메뉴 건너뛰기




Volumn 53, Issue 3, 2012, Pages 421-436

The pentose phosphate pathway: An antioxidant defense and a crossroad in tumor cell fate

Author keywords

Free radicals; Glucose 6 phosphate dehydrogenase; Oxidative stress; Pentose phosphate pathway; Tumor metabolism

Indexed keywords

ACETYLCYSTEINE; AMOSITE; ANGIOTENSIN II; ANTIOXIDANT; CROCIDOLITE; DOUBLE STRANDED DNA; DOXORUBICIN; GLUCOSE 6 PHOSPHATASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE; GUANINE NUCLEOTIDE BINDING PROTEIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; IMATINIB; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INCYCLINIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NITRIC OXIDE; PROTEIN P53; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; RIBOSE 5 PHOSPHATE; TRANSKETOLASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 84863486244     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.05.006     Document Type: Review
Times cited : (324)

References (174)
  • 1
    • 84871027415 scopus 로고
    • A death in a case of malarial fever undergoing treatment with plasmochin compound
    • Boston: United Fruit Co.
    • Cordes, W. A death in a case of malarial fever undergoing treatment with plasmochin compound. In: Annual Report, United Fruit Company, Medical Department, vol. 15. Boston: United Fruit Co.; 1926:72-73.
    • (1926) Annual Report, United Fruit Company, Medical Department , vol.15 , pp. 72-73
    • Cordes, W.1
  • 2
    • 0001355595 scopus 로고
    • The haemolytic effect of primaquine. VII. Biochemical studies of drug-sensitive erythrocytes
    • E. Beutler, R.J. Dern, and A.S. Alving The haemolytic effect of primaquine. VII. Biochemical studies of drug-sensitive erythrocytes J. Lab. Clin. Med. 45 1955 286 295
    • (1955) J. Lab. Clin. Med. , vol.45 , pp. 286-295
    • Beutler, E.1    Dern, R.J.2    Alving, A.S.3
  • 3
    • 0000616920 scopus 로고
    • Enzymatic deficiency in primaquine-sensitive erythrocytes
    • P.E. Carson, C.L. Flanagan, C.E. Ickes, and A.S. Alving Enzymatic deficiency in primaquine-sensitive erythrocytes Science 124 1956 484 485
    • (1956) Science , vol.124 , pp. 484-485
    • Carson, P.E.1    Flanagan, C.L.2    Ickes, C.E.3    Alving, A.S.4
  • 4
    • 0014483527 scopus 로고
    • Drug-induced haemolytic anemia
    • E. Beutler Drug-induced haemolytic anemia Pharm. Rev 21 1969 73 103
    • (1969) Pharm. Rev , vol.21 , pp. 73-103
    • Beutler, E.1
  • 5
    • 0001585429 scopus 로고    scopus 로고
    • Glucose 6-phosphate dehydrogenase deficiency
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, 8th ed McGraw-Hill Columbus
    • L. Luzzatto, A. Metha, and T. Vulliamy Glucose 6-phosphate dehydrogenase deficiency C.R. Scriver, A.L. Beaudet, W.S. Sly, The Metabolic and Molecular Bases of Inherited Disease 8th ed 2001 McGraw-Hill Columbus 4517 4553
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 4517-4553
    • Luzzatto, L.1    Metha, A.2    Vulliamy, T.3
  • 6
    • 22744434002 scopus 로고    scopus 로고
    • Transaldolase is part of a supramolecular complex containing glucose-6-phosphate dehydrogenase in human neutrophils that undergoes retrograde trafficking during pregnancy
    • DOI 10.1016/j.metabol.2005.03.005, PII S0026049505001289
    • J.B. Huang, J. Espinoza, R. Romero, and H.R. Petty Transaldolase is part of a supramolecular complex containing glucose-6-phosphate dehydrogenase in human neutrophils that undergoes retrograde trafficking during pregnancy Metabolism 54 2005 1027 1033 (Pubitemid 41033103)
    • (2005) Metabolism: Clinical and Experimental , vol.54 , Issue.8 , pp. 1027-1033
    • Huang, J.-B.1    Espinoza, J.2    Romero, R.3    Petty, H.R.4
  • 7
    • 0037795745 scopus 로고    scopus 로고
    • The oxidative pentose phosphate pathway: Structure and organisation
    • DOI 10.1016/S1369-5266(03)00039-6
    • N.J. Kruger, and A. von Schaewen The oxidative pentose phosphate pathway: structure and organisation Curr. Opin. Plant Biol. 6 2003 236 246 (Pubitemid 36704509)
    • (2003) Current Opinion in Plant Biology , vol.6 , Issue.3 , pp. 236-246
    • Kruger, N.J.1    Von Schaewen, A.2
  • 8
    • 84956662394 scopus 로고    scopus 로고
    • Carbon metabolism of enterobacterial human pathogens growing in epithelial colorectal adenocarcinoma (Caco-2) cells
    • A. Gotz, E. Eylert, W. Eisenreich, and W. Goebel Carbon metabolism of enterobacterial human pathogens growing in epithelial colorectal adenocarcinoma (Caco-2) cells PLoS One 5 2010 e10586
    • (2010) PLoS One , vol.5 , pp. 10586
    • Gotz, A.1    Eylert, E.2    Eisenreich, W.3    Goebel, W.4
  • 9
    • 0033372008 scopus 로고    scopus 로고
    • Activity and metabolic roles of the pentose phosphate cycle in several rat tissues
    • H. Cabezas, R.R. Raposo, and E. Meléndez-Hevia Activity and metabolic roles of the pentose phosphate cycle in several rat tissues Mol. Cell. Biochem. 201 1999 57 63 (Pubitemid 30019365)
    • (1999) Molecular and Cellular Biochemistry , vol.201 , Issue.1-2 , pp. 57-63
    • Cabezas, H.1    Raposo, R.R.2    Melendez-Hevia, E.3
  • 10
  • 11
    • 37549026846 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency
    • M.D. Cappellini, and G. Fiorelli Glucose-6-phosphate dehydrogenase deficiency Lancet 371 2008 64 74
    • (2008) Lancet , vol.371 , pp. 64-74
    • Cappellini, M.D.1    Fiorelli, G.2
  • 12
    • 0034654509 scopus 로고    scopus 로고
    • + molecule and provides insights into enzyme deficiency
    • DOI 10.1016/S0969-2126(00)00104-0
    • S.W. Au, S. Gover, V.M. Lam, and M.J. Adams Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP() molecule and provides insights into enzyme deficiency Structure 8 2000 293 303 (Pubitemid 30148695)
    • (2000) Structure , vol.8 , Issue.3 , pp. 293-303
    • Au, S.W.N.1    Gover, S.2    Lam, V.M.S.3    Adams, M.J.4
  • 14
    • 34547702206 scopus 로고    scopus 로고
    • G6PD deficiency: The genotype-phenotype association
    • DOI 10.1016/j.blre.2007.05.002, PII S0268960X0700032X
    • P. Mason, J.M. Bautista, and F. Gilsanz G6PD deficiency: the genotype-phenotype association Bloods Rev 21 2007 267 283 (Pubitemid 47212602)
    • (2007) Blood Reviews , vol.21 , Issue.5 , pp. 267-283
    • Mason, P.J.1    Bautista, J.M.2    Gilsanz, F.3
  • 15
    • 0016043671 scopus 로고
    • Regulation of the pentose phosphate cycle
    • L.V. Eggleston, and H.A. Krebs Regulation of the pentose phosphate cycle Biochem. J. 138 1974 425 435
    • (1974) Biochem. J. , vol.138 , pp. 425-435
    • Eggleston, L.V.1    Krebs, H.A.2
  • 16
    • 33845609248 scopus 로고    scopus 로고
    • Irreversible inhibition of glucose-6-phosphate dehydrogenase by the coenzyme A conjugate of ketoprofen: A key to oxidative stress induced by non-steroidal anti-inflammatory drugs?
    • DOI 10.1016/j.bcp.2006.09.026, PII S0006295206006150
    • C. Asensio, N. Levoin, C. Guillaume, M.J. Guerquin, K. Rouguieg, F. Chrétien, Y. Chapleur, P. Netter, A. Minn, and F. Lapicque Irreversible inhibition of glucose-6-phosphate dehydrogenase by the coenzyme A conjugate of ketoprofen: a key to oxidative stress induced by non-steroidal anti-inflammatory drugs? Biochem Pharmacol 73 2007 405 416 (Pubitemid 44958365)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.3 , pp. 405-416
    • Asensio, C.1    Levoin, N.2    Guillaume, C.3    Guerquin, M.-J.4    Rouguieg, K.5    Chretien, F.6    Chapleur, Y.7    Netter, P.8    Minn, A.9    Lapicque, F.10
  • 17
    • 0037163115 scopus 로고    scopus 로고
    • Inhibition of the splicing of glucose-6-phosphate dehydrogenase precursor mRNA by polyunsaturated fatty acids
    • DOI 10.1074/jbc.M203196200
    • H. Tao, W. Szeszel-Fedorowicz, B. Amir-Ahmady, M.A. Gibson, L.P. Stabile, and L.M. Salati Inhibition of the splicing of glucose-6-phosphate dehydrogenase precursor mRNA by polyunsaturated fatty acids J. Biol. Chem. 277 2002 31270 31278 (Pubitemid 34970836)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 31270-31278
    • Tao, H.1    Szeszel-Fedorowicz, W.2    Amir-Ahmady, B.3    Gibson, M.A.4    Stabile, L.P.5    Salati, L.M.6
  • 18
    • 68949154433 scopus 로고    scopus 로고
    • A role for AMPK in the inhibition of glucose-6-phosphate dehydrogenase by polyunsaturated fatty acids
    • A.B. Kohan, I. Talukdar, C.M. Walsh, and L.M. Salati A role for AMPK in the inhibition of glucose-6-phosphate dehydrogenase by polyunsaturated fatty acids Biochem. Biophys. Res. Commun. 388 2009 117 121
    • (2009) Biochem. Biophys. Res. Commun. , vol.388 , pp. 117-121
    • Kohan, A.B.1    Talukdar, I.2    Walsh, C.M.3    Salati, L.M.4
  • 19
    • 33644860769 scopus 로고    scopus 로고
    • Evidence that the 11 β-hydroxysteroid dehydrogenase (11 β-HSD1) is regulated by pentose pathway flux: Studies in rat adipocytes and microsomes
    • DOI 10.1074/jbc.M506026200
    • K.L. McCormick, X. Wang, and G.J. Mick Evidence that the 11β-hydroxysteroid dehydrogenase (11β-HSD1) is regulated by pentose pathway flux J. Biol. Chem. 281 2006 341 347 (Pubitemid 43671194)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 341-347
    • McCormick, K.L.1    Wang, X.2    Mick, G.J.3
  • 20
    • 0036569998 scopus 로고    scopus 로고
    • Crocidolite asbestos inhibits pentose phosphate oxidative pathway and glucose 6-phosphate dehydrogenase activity in human lung epithelial cells
    • DOI 10.1016/S0891-5849(02)00800-6, PII S0891584902008006
    • C. Riganti, E. Aldieri, L. Bergandi, I. Fenoglio, C. Costamagna, B. Fubini, A. Bosia, and D. Ghigo Crocidolite asbestos inhibits pentose phosphate oxidative pathway and glucose 6-phosphate dehydrogenase activity in human lung epithelial cells Free Radic. Biol. Med. 32 2002 938 949 (Pubitemid 34439265)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 938-949
    • Riganti, C.1    Aldieri, E.2    Bergandi, L.3    Fenoglio, I.4    Costamagna, C.5    Fubini, B.6    Bosia, A.7    Ghigo, D.8
  • 24
    • 79955476581 scopus 로고    scopus 로고
    • The toxic effect of fluoride on MG-63 osteoblast cells is also dependent on the production of nitric oxide
    • L. Bergandi, V. Aina, G. Malavasi, C. Morterra, and D. Ghigo The toxic effect of fluoride on MG-63 osteoblast cells is also dependent on the production of nitric oxide Chem. Biol. Interact. 190 2011 179 186
    • (2011) Chem. Biol. Interact. , vol.190 , pp. 179-186
    • Bergandi, L.1    Aina, V.2    Malavasi, G.3    Morterra, C.4    Ghigo, D.5
  • 25
    • 0038530446 scopus 로고    scopus 로고
    • Induction of glucose-6-phosphate dehydrogenase by lipopolysaccharide contributes to preventing nitric oxide-mediated glutathione depletion in cultured rat astrocytes
    • DOI 10.1046/j.1471-4159.1999.721750.x
    • P. Garcìa-Nogales, A. Almeida, E. Fernàndez, J.M. Medina, and J.P. Bolanos Induction of glucose-6-phosphate dehydrogenase by lipopolysaccharide contributes to preventing nitric oxide-mediated glutathione depletion in cultured rat astrocytes J. Neurochem. 72 1999 1750 1758 (Pubitemid 29140853)
    • (1999) Journal of Neurochemistry , vol.72 , Issue.4 , pp. 1750-1758
    • Garcia-Nogales, P.1    Almeida, A.2    Fernandez, E.3    Medina, J.M.4    Bolanos, J.P.5
  • 27
    • 28844478772 scopus 로고    scopus 로고
    • Arachidonic acid inhibits the insulin induction of glucose-6-phosphate dehydrogenase via p38 MAP kinase
    • DOI 10.1074/jbc.M505531200
    • I. Talukdar, W. Szeszel-Fedorowicz, and L.M. Salati Arachidonic acid inhibits the insulin induction of glucose-6-phosphate dehydrogenase via p38 MAP kinase J. Biol. Chem. 280 2005 40660 40667 (Pubitemid 41780557)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40660-40667
    • Talukdar, I.1    Szeszel-Fedorowicz, W.2    Salati, L.M.3
  • 28
    • 67349123432 scopus 로고    scopus 로고
    • Synergistic activation of glucose-6-phosphate dehydrogenase and NAD(P)H oxidase by Src kinase elevates superoxide in type 2 diabetic, Zucker fa/fa, rat liver
    • R.S. Gupte, B.C. Floyd, M. Kozicky, S. George, Z.I. Ungvari, V. Neito, M.S. Wolin, and S.A. Gupte Synergistic activation of glucose-6-phosphate dehydrogenase and NAD(P)H oxidase by Src kinase elevates superoxide in type 2 diabetic, Zucker fa/fa, rat liver Free Radic. Biol. Med. 47 2009 219 228
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 219-228
    • Gupte, R.S.1    Floyd, B.C.2    Kozicky, M.3    George, S.4    Ungvari, Z.I.5    Neito, V.6    Wolin, M.S.7    Gupte, S.A.8
  • 29
    • 0033924228 scopus 로고    scopus 로고
    • Stimulation of the pentose phosphate pathway and glutathione levels by dehydroascorbate, the oxidized form of vitamin C
    • F. Puskas, P. Gergely Jr., K. Banki, and A. Perl Stimulation of the pentose phosphate pathway and glutathione levels by dehydroascorbate, the oxidized form of vitamin C FASEB J. 14 2000 1352 1361 (Pubitemid 30439744)
    • (2000) FASEB Journal , vol.14 , Issue.10 , pp. 1352-1361
    • Puskas, F.1    Gergely, P.2    Banki, K.3    Perl, A.4
  • 30
    • 3042547565 scopus 로고    scopus 로고
    • Induction of the glucose-6-phosphate dehydrogenase gene expression by chronic hypoxia in PC12 cells
    • DOI 10.1016/j.febslet.2004.06.004, PII S0014579304007148
    • L. Gao, R. Mejìas, M. Echevarrìa, and J. Lòpez-Barneo Induction of the glucose-6-phosphate dehydrogenase gene expression by chronic hypoxia in PC12 cells FEBS Lett 569 2004 256 260 (Pubitemid 38844628)
    • (2004) FEBS Letters , vol.569 , Issue.1-3 , pp. 256-260
    • Gao, L.1    Mejias, R.2    Echevarria, M.3    Lopez-Barneo, J.4
  • 31
    • 77952756102 scopus 로고    scopus 로고
    • Targeting the pentose phosphate pathway in syndrome X related cardiovascular complications
    • S.A. Gupte Targeting the pentose phosphate pathway in syndrome X related cardiovascular complications Drug Dev. Res 71 2010 161 167
    • (2010) Drug Dev. Res , vol.71 , pp. 161-167
    • Gupte, S.A.1
  • 34
    • 1842343256 scopus 로고
    • The distribution of C14 in the hexose phosphates and the effect of recycling in the pentose cycle
    • H.G. Wood, and J. Katz The distribution of C14 in the hexose phosphates and the effect of recycling in the pentose cycle J. Biol. Chem 233 1958 1279 1282
    • (1958) J. Biol. Chem , vol.233 , pp. 1279-1282
    • Wood, H.G.1    Katz, J.2
  • 35
    • 0020538243 scopus 로고
    • Non-oxidative synthesis of pentose 5-phosphate from hexose 6-phosphate and triose phosphate by the L-type pentose pathway
    • DOI 10.1016/0020-711X(83)90152-0
    • J.F. Williams, and P.F. Blackmore Non-oxidative synthesis of pentose 5-phosphate from hexose 6-phosphate and triose phosphate by the L-type pentose pathway Int. J. Biochem 15 1983 797 816 (Pubitemid 13105189)
    • (1983) International Journal of Biochemistry , vol.15 , Issue.6 , pp. 797-816
    • Williams, J.F.1    Blackmore, P.F.2
  • 38
    • 63049112606 scopus 로고    scopus 로고
    • Transaldolase: From biochemistry to human disease
    • A.K. Samland, and G.A. Sprenger Transaldolase: from biochemistry to human disease Int. J. Biochem. Cell Biol. 41 2009 1482 1494
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1482-1494
    • Samland, A.K.1    Sprenger, G.A.2
  • 39
    • 1842530284 scopus 로고    scopus 로고
    • ZNF143 Mediates Basal and Tissue-specific Expression of Human Transaldolase
    • DOI 10.1074/jbc.M307039200
    • C.E. Grossman, Y. Qian, K. Banki, and A. Perl ZNF143 mediates basal and tissue-specific expression of human transaldolase J. Biol. Chem. 279 2004 12190 12205 (Pubitemid 38445784)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12190-12205
    • Grossman, C.E.1    Qian, Y.2    Banki, K.3    Perl, A.4
  • 40
    • 12644275745 scopus 로고    scopus 로고
    • Glutathione levels and sensitivity to apoptosis are regulated by changes in transaldolase expression
    • DOI 10.1074/jbc.271.51.32994
    • K. Banki, E. Hutter, E. Colombo, N.J. Gonchoroff, and A. Perl Glutathione levels and sensitivity to apoptosis are regulated by changes in transaldolase expression J. Biol. Chem. 271 1996 32994 33001 (Pubitemid 27008736)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.51 , pp. 32994-33001
    • Banki, K.1    Hutter, E.2    Colombo, E.3    Gonchoroff, N.J.4    Perl, A.5
  • 41
    • 0028786549 scopus 로고
    • Purification and characterization of a novel xylulose 5-phosphate-activated protein phosphatase catalyzing dephosphorylation of fructose-6-phosphate, 2-kinase:fructose-2,6-bisphosphatase
    • M. Nishimura, and K. Uyeda Purification and characterization of a novel xylulose 5-phosphate-activated protein phosphatase catalyzing dephosphorylation of fructose-6-phosphate, 2-kinase:fructose-2,6-bisphosphatase J. Biol. Chem 270 1995 26341 26346
    • (1995) J. Biol. Chem , vol.270 , pp. 26341-26346
    • Nishimura, M.1    Uyeda, K.2
  • 42
    • 33746536677 scopus 로고    scopus 로고
    • Carbohydrate response element binding protein, ChREBP, a transcription factor coupling hepatic glucose utilization and lipid synthesis
    • DOI 10.1016/j.cmet.2006.06.008, PII S1550413106002385
    • K. Uyeda, and J.J. Repa Carbohydrate response element binding protein, ChREBP, a transcription factor coupling hepatic glucose utilization and lipid synthesis Cell Metab 4 2006 107 110 (Pubitemid 44138720)
    • (2006) Cell Metabolism , vol.4 , Issue.2 , pp. 107-110
    • Uyeda, K.1    Repa, J.J.2
  • 43
    • 44649108165 scopus 로고    scopus 로고
    • The role of glucose metabolism and glucose-associated signalling in cancer
    • R. Wittig, and J.F. Coy The role of glucose metabolism and glucose-associated signalling in cancer Perspect. Med. Chem. 1 2007 64 82
    • (2007) Perspect. Med. Chem. , vol.1 , pp. 64-82
    • Wittig, R.1    Coy, J.F.2
  • 47
    • 77949267064 scopus 로고    scopus 로고
    • Glycolytic network restructuring integral to the energetics of embryonic stem cell cardiac differentiation
    • S. Chung, D. Kent Arrell, R.S. Faustino, A. Terzic, and P.P. Dzeja Glycolytic network restructuring integral to the energetics of embryonic stem cell cardiac differentiation J. Mol. Cell. Cardiol. 48 2010 725 734
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 725-734
    • Chung, S.1    Kent Arrell, D.2    Faustino, R.S.3    Terzic, A.4    Dzeja, P.P.5
  • 49
    • 22144461029 scopus 로고    scopus 로고
    • Glucose-6 phosphate dehydrogenase deficiency decreases the vascular response to angiotensin II
    • DOI 10.1161/CIRCULATIONAHA.104.499095
    • R. Matsui, S. Xu, K.A. Maitland, A. Hayes, J.A. Leopold, D.E. Handy, J. Loscalzo, and R.A. Cohen Glucose-6 phosphate dehydrogenase deficiency decreases the vascular response to angiotensin II Circulation 112 2005 257 263 (Pubitemid 40982309)
    • (2005) Circulation , vol.112 , Issue.2 , pp. 257-263
    • Matsui, R.1    Xu, S.2    Maitland, K.A.3    Hayes, A.4    Leopold, J.A.5    Handy, D.E.6    Loscalzo, J.7    Cohen, R.A.8
  • 51
    • 1542358824 scopus 로고    scopus 로고
    • Inhibition of the pentose phosphate pathway decreases ischemia-reperfusion- induced creatine kinase release in the heart
    • DOI 10.1016/j.cardiores.2004.01.010, PII S0008636304000173
    • C.J. Zuurbier, O. Eerbeek, P.T. Goedhart, E.A. Struys, N.M. Verhoeven, C. Jakobs, and C. Ince Inhibition of the pentose phosphate pathway decreases ischemia-reperfusion-induced creatine kinase release in the heart Cardiovasc. Res. 62 2004 145 153 (Pubitemid 38326820)
    • (2004) Cardiovascular Research , vol.62 , Issue.1 , pp. 145-153
    • Zuurbier, C.J.1    Eerbeek, O.2    Goedhart, P.T.3    Struys, E.A.4    Verhoeven, N.M.5    Jakobs, C.6    Ince, C.7
  • 53
    • 4544375706 scopus 로고    scopus 로고
    • Functional significance of the pentose phosphate pathway and glutathione reductase in the antioxidant defenses of human sperm
    • DOI 10.1095/biolreprod.104.028407
    • A.C. Williams, and W.C.L. Ford Functional significance of the pentose phosphate pathway and glutathione reductase in the antioxidant defenses of human sperm Biol. Reprod 71 2004 1309 1316 (Pubitemid 39249817)
    • (2004) Biology of Reproduction , vol.71 , Issue.4 , pp. 1309-1316
    • Williams, A.C.1    Ford, W.C.L.2
  • 56
    • 33845596741 scopus 로고    scopus 로고
    • Increase in glucose-6-phosphate dehydrogenase in adipocytes stimulates oxidative stress and inflammatory signals
    • DOI 10.2337/db05-1570
    • J. Park, S.S. Choe, A.H. Choi, K.H. Kim, M.J. Yoon, T. Suganami, Y. Ogawa, and J.B. Kim Increase in glucose-6-phosphate dehydrogenase in adipocytes stimulates oxidative stress and inflammatory signals Diabetes 55 2006 2939 2949 (Pubitemid 44929428)
    • (2006) Diabetes , vol.55 , Issue.11 , pp. 2939-2949
    • Park, J.1    Sung, S.C.2    Choi, A.H.3    Kang, H.K.4    Myeong, J.Y.5    Suganami, T.6    Ogawa, Y.7    Jae, B.K.8
  • 57
    • 67650095384 scopus 로고    scopus 로고
    • Superoxide production by NAD(P)H oxidase and mitochondria is increased in genetically obese and hyperglycemic rat heart and aorta before the development of cardiac dysfunction: The role of glucose-6-phosphate dehydrogenase-derived NADPH
    • S. Serpillon, B.C. Floyd, R.S. Gupte, S. George, M. Kozicky, V. Neito, F. Recchia, W. Stanley, M.S. Wolin, and S.A. Gupte Superoxide production by NAD(P)H oxidase and mitochondria is increased in genetically obese and hyperglycemic rat heart and aorta before the development of cardiac dysfunction: the role of glucose-6-phosphate dehydrogenase-derived NADPH Am. J. Physiol. Heart Circ. Physiol 297 2009 H153 H162
    • (2009) Am. J. Physiol. Heart Circ. Physiol , vol.297
    • Serpillon, S.1    Floyd, B.C.2    Gupte, R.S.3    George, S.4    Kozicky, M.5    Neito, V.6    Recchia, F.7    Stanley, W.8    Wolin, M.S.9    Gupte, S.A.10
  • 60
    • 0021248051 scopus 로고    scopus 로고
    • The pathways of glutamate and glutamine oxidation by tumor cell mitochondria: Role of mitochondrial NAD(P)-dependent malic enzyme
    • R.W. Moreadith, and A.L. Lehninger The pathways of glutamate and glutamine oxidation by tumor cell mitochondria: role of mitochondrial NAD(P)-dependent malic enzyme J. Biol. Chem 259 2004 6215 6221
    • (2004) J. Biol. Chem , vol.259 , pp. 6215-6221
    • Moreadith, R.W.1    Lehninger, A.L.2
  • 61
    • 79960221714 scopus 로고    scopus 로고
    • Oxidative stress, inflammation and carcinogenesis are controlled through the pentose phosphate pathway by transaldolase
    • A. Perl, R. Hanczko, T. Telarico, Z. Oaks, and S. Landas Oxidative stress, inflammation and carcinogenesis are controlled through the pentose phosphate pathway by transaldolase Trends Mol. Med. 17 2011 395 403
    • (2011) Trends Mol. Med. , vol.17 , pp. 395-403
    • Perl, A.1    Hanczko, R.2    Telarico, T.3    Oaks, Z.4    Landas, S.5
  • 64
    • 1842592038 scopus 로고    scopus 로고
    • Ribose-5-Phosphate Isomerase Deficiency: New Inborn Error in the Pentose Phosphate Pathway Associated with a Slowly Progressive Leukoencephalopathy
    • DOI 10.1086/383204
    • J.H.J. Huck, N.M. Verhoeven, E.A. Struys, G.S. Salomons, C. Jakobs, and M.S. van der Knaap Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy Am. J. Hum. Genet. 74 2004 745 751 (Pubitemid 38420104)
    • (2004) American Journal of Human Genetics , vol.74 , Issue.4 , pp. 745-751
    • Huck, J.H.J.1    Verhoeven, N.M.2    Struys, E.A.3    Salomons, G.S.4    Jakobs, C.5    Van Der Knaap, M.S.6
  • 65
    • 29144504313 scopus 로고    scopus 로고
    • + T cell-mediated HLA-A*0201-restricted cytotoxicity to transaldolase peptide 168-176 in patients with multiple sclerosis
    • B. Niland, K. Banki, W.E. Biddison, and A. Perl CD8 T cell-mediated HLA-A0201-restricted cytotoxicity to transaldolase peptide 168-176 in patients with multiple sclerosis J. Immunol. 175 2005 8365 8378 (Pubitemid 41798403)
    • (2005) Journal of Immunology , vol.175 , Issue.12 , pp. 8365-8378
    • Niland, B.1    Banki, K.2    Biddison, W.E.3    Perl, A.4
  • 66
    • 23344432659 scopus 로고    scopus 로고
    • Cellular mucosal defense during Helicobocter pylori infection: A review of the role of glutathione and the oxidative pentose pathway
    • DOI 10.1111/j.1523-5378.2005.00327.x
    • G.M. Matthews, and R.N. Butler Cellular mucosal defence during Helicobacter pylori infection: a review of the role of glutathione and the oxidative pentose pathway Helicobacter 10 2005 298 306 (Pubitemid 41104968)
    • (2005) Helicobacter , vol.10 , Issue.4 , pp. 298-306
    • Matthews, G.M.1    Butler, R.N.2
  • 70
    • 0031032145 scopus 로고    scopus 로고
    • The pentose phosphate pathway and parasitic protozoa
    • DOI 10.1016/S0169-4758(96)10075-2
    • M.P. Barrett The pentose phosphate pathway and parasitic protozoa Parasitol. Today 13 1997 11 16 (Pubitemid 27072541)
    • (1997) Parasitology Today , vol.13 , Issue.1 , pp. 11-16
    • Barrett, M.P.1
  • 71
    • 33846690105 scopus 로고    scopus 로고
    • Trypanosoma cruzi strains, Tulahuen 2 and Y, besides the difference in resistance to oxidative stress, display differential glucose-6-phosphate and 6-phosphogluconate dehydrogenases activities
    • DOI 10.1016/j.actatropica.2006.12.001, PII S0001706X06002452
    • A.A. Mielniczki-Pereira, C.M. Chiavegatto, J.A. Lopez, W. Colli, M.J.M. Alves, and F.R. Gadelha Trypanosoma cruzi strains, Tulahuen 2 and Y, besides the difference in resistance to oxidative stress, display differential glucose-6-phosphate and 6-phosphogluconate dehydrogenases activities Acta Trop. 101 2007 54 60 (Pubitemid 46198791)
    • (2007) Acta Tropica , vol.101 , Issue.1 , pp. 54-60
    • Mielniczki-Pereira, A.A.1    Chiavegatto, C.M.2    Lopez, J.A.3    Colli, W.4    Alves, M.J.M.5    Gadelha, F.R.6
  • 72
    • 77954217194 scopus 로고    scopus 로고
    • 16-Bromoepiandrosterone, an activator of the mammalian immune system, inhibits glucose 6-phosphate dehydrogenase from Trypanosoma cruzi and is toxic to these parasites grown in culture
    • A.T. Cordeiro, and O.H. Thiemann 16-Bromoepiandrosterone, an activator of the mammalian immune system, inhibits glucose 6-phosphate dehydrogenase from Trypanosoma cruzi and is toxic to these parasites grown in culture Bioorg. Med. Chem 18 2010 4762 4768
    • (2010) Bioorg. Med. Chem , vol.18 , pp. 4762-4768
    • Cordeiro, A.T.1    Thiemann, O.H.2
  • 73
    • 79957693495 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: A unique bifunctional enzyme from Plasmodium falciparum
    • E. Jortzik, B. Mailu, J. Preuss, M. Fischer, L. Bode, S. Rahlfs, and K. Becker Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: a unique bifunctional enzyme from Plasmodium falciparum Biochem. J. 436 2011 641 650
    • (2011) Biochem. J. , vol.436 , pp. 641-650
    • Jortzik, E.1    Mailu, B.2    Preuss, J.3    Fischer, M.4    Bode, L.5    Rahlfs, S.6    Becker, K.7
  • 75
    • 0028362335 scopus 로고
    • Glucose-6-phosphate dehydrogenase gene expression in fetal hepatocyte primary cultures under nonproliferative and proliferative conditions
    • DOI 10.1006/excr.1994.1004
    • C. Moler, M. Benito, and M. Lorenzo Glucose-6-phosphate dehydrogenase gene expression in fetal hepatocyte primary cultures under nonproliferative conditions Exp. Cell Res 210 1994 26 32 (Pubitemid 24168490)
    • (1994) Experimental Cell Research , vol.210 , Issue.1 , pp. 26-32
    • Molero, C.1    Benito, M.2    Lorenzo, M.3
  • 76
    • 0026780928 scopus 로고
    • Increased activity of 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase in purified cell suspension and single cells from the uterine cervix in cervical intraepithelial neoplasia
    • S.K. Jonas, C. Benedetto, A. Flatman, R.H. Hammond, L. Micheletti, C. Riley, P.A. Riley, D.J. Spargo, M. Zonca, and T.F. Slater Increased activity of 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase in purified cell suspension and single cells from the uterine cervix in cervical intraepithelial neoplasia Br. J. Cancer 66 1992 185 191
    • (1992) Br. J. Cancer , vol.66 , pp. 185-191
    • Jonas, S.K.1    Benedetto, C.2    Flatman, A.3    Hammond, R.H.4    Micheletti, L.5    Riley, C.6    Riley, P.A.7    Spargo, D.J.8    Zonca, M.9    Slater, T.F.10
  • 77
    • 0034161904 scopus 로고    scopus 로고
    • Transforming growth factor β2 promotes glucose carbon incorporation into nucleic acid ribose through the nonoxidative pentose cycle in lung epithelial carcinoma cells
    • L.G. Boros, J.S. Torday, S. Lim, S. Bassilian, M. Cascante, and W.N. Lee Transforming growth factor β2 promotes glucose carbon incorporation into nucleic acid ribose through the nonoxidative pentose cycle in lung epithelial carcinoma cells Cancer Res. 60 2000 1183 1185 (Pubitemid 30151978)
    • (2000) Cancer Research , vol.60 , Issue.5 , pp. 1183-1185
    • Boros, L.G.1    Torday, J.S.2    Lim, S.3    Bassilian, S.4    Cascante, M.5    Lee, W.-N.P.6
  • 78
  • 79
    • 0040697067 scopus 로고    scopus 로고
    • Analysis of phosphofructokinase subunits and isozymes in ascites tumor cells and its original tissue, murine mammary gland
    • DOI 10.1016/S0014-5793(97)00496-1, PII S0014579397004961
    • C. Sanchez-Martinez, and J.J. Aragon Analysis of phosphofructokinase subunits and isozymes in ascites tumor cells and its original tissue, murine mammary gland FEBS Lett 409 1997 86 90 (Pubitemid 27248572)
    • (1997) FEBS Letters , vol.409 , Issue.1 , pp. 86-90
    • Sanchez-Martinez, C.1    Aragon, J.2
  • 80
    • 33745303045 scopus 로고    scopus 로고
    • Hypoxia signalling in cancer and approaches to enforce tumour regression
    • DOI 10.1038/nature04871, PII NATURE04871
    • J. Pouyssegur, F. Dayan, and N.M. Mazure Hypoxia signalling in cancer and approaches to enforce tumor regression Nature 441 2006 437 443 (Pubitemid 44050138)
    • (2006) Nature , vol.441 , Issue.7092 , pp. 437-443
    • Pouyssegur, J.1    Dayan, F.2    Mazure, N.M.3
  • 81
    • 33746879141 scopus 로고    scopus 로고
    • Glycolysis inhibition for anticancer treatment
    • DOI 10.1038/sj.onc.1209597, PII 1209597
    • H. Pelicano, D.S. Martin, R.H. Xu, and P. Huang Glycolysis inhibition for anticancer treatment Oncogene 25 2006 4633 4646 (Pubitemid 44187614)
    • (2006) Oncogene , vol.25 , Issue.34 , pp. 4633-4646
    • Pelicano, H.1    Martin, D.S.2    Xu, R.-H.3    Huang, P.4
  • 82
    • 37549005208 scopus 로고    scopus 로고
    • Detection of reactive oxygen species via endogenous oxidative pentose phosphate cycle activity in response to oxygen concentration: Implications for the mechanism of HIF-1α stabilization under moderate hypoxia
    • S.W. Tuttle, A. Maity, P.R. Oprysko, A.V. Kachur, I.S. Ayene, J.E. Biaglow, and C.J. Koch Detection of reactive oxygen species via endogenous oxidative pentose phosphate cycle activity in response to oxygen concentration: implications for the mechanism of HIF-1α stabilization under moderate hypoxia J. Biol. Chem. 282 2007 36790 36796
    • (2007) J. Biol. Chem. , vol.282 , pp. 36790-36796
    • Tuttle, S.W.1    Maity, A.2    Oprysko, P.R.3    Kachur, A.V.4    Ayene, I.S.5    Biaglow, J.E.6    Koch, C.J.7
  • 83
    • 79955600638 scopus 로고    scopus 로고
    • Carbon metabolism and the sign of control coefficients in metabolic adaptations underlying K-ras transformation
    • P. de Atauri, A. Benito, P. Vizán, M. Zanuy, R. Mangues, S. Marín, and M. Cascante Carbon metabolism and the sign of control coefficients in metabolic adaptations underlying K-ras transformation Biochim. Biophys. Acta 1807 2011 746 754
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 746-754
    • De Atauri, P.1    Benito, A.2    Vizán, P.3    Zanuy, M.4    Mangues, R.5    Marín, S.6    Cascante, M.7
  • 84
    • 0037041277 scopus 로고    scopus 로고
    • Loss of heterozygosity on chromosome 11 in esophageal squamous cell carcinomas
    • DOI 10.1016/S0304-3835(01)00814-X, PII S030438350100814X
    • C.T. Lam, C.M. Tang, K.W. Lau, and M.L. Lung Loss of heterozygosity on chromosome 11 in esophageal squamous cell carcinomas Cancer Lett. 178 2002 75 81 (Pubitemid 34159244)
    • (2002) Cancer Letters , vol.178 , Issue.1 , pp. 75-81
    • Lam, C.T.1    Tang, C.M.C.2    Lau, K.W.3    Lung, M.L.4
  • 87
    • 34249905885 scopus 로고    scopus 로고
    • Gene silencing of TKTL1 by RNAi inhibits cell proliferation in human hepatoma cells
    • DOI 10.1016/j.canlet.2007.01.010, PII S0304383507000171
    • S. Zhang, J.H. Yang, C.K. Guo, and P.C. Cai Gene silencing of TKTL1 by RNAi inhibits cell proliferation in human hepatoma cells Cancer Lett. 253 2007 108 114 (Pubitemid 46874727)
    • (2007) Cancer Letters , vol.253 , Issue.1 , pp. 108-114
    • Zhang, S.1    Yang, J.-H.2    Guo, C.-K.3    Cai, P.-c.4
  • 89
    • 21244460340 scopus 로고    scopus 로고
    • Mutations in the transketolase-like gene TKTL1: Clinical implications for neurodegenerative diseases, diabetes and cancer
    • J.F. Coy, D. Dressler, J. Wilde, and P. Schubert Mutations in the transketolase-like gene TKTL1: clinical implications for neurodegenerative diseases, diabetes and cancer Clin. Lab. 51 2005 257 273 (Pubitemid 40895125)
    • (2005) Clinical Laboratory , vol.51 , Issue.5-6 , pp. 257-273
    • Coy, J.F.1    Dressler, D.2    Wilde, J.3    Schubert, P.4
  • 90
    • 34247592022 scopus 로고    scopus 로고
    • The TKTL1 gene influences total transketolase activity and cell proliferation in human colon cancer LoVo cells
    • DOI 10.1097/CAD.0b013e328013d99e, PII 0000181320070400000008
    • L.H. Hu, J.H. Yang, D.T. Zhang, S. Zhang, L. Wang, P.C. Cai, J.F. Zheng, and J.S. Huang The TKTL1 gene influences total transketolase activity and cell proliferation in human colon cancer LoVo cells Anticancer Drugs 18 2007 427 433 (Pubitemid 46712406)
    • (2007) Anti-Cancer Drugs , vol.18 , Issue.4 , pp. 427-433
    • Hu, L.-H.1    Yang, J.-H.2    Zhang, D.-T.3    Zhang, S.4    Wang, L.5    Cai, P.-C.6    Zheng, J.-F.7    Huang, J.-S.8
  • 91
    • 52949125204 scopus 로고    scopus 로고
    • Genetic variation in transaldolase 1 and risk of squamous cell carcinoma of the head and neck
    • P.V. Basta, J.T. Bensen, C. Tse, C.M. Perou, P.F. Sullivan, and A.F. Olshan Genetic variation in transaldolase 1 and risk of squamous cell carcinoma of the head and neck Cancer Detect. Prev. 32 2008 200 208
    • (2008) Cancer Detect. Prev. , vol.32 , pp. 200-208
    • Basta, P.V.1    Bensen, J.T.2    Tse, C.3    Perou, C.M.4    Sullivan, P.F.5    Olshan, A.F.6
  • 92
    • 77957761380 scopus 로고    scopus 로고
    • Proteomic analysis of anti-tumor effects by tetrandrine treatment in HepG2 cells
    • Z. Cheng, K. Wang, J. Wei, X. Lu, and B. Liu Proteomic analysis of anti-tumor effects by tetrandrine treatment in HepG2 cells Phytomedicine 17 2010 1000 1005
    • (2010) Phytomedicine , vol.17 , pp. 1000-1005
    • Cheng, Z.1    Wang, K.2    Wei, J.3    Lu, X.4    Liu, B.5
  • 93
    • 65649120706 scopus 로고    scopus 로고
    • Modulation of pentose phosphate pathway during cell cycle progression in human colon adenocarcinoma cell line HT29
    • P. Vizán, G. Alcarraz-Vizán, S. Díaz-Moralli, O.N. Solovjeva, W.M. Frederiks, and M. Cascante Modulation of pentose phosphate pathway during cell cycle progression in human colon adenocarcinoma cell line HT29 Int. J. Cancer 124 2009 2789 2796
    • (2009) Int. J. Cancer , vol.124 , pp. 2789-2796
    • Vizán, P.1    Alcarraz-Vizán, G.2    Díaz-Moralli, S.3    Solovjeva, O.N.4    Frederiks, W.M.5    Cascante, M.6
  • 94
    • 80051634012 scopus 로고    scopus 로고
    • Resveratrol suppresses human colon cancer cell proliferation and induces apoptosis via targeting the pentose phosphate and the talin-FAK signalling pathways - A proteomic approach
    • J. Vanamala, S. Radhakrishnan, L. Reddivari, V.B. Bhat, and A.B. Ptitsyn Resveratrol suppresses human colon cancer cell proliferation and induces apoptosis via targeting the pentose phosphate and the talin-FAK signalling pathways - a proteomic approach Proteome Sci 9 2011 49
    • (2011) Proteome Sci , vol.9 , pp. 49
    • Vanamala, J.1    Radhakrishnan, S.2    Reddivari, L.3    Bhat, V.B.4    Ptitsyn, A.B.5
  • 96
    • 34548478493 scopus 로고    scopus 로고
    • Pro-oxidative effects of tea and polyphenols, epigallocatechin-3-gallate and epigallocatechin, on G6PD-deficient erythrocytes in vitro
    • C.H.; L, K. Ko, P.C. Ng, K.P. Fung, C.L. Li, R.P.-O. Wong, K.M. Chui, G.J.-L. Gu, E. Yung, C.C. Wang, and T.F. Fok Pro-oxidative effects of tea and polyphenols, epigallocatechin-3-gallate and epigallocatechin, on G6PD-deficient erythrocytes in vitro Int. J. Mol. Med. 18 2006 987 994
    • (2006) Int. J. Mol. Med. , vol.18 , pp. 987-994
    • Ko, C.H.L.K.1    Ng, P.C.2    Fung, K.P.3    Li, C.L.4    Wong, R.P.-O.5    Chui, K.M.6    Gu, G.J.-L.7    Yung, E.8    Wang, C.C.9    Fok, T.F.10
  • 99
    • 0345410965 scopus 로고    scopus 로고
    • Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery
    • DOI 10.1006/excr.1998.4347
    • X. Preville, F. Salvemini, S. Giraud, S. Chaufour, C. Paul, G. Stepien, M.V. Ursini, and A.P. Arrigo Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery Exp. Cell Res. 247 1999 61 78 (Pubitemid 29393962)
    • (1999) Experimental Cell Research , vol.247 , Issue.1 , pp. 61-78
    • Preville, X.1    Salvemini, F.2    Giraud, S.3    Chaufour, S.4    Paul, C.5    Stepien, G.6    Ursini, M.V.7    Arrigo, A.-P.8
  • 103
    • 0028909713 scopus 로고
    • Increased induction of apoptosis in mononuclear cells of a glucose-6-phosphate dehydrogenase deficient patient
    • T. Efferth, U. Fabry, P. Glatte, and R. Osieka Increased induction of apoptosis in mononuclear cells of a glucose-6-phosphate dehydrogenase deficient patient J. Mol. Med. (Berlin) 73 1995 47 49
    • (1995) J. Mol. Med. (Berlin) , vol.73 , pp. 47-49
    • Efferth, T.1    Fabry, U.2    Glatte, P.3    Osieka, R.4
  • 104
    • 0034045004 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase and the oxidative pentose phosphate cycle protect cells against apoptosis induced by low doses of ionizing radiation
    • S. Tuttle, T. Stamato, M.L. Perez, and J. Biaglow Glucose-6-phosphate dehydrogenase and the oxidative pentose phosphate cycle protect cells against apoptosis induced by low doses of ionizing radiation Radiat. Res 153 2000 781 787 (Pubitemid 30349553)
    • (2000) Radiation Research , vol.153 , Issue.6 , pp. 781-787
    • Tuttle, S.1    Stamato, T.2    Perez, M.L.3    Biaglow, J.4
  • 106
    • 79952280229 scopus 로고    scopus 로고
    • P53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase
    • P. Jiang, W. Du, X. Wang, A. Mancuso, X. Gao, M. Wu, and X. Yang p53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase Nat. Cell Biol. 13 2011 310 316
    • (2011) Nat. Cell Biol. , vol.13 , pp. 310-316
    • Jiang, P.1    Du, W.2    Wang, X.3    Mancuso, A.4    Gao, X.5    Wu, M.6    Yang, X.7
  • 109
    • 0034717224 scopus 로고    scopus 로고
    • Non-steroidal anti-inflammatory drugs and apoptosis in the gastrointestinal tract: Potential role of the pentose phosphate pathways
    • DOI 10.1016/S0014-2999(00)00237-5, PII S0014299900002375
    • S.N. Porter, G.S. Howarth, and R.N. Butler Non-steroidal anti-inflammatory drugs and apoptosis in the gastrointestinal tract: potential role of the pentose phosphate pathways Eur. J. Pharmacol. 397 2000 1 9 (Pubitemid 30323804)
    • (2000) European Journal of Pharmacology , vol.397 , Issue.1 , pp. 1-9
    • Porter, S.N.1    Howarth, G.S.2    Butler, R.N.3
  • 110
    • 79960263592 scopus 로고    scopus 로고
    • Metabolic oxidative stress elicited by the copper(II) complex [Cu(isaepy)2] triggers apoptosis in SH-SY5Y cells through the induction of the AMP-activated protein kinase/p38MAPK/p53 signalling axis: Evidence for a combined use with 3-bromopyruvate in neuroblastoma treatment
    • G. Filomeni, S. Cardaci, A.M. Da Costa Ferreira, G. Rotilio, and M.R. Ciriolo Metabolic oxidative stress elicited by the copper(II) complex [Cu(isaepy)2] triggers apoptosis in SH-SY5Y cells through the induction of the AMP-activated protein kinase/p38MAPK/p53 signalling axis: evidence for a combined use with 3-bromopyruvate in neuroblastoma treatment Biochem. J. 437 2011 443 453
    • (2011) Biochem. J. , vol.437 , pp. 443-453
    • Filomeni, G.1    Cardaci, S.2    Da Costa Ferreira, A.M.3    Rotilio, G.4    Ciriolo, M.R.5
  • 111
    • 0036277102 scopus 로고    scopus 로고
    • Apoptosis in mitotic competent undifferentiated cells is induced by cellular redox imbalance independent of reactive oxygen species production
    • DOI 10.1096/fj.01-0784com
    • E.K. Pias, and T.Y. Aw Apoptosis in mitotic competent undifferentiated cells is induced by cellular redox imbalance independent of reactive oxygen species production FASEB J. 16 2002 781 790 (Pubitemid 34615126)
    • (2002) FASEB Journal , vol.16 , Issue.8 , pp. 781-790
    • Pias, E.K.1    Tak Yee, A.W.2
  • 112
    • 60849114962 scopus 로고    scopus 로고
    • A new G6PD knockdown tumor-cell line with reduced proliferation and increased susceptibility to oxidative stress
    • D. Li, Y. Zhu, Q. Tang, H Lu, H Li, Y. Yang, Z. Li, and S. Tong A new G6PD knockdown tumor-cell line with reduced proliferation and increased susceptibility to oxidative stress Cancer Biother. Radiopharm. 24 2009 81 90
    • (2009) Cancer Biother. Radiopharm. , vol.24 , pp. 81-90
    • Li, D.1    Zhu, Y.2    Tang, Q.3    Lu, H.4    Li, H.5    Yang, Y.6    Li, Z.7    Tong, S.8
  • 115
    • 0032496222 scopus 로고    scopus 로고
    • Molecular ordering in HIV-induced apoptosis: Oxidative stress, activation of caspases, and cell survival are regulated by transaldolase
    • DOI 10.1074/jbc.273.19.11944
    • K. Banki, E. Hutter, N.J. Gonchoroff, and A. Perl Molecular ordering in HIV-induced apoptosis: oxidative stress, activation of caspases, and cell survival are regulated by transaldolase J. Biol. Chem. 273 1998 11944 11953 (Pubitemid 28272104)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.19 , pp. 11944-11953
    • Banki, K.1    Hutter, E.2    Gonchoroff, N.J.3    Perl, A.4
  • 116
    • 2242485601 scopus 로고    scopus 로고
    • Fermented wheat germ extract inhibits glycolysis/pentose cycle enzymes and induces apoptosis through poly(ADP-ribose) polymerase activation in Jurkat T-cell leukemia tumor cells
    • DOI 10.1074/jbc.M206150200
    • B. Comin-Anduix, L.G. Boros, S. Marin, J. Boren, C. Callol-Massot, J.J. Centelles, J.L. Torres, N. Agell, S. Bassilian, and M. Cascante Fermented wheat germ extract inhibits glycolysis/pentose cycle enzymes and induces apoptosis through poly(ADP-ribose) polymerase activation in Jurkat T-cell leukemia tumor cells J. Biol. Chem. 277 2002 46408 46414 (Pubitemid 35417635)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46408-46414
    • Comin-Anduix, B.1    Boros, L.G.2    Marin, S.3    Boren, J.4    Callol-Massot, C.5    Centelles, J.J.6    Torres, J.L.7    Agell, N.8    Bassilian, S.9    Cascante, M.10
  • 117
    • 79951675742 scopus 로고    scopus 로고
    • Combined arginine and ascorbic acid treatment induces apoptosis in the hepatoma cell line HA22T/VGH and changes in redox status involving the pentose phosphate pathway and reactive oxygen and nitrogen species
    • B.S. Hsieh, L.W. Huang, S.J. Su, H.L. Cheng, Y.C. Hu, T.C. Hung, and K.L. Chang Combined arginine and ascorbic acid treatment induces apoptosis in the hepatoma cell line HA22T/VGH and changes in redox status involving the pentose phosphate pathway and reactive oxygen and nitrogen species J. Nutr. Biochem. 22 2011 234 241
    • (2011) J. Nutr. Biochem. , vol.22 , pp. 234-241
    • Hsieh, B.S.1    Huang, L.W.2    Su, S.J.3    Cheng, H.L.4    Hu, Y.C.5    Hung, T.C.6    Chang, K.L.7
  • 119
    • 0035802278 scopus 로고    scopus 로고
    • Mechanisms of ascorbic acid recycling in human erythrocytes
    • DOI 10.1016/S0304-4165(01)00188-X, PII S030441650100188X
    • J.M. May, Z. Qu, and J.D. Morrow Mechanisms of ascorbic acid recycling in human erythrocytes Biochim. Biophys. Acta 1528 2001 159 166 (Pubitemid 33001277)
    • (2001) Biochimica et Biophysica Acta - General Subjects , vol.1528 , Issue.2-3 , pp. 159-166
    • May, J.M.1    Qu, Z.-C.2    Morrow, J.D.3
  • 120
    • 79551580561 scopus 로고    scopus 로고
    • ATM activates the pentose phosphate pathway promoting anti-oxidant defence and DNA repair
    • C. Cosentino, D. Grieco, and V. Costanzo ATM activates the pentose phosphate pathway promoting anti-oxidant defence and DNA repair EMBO J. 30 2011 546 555
    • (2011) EMBO J. , vol.30 , pp. 546-555
    • Cosentino, C.1    Grieco, D.2    Costanzo, V.3
  • 121
    • 0035100719 scopus 로고    scopus 로고
    • DNA damage and apoptosis in mononuclear cells from glucose-6-phosphate dehydrogenase-deficient patients (G6PD Aachen variant) after UV irradiation
    • Y. Efferth, U. Fabry, and R. Osieka DNA damage and apoptosis in mononuclear cells from glucose-6-phosphate dehydrogenase-deficient patients (G6PD Aachen variant) after UV irradiation J. Leukocyte Biol 69 2001 340 342 (Pubitemid 32221436)
    • (2001) Journal of Leukocyte Biology , vol.69 , Issue.3 , pp. 340-342
    • Efferth, T.1    Fabry, U.2    Osieka, R.3
  • 122
    • 33645812852 scopus 로고    scopus 로고
    • Effects of small molecules on chaperone-mediated autophagy
    • P.F. Finn, N.T. Mesires, M. Vine, and J.F. Dice Effects of small molecules on chaperone-mediated autophagy Autophagy 1 2005 141 145
    • (2005) Autophagy , vol.1 , pp. 141-145
    • Finn, P.F.1    Mesires, N.T.2    Vine, M.3    Dice, J.F.4
  • 123
    • 44849097091 scopus 로고    scopus 로고
    • Central carbon metabolism in the progression of mammary carcinoma
    • DOI 10.1007/s10549-007-9732-3
    • A.D. Richardson, C. Yang, A. Osterman, and J.W. Smith Central carbon metabolism in the progression of mammary carcinoma Breast Cancer Res. Treat. 110 2008 297 307 (Pubitemid 351793887)
    • (2008) Breast Cancer Research and Treatment , vol.110 , Issue.2 , pp. 297-307
    • Richardson, A.D.1    Yang, C.2    Osterman, A.3    Smith, J.W.4
  • 124
    • 77951242628 scopus 로고    scopus 로고
    • Metabolomic changes accompanying transformation and acquisition of metastatic potential in a syngeneic mouse mammary tumor model
    • X. Lu, B. Bennet, E. Mu, J. Rabinowitz, and Y. Kang Metabolomic changes accompanying transformation and acquisition of metastatic potential in a syngeneic mouse mammary tumor model J. Biol. Chem. 285 2010 9317 9321
    • (2010) J. Biol. Chem. , vol.285 , pp. 9317-9321
    • Lu, X.1    Bennet, B.2    Mu, E.3    Rabinowitz, J.4    Kang, Y.5
  • 128
    • 0035851102 scopus 로고    scopus 로고
    • Gleevec (STI571) influences metabolic enzyme activities and glucose carbon flow toward nucleic acid and fatty acid synthesis in myeloid tumor cells
    • J. Boren, M. Cascante, S. Marin, B. Comìn-Anduix, J.J. Centelles, S. Lim, S. Bassilian, S. Ahmed, W.N.-P. Lee, and L.G. Boros Gleevec (STI571) influences metabolic enzyme activities and glucose carbon flow toward nucleic acid and fatty acid synthesis in myeloid tumor cells J. Biol. Chem. 276 2001 37747 37753
    • (2001) J. Biol. Chem. , vol.276 , pp. 37747-37753
    • Boren, J.1    Cascante, M.2    Marin, S.3    Comìn-Anduix, B.4    Centelles, J.J.5    Lim, S.6    Bassilian, S.7    Ahmed, S.8    Lee, W.N.-P.9    Boros, L.G.10
  • 129
    • 0035158183 scopus 로고    scopus 로고
    • Genistein inhibits nonoxidative ribose synthesis in MIA pancreatic adenocarcinoma cells: A new mechanism of controlling tumor growth
    • DOI 10.1097/00006676-200101000-00001
    • L.G. Boros, S. Bassilian, S. Lim, and W.N.-P. Lee Genistein inhibits nonoxidative ribose synthesis in MIA pancreatic adenocarcinoma cells: a new mechanism of controlling tumor growth Pancreas 22 2001 1 7 (Pubitemid 32046207)
    • (2001) Pancreas , vol.22 , Issue.1 , pp. 1-7
    • Boros, L.G.1    Bassilian, S.2    Lim, S.3    Lee, W.-N.P.4
  • 130
    • 0037189542 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 activation by aerobic glycolysis implicates the Warburg effect in carcinogenesis
    • DOI 10.1074/jbc.M202487200
    • H. Lu, R.A. Forbes, and A. Verma Hypoxia-inducible factor 1 activation by aerobic glycolysis implicates the Warburg effect in carcinogenesis J. Biol. Chem. 277 2002 23111 23115 (Pubitemid 34952134)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23111-23115
    • Lu, H.1    Forbes, R.A.2    Verma, A.3
  • 131
    • 66349107721 scopus 로고    scopus 로고
    • Glucose 6-phosphate dehydrogenase is regulated through c-Src-mediated tyrosine phosphorylation in endothelial cells
    • S. Pan, C.J. World, C.J. Kovacs, and B.C. Berk Glucose 6-phosphate dehydrogenase is regulated through c-Src-mediated tyrosine phosphorylation in endothelial cells Arterioscler. Thromb. Vasc. Biol. 29 2009 895 901
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , pp. 895-901
    • Pan, S.1    World, C.J.2    Kovacs, C.J.3    Berk, B.C.4
  • 133
    • 77956177426 scopus 로고    scopus 로고
    • Benfotiamine improves functional recovery of the infarcted heart via activation of pro-survival G6PD/Akt signaling pathway and modulation of neurohormonal response
    • R. Katare, A. Caporali, C. Emanueli, and P. Madeddu Benfotiamine improves functional recovery of the infarcted heart via activation of pro-survival G6PD/Akt signaling pathway and modulation of neurohormonal response J. Mol. Cell. Cardiol 49 2010 625 638
    • (2010) J. Mol. Cell. Cardiol , vol.49 , pp. 625-638
    • Katare, R.1    Caporali, A.2    Emanueli, C.3    Madeddu, P.4
  • 134
    • 33644891878 scopus 로고    scopus 로고
    • Long-term effect of therapeutic laser photocoagulation on gene expression in the eye
    • DOI 10.1096/fj.05-3890fje
    • N. Binz, C.E. Graham, K. Simpson, Y.K.Y. Lai, W.-Y. Shen, C.-M. Lai, T.P. Speed, and P.E. Rakoczy Long-term effect of therapeutic laser photocoagulation on gene expression in the eye FASEB J. 20 2006 383 385 (Pubitemid 46671179)
    • (2006) FASEB Journal , vol.20 , Issue.2 , pp. 383-385
    • Binz, N.1    Graham, C.E.2    Simpson, K.3    Lai, Y.K.Y.4    Shen, W.-Y.5    Lai, C.-M.6    Speed, T.P.7    Rakoczy, P.E.8
  • 135
    • 66749132763 scopus 로고    scopus 로고
    • Characterization of the metabolic changes underlying growth factor angiogenic activation: Identification of new potential therapeutic targets
    • P. Vizàn, S. Sànchez-Tena, G. Alcarraz-Vizàn, M. Soler, R. Messeguer, M.D. Pujol, W.-N.P. Lee, and M. Cascante Characterization of the metabolic changes underlying growth factor angiogenic activation: identification of new potential therapeutic targets Carcinogenesis 30 2009 946 952
    • (2009) Carcinogenesis , vol.30 , pp. 946-952
    • Vizàn, P.1    Sànchez-Tena, S.2    Alcarraz-Vizàn, G.3    Soler, M.4    Messeguer, R.5    Pujol, M.D.6    Lee, W.-N.P.7    Cascante, M.8
  • 137
    • 16644364379 scopus 로고    scopus 로고
    • Identification of novel small-molecule inhibitors for human transketolase by high-throughput screening with fluorescent intensity (FLINT) assay
    • M.X. Du, J. Sim, L. Fang, Z. Yin, S. Koh, J. Stratton, J. Pons, J.J. Wang, and B. Carte Identification of novel small-molecule inhibitors for human transketolase by high-throughput screening with fluorescent intensity (FLINT) assay J. Biomol. Screen. 9 2004 427 433
    • (2004) J. Biomol. Screen. , vol.9 , pp. 427-433
    • Du, M.X.1    Sim, J.2    Fang, L.3    Yin, Z.4    Koh, S.5    Stratton, J.6    Pons, J.7    Wang, J.J.8    Carte, B.9
  • 140
    • 4344625883 scopus 로고    scopus 로고
    • A critical role of glutathione in determining apoptosis sensitivity and resistance in leukemia cells
    • C. Friesen, Y. Kiess, and K.M. Debatin A critical role of glutathione in determining apoptosis sensitivity and resistance in leukemia cells Cell Death Differ 11 2004 S73 S85
    • (2004) Cell Death Differ , vol.11
    • Friesen, C.1    Kiess, Y.2    Debatin, K.M.3
  • 141
    • 33746879141 scopus 로고    scopus 로고
    • Glycolysis inhibition for anticancer treatment
    • DOI 10.1038/sj.onc.1209597, PII 1209597
    • H. Pelicano, D.S. Martin, R.-H. Xu, and P. Huang Glycolysis inhibition for anticancer treatment Oncogene 25 2006 4633 4646 (Pubitemid 44187614)
    • (2006) Oncogene , vol.25 , Issue.34 , pp. 4633-4646
    • Pelicano, H.1    Martin, D.S.2    Xu, R.-H.3    Huang, P.4
  • 144
    • 50849127129 scopus 로고    scopus 로고
    • Combined action and regulation of phase II enzymes and multidrug resistance proteins in multidrug resistance in cancer
    • I. Meijerman, J.H. Beijnen, and J.H. Schellens Combined action and regulation of phase II enzymes and multidrug resistance proteins in multidrug resistance in cancer Cancer Treat. Rev 34 2008 505 520
    • (2008) Cancer Treat. Rev , vol.34 , pp. 505-520
    • Meijerman, I.1    Beijnen, J.H.2    Schellens, J.H.3
  • 145
    • 0025289481 scopus 로고
    • Elevated pentose cycle and glucuronyltransferase in daunorubicin- resistant P388 cells
    • T. Gessner, L.A. Vaughan, B.C. Beehler, C.J. Bartels, and R.M. Baker Elevated pentose cycle and glucuronyltransferase in daunorubicin-resistant P388 cells Cancer Res. 50 1990 3921 3927 (Pubitemid 20225607)
    • (1990) Cancer Research , vol.50 , Issue.13 , pp. 3921-3927
    • Gessner, T.1    Vaughan, L.A.2    Beehler, B.C.3    Bartels, C.J.4    Baker, R.M.5
  • 147
    • 0027892859 scopus 로고
    • Glucose metabolism in adriamycin-sensitive and -resistant LoVo human colon carcinoma cells
    • M. Fanciulli, T. Bruno, S. Castiglione, C. Del Carlo, M.G. Paggi, and A. Floridi Glucose metabolism in adriamycin-sensitive and -resistant LoVo human colon carcinoma cells Oncol. Res. 5 1993 357 362 (Pubitemid 24145947)
    • (1993) Oncology Research , vol.5 , Issue.9 , pp. 357-362
    • Fanciulli, M.1    Bruno, T.2    Castiglione, S.3    Del Carlo, C.4    Paggi, M.G.5    Floridi, A.6
  • 148
    • 0030009424 scopus 로고    scopus 로고
    • Energy metabolism of adriamycin-sensitive and -resistant Ehrlich ascites tumor cells
    • S. Miccadei, M. Fanciulli, T. Bruno, M.G. Paggi, and A. Floridi Energy metabolism of adriamycin-sensitive and -resistant Ehrlich ascites tumor cells Oncol. Res. 8 1996 27 35 (Pubitemid 26107684)
    • (1996) Oncology Research , vol.8 , Issue.1 , pp. 27-35
    • Miccadei, S.1    Fanciulli, M.2    Bruno, T.3    Paggi, M.G.4    Floridi, A.5
  • 149
    • 57749113487 scopus 로고    scopus 로고
    • Altered detoxification status and increased resistance to oxidative stress by K-ras transformation
    • C.V. Recktenwald, R. Kellner, R. Lichtenfels, and B. Seliger Altered detoxification status and increased resistance to oxidative stress by K-ras transformation Cancer Res. 68 2008 10086 10093
    • (2008) Cancer Res. , vol.68 , pp. 10086-10093
    • Recktenwald, C.V.1    Kellner, R.2    Lichtenfels, R.3    Seliger, B.4
  • 152
    • 0026610928 scopus 로고
    • 13C NMR studies of glucose metabolism in human leukemic CEM-C7 and CEM-C1 cells
    • 13C NMR studies of glucose metabolism in human leukemic CEM-C7 and CEM-C1 cells Magn. Reson. Med. 23 1992 356 366
    • (1992) Magn. Reson. Med. , vol.23 , pp. 356-366
    • Post, J.F.1    Baum, E.2    Ezell, E.L.3
  • 153
    • 0031012644 scopus 로고    scopus 로고
    • The correlation of membranous glycoprotein-gp-170, cytoplasmic glutathione and glucose-6-phosphate dehydrogenase levels with multidrug resistance in transitional cell carcinoma cell lines of the urinary tract
    • D.S. Yu, S.Y. Chang, and C.P. Ma The correlation of membranous glycoprotein-gp-170, cytoplasmic glutathione and glucose-6-phosphate dehydrogenase levels with multidrug resistance in transitional cell carcinoma cell lines of the urinary tract J. Urol 157 1997 727 731
    • (1997) J. Urol , vol.157 , pp. 727-731
    • Yu, D.S.1    Chang, S.Y.2    Ma, C.P.3
  • 154
    • 23044517485 scopus 로고    scopus 로고
    • The role of bioreductive activation of doxorubicin in cytotoxic activity against leukaemia HL60-sensitive cell line and its multidrug-resistant sublines
    • DOI 10.1038/sj.bjc.6602639
    • D. Kostrzewa-Nowak, M.J. Paine, C.R. Wolf, and J. Tarasiuk The role of bioreductive activation of doxorubicin in cytotoxic activity against leukaemia HL60-sensitive cell line and its multidrug-resistant sublines Br. J. Cancer 11 2005 89 97 (Pubitemid 41076256)
    • (2005) British Journal of Cancer , vol.93 , Issue.1 , pp. 89-97
    • Kostrzewa-Nowak, D.1    Paine, M.2    Wolf, C.R.3    Tarasiuk, J.4
  • 155
    • 33845672083 scopus 로고    scopus 로고
    • Bioreductive activation of mitoxantrone by NADPH cytochrome P450 reductase. Implications for increasing its ability to inhibit the growth of sensitive and multidrug resistant leukaemia HL60 cells
    • DOI 10.1016/j.canlet.2006.01.012, PII S0304383506000577
    • D. Kostrzewa-Nowak, M.J. Paine, A. Korytowska, K. Serwatka, S. Piotrowska, C.R. Wolf, and J. Tarasiuk Bioreductive activation of mitoxantrone by NADPH cytochrome P450 reductase: implications for increasing its ability to inhibit the growth of sensitive and multidrug resistant leukaemia HL60 cells Cancer Lett. 245 2007 252 262 (Pubitemid 44959360)
    • (2007) Cancer Letters , vol.245 , Issue.1-2 , pp. 252-262
    • Kostrzewa-Nowak, D.1    Paine, M.J.I.2    Korytowska, A.3    Serwatka, K.4    Piotrowska, S.5    Wolf, C.R.6    Tarasiuk, J.7
  • 156
    • 41349117220 scopus 로고    scopus 로고
    • Schisandra fructus extract ameliorates doxorubicin-induce cytotoxicity in cardiomyocytes: Altered gene expression for detoxification enzymes
    • DOI 10.1007/s12263-007-0073-y
    • E.H. Choi, N. Lee, H.J. Kim, M.K. Kim, S.G. Chi, D.Y. Kwon, and H.S. Chun Schisandra fructus extract ameliorates doxorubicin-induced cytotoxicity in cardiomyocytes: altered gene expression for detoxification enzymes Genes Nutr 2 2008 337 345 (Pubitemid 351447709)
    • (2008) Genes and Nutrition , vol.2 , Issue.4 , pp. 337-345
    • Choi, E.H.1    Lee, N.2    Kim, H.J.3    Kim, M.K.4    Chi, S.-G.5    Kwon, D.Y.6    Chun, H.S.7
  • 158
    • 69449090754 scopus 로고    scopus 로고
    • Upregulation of glycolytic enzymes in proteins secreted from human colon cancer cells with 5-fluorouracil resistance
    • Y.K. Shin, B.C. Yoo, Y.S. Hong, H.J. Chang, K.H. Jumg, S.Y. Jeong, and J.G. Park Upregulation of glycolytic enzymes in proteins secreted from human colon cancer cells with 5-fluorouracil resistance Electrophoresis 30 2009 2182 2192
    • (2009) Electrophoresis , vol.30 , pp. 2182-2192
    • Shin, Y.K.1    Yoo, B.C.2    Hong, Y.S.3    Chang, H.J.4    Jumg, K.H.5    Jeong, S.Y.6    Park, J.G.7
  • 160
    • 0026047307 scopus 로고
    • Contribution of glutathione and glutathione-dependent enzymes in the reversal of adriamycin resistance in colon carcinoma cell lines
    • G.M. Lai, J.A. Moscow, M.G. Alvarez, T. Fojo, and S.E. Bates Contribution of glutathione and glutathione-dependent enzymes in the reversal of adriamycin resistance in colon carcinoma cell lines Int. J. Cancer 49 1991 688 695
    • (1991) Int. J. Cancer , vol.49 , pp. 688-695
    • Lai, G.M.1    Moscow, J.A.2    Alvarez, M.G.3    Fojo, T.4    Bates, S.E.5
  • 162
    • 77954028765 scopus 로고    scopus 로고
    • Metabolic oxidative stress induced by a combination of 2-DG and 6-AN enhances radiation damage selectively in malignant cells via non-coordinated expression of antioxidant enzymes
    • P.K. Sharma, R. Bhardwaj, B.S. Dwarakanath, and R. Varshney Metabolic oxidative stress induced by a combination of 2-DG and 6-AN enhances radiation damage selectively in malignant cells via non-coordinated expression of antioxidant enzymes Cancer Lett 295 2010 154 166
    • (2010) Cancer Lett , vol.295 , pp. 154-166
    • Sharma, P.K.1    Bhardwaj, R.2    Dwarakanath, B.S.3    Varshney, R.4
  • 163
    • 23644437291 scopus 로고    scopus 로고
    • Radiosensitization by 6-aminonicotinamide and 2-deoxy-D-glucose in human cancer cells
    • DOI 10.1080/09553000500148590
    • R. Varshney, B.S. Dwarakanath, and V. Jain Radiosensitization by 6-aminonicotinamide and 2-deoxy-d-glucose in human cancer cells Int. J. Radiat. Biol. 81 2005 397 408 (Pubitemid 41117010)
    • (2005) International Journal of Radiation Biology , vol.81 , Issue.5 , pp. 397-408
    • Varshney, R.1    Dwarakanath, B.S.2    Jain, V.3
  • 164
    • 0003167864 scopus 로고    scopus 로고
    • Modifications of radiation responses by 2-deoxy-d-glucose in normal and cancer cells
    • V. Jain Modifications of radiation responses by 2-deoxy-d-glucose in normal and cancer cells Indian J. Nucl. Med 11 1996 8 17
    • (1996) Indian J. Nucl. Med , vol.11 , pp. 8-17
    • Jain, V.1
  • 165
    • 0037090046 scopus 로고    scopus 로고
    • Heat shock inactivates cellular antioxidant defenses against hydrogen peroxide: Protection by glucose
    • DOI 10.1016/S0891-5849(02)00769-4, PII S0891584902007694
    • S. Lord-Fontaine, and D.A. Averill-Bates Heat shock inactivates cellular antioxidant defenses against hydrogen peroxide: protection by glucose Free Radic. Biol. Med. 32 2002 752 765 (Pubitemid 34286596)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.8 , pp. 752-765
    • Lord-Fontaine, S.1    Averill-Bates, D.A.2
  • 167
    • 3042689052 scopus 로고    scopus 로고
    • Antioxidant enzymes and redox regulating thiol proteins in malignancies of human lung
    • DOI 10.1016/j.febslet.2004.05.045, PII S0014579304006866
    • V.L. Kinnula, P. Pääkko, and Y. Soini Antioxidant enzymes and redox regulating thiol proteins in malignancies of human lung FEBS Lett 569 2004 1 6 (Pubitemid 38844583)
    • (2004) FEBS Letters , vol.569 , Issue.1-3 , pp. 1-6
    • Kinnula, V.L.1    Paakko, P.2    Soini, Y.3
  • 168
    • 80054693822 scopus 로고    scopus 로고
    • Catalase overexpression in mammary cancer cells leads to a less aggressive phenotype and an altered response to chemotherapy
    • C. Glorieux, N. Dejeans, B. Sid, R. Beck, P.B. Calderon, and J. Verrax Catalase overexpression in mammary cancer cells leads to a less aggressive phenotype and an altered response to chemotherapy Biochem. Pharmacol. 82 2011 1384 1390
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 1384-1390
    • Glorieux, C.1    Dejeans, N.2    Sid, B.3    Beck, R.4    Calderon, P.B.5    Verrax, J.6
  • 169
    • 72649092649 scopus 로고    scopus 로고
    • Glutathione peroxidases in different stages of carcinogenesis
    • R. Brigelius-Flohé, and A. Kipp Glutathione peroxidases in different stages of carcinogenesis Biochim. Biophys. Acta 1790 2009 1555 1568
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1555-1568
    • Brigelius-Flohé, R.1    Kipp, A.2
  • 170
    • 80052000670 scopus 로고    scopus 로고
    • Glutathione peroxidase-1 in health and disease: From molecular mechanisms to therapeutic opportunities
    • E. Lubos, J. Loscalzo, and D.E. Handy Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities Antioxid. Redox Signaling 15 2011 1957 1997
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 1957-1997
    • Lubos, E.1    Loscalzo, J.2    Handy, D.E.3
  • 171
    • 1642288979 scopus 로고    scopus 로고
    • Redox regulation of pancreatic cancer cell growth: Role of glutathione peroxidase in the suppression of the malignant phenotype
    • DOI 10.1089/104303404322886093
    • J. Liu, M.M. Hinkhouse, W. Sun, C.J. Weydert, J.M. Ritchie, L.W. Oberley, and J.J. Cullen Redox regulation of pancreatic cancer cell growth: role of glutathione peroxidase in the suppression of the malignant phenotype Hum. Gene Ther. 15 2004 239 250 (Pubitemid 38365913)
    • (2004) Human Gene Therapy , vol.15 , Issue.3 , pp. 239-250
    • Liu, J.1    Hinkhouse, M.M.2    Sun, W.3    Weydert, C.J.4    Ritchie, J.M.5    Oberley, L.W.6    Cullen, J.J.7
  • 172
    • 0030897373 scopus 로고    scopus 로고
    • Enhanced skin carcinogenesis in transgenic mice with high expression of glutathione peroxidase or both glutathione peroxidase and superoxide dismutase
    • Y.P. Lu, Y.R. Lou, P. Yen, H.L. Newmark, O.I. Mirochnitchenko, M. Inouye, and M.T. Huang Enhanced skin carcinogenesis in transgenic mice with high expression of glutathione peroxidase or both glutathione peroxidase and superoxide dismutase Cancer Res. 57 1997 1468 1474 (Pubitemid 27175562)
    • (1997) Cancer Research , vol.57 , Issue.8 , pp. 1468-1474
    • Lu, Y.-P.1    Lou, Y.-R.2    Yen, P.3    Newmark, H.L.4    Mirochnitchenko, O.I.5    Inouye, M.6    Huang, M.-T.7
  • 173
    • 34548080939 scopus 로고    scopus 로고
    • Are peroxiredoxins tumor suppressors?
    • DOI 10.1016/j.coph.2007.04.007, PII S1471489207000951, Cancer/Immunomodulation
    • C.A. Neumann, and Q. Fang Are peroxiredoxins tumor suppressors? Curr. Opin. Pharmacol 7 2007 375 380 (Pubitemid 47289263)
    • (2007) Current Opinion in Pharmacology , vol.7 , Issue.4 , pp. 375-380
    • Neumann, C.A.1    Fang, Q.2
  • 174
    • 71549168293 scopus 로고    scopus 로고
    • Peroxiredoxins, a novel target in cancer radiotherapy
    • B. Zhang, Y. Wang, and Y. Su Peroxiredoxins, a novel target in cancer radiotherapy Cancer Lett. 286 2009 154 160
    • (2009) Cancer Lett. , vol.286 , pp. 154-160
    • Zhang, B.1    Wang, Y.2    Su, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.