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Volumn 4, Issue 15, 2004, Pages 1623-1635

Iron chelators in cancer chemotherapy

Author keywords

Apoptosis; Cancer; Cell cycle; Cytotoxicity; Desferrioxamine; Drug design; Iron depletion; Ribonucleotide reductase

Indexed keywords

1 FORMYLISOQUINOLINE THIOSEMICARBAZONE; 1,2 PROPANEDIAMINE N,N' DIACETAMIDE N,N' DIACETIC ACID; 2 HYDROXY 1 NAPHTHYLALDEHYDE ISONICOTINOYLHYDRAZONE; 3 AMINOPICOLINALDEHYDE THIOSEMICARBAZONE; 5 AMINO 4 METHYLISOQUINOLINE 1 CARBOXALDEHYDE THIOSEMICARBAZONE; 5 HYDROXYPICOLINALDEHYDE THIOSEMICARBAZONE; ANTHRACYCLINE DERIVATIVE; CICLOPIROXOLAMINE; DAUNORUBICIN; DEFEROXAMINE; DEFERRIFERRITHIOCIN; DITHIZONE; DOXORUBICIN; HYDROXYUREA; IRON CHELATING AGENT; IRON COMPLEX; MIMOSINE; N(G) METHYLARGININE; PROTOCATECHUIC ACID; PYRIDINE DERIVATIVE; PYRIDOXAL 3 FLUOROBENZOYLHYDRAZONE; PYRIDOXAL ISONICOTINOYLHYDRAZONE; QUINOLINOL DERIVATIVE; RAZOXANE; REACTIVE OXYGEN METABOLITE; TACHPYRIDINE; THIOSEMICARBAZONE DERIVATIVE; THUJAPLICIN; TRENSOX; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 10644257442     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/1568026043387269     Document Type: Review
Times cited : (185)

References (172)
  • 1
    • 0037631496 scopus 로고    scopus 로고
    • Iron chelators for the treatment of iron overload disease: Relationship between structure, redox activity, and toxicity
    • Chaston, T. B. and Richardson, D. R. Iron chelators for the treatment of iron overload disease: relationship between structure, redox activity, and toxicity. Am. J. Hematol. 2003, 73, 200-210.
    • (2003) Am. J. Hematol. , vol.73 , pp. 200-210
    • Chaston, T.B.1    Richardson, D.R.2
  • 2
    • 0013192406 scopus 로고    scopus 로고
    • Pyridoxal isonicotinoyl hydrazone and its analogues
    • Hershko, C. Ed.; Plenum Press: New York
    • Buss, J. L.; Hermes-Lima, M.; and Ponka, P. Pyridoxal isonicotinoyl hydrazone and its analogues. In Iron Chelating Therapy Hershko, C. Ed.; Plenum Press: New York, 2002.
    • (2002) Iron Chelating Therapy
    • Buss, J.L.1    Hermes-Lima, M.2    Ponka, P.3
  • 3
    • 0024307575 scopus 로고
    • Early treatment with deferoxamine limits myocardial ischemic/reperfusion injury
    • Reddy, B. R.; Kloner, R. A.; and Przyklenk, K. Early treatment with deferoxamine limits myocardial ischemic/reperfusion injury. Free Rad. Biol. Med. 1989, 7, 45-52.
    • (1989) Free Rad. Biol. Med. , vol.7 , pp. 45-52
    • Reddy, B.R.1    Kloner, R.A.2    Przyklenk, K.3
  • 4
    • 0024580950 scopus 로고
    • Modification of disease by preventing free radical formation: A new concept in pharmacological intervention
    • Ward, P. A.; Warren, J. S.; Till, G. O.; Varani, J.; and Johnson, K. J. Modification of disease by preventing free radical formation: a new concept in pharmacological intervention. Bailliere's Clin. Haematol. 1989, 2, 391-402.
    • (1989) Bailliere's Clin. Haematol. , vol.2 , pp. 391-402
    • Ward, P.A.1    Warren, J.S.2    Till, G.O.3    Varani, J.4    Johnson, K.J.5
  • 6
    • 0030891276 scopus 로고    scopus 로고
    • The potential role of iron chelators in the treatment of Parkinson's disease and related neurological disorders
    • Gassen, M. and Youdim, M. B. The potential role of iron chelators in the treatment of Parkinson's disease and related neurological disorders. Pharmacol. Toxicol. 1997, 80, 159-166.
    • (1997) Pharmacol. Toxicol. , vol.80 , pp. 159-166
    • Gassen, M.1    Youdim, M.B.2
  • 7
    • 0023880378 scopus 로고
    • Superoxide dependent iron release from ferritin in inflammatory diseases
    • Biemond, P.; Swaak, A. J.; van Eijk, H. G.; and Koster, J. F. Superoxide dependent iron release from ferritin in inflammatory diseases. Free Rad. Biol. Med. 1988, 4, 185-198.
    • (1988) Free Rad. Biol. Med. , vol.4 , pp. 185-198
    • Biemond, P.1    Swaak, A.J.2    van Eijk, H.G.3    Koster, J.F.4
  • 8
    • 0036269005 scopus 로고    scopus 로고
    • Iron chelators as therapeutic agents for the treatment of cancer
    • Richardson, D. R. Iron chelators as therapeutic agents for the treatment of cancer. Crit. Rev. Oncol. Hematol. 2002, 42, 267-281.
    • (2002) Crit. Rev. Oncol. Hematol. , vol.42 , pp. 267-281
    • Richardson, D.R.1
  • 9
    • 0031436976 scopus 로고    scopus 로고
    • Potential of iron chelators as effective antiproliferative agents
    • Richardson, D. R. Potential of iron chelators as effective antiproliferative agents. Can. J. Physiol. Pharmacol. 1997, 75, 1164-1180.
    • (1997) Can. J. Physiol. Pharmacol. , vol.75 , pp. 1164-1180
    • Richardson, D.R.1
  • 10
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson, D. R. and Ponka, P. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta 1997, 1331, 1-40.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 13
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti, F. M. and Torti, S. V. Regulation of ferritin genes and protein. Blood 2002, 99, 3505-3516.
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 14
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P. M. and Arosio, P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1996, 1275, 161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 15
    • 0041893905 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in eukaryotes: A novel task of mitochondria that is inherited from bacteria
    • Muhlenhoff, U. and Lill, R. Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria. Biochim. Biophys. Acta 2000, 1459, 370-382.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 370-382
    • Muhlenhoff, U.1    Lill, R.2
  • 16
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • Guo, B.; Phillips, J. D.; Yu, Y.; and Leibold, E. A. Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. J. Biol. Chem. 1995, 270, 21645-21651.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 17
    • 0029833706 scopus 로고    scopus 로고
    • The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase
    • Cooper, C. E.; Lynagh, G. R.; Hoyes, K. P.; Hider, R. C.; Cammack, R.; and Porter, J. B. The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase. J. Biol. Chem. 1996, 271, 20291-20299.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20291-20299
    • Cooper, C.E.1    Lynagh, G.R.2    Hoyes, K.P.3    Hider, R.C.4    Cammack, R.5    Porter, J.B.6
  • 18
    • 0036570964 scopus 로고    scopus 로고
    • A review of fluorescence methods for assessing labile iron in cells and biological fluids
    • Esposito, B. P.; Epsztejn, S.; Breuer, W.; and Cabantchik, Z. I. A review of fluorescence methods for assessing labile iron in cells and biological fluids. Anal. Biochem. 2002, 304, 1-18.
    • (2002) Anal. Biochem. , vol.304 , pp. 1-18
    • Esposito, B.P.1    Epsztejn, S.2    Breuer, W.3    Cabantchik, Z.I.4
  • 19
    • 0027251053 scopus 로고
    • The pecking order of free radicals and antioxidants: Lipid peroxidation, alpha-tocopherol, and ascorbate
    • Buettner, G. R. The pecking order of free radicals and antioxidants: lipid peroxidation, alpha-tocopherol, and ascorbate. Arch. Biochem. Biophys. 1993, 300, 535-543.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 535-543
    • Buettner, G.R.1
  • 20
    • 0035874476 scopus 로고    scopus 로고
    • Subcellular distribution of chelatable iron: A laser scanning microscopic study in isolated hepatocytes and liver endothelial cells
    • Petrat, F.; de Groot, H.; and Rauen, U. Subcellular distribution of chelatable iron: a laser scanning microscopic study in isolated hepatocytes and liver endothelial cells. Biochem. J. 2001, 356, 61-69.
    • (2001) Biochem. J. , vol.356 , pp. 61-69
    • Petrat, F.1    de Groot, H.2    Rauen, U.3
  • 21
    • 0018850974 scopus 로고
    • Transferrin and transferrin receptors in carcinoma of the breast
    • Faulk, W. P.; Hsi, B. L.; and Stevens, P. J. Transferrin and transferrin receptors in carcinoma of the breast. Lancet 1980 2, 390-392.
    • (1980) Lancet , vol.2 , pp. 390-392
    • Faulk, W.P.1    Hsi, B.L.2    Stevens, P.J.3
  • 22
    • 0026034726 scopus 로고
    • Transferrin receptor activity as a marker in transitional cell carcinoma of the bladder
    • Basar, I.; Ayhan, A.; Bircan, K.; Ergen, A.; and Tasar, C. Transferrin receptor activity as a marker in transitional cell carcinoma of the bladder. Br. J. Urol. 1991, 67, 165-168.
    • (1991) Br. J. Urol. , vol.67 , pp. 165-168
    • Basar, I.1    Ayhan, A.2    Bircan, K.3    Ergen, A.4    Tasar, C.5
  • 23
    • 0025057114 scopus 로고
    • Elevated transferrin receptor content in human prostate cancer cell lines assessed in vitro and in vivo
    • Keer, H. N.; Kozlowski, J. M.; Tsai, Y. C.; Lee, C.; McEwan, R. N.; and Grayhack, J. T. Elevated transferrin receptor content in human prostate cancer cell lines assessed in vitro and in vivo. J. Urol. 1990, 143, 381-385.
    • (1990) J. Urol. , vol.143 , pp. 381-385
    • Keer, H.N.1    Kozlowski, J.M.2    Tsai, Y.C.3    Lee, C.4    McEwan, R.N.5    Grayhack, J.T.6
  • 24
    • 0019586989 scopus 로고
    • Ubiquitous cell-surface glycoprotein on tumor cells is proliferation-associated receptor for transferrin
    • Sutherland, R.; Delia, D.; Schneider, C.; Newman, R.; Kemshead, J.; and Greaves, M. Ubiquitous cell-surface glycoprotein on tumor cells is proliferation-associated receptor for transferrin. Proc. Natl. Acad. Sci. USA 1981, 78, 4515-4519.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4515-4519
    • Sutherland, R.1    Delia, D.2    Schneider, C.3    Newman, R.4    Kemshead, J.5    Greaves, M.6
  • 25
    • 0018603336 scopus 로고
    • Modulation of cell surface iron transferrin receptors by cellular density and state of activation
    • Larrick, J. W. and Cresswell, P. Modulation of cell surface iron transferrin receptors by cellular density and state of activation. J Supramol. Struct. 1979, 11, 579-586.
    • (1979) J. Supramol. Struct. , vol.11 , pp. 579-586
    • Larrick, J.W.1    Cresswell, P.2
  • 26
    • 0033613854 scopus 로고    scopus 로고
    • Coordinated regulation of iron-controlling genes, H-ferritin and IRP2, by c-MYC
    • Wu, K. J.; Polack, A.; and Dalla-Favera, R. Coordinated regulation of iron-controlling genes, H-ferritin and IRP2, by c-MYC. Science 1999, 283, 676-679.
    • (1999) Science , vol.283 , pp. 676-679
    • Wu, K.J.1    Polack, A.2    Dalla-Favera, R.3
  • 29
    • 0018955647 scopus 로고
    • The pathogenesis of rat liver cancer caused by chemical carcinogens
    • Williams, G. M. The pathogenesis of rat liver cancer caused by chemical carcinogens. Biochim. Biophys. Acta 1980, 605 167-189.
    • (1980) Biochim. Biophys. Acta , vol.605 , pp. 167-189
    • Williams, G.M.1
  • 30
    • 0014834767 scopus 로고
    • Rat ferritin isoproteins and their response to iron administration in a series of hepatic tumors and in normal and regenerating liver
    • Linder, M.; Munro, H. N.; and Morris, H. P. Rat ferritin isoproteins and their response to iron administration in a series of hepatic tumors and in normal and regenerating liver. Cancer Res. 1970, 30, 2231-2239.
    • (1970) Cancer Res. , vol.30 , pp. 2231-2239
    • Linder, M.1    Munro, H.N.2    Morris, H.P.3
  • 31
    • 0018837540 scopus 로고
    • Serum ferritin as a guide to therapy in neuroblastoma
    • Hann, H. W.; Levy, H. M.; and Evans, A. E. Serum ferritin as a guide to therapy in neuroblastoma. Cancer Res. 1980, 40 1411-1413.
    • (1980) Cancer Res. , vol.40 , pp. 1411-1413
    • Hann, H.W.1    Levy, H.M.2    Evans, A.E.3
  • 32
    • 0021123640 scopus 로고
    • Human ferritins present in the sera of nude mice transplanted with human neuroblastoma or hepatocellular carcinoma
    • Hann, H. L.; Stahlhut, M. W.; and Millman, I. Human ferritins present in the sera of nude mice transplanted with human neuroblastoma or hepatocellular carcinoma. Cancer Res. 1984, 44, 3898-3901.
    • (1984) Cancer Res. , vol.44 , pp. 3898-3901
    • Hann, H.L.1    Stahlhut, M.W.2    Millman, I.3
  • 33
    • 0028609224 scopus 로고
    • Iron metabolism in inflammation
    • Konijn, A. M. Iron metabolism in inflammation. Bailliere's Clin. Haematol. 1994, 7, 829-849.
    • (1994) Bailliere's Clin. Haematol. , vol.7 , pp. 829-849
    • Konijn, A.M.1
  • 35
    • 0028216949 scopus 로고
    • Moderate elevation of body iron level and increased risk of cancer occurrence and death
    • Stevens, R. G.; Graubard, B. I.; Micozzi, M. S.; Neriishi, K.; and Blumberg, B. S. Moderate elevation of body iron level and increased risk of cancer occurrence and death. Int. J. Cancer 1994, 56, 364-369.
    • (1994) Int. J. Cancer , vol.56 , pp. 364-369
    • Stevens, R.G.1    Graubard, B.I.2    Micozzi, M.S.3    Neriishi, K.4    Blumberg, B.S.5
  • 36
    • 0026795025 scopus 로고
    • Influence of dietary iron overload on cell proliferation and intestinal tumorigenesis in mice
    • Siegers, C. P.; Bumann, D.; Trepkau, H. D.; Schadwinkel, B.; and Baretton, G. Influence of dietary iron overload on cell proliferation and intestinal tumorigenesis in mice. Cancer Lett. 1992, 65, 245-249.
    • (1992) Cancer Lett. , vol.65 , pp. 245-249
    • Siegers, C.P.1    Bumann, D.2    Trepkau, H.D.3    Schadwinkel, B.4    Baretton, G.5
  • 37
    • 0023778722 scopus 로고
    • Dietary iron enhances the tumor rate in dimethylhydrazine-induced colon carcinogenesis in mice
    • Siegers, C. P.; Bumann, D.; Baretton, G.; and Younes, M. Dietary iron enhances the tumor rate in dimethylhydrazine-induced colon carcinogenesis in mice. Cancer Lett. 1988, 41, 251-256.
    • (1988) Cancer Lett. , vol.41 , pp. 251-256
    • Siegers, C.P.1    Bumann, D.2    Baretton, G.3    Younes, M.4
  • 38
    • 0036046677 scopus 로고    scopus 로고
    • Molecular targets for prevention of hepatocellular carcinoma
    • Blum, H. E. Molecular targets for prevention of hepatocellular carcinoma. Dig. Dis. 2002, 20, 81-90.
    • (2002) Dig. Dis. , vol.20 , pp. 81-90
    • Blum, H.E.1
  • 40
    • 0034903090 scopus 로고    scopus 로고
    • Inhibition of growth of human breast carcinoma cells by an antisense oligonucleotide targeted to the transferrin receptor gene
    • Yang, D. C.; Jiang, X. P.; Elliott, R. L.; and Head, J. F. Inhibition of growth of human breast carcinoma cells by an antisense oligonucleotide targeted to the transferrin receptor gene. Anticancer Res. 2001, 21, 1777-1787.
    • (2001) Anticancer Res. , vol.21 , pp. 1777-1787
    • Yang, D.C.1    Jiang, X.P.2    Elliott, R.L.3    Head, J.F.4
  • 41
    • 0027529956 scopus 로고
    • Antisense suppression of transferrin receptor gene expression in a human hepatoma cell (HuH-7) line
    • Sasaki, K.; Zak, O.; and Aisen, P. Antisense suppression of transferrin receptor gene expression in a human hepatoma cell (HuH-7) line. Am. J. Hematol. 1993, 42, 74-80.
    • (1993) Am. J. Hematol. , vol.42 , pp. 74-80
    • Sasaki, K.1    Zak, O.2    Aisen, P.3
  • 42
    • 0022616986 scopus 로고
    • Mechanisms of growth inhibition by anti-transferrin receptor monoclonal antibodies
    • Taetle, R.; Castagnola, J.; and Mendelsohn, J. Mechanisms of growth inhibition by anti-transferrin receptor monoclonal antibodies. Cancer Res. 1986, 46, 1759-1763.
    • (1986) Cancer Res. , vol.46 , pp. 1759-1763
    • Taetle, R.1    Castagnola, J.2    Mendelsohn, J.3
  • 43
    • 0000302649 scopus 로고
    • Monoclonal antibody to transferrin receptor blocks transferrin binding and inhibits human tumor cell growth in vitro
    • Trowbridge, I. S. and Lopez, F. Monoclonal antibody to transferrin receptor blocks transferrin binding and inhibits human tumor cell growth in vitro. Proc. Natl. Acad. Sci. USA 1982, 79 1175-1179.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1175-1179
    • Trowbridge, I.S.1    Lopez, F.2
  • 44
    • 0029132960 scopus 로고
    • Inhibition of lymphoma growth in vivo by combined treatment with hydroxyethyl starch deferoxamine conjugate and IgG monoclonal antibodies against the transferrin receptor
    • Kemp, J. D.; Cardillo, T.; Stewart, B. C.; Kehrberg, E.; Weiner, G.; Hedlund, B.; and Naumann, P. W. Inhibition of lymphoma growth in vivo by combined treatment with hydroxyethyl starch deferoxamine conjugate and IgG monoclonal antibodies against the transferrin receptor. Cancer Res. 1995, 55, 3817-3824.
    • (1995) Cancer Res. , vol.55 , pp. 3817-3824
    • Kemp, J.D.1    Cardillo, T.2    Stewart, B.C.3    Kehrberg, E.4    Weiner, G.5    Hedlund, B.6    Naumann, P.W.7
  • 45
    • 0019802750 scopus 로고
    • Effect of iron deficiency on transplantable murine plasmacytoma
    • Benbassat, J.; Hershko, C.; Laskov, R.; and Eliakim, M. Effect of iron deficiency on transplantable murine plasmacytoma. Nutr. Cancer 1981, 3, 20-26.
    • (1981) Nutr. Cancer , vol.3 , pp. 20-26
    • Benbassat, J.1    Hershko, C.2    Laskov, R.3    Eliakim, M.4
  • 46
    • 0023681960 scopus 로고
    • Iron nutrition and tumor growth: Decreased tumor growth in iron-deficient mice
    • Hann, H. W., Stahlhut, M. W.; and Blumberg, B. S. Iron nutrition and tumor growth: decreased tumor growth in iron-deficient mice. Cancer Res. 1988, 48, 4168-4170.
    • (1988) Cancer Res. , vol.48 , pp. 4168-4170
    • Hann, H.W.1    Stahlhut, M.W.2    Blumberg, B.S.3
  • 48
    • 7444249085 scopus 로고
    • The biochemistry of desferrioxamine and its relation to iron metabolism
    • Keberle, H. The biochemistry of desferrioxamine and its relation to iron metabolism. Ann. N. Y. Acad. Sci. 1964, 119, 758-768.
    • (1964) Ann. N. Y. Acad. Sci. , vol.119 , pp. 758-768
    • Keberle, H.1
  • 49
    • 0018777993 scopus 로고
    • Studies in desferrioxamine and ferrioxamine metabolism in normal and iron-loaded subjects
    • Summers, M. R.; Jacobs, A.; Tudway, D.; Perera, P.; and Ricketts, C. Studies in desferrioxamine and ferrioxamine metabolism in normal and iron-loaded subjects. Br. J. Haematol. 1979, 42 547-555.
    • (1979) Br. J. Haematol. , vol.42 , pp. 547-555
    • Summers, M.R.1    Jacobs, A.2    Tudway, D.3    Perera, P.4    Ricketts, C.5
  • 50
    • 0009498234 scopus 로고
    • Piperazine derivatives
    • [1,234,935]. U. K
    • Creighton, A. M. Piperazine derivatives. [1,234,935]. 1971. U. K.
    • (1971)
    • Creighton, A.M.1
  • 51
    • 0025324554 scopus 로고
    • The hydrolysis activation of the doxorubicin cardioprotective agent ICRF-187 [(+)-1,2-bis(3,5-dioxopiperazinyl-1-yl)propane)]
    • Hasinoff, B. B. The hydrolysis activation of the doxorubicin cardioprotective agent ICRF-187 [(+)-1,2-bis(3,5-dioxopiperazinyl-1-yl)propane)]. Drug Metab. Dispos. 1990, 18, 344-349.
    • (1990) Drug Metab. Dispos. , vol.18 , pp. 344-349
    • Hasinoff, B.B.1
  • 52
    • 0027486375 scopus 로고
    • Enzymatic ring-opening reactions of the chiral cardioprotective agent (+) (S)-ICRF-187 and its (-) (R)-enantiomer ICRF-186 by dihydropyrimidine amidohydrolase
    • Hasinoff, B. B. Enzymatic ring-opening reactions of the chiral cardioprotective agent (+) (S)-ICRF-187 and its (-) (R -enantiomer ICRF-186 by dihydropyrimidine amidohydrolase. Drug Metab. Dispos. 1993, 21, 883-888.
    • (1993) Drug Metab. Dispos. , vol.21 , pp. 883-888
    • Hasinoff, B.B.1
  • 53
    • 1842866539 scopus 로고    scopus 로고
    • Dihydroorotase Catalyzes the Ring Opening of the Hydrolysis Intermediates of the Cardioprotective Drug Dexrazoxane (ICRF-187)
    • Schroeder, P. E.; Davidson, J. N.; and Hasinoff, B. B. Dihydroorotase Catalyzes the Ring Opening of the Hydrolysis Intermediates of the Cardioprotective Drug Dexrazoxane (ICRF-187). Drug Metab. Dispos. 2002, 30, 1431-1435.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 1431-1435
    • Schroeder, P.E.1    Davidson, J.N.2    Hasinoff, B.B.3
  • 54
    • 0020398870 scopus 로고
    • Metal binding by pharmaceuticals. Part 2. Interactions of Ca(II), Cu(II), Fe(II), Mg(II), Mn(II) and Zn(II) with the intracellular hydrolysis products of the antitumour agent ICRF 159 and its inactive homologue ICRF 192
    • Huang, Z. X.; May, P. M.; Quinlan, K. M.; Williams, D. R.; and Creighton, A. M. Metal binding by pharmaceuticals. Part 2. Interactions of Ca(II), Cu(II), Fe(II), Mg(II), Mn(II) and Zn(II) with the intracellular hydrolysis products of the antitumour agent ICRF 159 and its inactive homologue ICRF 192. Agents Actions 1982, 12, 536-542.
    • (1982) Agents Actions , vol.12 , pp. 536-542
    • Huang, Z.X.1    May, P.M.2    Quinlan, K.M.3    Williams, D.R.4    Creighton, A.M.5
  • 55
    • 0013941506 scopus 로고
    • The carcinostatic activity of α-(N)-heterocyclic carboxaldehyde thiosemicarbazones. II. 3-Hydroxypyridine-2-carboxaldehyde thiosemicarbazone
    • French, F. A. and Blanz, E. J., Jr. The carcinostatic activity of α-(N)-heterocyclic carboxaldehyde thiosemicarbazones. II. 3-Hydroxypyridine-2-carboxaldehyde thiosemicarbazone. Cancer Res. 1966, 26, 1638-1640.
    • (1966) Cancer Res. , vol.26 , pp. 1638-1640
    • French, F.A.1    Blanz Jr., E.J.2
  • 56
    • 0032055861 scopus 로고    scopus 로고
    • Pyridoxal isonicotinoyl hydrazone and its analogs: Potential orally effective iron-chelating agents for the treatment of iron overload disease
    • Richardson, D. R. and Ponka, P. Pyridoxal isonicotinoyl hydrazone and its analogs: potential orally effective iron-chelating agents for the treatment of iron overload disease. J. Lab. Clin. Med. 1998, 131, 306-315.
    • (1998) J. Lab. Clin. Med. , vol.131 , pp. 306-315
    • Richardson, D.R.1    Ponka, P.2
  • 57
    • 0023673152 scopus 로고
    • Pyridoxal isonicotinoyl hydrazone (PIH): A promising new iron chelator
    • Webb, J. and Vitolo, M. L. Pyridoxal isonicotinoyl hydrazone (PIH): a promising new iron chelator. Birth Defects: Orig. Art. Ser. 1988, 23, 63-70.
    • (1988) Birth Defects: Orig. Art Ser. , vol.23 , pp. 63-70
    • Webb, J.1    Vitolo, M.L.2
  • 58
    • 0030174279 scopus 로고    scopus 로고
    • Mode of action of iron (III) chelators as antimalarials. IV. Potentiation of desferal action by benzoyl and isonicotinoyl hydrazone derivatives
    • Tsafack, A.; Loyevsky, M.; Ponka, P.; and Cabantchik, Z. I. Mode of action of iron (III) chelators as antimalarials. IV. Potentiation of desferal action by benzoyl and isonicotinoyl hydrazone derivatives. J. Lab. Clin. Med. 1996, 127, 574-582.
    • (1996) J. Lab. Clin. Med. , vol.127 , pp. 574-582
    • Tsafack, A.1    Loyevsky, M.2    Ponka, P.3    Cabantchik, Z.I.4
  • 59
    • 0030946105 scopus 로고    scopus 로고
    • The treatment of animal models of malaria with iron chelators by use of a novel polymeric device for slow drug release
    • Golenser, J.; Dumb, A.; Teomim, D.; Tsafack, A.; Nisim, O.; Eling, W.; and Cabantchik, Z. I. The treatment of animal models of malaria with iron chelators by use of a novel polymeric device for slow drug release. J. Pharm. Exp. Ther. 1997, 281, 1127-1135.
    • (1997) J. Pharm. Exp. Ther. , vol.281 , pp. 1127-1135
    • Golenser, J.1    Dumb, A.2    Teomim, D.3    Tsafack, A.4    Nisim, O.5    Eling, W.6    Cabantchik, Z.I.7
  • 60
    • 0031674853 scopus 로고    scopus 로고
    • Analogues of pyridoxal isonicotinoyl hydrazone (PIH) as potential iron chelators for the treatment of neoplasia
    • Richardson, D. R. Analogues of pyridoxal isonicotinoyl hydrazone (PIH) as potential iron chelators for the treatment of neoplasia. Leuk. Lymph. 1998, 31, 47-60.
    • (1998) Leuk. Lymph. , vol.31 , pp. 47-60
    • Richardson, D.R.1
  • 61
    • 0002653698 scopus 로고
    • Structural studies of iron(III) complexes of the new iron-binding drug, pyridoxal isonicotinoyl hydrazone
    • Murphy, T. B.; Johnson, D. K.; Rose, N. J.; Aruffo, A.; and Schomaker, V. Structural studies of iron(III) complexes of the new iron-binding drug, pyridoxal isonicotinoyl hydrazone. Inorg. Chim. Acta 1982, 66, L67-L68.
    • (1982) Inorg. Chim. Acta , vol.66
    • Murphy, T.B.1    Johnson, D.K.2    Rose, N.J.3    Aruffo, A.4    Schomaker, V.5
  • 63
    • 0032771646 scopus 로고    scopus 로고
    • Crystal and molecular structure of 2-hydroxy-l-naphthaldehyde isonicotinoyl hydrazone (NIH) and its iron(III) complex: An iron chelator with anti-tumour activity
    • Richardson, D. R. and Bernhardt, P. V. Crystal and molecular structure of 2-hydroxy-l-naphthaldehyde isonicotinoyl hydrazone (NIH) and its iron(III) complex: an iron chelator with anti-tumour activity. J. Biol. Inorg. Chem. 1999, 4, 266-273.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 266-273
    • Richardson, D.R.1    Bernhardt, P.V.2
  • 64
    • 0018394556 scopus 로고
    • Mobilization of iron from reticulocytes. Identification of pyridoxal isonicotinoyl hydrazone as a new iron chelating agent
    • Ponka, P.; Borova, J.; Neuwirt, J.; and Fuchs, O. Mobilization of iron from reticulocytes. Identification of pyridoxal isonicotinoyl hydrazone as a new iron chelating agent. FEBS Lett. 1979, 97, 317-321.
    • (1979) FEBS Lett. , vol.97 , pp. 317-321
    • Ponka, P.1    Borova, J.2    Neuwirt, J.3    Fuchs, O.4
  • 65
    • 0033230124 scopus 로고    scopus 로고
    • Development of novel aroylhydrazone ligands for iron chelation therapy: 2-pyridylcarboxaldehyde isonicotinoyl hydrazone analogs
    • Becker, E. and Richardson, D. R. Development of novel aroylhydrazone ligands for iron chelation therapy: 2-pyridylcarboxaldehyde isonicotinoyl hydrazone analogs. J. Lab. Clin. Med. 1999, 134, 510-521.
    • (1999) J. Lab. Clin. Med. , vol.134 , pp. 510-521
    • Becker, E.1    Richardson, D.R.2
  • 66
    • 0037100453 scopus 로고    scopus 로고
    • Novel "hybrid" iron chelators derived from aroylhydrazones and thiosemicarbazones demonstrate selective antiproliferative activity against tumor cells
    • Lovejoy, D. B. and Richardson, D. R. Novel "hybrid" iron chelators derived from aroylhydrazones and thiosemicarbazones demonstrate selective antiproliferative activity against tumor cells. Blood 2002, 100, 666-676.
    • (2002) Blood , vol.100 , pp. 666-676
    • Lovejoy, D.B.1    Richardson, D.R.2
  • 68
    • 0031755277 scopus 로고    scopus 로고
    • Novel iron complexes and chelators based on c i s,cis-1,3,5-triaminocyclohexane: Iron-mediated ligand oxidation and biochemical properties
    • Park, G.; Lu, F. H.; Ye, N.; Brechbiel, M. W.; Torti, S. V.; Torti, F. M.; and Planalp, R. P. Novel iron complexes and chelators based on c i s,cis-1,3,5-triaminocyclohexane: iron-mediated ligand oxidation and biochemical properties. J. Biol. Inorg. Chem. 1998 3, 449-457.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 449-457
    • Park, G.1    Lu, F.H.2    Ye, N.3    Brechbiel, M.W.4    Torti, S.V.5    Torti, F.M.6    Planalp, R.P.7
  • 71
    • 0029562526 scopus 로고
    • Metabolization of iron by plant cells using O-Trensox, a high-affinity abiotic iron-chelating agent
    • Caris, C.; Baret, P.; Beguin, C.; Serratrice, G.; Pierre, J. L.; and Laulhere, J. P. Metabolization of iron by plant cells using O-Trensox, a high-affinity abiotic iron-chelating agent. Biochem. J. 1995, 312 (Pt 3), 879-885.
    • (1995) Biochem. J. , vol.312 , Issue.PART 3 , pp. 879-885
    • Caris, C.1    Baret, P.2    Beguin, C.3    Serratrice, G.4    Pierre, J.L.5    Laulhere, J.P.6
  • 72
    • 0025088608 scopus 로고
    • Metal complex formation of a new siderophore desferrithiocin and of three related ligands
    • Anderegg, G. and Raber, M. Metal complex formation of a new siderophore desferrithiocin and of three related ligands. J. Chem. Soc. Chem. Commun. 1990, 1194-1196.
    • (1990) J. Chem. Soc. Chem. Commun. , pp. 1194-1196
    • Anderegg, G.1    Raber, M.2
  • 73
    • 0033066791 scopus 로고    scopus 로고
    • Cellular uptake and release of two contrasting iron chelators
    • Cable, H. and Lloyd, J. B. Cellular uptake and release of two contrasting iron chelators. Journal of Pharmacy and Pharmacology 1999, 51, 131-134.
    • (1999) Journal of Pharmacy and Pharmacology , vol.51 , pp. 131-134
    • Cable, H.1    Lloyd, J.B.2
  • 74
    • 0028891974 scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents
    • Richardson, D. R.; Tran, E. H.; and Ponka, P. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents. Blood 1995, 86, 4295-4306.
    • (1995) Blood , vol.86 , pp. 4295-4306
    • Richardson, D.R.1    Tran, E.H.2    Ponka, P.3
  • 75
    • 0037237032 scopus 로고    scopus 로고
    • Examination of the antiproliferative activity of iron chelators: Multiple cellular targets and the different mechanism of action of triapine compared with desferrioxamine and the potent pyridoxal isonicotinoyl hydrazone analogue 311
    • Chaston, T. B.; Lovejoy, D. B.; Watts, R. N.; and Richardson, D. R. Examination of the antiproliferative activity of iron chelators: multiple cellular targets and the different mechanism of action of triapine compared with desferrioxamine and the potent pyridoxal isonicotinoyl hydrazone analogue 311. Clin. Cancer Res. 2003, 9, 402-414.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 402-414
    • Chaston, T.B.1    Lovejoy, D.B.2    Watts, R.N.3    Richardson, D.R.4
  • 76
    • 0030790471 scopus 로고    scopus 로고
    • Modulation of transferrin receptor expression by dexrazoxane (ICRF-187) via activation of iron regulatory protein
    • Weiss, G.; Kastner, S.; Brock, J.; Thaler, J.; and Grunewald, K. Modulation of transferrin receptor expression by dexrazoxane (ICRF-187) via activation of iron regulatory protein. Biochem. Pharmacol. 1997, 53, 1419-1424.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 1419-1424
    • Weiss, G.1    Kastner, S.2    Brock, J.3    Thaler, J.4    Grunewald, K.5
  • 77
    • 0034089867 scopus 로고    scopus 로고
    • Effects of interferon-gamma and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2
    • Kim, S. and Ponka, P. Effects of interferon-gamma and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2. J. Biol. Chem. 2000, 275, 6220-6226.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6220-6226
    • Kim, S.1    Ponka, P.2
  • 79
    • 0026725057 scopus 로고
    • Desferrithiocin is an effective iron chelator in vivo and in vitro but ferrithiocin is toxic
    • Baker, E.; Wong, A.; Peter, H.; and Jacobs, A. Desferrithiocin is an effective iron chelator in vivo and in vitro but ferrithiocin is toxic. Br. J. Haematol. 1992, 81, 424-431.
    • (1992) Br. J. Haematol. , vol.81 , pp. 424-431
    • Baker, E.1    Wong, A.2    Peter, H.3    Jacobs, A.4
  • 80
    • 0037114461 scopus 로고    scopus 로고
    • Mobilization of intracellular iron by analogs of pyridoxal isonicotinoyl hydrazone (PIH) is determined by the membrane permeability of the iron-chelator complexes
    • Buss, J. L.; Arduini, E.; and Ponka, P. Mobilization of intracellular iron by analogs of pyridoxal isonicotinoyl hydrazone (PIH) is determined by the membrane permeability of the iron-chelator complexes. Biochem. Pharmacol. 2002, 64, 1689-1701.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1689-1701
    • Buss, J.L.1    Arduini, E.2    Ponka, P.3
  • 81
    • 0035812772 scopus 로고    scopus 로고
    • HIF-1, O(2), and the 3 PHDs: How animal cells signal hypoxia to the nucleus
    • Semenza, G. L. HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell 2001, 107, 1-3.
    • (2001) Cell , vol.107 , pp. 1-3
    • Semenza, G.L.1
  • 83
    • 0029858079 scopus 로고    scopus 로고
    • Identification of hypoxically inducible mRNAs in HeLa cells using differential-display PCR. Role of hypoxia-inducible factor-1
    • O'Rourke, J. F.; Pugh, C. W.; Bartlett, S. M.; and Ratcliffe, P. J. Identification of hypoxically inducible mRNAs in HeLa cells using differential-display PCR. Role of hypoxia-inducible factor-1. Eur. J. Biochem. 1996, 241, 403-410.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 403-410
    • O'Rourke, J.F.1    Pugh, C.W.2    Bartlett, S.M.3    Ratcliffe, P.J.4
  • 85
    • 0037390915 scopus 로고    scopus 로고
    • The antimycotic ciclopirox olamine induces HIF-1α stability, VEGF expression, and angiogenesis
    • Linden, T.; Katschinski, D. M.; Eckhardt, K.; Scheid, A.; Pagel, H.; and Wenger, R. H. The antimycotic ciclopirox olamine induces HIF-1α stability, VEGF expression, and angiogenesis. FASEB J. 2003, 17, 761-763.
    • (2003) FASEB J. , vol.17 , pp. 761-763
    • Linden, T.1    Katschinski, D.M.2    Eckhardt, K.3    Scheid, A.4    Pagel, H.5    Wenger, R.H.6
  • 86
    • 0037454654 scopus 로고    scopus 로고
    • Genetic regulation of cell function in response to iron overload or chelation
    • Templeton, D. M. and Liu, Y. Genetic regulation of cell function in response to iron overload or chelation. Biochim. Biophys. Acta 2003, 1619, 113-124.
    • (2003) Biochim. Biophys. Acta , vol.1619 , pp. 113-124
    • Templeton, D.M.1    Liu, Y.2
  • 87
    • 0034255036 scopus 로고    scopus 로고
    • Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia
    • Bruick, R. K. Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia. Proc. Natl. Acad. Sci. U. S. A 2000, 97, 9082-9087.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9082-9087
    • Bruick, R.K.1
  • 88
    • 0027521831 scopus 로고
    • Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators
    • Nyholm, S.; Mann, G. J.; Johansson, A. G.; Bergeron, R. J., Graslund, A.; and Thelander, L. Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators. J. Biol. Chem. 1993, 268, 26200-26205.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26200-26205
    • Nyholm, S.1    Mann, G.J.2    Johansson, A.G.3    Bergeron, R.J.4    Graslund, A.5    Thelander, L.6
  • 89
    • 0015153126 scopus 로고
    • Mechanism of inhibition of ribonucleoside diphosphate reductase by α-(N)-heterocyclic aldehyde thiosemicarbazones
    • Sartorelli, A. C.; Agrawal, K. C.; and Moore, E. C. Mechanism of inhibition of ribonucleoside diphosphate reductase by α -(N -heterocyclic aldehyde thiosemicarbazones. Biochem. Pharmacol. 1971, 20, 3119-3123.
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 3119-3123
    • Sartorelli, A.C.1    Agrawal, K.C.2    Moore, E.C.3
  • 90
    • 0014940591 scopus 로고
    • Inhibition of ribonucleoside diphosphate reductase by 1-formylisoquinoline thiosemicarbazone and related compounds
    • Moore, E. C.; Zedeck, M. S.; Agrawal, K. C.; and Sartorelli, A. C. Inhibition of ribonucleoside diphosphate reductase by 1-formylisoquinoline thiosemicarbazone and related compounds. Biochemistry 1970, 9, 4492-4498.
    • (1970) Biochemistry , vol.9 , pp. 4492-4498
    • Moore, E.C.1    Zedeck, M.S.2    Agrawal, K.C.3    Sartorelli, A.C.4
  • 91
    • 0030426531 scopus 로고    scopus 로고
    • Characterization of mouse leukemia L1210 cells resistant to the ribonucleotide reductase inhibitor 4-methyl-5-amino-1-formyl-isoquinoline thiosemicarbazone
    • Cory, A. H.; Sato, A.; Thompson, D. P.; and Cory, J. G. Characterization of mouse leukemia L1210 cells resistant to the ribonucleotide reductase inhibitor 4-methyl-5-amino-1-formyl-isoquinoline thiosemicarbazone. Oncol. Res. 1996, 8, 449-456.
    • (1996) Oncol. Res. , vol.8 , pp. 449-456
    • Cory, A.H.1    Sato, A.2    Thompson, D.P.3    Cory, J.G.4
  • 92
    • 0035181433 scopus 로고    scopus 로고
    • Inhibition of malignant cell growth by 311, a novel iron chelator of the pyridoxal isonicotinoyl hydrazone class: Effect on the R2 subunit of ribonucleotide reductase
    • Green, D. A.; Antholine, W. E., Wong, S. J.; Richardson, D. R.; and Chitambar, C. R. Inhibition of malignant cell growth by 311, a novel iron chelator of the pyridoxal isonicotinoyl hydrazone class: effect on the R2 subunit of ribonucleotide reductase. Clin. Cancer Res. 2001, 7, 3574-3579.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 3574-3579
    • Green, D.A.1    Antholine, W.E.2    Wong, S.J.3    Richardson, D.R.4    Chitambar, C.R.5
  • 93
    • 0021259518 scopus 로고
    • Deferoxamine: A reversible S-phase inhibitor of human lymphocyte proliferation
    • Lederman, H. M.; Cohen, A.; Lee, J. W.; Freedman, M. H.; and Gelfand, E. W. Deferoxamine: a reversible S-phase inhibitor of human lymphocyte proliferation. Blood 1984, 64, 748-753.
    • (1984) Blood , vol.64 , pp. 748-753
    • Lederman, H.M.1    Cohen, A.2    Lee, J.W.3    Freedman, M.H.4    Gelfand, E.W.5
  • 94
    • 0017045298 scopus 로고
    • Characterization of the biochemical mechanism of action of α-(N)-heterocyclic carboxaldehyde thiosemicarbazones
    • Sartorelli, A. C.; Agrawal, K. C.; Tsiftsoglou, A. S.; and Moore, E. C. Characterization of the biochemical mechanism of action of α-(N)-heterocyclic carboxaldehyde thiosemicarbazones. Adv. Enzyme Regul. 1976, 15, 117-139.
    • (1976) Adv. Enzyme Regul. , vol.15 , pp. 117-139
    • Sartorelli, A.C.1    Agrawal, K.C.2    Tsiftsoglou, A.S.3    Moore, E.C.4
  • 95
    • 0020567471 scopus 로고
    • Mechanism of inhibition of mammalian ribonucleotide reductase by the iron chelate of 1-formylisoquinoline thiosemicarbazone. Destruction of the tyrosine free radical of the enzyme in an oxygen-requiring reaction
    • Thelander, L. and Graslund, A. Mechanism of inhibition of mammalian ribonucleotide reductase by the iron chelate of 1-formylisoquinoline thiosemicarbazone. Destruction of the tyrosine free radical of the enzyme in an oxygen-requiring reaction. J. Biol. Chem. 1983, 258, 4063-4066.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4063-4066
    • Thelander, L.1    Graslund, A.2
  • 96
    • 0019182280 scopus 로고
    • Effects of the ferrous chelate of 4-methyl-5-amino-1-formylisoquinoline thiosemicarbazone (MAIQ-1) on the kinetics of reduction of CDP by ribonucleotide reductase of the Novikoff tumor
    • Preidecker, P. J.; Agrawal, K. C.; Sartorelli, A. C.; and Moore, E. C. Effects of the ferrous chelate of 4-methyl-5-amino-1-formylisoquinoline thiosemicarbazone (MAIQ-1) on the kinetics of reduction of CDP by ribonucleotide reductase of the Novikoff tumor. Mol. Pharmacol. 1980, 18, 507-512.
    • (1980) Mol. Pharmacol. , vol.18 , pp. 507-512
    • Preidecker, P.J.1    Agrawal, K.C.2    Sartorelli, A.C.3    Moore, E.C.4
  • 97
    • 0018686777 scopus 로고
    • Comparative cytotoxic and biochemical effects of ligands and metal complexes of α-N-heterocyclic carboxaldehyde thiosemicarbazones
    • Saryan, L. A.; Ankel, E.; Krishnamurti, C.; Petering, D. H.; and Elford, H. Comparative cytotoxic and biochemical effects of ligands and metal complexes of α-N-heterocyclic carboxaldehyde thiosemicarbazones. J. Med. Chem. 1979, 22, 1218-1221.
    • (1979) J. Med. Chem. , vol.22 , pp. 1218-1221
    • Saryan, L.A.1    Ankel, E.2    Krishnamurti, C.3    Petering, D.H.4    Elford, H.5
  • 98
    • 0027934897 scopus 로고
    • Inhibitors of ribonucleotide reductase. Comparative effects of amino- and hydroxy-substituted pyridine-2-carboxaldehyde thiosemicarbazones
    • Cory, J. G.; Cory, A. H.; Rappa, G.; Lorico, A.; Liu, M. C.; Lin, T. S.; and Sartorelli, A. C. Inhibitors of ribonucleotide reductase. Comparative effects of amino- and hydroxy-substituted pyridine-2-carboxaldehyde thiosemicarbazones. Biochem. Pharmacol. 1994, 48, 335-344.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 335-344
    • Cory, J.G.1    Cory, A.H.2    Rappa, G.3    Lorico, A.4    Liu, M.C.5    Lin, T.S.6    Sartorelli, A.C.7
  • 99
    • 0030894798 scopus 로고    scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents II: The mechanism of action of ligands derived from salicylaidehyde benzoyl hydrazone and 2-hydroxy-1-naphthylaldehyde benzoyl hydrazone
    • Richardson, D. R. and Milnes, K. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents II: the mechanism of action of ligands derived from salicylaidehyde benzoyl hydrazone and 2-hydroxy-1-naphthylaldehyde benzoyl hydrazone. Blood 1997, 89, 3025-3038.
    • (1997) Blood , vol.89 , pp. 3025-3038
    • Richardson, D.R.1    Milnes, K.2
  • 101
    • 0028292020 scopus 로고
    • Antisense oligodeoxynucleotides for IL-2, c-myc and transferrin receptor synchronize mitogen-activated lymphocytes in the G1 phase
    • Kato, J.; Kohgo, Y.; Kondo, H.; Sasaki, K.; and Niitsu, Y. Antisense oligodeoxynucleotides for IL-2, c-myc and transferrin receptor synchronize mitogen-activated lymphocytes in the G1 phase. Scand. J. Immunol. 1994, 39, 499-504.
    • (1994) Scand. J. Immunol. , vol.39 , pp. 499-504
    • Kato, J.1    Kohgo, Y.2    Kondo, H.3    Sasaki, K.4    Niitsu, Y.5
  • 102
    • 0036565766 scopus 로고    scopus 로고
    • Ferritin expression modulates cell cycle dynamics and cell responsiveness to H-ras-induced growth via expansion of the labile iron pool
    • Kakhlon, O.; Gruenbaum, Y.; and Cabantchik, Z. I. Ferritin expression modulates cell cycle dynamics and cell responsiveness to H-ras-induced growth via expansion of the labile iron pool. Biochem. J. 2002, 363, 431-436.
    • (2002) Biochem. J. , vol.363 , pp. 431-436
    • Kakhlon, O.1    Gruenbaum, Y.2    Cabantchik, Z.I.3
  • 103
    • 0030063939 scopus 로고    scopus 로고
    • Cell cycle-dependent inhibition of the proliferation of human neural tumor cell lines by iron chelators
    • Renton, F. J. and Jeitner, T. M. Cell cycle-dependent inhibition of the proliferation of human neural tumor cell lines by iron chelators. Biochem. Pharmacol. 1996, 51, 1553-1561.
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 1553-1561
    • Renton, F.J.1    Jeitner, T.M.2
  • 104
    • 0035437183 scopus 로고    scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents, IV: The mechanisms involved in inhibiting cell-cycle progression
    • Gao, J. and Richardson, D. R. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents, IV: The mechanisms involved in inhibiting cell-cycle progression. Blood 2001, 98, 842-850.
    • (2001) Blood , vol.98 , pp. 842-850
    • Gao, J.1    Richardson, D.R.2
  • 105
    • 0029087637 scopus 로고
    • Effects of iron-depletion on cell cycle progression in normal human T lymphocytes: Selective inhibition of the appearance of the cyclin A-associated component of the p33cdk2 kinase
    • Lucas, J. J.; Szepesi, A.; Domenico, J.; Takase, K.; Tordai, A.; Terada, N.; and Gelfand, E. W. Effects of iron-depletion on cell cycle progression in normal human T lymphocytes: selective inhibition of the appearance of the cyclin A-associated component of the p33cdk2 kinase. Blood 1995, 86, 2268-2280.
    • (1995) Blood , vol.86 , pp. 2268-2280
    • Lucas, J.J.1    Szepesi, A.2    Domenico, J.3    Takase, K.4    Tordai, A.5    Terada, N.6    Gelfand, E.W.7
  • 106
    • 0030601987 scopus 로고    scopus 로고
    • Iron deprivation inhibits cyclin-dependent kinase activity and decreases cyclin D/CDK4 protein levels in asynchronous MDA-MB-453 human breast cancer cells
    • Kulp, K. S.; Green, S. L.; and Vulliet, P. R. Iron deprivation inhibits cyclin-dependent kinase activity and decreases cyclin D/CDK4 protein levels in asynchronous MDA-MB-453 human breast cancer cells. Exp. Cell Res. 1996, 229, 60-68.
    • (1996) Exp. Cell Res. , vol.229 , pp. 60-68
    • Kulp, K.S.1    Green, S.L.2    Vulliet, P.R.3
  • 107
    • 0038687772 scopus 로고    scopus 로고
    • Potent iron chelators increase the mRNA levels of the universal cyclin-dependent kinase inhibitor p21(CIP1/WAF1), but paradoxically inhibit its translation: A potential mechanism of cell cycle dysregulation
    • Le, N. T. and Richardson, D. R. Potent iron chelators increase the mRNA levels of the universal cyclin-dependent kinase inhibitor p21(CIP1/WAF1), but paradoxically inhibit its translation: a potential mechanism of cell cycle dysregulation. Carcinogenesis 2003, 24, 1045-1058.
    • (2003) Carcinogenesis , vol.24 , pp. 1045-1058
    • Le, N.T.1    Richardson, D.R.2
  • 109
    • 0034855827 scopus 로고    scopus 로고
    • Expression of multiple genes regulating cell cycle and apoptosis in differentiating hematopoietic cells is dependent on iron
    • Alcantara, O.; Kalidas, M.; Baltathakis, I.; and Boldt, D. H. Expression of multiple genes regulating cell cycle and apoptosis in differentiating hematopoietic cells is dependent on iron. Exp. Hematol. 2001, 29, 1060-1069.
    • (2001) Exp. Hematol. , vol.29 , pp. 1060-1069
    • Alcantara, O.1    Kalidas, M.2    Baltathakis, I.3    Boldt, D.H.4
  • 110
    • 0030873298 scopus 로고    scopus 로고
    • G1 accumulation caused by iron deprivation with deferoxamine does not accompany change of pRB status in ML-1 cells
    • Fukuchi, K.; Tomoyasu, S.; Watanabe, H.; Tsuruoka, N.; and Gomi, K. G1 accumulation caused by iron deprivation with deferoxamine does not accompany change of pRB status in ML-1 cells. Biochim. Biophys. Acta 1997, 1357, 297-305.
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 297-305
    • Fukuchi, K.1    Tomoyasu, S.2    Watanabe, H.3    Tsuruoka, N.4    Gomi, K.5
  • 111
    • 0001101307 scopus 로고    scopus 로고
    • Electrochemical Behavior of the Fe(III) Complexes of the Cyclic Hydroxamate Siderophores Alcaligin and Desferrioxamine E
    • Spasojevic, I.; Armstrong, S. K.; Brickman, T. J.; and Crumbliss, A. L. Electrochemical Behavior of the Fe(III) Complexes of the Cyclic Hydroxamate Siderophores Alcaligin and Desferrioxamine E. Inorg. Chem 1999, 38, 449-454.
    • (1999) Inorg. Chem. , vol.38 , pp. 449-454
    • Spasojevic, I.1    Armstrong, S.K.2    Brickman, T.J.3    Crumbliss, A.L.4
  • 112
    • 0034949363 scopus 로고    scopus 로고
    • Iron metabolism, free radicals, and oxidative injury
    • Emerit, J.; Beaumont, C.; and Trivin, F. Iron metabolism, free radicals, and oxidative injury. Biomed. Pharmacother. 2001 55, 333-339.
    • (2001) Biomed. Pharmacother. , vol.55 , pp. 333-339
    • Emerit, J.1    Beaumont, C.2    Trivin, F.3
  • 113
    • 0000622485 scopus 로고
    • In vitro antioxidant properties of the iron chelator pyridoxal isonicotinoyl hydrazone and some of its analogs
    • Schulman, H. M.; Hermes-Lima, M.; Wang, E. M.; and Ponka, P. In vitro antioxidant properties of the iron chelator pyridoxal isonicotinoyl hydrazone and some of its analogs. Redox Rep. 1995 1, 373-378.
    • (1995) Redox Rep. , vol.1 , pp. 373-378
    • Schulman, H.M.1    Hermes-Lima, M.2    Wang, E.M.3    Ponka, P.4
  • 115
    • 0037300716 scopus 로고    scopus 로고
    • Lipophilicity of analogs of pyridoxal isonicotinoyl hydrazone (PIH) determines the efflux of iron complexes and toxicity in K562 cells
    • Buss, J. L.; Arduini, E.; Shephard, K. C.; and Ponka, P. Lipophilicity of analogs of pyridoxal isonicotinoyl hydrazone (PIH) determines the efflux of iron complexes and toxicity in K562 cells. Biochem. Pharmacol. 2003, 65, 349-360.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 349-360
    • Buss, J.L.1    Arduini, E.2    Shephard, K.C.3    Ponka, P.4
  • 116
    • 0034213869 scopus 로고    scopus 로고
    • Protection of erythrocytes against oxidative damage and autologous immunoglobulin G (IgG) binding by iron chelator fluor-benzoil-pyridoxal hydrazone
    • Ferrali, M.; Signorini, C.; Ciccoli, L.; Bambagioni, S.; Rossi, V.; Pompella, A.; and Comporti, M. Protection of erythrocytes against oxidative damage and autologous immunoglobulin G (IgG) binding by iron chelator fluor-benzoil-pyridoxal hydrazone. Biochem. Pharmacol. 2000, 59, 1365-1373.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 1365-1373
    • Ferrali, M.1    Signorini, C.2    Ciccoli, L.3    Bambagioni, S.4    Rossi, V.5    Pompella, A.6    Comporti, M.7
  • 117
    • 0028959660 scopus 로고
    • Ferrous ion strongly promotes the ring opening of the hydrolysis intermediates of the antioxidant cardioprotective agent dexrazoxane (ICRF-187)
    • Buss, J. L. and Hasinoff, B. B. Ferrous ion strongly promotes the ring opening of the hydrolysis intermediates of the antioxidant cardioprotective agent dexrazoxane (ICRF-187). Arch. Biochem. Biophys. 1995, 317, 121-127.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 121-127
    • Buss, J.L.1    Hasinoff, B.B.2
  • 118
    • 0038814301 scopus 로고    scopus 로고
    • Interactions of the pyridine-2-carboxaldehyde isonicotinoyl hydrazone class of chelators with iron and DNA: Implications for toxicity in the treatment of iron overload disease
    • Chaston, T. B. and Richardson, D. R. Interactions of the pyridine-2-carboxaldehyde isonicotinoyl hydrazone class of chelators with iron and DNA: implications for toxicity in the treatment of iron overload disease. J. Biol. Inorg. Chem 2003, 8, 427-438.
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 427-438
    • Chaston, T.B.1    Richardson, D.R.2
  • 119
    • 10644243132 scopus 로고    scopus 로고
    • Lipophilicity of analogs of pyridoxal isonicotinoyl hydrazone (PIH) determines efflux of Fe complexes, which determines their chelating efficiency and toxicity in K562 cells
    • Buss, J. L.; Arduini, E.; Shephard, K. C.; and Ponka, P. Lipophilicity of analogs of pyridoxal isonicotinoyl hydrazone (PIH) determines efflux of Fe complexes, which determines their chelating efficiency and toxicity in K562 cells. Biochem. Pharmacol. 2002.
    • (2002) Biochem. Pharmacol.
    • Buss, J.L.1    Arduini, E.2    Shephard, K.C.3    Ponka, P.4
  • 120
    • 0037437796 scopus 로고    scopus 로고
    • Pyridoxal isonicotinoyl hydrazone analogs induce apoptosis in hematopoietic cells due to their iron-chelating properties
    • Buss, J. L.; Neuzil, J.; Gellert, N.; Weber, C.; and Ponka, P. Pyridoxal isonicotinoyl hydrazone analogs induce apoptosis in hematopoietic cells due to their iron-chelating properties. Biochem. Pharmacol. 2003, 65, 161-172.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 161-172
    • Buss, J.L.1    Neuzil, J.2    Gellert, N.3    Weber, C.4    Ponka, P.5
  • 121
    • 0022903110 scopus 로고
    • Role of iron in the proliferation of the established human tumor cell lines U-937 and K-562: Effects of suramin and a lipophilic iron chelator (PIH)
    • Forsbeck, K.; Bjelkenkrantz, K.; and Nilsson, K. Role of iron in the proliferation of the established human tumor cell lines U-937 and K-562: effects of suramin and a lipophilic iron chelator (PIH). Scand. J. Haematol. 1986, 37, 429-437.
    • (1986) Scand. J. Haematol. , vol.37 , pp. 429-437
    • Forsbeck, K.1    Bjelkenkrantz, K.2    Nilsson, K.3
  • 122
    • 0023616864 scopus 로고
    • Regulation of growth of cultured hepatic epithelial cells by transferrin
    • Tsao, M. S.; Sanders, G. H.; and Grisham, J. W. Regulation of growth of cultured hepatic epithelial cells by transferrin. Exp. Cell Res. 1987, 171, 52-62.
    • (1987) Exp. Cell Res. , vol.171 , pp. 52-62
    • Tsao, M.S.1    Sanders, G.H.2    Grisham, J.W.3
  • 123
    • 0023234092 scopus 로고
    • Replacement of transferrin in serum-free cultures of mitogen-stimulated mouse lymphocytes by a lipophilic iron chelator
    • Brock, J. H. and Stevenson, J. Replacement of transferrin in serum-free cultures of mitogen-stimulated mouse lymphocytes by a lipophilic iron chelator. Immunol. Lett. 1986, 15, 23-25.
    • (1986) Immunol. Lett. , vol.15 , pp. 23-25
    • Brock, J.H.1    Stevenson, J.2
  • 124
    • 0031906718 scopus 로고    scopus 로고
    • Chemical, biological and clinical aspects of dexrazoxane and other bisdioxopiperazines
    • Hasinoff, B. B.; Hellmann, K.; Herman, E. H.; and Ferrans, V. J. Chemical, biological and clinical aspects of dexrazoxane and other bisdioxopiperazines. Curr. Med. Chem. 1998, 5, 1-28.
    • (1998) Curr. Med. Chem. , vol.5 , pp. 1-28
    • Hasinoff, B.B.1    Hellmann, K.2    Herman, E.H.3    Ferrans, V.J.4
  • 125
    • 0027740137 scopus 로고
    • The one-ring open hydrolysis product intermediates of the cardioprotective agent ICRF-187 (dexrazoxane) displace iron from iron-anthracycline complexes
    • Buss, J. L. and Hasinoff, B. B. The one-ring open hydrolysis product intermediates of the cardioprotective agent ICRF-187 (dexrazoxane) displace iron from iron-anthracycline complexes. Agents Actions 1993, 40, 86-95.
    • (1993) Agents Actions , vol.40 , pp. 86-95
    • Buss, J.L.1    Hasinoff, B.B.2
  • 126
    • 0037098878 scopus 로고    scopus 로고
    • Deferiprone protects against doxorubicin-induced myocyte cytotoxicity
    • Barnabe, N.; Zastre, J. A.; Venkataram, S.; and Hasinoff, B. B. Deferiprone protects against doxorubicin-induced myocyte cytotoxicity. Free Rad. Biol. Med. 2002, 33, 266-275.
    • (2002) Free Rad. Biol. Med. , vol.33 , pp. 266-275
    • Barnabe, N.1    Zastre, J.A.2    Venkataram, S.3    Hasinoff, B.B.4
  • 127
    • 0034957066 scopus 로고    scopus 로고
    • The preventive role of deferoxamine against acute doxorubicin-induced cardiac, renal and hepatic toxicity in rats
    • Saad, S. Y.; Najjar, T. A.; and Al Rikabi, A. C. The preventive role of deferoxamine against acute doxorubicin-induced cardiac, renal and hepatic toxicity in rats. Pharmacol. Res. 2001, 43, 211-218.
    • (2001) Pharmacol. Res. , vol.43 , pp. 211-218
    • Saad, S.Y.1    Najjar, T.A.2    Al Rikabi, A.C.3
  • 128
    • 0023629091 scopus 로고
    • Effect of deferoxamine on DNA synthesis, DNA repair, cell proliferation, and differentiation of HL-60 cells
    • Kaplinsky, C.; Estrov, Z.; Freedman, M. H.; Gelfand, E. W.; and Cohen, A. Effect of deferoxamine on DNA synthesis, DNA repair, cell proliferation, and differentiation of HL-60 cells. Leukemia 1987 1, 437-441.
    • (1987) Leukemia , vol.1 , pp. 437-441
    • Kaplinsky, C.1    Estrov, Z.2    Freedman, M.H.3    Gelfand, E.W.4    Cohen, A.5
  • 129
    • 0030928276 scopus 로고    scopus 로고
    • Induction of embryonal carcinoma cell differentiation by deferoxamine, a potent therapeutic iron chelator
    • Tanaka, T.; Muto, N.; Ido, Y.; Itoh, N.; and Tanaka, K. Induction of embryonal carcinoma cell differentiation by deferoxamine, a potent therapeutic iron chelator. Biochim. Biophys. Acta 1997 1357, 91-97.
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 91-97
    • Tanaka, T.1    Muto, N.2    Ido, Y.3    Itoh, N.4    Tanaka, K.5
  • 130
    • 0020600375 scopus 로고
    • Desferrioxamine inhibits induced erythroid differentiation of human leukemic K-562 cells
    • Gambari, R.; Raschella, G.; Tripodi, M.; Farace, M. G.; and Fantoni, A. Desferrioxamine inhibits induced erythroid differentiation of human leukemic K-562 cells. Cell Differ. 1983, 12, 249-255.
    • (1983) Cell Differ. , vol.12 , pp. 249-255
    • Gambari, R.1    Raschella, G.2    Tripodi, M.3    Farace, M.G.4    Fantoni, A.5
  • 131
    • 0032461935 scopus 로고    scopus 로고
    • Apoptotic signal transduction: Emerging pathways
    • Wilson, M. R. Apoptotic signal transduction: emerging pathways. Biochem. Cell Biol. 1998, 76, 573-582.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 573-582
    • Wilson, M.R.1
  • 134
    • 0037013206 scopus 로고    scopus 로고
    • A zinc-finger protein, PLAGL2, induces the expression of a proapoptotic protein Nip3, leading to cellular apoptosis
    • Mizutani, A.; Furukawa, T.; Adachi, Y.; Ikehara, S.; and Taketani, S. A zinc-finger protein, PLAGL2, induces the expression of a proapoptotic protein Nip3, leading to cellular apoptosis. J. Biol. Chem 2002, 277, 15851-15858.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15851-15858
    • Mizutani, A.1    Furukawa, T.2    Adachi, Y.3    Ikehara, S.4    Taketani, S.5
  • 135
    • 0034069521 scopus 로고    scopus 로고
    • Antiproliferative and apoptotic effects of O-Trensox, a new synthetic iron chelator, on differentiated human hepatoma cell lines
    • Rakba, N.; Loyer, P.; Gilot, D.; Delcros, J. G.; Glaise, D.; Baret, P.; Pierre, J. L.; Brissot, P.; and Lescoat, G. Antiproliferative and apoptotic effects of O-Trensox, a new synthetic iron chelator, on differentiated human hepatoma cell lines. Carcinogenesis 2000 21, 943-951.
    • (2000) Carcinogenesis , vol.21 , pp. 943-951
    • Rakba, N.1    Loyer, P.2    Gilot, D.3    Delcros, J.G.4    Glaise, D.5    Baret, P.6    Pierre, J.L.7    Brissot, P.8    Lescoat, G.9
  • 136
    • 0037448105 scopus 로고    scopus 로고
    • Intralysosomal iron: A major determinant of oxidant-induced cell death
    • Yu, Z.; Persson, H. L.; Eaton, J. W.; and Brunk, U. T. Intralysosomal iron: a major determinant of oxidant-induced cell death. Free Radic. Biol. Med. 2003, 34, 1243-1252.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1243-1252
    • Yu, Z.1    Persson, H.L.2    Eaton, J.W.3    Brunk, U.T.4
  • 137
    • 0030865104 scopus 로고    scopus 로고
    • Characterization of the p53 tumor suppressor pathway in cell lines of the National Cancer Institute anticancer drug screen and correlations with the growth-inhibitory potency of 123 anticancer agents
    • O'Connor, P. M.; Jackman, J.; Bae, I.; Myers, T. G.; Fan, S.; Mutoh, M.; Scudiero, D. A.; Monks, A.; Sausville, E. A.; Weinstein, J. N.; Friend, S.; Fornace, A. J., Jr.; and Kohn, K. W. Characterization of the p53 tumor suppressor pathway in cell lines of the National Cancer Institute anticancer drug screen and correlations with the growth-inhibitory potency of 123 anticancer agents. Cancer Res. 1997, 57, 4285-4300.
    • (1997) Cancer Res. , vol.57 , pp. 4285-4300
    • O'Connor, P.M.1    Jackman, J.2    Bae, I.3    Myers, T.G.4    Fan, S.5    Mutoh, M.6    Scudiero, D.A.7    Monks, A.8    Sausville, E.A.9    Weinstein, J.N.10    Friend, S.11    Fornace Jr., A.J.12    Kohn, K.W.13
  • 139
    • 0026699860 scopus 로고
    • Antitumor effect of deferoxamine on human hepatocellular carcinoma growing in athymic nude mice
    • Hann, H. W.; Stahlhut, M. W.; Rubin, R.; and Maddrey, W. C. Antitumor effect of deferoxamine on human hepatocellular carcinoma growing in athymic nude mice. Cancer 1992, 70, 2051-2056.
    • (1992) Cancer , vol.70 , pp. 2051-2056
    • Hann, H.W.1    Stahlhut, M.W.2    Rubin, R.3    Maddrey, W.C.4
  • 140
    • 0032006798 scopus 로고    scopus 로고
    • Failure of iron chelators to reduce tumor growth in human neuroblastoma xenografts
    • Selig, R. A.; White, L.; Gramacho, C.; Sterling-Levis, K.; Fraser, I. W.; and Naidoo, D. Failure of iron chelators to reduce tumor growth in human neuroblastoma xenografts. Cancer Res. 1998, 58, 473-478.
    • (1998) Cancer Res. , vol.58 , pp. 473-478
    • Selig, R.A.1    White, L.2    Gramacho, C.3    Sterling-Levis, K.4    Fraser, I.W.5    Naidoo, D.6
  • 141
    • 0038500738 scopus 로고    scopus 로고
    • Iron withdrawal strategies fail to prevent the growth of SiHa-induced tumors in mice
    • Simonart, T.; Boelaert, J. R.; Andrei, G.; Clercq, E. D.; and Snoeck, R. Iron withdrawal strategies fail to prevent the growth of SiHa-induced tumors in mice. Gynecol. Oncol. 2003, 90, 91-95.
    • (2003) Gynecol. Oncol. , vol.90 , pp. 91-95
    • Simonart, T.1    Boelaert, J.R.2    Andrei, G.3    Clercq, E.D.4    Snoeck, R.5
  • 144
    • 0015303832 scopus 로고
    • Studies of the antineoplastic activity and metabolism of α-(N)-heterocyclic carboxaldehyde thiosemicarbazones in dogs and mice
    • Creasey, W. A.; Agrawal, K. C.; Capizzi, R. L.; Stinson, K. K.; and Sartorelli, A. C. Studies of the antineoplastic activity and metabolism of α-(N)-heterocyclic carboxaldehyde thiosemicarbazones in dogs and mice. Cancer Res. 1972, 32, 565-572.
    • (1972) Cancer Res. , vol.32 , pp. 565-572
    • Creasey, W.A.1    Agrawal, K.C.2    Capizzi, R.L.3    Stinson, K.K.4    Sartorelli, A.C.5
  • 145
    • 0013805463 scopus 로고
    • The carcinostatic activity of α-(N) heterocyclic carboxaldehyde thiosemicarbazones. I. Isoquinoline-1-carboxaldehyde thiosemicarbazone
    • French, F. A. and Blanz, E. J., Jr. The carcinostatic activity of α-(N) heterocyclic carboxaldehyde thiosemicarbazones. I. Isoquinoline-1-carboxaldehyde thiosemicarbazone. Cancer Res. 1965, 25, 1454-1458.
    • (1965) Cancer Res. , vol.25 , pp. 1454-1458
    • French, F.A.1    Blanz Jr., E.J.2
  • 146
    • 0033975268 scopus 로고    scopus 로고
    • Triapine (3-aminopyridine-2-carboxaldehyde-thiosemicarbazone): A potent inhibitor of ribonucleotide reductase activity with broad spectrum antitumor activity
    • Finch, R. A.; Liu, M.; Grill, S. P.; Rose, W. C.; Loomis, R.; Vasquez, K. M.; Cheng, Y.; and Sartorelli, A. C. Triapine (3-aminopyridine-2-carboxaldehyde-thiosemicarbazone): A potent inhibitor of ribonucleotide reductase activity with broad spectrum antitumor activity. Biochem. Pharmacol. 2000, 59, 983-991.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 983-991
    • Finch, R.A.1    Liu, M.2    Grill, S.P.3    Rose, W.C.4    Loomis, R.5    Vasquez, K.M.6    Cheng, Y.7    Sartorelli, A.C.8
  • 147
    • 0026666125 scopus 로고
    • Synthesis and antitumor activity of amino derivatives of pyridine-2-carboxaldehyde thiosemicarbazone
    • Liu, M. C.; Lin, T. S.; and Sartorelli, A. C. Synthesis and antitumor activity of amino derivatives of pyridine-2-carboxaldehyde thiosemicarbazone. J. Med. Chem. 1992, 35, 3672-3677.
    • (1992) J. Med. Chem. , vol.35 , pp. 3672-3677
    • Liu, M.C.1    Lin, T.S.2    Sartorelli, A.C.3
  • 151
    • 0023037399 scopus 로고
    • An animal model of iron overload and its application to study hepatic ferritin iron mobilization by chelators
    • Longueville, A. and Crichton, R. R. An animal model of iron overload and its application to study hepatic ferritin iron mobilization by chelators. Biochem. Pharmacol. 1986, 35, 3669-3678.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 3669-3678
    • Longueville, A.1    Crichton, R.R.2
  • 153
    • 0019518135 scopus 로고
    • Mechanism of in vivo iron chelation by pyridoxal isonicotinoyl hydrazone and other imino derivatives of pyridoxal
    • Hershko, C.; Avramovici-Grisaru, S.; Link, G.; Gelfand, L.; and Sarel, S. Mechanism of in vivo iron chelation by pyridoxal isonicotinoyl hydrazone and other imino derivatives of pyridoxal. J. Lab. Chn. Med. 1981, 98, 99-108.
    • (1981) J. Lab. Clin. Med. , vol.98 , pp. 99-108
    • Hershko, C.1    Avramovici-Grisaru, S.2    Link, G.3    Gelfand, L.4    Sarel, S.5
  • 154
    • 0020051325 scopus 로고
    • An in vivo evaluation of iron-chelating drugs derived from pyridoxal and its analogs
    • Johnson, D. K.; Pippard, M. J.; Murphy, T. B.; and Rose, N. J. An in vivo evaluation of iron-chelating drugs derived from pyridoxal and its analogs. J. Pharm. Exp. Ther. 1982, 221 399-403.
    • (1982) J. Pharm. Exp. Ther. , vol.221 , pp. 399-403
    • Johnson, D.K.1    Pippard, M.J.2    Murphy, T.B.3    Rose, N.J.4
  • 155
    • 0020214635 scopus 로고
    • Pyridoxal complexes as potential chelating agents for oral therapy in transfusional iron overload
    • Williams, A.; Hoy, T.; Pugh, A.; and Jacobs, A. Pyridoxal complexes as potential chelating agents for oral therapy in transfusional iron overload. J. Pharm. Pharmacol. 1982, 34, 730-732.
    • (1982) J. Pharm. Pharmacol. , vol.34 , pp. 730-732
    • Williams, A.1    Hoy, T.2    Pugh, A.3    Jacobs, A.4
  • 156
    • 0020691816 scopus 로고
    • Syntheses of iron bis(pyridoxal isonicotinoylhydrazone)s and the in vivo iron-removal properties of some pyridoxal derivatives
    • Avramovici-Grisaru, S.; Sarel, S.; Link, G.; and Hershko, C. Syntheses of iron bis(pyridoxal isonicotinoylhydrazone)s and the in vivo iron-removal properties of some pyridoxal derivatives. J. Med. Chem. 1983, 26, 298-302.
    • (1983) J. Med. Chem. , vol.26 , pp. 298-302
    • Avramovici-Grisaru, S.1    Sarel, S.2    Link, G.3    Hershko, C.4
  • 157
    • 0018831805 scopus 로고
    • Biliary iron excretion in rats following pyridoxal isonicotinoyl hydrazone
    • Cikrt, M.; Ponka, P.; Necas, E.; and Neuwirt, J. Biliary iron excretion in rats following pyridoxal isonicotinoyl hydrazone. Br. J. Haematol. 1980, 45, 275-283.
    • (1980) Br. J. Haematol. , vol.45 , pp. 275-283
    • Cikrt, M.1    Ponka, P.2    Necas, E.3    Neuwirt, J.4
  • 158
    • 2642709214 scopus 로고    scopus 로고
    • Biliary iron excretion in rats following treatment with analogs of pyridoxal isonicotinoyl hydrazone
    • Blaha, K.; Cikrt, M.; Nerudova, J.; Fornuskova, H.; and Ponka, P. Biliary iron excretion in rats following treatment with analogs
    • (1998) Blood , vol.91 , pp. 4368-4372
    • Blaha, K.1    Cikrt, M.2    Nerudova, J.3    Fornuskova, H.4    Ponka, P.5
  • 162
    • 0028585886 scopus 로고
    • Deferoxamine in children with recurrent neuroblastoma
    • Blatt, J. Deferoxamine in children with recurrent neuroblastoma. Anticancer Res. 1994, 14, 2109-2112.
    • (1994) Anticancer Res. , vol.14 , pp. 2109-2112
    • Blatt, J.1
  • 163
    • 0029066979 scopus 로고
    • Deferoxamine followed by cyclophosphamide, etoposide, carboplatin, thiotepa, induction regimen in advanced neuroblastoma: Preliminary results
    • Italian Neuroblastoma Cooperative Group
    • Donfrancesco, A.; De Bernardi, B.; Carli, M.; Mancini, A.; Nigro, M.; De Sio, L.; Casale, F.; Bagnulo, S.; Helson, L.; and Deb, G. Deferoxamine followed by cyclophosphamide, etoposide, carboplatin, thiotepa, induction regimen in advanced neuroblastoma: preliminary results. Italian Neuroblastoma Cooperative Group. Eur. J. Cancer 1995, 31A, 612-615.
    • (1995) Eur. J. Cancer , vol.31 A , pp. 612-615
    • Donfrancesco, A.1    De Bernardi, B.2    Carli, M.3    Mancini, A.4    Nigro, M.5    De Sio, L.6    Casale, F.7    Bagnulo, S.8    Helson, L.9    Deb, G.10
  • 167
    • 0014691658 scopus 로고
    • Antitumour activity in a series of bisdiketopiperazines
    • Creighton, A. M.; Hellmann, K.; and Whitecross, S. Antitumour activity in a series of bisdiketopiperazines. Nature 1969, 222, 384-385.
    • (1969) Nature , vol.222 , pp. 384-385
    • Creighton, A.M.1    Hellmann, K.2    Whitecross, S.3
  • 169
    • 0031688723 scopus 로고    scopus 로고
    • Efficacy of dexrazoxane as a cardioprotective agent in patients receiving mitoxantrone- and daunorubicin-based chemotherapy
    • Lemez, P. and Maresova, J. Efficacy of dexrazoxane as a cardioprotective agent in patients receiving mitoxantrone- and daunorubicin-based chemotherapy. Semin. Hematol. 1998, 25 61-65.
    • (1998) Semin. Hematol. , vol.25 , pp. 61-65
    • Lemez, P.1    Maresova, J.2
  • 170
    • 0001473294 scopus 로고    scopus 로고
    • O-Trensox, a new tripodal iron chelator based on 8-hydroxyquinoline subunits: Thermodynamic and kinetic studies
    • Serratrice, G.; Boukhalfa, H.; Beguin, C.; Baret, P.; Caris, C.; and Pierre, J. L. O-Trensox, a new tripodal iron chelator based on 8-hydroxyquinoline subunits: thermodynamic and kinetic studies. Inorg. Chem. 1997, 36, 3898-3910.
    • (1997) Inorg. Chem. , vol.36 , pp. 3898-3910
    • Serratrice, G.1    Boukhalfa, H.2    Beguin, C.3    Baret, P.4    Caris, C.5    Pierre, J.L.6
  • 171
    • 0034136253 scopus 로고    scopus 로고
    • Iron complexes of the cardioprotective agent dexrazoxane (ICRF-187) and its desmethyl derivative, ICRF-154: Solid state structure, solution thermodynamics, and DNA cleavage activity
    • Diop, N. K.; Vitellaro, L. K.; Arnold, P.; Shang, M.; and Marusak, R. A. Iron complexes of the cardioprotective agent dexrazoxane (ICRF-187) and its desmethyl derivative, ICRF-154: solid state structure, solution thermodynamics, and DNA cleavage activity. J. Inorg. Biochem. 2000, 78, 209-216.
    • (2000) J. Inorg. Biochem. , vol.78 , pp. 209-216
    • Diop, N.K.1    Vitellaro, L.K.2    Arnold, P.3    Shang, M.4    Marusak, R.A.5
  • 172
    • 0037454748 scopus 로고    scopus 로고
    • Hydrolysis of pyridoxal isonicotinoyl hydrazone and its analogs
    • Buss, J. L. and Ponka, P. Hydrolysis of pyridoxal isonicotinoyl hydrazone and its analogs. Biochim., Biophys. Acta 2003, 1619, 177-186.
    • (2003) Biochim. Biophys. Acta , vol.1619 , pp. 177-186
    • Buss, J.L.1    Ponka, P.2


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