메뉴 건너뛰기




Volumn 25, Issue 7, 2012, Pages 1502-1511

A new mechanism of action for the anticancer drug Mitomycin C: Mechanism-based inhibition of thioredoxin reductase

Author keywords

[No Author keywords available]

Indexed keywords

MITOMYCIN C; NUCLEOPHILE; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN REDUCTASE; XANTHIC ACID DERIVATIVE;

EID: 84863899034     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx3002065     Document Type: Article
Times cited : (96)

References (68)
  • 1
    • 84889379110 scopus 로고    scopus 로고
    • Antitumour Antibiotics
    • (Missailidis, S. Ed.), John Wiley and Sons, Chichester, United Kingdom
    • Paz, M. M. (2008) Antitumour Antibiotics. In Anticancer Therapeutics (Missailidis, S., Ed.), pp 112-115, John Wiley and Sons, Chichester, United Kingdom.
    • (2008) Anticancer Therapeutics , pp. 112-115
    • Paz, M.M.1
  • 2
    • 77954034365 scopus 로고    scopus 로고
    • Use of mitomycin-C for phototherapeutic keratectomy and photorefractive keratectomy surgery
    • Shah, R. and Wilson, S. (2010) Use of mitomycin-C for phototherapeutic keratectomy and photorefractive keratectomy surgery Curr. Opin. Ophthalmol. 21, 269-273
    • (2010) Curr. Opin. Ophthalmol. , vol.21 , pp. 269-273
    • Shah, R.1    Wilson, S.2
  • 5
    • 0029360580 scopus 로고
    • Mitomycin C: Small, fast and deadly (but very selective)
    • Tomasz, M. (1995) Mitomycin C: Small, fast and deadly (but very selective) Chem. Biol. 2, 575-579
    • (1995) Chem. Biol. , vol.2 , pp. 575-579
    • Tomasz, M.1
  • 6
    • 77953397142 scopus 로고    scopus 로고
    • Distinct roles of cytochrome P450 reductase in mitomycin C redox cycling and cytotoxicity
    • Wang, Y., Gray, J. P., Mishin, V., Heck, D. E., Laskin, D. L., and Laskin, J. D. (2010) Distinct roles of cytochrome P450 reductase in mitomycin C redox cycling and cytotoxicity Mol. Cancer Ther. 9, 1852-1863
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 1852-1863
    • Wang, Y.1    Gray, J.P.2    Mishin, V.3    Heck, D.E.4    Laskin, D.L.5    Laskin, J.D.6
  • 7
    • 0024278435 scopus 로고
    • Reductive activation of mitomycin C
    • Hoey, B. M., Butler, J., and Swallow, A. J. (1988) Reductive activation of mitomycin C Biochemistry 27, 2608-2614
    • (1988) Biochemistry , vol.27 , pp. 2608-2614
    • Hoey, B.M.1    Butler, J.2    Swallow, A.J.3
  • 8
    • 0031278015 scopus 로고    scopus 로고
    • The mitomycin bioreductive antitumor agents: Cross-linking and alkylation of DNA as the molecular basis of their activity
    • Tomasz, M. and Palom, Y. (1997) The mitomycin bioreductive antitumor agents: cross-linking and alkylation of DNA as the molecular basis of their activity Pharmacol. Ther. 76, 73-87
    • (1997) Pharmacol. Ther. , vol.76 , pp. 73-87
    • Tomasz, M.1    Palom, Y.2
  • 9
    • 0036852787 scopus 로고    scopus 로고
    • Relative toxicities of DNA cross-links and monoadducts: New insights from studies of decarbamoyl mitomycin C and mitomycin C
    • Palom, Y., Suresh Kumar, G., Tang, L.-Q., Paz, M. M., Musser, S. M., Rockwell, S., and Tomasz, M. (2002) Relative toxicities of DNA cross-links and monoadducts: new insights from studies of decarbamoyl mitomycin C and mitomycin C Chem. Res. Toxicol. 15, 1398-1406
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 1398-1406
    • Palom, Y.1    Suresh Kumar, G.2    Tang, L.-Q.3    Paz, M.M.4    Musser, S.M.5    Rockwell, S.6    Tomasz, M.7
  • 10
    • 0028300426 scopus 로고
    • Conjugation of glutathione and other thiols with bioreductively activated mitomycin C. Effect of thiols on the reductive activation rate
    • Sharma, M. and Tomasz, M. (1994) Conjugation of glutathione and other thiols with bioreductively activated mitomycin C. Effect of thiols on the reductive activation rate Chem. Res. Toxicol. 7, 390-400
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 390-400
    • Sharma, M.1    Tomasz, M.2
  • 11
    • 0028230878 scopus 로고
    • Effects of glutathione on alkylation and cross-linking of DNA by mitomycin C. Isolation of a ternary glutathione-mitomycin-DNA adduct
    • Sharma, M., He, Q. Y., and Tomasz, M. (1994) Effects of glutathione on alkylation and cross-linking of DNA by mitomycin C. Isolation of a ternary glutathione-mitomycin-DNA adduct Chem. Res. Toxicol. 7, 401-407
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 401-407
    • Sharma, M.1    He, Q.Y.2    Tomasz, M.3
  • 12
    • 77953486102 scopus 로고    scopus 로고
    • Mitomycin C inhibits ribosomal RNA: A novel cytotoxic mechanism for bioreductive drugs
    • Snodgrass, R. G., Collier, A. C., Coon, A. E., and Pritsos, C. A. (2010) Mitomycin C inhibits ribosomal RNA: A novel cytotoxic mechanism for bioreductive drugs J. Biol. Chem. 285, 19068-19075
    • (2010) J. Biol. Chem. , vol.285 , pp. 19068-19075
    • Snodgrass, R.G.1    Collier, A.C.2    Coon, A.E.3    Pritsos, C.A.4
  • 13
    • 35848968258 scopus 로고    scopus 로고
    • Thioredoxin-like domains required for glucose regulatory protein 58 mediated reductive activation of mitomycin C leading to DNA cross-linking
    • Adikesavan, A. K. and Jaiswal, A. K. (2007) Thioredoxin-like domains required for glucose regulatory protein 58 mediated reductive activation of mitomycin C leading to DNA cross-linking Mol. Cancer Ther. 6, 2719-2727
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 2719-2727
    • Adikesavan, A.K.1    Jaiswal, A.K.2
  • 14
    • 0141619285 scopus 로고    scopus 로고
    • Role of GRP58 in mitomycin C-induced DNA cross-linking
    • Celli, C. M. and Jaiswal, A. K. (2003) Role of GRP58 in mitomycin C-induced DNA cross-linking Cancer Res. 63, 6016-6025
    • (2003) Cancer Res. , vol.63 , pp. 6016-6025
    • Celli, C.M.1    Jaiswal, A.K.2
  • 15
    • 33746035307 scopus 로고    scopus 로고
    • Si RNA inhibition of GRP58 associated with decrease in mitomycin C-induced DNA cross-linking and cytotoxicity
    • Su, S., Adikesavan, A. K., and Jaiswal, A. K. (2006) Si RNA inhibition of GRP58 associated with decrease in mitomycin C-induced DNA cross-linking and cytotoxicity Chem.-Biol. Interact. 162, 81-87
    • (2006) Chem.-Biol. Interact. , vol.162 , pp. 81-87
    • Su, S.1    Adikesavan, A.K.2    Jaiswal, A.K.3
  • 16
    • 70350239993 scopus 로고    scopus 로고
    • Reductive activation of mitomycin C by thiols: Kinetics, mechanism, and biological implications
    • Paz, M. M. (2009) Reductive activation of mitomycin C by thiols: Kinetics, mechanism, and biological implications Chem. Res. Toxicol. 22, 1663-1668
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1663-1668
    • Paz, M.M.1
  • 17
    • 77955686271 scopus 로고    scopus 로고
    • Cross-linking of dithiols by mitomycin C
    • Paz, M. M. (2010) Cross-linking of dithiols by mitomycin C Chem. Res. Toxicol. 23, 1384-1392
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1384-1392
    • Paz, M.M.1
  • 18
    • 0034705133 scopus 로고    scopus 로고
    • Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
    • Zhong, L., Arnér, E. S. J., and Holmgren, A. (2000) Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Proc. Natl. Acad. Sci. U.S.A. 97, 5854-5859
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5854-5859
    • Zhong, L.1    Arnér, E.S.J.2    Holmgren, A.3
  • 20
    • 77952311188 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
    • Holmgren, A. and Lu, J. (2010) Thioredoxin and thioredoxin reductase: Current research with special reference to human disease Biochem. Biophys. Res. Commun. 396, 120-124
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 120-124
    • Holmgren, A.1    Lu, J.2
  • 21
  • 22
    • 33744958179 scopus 로고    scopus 로고
    • Thioredoxin reductase 1 deficiency reverses tumor phenotype and tumorigenicity of lung carcinoma cells
    • Yoo, M.-H., Xu, X.-M., Carlson, B. a, Gladyshev, V. N., and Hatfield, D. L. (2006) Thioredoxin reductase 1 deficiency reverses tumor phenotype and tumorigenicity of lung carcinoma cells J. Biol. Chem. 281, 13005-13008
    • (2006) J. Biol. Chem. , vol.281 , pp. 13005-13008
    • Yoo, M.-H.1    Xu, X.-M.2    Carlson, B.A.3    Gladyshev, V.N.4    Hatfield, D.L.5
  • 24
    • 0033536575 scopus 로고    scopus 로고
    • High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes
    • Arnér, E. S. J., Sarioglu, H., Lottspeich, F., Holmgren, A., and Böck, A. (1999) High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes J. Mol. Biol. 292, 1003-1016
    • (1999) J. Mol. Biol. , vol.292 , pp. 1003-1016
    • Arnér, E.S.J.1    Sarioglu, H.2    Lottspeich, F.3    Holmgren, A.4    Böck, A.5
  • 25
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • Holmgren, A. and Björnstedt, M. (1995) Thioredoxin and thioredoxin reductase Methods Enzymol. 252, 199-208
    • (1995) Methods Enzymol. , vol.252 , pp. 199-208
    • Holmgren, A.1    Björnstedt, M.2
  • 26
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R. and Wilson, I. B. (1962) Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase J. Biol. Chem. 237, 3245-3249
    • (1962) J. Biol. Chem. , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 27
    • 0016612022 scopus 로고
    • Structure and stereochemistry of some 1,2-disubstituted mitosenes from solvolysis of mitomycin C and Mitomycin A
    • Taylor, W. G. and Remers, W. A. (1975) Structure and stereochemistry of some 1,2-disubstituted mitosenes from solvolysis of mitomycin C and Mitomycin A J. Med. Chem. 18, 307-311
    • (1975) J. Med. Chem. , vol.18 , pp. 307-311
    • Taylor, W.G.1    Remers, W.A.2
  • 28
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. (1983) Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays J. Immunol. Methods 65, 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 29
    • 0028930481 scopus 로고
    • Mechanism-based enzyme inactivators
    • Silverman, R. B. (1995) Mechanism-based enzyme inactivators Methods Enzymol. 249, 240-283
    • (1995) Methods Enzymol. , vol.249 , pp. 240-283
    • Silverman, R.B.1
  • 31
    • 0035818011 scopus 로고    scopus 로고
    • Reductive activation of mitomycin A by thiols
    • Paz, M. M. and Tomasz, M. (2001) Reductive activation of mitomycin A by thiols Org. Lett. 3, 2789-2792
    • (2001) Org. Lett. , vol.3 , pp. 2789-2792
    • Paz, M.M.1    Tomasz, M.2
  • 32
    • 0021721159 scopus 로고
    • Circular dichroism spectroscopy as a probe for the stereochemistry of aziridine cleavage reactions of mitomycin C. Application to adducts of mitomycin with DNA constituents
    • Tomasz, M., Jung, M., Verdine, G., and Nakanishi, K. (1984) Circular dichroism spectroscopy as a probe for the stereochemistry of aziridine cleavage reactions of mitomycin C. Application to adducts of mitomycin with DNA constituents J. Am. Chem. Soc. 106, 7367-7370
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 7367-7370
    • Tomasz, M.1    Jung, M.2    Verdine, G.3    Nakanishi, K.4
  • 33
    • 0026571917 scopus 로고
    • Mechanism-based inhibition of thioredoxin reductase by antitumor quinoid compounds
    • Mau, B. L. and Powis, G. (1992) Mechanism-based inhibition of thioredoxin reductase by antitumor quinoid compounds Biochem. Pharmacol. 43, 1613-1620
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 1613-1620
    • Mau, B.L.1    Powis, G.2
  • 35
    • 0018567024 scopus 로고
    • Formation of 1-ethylxanthyl-2,7-diaminomitosene and 1,10-diethylxanthyl- 2,7-diaminodecarbamoylmitosene in aqueous solution upon reduction-reoxidation of mitomycin C in the presence of potassium ethylxanthate
    • Hornemann, U., Keller, P. J., and Kozlowski, J. F. (1979) Formation of 1-ethylxanthyl-2,7-diaminomitosene and 1,10-diethylxanthyl-2,7- diaminodecarbamoylmitosene in aqueous solution upon reduction-reoxidation of mitomycin C in the presence of potassium ethylxanthate J. Am. Chem. Soc. 101, 7121-7124
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 7121-7124
    • Hornemann, U.1    Keller, P.J.2    Kozlowski, J.F.3
  • 36
    • 0021078732 scopus 로고
    • Reactions of mitomycin C with potassium ethyl xanthate in neutral aqueous solution
    • Hornemann, U., Iguchi, K., Keller, P. J., Vu, H. M., Kozlowski, J. F., and Kohn, H. (1983) Reactions of mitomycin C with potassium ethyl xanthate in neutral aqueous solution J. Org. Chem. 48, 5026-5033
    • (1983) J. Org. Chem. , vol.48 , pp. 5026-5033
    • Hornemann, U.1    Iguchi, K.2    Keller, P.J.3    Vu, H.M.4    Kozlowski, J.F.5    Kohn, H.6
  • 37
    • 0035859927 scopus 로고    scopus 로고
    • Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme
    • Sandalova, T., Zhong, L., Lindqvist, Y., Holmgren, A., and Schneider, G. (2001) Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme Proc. Natl. Acad. Sci. U.S.A. 98, 9533-9538
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9533-9538
    • Sandalova, T.1    Zhong, L.2    Lindqvist, Y.3    Holmgren, A.4    Schneider, G.5
  • 38
    • 0027717389 scopus 로고
    • PH-dependent inactivation of DT-diaphorase by mitomycin C and porfiromycin
    • Siegel, D., Beall, H., Kasai, M., Arai, H., Gibson, N. W., and Ross, D. (1993) pH-dependent inactivation of DT-diaphorase by mitomycin C and porfiromycin Mol. Pharmacol. 44, 1128-1134
    • (1993) Mol. Pharmacol. , vol.44 , pp. 1128-1134
    • Siegel, D.1    Beall, H.2    Kasai, M.3    Arai, H.4    Gibson, N.W.5    Ross, D.6
  • 39
    • 27144469008 scopus 로고    scopus 로고
    • Selenocysteine in proteins-properties and biotechnological use
    • Johansson, L., Gafvelin, G., and Arnér, E. S. J. (2005) Selenocysteine in proteins-properties and biotechnological use Biochim. Biophys. Acta 1726, 1-13
    • (2005) Biochim. Biophys. Acta , vol.1726 , pp. 1-13
    • Johansson, L.1    Gafvelin, G.2    Arnér, E.S.J.3
  • 40
    • 0343131152 scopus 로고
    • Use of differential second-derivative UV and FTIR spectroscopy in structural studies of multichromophoric compounds
    • Verdine, G. L. and Nakanishi, K. (1985) Use of differential second-derivative UV and FTIR spectroscopy in structural studies of multichromophoric compounds J. Am. Chem. Soc. 107, 6118-6120
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 6118-6120
    • Verdine, G.L.1    Nakanishi, K.2
  • 41
    • 0001229584 scopus 로고    scopus 로고
    • 2,7-Diaminomitosene, a Monofunctional Mitomycin C Derivative, Alkylates DNA in the Major Groove. Structure and Base-Sequence Specificity of the DNA Adduct and Mechanism of the Alkylation
    • Suresh Kumar, G., Musser, S. M., Cummings, J., Tomasz, M., and Kumar, G. S. (1996) 2,7-Diaminomitosene, a Monofunctional Mitomycin C Derivative, Alkylates DNA in the Major Groove. Structure and Base-Sequence Specificity of the DNA Adduct and Mechanism of the Alkylation J. Am. Chem. Soc. 118, 9209-9217
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9209-9217
    • Suresh Kumar, G.1    Musser, S.M.2    Cummings, J.3    Tomasz, M.4    Kumar, G.S.5
  • 42
    • 0000797824 scopus 로고    scopus 로고
    • Structure of adduct X, the last unknown of the six major DNA adducts of mitomycin C formed in EMT6 mouse mammary tumor cells
    • Palom, Y., Belcourt, M. F., Musser, S. M., Sartorelli, A. C., Rockwell, S., and Tomasz, M. (2000) Structure of adduct X, the last unknown of the six major DNA adducts of mitomycin C formed in EMT6 mouse mammary tumor cells Chem. Res. Toxicol. 13, 479-488
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 479-488
    • Palom, Y.1    Belcourt, M.F.2    Musser, S.M.3    Sartorelli, A.C.4    Rockwell, S.5    Tomasz, M.6
  • 43
    • 0031594193 scopus 로고    scopus 로고
    • A mitomycin-N6-deoxyadenosine adduct isolated from DNA
    • Palom, Y., Lipman, R., Musser, S. M., and Tomasz, M. (1998) A mitomycin-N6-deoxyadenosine adduct isolated from DNA Chem. Res. Toxicol. 11, 203-210
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 203-210
    • Palom, Y.1    Lipman, R.2    Musser, S.M.3    Tomasz, M.4
  • 44
    • 0023123806 scopus 로고
    • Isolation and structure of a covalent cross-link adduct between mitomycin C and DNA
    • Tomasz, M., Lipman, R., Chowdary, D., Pawlak, J., Verdine, G. L., and Nakanishi, K. (1987) Isolation and structure of a covalent cross-link adduct between mitomycin C and DNA Science 235, 1204-1208
    • (1987) Science , vol.235 , pp. 1204-1208
    • Tomasz, M.1    Lipman, R.2    Chowdary, D.3    Pawlak, J.4    Verdine, G.L.5    Nakanishi, K.6
  • 45
    • 0030726348 scopus 로고    scopus 로고
    • Mitomycin C-DNA adducts generated by DT-diaphorase. Revised mechanism of the enzymatic reductive activation of mitomycin C
    • Suresh Kumar, G., Lipman, R., Cummings, J., and Tomasz, M. (1997) Mitomycin C-DNA adducts generated by DT-diaphorase. Revised mechanism of the enzymatic reductive activation of mitomycin C Biochemistry 36, 14128-14136
    • (1997) Biochemistry , vol.36 , pp. 14128-14136
    • Suresh Kumar, G.1    Lipman, R.2    Cummings, J.3    Tomasz, M.4
  • 47
    • 78651117965 scopus 로고
    • A molecular mechanism of mitomycin action: Linking of complementary DNA strands
    • Iyer, V. N. and Szybalski, W. (1963) A molecular mechanism of mitomycin action: linking of complementary DNA strands Proc. Natl. Acad. Sci. U.S.A. 50, 355-362
    • (1963) Proc. Natl. Acad. Sci. U.S.A. , vol.50 , pp. 355-362
    • Iyer, V.N.1    Szybalski, W.2
  • 48
    • 0002548343 scopus 로고
    • Mitomycins and Porfiromycin: Chemical Mechanism of Activation and Cross-linking of DNA
    • Iyer, V. N. and Szybalski, W. (1964) Mitomycins and Porfiromycin: Chemical Mechanism of Activation and Cross-linking of DNA Science 145, 55-58
    • (1964) Science , vol.145 , pp. 55-58
    • Iyer, V.N.1    Szybalski, W.2
  • 49
    • 39749177838 scopus 로고    scopus 로고
    • Targeting thioredoxin reductase 1 reduction in cancer cells inhibits self-sufficient growth and DNA replication
    • Yoo, M.-H., Xu, X.-M., Carlson, B. A., Patterson, A. D., Gladyshev, V. N., and Hatfield, D. L. (2007) Targeting thioredoxin reductase 1 reduction in cancer cells inhibits self-sufficient growth and DNA replication PloS One 2, e1112
    • (2007) PloS One , vol.2 , pp. 1112
    • Yoo, M.-H.1    Xu, X.-M.2    Carlson, B.A.3    Patterson, A.D.4    Gladyshev, V.N.5    Hatfield, D.L.6
  • 50
    • 36749022747 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase as redox-sensitive molecular targets for cancer therapy
    • Pennington, J. D., Jacobs, K. M., Sun, L., Bar-Sela, G., Mishra, M., and Gius, D. (2007) Thioredoxin and thioredoxin reductase as redox-sensitive molecular targets for cancer therapy Curr. Pharm. Des. 13, 3368-3377
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 3368-3377
    • Pennington, J.D.1    Jacobs, K.M.2    Sun, L.3    Bar-Sela, G.4    Mishra, M.5    Gius, D.6
  • 51
    • 24644441050 scopus 로고    scopus 로고
    • The thioredoxin reductase/thioredoxin system: Novel redox targets for cancer therapy
    • Biaglow, J. E. and Miller, R. A. (2005) The thioredoxin reductase/thioredoxin system: Novel redox targets for cancer therapy Cancer Biol. Ther. 4, 6-13
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 6-13
    • Biaglow, J.E.1    Miller, R.A.2
  • 52
    • 84856837495 scopus 로고    scopus 로고
    • HIF-Independent Regulation of Thioredoxin Reductase 1 Contributes to the High Levels of Reactive Oxygen Species Induced by Hypoxia
    • Naranjo-Suarez, S., Carlson, B. A., Tsuji, P. A., Yoo, M.-H., Gladyshev, V. N., and Hatfield, D. L. (2012) HIF-Independent Regulation of Thioredoxin Reductase 1 Contributes to the High Levels of Reactive Oxygen Species Induced by Hypoxia PLoS One 7, e30470
    • (2012) PLoS One , vol.7 , pp. 30470
    • Naranjo-Suarez, S.1    Carlson, B.A.2    Tsuji, P.A.3    Yoo, M.-H.4    Gladyshev, V.N.5    Hatfield, D.L.6
  • 53
    • 0023233931 scopus 로고
    • Generation of photoemissive species by mitomycin C redox cycling in rat liver microsomes
    • Napetschnig, S. and Sies, H. (1987) Generation of photoemissive species by mitomycin C redox cycling in rat liver microsomes Biochem. Pharmacol. 36, 1617-21
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 1617-1621
    • Napetschnig, S.1    Sies, H.2
  • 54
    • 0020385188 scopus 로고
    • Generation of hydroxyl radical by anticancer quinone drugs, carbazilquinone, mitomycin C, aclacinomycin A and adriamycin, in the presence of NADPH-cytochrome P-450 reductase
    • Komiyama, T., Kikuchi, T., and Sugiura, Y. (1982) Generation of hydroxyl radical by anticancer quinone drugs, carbazilquinone, mitomycin C, aclacinomycin A and adriamycin, in the presence of NADPH-cytochrome P-450 reductase Biochem. Pharmacol. 31, 3651-3656
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 3651-3656
    • Komiyama, T.1    Kikuchi, T.2    Sugiura, Y.3
  • 55
    • 0029051872 scopus 로고
    • Cellular levels of thioredoxin associated with drug sensitivity to cisplatin, mitomycin C, doxorubicin, and etoposide
    • Yokomizo, A., Ono, M., Nanri, H., Makino, Y., Ohga, T., Wada, M., Okamoto, T., Yodoi, J., Kuwano, M., and Kohno, K. (1995) Cellular levels of thioredoxin associated with drug sensitivity to cisplatin, mitomycin C, doxorubicin, and etoposide Cancer Res. 55, 4293-4296
    • (1995) Cancer Res. , vol.55 , pp. 4293-4296
    • Yokomizo, A.1    Ono, M.2    Nanri, H.3    Makino, Y.4    Ohga, T.5    Wada, M.6    Okamoto, T.7    Yodoi, J.8    Kuwano, M.9    Kohno, K.10
  • 56
    • 67349120863 scopus 로고    scopus 로고
    • Focus on mammalian thioredoxin reductases-Important selenoproteins with versatile functions
    • Arnér, E. S. J. (2009) Focus on mammalian thioredoxin reductases-Important selenoproteins with versatile functions Biochim. Biophys. Acta 1790, 495-526
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 495-526
    • Arnér, E.S.J.1
  • 57
    • 0035890009 scopus 로고    scopus 로고
    • Analysis of the inhibition of mammalian thioredoxin, thioredoxin reductase, and glutaredoxin by cis-diamminedichloroplatinum (II) and its major metabolite, the glutathione-platinum complex
    • Arnér, E. S. J., Nakamura, H., Sasada, T., Yodoi, J., Holmgren, A., and Spyrou, G. (2001) Analysis of the inhibition of mammalian thioredoxin, thioredoxin reductase, and glutaredoxin by cis-diamminedichloroplatinum (II) and its major metabolite, the glutathione-platinum complex Free Radical Biol. Med. 31, 1170-1178
    • (2001) Free Radical Biol. Med. , vol.31 , pp. 1170-1178
    • Arnér, E.S.J.1    Nakamura, H.2    Sasada, T.3    Yodoi, J.4    Holmgren, A.5    Spyrou, G.6
  • 58
    • 23444435104 scopus 로고    scopus 로고
    • Inhibition of thioredoxin reductase but not of glutathione reductase by the major classes of alkylating and platinum-containing anticancer compounds
    • Witte, A.-B., Anestål, K., Jerremalm, E., Ehrsson, H., and Arnér, E. S. J. (2005) Inhibition of thioredoxin reductase but not of glutathione reductase by the major classes of alkylating and platinum-containing anticancer compounds Free Radical Biol. Med. 39, 696-703
    • (2005) Free Radical Biol. Med. , vol.39 , pp. 696-703
    • Witte, A.-B.1    Anestål, K.2    Jerremalm, E.3    Ehrsson, H.4    Arnér, E.S.J.5
  • 59
    • 37549006456 scopus 로고    scopus 로고
    • Thioredoxin reductase inactivation as a pivotal mechanism of ifosfamide in cancer therapy
    • Wang, X., Zhang, J., and Xu, T. (2008) Thioredoxin reductase inactivation as a pivotal mechanism of ifosfamide in cancer therapy Eur. J. Pharmacol. 579, 66-73
    • (2008) Eur. J. Pharmacol. , vol.579 , pp. 66-73
    • Wang, X.1    Zhang, J.2    Xu, T.3
  • 60
    • 1642535437 scopus 로고    scopus 로고
    • Interactions of quinones with thioredoxin reductase: A challenge to the antioxidant role of the mammalian selenoprotein
    • Cenas, N., Nivinskas, H., Anusevicius, Z., Sarlauskas, J., Lederer, F., and Arnér, E. S. J. (2004) Interactions of quinones with thioredoxin reductase: a challenge to the antioxidant role of the mammalian selenoprotein J. Biol. Chem. 279, 2583-2592
    • (2004) J. Biol. Chem. , vol.279 , pp. 2583-2592
    • Cenas, N.1    Nivinskas, H.2    Anusevicius, Z.3    Sarlauskas, J.4    Lederer, F.5    Arnér, E.S.J.6
  • 61
    • 33751181030 scopus 로고    scopus 로고
    • On the potential of thioredoxin reductase inhibitors for cancer therapy
    • Urig, S. and Becker, K. (2006) On the potential of thioredoxin reductase inhibitors for cancer therapy Sem. Cancer Biol. 16, 452-465
    • (2006) Sem. Cancer Biol. , vol.16 , pp. 452-465
    • Urig, S.1    Becker, K.2
  • 62
    • 33746430147 scopus 로고    scopus 로고
    • Thioredoxin reductase as a novel molecular target for cancer therapy
    • Nguyen, P., Awwad, R. T., Smart, D. D. K., Spitz, D. R., and Gius, D. (2006) Thioredoxin reductase as a novel molecular target for cancer therapy Cancer Lett. 236, 164-174
    • (2006) Cancer Lett. , vol.236 , pp. 164-174
    • Nguyen, P.1    Awwad, R.T.2    Smart, D.D.K.3    Spitz, D.R.4    Gius, D.5
  • 63
    • 70350140433 scopus 로고    scopus 로고
    • Synthesis of the First Selenium-Containing Acyclic Nucleosides and Anomeric Spironucleosides from Carbohydrate Precursors
    • Maza, S., López, Ó., Martos, S., Maya, I., and Fernández-Bolaños, J. G. (2009) Synthesis of the First Selenium-Containing Acyclic Nucleosides and Anomeric Spironucleosides from Carbohydrate Precursors Eur. J. Org. Chem. 2009, 5239-5246
    • (2009) Eur. J. Org. Chem. , vol.2009 , pp. 5239-5246
    • Maza, S.1    López, Ó.2    Martos, S.3    Maya, I.4    Fernández- Bolaños, J.G.5
  • 64
    • 77649261685 scopus 로고    scopus 로고
    • Selenium and the Selenoprotein Thioredoxin Reductase in the Prevention, Treatment and Diagnostics of Cancer
    • Selenius, M., Rundlöf, A.-K., Olm, E., Fernandes, A. P., and Björnstedt, M. (2010) Selenium and the Selenoprotein Thioredoxin Reductase in the Prevention, Treatment and Diagnostics of Cancer Antioxid. Redox Signaling 12, 867-880
    • (2010) Antioxid. Redox Signaling , vol.12 , pp. 867-880
    • Selenius, M.1    Rundlöf, A.-K.2    Olm, E.3    Fernandes, A.P.4    Björnstedt, M.5
  • 65
    • 41549108420 scopus 로고    scopus 로고
    • From single- to multi-target drugs in cancer therapy: When aspecificity becomes an advantage
    • Petrelli, A. and Giordano, S. (2008) From single- to multi-target drugs in cancer therapy: When aspecificity becomes an advantage Curr. Med. Chem. 15, 422-432
    • (2008) Curr. Med. Chem. , vol.15 , pp. 422-432
    • Petrelli, A.1    Giordano, S.2
  • 66
    • 27144443099 scopus 로고    scopus 로고
    • Drug discovery: Playing dirty
    • Frantz, S. (2005) Drug discovery: Playing dirty Nature 437, 942-943
    • (2005) Nature , vol.437 , pp. 942-943
    • Frantz, S.1
  • 67
    • 27544446579 scopus 로고    scopus 로고
    • Promiscuous drugs compared to selective drugs (promiscuity can be a virtue)
    • Mencher, S. K. and Wang, L. G. (2005) Promiscuous drugs compared to selective drugs (promiscuity can be a virtue) BMC Clin. Pharmacol. 5, 3
    • (2005) BMC Clin. Pharmacol. , vol.5 , pp. 3
    • Mencher, S.K.1    Wang, L.G.2
  • 68
    • 26844501695 scopus 로고    scopus 로고
    • Anticancer therapeutics: "addictive" targets, multi-targeted drugs, new drug combinations
    • Broxterman, H. J. and Georgopapadakou, N. H. (2005) Anticancer therapeutics: "Addictive" targets, multi-targeted drugs, new drug combinations Drug Resist. Updates 8, 183-197
    • (2005) Drug Resist. Updates , vol.8 , pp. 183-197
    • Broxterman, H.J.1    Georgopapadakou, N.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.