메뉴 건너뛰기




Volumn 16, Issue 13, 2009, Pages 1561-1587

Metabolic targeting of cancers: From molecular mechanisms to therapeutic strategies

Author keywords

Fatty acid; Glucose; Glutamine; Metabolic interference; Oncogenic signals; Tumor energy metabolism

Indexed keywords

2,5 ANHYDRO DEXTRO MANNITOL; 3 (3 PYRIDINYL) 1 (4 PYRIDINYL) 2 PROPEN 1 ONE; 6 PHOSPHOFRUCTOKINASE; ALKYLATING AGENT; ANTINEOPLASTIC AGENT; ANTISENSE OLIGONUCLEOTIDE; BROMOPYRUVIC ACID; CHLORAMBUCIL; DEOXYGLUCOSE; DICHLOROACETIC ACID; FATTY ACID SYNTHASE INHIBITOR; FLAVONOL; GLUCOSE TRANSPORTER; GLUFOSFAMIDE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOGEN SYNTHASE KINASE 3BETA; GLYCOGEN SYNTHASE KINASE 3BETA INHIBITOR; GOSSYPOL; HEXOKINASE INHIBITOR; IODOACETIC ACID; LACTATE DEHYDROGENASE; LACTATE DEHYDROGENASE INHIBITOR; LONIDAMINE; MAMMALIAN TARGET OF RAPAMYCIN INHIBITOR; PLATINUM COMPLEX; PROTEIN KINASE B INHIBITOR; PYRUVATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE INHIBITOR; SODIUM GLUCOSE COTRANSPORTER; UNCLASSIFIED DRUG; UNINDEXED DRUG; FATTY ACID; GLUCOSE;

EID: 67650254751     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986709788186255     Document Type: Review
Times cited : (26)

References (221)
  • 1
    • 37449024702 scopus 로고    scopus 로고
    • The biology of cancer:mEtabolic reprogramming fuels cell growth and proliferation
    • DeBerardinis, R.J.; Lum, J.J.; Hatzivassiliou, G.; Thompson, C.B. The biology of cancer:mEtabolic reprogramming fuels cell growth and proliferation. Cell. Metab., 2008, 7, 11-20.
    • (2008) Cell. Metab , vol.7 , pp. 11-20
    • DeBerardinis, R.J.1    Lum, J.J.2    Hatzivassiliou, G.3    Thompson, C.B.4
  • 2
    • 33744969828 scopus 로고    scopus 로고
    • Energy deregulation: Licensing tumors to grow
    • Garber, K. Energy deregulation: Licensing tumors to grow. Science, 2006, 312, 1158-1159.
    • (2006) Science , vol.312 , pp. 1158-1159
    • Garber, K.1
  • 3
    • 52649107626 scopus 로고    scopus 로고
    • Cancer cell metabolism: Warburg and beyond
    • Hsu, P.P.; Sabatini, D.M. Cancer cell metabolism: Warburg and beyond. Cell, 2008, 134, 703-707.
    • (2008) Cell , vol.134 , pp. 703-707
    • Hsu, P.P.1    Sabatini, D.M.2
  • 4
    • 33746879141 scopus 로고    scopus 로고
    • Glycolysis inhibition for anticancer treatment
    • Pelicano, H.; Martin, D.S.; Xu, R.H.; Huang, P. Glycolysis inhibition for anticancer treatment. Oncogene, 2006, 25, 4633-4646.
    • (2006) Oncogene , vol.25 , pp. 4633-4646
    • Pelicano, H.1    Martin, D.S.2    Xu, R.H.3    Huang, P.4
  • 5
    • 34447094919 scopus 로고    scopus 로고
    • Glycolysis in cancer: A potential target for therapy
    • Gatenby, R.A.; Gillies, R.J. Glycolysis in cancer: A potential target for therapy. Int. J. Biochem. Cell Biol., 2007, 39, 1358-1366.
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 1358-1366
    • Gatenby, R.A.1    Gillies, R.J.2
  • 6
    • 38949107594 scopus 로고    scopus 로고
    • Robust metabolic adaptation underlying tumor progression
    • Vizán, P.; Mazurek, S.; Cascante, M. Robust metabolic adaptation underlying tumor progression. Metabolomics, 2008, 4, 1-12.
    • (2008) Metabolomics , vol.4 , pp. 1-12
    • Vizán, P.1    Mazurek, S.2    Cascante, M.3
  • 7
    • 34748912615 scopus 로고    scopus 로고
    • Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis
    • Menendez, J.A.; Lupu, R. Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis. Nat. Rev. Cancer, 2007, 7, 763-777.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 763-777
    • Menendez, J.A.1    Lupu, R.2
  • 9
    • 34250879525 scopus 로고    scopus 로고
    • Tumor metabolism: New opportunities for cancer therapy. Clin. Transl
    • Merida, I.; Avila-Flores, A. Tumor metabolism: New opportunities for cancer therapy. Clin. Transl. Oncol., 2006, 8, 711-716.
    • (2006) Oncol , vol.8 , pp. 711-716
    • Merida, I.1    Avila-Flores, A.2
  • 12
    • 47749116480 scopus 로고    scopus 로고
    • Achilles' heel of cancer: The role of glucose and glutamine metabolism in the survival of transformed cells
    • Yuneva, M. Finding an "Achilles' heel" of cancer: The role of glucose and glutamine metabolism in the survival of transformed cells. Cell Cycle, 2008, 7, 2083-2089.
    • (2008) Cell Cycle , vol.7 , pp. 2083-2089
    • Yuneva1    Finding an, M.2
  • 14
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K.; Zhu, T.; Guan, K.L. TSC2 mediates cellular energy response to control cell growth and survival Cell. 2003, 115, 577-590.
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 15
    • 12544256565 scopus 로고    scopus 로고
    • Inhibition of glycolysis in cancer cells: A novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia
    • Xu, R.H.; Pelicano, H.; Zhou, Y.; Carew, J.S.; Feng, L.; Bhalla, K.N.; Keating, M.J.; Huang, P. Inhibition of glycolysis in cancer cells: A novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia. Cancer Res., 2005, 65, 613-621.
    • (2005) Cancer Res , vol.65 , pp. 613-621
    • Xu, R.H.1    Pelicano, H.2    Zhou, Y.3    Carew, J.S.4    Feng, L.5    Bhalla, K.N.6    Keating, M.J.7    Huang, P.8
  • 16
    • 0028946933 scopus 로고
    • Effects of a ketogenic diet on tumor metabolism and nutritional status in pediatric oncology patients: Two case reports
    • Nebeling, L.C.; Miraldi, F.; Shurin, S.B.; Lerner, E. Effects of a ketogenic diet on tumor metabolism and nutritional status in pediatric oncology patients: Two case reports. J. Am. Coll. Nutr., 1995, 14, 202-208.
    • (1995) J. Am. Coll. Nutr , vol.14 , pp. 202-208
    • Nebeling, L.C.1    Miraldi, F.2    Shurin, S.B.3    Lerner, E.4
  • 17
    • 0037386997 scopus 로고    scopus 로고
    • The ketogenic diet for the treatment of epilepsy: A challenge for nutritional neuroscientists
    • Stafstrom, C.E.; Bough, K.J. The ketogenic diet for the treatment of epilepsy: A challenge for nutritional neuroscientists. Nutr. Neurosci., 2003, 6, 67-79.
    • (2003) Nutr. Neurosci , vol.6 , pp. 67-79
    • Stafstrom, C.E.1    Bough, K.J.2
  • 18
    • 68449101246 scopus 로고    scopus 로고
    • http://www.time.com/time/health/article/0,8599,1662484,00.html (The date of visit: March 8, 2009).
    • http://www.time.com/time/health/article/0,8599,1662484,00.html (The date of visit: March 8, 2009).
  • 20
    • 35448987680 scopus 로고    scopus 로고
    • Complement susceptibility in glutamine deprived breast cancer cells
    • Ellison Bradley, S.; Zanin Mary, K.; Boackle Robert, J. Complement susceptibility in glutamine deprived breast cancer cells. Cell Div., 2007, 2, 20.
    • (2007) Cell Div , vol.2 , pp. 20
    • Ellison Bradley, S.1    Zanin Mary, K.2    Boackle Robert, J.3
  • 21
    • 37149044521 scopus 로고    scopus 로고
    • Molecular mechanisms contributing to glutamine-mediated intestinal cell survival
    • Larson, S.D.; Li, J.; Chung, D.H.; Evers, B.M. Molecular mechanisms contributing to glutamine-mediated intestinal cell survival. Am. J. Physiol., 2007, 293, G1262-G1271.
    • (2007) Am. J. Physiol , vol.293
    • Larson, S.D.1    Li, J.2    Chung, D.H.3    Evers, B.M.4
  • 22
    • 12944265179 scopus 로고    scopus 로고
    • Rapid induction of the intrinsic apoptotic pathway by L-glutamine starvation
    • Paquette, J.C.; Guerin, P.J.; Gauthier, E.R. Rapid induction of the intrinsic apoptotic pathway by L-glutamine starvation. J. Cell. Physiol., 2004, 202, 912-921.
    • (2004) J. Cell. Physiol , vol.202 , pp. 912-921
    • Paquette, J.C.1    Guerin, P.J.2    Gauthier, E.R.3
  • 25
    • 1642494855 scopus 로고    scopus 로고
    • 2-deoxy-D-glucose increases the efficacy of adriamycin and paclitaxel in human osteosarcoma and non-small cell lung cancers in vivo
    • Maschek, G.; Savaraj, N.; Priebe, W.; Braunschweiger, P.; Hamilton, K.; Tidmarsh, G.F.; De Young, L.R.; Lampidis, T.J. 2-deoxy-D-glucose increases the efficacy of adriamycin and paclitaxel in human osteosarcoma and non-small cell lung cancers in vivo. Cancer Res., 2004, 64, 31-34.
    • (2004) Cancer Res , vol.64 , pp. 31-34
    • Maschek, G.1    Savaraj, N.2    Priebe, W.3    Braunschweiger, P.4    Hamilton, K.5    Tidmarsh, G.F.6    De Young, L.R.7    Lampidis, T.J.8
  • 26
    • 68449098224 scopus 로고    scopus 로고
    • Lampidis, T., Priebe, W. PCT WO0182926.
    • Lampidis, T., Priebe, W. PCT WO0182926.
  • 27
    • 13244272100 scopus 로고    scopus 로고
    • RCM-based synthesis of a variety of β-C-glycosides and their in vitro anti-solid tumor activity
    • Postema, M.H.D.; Piper, J.L.; Betts, R.L.; Valeriote, F.A.; Pietraszkewicz, H. RCM-based synthesis of a variety of β-C-glycosides and their in vitro anti-solid tumor activity. J. Org. Chem., 2005, 70, 829-836.
    • (2005) J. Org. Chem , vol.70 , pp. 829-836
    • Postema, M.H.D.1    Piper, J.L.2    Betts, R.L.3    Valeriote, F.A.4    Pietraszkewicz, H.5
  • 30
    • 68449104323 scopus 로고    scopus 로고
    • The date of visit: March 8
    • http://www.thresholdpharm.com/sec/glufosfamide (The date of visit: March 8, 2009).
    • (2009)
  • 31
    • 0033975038 scopus 로고    scopus 로고
    • Mechanistic aspects of the cytotoxic activity of glufosfamide, a new tumour therapeutic agent
    • Seker, H.; Bertram, B.; Burkle, A.; Kaina, B.; Pohl, J.; Koepsell, H.; Wiessler, M. Mechanistic aspects of the cytotoxic activity of glufosfamide, a new tumour therapeutic agent. Br. J. Cancer, 2000, 82, 629-634.
    • (2000) Br. J. Cancer , vol.82 , pp. 629-634
    • Seker, H.1    Bertram, B.2    Burkle, A.3    Kaina, B.4    Pohl, J.5    Koepsell, H.6    Wiessler, M.7
  • 32
    • 34548211906 scopus 로고    scopus 로고
    • A novel alkylating agent, glufosfamide, enhances the activity of gemcitabine in vitro and in vivo
    • Ammons, W.S.; Wang, J.W.; Yang, Z.; Tidmarsh, G.F.; Hoffman, R.M. A novel alkylating agent, glufosfamide, enhances the activity of gemcitabine in vitro and in vivo. Neoplasia, 2007, 9, 625-633.
    • (2007) Neoplasia , vol.9 , pp. 625-633
    • Ammons, W.S.1    Wang, J.W.2    Yang, Z.3    Tidmarsh, G.F.4    Hoffman, R.M.5
  • 36
    • 35348988808 scopus 로고    scopus 로고
    • A glucose derivative as natural alternative to the cyclohexane-1,2-diamine ligand in the anticancer drug oxaliplatin?
    • Berger, I.; Nazarov, A.A.; Hartinger, C.G.; Groessl, M.; Valiahdi, S.M.; Jakupec, M.A.; Keppler, B.K. A glucose derivative as natural alternative to the cyclohexane-1,2-diamine ligand in the anticancer drug oxaliplatin?. ChemMedChem, 2007, 2, 505-514.
    • (2007) ChemMedChem , vol.2 , pp. 505-514
    • Berger, I.1    Nazarov, A.A.2    Hartinger, C.G.3    Groessl, M.4    Valiahdi, S.M.5    Jakupec, M.A.6    Keppler, B.K.7
  • 38
    • 12944262229 scopus 로고    scopus 로고
    • Molecular and cellular regulation of glucose transporter (GLUT) proteins in cancer
    • Macheda, M.L.; Rogers, S.; Best, J.D. Molecular and cellular regulation of glucose transporter (GLUT) proteins in cancer. J. Cell Physiol., 2005, 202, 654-662.
    • (2005) J. Cell Physiol , vol.202 , pp. 654-662
    • Macheda, M.L.1    Rogers, S.2    Best, J.D.3
  • 39
    • 0036077547 scopus 로고    scopus 로고
    • Glucose transporters: Expression, regulation and cancer
    • Medina, R.A.; Owen, G.I. 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
  • 40
    • 0037267005 scopus 로고    scopus 로고
    • Glucose transporters (GLUT and SGLT): Expanded families of sugar transport proteins
    • Wood, I.S.; Trayhurn, P. Glucose transporters (GLUT and SGLT): Expanded families of sugar transport proteins. Br. J. Nutr., 2003, 89, 3-9.
    • (2003) Br. J. Nutr , vol.89 , pp. 3-9
    • Wood, I.S.1    Trayhurn, P.2
  • 42
    • 0017306757 scopus 로고
    • The regulatory principles of glycolysis in erythrocytes in vivo and in vitro. A minimal comprehensive model describing steady states, quasi-steady states and time-dependent processes
    • Rapoport, T.A.; Heinrich, R.; Rapoport, S.M. The regulatory principles of glycolysis in erythrocytes in vivo and in vitro. A minimal comprehensive model describing steady states, quasi-steady states and time-dependent processes. Biochem. J., 1976, 154, 449-469.
    • (1976) Biochem. J , vol.154 , pp. 449-469
    • Rapoport, T.A.1    Heinrich, R.2    Rapoport, S.M.3
  • 43
    • 0022499217 scopus 로고
    • Kinetics of metabolic pathways. A system in vitro to study the control of flux
    • Torres, N.V.; Mateo, F.; Melendez-Hevia, E.; Kacser, H. Kinetics of metabolic pathways. A system in vitro to study the control of flux. Biochem. J., 1986, 234, 169-174.
    • (1986) Biochem. J , vol.234 , pp. 169-174
    • Torres, N.V.1    Mateo, F.2    Melendez-Hevia, E.3    Kacser, H.4
  • 45
    • 35148870732 scopus 로고    scopus 로고
    • Glut-1 antibodies induce growth arrest and apoptosis in human cancer cell lines
    • Rastogi, S.; Banerjee, S.; Chellappan, S.; Simon, G.R. Glut-1 antibodies induce growth arrest and apoptosis in human cancer cell lines. Cancer Lett., 2007, 257, 244-251.
    • (2007) Cancer Lett , vol.257 , pp. 244-251
    • Rastogi, S.1    Banerjee, S.2    Chellappan, S.3    Simon, G.R.4
  • 46
    • 0033612152 scopus 로고    scopus 로고
    • Inhibition of glucose transporter gene expression by antisense nucleic acids in HL-60 leukemia cells
    • Chan, J.Y.; Kong, S.K.; Choy, Y.M.; Lee, C.Y.; Fung, K.P. Inhibition of glucose transporter gene expression by antisense nucleic acids in HL-60 leukemia cells. Life Sci., 1999, 65, 63-70.
    • (1999) Life Sci , vol.65 , pp. 63-70
    • Chan, J.Y.1    Kong, S.K.2    Choy, Y.M.3    Lee, C.Y.4    Fung, K.P.5
  • 47
    • 21644463042 scopus 로고    scopus 로고
    • Inhibition of cell proliferation in human breast tumor cells by antisense oligonucleotides against facilitative glucose transporter 5
    • Chan, K.K.; Chan, J.Y.; Chung, K.K.; Fung, K.P. Inhibition of cell proliferation in human breast tumor cells by antisense oligonucleotides against facilitative glucose transporter 5. J. Cell Biochem., 2004, 93, 1134-1142.
    • (2004) J. Cell Biochem , vol.93 , pp. 1134-1142
    • Chan, K.K.1    Chan, J.Y.2    Chung, K.K.3    Fung, K.P.4
  • 48
    • 0036000133 scopus 로고    scopus 로고
    • Synthesis of antisense oligonucleotide-peptide conjugate targeting to GLUT-1 in HepG-2 and MCF-7 cells
    • Chen, C.P.; Li, X.X.; Zhang, L.R.; Min, J.M.; Chan, J.Y.W.; Fung, K.P.; Wang, S.Q.; Zhang, L.H. Synthesis of antisense oligonucleotide-peptide conjugate targeting to GLUT-1 in HepG-2 and MCF-7 cells. Bioconjugate Chem., 2002, 13, 525-529.
    • (2002) Bioconjugate Chem , vol.13 , pp. 525-529
    • Chen, C.P.1    Li, X.X.2    Zhang, L.R.3    Min, J.M.4    Chan, J.Y.W.5    Fung, K.P.6    Wang, S.Q.7    Zhang, L.H.8
  • 49
    • 34548845307 scopus 로고    scopus 로고
    • Glucosylated heparin derivatives as non-toxic anti-cancer drugs
    • Lee, G.Y.; Kim, S.K.; Byun, Y. Glucosylated heparin derivatives as non-toxic anti-cancer drugs. J. Controlled Release, 2007, 123, 46-55.
    • (2007) J. Controlled Release , vol.123 , pp. 46-55
    • Lee, G.Y.1    Kim, S.K.2    Byun, Y.3
  • 50
    • 0030607725 scopus 로고    scopus 로고
    • Synthesis of glucose-chlorambucil derivatives and their recognition by the human GLUT1 glucose transporter
    • Halmos, T.; Santarromana, M.; Antonakis, K.; Scherman, D. Synthesis of glucose-chlorambucil derivatives and their recognition by the human GLUT1 glucose transporter. Eur. J. Pharmacol., 1996, 318, 477-484.
    • (1996) Eur. J. Pharmacol , vol.318 , pp. 477-484
    • Halmos, T.1    Santarromana, M.2    Antonakis, K.3    Scherman, D.4
  • 52
    • 33846803914 scopus 로고    scopus 로고
    • Inhibition of the intestinal glucose transporter GLUT2 by flavonoids
    • Kwon, O.; Eck, P.; Chen, S.; Corpe, C.P.; Lee, J.H.; Kruhlak, M.; Levine, M. Inhibition of the intestinal glucose transporter GLUT2 by flavonoids. FASEB J, 2007, 21, 366-377.
    • (2007) FASEB J , vol.21 , pp. 366-377
    • Kwon, O.1    Eck, P.2    Chen, S.3    Corpe, C.P.4    Lee, J.H.5    Kruhlak, M.6    Levine, M.7
  • 53
    • 3342944401 scopus 로고    scopus 로고
    • Naringenin inhibits glucose uptake in MCF-7 breast cancer cells: A mechanism for impaired cellular proliferation
    • Harmon, A.W.; Patel, Y.M. Naringenin inhibits glucose uptake in MCF-7 breast cancer cells: A mechanism for impaired cellular proliferation. Breast Cancer Res. Treat., 2004, 85, 103-110.
    • (2004) Breast Cancer Res. Treat , vol.85 , pp. 103-110
    • Harmon, A.W.1    Patel, Y.M.2
  • 54
    • 0033933720 scopus 로고    scopus 로고
    • Synthesis and evaluation of fructose analogues as inhibitors of the D-fructose transporter GLUT5
    • Tatibouet, A.; Yang, J.; Morin, C.; Holman, G.D. Synthesis and evaluation of fructose analogues as inhibitors of the D-fructose transporter GLUT5. Bioorg. Med. Chem., 2000, 8, 1825-1833.
    • (2000) Bioorg. Med. Chem , vol.8 , pp. 1825-1833
    • Tatibouet, A.1    Yang, J.2    Morin, C.3    Holman, G.D.4
  • 55
    • 0037418787 scopus 로고    scopus 로고
    • Inhibition of the D-fructose transporter protein GLUT5 by fused-ring glyco-1,3-oxazolidin-2-thiones and -oxazolidin-2-ones
    • Girniene, J.; Tatibouet, A.; Sackus, A.; Yang, J.; Holman, G.D.; Rollin, P. Inhibition of the D-fructose transporter protein GLUT5 by fused-ring glyco-1,3-oxazolidin-2-thiones and -oxazolidin-2-ones. Carbohydr. Res., 2003, 338, 711-719.
    • (2003) Carbohydr. Res , vol.338 , pp. 711-719
    • Girniene, J.1    Tatibouet, A.2    Sackus, A.3    Yang, J.4    Holman, G.D.5    Rollin, P.6
  • 59
    • 42949176742 scopus 로고    scopus 로고
    • Survival of cancer cells is maintained by EGFR independent of its kinase activity
    • Weihua, Z.; Tsan, R.; Huang, W.C.; Wu, Q.; Chiu, C.H.; Fidler, I.J.; Hung, M.C. Survival of cancer cells is maintained by EGFR independent of its kinase activity. Cancer Cell, 2008, 13, 385-393.
    • (2008) Cancer Cell , vol.13 , pp. 385-393
    • Weihua, Z.1    Tsan, R.2    Huang, W.C.3    Wu, Q.4    Chiu, C.H.5    Fidler, I.J.6    Hung, M.C.7
  • 61
    • 33746218416 scopus 로고    scopus 로고
    • GSK-3beta as a driving force in ovarian cancer
    • Li, D. GSK-3beta as a driving force in ovarian cancer. Cell Res., 2006, 16, 609.
    • (2006) Cell Res , vol.16 , pp. 609
    • Li, D.1
  • 62
    • 0036273020 scopus 로고    scopus 로고
    • Martinez, A.; Castro, A.; Dorronsoro, I.; Alonso, M. Glycogen synthase kinase 3 (GSK-3) inhibitors as new promising drugs for diabetes, neurodegeneration, cancer, and inflammation. Med. Res. Rev., 2002, 22, 373-384.
    • Martinez, A.; Castro, A.; Dorronsoro, I.; Alonso, M. Glycogen synthase kinase 3 (GSK-3) inhibitors as new promising drugs for diabetes, neurodegeneration, cancer, and inflammation. Med. Res. Rev., 2002, 22, 373-384.
  • 63
    • 0033014180 scopus 로고    scopus 로고
    • The mood-stabilizing agent valproate inhibits the activity of glycogen synthase kinase-3
    • Chen, G.; Huang, L.D.; Jiang, Y.M.; Manji, H.K. The mood-stabilizing agent valproate inhibits the activity of glycogen synthase kinase-3. J. Neurochem., 1999, 72, 1327-1330.
    • (1999) J. Neurochem , vol.72 , pp. 1327-1330
    • Chen, G.1    Huang, L.D.2    Jiang, Y.M.3    Manji, H.K.4
  • 65
    • 0037387215 scopus 로고    scopus 로고
    • Lahusen, T.; de Siervi, A.; Kunick, C.; Senderowica, A.M. Alsterpaullone, a novel cyclin-dependent kinase inhibitor, induces apoptosis by activation of caspase-9 due to perturbation in mitochondrial membrane potential. Mol. Carcinog., 2003, 36, 183-194.
    • Lahusen, T.; de Siervi, A.; Kunick, C.; Senderowica, A.M. Alsterpaullone, a novel cyclin-dependent kinase inhibitor, induces apoptosis by activation of caspase-9 due to perturbation in mitochondrial membrane potential. Mol. Carcinog., 2003, 36, 183-194.
  • 66
    • 8144228566 scopus 로고    scopus 로고
    • Why do cancers have high aerobic glycolysis?
    • Gatenby, R.A.; Gillies, R.J. Why do cancers have high aerobic glycolysis? Nat. Rev. Cancer, 2004, 4, 891-899
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 891-899
    • Gatenby, R.A.1    Gillies, R.J.2
  • 67
    • 14744284637 scopus 로고    scopus 로고
    • Multifaceted roles of glycolytic enzymes
    • Kim, J.W.; Dang, C.V. Multifaceted roles of glycolytic enzymes. Trends Biochem. Sci., 2005, 30, 142-150.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 142-150
    • Kim, J.W.1    Dang, C.V.2
  • 69
    • 33750619348 scopus 로고    scopus 로고
    • Glucose metabolism and cancer
    • Shaw, R.J. Glucose metabolism and cancer. Curr. Opin. Cell Biol., 2006, 18, 598-608.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 598-608
    • Shaw, R.J.1
  • 71
    • 33746927077 scopus 로고    scopus 로고
    • Mitochondrial hexokinases, novel mediators of the antiapoptotic effects of growth factors and Akt
    • Robey, R.B.; Hay, N. Mitochondrial hexokinases, novel mediators of the antiapoptotic effects of growth factors and Akt. Oncogene, 2006, 25, 4683-4696.
    • (2006) Oncogene , vol.25 , pp. 4683-4696
    • Robey, R.B.1    Hay, N.2
  • 73
    • 32044448517 scopus 로고    scopus 로고
    • 2-Deoxyglucose: An anticancer and antiviral therapeutic, but not any more a low glucose mimetic
    • Kang, H.T.; Hwang, E.S. 2-Deoxyglucose: An anticancer and antiviral therapeutic, but not any more a low glucose mimetic. Life Sci., 2006, 78, 1392-1399.
    • (2006) Life Sci , vol.78 , pp. 1392-1399
    • Kang, H.T.1    Hwang, E.S.2
  • 74
    • 0037114462 scopus 로고
    • Hypoxia increases tumor cell sensitivity to glycolytic inhibitors: A strategy for solid tumor therapy (Model C)
    • Liu, H.; Savaraj, N.; Priebe, W.; Lampidis, T.J. Hypoxia increases tumor cell sensitivity to glycolytic inhibitors: A strategy for solid tumor therapy (Model C). Biochem. Pharmacol., 2002, 64, 1745-1751.
    • (1745) Biochem. Pharmacol , vol.2002 , pp. 64
    • Liu, H.1    Savaraj, N.2    Priebe, W.3    Lampidis, T.J.4
  • 75
    • 0442313668 scopus 로고    scopus 로고
    • Greater cell cycle inhibition and cytotoxicity induced by 2-deoxy-D-glucose in tumor cells treated under hypoxic vs aerobic conditions
    • Maher, J.C.; Krishan, A.; Lampidis, T.J. Greater cell cycle inhibition and cytotoxicity induced by 2-deoxy-D-glucose in tumor cells treated under hypoxic vs aerobic conditions. Cancer Chemother. Pharmacol., 2004, 53, 116-122.
    • (2004) Cancer Chemother. Pharmacol , vol.53 , pp. 116-122
    • Maher, J.C.1    Krishan, A.2    Lampidis, T.J.3
  • 78
    • 35448961939 scopus 로고    scopus 로고
    • The Warburg effect and its cancer therapeutic implications
    • Chen, Z.; Lu, W.; Garcia-Prieto, C.; Huang, P. The Warburg effect and its cancer therapeutic implications. J. Bioenerg. Biomembr., 2007, 39, 267-274.
    • (2007) J. Bioenerg. Biomembr , vol.39 , pp. 267-274
    • Chen, Z.1    Lu, W.2    Garcia-Prieto, C.3    Huang, P.4
  • 79
    • 33645124651 scopus 로고    scopus 로고
    • Lonidamine: Basic science and rationale for treatment of prostatic proliferative disorders
    • Brawer, M.K. Lonidamine: Basic science and rationale for treatment of prostatic proliferative disorders. Rev. Urol., 2005, 7 Suppl 7, S21-S26.
    • (2005) Rev. Urol , vol.7 , Issue.SUPPL. 7
    • Brawer, M.K.1
  • 84
    • 52949113383 scopus 로고    scopus 로고
    • Effects of the Anti-Tumor Agent 3-Bromopyruvate (3BrPA) on Glycolytic Energy Metabolism
    • Robey, R.B.; Hong, R.; Zhong, L.; Feng, L.; Zhang, H. Effects of the Anti-Tumor Agent 3-Bromopyruvate (3BrPA) on Glycolytic Energy Metabolism. FASEB J., 2007, 21, 890-896.
    • (2007) FASEB J , vol.21 , pp. 890-896
    • Robey, R.B.1    Hong, R.2    Zhong, L.3    Feng, L.4    Zhang, H.5
  • 85
    • 33845526182 scopus 로고    scopus 로고
    • Local toxicity of hepatic arterial infusion of hexokinase II inhibitor, 3-bromopyruvate: In vivo investigation in normal rabbit model
    • Chang, J.M.; Chung, J.W.; Jae, H.J.; Eh, H.; Son, K.R.; Lee, K.C.; Park, J.H. Local toxicity of hepatic arterial infusion of hexokinase II inhibitor, 3-bromopyruvate: In vivo investigation in normal rabbit model. Acad. Radiol., 2007, 14, 85-92.
    • (2007) Acad. Radiol , vol.14 , pp. 85-92
    • Chang, J.M.1    Chung, J.W.2    Jae, H.J.3    Eh, H.4    Son, K.R.5    Lee, K.C.6    Park, J.H.7
  • 87
    • 12544256565 scopus 로고    scopus 로고
    • Inhibition of glycolysis in cancer cells: A novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia
    • Xu, R.H.; Pelicano, H.; Zhou, Y.; Carew, J.S.; Feng, L.; Bhalla, K.N.; Keating, M.J.; Huang, P. Inhibition of glycolysis in cancer cells: A novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia. Cancer Res., 2005, 65, 613-621.
    • (2005) Cancer Res , vol.65 , pp. 613-621
    • Xu, R.H.1    Pelicano, H.2    Zhou, Y.3    Carew, J.S.4    Feng, L.5    Bhalla, K.N.6    Keating, M.J.7    Huang, P.8
  • 89
    • 0141863388 scopus 로고    scopus 로고
    • Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival
    • 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., 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
  • 90
    • 23844517036 scopus 로고    scopus 로고
    • Phosphorylation of the 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase/PFKFB3 family of glycolytic regulators in human cancer
    • Bando, H.; Atsumi, T.; Nishio, T.; Niwa, H.; Mishima, S.; Shimizu, C.; Yoshioka, N.; Bucala, R.; Koike, T. Phosphorylation of the 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase/PFKFB3 family of glycolytic regulators in human cancer. Clin. Cancer Res., 2005, 11, 5784-5792.
    • (2005) Clin. Cancer Res , vol.11 , pp. 5784-5792
    • Bando, H.1    Atsumi, T.2    Nishio, T.3    Niwa, H.4    Mishima, S.5    Shimizu, C.6    Yoshioka, N.7    Bucala, R.8    Koike, T.9
  • 91
    • 33747505788 scopus 로고    scopus 로고
    • 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and tumor cell glycolysis
    • Chesney, J. 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and tumor cell glycolysis. Curr. Opin. Clin. Nutr. Metab. Care, 2006, 9, 535-539.
    • (2006) Curr. Opin. Clin. Nutr. Metab. Care , vol.9 , pp. 535-539
    • Chesney, J.1
  • 95
    • 33644662620 scopus 로고    scopus 로고
    • Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase
    • Ismail, S.A.; Park, H.W. Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallogr. D Biol. Crystallogr., 2005, 61, 1508-1513.
    • (2005) Acta Crystallogr. D Biol. Crystallogr , vol.61 , pp. 1508-1513
    • Ismail, S.A.1    Park, H.W.2
  • 96
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • Lin, S.J.; Guarente, L. Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr. Opin. Cell Biol., 2003, 15, 241-246.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 241-246
    • Lin, S.J.1    Guarente, L.2
  • 98
    • 34547558087 scopus 로고    scopus 로고
    • GAPDH and the search for alternative energy
    • Song, S.; Finkel, T. GAPDH and the search for alternative energy. Nat. Cell Biol., 2007, 9, 869-870.
    • (2007) Nat. Cell Biol , vol.9 , pp. 869-870
    • Song, S.1    Finkel, T.2
  • 100
    • 68449095689 scopus 로고    scopus 로고
    • Lai1, J.C.K.; Bhardwaj, V.; Rizvi, N.; Chatterji, T.; Isaac, A.O.; Lai, M.B.; Johnson, T.; Leung, S.W.; Daniels, C.K.; Bhushan, A., Glycolytic enzyme inhibitors as novel anti-cancer drugs. The Northwest Regional Meeting, 2007, June 17-20, Boise, ID.
    • Lai1, J.C.K.; Bhardwaj, V.; Rizvi, N.; Chatterji, T.; Isaac, A.O.; Lai, M.B.; Johnson, T.; Leung, S.W.; Daniels, C.K.; Bhushan, A., Glycolytic enzyme inhibitors as novel anti-cancer drugs. The Northwest Regional Meeting, 2007, June 17-20, Boise, ID.
  • 101
    • 45949094910 scopus 로고    scopus 로고
    • Targeting Bcl-2 family members with the BH3 mimetic AT-101 markedly enhances the therapeutic effects of chemotherapeutic agents in in vitro and in vivo models of B-cell lymphoma
    • Paoluzzi, L.; Gonen, M.; Gardner, J.R.; Mastrella, J.; Yang, D.; Holmlund, J.; Sorensen, M.; Leopold, L.; Manova, K.; Marcucci, G.; Heaney, M.L.; O'Connor, O.A. Targeting Bcl-2 family members with the BH3 mimetic AT-101 markedly enhances the therapeutic effects of chemotherapeutic agents in in vitro and in vivo models of B-cell lymphoma. Blood, 2008, 111, 5350-5361.
    • (2008) Blood , vol.111 , pp. 5350-5361
    • Paoluzzi, L.1    Gonen, M.2    Gardner, J.R.3    Mastrella, J.4    Yang, D.5    Holmlund, J.6    Sorensen, M.7    Leopold, L.8    Manova, K.9    Marcucci, G.10    Heaney, M.L.11    O'Connor, O.A.12
  • 102
    • 23044500915 scopus 로고    scopus 로고
    • Pyruvate kinase type M2 and its role in tumor growth and spreading
    • Mazurek, S.; Boschek, C.B.; Hugo, F.; Eigenbrodt, E. Pyruvate kinase type M2 and its role in tumor growth and spreading. Semin. Cancer Biol., 2005, 15, 300-308.
    • (2005) Semin. Cancer Biol , vol.15 , pp. 300-308
    • Mazurek, S.1    Boschek, C.B.2    Hugo, F.3    Eigenbrodt, E.4
  • 103
    • 0035983766 scopus 로고    scopus 로고
    • Synthesis of phosphoenol pyruvate (PEP) analogues and evaluation as inhibitors of PEP-utilizing enzymes
    • Garcia-Alles, L.F.; Erni, B. Synthesis of phosphoenol pyruvate (PEP) analogues and evaluation as inhibitors of PEP-utilizing enzymes. Eur. J. Biochem., 2002, 269, 3226-3236.
    • (2002) Eur. J. Biochem , vol.269 , pp. 3226-3236
    • Garcia-Alles, L.F.1    Erni, B.2
  • 105
    • 68449100673 scopus 로고    scopus 로고
    • The date of visit: March 8
    • http://www.thallion.com/en/index.php (The date of visit: March 8, 2009).
    • (2009)
  • 106
    • 43249126494 scopus 로고    scopus 로고
    • Factors associated with outcome in patients with advanced renal cell carcinoma in the era of antiangiogenic agents
    • Choueiri, T.K. Factors associated with outcome in patients with advanced renal cell carcinoma in the era of antiangiogenic agents. Clin. Genitourin Cancer, 2008, 6, 15-20.
    • (2008) Clin. Genitourin Cancer , vol.6 , pp. 15-20
    • Choueiri, T.K.1
  • 107
    • 48149091757 scopus 로고    scopus 로고
    • Lactate dehydrogenase-5 (LDH-5) expression in human gastric cancer: Association with hypoxia-inducible factor (HIF-1alpha) pathway, angiogenic factors production and poor prognosis
    • Kolev, Y.; Uetake, H.; Takagi, Y.; Sugihara, K. Lactate dehydrogenase-5 (LDH-5) expression in human gastric cancer: Association with hypoxia-inducible factor (HIF-1alpha) pathway, angiogenic factors production and poor prognosis. Ann. Surg. Oncol., 2008, 15, 2336-2344.
    • (2008) Ann. Surg. Oncol , vol.15 , pp. 2336-2344
    • Kolev, Y.1    Uetake, H.2    Takagi, Y.3    Sugihara, K.4
  • 108
    • 33744783432 scopus 로고    scopus 로고
    • Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance
    • Fantin, V.R.; St-Pierre, J.; Leder, P. Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance. Cancer Cell, 2006, 9, 425-434.
    • (2006) Cancer Cell , vol.9 , pp. 425-434
    • Fantin, V.R.1    St-Pierre, J.2    Leder, P.3
  • 109
    • 34548069772 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of Plasmodium falciparum lactate dehydrogenase inhibitors
    • Choi, S.R.; Pradhan, A.; Hammond, N.L.; Chittiboyina, A.G.; Tekwani, B.L.; Avery, M.A. Design, synthesis, and biological evaluation of Plasmodium falciparum lactate dehydrogenase inhibitors. J. Med. Chem., 2007, 50, 3841-3850.
    • (2007) J. Med. Chem , vol.50 , pp. 3841-3850
    • Choi, S.R.1    Pradhan, A.2    Hammond, N.L.3    Chittiboyina, A.G.4    Tekwani, B.L.5    Avery, M.A.6
  • 112
    • 68449095688 scopus 로고    scopus 로고
    • The date of visit: March 8
    • http://www.medicorcancer.com/DCAtherapy.html (The date of visit: March 8, 2009)
    • (2009)
  • 113
    • 34249945104 scopus 로고    scopus 로고
    • The cancer cell's "power plants" as promising therapeutic targets: An overview
    • Pedersen, P.L. The cancer cell's "power plants" as promising therapeutic targets: An overview. J. Bioenerg. Biomembr., 2007, 39, 1-12.
    • (2007) J. Bioenerg. Biomembr , vol.39 , pp. 1-12
    • Pedersen, P.L.1
  • 114
    • 0017306750 scopus 로고
    • L-lactate transport in Ehrlich ascites-tumour cells
    • Spencer, T.L.; Lehninger, A.L. L-lactate transport in Ehrlich ascites-tumour cells. Biochem. J., 1976, 154, 405-414.
    • (1976) Biochem. J , vol.154 , pp. 405-414
    • Spencer, T.L.1    Lehninger, A.L.2
  • 115
    • 0019304867 scopus 로고
    • Inhibition of lactate transport in Ehrlich ascites tumor cells and human erythrocytes by a synthetic anhydride of lactic acid
    • Johnson, J.H.; Belt, J.A.; Dubinsky, W.P.; Zimniak, A.; Racker, E. Inhibition of lactate transport in Ehrlich ascites tumor cells and human erythrocytes by a synthetic anhydride of lactic acid. Biochemistry, 1980, 19, 3836-3840.
    • (1980) Biochemistry , vol.19 , pp. 3836-3840
    • Johnson, J.H.1    Belt, J.A.2    Dubinsky, W.P.3    Zimniak, A.4    Racker, E.5
  • 116
    • 10044278250 scopus 로고    scopus 로고
    • Silencing of monocarboxylate transporters via small interfering ribonucleic acid inhibits glycolysis and induces cell death in malignant glioma: An in vitro study
    • Mathupala, S.P.; Parajuli, P.; Sloan, A.E. Silencing of monocarboxylate transporters via small interfering ribonucleic acid inhibits glycolysis and induces cell death in malignant glioma: An in vitro study. Neurosurgery, 2004, 55, 1410-1419.
    • (2004) Neurosurgery , vol.55 , pp. 1410-1419
    • Mathupala, S.P.1    Parajuli, P.2    Sloan, A.E.3
  • 117
    • 33751091519 scopus 로고    scopus 로고
    • The H+-linked monocarboxylate transporter (MCT1/SLC16A1): A potential therapeutic target for high-risk neuroblastoma
    • Fang, J.; Quinones, Q.J.; Holman, T.L.; Morowitz, M.J.; Wang, Q.; Zhao, H,; Sivo, F.; Maris, J.M.; Wahl, M.L. The H+-linked monocarboxylate transporter (MCT1/SLC16A1): A potential therapeutic target for high-risk neuroblastoma. Mol. Pharmacol., 2006, 70, 2108-2115.
    • (2006) Mol. Pharmacol , vol.70 , pp. 2108-2115
    • Fang, J.1    Quinones, Q.J.2    Holman, T.L.3    Morowitz, M.J.4    Wang, Q.5    Zhao, H.6    Sivo, F.7    Maris, J.M.8    Wahl, M.L.9
  • 118
    • 36349001899 scopus 로고    scopus 로고
    • Targeting vacuolar H+-ATPases as a new strategy against cancer
    • Fais, S.; De Milito, A.; You, H.; Qin, W. Targeting vacuolar H+-ATPases as a new strategy against cancer. Cancer Res., 2007, 67, 10627-10630.
    • (2007) Cancer Res , vol.67 , pp. 10627-10630
    • Fais, S.1    De Milito, A.2    You, H.3    Qin, W.4
  • 119
    • 0242577147 scopus 로고    scopus 로고
    • Acetate and butyrate are the major substrates for de novo lipogenesis in rat colonic epithelial cells
    • Zambell, K.L.; Fitch, M.D.; Fleming, S.E. Acetate and butyrate are the major substrates for de novo lipogenesis in rat colonic epithelial cells. J. Nutr., 2003, 133, 3509-3515.
    • (2003) J. Nutr , vol.133 , pp. 3509-3515
    • Zambell, K.L.1    Fitch, M.D.2    Fleming, S.E.3
  • 120
    • 0024315871 scopus 로고
    • Fatty acid synthase, a proficient multifunctional enzyme
    • Wakil, S.J. Fatty acid synthase, a proficient multifunctional enzyme. Biochemistry, 1989, 28, 4523-4530.
    • (1989) Biochemistry , vol.28 , pp. 4523-4530
    • Wakil, S.J.1
  • 122
    • 2542445809 scopus 로고    scopus 로고
    • Fatty acid synthase: A metabolic oncogene in prostate cancer?
    • Baron, A.; Migita, T.; Tang, D.; Loda, M. Fatty acid synthase: A metabolic oncogene in prostate cancer? J. Cell Biochem., 2004, 91, 47-53.
    • (2004) J. Cell Biochem , vol.91 , pp. 47-53
    • Baron, A.1    Migita, T.2    Tang, D.3    Loda, M.4
  • 123
    • 33748260777 scopus 로고    scopus 로고
    • Fatty acid oxidation is a dominant bioenergetic pathway in prostate cancer
    • Liu, Y. Fatty acid oxidation is a dominant bioenergetic pathway in prostate cancer. Prostate Cancer Prostatic Dis., 2006, 9, 230-234.
    • (2006) Prostate Cancer Prostatic Dis , vol.9 , pp. 230-234
    • Liu, Y.1
  • 126
    • 0029949512 scopus 로고    scopus 로고
    • Inhibition of fatty acid synthesis induces programmed cell death in human breast cancer cells
    • Pizer, E.S.; Jackisch, C.; Wood, F.D.; Pasternack, G.R.; Davidson, N.E.; Kuhajda, F.P. Inhibition of fatty acid synthesis induces programmed cell death in human breast cancer cells. Cancer Res., 1996, 56, 2745-2747.
    • (1996) Cancer Res , vol.56 , pp. 2745-2747
    • Pizer, E.S.1    Jackisch, C.2    Wood, F.D.3    Pasternack, G.R.4    Davidson, N.E.5    Kuhajda, F.P.6
  • 127
    • 0029971427 scopus 로고    scopus 로고
    • Inhibition of fatty acid synthesis delays disease progression in a xenograft model of ovarian cancer
    • Pizer, E.S.; Wood, F.D.; Heine, H.S.; Romantsev, F.E.; Pasternack, G.R.; Kuhajda, F.P. Inhibition of fatty acid synthesis delays disease progression in a xenograft model of ovarian cancer. Cancer Res., 1996, 56, 1189-1193.
    • (1996) Cancer Res , vol.56 , pp. 1189-1193
    • Pizer, E.S.1    Wood, F.D.2    Heine, H.S.3    Romantsev, F.E.4    Pasternack, G.R.5    Kuhajda, F.P.6
  • 128
    • 0035133059 scopus 로고    scopus 로고
    • Increased fatty acid synthase is a therapeutic target in mesothelioma
    • Gabrielson, E.W.; Pinn, M.L.; Testa, J.R.; Kuhajda, F.P. Increased fatty acid synthase is a therapeutic target in mesothelioma. Clin. Cancer Res., 2001, 7, 153-157.
    • (2001) Clin. Cancer Res , vol.7 , pp. 153-157
    • Gabrielson, E.W.1    Pinn, M.L.2    Testa, J.R.3    Kuhajda, F.P.4
  • 129
    • 19944374798 scopus 로고    scopus 로고
    • Positive feedback regulation between AKT activation and fatty acid synthase expression in ovarian carcinoma cells
    • Wang, H.Q.; Altomare, D.A.; Skele, K.L.; Poulikakos, P.I.; Kuhajda, F.P.; Di Cristofano, A.; Testa, J.R. Positive feedback regulation between AKT activation and fatty acid synthase expression in ovarian carcinoma cells. Oncogene, 2005, 24, 3574-3582
    • (2005) Oncogene , vol.24 , pp. 3574-3582
    • Wang, H.Q.1    Altomare, D.A.2    Skele, K.L.3    Poulikakos, P.I.4    Kuhajda, F.P.5    Di Cristofano, A.6    Testa, J.R.7
  • 131
    • 12444252156 scopus 로고    scopus 로고
    • Fatty acid synthase inhibitors are chemopreventive for mammary cancer in neu-N transgenic mice
    • Alli, P.M.; Pinn, M.L.; Jaffee, E.M.; McFadden, J.M.; Kuhajda, F.P. Fatty acid synthase inhibitors are chemopreventive for mammary cancer in neu-N transgenic mice. Oncogene, 2005, 24, 39-46
    • (2005) Oncogene , vol.24 , pp. 39-46
    • Alli, P.M.1    Pinn, M.L.2    Jaffee, E.M.3    McFadden, J.M.4    Kuhajda, F.P.5
  • 132
    • 0035794127 scopus 로고    scopus 로고
    • Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism
    • Price, A.C.; Choi, K.H.; Heath, R.J.; Li, Z.; White, S.W.; Rock, C.O. Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism. J. Biol. Chem., 2001, 276, 6551-6559.
    • (2001) J. Biol. Chem , vol.276 , pp. 6551-6559
    • Price, A.C.1    Choi, K.H.2    Heath, R.J.3    Li, Z.4    White, S.W.5    Rock, C.O.6
  • 133
    • 0034650757 scopus 로고    scopus 로고
    • Malonyl-coenzyme-A is a potential mediator of cytotoxicity induced by fatty-acid synthase inhibition in human breast cancer cells and xenografts
    • Pizer, E.S.; Thupari, J.; Han, W.F.; Pinn, M.L.; Chrest, F.J.; Frehywot, G.L.; Townsend, C.A.; Kuhajda, F.P. Malonyl-coenzyme-A is a potential mediator of cytotoxicity induced by fatty-acid synthase inhibition in human breast cancer cells and xenografts. Cancer Res., 2000, 60, 213.
    • (2000) Cancer Res , vol.60 , pp. 213
    • Pizer, E.S.1    Thupari, J.2    Han, W.F.3    Pinn, M.L.4    Chrest, F.J.5    Frehywot, G.L.6    Townsend, C.A.7    Kuhajda, F.P.8
  • 134
    • 1542720382 scopus 로고    scopus 로고
    • Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity
    • Kridel, S.J.; Axelrod, F.; Rozenkrantz, N.; Smith, J.W. Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity. Cancer Res., 2004, 64, 2070-2075.
    • (2004) Cancer Res , vol.64 , pp. 2070-2075
    • Kridel, S.J.1    Axelrod, F.2    Rozenkrantz, N.3    Smith, J.W.4
  • 135
    • 3142713030 scopus 로고    scopus 로고
    • A fatty acid synthase blockade induces tumor cell-cycle arrest by down-regulating Skp2
    • Knowles, L.M.; Axelrod, F.; Browne, C.D.; Smith, J.W. A fatty acid synthase blockade induces tumor cell-cycle arrest by down-regulating Skp2. J. Biol. Chem., 2004, 279, 30540-30545.
    • (2004) J. Biol. Chem , vol.279 , pp. 30540-30545
    • Knowles, L.M.1    Axelrod, F.2    Browne, C.D.3    Smith, J.W.4
  • 137
    • 33750075043 scopus 로고    scopus 로고
    • Total synthesis and comparative analysis of orlistat, valilactone, and a transposed orlistat derivative: Inhibitors of fatty acid synthase
    • Ma, G.; Zancanella, M.; Oyola, Y.; Richardson, R.D.; Smith, J.W.; Romo, D. Total synthesis and comparative analysis of orlistat, valilactone, and a transposed orlistat derivative: inhibitors of fatty acid synthase. Org. Lett., 2006, 8, 4497-4500.
    • (2006) Org. Lett , vol.8 , pp. 4497-4500
    • Ma, G.1    Zancanella, M.2    Oyola, Y.3    Richardson, R.D.4    Smith, J.W.5    Romo, D.6
  • 138
    • 33744898777 scopus 로고    scopus 로고
    • Practical, catalytic, asymmetric synthesis of β-lactones via a sequential ketene dimerization/hydrogenation process: Inhibitors of the thioesterase domain of fatty acid synthase
    • Purohit, V.C.; Richardson, R.D.; Smith, J.W.; Romo, D. Practical, catalytic, asymmetric synthesis of β-lactones via a sequential ketene dimerization/hydrogenation process: Inhibitors of the thioesterase domain of fatty acid synthase. J. Org. Chem., 2006, 71, 4549-4558.
    • (2006) J. Org. Chem , vol.71 , pp. 4549-4558
    • Purohit, V.C.1    Richardson, R.D.2    Smith, J.W.3    Romo, D.4
  • 139
    • 32944475076 scopus 로고    scopus 로고
    • Structure-activity relationship of polyphenols that inhibit fatty acid synthase
    • Li, B.H.; Ma, X.F.; Wang, Y.; Tian, W.X. Structure-activity relationship of polyphenols that inhibit fatty acid synthase. J. Biochem. (Tokyo), 2005, 138, 679-685.
    • (2005) J. Biochem. (Tokyo) , vol.138 , pp. 679-685
    • Li, B.H.1    Ma, X.F.2    Wang, Y.3    Tian, W.X.4
  • 140
    • 0035900577 scopus 로고    scopus 로고
    • Green tea epigallocatechin gallate: A natural inhibitor of fatty-acid synthase
    • Wang, X.; Tian, W. Green tea epigallocatechin gallate: A natural inhibitor of fatty-acid synthase. Biochem. Biophys. Res. Commun., 2001, 288, 1200-1206.
    • (2001) Biochem. Biophys. Res. Commun , vol.288 , pp. 1200-1206
    • Wang, X.1    Tian, W.2
  • 141
    • 0041337028 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate is a potent natural inhibitor of fatty acid synthase in intact cells and selectively induces apoptosis in prostate cancer cells
    • Brusselmans, K.; De Schrijver, E.; Heyns, W.; Verhoeven, G.; Swinnen, J.V. Epigallocatechin-3-gallate is a potent natural inhibitor of fatty acid synthase in intact cells and selectively induces apoptosis in prostate cancer cells. Int. J. Cancer, 2003, 106, 856-862.
    • (2003) Int. J. Cancer , vol.106 , pp. 856-862
    • Brusselmans, K.1    De Schrijver, E.2    Heyns, W.3    Verhoeven, G.4    Swinnen, J.V.5
  • 142
    • 14044267753 scopus 로고    scopus 로고
    • Induction of cancer cell apoptosis by flavonoids is associated with their ability to inhibit fatty acid synthase activity
    • Brusselmans, K.; Vrolix, R.; Verhoeven, G.; Swinnen, J.V. Induction of cancer cell apoptosis by flavonoids is associated with their ability to inhibit fatty acid synthase activity. J. Biol. Chem., 2005, 280, 5636-5645.
    • (2005) J. Biol. Chem , vol.280 , pp. 5636-5645
    • Brusselmans, K.1    Vrolix, R.2    Verhoeven, G.3    Swinnen, J.V.4
  • 143
    • 1642503947 scopus 로고    scopus 로고
    • Inhibitory effects of flavonoids on animal fatty acid synthase
    • Li, B.H.; Tian, W.X. Inhibitory effects of flavonoids on animal fatty acid synthase. J. Biochem., 2004, 135, 85-91.
    • (2004) J. Biochem , vol.135 , pp. 85-91
    • Li, B.H.1    Tian, W.X.2
  • 144
    • 0018769394 scopus 로고
    • Lipogenetic and glycolytic enzyme activities in carcinoma and nonmalignant diseases of the human breast
    • Szutowicz, A.; Kwiatkowski, J.; Angielski, S. Lipogenetic and glycolytic enzyme activities in carcinoma and nonmalignant diseases of the human breast. Br. J. Cancer, 1979, 39, 681-687.
    • (1979) Br. J. Cancer , vol.39 , pp. 681-687
    • Szutowicz, A.1    Kwiatkowski, J.2    Angielski, S.3
  • 146
    • 0032529044 scopus 로고    scopus 로고
    • The role of ATP citrate-lyase in the metabolic regulation of plasma lipids. Hypolipidaemic effects of SB-204990, a lactone prodrug of the potent ATP citrate-lyase inhibitor SB-201076
    • Pearce, N.J.; Yates, J.W.; Berkhout, T.A.; Jackson, B.; Tew, D.; Boyd, H.; Camilleri, P.; Sweeney, P.; Gribble, A.D.; Shaw, A.; Groot, P.H. The role of ATP citrate-lyase in the metabolic regulation of plasma lipids. Hypolipidaemic effects of SB-204990, a lactone prodrug of the potent ATP citrate-lyase inhibitor SB-201076. Biochem. J., 1998, 334, 113-119.
    • (1998) Biochem. J , vol.334 , pp. 113-119
    • Pearce, N.J.1    Yates, J.W.2    Berkhout, T.A.3    Jackson, B.4    Tew, D.5    Boyd, H.6    Camilleri, P.7    Sweeney, P.8    Gribble, A.D.9    Shaw, A.10    Groot, P.H.11
  • 151
    • 23044482013 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of the acetyl-CoA-carboxylase-alpha gene induces growth inhibition and apoptosis of prostate cancer cells
    • Brusselmans, K.; De Schrijver, E.; Verhoeven, G.; Swinnen, J.V. RNA interference-mediated silencing of the acetyl-CoA-carboxylase-alpha gene induces growth inhibition and apoptosis of prostate cancer cells. Cancer Res., 2005, 65, 6719-6725.
    • (2005) Cancer Res , vol.65 , pp. 6719-6725
    • Brusselmans, K.1    De Schrijver, E.2    Verhoeven, G.3    Swinnen, J.V.4
  • 152
    • 33744808464 scopus 로고    scopus 로고
    • Acetyl-CoA carboxylase alpha is essential to breast cancer cell survival
    • Chajes, V.; Cambot, M.; Moreau, K.; Lenoir, G.M.; Joulin, V. Acetyl-CoA carboxylase alpha is essential to breast cancer cell survival. Cancer Res., 2006, 66, 5287-5294.
    • (2006) Cancer Res , vol.66 , pp. 5287-5294
    • Chajes, V.1    Cambot, M.2    Moreau, K.3    Lenoir, G.M.4    Joulin, V.5
  • 154
    • 10944226843 scopus 로고    scopus 로고
    • A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product
    • Shen, Y.; Volrath, S.L.; Weatherly, S.C.; Elich, T.D.; Tong, L. A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product. Mol. Cell., 2004, 16, 881-891.
    • (2004) Mol. Cell , vol.16 , pp. 881-891
    • Shen, Y.1    Volrath, S.L.2    Weatherly, S.C.3    Elich, T.D.4    Tong, L.5
  • 155
  • 156
    • 1542315585 scopus 로고    scopus 로고
    • Structure and function of choline kinase isoforms in mammalian cells
    • Aoyama, C.; Liao, H.; Ishidate, K. Structure and function of choline kinase isoforms in mammalian cells. Prog. Lipid Res., 2004, 43, 266-281.
    • (2004) Prog. Lipid Res , vol.43 , pp. 266-281
    • Aoyama, C.1    Liao, H.2    Ishidate, K.3
  • 157
    • 0037142610 scopus 로고    scopus 로고
    • Increased choline kinase activity in human breast carcinomas: Clinical evidence for a potential novel antitumor strategy
    • Ramirez de Molina, A.; Gutierrez, R.; Ramos, M.A.; Silva, J.M.; Silva, J.; Bonilla, F.; Sanchez, J.J.; Lacal, J.C. Increased choline kinase activity in human breast carcinomas: Clinical evidence for a potential novel antitumor strategy. Oncogene, 2002, 21, 4317-4322.
    • (2002) Oncogene , vol.21 , pp. 4317-4322
    • Ramirez de Molina, A.1    Gutierrez, R.2    Ramos, M.A.3    Silva, J.M.4    Silva, J.5    Bonilla, F.6    Sanchez, J.J.7    Lacal, J.C.8
  • 158
    • 33645962844 scopus 로고    scopus 로고
    • Choline kinase: An important target for cancer
    • Janardhan, S.; Srivani, P.; Sastry, G.N. Choline kinase: An important target for cancer. Curr. Med. Chem., 2006, 13, 1169-1186.
    • (2006) Curr. Med. Chem , vol.13 , pp. 1169-1186
    • Janardhan, S.1    Srivani, P.2    Sastry, G.N.3
  • 159
    • 31544473808 scopus 로고    scopus 로고
    • Al-Saffar, N.M.; Troy, H.; Ramirez de Molina, A.; Jackson, L.E.; Madhu, B.; Griffiths, J.R.; Leach, M.O.; Workman, P.; Lacal, J.C.; Judson, I.R.; Chung, Y.L. Noninvasive magnetic resonance spectroscopic pharmacodynamic markers of the choline kinase inhibitor MN58b in human carcinoma models. Cancer Res., 2006, 66, 427- 34.
    • Al-Saffar, N.M.; Troy, H.; Ramirez de Molina, A.; Jackson, L.E.; Madhu, B.; Griffiths, J.R.; Leach, M.O.; Workman, P.; Lacal, J.C.; Judson, I.R.; Chung, Y.L. Noninvasive magnetic resonance spectroscopic pharmacodynamic markers of the choline kinase inhibitor MN58b in human carcinoma models. Cancer Res., 2006, 66, 427- 34.
  • 160
    • 0038089964 scopus 로고    scopus 로고
    • In vivo antitumor activity of choline kinase inhibitors: A novel target for anticancer drug discovery
    • Hernandez-Alcoceba, R.; Fernandez, F.; Lacal, J.C. In vivo antitumor activity of choline kinase inhibitors: A novel target for anticancer drug discovery. Cancer Res., 1999, 59, 3112-3118.
    • (1999) Cancer Res , vol.59 , pp. 3112-3118
    • Hernandez-Alcoceba, R.1    Fernandez, F.2    Lacal, J.C.3
  • 161
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: The central role of the HIF hydroxylase pathway
    • Kaelin, W.G., Jr.; Ratcliffe, P.J. Oxygen sensing by metazoans: The central role of the HIF hydroxylase pathway. Mol. Cell, 2008, 30, 393-402.
    • (2008) Mol. Cell , vol.30 , pp. 393-402
    • Kaelin Jr., W.G.1    Ratcliffe, P.J.2
  • 164
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco, I.; Sawyers, C.L. The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat. Rev. Cancer, 2002, 2, 489-501.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 166
    • 0032431032 scopus 로고    scopus 로고
    • The PTEN/ MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway
    • Wu, X.; Senechal, K.; Neshat, M.S.; Whang, Y.E.; Sawyers, C.L. The PTEN/ MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway. Proc. Natl. Acad. Sci. USA, 1998, 95, 15587-15591.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15587-15591
    • Wu, X.1    Senechal, K.2    Neshat, M.S.3    Whang, Y.E.4    Sawyers, C.L.5
  • 167
    • 27844461512 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition in development and cancer: Role of phosphatidylinositol 3′ kinase/AKT pathways
    • Larue, L.; Bellacosa, A. Epithelial-mesenchymal transition in development and cancer: Role of phosphatidylinositol 3′ kinase/AKT pathways. Oncogene, 2005, 24, 7443-7454.
    • (2005) Oncogene , vol.24 , pp. 7443-7454
    • Larue, L.1    Bellacosa, A.2
  • 169
    • 33746637660 scopus 로고    scopus 로고
    • Current development of mTOR inhibitors as anticancer agents
    • Faivre, S.; Kroemer, G.; Raymond, E. Current development of mTOR inhibitors as anticancer agents. Nat. Rev. Drug Discov., 2006, 5, 671-688.
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 671-688
    • Faivre, S.1    Kroemer, G.2    Raymond, E.3
  • 170
    • 0034644525 scopus 로고    scopus 로고
    • Schmelzle, T.; Hall, M.N. TOR, a central controller of cell growth. Cell, 2000, 103, 253-262.
    • Schmelzle, T.; Hall, M.N. TOR, a central controller of cell growth. Cell, 2000, 103, 253-262.
  • 171
    • 16844381988 scopus 로고    scopus 로고
    • Proapoptotic activity of cell-permeable anti-Akt single-chain antibodies
    • Shin, I.; Edl, J.; Biswas, S.; Lin, P.C.; Mernaugh, R.; Arteaga, C.L. Proapoptotic activity of cell-permeable anti-Akt single-chain antibodies. Cancer Res., 2005, 65, 2815-2824.
    • (2005) Cancer Res , vol.65 , pp. 2815-2824
    • Shin, I.1    Edl, J.2    Biswas, S.3    Lin, P.C.4    Mernaugh, R.5    Arteaga, C.L.6
  • 172
    • 0036718911 scopus 로고    scopus 로고
    • Targeting serine/threonine protein kinase B/Akt and cell-cycle checkpoint kinases for treating cancer
    • Li, Q.; Zhu, G.D. Targeting serine/threonine protein kinase B/Akt and cell-cycle checkpoint kinases for treating cancer. Curr. Top. Med. Chem., 2002, 2, 939-971.
    • (2002) Curr. Top. Med. Chem , vol.2 , pp. 939-971
    • Li, Q.1    Zhu, G.D.2
  • 173
    • 34248366501 scopus 로고    scopus 로고
    • Inhibitors of Akt Activity
    • Lippa, B. Inhibitors of Akt Activity. Expert Opin. Ther. Patents, 2007, 17, 577-581.
    • (2007) Expert Opin. Ther. Patents , vol.17 , pp. 577-581
    • Lippa, B.1
  • 175
    • 32044433797 scopus 로고    scopus 로고
    • Li, Q.; Li, T.; Zhu, G.D.; Gong, J.; Claibone, A.; Dalton, C.; Luo, Y.; Johnson, E.F.; Shi, Y.; Liu, X.; Klinghofer, V.; Bauch, J.L.; Marsh, K.C.; Bouska, J.J.; Arries, S.; De Jong, R.; Oltersdorf, T.; Stoll, V.S.; Jakob, C.G.; Rosenberg, S.H.; Giranda, V.L. Discovery of trans-3,4′-bispyridinylethylenes as potent and novel inhibitors of protein kinase B (PKB/Akt) for the treatment of cancer: Synthesis and biological evaluation. Bioorg. Med. Chem. Lett., 2006, 16, 1679-1685.
    • Li, Q.; Li, T.; Zhu, G.D.; Gong, J.; Claibone, A.; Dalton, C.; Luo, Y.; Johnson, E.F.; Shi, Y.; Liu, X.; Klinghofer, V.; Bauch, J.L.; Marsh, K.C.; Bouska, J.J.; Arries, S.; De Jong, R.; Oltersdorf, T.; Stoll, V.S.; Jakob, C.G.; Rosenberg, S.H.; Giranda, V.L. Discovery of trans-3,4′-bispyridinylethylenes as potent and novel inhibitors of protein kinase B (PKB/Akt) for the treatment of cancer: Synthesis and biological evaluation. Bioorg. Med. Chem. Lett., 2006, 16, 1679-1685.
  • 176
    • 33144478148 scopus 로고    scopus 로고
    • Li, Q.; Woods, K.W.; Thomas, S.; Zhu, G.D.; Packard, G.; Fisher, J.; Li, T.; Gong, J.; Dinges, J.; Song, X.; Abrams, J.; Luo, Y.; Johnson, E.F.; Shi, Y.; Liu, X.; Klinghofer, V.; Des Jong, R.; Oltersdorf, T.; Stoll, V.S.; Jakob, C.G.; Rosenberg, S.H.; Giranda, V.L. Synthesis and structure-activity relationship of 3,4′-bispyridinylethylenes: discovery of a potent 3-isoquinolinylpyridine inhibitor of protein kinase B (PKB/Akt) for the treatment of cancer. Bioorg. Med. Chem. Lett., 2006, 16, 2000-2007.
    • Li, Q.; Woods, K.W.; Thomas, S.; Zhu, G.D.; Packard, G.; Fisher, J.; Li, T.; Gong, J.; Dinges, J.; Song, X.; Abrams, J.; Luo, Y.; Johnson, E.F.; Shi, Y.; Liu, X.; Klinghofer, V.; Des Jong, R.; Oltersdorf, T.; Stoll, V.S.; Jakob, C.G.; Rosenberg, S.H.; Giranda, V.L. Synthesis and structure-activity relationship of 3,4′-bispyridinylethylenes: discovery of a potent 3-isoquinolinylpyridine inhibitor of protein kinase B (PKB/Akt) for the treatment of cancer. Bioorg. Med. Chem. Lett., 2006, 16, 2000-2007.
  • 181
    • 33750510883 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of 5-arylamino-6-chloro-1H-indazole-4,7-diones as inhibitors of protein kinase B/Akt
    • Ko, J.H.; Yeon, S.W.; Ryu, J.S.; Kim, T.Y.; Song, E.H.; You, H.J.; Park, R.E.; Ryu, C.K. Synthesis and biological evaluation of 5-arylamino-6-chloro-1H-indazole-4,7-diones as inhibitors of protein kinase B/Akt. Bioorg. Med. Chem. Lett., 2006, 16, 6001-6005.
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , pp. 6001-6005
    • Ko, J.H.1    Yeon, S.W.2    Ryu, J.S.3    Kim, T.Y.4    Song, E.H.5    You, H.J.6    Park, R.E.7    Ryu, C.K.8
  • 182
    • 3543117821 scopus 로고    scopus 로고
    • The development of phosphatidylinositol ether lipid analogues as inhibitors of the serine/threonine kinase, Akt
    • Gills, J.J.; Dennis, P.A. The development of phosphatidylinositol ether lipid analogues as inhibitors of the serine/threonine kinase, Akt. Expert Opin. Investig. Drugs, 2004, 13, 787-797.
    • (2004) Expert Opin. Investig. Drugs , vol.13 , pp. 787-797
    • Gills, J.J.1    Dennis, P.A.2
  • 184
    • 0028904018 scopus 로고
    • Synthesis and biology of 1D-3-deoxyphosphatidylinositol: A putative antimetabolite of phosphatidylinositol-3-phosphate and an inhibitor of cancer cell colony formation
    • Kozikowski, A.P.; Kiddle, J.J.; Frew, T.; Berggren, M.; Powis, G. Synthesis and biology of 1D-3-deoxyphosphatidylinositol: A putative antimetabolite of phosphatidylinositol-3-phosphate and an inhibitor of cancer cell colony formation. J. Med. Chem., 1995, 38, 1053-1056.
    • (1995) J. Med. Chem , vol.38 , pp. 1053-1056
    • Kozikowski, A.P.1    Kiddle, J.J.2    Frew, T.3    Berggren, M.4    Powis, G.5
  • 185
    • 0032572649 scopus 로고    scopus 로고
    • 3-Deoxy-D-myo-inositol 1-phosphate, 1-phosphonate, and ether lipid analogues as inhibitors of phosphatidylinositol-3-kinase signaling and cancer cell growth
    • Qiao, L.; Nan, F.; Kunkel, M.; Gallegos, A.; Powis, G.; Kozikowski, A.P. 3-Deoxy-D-myo-inositol 1-phosphate, 1-phosphonate, and ether lipid analogues as inhibitors of phosphatidylinositol-3-kinase signaling and cancer cell growth. J. Med. Chem., 1998, 41, 3303-3036.
    • (1998) J. Med. Chem , vol.41 , pp. 3303-3036
    • Qiao, L.1    Nan, F.2    Kunkel, M.3    Gallegos, A.4    Powis, G.5    Kozikowski, A.P.6
  • 187
    • 3042743988 scopus 로고    scopus 로고
    • Akt/protein kinase B signaling inhibitor-2, a selective small molecule inhibitor of Akt signaling with antitumor activity in cancer cells overexpressing Akt
    • Yang, L.; Dan, H.C.; Sun, M.; Liu, Q.; Sun, X.M.; Feldman, R.I.; Hamilton, A.D.; Polokoff, M.; Nicosia, S.V.; Herlyn, M.; Sebti, S.M.; Cheng, J.Q. Akt/protein kinase B signaling inhibitor-2, a selective small molecule inhibitor of Akt signaling with antitumor activity in cancer cells overexpressing Akt. Cancer Res., 2004, 64, 4394-4399.
    • (2004) Cancer Res , vol.64 , pp. 4394-4399
    • Yang, L.1    Dan, H.C.2    Sun, M.3    Liu, Q.4    Sun, X.M.5    Feldman, R.I.6    Hamilton, A.D.7    Polokoff, M.8    Nicosia, S.V.9    Herlyn, M.10    Sebti, S.M.11    Cheng, J.Q.12
  • 188
    • 0027333359 scopus 로고
    • A phase II trial of tricyclic nucleoside phosphate in patients with advanced squamous cell carcinoma of the cervix. A Gynecologic Oncology Group Study
    • Feun, L.G.; Blessing, J.A.; Barrett, R.J.; Hanjani, P. A phase II trial of tricyclic nucleoside phosphate in patients with advanced squamous cell carcinoma of the cervix. A Gynecologic Oncology Group Study. Am. J. Clin. Oncol., 1993, 16, 506-508.
    • (1993) Am. J. Clin. Oncol , vol.16 , pp. 506-508
    • Feun, L.G.1    Blessing, J.A.2    Barrett, R.J.3    Hanjani, P.4
  • 190
    • 62549133225 scopus 로고    scopus 로고
    • SR13668: A novel indole derived inhibitor of phospho-Akt potently suppresses tumor growth in various murine xenograft models
    • Jong, L.; Chao, W.R.; Amin, K.; Laderoute, K.; Orduna, J.; Sato, B.; Rice, G. SR13668: A novel indole derived inhibitor of phospho-Akt potently suppresses tumor growth in various murine xenograft models. AACR Meeting Abstracts 2004, 2004, 849-850.
    • (2004) AACR Meeting Abstracts 2004 , pp. 849-850
    • Jong, L.1    Chao, W.R.2    Amin, K.3    Laderoute, K.4    Orduna, J.5    Sato, B.6    Rice, G.7
  • 194
    • 33846866035 scopus 로고    scopus 로고
    • The role of mammalian target of rapamycin inhibitors in the treatment of advanced renal cancer
    • Cho, D.; Signoretti, S.; Regan, M.; Mier, J.W.; Atkins, M.B., The role of mammalian target of rapamycin inhibitors in the treatment of advanced renal cancer. Clin. Cancer Res., 2007, 13, 758s-763s.
    • (2007) Clin. Cancer Res , vol.13
    • Cho, D.1    Signoretti, S.2    Regan, M.3    Mier, J.W.4    Atkins, M.B.5
  • 195
    • 0016713286 scopus 로고
    • Rapamycin AY-22,989, a new antifungal antibiotic. II. Fermentation, isolation and characterization
    • Sehgal, S.N.; Baker, H.; Vezina, C. Rapamycin (AY-22,989), a new antifungal antibiotic. II. Fermentation, isolation and characterization. J. Antibiot (Tokyo), 1975, 28, 727-732.
    • (1975) J. Antibiot (Tokyo) , vol.28 , pp. 727-732
    • Sehgal, S.N.1    Baker, H.2    Vezina, C.3
  • 196
    • 0036275356 scopus 로고    scopus 로고
    • Hypoxia enhances vascular cell proliferation and angiogenesis in vitro via rapamycin (mTOR)-dependent signaling
    • Humar, R.; Kiefer, F.N.; Berns, H.; Resink, T.J.; Battegay, E.J. Hypoxia enhances vascular cell proliferation and angiogenesis in vitro via rapamycin (mTOR)-dependent signaling. FASEB J., 2002, 16, 771-780.
    • (2002) FASEB J , vol.16 , pp. 771-780
    • Humar, R.1    Kiefer, F.N.2    Berns, H.3    Resink, T.J.4    Battegay, E.J.5
  • 197
    • 0000375616 scopus 로고    scopus 로고
    • The effect of CCI-779, a novel macrolide antitumor agent, on the growth of human tumor cells in vitro and in nude mouse xenograft in vivo
    • Gibbons, J.J.; Discafani, C.; Peterson, R.; Hernandez, R.; Skotnicki, J.; Frost, P. The effect of CCI-779, a novel macrolide antitumor agent, on the growth of human tumor cells in vitro and in nude mouse xenograft in vivo. Proc. Am. Assoc. Cancer Res., 2000, 40, 301.
    • (2000) Proc. Am. Assoc. Cancer Res , vol.40 , pp. 301
    • Gibbons, J.J.1    Discafani, C.2    Peterson, R.3    Hernandez, R.4    Skotnicki, J.5    Frost, P.6
  • 198
    • 33846866035 scopus 로고    scopus 로고
    • The role of mammalian target of rapamycin inhibitors in the treatment of advanced renal cancer
    • Cho, D.; Signoretti, S.; Regan, M.; Mier, J. W.; Atkins, M. B. The role of mammalian target of rapamycin inhibitors in the treatment of advanced renal cancer. Clin. Cancer Res., 2007, 13, 758s-763s.
    • (2007) Clin. Cancer Res , vol.13
    • Cho, D.1    Signoretti, S.2    Regan, M.3    Mier, J.W.4    Atkins, M.B.5
  • 199
    • 0035716926 scopus 로고    scopus 로고
    • Inhibitors of mammalian target of rapamycin
    • Klupp, J.; Langrehr, M.L.; Junge, G.; Neuhaus, P. Inhibitors of mammalian target of rapamycin. Drugs Fut., 2001, 26, 1179-1189.
    • (2001) Drugs Fut , vol.26 , pp. 1179-1189
    • Klupp, J.1    Langrehr, M.L.2    Junge, G.3    Neuhaus, P.4
  • 201
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1 alpha is required for solid tumor formation and embryonic vascularization
    • Ryan, H.E.; Lo, J.; Johnson, R.S. HIF-1 alpha is required for solid tumor formation and embryonic vascularization. EMBO J., 1998, 17, 3005-3015.
    • (1998) EMBO J , vol.17 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 203
    • 33644614520 scopus 로고    scopus 로고
    • A metabolic switch required for cellular adaptation to hypoxia
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase
    • Kim, J.W.; Tchernyshyov, I.; Semenza, G.L.; Dang, C.V., HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia. Cell Metab., 2006, 3, 177-185.
    • (2006) Cell Metab , vol.3 , pp. 177-185
    • Kim, J.W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 204
    • 0037515549 scopus 로고    scopus 로고
    • MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300
    • Sang, N.; Stiehl, D.P.; Bohensky, J.; Leshchinsky, I.; Srinivas, V.; Caro, J. MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300. J. Biol. Chem., 2003, 278, 14013-14019.
    • (2003) J. Biol. Chem , vol.278 , pp. 14013-14019
    • Sang, N.1    Stiehl, D.P.2    Bohensky, J.3    Leshchinsky, I.4    Srinivas, V.5    Caro, J.6
  • 205
    • 4444369682 scopus 로고    scopus 로고
    • Antitumor activity and pharmacodynamic properties of PX-478, an inhibitor of hypoxia-inducible factor-1alpha
    • Welsh, S.; Williams, R.; Kirkpatrick, L.; Paine-Murrieta, G.; Powis, G. Antitumor activity and pharmacodynamic properties of PX-478, an inhibitor of hypoxia-inducible factor-1alpha. Mol. Cancer Ther., 2004, 3, 233-244.
    • (2004) Mol. Cancer Ther , vol.3 , pp. 233-244
    • Welsh, S.1    Williams, R.2    Kirkpatrick, L.3    Paine-Murrieta, G.4    Powis, G.5
  • 207
    • 25444523184 scopus 로고    scopus 로고
    • Kong, D.; Park, E.J.; Stephen, A.G.; Calvani, M.; Cardellina, J.H.; Monks, A.; Fisher, R.J.; Shoemaker, R.H.; Melillo, G. Echinomycin, a small-molecule inhibitor of hypoxia-inducible factor-1 DNA-binding activity. Cancer Res., 2005, 65, 9047-9055.
    • Kong, D.; Park, E.J.; Stephen, A.G.; Calvani, M.; Cardellina, J.H.; Monks, A.; Fisher, R.J.; Shoemaker, R.H.; Melillo, G. Echinomycin, a small-molecule inhibitor of hypoxia-inducible factor-1 DNA-binding activity. Cancer Res., 2005, 65, 9047-9055.
  • 208
    • 23144447809 scopus 로고    scopus 로고
    • Flavopiridol downregulates hypoxia-mediated hypoxia-inducible factor-1alpha expression in human glioma cells by a proteasome-independent pathway: Implications for in vivo therapy
    • Newcomb, E.W.; Ali, M.A.; Schnee, T.; Lan, L.; Lukyanov, Y.; Fowkes, M.; Miller, D.C.; Zagzag, D. Flavopiridol downregulates hypoxia-mediated hypoxia-inducible factor-1alpha expression in human glioma cells by a proteasome-independent pathway: Implications for in vivo therapy. Neuro. Oncol., 2005, 7, 225-235.
    • (2005) Neuro. Oncol , vol.7 , pp. 225-235
    • Newcomb, E.W.1    Ali, M.A.2    Schnee, T.3    Lan, L.4    Lukyanov, Y.5    Fowkes, M.6    Miller, D.C.7    Zagzag, D.8
  • 210
    • 0035012605 scopus 로고    scopus 로고
    • HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1alpha (HIF-1alpha) synthesis: Novel mechanism for HIF-1-mediated vascular endothelial growth factor expression
    • Laughner, E.; Taghavi, P.; Chiles, K.; Mahon, P.C.; Semenza, G.L. HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1alpha (HIF-1alpha) synthesis: Novel mechanism for HIF-1-mediated vascular endothelial growth factor expression. Mol. Cell Biol., 2001, 21, 3995-4004.
    • (2001) Mol. Cell Biol , vol.21 , pp. 3995-4004
    • Laughner, E.1    Taghavi, P.2    Chiles, K.3    Mahon, P.C.4    Semenza, G.L.5
  • 211
    • 0037111665 scopus 로고    scopus 로고
    • BCR/ ABL induces expression of vascular endothelial growth factor and its transcriptional activator, hypoxia inducible factor-1alpha, through a pathway involving phosphoinositide 3-kinase and the mammalian target of rapamycin
    • Mayerhofer, M.; Valent, P.; Sperr. W.R.; Griffin, J.D.; Sillaber, C. BCR/ ABL induces expression of vascular endothelial growth factor and its transcriptional activator, hypoxia inducible factor-1alpha, through a pathway involving phosphoinositide 3-kinase and the mammalian target of rapamycin. Blood, 2002, 100, 3767-3775.
    • (2002) Blood , vol.100 , pp. 3767-3775
    • Mayerhofer, M.1    Valent, P.2    Sperr, W.R.3    Griffin, J.D.4    Sillaber, C.5
  • 212
    • 0037862921 scopus 로고    scopus 로고
    • The effect of trastuzumab/ docatexel combination on breast cancer angiogenesis: Dichotomus effect predictable by the HIFI alpha/VEGF pre-treatment status?
    • Koukourakis, M.I.; Simopoulos, C.; Polychronidis, A.; Perente, S.; Botaitis, S.; Giatromanolaki, A.; Sivridis, E. The effect of trastuzumab/ docatexel combination on breast cancer angiogenesis: Dichotomus effect predictable by the HIFI alpha/VEGF pre-treatment status?. Anticancer Res., 2003, 23, 1673-1680.
    • (2003) Anticancer Res , vol.23 , pp. 1673-1680
    • Koukourakis, M.I.1    Simopoulos, C.2    Polychronidis, A.3    Perente, S.4    Botaitis, S.5    Giatromanolaki, A.6    Sivridis, E.7
  • 213
    • 0035877728 scopus 로고    scopus 로고
    • Rac1 activity is required for the activation of hypoxia-inducible factor 1
    • Hirota, K.; Semenza, G.L. Rac1 activity is required for the activation of hypoxia-inducible factor 1. J. Biol. Chem., 2001, 276, 21166-21172.
    • (2001) J. Biol. Chem , vol.276 , pp. 21166-21172
    • Hirota, K.1    Semenza, G.L.2
  • 214
    • 0032725554 scopus 로고    scopus 로고
    • p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1
    • Richard, D.E.; Berra, E.; Gothie, E.; Roux, D.; Pouyssegur, J. p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1. J. Biol. Chem., 1999, 274, 32631-32637.
    • (1999) J. Biol. Chem , vol.274 , pp. 32631-32637
    • Richard, D.E.1    Berra, E.2    Gothie, E.3    Roux, D.4    Pouyssegur, J.5
  • 215
    • 0038199737 scopus 로고    scopus 로고
    • Management of cellular energy by the AMP-activated protein kinase system
    • Hardie, D.G.; Scott, J.W.; Pan, D.A.; Hudson, E.R. Management of cellular energy by the AMP-activated protein kinase system. FEBS Lett., 2003, 546, 113-120.
    • (2003) FEBS Lett , vol.546 , pp. 113-120
    • Hardie, D.G.1    Scott, J.W.2    Pan, D.A.3    Hudson, E.R.4
  • 216
    • 0037025356 scopus 로고    scopus 로고
    • AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling
    • Bolster, D.R.; Crozier, S.J.; Kimball, S.R.; Jefferson, L.S. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J. Biol. Chem., 2002, 277, 23977-23980.
    • (2002) J. Biol. Chem , vol.277 , pp. 23977-23980
    • Bolster, D.R.1    Crozier, S.J.2    Kimball, S.R.3    Jefferson, L.S.4
  • 217
    • 33745213627 scopus 로고    scopus 로고
    • AMPK and cell proliferation - AMPK as a therapeutic target for atherosclerosis and cancer
    • Motoshima, H.; Goldstein, B.J.; Igata, M.; Araki, E. AMPK and cell proliferation - AMPK as a therapeutic target for atherosclerosis and cancer. J. Physiol., 2006, 574, 63-71.
    • (2006) J. Physiol , vol.574 , pp. 63-71
    • Motoshima, H.1    Goldstein, B.J.2    Igata, M.3    Araki, E.4
  • 219
    • 33746592505 scopus 로고
    • Increased cancer-related mortality for patients with type 2 diabetes who use sulfonylureas or insulin: Response to Farooki and Schneider
    • Bowker, S.L.; Majumdar, S.R.; Veugelers, P.; Johnson, J.A. Increased cancer-related mortality for patients with type 2 diabetes who use sulfonylureas or insulin: Response to Farooki and Schneider. Diabetes Care, 2006, 29, 1990-1991.
    • (1990) Diabetes Care , vol.2006 , pp. 29
    • Bowker, S.L.1    Majumdar, S.R.2    Veugelers, P.3    Johnson, J.A.4
  • 220
    • 33751284806 scopus 로고    scopus 로고
    • Metformin is an AMP kinase-dependent growth inhibitor for breast cancer cells
    • Zakikhani, M.; Dowling, R.; Fantus, I.G.; Sonenberg, N.; Pollak, M. Metformin is an AMP kinase-dependent growth inhibitor for breast cancer cells. Cancer Res., 2006, 66, 10269-10273.
    • (2006) Cancer Res , vol.66 , pp. 10269-10273
    • Zakikhani, M.1    Dowling, R.2    Fantus, I.G.3    Sonenberg, N.4    Pollak, M.5
  • 221
    • 3543025724 scopus 로고    scopus 로고
    • AMP-activated protein kinase activators can inhibit the growth of prostate cancer cells by multiple mechanisms
    • Xiang, X.; Saha, A.K.; Wen, R.; Ruderman, N.B.; Luo, Z. AMP-activated protein kinase activators can inhibit the growth of prostate cancer cells by multiple mechanisms. Biochem. Biophys. Res. Commun., 2004, 321, 161-167.
    • (2004) Biochem. Biophys. Res. Commun , vol.321 , pp. 161-167
    • Xiang, X.1    Saha, A.K.2    Wen, R.3    Ruderman, N.B.4    Luo, Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.