메뉴 건너뛰기




Volumn 33, Issue 34, 2014, Pages 4279-4285

Post-translational modifications and the Warburg effect

Author keywords

cancer metabolism; post translational modifications; the Warburg effect

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ENZYME; GLUCOSE TRANSPORTER; GLUCOSE TRANSPORTER 1; HEXOKINASE; LACTATE DEHYDROGENASE; PHOSPHOGLYCERATE MUTASE; PYRUVATE DEHYDROGENASE KINASE; PYRUVATE KINASE;

EID: 84906937144     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2013.406     Document Type: Review
Times cited : (104)

References (71)
  • 1
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg O. On the origin of cancer cells. Science 1956; 123: 309-314
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 2
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan D, Weinberg RA. Hallmarks of cancer: The next generation. Cell 2011; 144: 646-674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 3
  • 4
    • 84869077946 scopus 로고    scopus 로고
    • Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth
    • Hitosugi T, Zhou L, Elf S, Fan J, Kang HB, Seo JH et al. Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth. Cancer Cell 2012; 22: 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
  • 6
    • 80051923932 scopus 로고    scopus 로고
    • Functional genomics reveal that the serine synthesis pathway is essential in breast cancer
    • Possemato R, Marks KM, Shaul YD, Pacold ME, Kim D, Birsoy K et al. Functional genomics reveal that the serine synthesis pathway is essential in breast cancer. Nature 2011; 476: 346-350
    • (2011) Nature , vol.476 , pp. 346-350
    • Possemato, R.1    Marks, K.M.2    Shaul, Y.D.3    Pacold, M.E.4    Kim, D.5    Birsoy, K.6
  • 8
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P, Hunter T. Oncogenic kinase signalling. Nature 2001; 411: 355-365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 10
    • 0021254544 scopus 로고
    • Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro
    • Cooper JA, Esch FS, Taylor SS, Hunter T. Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro. J Biol Chem 1984; 259: 7835-7841
    • (1984) J Biol Chem , vol.259 , pp. 7835-7841
    • Cooper, J.A.1    Esch, F.S.2    Taylor, S.S.3    Hunter, T.4
  • 11
    • 0020529805 scopus 로고
    • Three glycolytic enzymes are phosphorylated at tyrosine in cells transformed by Rous sarcoma virus
    • Cooper JA, Reiss NA, Schwartz RJ, Hunter T. Three glycolytic enzymes are phosphorylated at tyrosine in cells transformed by Rous sarcoma virus. Nature 1983; 302: 218-223
    • (1983) Nature , vol.302 , pp. 218-223
    • Cooper, J.A.1    Reiss, N.A.2    Schwartz, R.J.3    Hunter, T.4
  • 12
    • 0019862081 scopus 로고
    • Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins
    • Cooper JA, Hunter T. Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins. Mol Cell Biol 1981; 1: 394-407
    • (1981) Mol Cell Biol , vol.1 , pp. 394-407
    • Cooper, J.A.1    Hunter, T.2
  • 13
    • 0036077547 scopus 로고    scopus 로고
    • Glucose transporters: Expression, regulation and cancer
    • Medina RA, Owen GI. Glucose transporters: Expression, regulation and cancer. Biol Res 2002; 35: 9-26
    • (2002) Biol Res , vol.35 , pp. 9-26
    • Medina, R.A.1    Owen, G.I.2
  • 14
    • 0033215390 scopus 로고    scopus 로고
    • Protein kinase B stimulates the translocation of GLUT4 but not GLUT1 or transferrin receptors in 3T3-L1 adipocytes by a pathway involving SNAP-23, synaptobrevin-2, and/or cellubrevin
    • Foran PG, Fletcher LM, Oatey PB, Mohammed N, Dolly JO, Tavare JM. Protein kinase B stimulates the translocation of GLUT4 but not GLUT1 or transferrin receptors in 3T3-L1 adipocytes by a pathway involving SNAP-23, synaptobrevin-2, and/or cellubrevin. J Biol Chem 1999; 274: 28087-28095
    • (1999) J Biol Chem , vol.274 , pp. 28087-28095
    • Foran, P.G.1    Fletcher, L.M.2    Oatey, P.B.3    Mohammed, N.4    Dolly, J.O.5    Tavare, J.M.6
  • 16
    • 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
    • Kohn AD, Summers SA, Birnbaum MJ, Roth RA. Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J Biol Chem 1996; 271: 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
  • 17
    • 0033556016 scopus 로고    scopus 로고
    • Akt-2 binds to Glut4-containing vesicles and phosphorylates their component proteins in response to insulin
    • Kupriyanova TA, Kandror KV. Akt-2 binds to Glut4-containing vesicles and phosphorylates their component proteins in response to insulin. J Biol Chem 1999; 274: 1458-1464
    • (1999) J Biol Chem , vol.274 , pp. 1458-1464
    • Kupriyanova, T.A.1    Kandror, K.V.2
  • 19
    • 60549111398 scopus 로고    scopus 로고
    • Is Akt the "warburg kinase"?-Akt-energy metabolism interactions and oncogenesis
    • Robey RB, Hay N. Is Akt the "Warburg kinase"?-Akt-energy metabolism interactions and oncogenesis. Sem Cancer Biol 2009; 19: 25-31
    • (2009) Sem Cancer Biol , vol.19 , pp. 25-31
    • Robey, R.B.1    Hay, N.2
  • 20
    • 0035853833 scopus 로고    scopus 로고
    • Akt and Bcl-xL promote growth factor-independent survival through distinct effects on mitochondrial physiology
    • Plas DR, Talapatra S, Edinger AL, Rathmell JC, Thompson CB. Akt and Bcl-xL promote growth factor-independent survival through distinct effects on mitochondrial physiology. J Biol Chem 2001; 276: 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
  • 21
    • 0141863388 scopus 로고    scopus 로고
    • Aktdirected glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival
    • Rathmell JC, Fox CJ, Plas DR, Hammerman PS, Cinalli RM, Thompson CB. Aktdirected glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival. Mol Cell Biol 2003; 23: 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
  • 23
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase
    • Gottlob K, Majewski N, Kennedy S, Kandel E, Robey RB, Hay N. Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. Genes Dev 2001; 15: 1406-1418
    • (2001) Genes Dev , vol.15 , pp. 1406-1418
    • Gottlob, K.1    Majewski, N.2    Kennedy, S.3    Kandel, E.4    Robey, R.B.5    Hay, N.6
  • 24
    • 39449114808 scopus 로고    scopus 로고
    • Akt mediates mitochondrial protection in cardiomyocytes through phosphorylation of mitochondrial hexokinase-II
    • Miyamoto S, Murphy AN, Brown JH. Akt mediates mitochondrial protection in cardiomyocytes through phosphorylation of mitochondrial hexokinase-II. Cell Death Diff 2008; 15: 521-529
    • (2008) Cell Death Diff , vol.15 , pp. 521-529
    • Miyamoto, S.1    Murphy, A.N.2    Brown, J.H.3
  • 25
    • 0030748651 scopus 로고    scopus 로고
    • Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades
    • Deprez J, Vertommen D, Alessi DR, Hue L, Rider MH. Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades. J Biol Chem 1997; 272: 17269-17275
    • (1997) J Biol Chem , vol.272 , pp. 17269-17275
    • Deprez, J.1    Vertommen, D.2    Alessi, D.R.3    Hue, L.4    Rider, M.H.5
  • 26
    • 84865300414 scopus 로고    scopus 로고
    • Phosphofructokinase 1 glycosylation regulates cell growth and metabolism
    • Yi W, Clark PM, Mason DE, Keenan MC, Hill C, Goddard 3rd WA et al. Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. Science 2012; 337: 975-980
    • (2012) Science , vol.337 , pp. 975-980
    • Yi, W.1    Clark, P.M.2    Mason, D.E.3    Keenan, M.C.4    Hill, C.5    Goddard III, W.A.6
  • 27
    • 0015424168 scopus 로고
    • Mechanism of the 2,3-diphosphoglycerate-dependent phosphoglycerate mutase from rabbit muscle
    • Britton HG, Clarke JB. Mechanism of the 2,3-diphosphoglycerate-dependent phosphoglycerate mutase from rabbit muscle. Biochemical J 1972; 130: 397-410
    • (1972) Biochemical J , vol.130 , pp. 397-410
    • Britton, H.G.1    Clarke, J.B.2
  • 29
    • 0014264606 scopus 로고
    • Influence of salt, substrate, and cofactor concentrations on the kinetic and mechanistic behavior of phosphoglycerate mutase
    • Grisolia S, Cleland WW. Influence of salt, substrate, and cofactor concentrations on the kinetic and mechanistic behavior of phosphoglycerate mutase. Biochemistry 1968; 7: 1115-1121
    • (1968) Biochemistry , vol.7 , pp. 1115-1121
    • Grisolia, S.1    Cleland, W.W.2
  • 30
    • 0017137853 scopus 로고
    • Rates of phosphorylation and dephosphorylation of phosphoglycerate mutase and bisphosphoglycerate synthase
    • Rose ZB, Dube S. Rates of phosphorylation and dephosphorylation of phosphoglycerate mutase and bisphosphoglycerate synthase. J Biol Chem 1976; 251: 4817-4822
    • (1976) J Biol Chem , vol.251 , pp. 4817-4822
    • Rose, Z.B.1    Dube, S.2
  • 31
    • 0016802758 scopus 로고
    • The sequence of a peptide containing the active site phosphohistidine residue of phosphoglycerate mutase from chicken breast muscle
    • Rose ZB, Hamasaki N, Dube S. The sequence of a peptide containing the active site phosphohistidine residue of phosphoglycerate mutase from chicken breast muscle. J Biol Chem 1975; 250: 7939-7942
    • (1975) J Biol Chem , vol.250 , pp. 7939-7942
    • Rose, Z.B.1    Hamasaki, N.2    Dube, S.3
  • 32
    • 33846948971 scopus 로고    scopus 로고
    • The regulation of energy generating metabolic pathways by p53
    • Corcoran CA, Huang Y, Sheikh MS. The regulation of energy generating metabolic pathways by p53. Cancer Biol Ther 2006; 5: 1610-1613
    • (2006) Cancer Biol Ther , vol.5 , pp. 1610-1613
    • Corcoran, C.A.1    Huang, Y.2    Sheikh, M.S.3
  • 34
    • 77949967131 scopus 로고    scopus 로고
    • Targeting metabolic transformation for cancer therapy
    • Tennant DA, Duran RV, Gottlieb E. Targeting metabolic transformation for cancer therapy. Nat Rev Cancer 2010; 10: 267-277
    • (2010) Nat Rev Cancer , vol.10 , pp. 267-277
    • Tennant, D.A.1    Duran, R.V.2    Gottlieb, E.3
  • 35
    • 84877781067 scopus 로고    scopus 로고
    • Tyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours by stabilizing the active conformation
    • Hitosugi T, Zhou L, Fan J, Elf S, Zhang L, Xie J et al. Tyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours by stabilizing the active conformation. Nat Commun 2013; 4: 1790
    • (2013) Nat Commun , vol.4 , pp. 1790
    • Hitosugi, T.1    Zhou, L.2    Fan, J.3    Elf, S.4    Zhang, L.5    Xie, J.6
  • 36
    • 84856742769 scopus 로고    scopus 로고
    • Regulation of glycolytic enzyme phosphoglycerate mutase-1 by Sirt1 protein-mediated deacetylation
    • Hallows WC, Yu W, Denu JM. Regulation of glycolytic enzyme phosphoglycerate mutase-1 by Sirt1 protein-mediated deacetylation. J Biol Chem 2012; 287: 3850-3858
    • (2012) J Biol Chem , vol.287 , pp. 3850-3858
    • Hallows, W.C.1    Yu, W.2    Denu, J.M.3
  • 37
    • 34250731274 scopus 로고    scopus 로고
    • Mechanistic and structural requirements for active site labeling of phosphoglycerate mutase by spiroepoxides
    • Evans MJ, Morris GM, Wu J, Olson AJ, Sorensen EJ, Cravatt BF. Mechanistic and structural requirements for active site labeling of phosphoglycerate mutase by spiroepoxides. Mol Biosyst 2007; 3: 495-506
    • (2007) Mol Biosyst , vol.3 , pp. 495-506
    • Evans, M.J.1    Morris, G.M.2    Wu, J.3    Olson, A.J.4    Sorensen, E.J.5    Cravatt, B.F.6
  • 38
    • 27144510184 scopus 로고    scopus 로고
    • Target discovery in smallmolecule cell-based screens by in situ proteome reactivity profiling
    • Evans MJ, Saghatelian A, Sorensen EJ, Cravatt BF. Target discovery in smallmolecule cell-based screens by in situ proteome reactivity profiling. Nat Biotechnol 2005; 23: 1303-1307
    • (2005) Nat Biotechnol , vol.23 , pp. 1303-1307
    • Evans, M.J.1    Saghatelian, A.2    Sorensen, E.J.3    Cravatt, B.F.4
  • 41
    • 77449160135 scopus 로고    scopus 로고
    • PKM2 tyrosine phosphorylation and glutamine metabolism signal a different view of the Warburg effect
    • Dang CV. PKM2 tyrosine phosphorylation and glutamine metabolism signal a different view of the Warburg effect. Sci Signaling 2009; 2: Pe75
    • (2009) Sci Signaling , vol.2
    • Dang, C.V.1
  • 42
    • 84862776933 scopus 로고    scopus 로고
    • Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase
    • Gao X, Wang H, Yang JJ, Liu X, Liu ZR. Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase. Mol Cell 2012; 45: 598-609
    • (2012) Mol Cell , vol.45 , pp. 598-609
    • Gao, X.1    Wang, H.2    Yang, J.J.3    Liu, X.4    Liu, Z.R.5
  • 43
    • 34547130319 scopus 로고    scopus 로고
    • Regulation of cell proliferation by interleukin-3-induced nuclear translocation of pyruvate kinase
    • Hoshino A, Hirst JA, Fujii H. Regulation of cell proliferation by interleukin-3-induced nuclear translocation of pyruvate kinase. J Biol Chem 2007; 282: 17706-17711
    • (2007) J Biol Chem , vol.282 , pp. 17706-17711
    • Hoshino, A.1    Hirst, J.A.2    Fujii, H.3
  • 44
    • 79957567239 scopus 로고    scopus 로고
    • Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1
    • Luo W, Hu H, Chang R, Zhong J, Knabel M, O'Meally R et al. Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1. Cell 2011; 145: 732-744
    • (2011) Cell , vol.145 , pp. 732-744
    • Luo, W.1    Hu, H.2    Chang, R.3    Zhong, J.4    Knabel, M.5    O'meally, R.6
  • 45
    • 33847699250 scopus 로고    scopus 로고
    • Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death
    • Stetak A, Veress R, Ovadi J, Csermely P, Keri G, Ullrich A. Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death. Cancer Res 2007; 67: 1602-1608
    • (2007) Cancer Res , vol.67 , pp. 1602-1608
    • Stetak, A.1    Veress, R.2    Ovadi, J.3    Csermely, P.4    Keri, G.5    Ullrich, A.6
  • 46
    • 84865266173 scopus 로고    scopus 로고
    • PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis
    • Yang W, Xia Y, Hawke D, Li X, Liang J, Xing D et al. PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis. Cell 2012; 150: 685-696
    • (2012) Cell , vol.150 , pp. 685-696
    • Yang, W.1    Xia, Y.2    Hawke, D.3    Li, X.4    Liang, J.5    Xing, D.6
  • 47
    • 84870598190 scopus 로고    scopus 로고
    • ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect
    • Yang W, Zheng Y, Xia Y, Ji H, Chen X, Guo F et al. ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect. Nat Cell Biol 2012; 14: 1295-1304
    • (2012) Nat Cell Biol , vol.14 , pp. 1295-1304
    • Yang, W.1    Zheng, Y.2    Xia, Y.3    Ji, H.4    Chen, X.5    Guo, F.6
  • 48
    • 82555170271 scopus 로고    scopus 로고
    • Nuclear PKM2 regulates beta-catenin transactivation upon EGFR activation
    • Yang W, Xia Y, Ji HT, Zheng YH, Liang J, Huang WH et al. Nuclear PKM2 regulates beta-catenin transactivation upon EGFR activation. Nature 2011; 480: 118-U289
    • (2011) Nature , vol.480
    • Yang, W.1    Xia, Y.2    Ji, H.T.3    Zheng, Y.H.4    Liang, J.5    Huang, W.H.6
  • 49
    • 79959371914 scopus 로고    scopus 로고
    • Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth
    • Lv L, Li D, Zhao D, Lin R, Chu Y, Zhang H et al. Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth. Mol Cell 2011; 42: 719-730
    • (2011) Mol Cell , vol.42 , pp. 719-730
    • Lv, L.1    Li, D.2    Zhao, D.3    Lin, R.4    Chu, Y.5    Zhang, H.6
  • 50
    • 82755166890 scopus 로고    scopus 로고
    • Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses
    • Anastasiou D, Poulogiannis G, Asara JM, Boxer MB, Jiang JK, Shen M et al. Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses. Science 2011; 334: 1278-1283
    • (2011) Science , vol.334 , pp. 1278-1283
    • Anastasiou, D.1    Poulogiannis, G.2    Asara, J.M.3    Boxer, M.B.4    Jiang, J.K.5    Shen, M.6
  • 53
    • 83255171153 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of lactate dehydrogenase A is important for NADH/NAD redox homeostasis in cancer cells
    • Fan J, Hitosugi T, Chung TW, Xie J, Ge Q, Gu TL et al. Tyrosine phosphorylation of lactate dehydrogenase A is important for NADH/NAD redox homeostasis in cancer cells. Mol Cell Biol 2011; 31: 4938-4950
    • (2011) Mol Cell Biol , vol.31 , pp. 4938-4950
    • Fan, J.1    Hitosugi, T.2    Chung, T.W.3    Xie, J.4    Ge, Q.5    Gu, T.L.6
  • 54
    • 84876417170 scopus 로고    scopus 로고
    • Lysine-5 acetylation negatively regulates lactate dehydrogenase a and is decreased in pancreatic cancer
    • Zhao D, Zou SW, Liu Y, Zhou X, Mo Y, Wang P et al. Lysine-5 acetylation negatively regulates lactate dehydrogenase a and is decreased in pancreatic cancer. Cancer Cell 2013; 23: 464-476
    • (2013) Cancer Cell , vol.23 , pp. 464-476
    • Zhao, D.1    Zou, S.W.2    Liu, Y.3    Zhou, X.4    Mo, Y.5    Wang, P.6
  • 55
    • 80054769188 scopus 로고    scopus 로고
    • SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity
    • Kim HS, Vassilopoulos A, Wang RH, Lahusen T, Xiao Z, Xu X et al. SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity. Cancer Cell 2011; 20: 487-499
    • (2011) Cancer Cell , vol.20 , pp. 487-499
    • Kim, H.S.1    Vassilopoulos, A.2    Wang, R.H.3    Lahusen, T.4    Xiao, Z.5    Xu, X.6
  • 56
    • 0035980919 scopus 로고    scopus 로고
    • Regulation of mammalian pyruvate dehydrogenase complex by phosphorylation: Complexity of multiple phosphorylation sites and kinases
    • Patel MS, Korotchkina LG. Regulation of mammalian pyruvate dehydrogenase complex by phosphorylation: Complexity of multiple phosphorylation sites and kinases. Exp Mol Med 2001; 33: 191-197
    • (2001) Exp Mol Med , vol.33 , pp. 191-197
    • Patel, M.S.1    Korotchkina, L.G.2
  • 57
    • 34247131735 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase regulatory mechanisms and inhibition in treating diabetes, heart ischemia, and cancer
    • Roche TE, Hiromasa Y. Pyruvate dehydrogenase kinase regulatory mechanisms and inhibition in treating diabetes, heart ischemia, and cancer. Cell Mol Life Sci 2007; 64: 830-849
    • (2007) Cell Mol Life Sci , vol.64 , pp. 830-849
    • Roche, T.E.1    Hiromasa, Y.2
  • 58
    • 84255162057 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of mitochondrial pyruvate dehydrogenase kinase 1 is important for cancer metabolism
    • Hitosugi T, Fan J, Chung TW, Lythgoe K, Wang X, Xie J et al. Tyrosine phosphorylation of mitochondrial pyruvate dehydrogenase kinase 1 is important for cancer metabolism. Mol Cell 2011; 44: 864-877
    • (2011) Mol Cell , vol.44 , pp. 864-877
    • Hitosugi, T.1    Fan, J.2    Chung, T.W.3    Lythgoe, K.4    Wang, X.5    Xie, J.6
  • 59
    • 33846002728 scopus 로고    scopus 로고
    • A mitochondria-K channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth
    • Bonnet S, Archer SL, Allalunis-Turner J, Haromy A, Beaulieu C, Thompson R et al. A mitochondria-K channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth. Cancer Cell 2007; 11: 37-51
    • (2007) Cancer Cell , vol.11 , pp. 37-51
    • Bonnet, S.1    Archer, S.L.2    Allalunis-Turner, J.3    Haromy, A.4    Beaulieu, C.5    Thompson, R.6
  • 62
    • 77951209414 scopus 로고    scopus 로고
    • The role of p53 in glucose metabolism
    • Cheung EC, Vousden KH. The role of p53 in glucose metabolism. Curr Opi Cell Biol 2010; 22: 186-191
    • (2010) Curr Opi Cell Biol , vol.22 , pp. 186-191
    • Cheung, E.C.1    Vousden, K.H.2
  • 63
    • 34547580590 scopus 로고    scopus 로고
    • HIF and c-Myc: Sibling rivals for control of cancer cell metabolism and proliferation
    • Gordan JD, Thompson CB, Simon MC. HIF and c-Myc: Sibling rivals for control of cancer cell metabolism and proliferation. Cancer Cell 2007; 12: 108-113
    • (2007) Cancer Cell , vol.12 , pp. 108-113
    • Gordan, J.D.1    Thompson, C.B.2    Simon, M.C.3
  • 65
    • 44449147036 scopus 로고    scopus 로고
    • Tumor cell metabolism: Cancer's Achilles' heel
    • Kroemer G, Pouyssegur J. Tumor cell metabolism: Cancer's Achilles' heel. Cancer Cell 2008; 13: 472-482
    • (2008) Cancer Cell , vol.13 , pp. 472-482
    • Kroemer, G.1    Pouyssegur, J.2
  • 66
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1
    • Semenza GL, Roth PH, Fang HM, Wang GL. Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1. J Biol Chem 1994; 269: 23757-23763
    • (1994) J Biol Chem , vol.269 , pp. 23757-23763
    • Semenza, G.L.1    Roth, P.H.2    Fang, H.M.3    Wang, G.L.4
  • 68
    • 22144477159 scopus 로고    scopus 로고
    • S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
    • Hara MR, Agrawal N, Kim SF, Cascio MB, Fujimuro M, Ozeki Y et al. S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol 2005; 7: 665-674
    • (2005) Nat Cell Biol , vol.7 , pp. 665-674
    • Hara, M.R.1    Agrawal, N.2    Kim, S.F.3    Cascio, M.B.4    Fujimuro, M.5    Ozeki, Y.6
  • 69
    • 0029854903 scopus 로고    scopus 로고
    • Recombinant human phenylalanine hydroxylase is a substrate for the ubiquitin-conjugating enzyme system
    • Doskeland AP, Flatmark T. Recombinant human phenylalanine hydroxylase is a substrate for the ubiquitin-conjugating enzyme system. Biochem J 1996; 319(Pt 3): 941-945
    • (1996) Biochem J , vol.319 , Issue.PART 3 , pp. 941-945
    • Doskeland, A.P.1    Flatmark, T.2
  • 71
    • 33750097998 scopus 로고    scopus 로고
    • The use of mass spectrometry for the proteomic analysis of glycosylation
    • Morelle W, Canis K, Chirat F, Faid V, Michalski JC. The use of mass spectrometry for the proteomic analysis of glycosylation. Proteomics 2006; 6: 3993-4015
    • (2006) Proteomics , vol.6 , pp. 3993-4015
    • Morelle, W.1    Canis, K.2    Chirat, F.3    Faid, V.4    Michalski, J.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.