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Volumn 20, Issue 12, 2007, Pages 1903-1912

Quinone formation as a chemoprevention strategy for hybrid drugs: Balancing cytotoxicity and cytoprotection

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLSALICYLIC ACID 3 (NITROXYMETHYL)PHENYL ESTER; BROMIDE; ESTERASE; LUCIFERASE; MESYLIC ACID; NCX 4040; NITRATE; NITRIC OXIDE; NITRIC OXIDE DONOR; NONSTEROID ANTIINFLAMMATORY AGENT; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); THIOL; UNCLASSIFIED DRUG;

EID: 38149120931     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx7002257     Document Type: Article
Times cited : (55)

References (60)
  • 1
    • 9644272830 scopus 로고    scopus 로고
    • Protection against electrophile and oxidative stress by induction of phase 2 genes: The quest for the elusive sensor that responds to inducers
    • Holtzclaw, W. D., Dinkova-Kostova, A. T., and Talalay, P. (2004) Protection against electrophile and oxidative stress by induction of phase 2 genes: The quest for the elusive sensor that responds to inducers. Adv. Enzyme Regul. 44, 335-367.
    • (2004) Adv. Enzyme Regul , vol.44 , pp. 335-367
    • Holtzclaw, W.D.1    Dinkova-Kostova, A.T.2    Talalay, P.3
  • 2
    • 1242274624 scopus 로고    scopus 로고
    • Role of nicotinamide quinone oxidoreductase 1 (NQO1) in protection against toxicity of electrophiles and reactive oxygen intermediates
    • Talalay, P., and Dinkova-Kostova, A. T. (2004) Role of nicotinamide quinone oxidoreductase 1 (NQO1) in protection against toxicity of electrophiles and reactive oxygen intermediates. Methods Enzymol. 382, 355-364.
    • (2004) Methods Enzymol , vol.382 , pp. 355-364
    • Talalay, P.1    Dinkova-Kostova, A.T.2
  • 3
    • 9644252648 scopus 로고
    • Delay of methylcholanthrene skin carcinogenesis in mice by 1,2,5,6-dibenzofluorene
    • Riegel, B., Wartman, W. B., Hill, W. T., Reeb, B. B., Shubik, P., and Stanger, D. W. (1951) Delay of methylcholanthrene skin carcinogenesis in mice by 1,2,5,6-dibenzofluorene. Cancer Res. 11, 301-303.
    • (1951) Cancer Res , vol.11 , pp. 301-303
    • Riegel, B.1    Wartman, W.B.2    Hill, W.T.3    Reeb, B.B.4    Shubik, P.5    Stanger, D.W.6
  • 4
    • 0343974179 scopus 로고
    • Inhibition of the carcinogenic action produced by a weakly carcinogenic hydrocarbon on a highly active carcinogenic hydrocarbon
    • Lacassagne, A., Buu, H., and Rudali, G. (1945) Inhibition of the carcinogenic action produced by a weakly carcinogenic hydrocarbon on a highly active carcinogenic hydrocarbon. Br. J. Exp. Pathol. 26, 5-12.
    • (1945) Br. J. Exp. Pathol , vol.26 , pp. 5-12
    • Lacassagne, A.1    Buu, H.2    Rudali, G.3
  • 5
    • 30344448851 scopus 로고    scopus 로고
    • Phase I and Phase II drug metabolism: Terminology that we should phase out?
    • Josephy, D. P., Guengerich, P. F., and Miners, J. O. (2005) "Phase I and Phase II" drug metabolism: Terminology that we should phase out? Drug Metab. Rev. 37, 575-580.
    • (2005) Drug Metab. Rev , vol.37 , pp. 575-580
    • Josephy, D.P.1    Guengerich, P.F.2    Miners, J.O.3
  • 6
    • 0029027838 scopus 로고
    • Electrophile and antioxidant regulation of enzymes that detoxify carcinogens
    • Prestera, T., and Talalay, P. (1995) Electrophile and antioxidant regulation of enzymes that detoxify carcinogens. Proc. Natl. Acad. Sci. U.S.A. 92, 8965-8969.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 8965-8969
    • Prestera, T.1    Talalay, P.2
  • 7
    • 0001143581 scopus 로고
    • On the mechanisms of induction of cancer-protective enzymes: A unifying proposal
    • Prochaska, H. J., De Long, M. J., and Talalay, P. (1985) On the mechanisms of induction of cancer-protective enzymes: A unifying proposal. Proc. Natl. Acad. Sci. U.S.A. 82, 8232-8236.
    • (1985) Proc. Natl. Acad. Sci. U.S.A , vol.82 , pp. 8232-8236
    • Prochaska, H.J.1    De Long, M.J.2    Talalay, P.3
  • 8
    • 33748994836 scopus 로고    scopus 로고
    • Bioactivation of selective estrogen receptor modulators (SERMs)
    • Dowers, T. S., Qin, Z. H., Thatcher, G. R., and Bolton, J. L. (2006) Bioactivation of selective estrogen receptor modulators (SERMs). Chem. Res. Toxicol. 19, 1125-1137.
    • (2006) Chem. Res. Toxicol , vol.19 , pp. 1125-1137
    • Dowers, T.S.1    Qin, Z.H.2    Thatcher, G.R.3    Bolton, J.L.4
  • 9
    • 34748889958 scopus 로고    scopus 로고
    • Structural modulation of reactivity/activity in design of improved benzothiophene SERMs: Induction of chemopreventive mechanisms
    • Yu, B., Dietz, B. M., Dunlap, T., Kastrati, I., Lantvit, D. L., Overk, C. R., Yao, P., Qin, Z., Bolton, J. L., and Thatcher, G. R. J. (2007) Structural modulation of reactivity/activity in design of improved benzothiophene SERMs: Induction of chemopreventive mechanisms. Mol. Cancer Ther. 6, 2418-2428.
    • (2007) Mol. Cancer Ther , vol.6 , pp. 2418-2428
    • Yu, B.1    Dietz, B.M.2    Dunlap, T.3    Kastrati, I.4    Lantvit, D.L.5    Overk, C.R.6    Yao, P.7    Qin, Z.8    Bolton, J.L.9    Thatcher, G.R.J.10
  • 10
    • 0034626064 scopus 로고    scopus 로고
    • Risk and prognosis of endometrial cancer after tamoxifen for breast cancer. Comprehensive Cancer Centres' ALERT Group. Assessment of liver and endometrial cancer risk following tamoxifen
    • Bergman, L., Beelen, M. L., Gallee, M. P., Hollema, H., Benraadt, J., and van Leeuwen, F. E. (2000) Risk and prognosis of endometrial cancer after tamoxifen for breast cancer. Comprehensive Cancer Centres' ALERT Group. Assessment of liver and endometrial cancer risk following tamoxifen. Lancet 356, 881-887.
    • (2000) Lancet , vol.356 , pp. 881-887
    • Bergman, L.1    Beelen, M.L.2    Gallee, M.P.3    Hollema, H.4    Benraadt, J.5    van Leeuwen, F.E.6
  • 11
    • 3042794987 scopus 로고    scopus 로고
    • Quinoids formed from estrogens and antiestrogens
    • Bolton, J. L., Yu, L., and Thatcher, G. R. J. (2004) Quinoids formed from estrogens and antiestrogens. Methods Enzymol. 378, 110-123.
    • (2004) Methods Enzymol , vol.378 , pp. 110-123
    • Bolton, J.L.1    Yu, L.2    Thatcher, G.R.J.3
  • 12
    • 1642281756 scopus 로고    scopus 로고
    • Drug-protein adducts: An industry perspective on minimizing the potential for drug bioactivation in drug discovery and development
    • Evans, D. C., Watt, A. P., Nicoll-Griffith, D. A., and Baillie, T. A. (2004) Drug-protein adducts: An industry perspective on minimizing the potential for drug bioactivation in drug discovery and development. Chem. Res. Toxicol. 17, 3-16.
    • (2004) Chem. Res. Toxicol , vol.17 , pp. 3-16
    • Evans, D.C.1    Watt, A.P.2    Nicoll-Griffith, D.A.3    Baillie, T.A.4
  • 14
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., and Talalay, P. (2002) Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc. Natl. Acad. Sci. U.S.A. 99, 11908-11913.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5    Katoh, Y.6    Yamamoto, M.7    Talalay, P.8
  • 15
    • 23844459602 scopus 로고    scopus 로고
    • Therapeutic potential of nitrate esters of commonly used drugs
    • Bolla, M., Almirante, N., and Benedini, F. (2005) Therapeutic potential of nitrate esters of commonly used drugs. Curr. Top. Med. Chem. 5, 707-720.
    • (2005) Curr. Top. Med. Chem , vol.5 , pp. 707-720
    • Bolla, M.1    Almirante, N.2    Benedini, F.3
  • 16
    • 0027729415 scopus 로고
    • Mechanism-based inactivation of prostatic acid phosphatase
    • Myers, J. K., and Widlanski, T. S. (1993) Mechanism-based inactivation of prostatic acid phosphatase. Science 262, 1451-1453.
    • (1993) Science , vol.262 , pp. 1451-1453
    • Myers, J.K.1    Widlanski, T.S.2
  • 17
    • 0028863679 scopus 로고
    • 4-(Fluoromethyl)phenyl phosphate acts as a mechanism-based inhibitor of calcineurin
    • Born, T. L., Myers, J. K., Widlanski, T. S., and Rusnak, F. (1995) 4-(Fluoromethyl)phenyl phosphate acts as a mechanism-based inhibitor of calcineurin. J. Biol. Chem. 270, 25651-25655.
    • (1995) J. Biol. Chem , vol.270 , pp. 25651-25655
    • Born, T.L.1    Myers, J.K.2    Widlanski, T.S.3    Rusnak, F.4
  • 18
    • 34249008406 scopus 로고    scopus 로고
    • Chemical insights in the concept of hybrid drugs: The antitumor effect of nitric oxide-donating aspirin involves a quinone methide but not nitric oxide nor aspirin
    • Hulsman, N., Medema, J. P., Bos, C., Jongejan, A., Leurs, R., Smit, M. J., Esch, I. J., Richel, D., and Wijtmans, M. (2007) Chemical insights in the concept of hybrid drugs: The antitumor effect of nitric oxide-donating aspirin involves a quinone methide but not nitric oxide nor aspirin. J. Med. Chem. 50, 2424-2431.
    • (2007) J. Med. Chem , vol.50 , pp. 2424-2431
    • Hulsman, N.1    Medema, J.P.2    Bos, C.3    Jongejan, A.4    Leurs, R.5    Smit, M.J.6    Esch, I.J.7    Richel, D.8    Wijtmans, M.9
  • 19
    • 4644231576 scopus 로고    scopus 로고
    • Nitrates and NO release: Contemporary aspects in biological and medicinal chemistry
    • Thatcher, G. R. J., Nicolescu, A. C., Bennett, B. M., and Toader, V. (2004) Nitrates and NO release: Contemporary aspects in biological and medicinal chemistry. Free Radical Biol. Med. 37, 1122-1143.
    • (2004) Free Radical Biol. Med , vol.37 , pp. 1122-1143
    • Thatcher, G.R.J.1    Nicolescu, A.C.2    Bennett, B.M.3    Toader, V.4
  • 20
    • 38149123809 scopus 로고    scopus 로고
    • Organic nitrates and nitrites as stores of NO and NO mimesis
    • van Fassen, E, and Vanin, A, Eds, Elsevier Science, Amsterdam
    • Thatcher, G. R. J. (2007) Organic nitrates and nitrites as stores of NO and NO mimesis. In Radicals for Life: The Various Forms of Nitric Oxide (van Fassen, E., and Vanin, A., Eds.) Elsevier Science, Amsterdam.
    • (2007) Radicals for Life: The Various Forms of Nitric Oxide
    • Thatcher, G.R.J.1
  • 22
    • 0034573074 scopus 로고    scopus 로고
    • Activation of antioxidant-response element (ARE), mitogen-activated protein kinases (MAPKs) and caspases by major green tea polyphenol components during cell survival and death
    • Chen, C., Yu, R., Owuor, E. D., and Kong, A. N. (2000) Activation of antioxidant-response element (ARE), mitogen-activated protein kinases (MAPKs) and caspases by major green tea polyphenol components during cell survival and death. Arch. Pharm. Res. 23, 605-612.
    • (2000) Arch. Pharm. Res , vol.23 , pp. 605-612
    • Chen, C.1    Yu, R.2    Owuor, E.D.3    Kong, A.N.4
  • 23
    • 0023930873 scopus 로고
    • Direct measurement of NAD(P)H:quinone reductase from cells cultured in microtiter wells: A screening assay for anticarcinogenic enzyme inducers
    • Prochaska, H. J., and Santamaria, A. B. (1988) Direct measurement of NAD(P)H:quinone reductase from cells cultured in microtiter wells: A screening assay for anticarcinogenic enzyme inducers. Anal. Biochem. 169, 328-336.
    • (1988) Anal. Biochem , vol.169 , pp. 328-336
    • Prochaska, H.J.1    Santamaria, A.B.2
  • 24
    • 0033083919 scopus 로고    scopus 로고
    • Cancer chemopreventive activity mediated by 4′-bromoflavone, a potent inducer of phase II detoxification enzymes
    • Song, L. L., Kosmeder, J. W., 2nd, Lee, S. K., Gerhauser, C., Lantvit, D., Moon, R. C., Moriarty, R. M., and Pezzuto, J. M. (1999) Cancer chemopreventive activity mediated by 4′-bromoflavone, a potent inducer of phase II detoxification enzymes. Cancer Res. 59, 578-585.
    • (1999) Cancer Res , vol.59 , pp. 578-585
    • Song, L.L.1    Kosmeder 2nd, J.W.2    Lee, S.K.3    Gerhauser, C.4    Lantvit, D.5    Moon, R.C.6    Moriarty, R.M.7    Pezzuto, J.M.8
  • 26
    • 1242319541 scopus 로고    scopus 로고
    • Induction of quinone reductase as a primary screen for natural product anticarcinogens
    • Kang, Y. H., and Pezzuto, J. M. (2004) Induction of quinone reductase as a primary screen for natural product anticarcinogens. Methods Enzymol. 382, 380-414.
    • (2004) Methods Enzymol , vol.382 , pp. 380-414
    • Kang, Y.H.1    Pezzuto, J.M.2
  • 27
    • 33645280058 scopus 로고    scopus 로고
    • NO-donating aspirin induces phase II enzymes in vitro and in vivo
    • Gao, J., Kashfi, K., Liu, X., and Rigas, B. (2006) NO-donating aspirin induces phase II enzymes in vitro and in vivo. Carcinogenesis 27, 803-810.
    • (2006) Carcinogenesis , vol.27 , pp. 803-810
    • Gao, J.1    Kashfi, K.2    Liu, X.3    Rigas, B.4
  • 28
    • 33748994836 scopus 로고    scopus 로고
    • Bioactivation of selective estrogen receptor modulators (SERMs)
    • Dowers, T. S., Qin, Z. H., Thatcher, G. R. J., and Bolton, J. L. (2006) Bioactivation of selective estrogen receptor modulators (SERMs). Chem. Res. Toxicol. 19, 1125-1137.
    • (2006) Chem. Res. Toxicol , vol.19 , pp. 1125-1137
    • Dowers, T.S.1    Qin, Z.H.2    Thatcher, G.R.J.3    Bolton, J.L.4
  • 29
    • 5144232811 scopus 로고    scopus 로고
    • Chemoprevention through the Keap1-Nrf2 signaling pathway by phase 2 enzyme inducers
    • Kwak, M. K., Wakabayashi, N., and Kensler, T. W. (2004) Chemoprevention through the Keap1-Nrf2 signaling pathway by phase 2 enzyme inducers. Mutat. Res. 555, 133-148.
    • (2004) Mutat. Res , vol.555 , pp. 133-148
    • Kwak, M.K.1    Wakabayashi, N.2    Kensler, T.W.3
  • 30
    • 33645993864 scopus 로고    scopus 로고
    • Quinone reductase induction as a biomarker for cancer chemoprevention
    • Cuendet, M., Oteham, C. P., Moon, R. C., and Pezzuto, J. M. (2006) Quinone reductase induction as a biomarker for cancer chemoprevention. J. Nat. Prod. 69, 460-463.
    • (2006) J. Nat. Prod , vol.69 , pp. 460-463
    • Cuendet, M.1    Oteham, C.P.2    Moon, R.C.3    Pezzuto, J.M.4
  • 31
    • 0035969989 scopus 로고    scopus 로고
    • Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase 1
    • Asher, G., Lotem, J., Cohen, B., Sachs, L., and Shaul, Y. (2001) Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase 1. Proc. Natl. Acad. Sci. U.S.A. 98, 1188-1193.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 1188-1193
    • Asher, G.1    Lotem, J.2    Cohen, B.3    Sachs, L.4    Shaul, Y.5
  • 33
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress
    • Zhang, D. D., and Hannink, M. (2003) Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol. Cell. Biol. 23, 8137-8151.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 34
    • 0037424262 scopus 로고    scopus 로고
    • Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival
    • Kwak, M. K., Wakabayashi, N., Itoh, K., Motohashi, H., Yamamoto, M., and Kensler, T. W. (2003) Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival. J. Biol. Chem. 278, 8135-8145.
    • (2003) J. Biol. Chem , vol.278 , pp. 8135-8145
    • Kwak, M.K.1    Wakabayashi, N.2    Itoh, K.3    Motohashi, H.4    Yamamoto, M.5    Kensler, T.W.6
  • 35
    • 28844469924 scopus 로고    scopus 로고
    • Molecular mechanism of nrf2 activation by oxidative stress
    • Kang, K. W., Lee, S. J., and Kim, S. G. (2005) Molecular mechanism of nrf2 activation by oxidative stress. Antioxid. Redox Signaling 7, 1664-1673.
    • (2005) Antioxid. Redox Signaling , vol.7 , pp. 1664-1673
    • Kang, K.W.1    Lee, S.J.2    Kim, S.G.3
  • 36
    • 33750430654 scopus 로고    scopus 로고
    • Butylated hydroxyanisole regulates ARE-mediated gene expression via Nrf2 coupled with ERK and JNK signaling pathway in HepG2 cells
    • Yuan, X., Xu, C., Pan, Z., Keum, Y. S., Kim, J. H., Shen, G., Yu, S., Oo, K. T., Ma, J., and Kong, A. N. (2006) Butylated hydroxyanisole regulates ARE-mediated gene expression via Nrf2 coupled with ERK and JNK signaling pathway in HepG2 cells. Mol. Carcinog. 45, 841-850.
    • (2006) Mol. Carcinog , vol.45 , pp. 841-850
    • Yuan, X.1    Xu, C.2    Pan, Z.3    Keum, Y.S.4    Kim, J.H.5    Shen, G.6    Yu, S.7    Oo, K.T.8    Ma, J.9    Kong, A.N.10
  • 38
    • 0034858876 scopus 로고    scopus 로고
    • Vasorelaxant effects of a nitric oxide-releasing aspirin derivative in normotensive and hypertensive rats
    • Muscara, M. N., Lovren, F., McKnight, W., Dicay, M., del Soldato, P., Triggle, C. R., and Wallace, J. L. (2001) Vasorelaxant effects of a nitric oxide-releasing aspirin derivative in normotensive and hypertensive rats. Br. J. Pharmacol. 133, 1314-1322.
    • (2001) Br. J. Pharmacol , vol.133 , pp. 1314-1322
    • Muscara, M.N.1    Lovren, F.2    McKnight, W.3    Dicay, M.4    del Soldato, P.5    Triggle, C.R.6    Wallace, J.L.7
  • 39
    • 0343832167 scopus 로고    scopus 로고
    • Effect of single and repeated doses of a new nitroderivative of acetylsalicylic acid on platelet TXA2 production in rats
    • Cuzzolin, L., Adami, A., Degan, M., Crivellente, F., Bonapace, S., Minuz, P., and Benoni, G. (1996) Effect of single and repeated doses of a new nitroderivative of acetylsalicylic acid on platelet TXA2 production in rats. Life Sci. 58, PL207-PL210.
    • (1996) Life Sci , vol.58
    • Cuzzolin, L.1    Adami, A.2    Degan, M.3    Crivellente, F.4    Bonapace, S.5    Minuz, P.6    Benoni, G.7
  • 40
    • 0032951722 scopus 로고    scopus 로고
    • In vivo antithrombotic effects of a nitric oxide-releasing aspirin derivative, NCX-4016
    • Wallace, J. L., Muscara, M. N., McKnight, W., Dicay, M., Del Soldato, P., and Cirino, G. (1999) In vivo antithrombotic effects of a nitric oxide-releasing aspirin derivative, NCX-4016. Thromb. Res. 93, 43-50.
    • (1999) Thromb. Res , vol.93 , pp. 43-50
    • Wallace, J.L.1    Muscara, M.N.2    McKnight, W.3    Dicay, M.4    Del Soldato, P.5    Cirino, G.6
  • 41
    • 0036681476 scopus 로고    scopus 로고
    • In vitro metabolism of a nitroderivative of acetylsalicylic acid (NCX4016) by rat liver: LC and LC-MS studies
    • Carini, M., Aldini, G., Orioli, M., and Maffei Facino, R. (2002) In vitro metabolism of a nitroderivative of acetylsalicylic acid (NCX4016) by rat liver: LC and LC-MS studies. J. Pharm. Biomed. Anal. 29, 1061-1071.
    • (2002) J. Pharm. Biomed. Anal , vol.29 , pp. 1061-1071
    • Carini, M.1    Aldini, G.2    Orioli, M.3    Maffei Facino, R.4
  • 42
    • 0034886127 scopus 로고    scopus 로고
    • Nitrosylhemoglobin, an unequivocal index of nitric oxide release from nitroaspirin: In vitro and in vivo studies in the rat by ESR spectroscopy
    • Carini, M., Aldini, G., Stefani, R., Orioli, M., and Facino, R. M. (2001) Nitrosylhemoglobin, an unequivocal index of nitric oxide release from nitroaspirin: in vitro and in vivo studies in the rat by ESR spectroscopy. J. Pharm. Biomed. Anal. 26, 509-518.
    • (2001) J. Pharm. Biomed. Anal , vol.26 , pp. 509-518
    • Carini, M.1    Aldini, G.2    Stefani, R.3    Orioli, M.4    Facino, R.M.5
  • 43
    • 28044436484 scopus 로고    scopus 로고
    • Nitric oxide-donating aspirin induces apoptosis in human colon cancer cells through induction of oxidative stress
    • Gao, J., Liu, X., and Rigas, B. (2005) Nitric oxide-donating aspirin induces apoptosis in human colon cancer cells through induction of oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 102, 17207-17212.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 17207-17212
    • Gao, J.1    Liu, X.2    Rigas, B.3
  • 45
    • 14344255689 scopus 로고    scopus 로고
    • Positional isomerism markedly affects the growth inhibition of colon cancer cells by NO-donating aspirin in vitro and in vivo
    • Kashfi, K., Borgo, S., Williams, J. L., Chen, J., Gao, J., Glekas, A., Benedini, F., Del Soldato, P., and Rigas, B. (2005) Positional isomerism markedly affects the growth inhibition of colon cancer cells by NO-donating aspirin in vitro and in vivo. J. Pharmacol. Exp. Ther. 312, 978-988.
    • (2005) J. Pharmacol. Exp. Ther , vol.312 , pp. 978-988
    • Kashfi, K.1    Borgo, S.2    Williams, J.L.3    Chen, J.4    Gao, J.5    Glekas, A.6    Benedini, F.7    Del Soldato, P.8    Rigas, B.9
  • 46
    • 37049156861 scopus 로고
    • Hydrolytic decomposition of esters of nitric acid. IV. Acid hydrolysis, and the effects of change in the nucleophilic reagent on the SN and ECO reactions
    • Baker, J. W., and Neale, A. J. (1955) Hydrolytic decomposition of esters of nitric acid. IV. Acid hydrolysis, and the effects of change in the nucleophilic reagent on the SN and ECO reactions. J. Chem. Soc. 608-615.
    • (1955) J. Chem. Soc , pp. 608-615
    • Baker, J.W.1    Neale, A.J.2
  • 47
    • 0007864586 scopus 로고
    • α-Deuterium isotope effect for displacement of the nitrate group
    • Koshy, K. M., and Robertson, R. E. (1974) α-Deuterium isotope effect for displacement of the nitrate group. J. Am. Chem. Soc. 96, 914-916.
    • (1974) J. Am. Chem. Soc , vol.96 , pp. 914-916
    • Koshy, K.M.1    Robertson, R.E.2
  • 48
    • 36949089540 scopus 로고
    • Importance of ion exchange with the solvent in kinetic studies
    • Baker, J. W., and Neale, A. J. (1953) Importance of ion exchange with the solvent in kinetic studies. Nature (London) 172, 583.
    • (1953) Nature (London) , vol.172 , pp. 583
    • Baker, J.W.1    Neale, A.J.2
  • 49
    • 12644277786 scopus 로고
    • Nucleophilic displacement of the nitrate group. 1. Hydrolysis of a series of benzyl nitrates in water
    • Koshy, K. M., and Robertson, R. E. (1974) Nucleophilic displacement of the nitrate group. 1. Hydrolysis of a series of benzyl nitrates in water. Can. J. Chem. 52, 2485-2490.
    • (1974) Can. J. Chem , vol.52 , pp. 2485-2490
    • Koshy, K.M.1    Robertson, R.E.2
  • 50
    • 38149044699 scopus 로고
    • The hydrolysis of substituted benzyl nitrates in water. II. Effect of ortho-substitution
    • Koshy, K. M., Robertson, R. E., Dyson, G. S., and Singh, S. (1976) The hydrolysis of substituted benzyl nitrates in water. II. Effect of ortho-substitution. Can. J. Chem. 54, 3614-3619.
    • (1976) Can. J. Chem , vol.54 , pp. 3614-3619
    • Koshy, K.M.1    Robertson, R.E.2    Dyson, G.S.3    Singh, S.4
  • 51
    • 38149123809 scopus 로고    scopus 로고
    • Organic nitrates and nitrites as stores of
    • van Fassen, E, and Vanin, A, Eds, Elsevier Science, Amsterdam
    • Thatcher, G. R. J. (2007) Organic nitrates and nitrites as stores of NO. In Radicals for Life: The Various Forms of Nitric Oxide (van Fassen, E., and Vanin, A., Eds.) Elsevier Science, Amsterdam.
    • (2007) Radicals for Life: The Various Forms of Nitric Oxide
    • Thatcher, G.R.J.1
  • 52
    • 0142185107 scopus 로고    scopus 로고
    • Role of mitochondrial aldehyde dehydrogenase in nitrate tolerance
    • DiFabio, J., Ji, Y., Vasiliou, V., Thatcher, G. R. J., and Bennett, B. M. (2003) Role of mitochondrial aldehyde dehydrogenase in nitrate tolerance. Mol. Pharmacol. 64, 1109-1116.
    • (2003) Mol. Pharmacol , vol.64 , pp. 1109-1116
    • DiFabio, J.1    Ji, Y.2    Vasiliou, V.3    Thatcher, G.R.J.4    Bennett, B.M.5
  • 53
    • 0034834142 scopus 로고    scopus 로고
    • Flash photolytic generation of ortho-quinone methide in aqueous solution and study of its chemistry in that medium
    • Chiang, Y., Kresge, A. J., and Zhu, Y. (2001) Flash photolytic generation of ortho-quinone methide in aqueous solution and study of its chemistry in that medium. J. Am. Chem. Soc. 123, 8089-8094.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 8089-8094
    • Chiang, Y.1    Kresge, A.J.2    Zhu, Y.3
  • 54
    • 0037024152 scopus 로고    scopus 로고
    • Flash photolytic generation and study of p-quinone methide in aqueous solution. An estimate of rate and equilibrium constants for heterolysis of the carbon-bromine bond in p-hydroxybenzyl bromide
    • Chiang, Y., Kresge, A. J., and Zhu, Y. (2002) Flash photolytic generation and study of p-quinone methide in aqueous solution. An estimate of rate and equilibrium constants for heterolysis of the carbon-bromine bond in p-hydroxybenzyl bromide. J. Am. Chem. Soc. 124, 6349-6356.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 6349-6356
    • Chiang, Y.1    Kresge, A.J.2    Zhu, Y.3
  • 56
    • 0032714220 scopus 로고    scopus 로고
    • Polar molecular surface as a dominating determinant for oral absorption and brain penetration of drugs
    • Kelder, J., Grootenhuis, P. D., Bayada, D. M., Delbressine, L. P., and Ploemen, J. P. (1999) Polar molecular surface as a dominating determinant for oral absorption and brain penetration of drugs. Pharm. Res. 16, 1514-1519.
    • (1999) Pharm. Res , vol.16 , pp. 1514-1519
    • Kelder, J.1    Grootenhuis, P.D.2    Bayada, D.M.3    Delbressine, L.P.4    Ploemen, J.P.5
  • 58
    • 0041315929 scopus 로고    scopus 로고
    • Kar, S., Lefterov, I. M., Wang, M., Lazo, J. S., Scott, C. N., Wilcox, C. S., and Carr, B. I. (2003) Binding and inhibition of Cdc25 phosphatases by vitamin K analogues. Biochemistry 42, 10490-10497.
    • Kar, S., Lefterov, I. M., Wang, M., Lazo, J. S., Scott, C. N., Wilcox, C. S., and Carr, B. I. (2003) Binding and inhibition of Cdc25 phosphatases by vitamin K analogues. Biochemistry 42, 10490-10497.
  • 60
    • 33746061276 scopus 로고    scopus 로고
    • Nitric oxide-releasing aspirin and indomethacin are potent inhibitors against colon cancer in azoxymethane-treated rats: Effects on molecular targets
    • Rao, C. V., Reddy, B. S., Steele, V. E., Wang, C. X., Liu, X., Ouyang, N., Patlolla, J. M., Simi, B., Kopelovich, L., and Rigas, B. (2006) Nitric oxide-releasing aspirin and indomethacin are potent inhibitors against colon cancer in azoxymethane-treated rats: effects on molecular targets. Mol. Cancer Ther. 5, 1530-1538.
    • (2006) Mol. Cancer Ther , vol.5 , pp. 1530-1538
    • Rao, C.V.1    Reddy, B.S.2    Steele, V.E.3    Wang, C.X.4    Liu, X.5    Ouyang, N.6    Patlolla, J.M.7    Simi, B.8    Kopelovich, L.9    Rigas, B.10


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