.R.1    Martinez, C.2    Liu, H.3    Jack, A.K.4    Birnbaum, M.J.5    Pilch, P.F.6
  • 84
    • 0035853833 scopus 로고    scopus 로고
    • Akt and Bcl-xL promote growth factor-independent survival through distinct effects on mitochondrial physiology
    • [84] Plas, D.R., Talapatra, S., Edinger, A.L., Rathmell, J.C., Thompson, C.B., Akt and Bcl-xL promote growth factor-independent survival through distinct effects on mitochondrial physiology. J Biol Chem 276 (2001), 12041–12048.
    • (2001) J Biol Chem , vol.276 , pp. 12041-12048
    • Plas, D.R.1    Talapatra, S.2    Edinger, A.L.3    Rathmell, J.C.4    Thompson, C.B.5
  • 85
    • 0036320205 scopus 로고    scopus 로고
    • Akt maintains cell size and survival by increasing mTOR-dependent nutrient uptake
    • [85] Edinger, A.L., Thompson, C.B., Akt maintains cell size and survival by increasing mTOR-dependent nutrient uptake. Mol Biol Cell 13 (2002), 2276–2288.
    • (2002) Mol Biol Cell , vol.13 , pp. 2276-2288
    • Edinger, A.L.1    Thompson, C.B.2
  • 86
    • 0141863388 scopus 로고    scopus 로고
    • Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival
    • [86] Rathmell, J.C., Fox, C.J., Plas, D.R., Hammerman, P.S., Cinalli, R.M., Thompson, C.B., Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival. Mol Cell Biol 23 (2003), 7315–7328.
    • (2003) Mol Cell Biol , vol.23 , pp. 7315-7328
    • Rathmell, J.C.1    Fox, C.J.2    Plas, D.R.3    Hammerman, P.S.4    Cinalli, R.M.5    Thompson, C.B.6
  • 87
    • 4544331713 scopus 로고    scopus 로고
    • Activation of PI3K is indispensable for interleukin 7-mediated viability, proliferation, glucose use, and growth of T cell acute lymphoblastic leukemia cells
    • [87] Barata, J.T., Silva, A., Brandao, J.G., Nadler, L.M., Cardoso, A.A., Boussiotis, V.A., Activation of PI3K is indispensable for interleukin 7-mediated viability, proliferation, glucose use, and growth of T cell acute lymphoblastic leukemia cells. J Exp Med 200 (2004), 659–669.
    • (2004) J Exp Med , vol.200 , pp. 659-669
    • Barata, J.T.1    Silva, A.2    Brandao, J.G.3    Nadler, L.M.4    Cardoso, A.A.5    Boussiotis, V.A.6
  • 89
    • 37549032776 scopus 로고    scopus 로고
    • The interplay between MYC and HIF in cancer
    • [89] Dang, C.V., Kim, J.W., Gao, P., Yustein, J., The interplay between MYC and HIF in cancer. Nat Rev Cancer 8 (2008), 51–56.
    • (2008) Nat Rev Cancer , vol.8 , pp. 51-56
    • Dang, C.V.1    Kim, J.W.2    Gao, P.3    Yustein, J.4
  • 90
    • 57749088701 scopus 로고    scopus 로고
    • Myc regulates a transcriptional program that stimulates mitochondrial glutaminolysis and leads to glutamine addiction
    • [90] Wise, D.R., DeBerardinis, R.J., Mancuso, A., Sayed, N., Zhang, X.Y., Pfeiffer, H.K., et al. Myc regulates a transcriptional program that stimulates mitochondrial glutaminolysis and leads to glutamine addiction. Proc Natl Acad Sci USA 105 (2008), 18782–18787.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18782-18787
    • Wise, D.R.1    DeBerardinis, R.J.2    Mancuso, A.3    Sayed, N.4    Zhang, X.Y.5    Pfeiffer, H.K.6
  • 91
    • 75149148563 scopus 로고    scopus 로고
    • Q's next: the diverse functions of glutamine in metabolism, cell biology and cancer
    • [91] DeBerardinis, R.J., Cheng, T., Q's next: the diverse functions of glutamine in metabolism, cell biology and cancer. Oncogene 29 (2010), 313–324.
    • (2010) Oncogene , vol.29 , pp. 313-324
    • DeBerardinis, R.J.1    Cheng, T.2
  • 93
    • 0030882879 scopus 로고    scopus 로고
    • Glucose catabolism in cancer cells. The type II hexokinase promoter contains functionally active response elements for the tumor suppressor p53
    • [93] Mathupala, S.P., Heese, C., Pedersen, P.L., Glucose catabolism in cancer cells. The type II hexokinase promoter contains functionally active response elements for the tumor suppressor p53. J Biol Chem 272 (1997), 22776–22780.
    • (1997) J Biol Chem , vol.272 , pp. 22776-22780
    • Mathupala, S.P.1    Heese, C.2    Pedersen, P.L.3
  • 94
    • 0033257077 scopus 로고    scopus 로고
    • Identification of seven genes regulated by wild-type p53 in a colon cancer cell line carrying a well-controlled wild-type p53 expression system
    • [94] Okamura, S., Ng, C.C., Koyama, K., Takei, Y., Arakawa, H., Monden, M., et al. Identification of seven genes regulated by wild-type p53 in a colon cancer cell line carrying a well-controlled wild-type p53 expression system. Oncol Res 11 (1999), 281–285.
    • (1999) Oncol Res , vol.11 , pp. 281-285
    • Okamura, S.1    Ng, C.C.2    Koyama, K.3    Takei, Y.4    Arakawa, H.5    Monden, M.6
  • 95
    • 1942506067 scopus 로고    scopus 로고
    • The tumor suppressor p53 down-regulates glucose transporters GLUT1 and GLUT4 gene expression
    • [95] Schwartzenberg-Bar-Yoseph, F., Armoni, M., Karnieli, E., The tumor suppressor p53 down-regulates glucose transporters GLUT1 and GLUT4 gene expression. Cancer Res 64 (2004), 2627–2633.
    • (2004) Cancer Res , vol.64 , pp. 2627-2633
    • Schwartzenberg-Bar-Yoseph, F.1    Armoni, M.2    Karnieli, E.3
  • 97
    • 33745918951 scopus 로고    scopus 로고
    • TIGAR, a p53-inducible regulator of glycolysis and apoptosis
    • [97] Bensaad, K., Tsuruta, A., Selak, M.A., Vidal, M.N., Nakano, K., Bartrons, R., et al. TIGAR, a p53-inducible regulator of glycolysis and apoptosis. Cell 126 (2006), 107–120.
    • (2006) Cell , vol.126 , pp. 107-120
    • Bensaad, K.1    Tsuruta, A.2    Selak, M.A.3    Vidal, M.N.4    Nakano, K.5    Bartrons, R.6
  • 98
    • 84869077946 scopus 로고    scopus 로고
    • Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth
    • [98] Hitosugi, T., Zhou, L., Elf, S., Fan, J., Kang, H.B., Seo, J.H., et al. Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth. Cancer Cell 22 (2012), 585–600.
    • (2012) Cancer Cell , vol.22 , pp. 585-600
    • Hitosugi, T.1    Zhou, L.2    Elf, S.3    Fan, J.4    Kang, H.B.5    Seo, J.H.6
  • 99
    • 52949127312 scopus 로고    scopus 로고
    • An integrated genomic analysis of human glioblastoma multiforme
    • [99] Parsons, D.W., Jones, S., Zhang, X., Lin, J.C., Leary, R.J., Angenendt, P., et al. An integrated genomic analysis of human glioblastoma multiforme. Science 321 (2008), 1807–1812.
    • (2008) Science , vol.321 , pp. 1807-1812
    • Parsons, D.W.1    Jones, S.2    Zhang, X.3    Lin, J.C.4    Leary, R.J.5    Angenendt, P.6
  • 100
    • 73649088347 scopus 로고    scopus 로고
    • Mutant metabolic enzymes are at the origin of gliomas
    • [100] Yan, H., Bigner, D.D., Velculescu, V., Parsons, D.W., Mutant metabolic enzymes are at the origin of gliomas. Cancer Res 69 (2009), 9157–9159.
    • (2009) Cancer Res , vol.69 , pp. 9157-9159
    • Yan, H.1    Bigner, D.D.2    Velculescu, V.3    Parsons, D.W.4
  • 102
    • 70149093912 scopus 로고    scopus 로고
    • Recurring mutations found by sequencing an acute myeloid leukemia genome
    • [102] Mardis, E.R., Ding, L., Dooling, D.J., Larson, D.E., McLellan, M.D., Chen, K., et al. Recurring mutations found by sequencing an acute myeloid leukemia genome. N Engl J Med 361 (2009), 1058–1066.
    • (2009) N Engl J Med , vol.361 , pp. 1058-1066
    • Mardis, E.R.1    Ding, L.2    Dooling, D.J.3    Larson, D.E.4    McLellan, M.D.5    Chen, K.6
  • 104
    • 64849098267 scopus 로고    scopus 로고
    • Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha
    • [104] Zhao, S., Lin, Y., Xu, W., Jiang, W., Zha, Z., Wang, P., et al. Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha. Science 324 (2009), 261–265.
    • (2009) Science , vol.324 , pp. 261-265
    • Zhao, S.1    Lin, Y.2    Xu, W.3    Jiang, W.4    Zha, Z.5    Wang, P.6
  • 105
    • 26444570010 scopus 로고    scopus 로고
    • Accumulation of Krebs cycle intermediates and over-expression of HIF1alpha in tumours which result from germline FH and SDH mutations
    • [105] Pollard, P.J., Brière, J.J., Alam, N.A., Barwell, J., Barclay, E., Wortham, N.C., et al. Accumulation of Krebs cycle intermediates and over-expression of HIF1alpha in tumours which result from germline FH and SDH mutations. Hum Mol Genet 14 (2005), 2231–2239.
    • (2005) Hum Mol Genet , vol.14 , pp. 2231-2239
    • Pollard, P.J.1    Brière, J.J.2    Alam, N.A.3    Barwell, J.4    Barclay, E.5    Wortham, N.C.6
  • 106
    • 19944433653 scopus 로고    scopus 로고
    • Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase
    • [106] Selak, M.A., Armour, S.M., MacKenzie, E.D., Boulahbel, H., Watson, D.G., Mansfield, K.D., et al. Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase. Cancer Cell 7 (2005), 77–85.
    • (2005) Cancer Cell , vol.7 , pp. 77-85
    • Selak, M.A.1    Armour, S.M.2    MacKenzie, E.D.3    Boulahbel, H.4    Watson, D.G.5    Mansfield, K.D.6
  • 108
    • 84921501276 scopus 로고    scopus 로고
    • Teaching the basics of autophagy and mitophagy to redox biologists – mechanisms and experimental approaches
    • [108] Zhang, J., Teaching the basics of autophagy and mitophagy to redox biologists – mechanisms and experimental approaches. Redox Biol 4 (2015), 242–259.
    • (2015) Redox Biol , vol.4 , pp. 242-259
    • Zhang, J.1
  • 110
    • 11244297916 scopus 로고    scopus 로고
    • Dysregulation of the TSC-mTOR pathway in human disease
    • [110] Inoki, K., Corradetti, M.N., Guan, K.L., Dysregulation of the TSC-mTOR pathway in human disease. Nat Genet 37 (2005), 19–24.
    • (2005) Nat Genet , vol.37 , pp. 19-24
    • Inoki, K.1    Corradetti, M.N.2    Guan, K.L.3
  • 111
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • [111] Liang, X.H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., et al. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature 402 (1999), 672–676.
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1    Jackson, S.2    Seaman, M.3    Brown, K.4    Kempkes, B.5    Hibshoosh, H.6
  • 112
    • 9144240441 scopus 로고    scopus 로고
    • Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene
    • [112] 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 112 (2003), 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
  • 113
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploin sufficient tumor suppressor
    • [113] Yue, Z., Jin, S., Yang, C., Levine, A.J., Heintz, N., Beclin 1, an autophagy gene essential for early embryonic development, is a haploin sufficient tumor suppressor. Proc Natl Acad Sci USA 100 (2003), 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
  • 114
    • 34547132328 scopus 로고    scopus 로고
    • Tissue-specific autophagy alterations and increased tumorigenesis in mice deficient in Atg4C/autophagin-3
    • [114] Mariño, G., Salvador-Montoliu, N., Fueyo, A., Knecht, E., Mizushima, N., López-Otín, C., Tissue-specific autophagy alterations and increased tumorigenesis in mice deficient in Atg4C/autophagin-3. J Biol Chem 282 (2007), 18573–18583.
    • (2007) J Biol Chem , vol.282 , pp. 18573-18583
    • Mariño, G.1    Salvador-Montoliu, N.2    Fueyo, A.3    Knecht, E.4    Mizushima, N.5    López-Otín, C.6
  • 116
    • 77949541314 scopus 로고    scopus 로고
    • High expression of gabarapl1 is associated with a better outcome for patients with lymph node-positive breast cancer
    • [116] Berthier, A., Seguin, S., Sasco, A.J., Bobin, J.Y., De Laroche, G., Datchary, J., et al. High expression of gabarapl1 is associated with a better outcome for patients with lymph node-positive breast cancer. Br J Cancer 102 (2010), 1024–1031.
    • (2010) Br J Cancer , vol.102 , pp. 1024-1031
    • Berthier, A.1    Seguin, S.2    Sasco, A.J.3    Bobin, J.Y.4    De Laroche, G.5    Datchary, J.6
  • 117
    • 84898605742 scopus 로고    scopus 로고
    • Low expression of GABARAPL1 is associated with a poor outcome for patients with hepatocellular carcinoma
    • [117] Liu, C., Xia, Y., Jiang, W., Liu, Y., Yu, L., Low expression of GABARAPL1 is associated with a poor outcome for patients with hepatocellular carcinoma. Oncol Rep 31 (2014), 2043–2048.
    • (2014) Oncol Rep , vol.31 , pp. 2043-2048
    • Liu, C.1    Xia, Y.2    Jiang, W.3    Liu, Y.4    Yu, L.5
  • 118
    • 77955172368 scopus 로고    scopus 로고
    • Autophagy negatively regulates Wnt signalling by promoting Dishevelled degradation
    • [118] Gao, C., Cao, W., Bao, L., Zuo, W., Xie, G., Cai, T., et al. Autophagy negatively regulates Wnt signalling by promoting Dishevelled degradation. Nat Cell Biol 12 (2010), 781–790.
    • (2010) Nat Cell Biol , vol.12 , pp. 781-790
    • Gao, C.1    Cao, W.2    Bao, L.3    Zuo, W.4    Xie, G.5    Cai, T.6
  • 119
    • 79959467280 scopus 로고    scopus 로고
    • GABARAPL1 negatively regulates Wnt/ß-catenin signaling by mediating Dvl2 degradation through the autophagy pathway
    • [119] Zhang, Y., Wang, F., Han, L., Wu, Y., Li, S., Yang, X., et al. GABARAPL1 negatively regulates Wnt/ß-catenin signaling by mediating Dvl2 degradation through the autophagy pathway. Cell Physiol Biochem 27 (2011), 503–512.
    • (2011) Cell Physiol Biochem , vol.27 , pp. 503-512
    • Zhang, Y.1    Wang, F.2    Han, L.3    Wu, Y.4    Li, S.5    Yang, X.6
  • 120
    • 84903601805 scopus 로고    scopus 로고
    • The role of GABARAPL1/GEC1 in autophagic flux and mitochondrial quality control in MDA-MB-436 breast cancer cells
    • [120] Boyer-Guittaut, M., Poillet, L., Liang, Q., Bôle-Richard, E., Ouyang, X., Benavides, G.A., et al. The role of GABARAPL1/GEC1 in autophagic flux and mitochondrial quality control in MDA-MB-436 breast cancer cells. Autophagy 10 (2014), 986–1003.
    • (2014) Autophagy , vol.10 , pp. 986-1003
    • Boyer-Guittaut, M.1    Poillet, L.2    Liang, Q.3    Bôle-Richard, E.4    Ouyang, X.5    Benavides, G.A.6
  • 121
    • 84876861153 scopus 로고    scopus 로고
    • Paracrine Wnt signaling both promotes and inhibits human breast tumor growth
    • [121] Green, J.L., La, J., Yum, K.W., Desai, P., Rodewald, L.W., Zhang, X., et al. Paracrine Wnt signaling both promotes and inhibits human breast tumor growth. Proc Natl Acad Sci USA 110 (2013), 6991–6996.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 6991-6996
    • Green, J.L.1    La, J.2    Yum, K.W.3    Desai, P.4    Rodewald, L.W.5    Zhang, X.6
  • 122
    • 84897482887 scopus 로고    scopus 로고
    • Tumour cell heterogeneity maintained by cooperating subclones in Wnt-driven mammary cancers
    • [122] Cleary, A.S., Leonard, T.L., Gestl, S.A., Gunther, E.J., Tumour cell heterogeneity maintained by cooperating subclones in Wnt-driven mammary cancers. Nature 508 (2014), 113–117.
    • (2014) Nature , vol.508 , pp. 113-117
    • Cleary, A.S.1    Leonard, T.L.2    Gestl, S.A.3    Gunther, E.J.4
  • 123
    • 79960401862 scopus 로고    scopus 로고
    • Suppression of autophagy by FIP200 deletion inhibits mammary tumorigenesis
    • [123] Wei, H., Wei, S., Gan, B., Peng, X., Zou, W., Guan, J.L., Suppression of autophagy by FIP200 deletion inhibits mammary tumorigenesis. Genes Dev 25 (2011), 1510–1527.
    • (2011) Genes Dev , vol.25 , pp. 1510-1527
    • Wei, H.1    Wei, S.2    Gan, B.3    Peng, X.4    Zou, W.5    Guan, J.L.6
  • 124
    • 84890018924 scopus 로고    scopus 로고
    • Autophagy-mediated tumor promotion
    • [124] Guo, J.Y., Xia, B., White, E., Autophagy-mediated tumor promotion. Cell 155 (2013), 1216–1219.
    • (2013) Cell , vol.155 , pp. 1216-1219
    • Guo, J.Y.1    Xia, B.2    White, E.3
  • 126
    • 78751556979 scopus 로고    scopus 로고
    • Autophagy as a therapeutic target in cancer
    • [126] Chen, N., Karantza, V., Autophagy as a therapeutic target in cancer. Cancer Biol Ther 11 (2011), 157–168.
    • (2011) Cancer Biol Ther , vol.11 , pp. 157-168
    • Chen, N.1    Karantza, V.2
  • 127
    • 0344441899 scopus 로고    scopus 로고
    • Alterations in the common fragile site gene Parkin in ovarian and other cancers
    • [127] Denison, S.R., Wang, F., Becker, N.A., Schüle, B., Kock, N., Phillips, L.A., et al. Alterations in the common fragile site gene Parkin in ovarian and other cancers. Oncogene 22 (2003), 8370–8378.
    • (2003) Oncogene , vol.22 , pp. 8370-8378
    • Denison, S.R.1    Wang, F.2    Becker, N.A.3    Schüle, B.4    Kock, N.5    Phillips, L.A.6
  • 128
    • 0038732456 scopus 로고    scopus 로고
    • Parkin, a gene implicated in autosomal recessive juvenile parkinsonism, is a candidate tumor suppressor gene on chromosome 6q25-q27
    • [128] Cesari, R., Martin, E.S., Calin, G.A., Pentimalli, F., Bichi, R., McAdams, H., et al. Parkin, a gene implicated in autosomal recessive juvenile parkinsonism, is a candidate tumor suppressor gene on chromosome 6q25-q27. Proc Natl Acad Sci USA 100 (2003), 5956–5961.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5956-5961
    • Cesari, R.1    Martin, E.S.2    Calin, G.A.3    Pentimalli, F.4    Bichi, R.5    McAdams, H.6
  • 129
    • 11144355981 scopus 로고    scopus 로고
    • Alterations of the tumor suppressor gene Parkin in non-small cell lung cancer
    • [129] Picchio, M.C., Martin, E.S., Cesari, R., Calin, G.A., Yendamuri, S., Kuroki, T., et al. Alterations of the tumor suppressor gene Parkin in non-small cell lung cancer. Clin Cancer Res 10 (2004), 2720–2724.
    • (2004) Clin Cancer Res , vol.10 , pp. 2720-2724
    • Picchio, M.C.1    Martin, E.S.2    Cesari, R.3    Calin, G.A.4    Yendamuri, S.5    Kuroki, T.6
  • 131
    • 53649108020 scopus 로고    scopus 로고
    • Parkin as a tumor suppressor gene for hepatocellular carcinoma
    • [131] Fujiwara, M., Marusawa, H., Wang, H.Q., Iwai, A., Ikeuchi, K., Imai, Y., et al. Parkin as a tumor suppressor gene for hepatocellular carcinoma. Oncogene 27 (2008), 6002–6011.
    • (2008) Oncogene , vol.27 , pp. 6002-6011
    • Fujiwara, M.1    Marusawa, H.2    Wang, H.Q.3    Iwai, A.4    Ikeuchi, K.5    Imai, Y.6
  • 132
    • 73349125417 scopus 로고    scopus 로고
    • Somatic mutations of the Parkinson's disease-associated gene PARK2 in glioblastoma and other human malignancies
    • [132] Veeriah, S., Taylor, B.S., Meng, S., Fang, F., Yilmaz, E., Vivanco, I., et al. Somatic mutations of the Parkinson's disease-associated gene PARK2 in glioblastoma and other human malignancies. Nat Genet 42 (2010), 77–82.
    • (2010) Nat Genet , vol.42 , pp. 77-82
    • Veeriah, S.1    Taylor, B.S.2    Meng, S.3    Fang, F.4    Yilmaz, E.5    Vivanco, I.6
  • 133
    • 84861111156 scopus 로고    scopus 로고
    • Parkin pathway activation mitigates glioma cell proliferation and predicts patient survival
    • [133] Yeo, C.W., Ng, F.S., Chai, C., Tan, J.M., Koh, G.R., Chong, Y.K., et al. Parkin pathway activation mitigates glioma cell proliferation and predicts patient survival. Cancer Res 72 (2012), 2543–2553.
    • (2012) Cancer Res , vol.72 , pp. 2543-2553
    • Yeo, C.W.1    Ng, F.S.2    Chai, C.3    Tan, J.M.4    Koh, G.R.5    Chong, Y.K.6
  • 134
    • 84875909195 scopus 로고    scopus 로고
    • Parkin deficiency contributes to pancreatic tumorigenesis by inducing spindle multipolarity and misorientation
    • [134] Sun, X., Liu, M., Hao, J., Li, D., Luo, Y., Wang, X., et al. Parkin deficiency contributes to pancreatic tumorigenesis by inducing spindle multipolarity and misorientation. Cell Cycle 12 (2013), 1133–1141.
    • (2013) Cell Cycle , vol.12 , pp. 1133-1141
    • Sun, X.1    Liu, M.2    Hao, J.3    Li, D.4    Luo, Y.5    Wang, X.6
  • 135
    • 84861204926 scopus 로고    scopus 로고
    • PINK1- and Parkin-mediated mitophagy at a glance
    • [135] Jin, S.M., Youle, R.J., PINK1- and Parkin-mediated mitophagy at a glance. J Cell Sci 125 (2012), 795–799.
    • (2012) J Cell Sci , vol.125 , pp. 795-799
    • Jin, S.M.1    Youle, R.J.2
  • 136
    • 84863430453 scopus 로고    scopus 로고
    • Mitophagy: a complex mechanism of mitochondrial removal
    • [136] Novak, I., Mitophagy: a complex mechanism of mitochondrial removal. Antioxid Redox Signal 17 (2012), 794–802.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 794-802
    • Novak, I.1
  • 137
    • 84867773087 scopus 로고    scopus 로고
    • Mitophagy: mechanisms, pathophysiological roles, and analysis
    • [137] Ding, W.X., Yin, X.M., Mitophagy: mechanisms, pathophysiological roles, and analysis. Biol Chem 393 (2012), 547–564.
    • (2012) Biol Chem , vol.393 , pp. 547-564
    • Ding, W.X.1    Yin, X.M.2
  • 138
    • 84876296881 scopus 로고    scopus 로고
    • Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
    • [138] Sarraf, S.A., Raman, M., Guarani-Pereira, V., Sowa, M.E., Huttlin, E.L., Gygi, S.P., et al. Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature 496 (2013), 372–376.
    • (2013) Nature , vol.496 , pp. 372-376
    • Sarraf, S.A.1    Raman, M.2    Guarani-Pereira, V.3    Sowa, M.E.4    Huttlin, E.L.5    Gygi, S.P.6
  • 139
    • 84876531457 scopus 로고    scopus 로고
    • 2nd. PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria
    • [139] Chen, Y., Dorn, G.W., 2nd. PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science 340 (2013), 471–475.
    • (2013) Science , vol.340 , pp. 471-475
    • Chen, Y.1    Dorn, G.W.2
  • 140
    • 81055140895 scopus 로고    scopus 로고
    • PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility
    • [140] Wang, X., Winter, D., Ashrafi, G., Schlehe, J., Wong, Y.L., Selkoe, D., et al. PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell 147 (2011), 893–906.
    • (2011) Cell , vol.147 , pp. 893-906
    • Wang, X.1    Winter, D.2    Ashrafi, G.3    Schlehe, J.4    Wong, Y.L.5    Selkoe, D.6
  • 141
    • 84938080852 scopus 로고    scopus 로고
    • Mitofusin-2 over-expresses and leads to dysregulation of cell cycle and cell invasion in lung adenocarcinoma
    • [141] Lou, Y., Li, R., Liu, J., Zhang, Y., Zhang, X., Jin, B., et al. Mitofusin-2 over-expresses and leads to dysregulation of cell cycle and cell invasion in lung adenocarcinoma. Med Oncol, 32, 2015, 132.
    • (2015) Med Oncol , vol.32 , pp. 132
    • Lou, Y.1    Li, R.2    Liu, J.3    Zhang, Y.4    Zhang, X.5    Jin, B.6
  • 142
    • 84655165023 scopus 로고    scopus 로고
    • Anti-tumour efficacy of mitofusin-2 in urinary bladder carcinoma
    • [142] Jin, B., Fu, G., Pan, H., Cheng, X., Zhou, L., Lv, J., et al. Anti-tumour efficacy of mitofusin-2 in urinary bladder carcinoma. Med Oncol 28 (2011), S373–S380.
    • (2011) Med Oncol , vol.28 , pp. S373-S380
    • Jin, B.1    Fu, G.2    Pan, H.3    Cheng, X.4    Zhou, L.5    Lv, J.6
  • 144
    • 84860914473 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fission prevents cell cycle progression in lung cancer
    • [144] Rehman, J., Zhang, H.J., Toth, P.T., Zhang, Y., Marsboom, G., Hong, Z., et al. Inhibition of mitochondrial fission prevents cell cycle progression in lung cancer. FASEB J 26 (2012), 2175–2186.
    • (2012) FASEB J , vol.26 , pp. 2175-2186
    • Rehman, J.1    Zhang, H.J.2    Toth, P.T.3    Zhang, Y.4    Marsboom, G.5    Hong, Z.6
  • 145
    • 80355127945 scopus 로고    scopus 로고
    • Gustafsson ÅB. Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes
    • [145] Lee, Y., Lee, H.Y., Hanna, R.A., Gustafsson ÅB. Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes. Am J Physiol Heart Circ Physiol 301 (2011), H1924–H1931.
    • (2011) Am J Physiol Heart Circ Physiol , vol.301 , pp. H1924-H1931
    • Lee, Y.1    Lee, H.Y.2    Hanna, R.A.3
  • 146
    • 84938690751 scopus 로고    scopus 로고
    • Autophagy capacity and sub-mitochondrial heterogeneity shape Bnip3-induced mitophagy regulation of apoptosis
    • [146] Choe, S.C., Hamacher-Brady, A., Brady, N.R., Autophagy capacity and sub-mitochondrial heterogeneity shape Bnip3-induced mitophagy regulation of apoptosis. Cell Commun Signal, 13, 2015, 37.
    • (2015) Cell Commun Signal , vol.13 , pp. 37
    • Choe, S.C.1    Hamacher-Brady, A.2    Brady, N.R.3
  • 147
    • 84940796811 scopus 로고    scopus 로고
    • Mitophagy defects arising from BNip3 loss promote mammary tumor progression to metastasis
    • [147] Chourasia, A.H., Tracy, K., Frankenberger, C., Boland, M.L., Sharifi, M.N., Drake, L.E., et al. Mitophagy defects arising from BNip3 loss promote mammary tumor progression to metastasis. EMBO Rep 16 (2015), 1145–1163.
    • (2015) EMBO Rep , vol.16 , pp. 1145-1163
    • Chourasia, A.H.1    Tracy, K.2    Frankenberger, C.3    Boland, M.L.4    Sharifi, M.N.5    Drake, L.E.6
  • 148
    • 0034255036 scopus 로고    scopus 로고
    • Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia
    • [148] Bruick, R.K., Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia. Proc Natl Acad Sci USA 97 (2000), 9082–9087.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9082-9087
    • Bruick, R.K.1
  • 149
    • 84940180529 scopus 로고    scopus 로고
    • The emerging theme of redox bioenergetics in health and disease
    • [149] Kramer, P.A., Darley-Usmar, V.M., The emerging theme of redox bioenergetics in health and disease. Biomed J 38 (2015), 294–300.
    • (2015) Biomed J , vol.38 , pp. 294-300
    • Kramer, P.A.1    Darley-Usmar, V.M.2
  • 150
    • 84902462980 scopus 로고    scopus 로고
    • Cell culture, oxidative stress, and antioxidants: avoiding pitfalls
    • [150] Halliwell, B., Cell culture, oxidative stress, and antioxidants: avoiding pitfalls. Biomed J 37 (2014), 99–105.
    • (2014) Biomed J , vol.37 , pp. 99-105
    • Halliwell, B.1
  • 151
    • 84902463475 scopus 로고    scopus 로고
    • Anti-cancer activities of omega -6 polyunsaturated fatty acids
    • [151] Xu, Y., Qian, S.Y., Anti-cancer activities of omega -6 polyunsaturated fatty acids. Biomed J 37 (2014), 112–119.
    • (2014) Biomed J , vol.37 , pp. 112-119
    • Xu, Y.1    Qian, S.Y.2
  • 152
    • 32444433202 scopus 로고    scopus 로고
    • Free radicals, metals and antioxidants in oxidative stress-induced cancer
    • [152] Valko, M., Rhodes, C.J., Moncol, J., Izakovic, M., Mazur, M., Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem Biol Interact 160 (2006), 1–40.
    • (2006) Chem Biol Interact , vol.160 , pp. 1-40
    • Valko, M.1    Rhodes, C.J.2    Moncol, J.3    Izakovic, M.4    Mazur, M.5
  • 153
    • 79251517382 scopus 로고    scopus 로고
    • Regulation of cancer cell metabolism
    • [153] Cairns, R.A., Harris, I.S., Mak, T.W., Regulation of cancer cell metabolism. Nat Rev Cancer 11 (2011), 85–95.
    • (2011) Nat Rev Cancer , vol.11 , pp. 85-95
    • Cairns, R.A.1    Harris, I.S.2    Mak, T.W.3
  • 154
    • 33746466098 scopus 로고    scopus 로고
    • Mitochondrial mutations in cancer
    • [154] Brandon, M., Baldi, P., Wallace, D.C., Mitochondrial mutations in cancer. Oncogene 25 (2006), 4647–4662.
    • (2006) Oncogene , vol.25 , pp. 4647-4662
    • Brandon, M.1    Baldi, P.2    Wallace, D.C.3
  • 155
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • [155] Murphy, M.P., How mitochondria produce reactive oxygen species. Biochem J 417 (2009), 1–13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 156
    • 84920971375 scopus 로고    scopus 로고
    • Interplay between ROS and autophagy in cancer cells, from tumor initiation to cancer therapy
    • [156] Poillet-Perez, L., Despouy, G., Delage-Mourroux, R., Boyer-Guittaut, M., Interplay between ROS and autophagy in cancer cells, from tumor initiation to cancer therapy. Redox Biol 4 (2015), 184–192.
    • (2015) Redox Biol , vol.4 , pp. 184-192
    • Poillet-Perez, L.1    Despouy, G.2    Delage-Mourroux, R.3    Boyer-Guittaut, M.4
  • 157
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • [157] Scherz-Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., Elazar, Z., Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 26 (2007), 1749–1760.
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 158
    • 77749233738 scopus 로고    scopus 로고
    • ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS
    • [158] Alexander, A., Cai, S.L., Kim, J., Nanez, A., Sahin, M., MacLean, K.H., et al. ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS. Proc Natl Acad Sci USA 107 (2010), 4153–4158.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4153-4158
    • Alexander, A.1    Cai, S.L.2    Kim, J.3    Nanez, A.4    Sahin, M.5    MacLean, K.H.6
  • 159
    • 77954599053 scopus 로고    scopus 로고
    • p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • [159] Jain, A., Lamark, T., Sjøttem, E., Larsen, K.B., Awuh, J.A., Øvervatn, A., et al. p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. J Biol Chem 285 (2010), 22576–22591.
    • (2010) J Biol Chem , vol.285 , pp. 22576-22591
    • Jain, A.1    Lamark, T.2    Sjøttem, E.3    Larsen, K.B.4    Awuh, J.A.5    Øvervatn, A.6
  • 160
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • [160] Komatsu, M., Kurokawa, H., Waguri, S., Taguchi, K., Kobayashi, A., Ichimura, Y., et al. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat Cell Biol 12 (2010), 213–223.
    • (2010) Nat Cell Biol , vol.12 , pp. 213-223
    • Komatsu, M.1    Kurokawa, H.2    Waguri, S.3    Taguchi, K.4    Kobayashi, A.5    Ichimura, Y.6
  • 161
    • 84939787271 scopus 로고    scopus 로고
    • Transcriptional control of autophagy-lysosome function drives pancreatic cancer metabolism
    • [161] Perera, R.M., Stoykova, S., Nicolay, B.N., Ross, K.N., Fitamant, J., Boukhali, M., et al. Transcriptional control of autophagy-lysosome function drives pancreatic cancer metabolism. Nature 524 (2015), 361–365.
    • (2015) Nature , vol.524 , pp. 361-365
    • Perera, R.M.1    Stoykova, S.2    Nicolay, B.N.3    Ross, K.N.4    Fitamant, J.5    Boukhali, M.6
  • 162
    • 84934281252 scopus 로고    scopus 로고
    • p53 in survival, death and metabolic health: a lifeguard with a licence to kill
    • [162] Kruiswijk, F., Labuschagne, C.F., Vousden, K.H., p53 in survival, death and metabolic health: a lifeguard with a licence to kill. Nat Rev Mol Cell Biol 16 (2015), 393–405.
    • (2015) Nat Rev Mol Cell Biol , vol.16 , pp. 393-405
    • Kruiswijk, F.1    Labuschagne, C.F.2    Vousden, K.H.3
  • 163
    • 84918523488 scopus 로고    scopus 로고
    • Cancer metabolism and elevated O-GlcNAc in oncogenic signaling
    • [163] Ma, Z., Vosseller, K., Cancer metabolism and elevated O-GlcNAc in oncogenic signaling. J Biol Chem 289 (2014), 34457–34465.
    • (2014) J Biol Chem , vol.289 , pp. 34457-34465
    • Ma, Z.1    Vosseller, K.2
  • 164
    • 84875210462 scopus 로고    scopus 로고
    • Cardiac O-GlcNAcylation blunts autophagic signaling in the diabetic heart
    • [164] Marsh, S.A., Powell, P.C., Dell'italia, L.J., Chatham, J.C., Cardiac O-GlcNAcylation blunts autophagic signaling in the diabetic heart. Life Sci 92 (2013), 648–656.
    • (2013) Life Sci , vol.92 , pp. 648-656
    • Marsh, S.A.1    Powell, P.C.2    Dell'italia, L.J.3    Chatham, J.C.4
  • 165
    • 84925284243 scopus 로고    scopus 로고
    • O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation
    • [165] Guo, B., Liang, Q., Li, L., Hu, Z., Wu, F., Zhang, P., et al. O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation. Nat Cell Biol 16 (2014), 1215–1226.
    • (2014) Nat Cell Biol , vol.16 , pp. 1215-1226
    • Guo, B.1    Liang, Q.2    Li, L.3    Hu, Z.4    Wu, F.5    Zhang, P.6
  • 167
    • 84922783167 scopus 로고    scopus 로고
    • Glutathione and thioredoxin antioxidant pathways synergize to drive cancer initiation and progression
    • [167] Harris, I.S., Treloar, A.E., Inoue, S., Sasaki, M., Gorrini, C., Lee, K.C., et al. Glutathione and thioredoxin antioxidant pathways synergize to drive cancer initiation and progression. Cancer Cell 27 (2015), 211–222.
    • (2015) Cancer Cell , vol.27 , pp. 211-222
    • Harris, I.S.1    Treloar, A.E.2    Inoue, S.3    Sasaki, M.4    Gorrini, C.5    Lee, K.C.6
  • 168
    • 84858796263 scopus 로고    scopus 로고
    • IDH1 mutation is sufficient to establish the glioma hypermethylator phenotype
    • [168] Turcan, S., Rohle, D., Goenka, A., Walsh, L.A., Fang, F., Yilmaz, E., et al. IDH1 mutation is sufficient to establish the glioma hypermethylator phenotype. Nature 483 (2012), 479–483.
    • (2012) Nature , vol.483 , pp. 479-483
    • Turcan, S.1    Rohle, D.2    Goenka, A.3    Walsh, L.A.4    Fang, F.5    Yilmaz, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.