메뉴 건너뛰기




Volumn 9, Issue 9, 2009, Pages 1084-1101

HIF-1α modulates energy metabolism in cancer cells by inducing over-expression of specific glycolytic isoforms

Author keywords

Glucose transporters; Glycolysis; Glycolytic inhibitors; Hexokinases; HIF 1 ; Mitochondria; Mitochondrial inhibitors

Indexed keywords

6 PHOSPHOFRUCTO 2 KINASE; 6 PHOSPHOFRUCTOKINASE; ANTINEOPLASTIC AGENT; CLOTRIMAZOLE; CYTOCHROME C OXIDASE; DEOXYGLUCOSE; DIGOXIN; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUCOSE 6 PHOSPHATE ISOMERASE; GLUCOSE TRANSPORTER; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOLYTIC ENZYME; GOSSYPOL; HEXOKINASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; KONINGIC ACID; LACTATE DEHYDROGENASE; MANASSANTIN B; MITOCHONDRIAL ENZYME; MONOCARBOXYLATE TRANSPORTER; OXALIC ACID; OXAMIC ACID; PHOSPHOGLYCERATE KINASE; PHOSPHOGLYCERATE MUTASE; PYRUVATE DEHYDROGENASE; PYRUVATE KINASE; TOPOTECAN; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG; UNINDEXED DRUG; ISOPROTEIN;

EID: 70349570410     PISSN: 13895575     EISSN: None     Source Type: Journal    
DOI: 10.2174/138955709788922610     Document Type: Review
Times cited : (382)

References (166)
  • 1
    • 0034842201 scopus 로고    scopus 로고
    • Hypoxia and oxidative stress in breast cancer. Hypoxia and tumourigenesis
    • Knowles, H.J.; Harris, A.L. Hypoxia and oxidative stress in breast cancer. Hypoxia and tumourigenesis. Breast Cancer Res., 2001, 3, 318-322
    • (2001) Breast Cancer Res. , vol.3 , pp. 318-322
    • Knowles, H.J.1    Harris, A.L.2
  • 2
    • 57649130593 scopus 로고    scopus 로고
    • Induction of pyruvate dehydrogenase kinase-3 by hypoxia-inducible factor-1 promotes metabolic switch and drug resistance
    • Lu, C.W.; Lin, S.C.; Chen, K.F.; Lai, Y.Y.; Tsai, S.J. Induction of pyruvate dehydrogenase kinase-3 by hypoxia-inducible factor-1 promotes metabolic switch and drug resistance. J. Biol. Chem., 2008, 283, 28106-28114
    • (2008) J. Biol. Chem. , vol.283 , pp. 28106-28114
    • Lu, C.W.1    Lin, S.C.2    Chen, K.F.3    Lai, Y.Y.4    Tsai, S.J.5
  • 4
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia -inducible factor 1
    • Semenza, G.L; Roth, P.H.; Fang, H.M.; Wang, G.L. Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia -inducible factor 1. J. Biol. Chem., 1994, 269, 23757-63,
    • (1994) J. Biol. Chem. , vol.269 , pp. 23757-23763
    • Semenza, G.L.1    Roth, P.H.2    Fang, H.M.3    Wang, G.L.4
  • 5
    • 50149097983 scopus 로고    scopus 로고
    • Hypoxia, HIF1 and glucose metabolism in the solid tumour
    • Denko, N. C. Hypoxia, HIF1 and glucose metabolism in the solid tumour. Nat. Rev. Cancer, 2008, 8, 705-713
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 705-713
    • Denko, N.C.1
  • 6
    • 34547130302 scopus 로고    scopus 로고
    • Effects of hypoxia on tumor metabolism
    • Kim, J.W.; Gao, P.; Dang, C.V. Effects of hypoxia on tumor metabolism. Cancer Metastasis Rev., 2007, 26, 291-298
    • (2007) Cancer Metastasis Rev. , vol.26 , pp. 291-298
    • Kim, J.W.1    Gao, P.2    Dang, C.V.3
  • 7
    • 40949132841 scopus 로고    scopus 로고
    • Turn me on: Regulating HIF transcriptional activity
    • Lisy, K; Peet, D.J. Turn me on: regulating HIF transcriptional activity. Cell Death Differ., 2008, 15, 642-649
    • (2008) Cell Death Differ. , vol.15 , pp. 642-649
    • Lisy, K.1    Peet, D.J.2
  • 10
    • 39749110780 scopus 로고    scopus 로고
    • Hypoxia and breast cancer: Prognostic and therapeutic implications
    • Lundgren, K.; Holm, C.; Landberg, G. Hypoxia and breast cancer: prognostic and therapeutic implications. Cell Mol. Life Sci., 2007, 64, 3233-3247
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 3233-3247
    • Lundgren, K.1    Holm, C.2    Landberg, G.3
  • 11
    • 34249982595 scopus 로고    scopus 로고
    • YC-1 inhibits HIF-1 expression in prostate cancer cells: Contribution of Akt/NF-kappaB signaling to HIF-1alpha accumulation during hypoxia
    • Sun, H.L.; Liu, Y.N.; Huang, Y.T.; Pan, S.L.; Huang, D.Y.; Guh, J.H.; Lee, F.Y.; Kuo, S.C.; Teng, C.M. YC-1 inhibits HIF-1 expression in prostate cancer cells: contribution of Akt/NF-kappaB signaling to HIF-1alpha accumulation during hypoxia. Oncogene, 2007, 26, 3941-3951
    • (2007) Oncogene , vol.26 , pp. 3941-3951
    • Sun, H.L.1    Liu, Y.N.2    Huang, Y.T.3    Pan, S.L.4    Huang, D.Y.5    Guh, J.H.6    Lee, F.Y.7    Kuo, S.C.8    Teng, C.M.9
  • 12
    • 33947307906 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1α regulates lung adenocarcinoma cell invasion
    • DOI 10.1016/j.yexcr.2007.01.013, PII S0014482707000365
    • Shyu, K.G.; Hsu, F.L.; Wang, M.J.; Wang, B.W.; Lin, S. Hypoxiainducible factor 1alpha regulates lung adenocarcinoma cell invasion. Exp. Cell. Res., 2007, 313, 1181-1191 (Pubitemid 46437248)
    • (2007) Experimental Cell Research , vol.313 , Issue.6 , pp. 1181-1191
    • Shyu, K.-G.1    Hsu, F.-L.2    Wang, M.J.3    Wang, B.-W.4    Lin, S.5
  • 13
    • 0033870281 scopus 로고    scopus 로고
    • The expression and distribution of the hypoxia-inducible factors HIF-1alpha and HIF-2alpha in normal human tissues, cancers, and tumor-associated macrophages
    • Talks, K.L.; Turley, H.; Gatter, K.C.; Maxwell, P.H.; Pugh, C.W.; Ratcliffe, P.J.; Harris, A.L. The expression and distribution of the hypoxia-inducible factors HIF-1alpha and HIF-2alpha in normal human tissues, cancers, and tumor-associated macrophages. Am. J. Pathol., 2000, 157, 411-421
    • (2000) Am. J. Pathol. , vol.157 , pp. 411-421
    • Talks, K.L.1    Turley, H.2    Gatter, K.C.3    Maxwell, P.H.4    Pugh, C.W.5    Ratcliffe, P.J.6    Harris, A.L.7
  • 14
    • 34547700020 scopus 로고    scopus 로고
    • Localization of immunoreactive HIF-1alpha and HIF- 2alpha in neuroendocrine cells of both benign and malignant prostate glands
    • Monsef, N.; Helczynski, L.; Lundwall, A.; Pahlman, S.; Anders- Bjartell . Localization of immunoreactive HIF-1alpha and HIF- 2alpha in neuroendocrine cells of both benign and malignant prostate glands. Prostate, 2007, 67, 1219-1229
    • (2007) Prostate , vol.67 , pp. 1219-1229
    • Monsef, N.1    Helczynski, L.2    Lundwall, A.3    Pahlman, S.4    Anders-Bjartell5
  • 15
    • 34547121206 scopus 로고    scopus 로고
    • Hypoxia in cancer: Significance and impact on clinical outcome
    • Vaupel, P.; Mayer, A. Hypoxia in cancer: significance and impact on clinical outcome. Cancer Metastasis Rev., 2007, 26, 225-239
    • (2007) Cancer Metastasis Rev. , vol.26 , pp. 225-239
    • Vaupel, P.1    Mayer, A.2
  • 16
    • 40949114950 scopus 로고    scopus 로고
    • Role and regulation of prolyl hydroxylase domain proteins
    • Fong, G.H.; Takeda, K. Role and regulation of prolyl hydroxylase domain proteins. Cell Death Differ., 2008, 15, 635-641
    • (2008) Cell Death Differ. , vol.15 , pp. 635-641
    • Fong, G.H.1    Takeda, K.2
  • 17
    • 37549071449 scopus 로고    scopus 로고
    • Oxygen sensors in context
    • Ward, J.P. Oxygen sensors in context. Biochim. Biophys. Acta, 2008, 1777, 1-14.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1-14
    • Ward, J.P.1
  • 18
    • 33749410367 scopus 로고    scopus 로고
    • The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases
    • DOI 10.1074/jbc.M604628200
    • Koivunen, P.; Hirsilä, M.; Kivirikko, K.I.; Myllyharju, J. The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases. J. Biol. Chem., 2006, 281, 28712-28720 (Pubitemid 44507013)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28712-28720
    • Koivunen, P.1    Hirsila, M.2    Kivirikko, K.I.3    Myllyharju, J.4
  • 21
    • 26044471689 scopus 로고    scopus 로고
    • Role of endothelial nitric oxide in microvascular oxygen delivery and consumption
    • DOI 10.1016/j.freeradbiomed.2005.06.019, PII S0891584905003552
    • Cabrales, P.; Tsai, A.G.; Frangos, J.A.; Intaglieta, M. Role of endothelial nitric oxide in microvascular oxygen delivery and consumption. Free Radic. Biol. Med., 2005, 39, 1229-1237 (Pubitemid 41407715)
    • (2005) Free Radical Biology and Medicine , vol.39 , Issue.9 , pp. 1229-1237
    • Cabrales, P.1    Tsai, A.G.2    Frangos, J.A.3    Intaglietta, M.4
  • 22
    • 33846415800 scopus 로고    scopus 로고
    • Hypoxia, drug therapy and toxicity
    • Lee, K.; Roth, R.A.; LaPres, J.J. Hypoxia, drug therapy and toxicity. Pharmacol. Ther., 2007, 113, 229-246
    • (2007) Pharmacol. Ther. , vol.113 , pp. 229-246
    • Lee, K.1    Roth, R.A.2    LaPres, J.J.3
  • 23
    • 33748187417 scopus 로고    scopus 로고
    • Regulating cellular oxygen sensing by hydroxylation
    • DOI 10.1016/j.cardiores.2006.05.005, PII S0008636306001891
    • Fandrey, J.; Gorr, T.A.; Gassmann, M. Regulating cellular oxygen sensing by hydroxylation. Cardiovasc. Res., 2006, 71, 642-651 (Pubitemid 44848002)
    • (2006) Cardiovascular Research , vol.71 , Issue.4 , pp. 642-651
    • Fandrey, J.1    Gorr, T.A.2    Gassmann, M.3
  • 24
  • 25
    • 33747660292 scopus 로고    scopus 로고
    • Increased prolyl 4-hydroxylase domain proteins compensate for decreased oxygen levels: Evidence for an autoregulatory oxygen-sensing system
    • DOI 10.1074/jbc.M601719200
    • Stiehl, D.P.; Wirthner, R.; Köditz, J.; Spielmann, P.; Camenisch, G.; Wenger, R.H. Increased prolyl 4-hydroxylase domain proteins compensate for decreased oxygen levels. Evidence for an autoregulatory oxygen-sensing system. J. Biol. Chem., 2006, 281, 23482-23491 (Pubitemid 44274123)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.33 , pp. 23482-23491
    • Stiehl, D.P.1    Wirthner, R.2    Koditz, J.3    Spielmann, P.4    Camenisch, G.5    Wenger, R.H.6
  • 26
    • 40949126440 scopus 로고    scopus 로고
    • Mitochondrial complex III regulates hypoxic activation of HIF
    • Klimova, T.; Chandel, N.S. Mitochondrial complex III regulates hypoxic activation of HIF. Cell Death Differ., 2008, 15, 660-666
    • (2008) Cell Death Differ. , vol.15 , pp. 660-666
    • Klimova, T.1    Chandel, N.S.2
  • 27
    • 38149059911 scopus 로고    scopus 로고
    • Mitochondria and cellular oxygen sensing in the HIF pathway
    • Taylor, C.T. Mitochondria and cellular oxygen sensing in the HIF pathway. Biochem J., 2008, 409, 19-26.
    • (2008) Biochem J. , vol.409 , pp. 19-26
    • Taylor, C.T.1
  • 28
    • 0037073797 scopus 로고    scopus 로고
    • 1 complex is independent of the Rieske protein redox state. Consequences for semiquinone stabilization in the quinol oxidation site
    • DOI 10.1074/jbc.M208060200
    • Covian, R.; Pardo, J.P.; Moreno-Sánchez, R. Tight binding of inhibitors to bovine bc1 complex is independent of the Rieske protein redox state. Consequences for semiquinone stabilization in the quinol oxidation site. J. Biol. Chem., 2002, 277, 48449-48455 (Pubitemid 35470803)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48449-48455
    • Covian, R.1    Pardo, J.P.2    Moreno-Sanchez, R.3
  • 29
    • 33750622643 scopus 로고    scopus 로고
    • Redox regulation of the hypoxia-inducible factor
    • DOI 10.1515/BC.2006.167, PII BCHM38710111337
    • Pouysségur, J.; Mechta-Grigoriou, F. Redox regulation of the hypoxia- inducible factor. Biol. Chem., 2006, 387, 1337-1346 (Pubitemid 44691412)
    • (2006) Biological Chemistry , vol.387 , Issue.10-11 , pp. 1337-1346
    • Pouyssegur, J.1    Mechta-Grigoriou, F.2
  • 30
    • 34250745912 scopus 로고    scopus 로고
    • The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production
    • Bell, E.L.; Klimova, T.A.; Eisenbart, J.; Moraes, C.T.; Murphy, M.P.; Budinger, G.R.S.; Chandel, N.S. The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production. J. Cell Biol., 2007, 177, 1029-1036.
    • (2007) J. Cell Biol. , vol.177 , pp. 1029-1036
    • Bell, E.L.1    Klimova, T.A.2    Eisenbart, J.3    Moraes, C.T.4    Murphy, M.P.5    Budinger, G.R.S.6    Chandel, N.S.7
  • 31
    • 33750070935 scopus 로고    scopus 로고
    • Effect of hypoxia on the transcription pattern of subunit isoforms and the kinetics of cytochrome c oxidase in cortical astrocytes and cerebellar neurons
    • DOI 10.1111/j.1471-4159.2006.04134.x
    • Horvat, S.; Beyer, C.; Arnold, S. Effect of hypoxia on the transcription pattern of subunit isoforms and the kinetics of cytochrome c oxidase in cortical astrocytes and cerebellar neurons. J. Neurochem., 2006, 99, 937-951 (Pubitemid 44583451)
    • (2006) Journal of Neurochemistry , vol.99 , Issue.3 , pp. 937-951
    • Horvat, S.1    Beyer, C.2    Arnold, S.3
  • 32
    • 34249934598 scopus 로고    scopus 로고
    • Mitocans as anti-cancer agents targeting mitochondria: Lessons from studies with vitamin e analogues, inhibitors of complex II
    • DOI 10.1007/s10863-006-9060-z, The Cancer Cell's Power Plants as Promising Therapeutic Targets
    • Neuzil, J.; Dyason, J.C.; Freeman, R.; Dong, L. F.; Prochazka, L.; Wang, X. F.; Scheffler, I.; Ralph, S.J. Mitocans as anti-cancer agents targeting mitochondria: lessons from studies with vitamin E analogues, inhibitors of complex II. J. Bioenerg. Biomembr., 2007, 39, 65-72. (Pubitemid 46877173)
    • (2007) Journal of Bioenergetics and Biomembranes , vol.39 , Issue.1 , pp. 65-72
    • Neuzil, J.1    Dyason, J.C.2    Freeman, R.3    Dong, L.-F.4    Prochazka, L.5    Wang, X.-F.6    Scheffler, I.7    Ralph, S.J.8
  • 33
    • 0030056515 scopus 로고    scopus 로고
    • Mitochondrial complex I deficiency leads to increased production of superoxide radicals and induction of superoxide dismutase
    • Pitkanen, S.; Robinson, B.H. Mitochondrial complex I deficiency leads to increased production of superoxide radicals and induction of superoxide dismutase. J. Clin. Invest., 1996, 98, 345-351
    • (1996) J. Clin. Invest. , vol.98 , pp. 345-351
    • Pitkanen, S.1    Robinson, B.H.2
  • 35
    • 11144241609 scopus 로고    scopus 로고
    • Regulation of 2-oxoglutarate (α-ketoglutarate) dehydrogenase stability by the RING finger ubiquitin ligase siah
    • DOI 10.1074/jbc.M410315200
    • Habelhah, H.; Laine, A.; Erdjument-Bromage, H.; Tempst, P.; Gershwin, M.E.; Bowtell, D.D.; Ronai, Z. Regulation of 2- oxoglutarate (alpha-ketoglutarate) dehydrogenase stability by the RING finger ubiquitin ligase Siah. J. Biol. Chem., 2004, 279, 53782-53788 (Pubitemid 40051887)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53782-53788
    • Habelhah, H.1    Laine, A.2    Erdjument-Bromage, H.3    Tempst, P.4    Gershwin, M.E.5    Bowtell, D.D.L.6    Ronai, Z.7
  • 36
    • 34548018979 scopus 로고    scopus 로고
    • Visualization of hypoxia in microscopic tumors by immunofluorescent microscopy
    • Li, X.F.; Carlin, S.; Urano, M.; Russell, J.; Ling, C.C.; O'Donoghue, J.A. Visualization of hypoxia in microscopic tumors by immunofluorescent microscopy. Cancer Res., 2007, 67, 7646-7653
    • (2007) Cancer Res. , vol.67 , pp. 7646-7653
    • Li, X.F.1    Carlin, S.2    Urano, M.3    Russell, J.4    Ling, C.C.5    O'Donoghue, J.A.6
  • 37
    • 33846008051 scopus 로고    scopus 로고
    • Tumor hypoxia and expression of c-met in cervical cancer
    • DOI 10.1016/j.ygyno.2006.07.040, PII S0090825806005634
    • Leo, C.; Horn, L.C.; Einenkel, J.; Hentschel, B.; Höckel, M. Tumor hypoxia and expression of c-met in cervical cancer. Gynecol. Oncol., 2007, 104, 181-185 (Pubitemid 46054122)
    • (2007) Gynecologic Oncology , vol.104 , Issue.1 , pp. 181-185
    • Leo, C.1    Horn, L.-C.2    Einenkel, J.3    Hentschel, B.4    Hockel, M.5
  • 38
    • 34547124062 scopus 로고    scopus 로고
    • Hypoxia: A key regulator of angiogenesis in cancer
    • Liao, D.; Johnson, R.S. Hypoxia: a key regulator of angiogenesis in cancer. Cancer Metastasis Rev., 2007, 26, 281-290
    • (2007) Cancer Metastasis Rev. , vol.26 , pp. 281-290
    • Liao, D.1    Johnson, R.S.2
  • 39
    • 0035847050 scopus 로고    scopus 로고
    • Role of exon 2-encoded β-domain of the von Hippel-Lindau tumor suppressor protein
    • DOI 10.1074/jbc.M008295200
    • Bonicalzi, M.E.; Groulx, I.; Paulsen, N.; Lee, S. Role of exon 2- encoded beta -domain of the von Hippel-Lindau tumor suppressor protein. J. Biol. Chem., 2001, 276, 1407-1416 (Pubitemid 32096572)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 1407-1416
    • Bonicalzi, M.-E.1    Groulx, I.2    De Paulsen, N.3    Lee, S.4
  • 40
    • 29644442625 scopus 로고    scopus 로고
    • Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1
    • Lu, H.; Dalgard, C.L.; Mohyeldin, A.; McFate, T.; Tait, A.S.; Varma, A. Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1. J. Biol. Chem., 2005, 280, 41928-41939
    • (2005) J. Biol. Chem. , vol.280 , pp. 41928-41939
    • Lu, H.1    Dalgard, C.L.2    Mohyeldin, A.3    McFate, T.4    Tait, A.S.5    Varma, A.6
  • 43
    • 23644436667 scopus 로고    scopus 로고
    • Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: Developmental culling and cancer
    • DOI 10.1016/j.ccr.2005.06.015, PII S1535610805002242
    • Lee, S.; Nakamura, E.; Yang, H.; Wei, W.; Linggi, M.S.; Sajan, M.P.; Farese, R.V.; Freeman, R.S.; Carter, B.D.; Kaelin, W.G. Jr.; Schlisio, S. Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer. Cancer Cell, 2005, 8, 155-167 (Pubitemid 41132744)
    • (2005) Cancer Cell , vol.8 , Issue.2 , pp. 155-167
    • Lee, S.1    Nakamura, E.2    Yang, H.3    Wei, W.4    Linggi, M.S.5    Sajan, M.P.6    Farese, R.V.7    Freeman, R.S.8    Carter, B.D.9    Kaelin Jr., W.G.10    Schlisio, S.11
  • 44
    • 40949142209 scopus 로고    scopus 로고
    • The role of hypoxia-inducible factors in tumorigenesis
    • Rankin, E.B.; Giaccia, A.J. The role of hypoxia-inducible factors in tumorigenesis. Cell Death Differ., 2008, 15, 678-685
    • (2008) Cell Death Differ. , vol.15 , pp. 678-685
    • Rankin, E.B.1    Giaccia, A.J.2
  • 45
    • 40949088476 scopus 로고    scopus 로고
    • Biology of hypoxia-inducible factor-2alpha in development and disease
    • Patel, S.A.; Simon, M.C. Biology of hypoxia-inducible factor-2alpha in development and disease. Cell Death Differ., 2008, 15, 628-634
    • (2008) Cell Death Differ. , vol.15 , pp. 628-634
    • Patel, S.A.1    Simon, M.C.2
  • 47
    • 0034816245 scopus 로고    scopus 로고
    • Hypoxiainducible factor 1alpha and 1beta proteins share common signaling pathways in human prostate cancer cells
    • Zhong, H.; Hanrahan, C.; van der Poel, H.; Simona, J.W. Hypoxiainducible factor 1alpha and 1beta proteins share common signaling pathways in human prostate cancer cells. Biochem. Biophys. Res. Commun., 2001, 284, 352-356
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 352-356
    • Zhong, H.1    Hanrahan, C.2    Van Der Poel, H.3    Simona, J.W.4
  • 48
    • 0033400541 scopus 로고    scopus 로고
    • Mitochondrial events in the life and death of animal cells: A brief overview
    • Pedersen, P.L. Mitochondrial events in the life and death of animal cells: a brief overview. J. Bioenerg. Biomembr., 1999, 31, 291-304.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 291-304
    • Pedersen, P.L.1
  • 50
    • 0032525935 scopus 로고    scopus 로고
    • Hypoxia-induced expression of phosphoglycerate mutase B in fibroblasts
    • DOI 10.1046/j.1432-1327.1998.2540497.x
    • Takahashi, Y.; Takahashi, S.; Yoshimi, T.; Miura, T. Hypoxiainduced expression of phosphoglycerate mutase B in fibroblasts. Eur. J. Biochem., 1998, 254, 497-504. (Pubitemid 28308099)
    • (1998) European Journal of Biochemistry , vol.254 , Issue.3 , pp. 497-504
    • Takahashi, Y.1    Takahashi, S.2    Yoshimi, T.3    Miura, T.4
  • 51
  • 52
    • 33646917296 scopus 로고    scopus 로고
    • The plasma membrane lactate transporter MCT4, but not MCT1, is up-regulated by hypoxia through a HIF-1alpha-dependent mechanism
    • Ullah, M.S.; Davies, A.J.; Halestrap, A.P. The plasma membrane lactate transporter MCT4, but not MCT1, is up-regulated by hypoxia through a HIF-1alpha-dependent mechanism. J. Biol. Chem. 2006, 281, 9030-9037
    • (2006) J. Biol. Chem. , vol.281 , pp. 9030-9037
    • Ullah, M.S.1    Davies, A.J.2    Halestrap, A.P.3
  • 53
    • 19944399717 scopus 로고    scopus 로고
    • 6-Phosphofructo-2-kinase (pfkfb3) gene promoter contains hypoxia-inducible factor-1 binding sites necessary for transactivation in response to hypoxia
    • DOI 10.1074/jbc.M406096200
    • Obach, M.; Navarro-Sabate, A.; Caro, J.; Kong, X.; Duran, J.; Gómez, M.; Perales, J.C.; Ventura, F.; Rosa, J.L.; Bartrons, R. 6- Phosphofructo-2-kinase (pfkfb3) gene promoter contains hypoxiainducible factor-1 binding sites necessary for transactivation in response to hypoxia. J. Biol. Chem., 2004, 279, 53562-53570 (Pubitemid 40051863)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53562-53570
    • Obach, M.1    Navarro-Sabate, A.2    Caro, J.3    Kong, X.4    Duran, J.5    Gomez, M.6    Perales, J.C.7    Ventura, F.8    Rosa, J.L.9    Bartrons, R.10
  • 54
    • 24644488689 scopus 로고    scopus 로고
    • Regulation of phosphoglucose isomerase/autocrine motility factor expression by hypoxia
    • DOI 10.1096/fj.05-3699com
    • Funasaka, T.; Yanagawa, T.; Hogan, V.; Raz, A. Regulation of phosphoglucose isomerase/autocrine motility factor expression by hypoxia. FASEB J., 2005, 19, 1422-1430 (Pubitemid 41279000)
    • (2005) FASEB Journal , vol.19 , Issue.11 , pp. 1422-1430
    • Funasaka, T.1    Yanagawa, T.2    Hogan, V.3    Raz, A.4
  • 55
    • 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
  • 57
    • 34247842999 scopus 로고    scopus 로고
    • Functional properties and genomics of glucose transporters
    • Zhao, F.Q.; Keating, A.F. Functional properties and genomics of glucose transporters. Curr. Genomics, 2007, 8, 113-128
    • (2007) Curr. Genomics , vol.8 , pp. 113-128
    • Zhao, F.Q.1    Keating, A.F.2
  • 58
    • 0026447087 scopus 로고
    • Mammalian facilitative glucose transporters: Evidence for similar substrate recognition sites in functionally monomeric proteins
    • Burant, C.F.; Bell, G.I. Mammalian facilitative glucose transporters: evidence for similar substrate recognition sites in functionally monomeric proteins. Biochemistry, 1992, 31, 10414-10420
    • (1992) Biochemistry , vol.31 , pp. 10414-10420
    • Burant, C.F.1    Bell, G.I.2
  • 59
    • 0025886960 scopus 로고
    • Expression of human glucose transporters in Xenopus oocytes: Kinetic characterization and substrate specificities of the erythrocyte, liver, and brain isoforms
    • Gould, G.W.; Thomas, H.M.; Jess, T.J.; Bell, G.I. Expression of human glucose transporters in Xenopus oocytes: kinetic characterization and substrate specificities of the erythrocyte, liver, and brain isoforms. Biochemistry, 1991, 30, 5139-5145
    • (1991) Biochemistry , vol.30 , pp. 5139-5145
    • Gould, G.W.1    Thomas, H.M.2    Jess, T.J.3    Bell, G.I.4
  • 60
    • 0035800060 scopus 로고    scopus 로고
    • The predicted ATP-binding domains in the hexose transporter GLUT1 critically affect transporter activity
    • Liu, Q.; Vera, J.C.; Peng, H.; Golde, H. The predicted ATP-binding domains in the hexose transporter GLUT1 critically affect transporter activity. Biochemistry, 2001, 40, 7874-7881
    • (2001) Biochemistry , vol.40 , pp. 7874-7881
    • Liu, Q.1    Vera, J.C.2    Peng, H.3    Golde, H.4
  • 61
    • 7944226627 scopus 로고    scopus 로고
    • Genes of glycolysis are ubiquitously overexpressed in 24 cancer classes
    • Alterberg, B.; Greulich, K.O. Genes of glycolysis are ubiquitously overexpressed in 24 cancer classes. Genomics, 2004, 84, 1014-1020
    • (2004) Genomics , vol.84 , pp. 1014-1020
    • Alterberg, B.1    Greulich, K.O.2
  • 63
    • 0038714272 scopus 로고    scopus 로고
    • Isozymes of mammalian hexokinase: Structure, subcellular localization and metabolic function
    • Wilson, J.E. Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function. J. Exp. Biol., 2003, 206, 2049-2057
    • (2003) J. Exp. Biol. , vol.206 , pp. 2049-2057
    • Wilson, J.E.1
  • 64
    • 0037056002 scopus 로고    scopus 로고
    • Mitochondrial bound type II hexokinase: A key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention
    • Pedersen, P.L.; Mathupala, S.; Rempel, A.; Geschwind, J.F.; Ko, Y.H. Mitochondrial bound type II hexokinase: a key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention. Biochim. Biophys. Acta, 2002, 1555, 14-20.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 14-20
    • Pedersen, P.L.1    Mathupala, S.2    Rempel, A.3    Geschwind, J.F.4    Ko, Y.H.5
  • 65
    • 0025103254 scopus 로고
    • Tetrameric structure of mitochondrially bound rat brain hexokinase: A crosslinking study
    • DOI 10.1016/0003-9861(90)90040-6
    • Xie, G.; Wilson, J.E. Tetrameric structure of mitochondrially bound rat brain hexokinase: a crosslinking study. Arch. Biochem. Biophys., 1990, 276, 285-293 (Pubitemid 20041847)
    • (1990) Archives of Biochemistry and Biophysics , vol.276 , Issue.1 , pp. 285-293
    • Xie, G.1    Wilson, J.E.2
  • 66
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • DOI 10.1074/jbc.M109950200
    • Pastorino, J.G.; Shulga, N.; Hoek, J.B. Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis. J. Biol. Chem., 2002, 277, 7610-7618 (Pubitemid 34953160)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.9 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 67
    • 0347986675 scopus 로고    scopus 로고
    • Akt Inhibits Apoptosis Downstream of BID Cleavage via a Glucose-Dependent Mechanism Involving Mitochondrial Hexokinases
    • DOI 10.1128/MCB.24.2.730-740.2004
    • Majewski, N.; Nogueira, V.; Robey, R.B.; Hay, N. Akt inhibits apoptosis downstream of BID cleavage via a glucose-dependent mechanism involving mitochondrial hexokinases. Mol. Cell. Biol., 2004, 24, 730-740 (Pubitemid 38057924)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.2 , pp. 730-740
    • Majewski, N.1    Nogueira, V.2    Robey, R.B.3    Hay, N.4
  • 68
    • 33744930897 scopus 로고    scopus 로고
    • Suppression of apoptosis by cyclophilin D via stabilization of hexokinase II mitochondrial binding in cancer cells
    • DOI 10.1074/jbc.M513297200
    • Machida, K.; Ohta, Y.; Osada, H. Suppression of apoptosis by cyclophilin D via stabilization of hexokinase II mitochondrial binding in cancer cells. J. Biol. Chem., 2006, 281, 14314-14320 (Pubitemid 43848360)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 14314-14320
    • Machida, K.1    Ohta, Y.2    Osada, H.3
  • 69
    • 0023881240 scopus 로고
    • Purification and characterization of a bindable form of mitochondrial bound hexokinase from the highly glycolytic AS-30D rat hepatoma cell line
    • Nakashima, R.; Paggi, M.; Scott, L.J.; Pedersen, P.L. Purification and characterization of a bindable form of mitochondrial bound hexokinase from the highly glycolytic AS-30D rat hepatoma cell line. Cancer Res., 1988, 48, 913-919
    • (1988) Cancer Res. , vol.48 , pp. 913-919
    • Nakashima, R.1    Paggi, M.2    Scott, L.J.3    Pedersen, P.L.4
  • 70
  • 71
    • 0023498025 scopus 로고
    • Rat brain hexokinase: Location of the allosteric regulatory site in a structural domain at the N-terminus of the enzyme
    • White, T.K.; Wilson, J.E. Rat brain hexokinase: location of the allosteric regulatory site in a structural domain at the N-terminus of the enzyme. Arch. Biochem. Biophys., 1987, 259, 402-411
    • (1987) Arch. Biochem. Biophys. , vol.259 , pp. 402-411
    • White, T.K.1    Wilson, J.E.2
  • 72
    • 0023090673 scopus 로고
    • Hexokinase isoenzymes from the Novikoff hepatoma. Purification, kinetic and structural characterization, with emphasis on hexokinase C
    • Radojkovic, J.; Ureta, T. Hexokinase isoenzymes from the Novikoff hepatoma. Purification, kinetic and structural characterization, with emphasis on hexokinase C. Biochem. J., 1987, 242, 895-903. (Pubitemid 17049510)
    • (1987) Biochemical Journal , vol.242 , Issue.3 , pp. 895-903
    • Radojkovic, J.1    Ureta, T.2
  • 73
    • 0035829074 scopus 로고    scopus 로고
    • Glucose catabolism in the rabbit VX2 tumor model for liver cancer: Characterization and targeting hexokinase
    • Ko, Y.H.; Pedersen, P.L.; Geschwind, J.F. Glucose catabolism in the rabbit VX2 tumor model for liver cancer: characterization and targeting hexokinase. Cancer Lett., 2001, 173, 83-91.
    • (2001) Cancer Lett. , vol.173 , pp. 83-91
    • Ko, Y.H.1    Pedersen, P.L.2    Geschwind, J.F.3
  • 75
    • 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.; 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.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
  • 76
    • 0028879393 scopus 로고
    • The anti-glycolytic activity of 3-bromopyruvate on mature boar spermatozoa in vitro
    • Jones, A.R.; Gillan, L.; Milmlow, D. The anti-glycolytic activity of 3-bromopyruvate on mature boar spermatozoa in vitro. Contraception, 1995, 52, 317-320
    • (1995) Contraception , vol.52 , pp. 317-320
    • Jones, A.R.1    Gillan, L.2    Milmlow, D.3
  • 78
    • 0036376689 scopus 로고    scopus 로고
    • Detachment of glycolytic enzymes from cytoskeleton of Lewis lung carcinoma and colon adenocarcinoma cells induced by clotrimazole and its correlation to cell viability and morphology
    • DOI 10.1016/S1096-7192(02)00046-X, PII S109671920200046X
    • Penso, J.; Beitner, R. Detachment of glycolytic enzymes from cytoskeleton of Lewis lung carcinoma and colon adenocarcinoma cells induced by clotrimazole and its correlation to cell viability and morphology. Mol. Genet. Metab., 2002, 76, 181-188 (Pubitemid 35034550)
    • (2002) Molecular Genetics and Metabolism , vol.76 , Issue.3 , pp. 181-188
    • Penso, J.1    Beitner, R.2
  • 80
    • 24944536806 scopus 로고    scopus 로고
    • Inhibition of tumor growth and prolonged survival of rats with intracranial gliomas following administration of clotrimazole
    • Khalid, M.H.; Tokunaga, Y.; Caputy, A. J.; Walters, E. Inhibition of tumor growth and prolonged survival of rats with intracranial gliomas following administration of clotrimazole. J. Neurosurg., 2005, 103, 79-86. (Pubitemid 43193938)
    • (2005) Journal of Neurosurgery , vol.103 , Issue.1 , pp. 79-86
    • Humayun Khalid, M.1    Tokunaga, Y.2    Caputy, A.J.3    Walters, E.4
  • 81
    • 28844488320 scopus 로고    scopus 로고
    • The energy-less red blood cell is lost: Erythrocyte enzyme abnormalities of glycolysis
    • van Wijk, R.; van Solinge, W.W. The energy-less red blood cell is lost: erythrocyte enzyme abnormalities of glycolysis. Blood, 2005, 106, 4034-4042
    • (2005) Blood , vol.106 , pp. 4034-4042
    • Van Wijk, R.1    Van Solinge, W.W.2
  • 82
    • 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
  • 83
    • 0016825429 scopus 로고
    • Mechanistic implications of the pH independence of inhibition of phosphoglucose isomerase by neutral sugar phosphates
    • Chirgwin, J.M.; Parsons, T.F.; Noltmann, E.A. Mechanistic implications of the pH independence of inhibition of phosphoglucose isomerase by neutral sugar phosphates. J. Biol. Chem., 1975, 250, 7277-7279
    • (1975) J. Biol. Chem. , vol.250 , pp. 7277-7279
    • Chirgwin, J.M.1    Parsons, T.F.2    Noltmann, E.A.3
  • 84
    • 0019332614 scopus 로고
    • The pentose cycle. Control and essential function in HeLa cell nucleic acid synthesis
    • Reitzer, L.J.; Wice, B.M.; Kennell, D. The pentose cycle. Control and essential function in HeLa cell nucleic acid synthesis. J. Biol. Chem., 1980, 255, 5616-5626
    • (1980) J. Biol. Chem. , vol.255 , pp. 5616-5626
    • Reitzer, L.J.1    Wice, B.M.2    Kennell, D.3
  • 85
    • 0015855708 scopus 로고
    • Enzymic and cerebral metabolic effects of 2-deoxy-D-glucose
    • Horton, R.W.; Meldrum, B.S.; Bachelard, H.S. Enzymic and cerebral metabolic effects of 2-deoxy-D-glucose. J. Neurochem., 1973, 21, 507-520
    • (1973) J. Neurochem. , vol.21 , pp. 507-520
    • Horton, R.W.1    Meldrum, B.S.2    Bachelard, H.S.3
  • 87
    • 0035826677 scopus 로고    scopus 로고
    • Hypersensitization of tumor cells to glycolytic inhibitors
    • DOI 10.1021/bi002426w
    • Liu, H.; Hu, Y.P.; Savaraj, N.; Priebe, W.; Lampidis, T.J. Hypersensitization of tumor cells to glycolytic inhibitors. Biochemistry, 2001, 40, 5542-5547 (Pubitemid 32458256)
    • (2001) Biochemistry , vol.40 , Issue.18 , pp. 5542-5547
    • Liu, H.1    Hu, Y.P.2    Savaraj, N.3    Priebe, W.4    Lampidis, T.J.5
  • 88
    • 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.; Pruebe, W.; Braunschweiger, P.; Hamilton, K.; Tudmarsh, 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    Pruebe, W.3    Braunschweiger, P.4    Hamilton, K.5    Tudmarsh, G.F.6    De Young, L.R.7    Lampidis, T.J.8
  • 89
    • 17644376230 scopus 로고    scopus 로고
    • 2-deoxy-D-glucose enhances the cytotoxicity of topoisomerase inhibitors in human tumor cell lines
    • Dwarakanath, B.S.; Khaitan, D.; Ravindranath, T. 2-deoxy-Dglucose enhances the cytotoxicity of topoisomerase inhibitors in human tumor cell lines. Cancer Biol. Ther., 2004, 3, 864-870 (Pubitemid 41351053)
    • (2004) Cancer Biology and Therapy , vol.3 , Issue.9 , pp. 864-870
    • Dwarakanath, B.S.1    Khaitan, D.2    Ravindranath, T.3
  • 90
    • 24644489711 scopus 로고    scopus 로고
    • The glycolytic inhibitor 2-deoxy-D-glucose enhances the efficacy of etoposide in Ehrlich ascites tumor-bearing mice
    • Gupta, S.; Mathur, R.; Dwarakanath, B.S. The glycolytic inhibitor 2-deoxy-D-glucose enhances the efficacy of etoposide in Ehrlich ascites tumor-bearing mice. Cancer Biol. Ther., 2005, 4, 87-94.
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 87-94
    • Gupta, S.1    Mathur, R.2    Dwarakanath, B.S.3
  • 91
    • 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
  • 92
    • 0025971079 scopus 로고
    • Modulation of hexokinase association with mitochondria analyzed with quantitative threedimensional confocal microscopy
    • Lynch, R.M.; Fogarty, K.E.; Fay, F.S. Modulation of hexokinase association with mitochondria analyzed with quantitative threedimensional confocal microscopy. J. Cell Biol., 1991, 112, 385-395
    • (1991) J. Cell Biol. , vol.112 , pp. 385-395
    • Lynch, R.M.1    Fogarty, K.E.2    Fay, F.S.3
  • 93
    • 0023918653 scopus 로고
    • Analysis of the phosphofructokinase subunits and isoenzymes in human tissues
    • Dunaway, G.A.; Kasten, T.P.; Sebo, T.; Trapo, R. Analysis of the phosphofructokinase subunits and isoenzymes in human tissues. Biochem. J., 1988, 251, 677-683 (Pubitemid 18121401)
    • (1988) Biochemical Journal , vol.251 , Issue.3 , pp. 677-683
    • Dunaway, G.A.1    Kasten, T.P.2    Sebo, T.3    Trapp, R.4
  • 96
    • 0022844699 scopus 로고
    • Hormonal control of fructose 2,6- bisphosphate concentration in the HT29 human colon adenocarcinoma cell line. Alpha 2-adrenergic agonists counteract effect of vasoactive intestinal peptide
    • Denis, C.; Paris, H.; Murat, J.C. Hormonal control of fructose 2,6- bisphosphate concentration in the HT29 human colon adenocarcinoma cell line. Alpha 2-adrenergic agonists counteract effect of vasoactive intestinal peptide. Biochem. J., 1986, 239, 531-536
    • (1986) Biochem. J. , vol.239 , pp. 531-536
    • Denis, C.1    Paris, H.2    Murat, J.C.3
  • 97
    • 0022357684 scopus 로고
    • Fructose 2,6-bisphosphate and the control of glycolysis by glucocorticoids and by other agents in rat hepatoma cells
    • Loiseau, A.M.; Rousseau, G.G.; Hue, L. Fructose 2,6-bisphosphate and the control of glycolysis by glucocorticoids and by other agents in rat hepatoma cells. Cancer Res., 1985, 45, 4263-4269 (Pubitemid 16224884)
    • (1985) Cancer Research , vol.45 , Issue.9 , pp. 4263-4269
    • Loiseau, A.M.1    Rousseau, G.G.2    Hue, L.3
  • 98
    • 0038269017 scopus 로고    scopus 로고
    • Spatial clustering of isozyme-specific residues reveals unlikely determinants of isozyme specificity in fructose- 1,6-bisphosphate aldolase
    • Pezza, J.A.; Choi, K.H.; Berardini, T.Z.; Beernink, P.T.; Allen, K.N.; Tolan, D.R. Spatial clustering of isozyme-specific residues reveals unlikely determinants of isozyme specificity in fructose- 1,6-bisphosphate aldolase. J. Biol. Chem., 2003, 278, 17307-17313
    • (2003) J. Biol. Chem. , vol.278 , pp. 17307-17313
    • Pezza, J.A.1    Choi, K.H.2    Berardini, T.Z.3    Beernink, P.T.4    Allen, K.N.5    Tolan, D.R.6
  • 99
    • 0030891065 scopus 로고    scopus 로고
    • Selective inhibition of mitochondrial respiration and glycolysis in human leukaemic leucocytes by methylglyoxal
    • Biswas, S.; Ray, M.; Misra, S.; Dutta, D.P.; Ray, S. Selective inhibition of mitochondrial respiration and glycolysis in human leukaemic leucocytes by methylglyoxal. Biochem. J., 1997, 323, 343-348 (Pubitemid 27183114)
    • (1997) Biochemical Journal , vol.323 , Issue.2 , pp. 343-348
    • Biswas, S.1    Ray, M.2    Misra, S.3    Dutta, D.P.4    Ray, S.5
  • 100
    • 0030746213 scopus 로고    scopus 로고
    • Role of the glycolytic protein, glyceraldehyde-3- phosphate dehydrogenase, in normal cell function and in cell pathology
    • Sirover, M.A. Role of the glycolytic protein, glyceraldehyde-3- phosphate dehydrogenase, in normal cell function and in cell pathology. J. Cell Biochem., 1997, 66, 133-140
    • (1997) J. Cell Biochem. , vol.66 , pp. 133-140
    • Sirover, M.A.1
  • 101
    • 0033998548 scopus 로고    scopus 로고
    • Human glyceraldehydes 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells
    • Welch, J.E.; Brown, P.L.; O'Brien, D.A.; Magyar, P.L.; Bunch, D.O.; Mori, C.; Eddy, E. M. Human glyceraldehydes 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells. J. Androl., 2000, 21, 328-338
    • (2000) J. Androl. , vol.21 , pp. 328-338
    • Welch, J.E.1    Brown, P.L.2    O'Brien, D.A.3    Magyar, P.L.4    Bunch, D.O.5    Mori, C.6    Eddy, E.M.7
  • 102
    • 0025175531 scopus 로고
    • Action of gossypol and rhodamine 123 on wild type and multidrug-resistant MCF-7 human breast cancer cells: 31P nuclear magnetic resonance and toxicity studies
    • Jaroszewski, J.W.; Kaplan, O.; Cohen, J.S. Action of gossypol and rhodamine 123 on wild type and multidrug-resistant MCF-7 human breast cancer cells: 31P nuclear magnetic resonance and toxicity studies. Cancer Res., 1990, 50, 6936-6943
    • (1990) Cancer Res. , vol.50 , pp. 6936-6943
    • Jaroszewski, J.W.1    Kaplan, O.2    Cohen, J.S.3
  • 103
    • 0021355071 scopus 로고
    • Differential cytotoxic effect of gossypol on human melanoma, colon carcinoma, and other tissue culture cell lines
    • Tuszynski, G.P.; Cossu, G. Differential cytotoxic effect of gossypol on human melanoma, colon carcinoma, and other tissue culture cell lines. Cancer Res., 1984, 44, 768-771 (Pubitemid 14184616)
    • (1984) Cancer Research , vol.44 , Issue.2 , pp. 768-771
    • Tuszynski, G.P.1    Cossu, G.2
  • 104
    • 13944262237 scopus 로고    scopus 로고
    • (-)-Gossypol acts directly on the mitochondria to overcome Bcl-2- and Bcl-X(L)-mediated apoptosis resistance
    • Oliver, C.L.; Miranda, M.B.; Shangary, S.; Land, S.; Wang, S.; Johnson, D.E. (-)-Gossypol acts directly on the mitochondria to overcome Bcl-2- and Bcl-X(L)-mediated apoptosis resistance. Mol. Cancer Ther., 2005, 4, 23-31.
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 23-31
    • Oliver, C.L.1    Miranda, M.B.2    Shangary, S.3    Land, S.4    Wang, S.5    Johnson, D.E.6
  • 105
    • 0024334136 scopus 로고
    • An in vitro and in vivo study of antitumor effects of gossypol on human SW-13 adrenocortical carcinoma
    • Wu, Y.W.; Chik, C.L.; Knazek, R.A. An in vitro and in vivo study of antitumor effects of gossypol on human SW-13 adrenocortical carcinoma. Cancer Res., 1989, 49, 3754-3758
    • (1989) Cancer Res. , vol.49 , pp. 3754-3758
    • Wu, Y.W.1    Chik, C.L.2    Knazek, R.A.3
  • 108
    • 36249018450 scopus 로고    scopus 로고
    • Glucose-dependent active ATP depletion by koningic acid kills high-glycolytic cells
    • DOI 10.1016/j.bbrc.2007.10.199, PII S0006291X07023777
    • Kumagai, S.; Narasaki, R,; Hasumi, K. Glucosa-dependent active ATP depletion by koningic acid kills high-glycolytic cells. Biochem. Biophys. Res. Commun., 2008, 365, 362-368 (Pubitemid 350137298)
    • (2008) Biochemical and Biophysical Research Communications , vol.365 , Issue.2 , pp. 362-368
    • Kumagai, S.1    Narasaki, R.2    Hasumi, K.3
  • 109
    • 43849087330 scopus 로고    scopus 로고
    • Arsenic-based antineoplastic drugs and their mechanisms of action
    • Article ID 260146
    • Ralph, S.J. Arsenic-based antineoplastic drugs and their mechanisms of action. Metal Based Drugs., 2008, 2008, Article ID 260146.
    • (2008) Metal Based Drugs. , vol.2008
    • Ralph, S.J.1
  • 110
    • 0034649626 scopus 로고    scopus 로고
    • Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase
    • Lay, A.J.; Jiang, X.M.; Kisker, O.; Flynn, E.; Underwood, A.; Condron, R.; Hogg, P.J. Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase. Nature, 2000, 408, 869-873
    • (2000) Nature , vol.408 , pp. 869-873
    • Lay, A.J.1    Jiang, X.M.2    Kisker, O.3    Flynn, E.4    Underwood, A.5    Condron, R.6    Hogg, P.J.7
  • 111
    • 14344263143 scopus 로고    scopus 로고
    • Phosphoglycerate mutase BB isoenzyme deficiency in a patient with non-spherocytic anemia: Familial and metabolic studies
    • Repiso, A.; Ramirez-Bajo, M.J.; Vives-Corrons, J.L.; Carreras, J.; Climent, F. Phosphoglycerate mutase BB isoenzyme deficiency in a patient with non-spherocytic anemia: familial and metabolic studies. Haematologica, 2005, 90, 257-259 (Pubitemid 40293291)
    • (2005) Haematologica , vol.90 , Issue.2 , pp. 257-259
    • Repiso, A.1    Ramirez Bajo, M.J.2    Vives Corrons, J.-L.3    Carreras, J.4    Climent, F.5
  • 112
    • 0021782346 scopus 로고
    • Purification and properties of the phosphoglycerate mutase isozymes from the mouse
    • Fundele, R.; Krietsch, W.K. Purification and properties of the phosphoglycerate mutase isozymes from the mouse. Comp. Biochem. Physiol. B., 1985, 81, 965-968
    • (1985) Comp. Biochem. Physiol. B. , vol.81 , pp. 965-968
    • Fundele, R.1    Krietsch, W.K.2
  • 113
    • 0030953014 scopus 로고    scopus 로고
    • Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas
    • Durany, N.; Joseph, J.; Campo, E.; Molina, R.; Carreras, J. Phosphoglycerate mutase, 2,3 bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas. Br. J. Cancer, 1997, 75, 969-977 (Pubitemid 27122614)
    • (1997) British Journal of Cancer , vol.75 , Issue.7 , pp. 969-977
    • Durany, N.1    Joseph, J.2    Campo, E.3    Molina, R.4    Carreras, J.5
  • 114
    • 0033986792 scopus 로고    scopus 로고
    • Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase, creatine kinase and enolase activity and isoenzymes in breast carcinoma
    • Durany, N.; Joseph, J.; Jimenez, O.M.; Climent, F.; Fernández, P.L.; Rivera, F.; Carreras, J. Phosphoglycerate mutase, 2,3- bisphosphoglycerate phosphatase, creatine kinase and enolase activity and isoenzymes in breast carcinoma. Br. J. Cancer, 2000, 82, 20-27 (Pubitemid 30008953)
    • (2000) British Journal of Cancer , vol.82 , Issue.1 , pp. 20-27
    • Durany, N.1    Joseph, J.2    Jimenez, O.M.3    Climent, F.4    Fernandez, P.L.5    Rivera, F.6    Carreras, J.7
  • 116
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional α-enolase: Its role in diseases
    • Pancholi, V. Multifunctional alpha-enolase: its role in diseases. Cell. Mol. Life Sci., 2001, 58, 902-920 (Pubitemid 32652817)
    • (2001) Cellular and Molecular Life Sciences , vol.58 , Issue.7 , pp. 902-920
    • Pancholi, V.1
  • 117
    • 0021028735 scopus 로고
    • Characterization of αα, ββ, γγ and αγ human enolase isozymes, and preparation of hybrid enolases (αγ, βγ and αβ) from homodimeric forms
    • DOI 10.1016/0167-4838(83)90305-9
    • Shimizu, A.; Suzuki, F.; Kato, K. Characterization of alpha alpha, beta beta, gamma gamma and alpha gamma human enolase isozymes, and preparation of hybrid enolases (alpha gamma, beta gamma and alpha beta) from homodimeric forms. BBA-Prot. Struct. Mol. Enzymol., 1983, 748, 278-284 (Pubitemid 14240272)
    • (1983) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.748 , Issue.2 , pp. 278-284
    • Shimizu, A.1    Suzuki, F.2    Kato, K.3
  • 118
    • 0020392647 scopus 로고
    • Pyruvate kinase isozymes from rat
    • Imamura, K.; Tanaka, T. Pyruvate kinase isozymes from rat. Methods Enzymol., 1982, 90, 150-165
    • (1982) Methods Enzymol. , vol.90 , pp. 150-165
    • Imamura, K.1    Tanaka, T.2
  • 121
    • 0029778381 scopus 로고    scopus 로고
    • Usefulness of lactate dehydrogenase and its isoenzymes as indicators of lung damage or inflammation
    • Drent, M.; Cobben, N.A.; Henderson, R.F.; Wouters, E.F.M.; van Dieijen-Visser, M. Usefulness of lactate dehydrogenase and its isoenzymes as indicators of lung damage or inflammation. Eur. Respir. J., 1996, 9, 1736-1742
    • (1996) Eur. Respir. J. , vol.9 , pp. 1736-1742
    • Drent, M.1    Cobben, N.A.2    Henderson, R.F.3    Wouters, E.F.M.4    Van Dieijen-Visser, M.5
  • 122
    • 0017692233 scopus 로고
    • The effect of temperature on the kinetic constants of human lactate dehydrogenase 1 and 5
    • Buhl, S.N.; Jackson, K.Y.; Vanderlinde, R.E. The effect of temperature on the kinetic constants of human lactate dehydrogenase 1 and 5. Clin. Chim. Acta, 1977, 80, 265-270
    • (1977) Clin. Chim. Acta , vol.80 , pp. 265-270
    • Buhl, S.N.1    Jackson, K.Y.2    Vanderlinde, R.E.3
  • 123
    • 23944498840 scopus 로고    scopus 로고
    • Lactate dehydrogenase 5 (LDH5) relates to up-regulated hypoxia inducible factor pathway and metastasis in colorectal cancer
    • DOI 10.1007/s10585-005-2343-7
    • Koukourakis, M.I.; Giatromanolaki, A.; Simopoulos, C.; Polychronidis, A.; Sivridis, E. Lactate dehydrogenase 5 (LDH5) relates to up-regulated hypoxia inducible factor pathway and metastasis in colorectal cancer. Clin. Exp. Metastasis, 2005, 22, 25-30. (Pubitemid 41185858)
    • (2005) Clinical and Experimental Metastasis , vol.22 , Issue.1 , pp. 25-30
    • Koukourakis, M.I.1    Giatromanolaki, A.2    Simopoulos, C.3    Polychronidis, A.4    Sivridis, E.5
  • 124
    • 0014337517 scopus 로고
    • Effect of oxamate on glycolysis and respiration in sarcoma 37 ascites cells
    • Elwood, J.C. Effect of oxamate on glycolysis and respiration in sarcoma 37 ascites cells. Cancer Res., 1968, 28, 2056-2060
    • (1968) Cancer Res. , vol.28 , pp. 2056-2060
    • Elwood, J.C.1
  • 125
    • 2442644929 scopus 로고    scopus 로고
    • Armepavine oxalate induces cell death on CCRF-CEM leukemia cell line through an apoptotic pathway
    • Jow, G.M.; Wu, Y.C.;Guh, J.H.; Teng, C.M. Armepavine oxalate induces cell death on CCRF-CEM leukemia cell line through an apoptotic pathway. Life Sci., 2004, 75, 549-557
    • (2004) Life Sci. , vol.75 , pp. 549-557
    • Jow, G.M.1    Wu, Y.C.2    Guh, J.H.3    Teng, C.M.4
  • 126
    • 0028170474 scopus 로고
    • 2- And pH-gradients in multicellular spheroids and their relationship to cellular metabolism and radiation sensitivity of malignant human tumor cells
    • DOI 10.1016/0925-4439(94)90085-X
    • Görlach, A.; Acker, H. pO2- and pH-gradients in multicellular spheroids and their relationship to cellular metabolism and radiation sensitivity of malignant human tumor cells. BBA-Mol. Basis Dis., 1994, 1227, 105-112 (Pubitemid 24371737)
    • (1994) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1227 , Issue.3 , pp. 105-112
    • Gorlach, A.1    Acker, H.2
  • 127
    • 0023008536 scopus 로고
    • Rate-limiting steps for hepatic gluconeogenesis. Mechanism of oxamate inhibition of mitochondrial pyruvate metabolism
    • Martin-Requero, A.; Ayuso, M.S.; Parrilla, R. Rate-limiting steps for hepatic gluconeogenesis. Mechanism of oxamate inhibition of mitochondrial pyruvate metabolism. J. Biol. Chem., 1986, 261, 13973-13978
    • (1986) J. Biol. Chem. , vol.261 , pp. 13973-13978
    • Martin-Requero, A.1    Ayuso, M.S.2    Parrilla, R.3
  • 128
    • 0023607979 scopus 로고
    • Effect of oxalate and malonate on red cell metabolism
    • Beutler, E.; Forman, L.; West, C. Effect of oxalate and malonate on red cell metabolism. Blood, 1987, 70, 1389-1393 (Pubitemid 18026143)
    • (1987) Blood , vol.70 , Issue.5 , pp. 1389-1393
    • Beutler, E.1    Forman, L.2    West, C.3
  • 129
    • 33744783432 scopus 로고    scopus 로고
    • Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance
    • DOI 10.1016/j.ccr.2006.04.023, PII S1535610806001450
    • 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 (Pubitemid 43832190)
    • (2006) Cancer Cell , vol.9 , Issue.6 , pp. 425-434
    • Fantin, V.R.1    St-Pierre, J.2    Leder, P.3
  • 131
    • 1242340302 scopus 로고    scopus 로고
    • The SLC16 gene family - From monocarboxylate transporters (MCTs) to aromatic amino acid transporters and beyond
    • DOI 10.1007/s00424-003-1067-2, The ABCs of Solute Carriers: Physiological, Pathological and Therapeutic Implications of Human Membrane Transport Proteins
    • Halestrap, A.P.; Meredith, D. The SLC16 gene family-from monocarboxylate transporters (MCTs) to aromatic amino acid transporters and beyond. Pflugers Arch., 2004, 447, 619-628 (Pubitemid 38241446)
    • (2004) Pflugers Archiv European Journal of Physiology , vol.447 , Issue.5 , pp. 619-628
    • Halestrap, A.P.1    Meredith, D.2
  • 133
    • 34249293335 scopus 로고    scopus 로고
    • Monocarboxylate transporter 4 regulates maturation and trafficking of CD147 to the plasma membrane in the metastatic breast cancer cell line MDA-MB-231
    • Gallagher, S.M.; Castorino, J.J.; Wang, D.; Philp, N.J. Monocarboxylate transporter 4 regulates maturation and trafficking of CD147 to the plasma membrane in the metastatic breast cancer cell line MDA-MB-231. Cancer Res., 2007, 67, 4182-4189
    • (2007) Cancer Res. , vol.67 , pp. 4182-4189
    • Gallagher, S.M.1    Castorino, J.J.2    Wang, D.3    Philp, N.J.4
  • 134
    • 33846028735 scopus 로고    scopus 로고
    • Monocarboxylate transporter 1 mediates DL-2-hydroxy-(4-methylthio) butanoic acid transport across the apical membrane of Caco-2 cell monolayers
    • Martín-Venegas, R.; Rodríguez-Lagunas, M.J.; Geraert, P.A.; Ferrer, R. Monocarboxylate transporter 1 mediates DL-2-Hydroxy-(4- methylthio)butanoic acid transport across the apical membrane of Caco-2 cell monolayers. J. Nutr., 2007, 137, 49-54. (Pubitemid 46052858)
    • (2007) Journal of Nutrition , vol.137 , Issue.1 , pp. 49-54
    • Martin-Venegas, R.1    Rodriguez-Lagunas, M.J.2    Geraert, P.-A.3    Ferrer, R.4
  • 137
    • 33745110220 scopus 로고    scopus 로고
    • Tumor pH controls the in vivo efficacy of weak acid and base chemotherapeutics
    • DOI 10.1158/1535-7163.MCT-06-0024
    • Gerweck, L.E.; Vijayappa, S.; Kozin, S. Tumor pH controls the in vivo efficacy of weak acid and base chemotherapeutics. Mol. Cancer Ther., 2006, 5, 1275-1279 (Pubitemid 43881320)
    • (2006) Molecular Cancer Therapeutics , vol.5 , Issue.5 , pp. 1275-1279
    • Gerweck, L.E.1    Vijayappa, S.2    Kozin, S.3
  • 139
    • 0242666433 scopus 로고    scopus 로고
    • Identification of a new chondropsin class of antitumor compound that selectively inhibits V-ATPases
    • Bowman, E.J.; Gustafson, K.R.; Bowman, B.J.; Boyd, M.R. Identification of a new chondropsin class of antitumor compound that selectively inhibits V-ATPases. J. Biol. Chem., 2003, 278, 44147-44152
    • (2003) J. Biol. Chem. , vol.278 , pp. 44147-44152
    • Bowman, E.J.1    Gustafson, K.R.2    Bowman, B.J.3    Boyd, M.R.4
  • 140
    • 23044467723 scopus 로고    scopus 로고
    • The growth and metastasis of human hepatocellular carcinoma xenografts are inhibited by small interfering RNA targeting to the subunit ATP6L of proton pump
    • DOI 10.1158/0008-5472.CAN-04-3822
    • Lu, X.; Qin, W.; Li, J.; Tan, N.; Pan, D.; Zhang, H.; Xie, L.; Yao, G.; Shu, H.; Yao, M.; Wan, D.; Gu, J.; Yang, S. The growth and metastasis of human hepatocellular carcinoma xenografts are inhibited by small interfering RNA targeting to the subunit ATP6L of proton pump. Cancer Res., 2005, 65, 6843-6849 (Pubitemid 41060723)
    • (2005) Cancer Research , vol.65 , Issue.15 , pp. 6843-6849
    • Lu, X.1    Qin, W.2    Li, J.3    Tan, N.4    Pan, D.5    Zhang, H.6    Xie, L.7    Yao, G.8    Shu, H.9    Yao, M.10    Wan, D.11    Gu, J.12    Yang, S.13
  • 141
    • 33947724515 scopus 로고    scopus 로고
    • HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells
    • Fukuda, R.; Zhang, H.; Kim, J.W.; Shimoda, L.; Dang, C.V.; Semenza, G.L. HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. Cell, 2007, 129, 111-122
    • (2007) Cell , vol.129 , pp. 111-122
    • Fukuda, R.1    Zhang, H.2    Kim, J.W.3    Shimoda, L.4    Dang, C.V.5    Semenza, G.L.6
  • 142
    • 34250361521 scopus 로고    scopus 로고
    • Cytochrome c oxidase activity and oxygen tolerance
    • Campian, J.L.; Gao, X.; Qian, M.; Eaton, J.W. Cytochrome c oxidase activity and oxygen tolerance. J. Biol. Chem., 2007, 282, 12430-12438
    • (2007) J. Biol. Chem. , vol.282 , pp. 12430-12438
    • Campian, J.L.1    Gao, X.2    Qian, M.3    Eaton, J.W.4
  • 144
    • 34247131735 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase regulatory mechanisms and inhibition in treating diabetes, heart ischemia, and cancer
    • DOI 10.1007/s00018-007-6380-z
    • Roche, T.E.; Hiromasa, Y. Pyruvate dehydrogenase kinase regulatory mechanisms and inhibition in treating diabetes, heart ischemia, and cancer. Cell Mol. Life Sci., 2007, 64, 830-849 (Pubitemid 46597752)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.7-8 , pp. 830-849
    • Roche, T.E.1    Hiromasa, Y.2
  • 145
  • 146
    • 0031972736 scopus 로고    scopus 로고
    • Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex
    • Bowker-Kinley, M.M.; Davis, W.I.; Wu, P.; Harris, R.A.; Popov, K.M. Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex. Biochem. J., 1998, 329, 191-196 (Pubitemid 28022308)
    • (1998) Biochemical Journal , vol.329 , Issue.1 , pp. 191-196
    • Bowker-Kinley, M.M.1    Davis, W.I.2    Wu, P.3    Harris, R.A.4    Popov, K.M.5
  • 147
    • 0035813150 scopus 로고    scopus 로고
    • Site Specificity of Four Pyruvate Dehydrogenase Kinase Isoenzymes toward the Three Phosphorylation Sites of Human Pyruvate Dehydrogenase
    • DOI 10.1074/jbc.M103069200
    • Korotchkina, L.G.; Patel, M.S. Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase. J. Biol. Chem., 2001, 276, 37223-37229 (Pubitemid 37384139)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.40 , pp. 37223-37229
    • Korotchkina, L.G.1    Patel, M.S.2
  • 148
    • 0035882093 scopus 로고    scopus 로고
    • Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites
    • DOI 10.1042/0264-6021:3580069
    • Kolobova, E.; Tuganova, A.; Boulatnikov, I.; Popov, K.M. Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites. Biochem. J., 2001, 358, 69-77. (Pubitemid 32778099)
    • (2001) Biochemical Journal , vol.358 , Issue.1 , pp. 69-77
    • Kolobova, E.1    Tuganova, A.2    Boulatnikov, I.3    Popov, K.M.4
  • 149
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • Papandreou, I.; Cairns, R.A.; Fontana, L.; Lim, A.L.; Denko, N.C. HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metab., 2006, 3, 187-197
    • (2006) Cell Metab. , vol.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 150
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1- mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia
    • 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
  • 153
    • 34247524169 scopus 로고    scopus 로고
    • Cellular redox status regulates hypoxia inducible factor-1 activity. Role in tumour development
    • Martínez-Sánchez, G.; Giuliani, A. Cellular redox status regulates hypoxia inducible factor-1 activity. Role in tumour development. J. Exp. Clin. Cancer Res., 2007, 26, 39-50. (Pubitemid 46656031)
    • (2007) Journal of Experimental and Clinical Cancer Research , vol.26 , Issue.1 , pp. 39-50
    • Martinez-Sanchez, G.1    Giuliani, A.2
  • 157
    • 43049158067 scopus 로고    scopus 로고
    • Inhibition of tumor cell growth in the liver by RNA interference-mediated suppression of HIF-1alpha expression in tumor cells and hepatocytes
    • Takahashi, Y.; Nishikawa, M.; Takakura, Y. Inhibition of tumor cell growth in the liver by RNA interference-mediated suppression of HIF-1alpha expression in tumor cells and hepatocytes. Gene Ther., 2008, 15, 572-582
    • (2008) Gene Ther. , vol.15 , pp. 572-582
    • Takahashi, Y.1    Nishikawa, M.2    Takakura, Y.3
  • 158
    • 33846110857 scopus 로고    scopus 로고
    • Vitexin, an HIF-1alpha inhibitor, has anti-metastatic potential in PC12 cells
    • Choi, H.J.; Eun, J.S.; Kim, B.G.; Kim, S.Y.; Jeon, H.; Soh, Y. Vitexin, an HIF-1alpha inhibitor, has anti-metastatic potential in PC12 cells. Mol. Cells, 2006, 22, 291-299
    • (2006) Mol. Cells , vol.22 , pp. 291-299
    • Choi, H.J.1    Eun, J.S.2    Kim, B.G.3    Kim, S.Y.4    Jeon, H.5    Soh, Y.6
  • 159
    • 51049095933 scopus 로고    scopus 로고
    • Topotecan inhibits vascular endothelial growth factor production and angiogenic activity induced by hypoxia in human neuroblastoma by targeting hypoxia-inducible factor- 1alpha and -2alpha
    • Puppo, M.; Battaglia, F., Ottaviano, C.; Delfino, S.; Ribatti, D.; Varesio, L.; Bosco, M.C. Topotecan inhibits vascular endothelial growth factor production and angiogenic activity induced by hypoxia in human neuroblastoma by targeting hypoxia-inducible factor- 1alpha and -2alpha. Mol. Cancer Ther., 2008, 7, 1974-1984
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1974-1984
    • Puppo, M.1    Battaglia, F.2    Ottaviano, C.3    Delfino, S.4    Ribatti, D.5    Varesio, L.6    Bosco, M.C.7
  • 161
    • 0041382820 scopus 로고    scopus 로고
    • The hypoxic response of tumors is dependent on their microenvironment
    • DOI 10.1016/S1535-6108(03)00194-6
    • Blouw, B,; Song, H.; Tihan, T.; Bosze, J.; Ferrara, N.; Gerber, H.P.; Johnson, R.S.; Bergers G. The hypoxic response of tumors is dependent on their microenvironment. Cancer Cell, 2003, 4, 133-146 (Pubitemid 37040829)
    • (2003) Cancer Cell , vol.4 , Issue.2 , pp. 133-146
    • Blouw, B.1    Song, H.2    Tihan, T.3    Bosze, J.4    Ferrara, N.5    Gerber, H.-P.6    Johnson, R.S.7    Bergers, G.8
  • 162
    • 20144370794 scopus 로고    scopus 로고
    • Physiological activation of hypoxia inducible factor-1 in human skeletal muscle
    • DOI 10.1096/fj.04-2304fje
    • Ameln, H.; Gustafsson, T.; Sundberg, C.J.; Okamoto, K.; Jansson, E,; Poellinger, L.; Makino, Y. Physiological activation of hypoxia inducible factor-1 in human skeletal muscle. FASEB J., 2005, 19, 1009-1011 (Pubitemid 40827734)
    • (2005) FASEB Journal , vol.19 , Issue.8 , pp. 1009-1011
    • Ameln, H.1    Gustafsson, T.2    Sundberg, C.J.3    Okamoto, K.4    Jansson, E.5    Poellinger, L.6    Makino, Y.7
  • 163
    • 30944462014 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha expression in human endometrium and its regulation by prostaglandin Eseries prostanoid receptor 2 (EP2)
    • Critchley, H.O.; Osei, J.; Henderson, T.A.; Boswell, L.; Sales, K.J.; Jabbour, H.N.; Hiranio, N. Hypoxia-inducible factor-1alpha expression in human endometrium and its regulation by prostaglandin Eseries prostanoid receptor 2 (EP2). Endocrinology, 2006, 147, 744-753
    • (2006) Endocrinology , vol.147 , pp. 744-753
    • Critchley, H.O.1    Osei, J.2    Henderson, T.A.3    Boswell, L.4    Sales, K.J.5    Jabbour, H.N.6    Hiranio, N.7
  • 164
    • 0037086662 scopus 로고    scopus 로고
    • α-Tocopheryl succinate, an agent with in vivo anti-tumour activity, induces apoptosis by causing lysosomal instability
    • DOI 10.1042/0264-6021:3620709
    • Neuzil, J., Zhao, M., Ostermann, G., Sticha, M., Gellert, N., Weber, C., Eaton, J.W., Brunk, U.T. Alpha-tocopheryl succinate, an agent with in vivo anti-tumour activity, induces apoptosis by causing lysosomal instability. Biochem. J., 2002, 362, 709-715 (Pubitemid 34242323)
    • (2002) Biochemical Journal , vol.362 , Issue.3 , pp. 709-715
    • Neuzil, J.1    Zhao, M.2    Ostermann, G.3    Sticha, M.4    Gellert, N.5    Weber, C.6    Eaton, J.W.7    Brunk, U.T.8
  • 165
    • 0021051165 scopus 로고
    • Isozyme patterns of normal, benign, and malignant human breast tissues
    • Balinsky, D.; Platz, C.E.; Lewis, J.W. Isozyme patterns of normal, benign, and malignant human breast tissues. Cancer Res., 1983, 43, 5895-5901
    • (1983) Cancer Res. , vol.43 , pp. 5895-5901
    • Balinsky, D.1    Platz, C.E.2    Lewis, J.W.3
  • 166
    • 0037108709 scopus 로고    scopus 로고
    • High expression of inducible 6-phosphofructo-2-kinase/fructose-2,6- bisphosphatase (iPFK-2; PFKFB3) in human cancers
    • Atsumi, T.; Chesney, J.; Metz, A.; Leng, L.; Donnelly, S.; Makita, Z.; Mitchell, R.; Bucala, R. High expression of inducible 6-phosphofructo- 2-kinase/fructose-2,6-bisphosphatase (iPFK-2; PFKFB3) in human cancers. Cancer Res., 2002, 62, 5881-5887 (Pubitemid 35204749)
    • (2002) Cancer Research , vol.62 , Issue.20 , pp. 5881-5887
    • Atsumi, T.1    Chesney, J.2    Metz, C.3    Leng, L.4    Donnelly, S.5    Makita, Z.6    Mitchell, R.7    Bucala, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.