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Volumn 2012, Issue , 2012, Pages

Drug-induced oxidative stress and toxicity

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; ALLOPURINOL; ALPHA TOCOPHEROL; AMIFOSTINE; ASCORBIC ACID; CARNITINE; CARVEDILOL; CHLORPROMAZINE; CISPLATIN; DICLOFENAC; DOXORUBICIN; MITOGEN ACTIVATED PROTEIN KINASE; PARACETAMOL; PITAVASTATIN; PROPOFOL; RAZOXANE; REACTIVE OXYGEN METABOLITE; TRASTUZUMAB; UBIDECARENONE; ZIDOVUDINE;

EID: 84866173741     PISSN: 16878191     EISSN: 16878205     Source Type: Journal    
DOI: 10.1155/2012/645460     Document Type: Review
Times cited : (542)

References (117)
  • 2
    • 0036285223 scopus 로고    scopus 로고
    • Nitric oxide modulates superoxide release and peroxynitrite formation in human blood vessels
    • DOI 10.1161/01.HYP.0000018041.48432.B5
    • Guzik T. J., West N. E. J., Pillai R., Taggart D. P., Channon K. M., Nitric oxide modulates superoxide release and peroxynitrite formation in human blood vessels. Hypertension 2002 39 6 1088 1094 2-s2.0-0036285223 10.1161/01.HYP.0000018041.48432.B5 (Pubitemid 34620129)
    • (2002) Hypertension , vol.39 , Issue.6 , pp. 1088-1094
    • Guzik, T.J.1    West, N.E.J.2    Pillai, R.3    Taggart, D.P.4    Channon, K.M.5
  • 3
    • 23844439393 scopus 로고    scopus 로고
    • Oxidative stress-induced apoptosis in neurons correlates with mitochondrial DNA base excision repair pathway imbalance
    • DOI 10.1093/nar/gki759
    • Harrison J. F., Hollensworth S. B., Spitz D. R., Copeland W. C., Wilson G. L., LeDoux S. P., Oxidative stress-induced apoptosis in neurons correlates with mitochondrial DNA base excision repair pathway imbalance. Nucleic Acids Research 2005 33 14 4660 4671 2-s2.0-23844439393 10.1093/nar/gki759 (Pubitemid 41222580)
    • (2005) Nucleic Acids Research , vol.33 , Issue.14 , pp. 4660-4671
    • Harrison, J.F.1    Hollensworth, S.B.2    Spitz, D.R.3    Copeland, W.C.4    Wilson, G.L.5    LeDoux, S.P.6
  • 4
    • 58949084649 scopus 로고    scopus 로고
    • Base excision repair of oxidative DNA damage and association with cancer and aging
    • 2-s2.0-58949084649 10.1093/carcin/bgn250
    • Maynard S., Schurman S. H., Harboe C., de Souza-Pinto N. C., Bohr V. A., Base excision repair of oxidative DNA damage and association with cancer and aging. Carcinogenesis 2009 30 1 2 10 2-s2.0-58949084649 10.1093/carcin/bgn250
    • (2009) Carcinogenesis , vol.30 , Issue.1 , pp. 2-10
    • Maynard, S.1    Schurman, S.H.2    Harboe, C.3    De Souza-Pinto, N.C.4    Bohr, V.A.5
  • 5
    • 33745265207 scopus 로고    scopus 로고
    • Reactive oxygen species: Role in the development of cancer and various chronic conditions
    • 2-s2.0-33745265207 10.1186/1477-3163-5-14
    • Waris G., Ahsan H., Reactive oxygen species: role in the development of cancer and various chronic conditions. Journal of Carcinogenesis 2006 5, article 14 2-s2.0-33745265207 10.1186/1477-3163-5-14
    • (2006) Journal of Carcinogenesis , vol.514
    • Waris, G.1    Ahsan, H.2
  • 6
    • 77953456203 scopus 로고    scopus 로고
    • Acute seizure activity promotes lipid peroxidation, increased nitrite levels and adaptive pathways against oxidative stress in the frontal cortex and striatum
    • 2-s2.0-77953456203
    • Nobre H. V. Jr., Fonteles M. M. D. F., De Freitas R. M. D., Acute seizure activity promotes lipid peroxidation, increased nitrite levels and adaptive pathways against oxidative stress in the frontal cortex and striatum. Oxidative Medicine and Cellular Longevity 2009 2 3 130 137 2-s2.0-77953456203
    • (2009) Oxidative Medicine and Cellular Longevity , vol.2 , Issue.3 , pp. 130-137
    • Nobre, Jr.H.V.1    Fonteles, M.M.D.F.2    De Freitas, R.M.D.3
  • 8
    • 33646080824 scopus 로고    scopus 로고
    • Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products
    • 2-s2.0-33646080824 10.1021/tx0600043
    • Neeley W. L., Essigmann J. M., Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products. Chemical Research in Toxicology 2006 19 4 491 505 2-s2.0-33646080824 10.1021/tx0600043
    • (2006) Chemical Research in Toxicology , vol.19 , Issue.4 , pp. 491-505
    • Neeley, W.L.1    Essigmann, J.M.2
  • 9
    • 0030965894 scopus 로고    scopus 로고
    • Influence of the local helical conformation on the guanine modifications generated from one-electron DNA oxidation
    • DOI 10.1021/bi962761d
    • Spassky A., Angelov D., Influence of the local helical conformation on the guanine modifications generated from one-electron DNA oxidation. Biochemistry 1997 36 22 6571 6576 2-s2.0-0030965894 10.1021/bi962761d (Pubitemid 27242314)
    • (1997) Biochemistry , vol.36 , Issue.22 , pp. 6571-6576
    • Spassky, A.1    Angelov, D.2
  • 10
    • 4444339833 scopus 로고    scopus 로고
    • Oxidative DNA damage and disease: Induction, repair and significance
    • DOI 10.1016/j.mrrev.2003.11.001, PII S138357420300139X
    • Evans M. D., Dizdaroglu M., Cooke M. S., Oxidative DNA damage and disease: induction, repair and significance. Mutation Research 2004 567 1 1 61 2-s2.0-4444339833 10.1016/j.mrrev.2003.11.001 (Pubitemid 39162992)
    • (2004) Mutation Research - Reviews in Mutation Research , vol.567 , Issue.1 , pp. 1-61
    • Evans, M.D.1    Dizdaroglu, M.2    Cooke, M.S.3
  • 11
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani S., Takeshita M., Grollman A. P., Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature 1991 349 6308 431 434 2-s2.0-0025981359 10.1038/349431a0 (Pubitemid 21926107)
    • (1991) Nature , vol.349 , Issue.6308 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 12
    • 79956191022 scopus 로고    scopus 로고
    • Role of oxidative stress and DNA damage in human carcinogenesis
    • 2-s2.0-79956191022 10.1016/j.mrfmmm.2010.12.016
    • Kryston T. B., Georgiev A. B., Pissis P., Georgakilas A. G., Role of oxidative stress and DNA damage in human carcinogenesis. Mutation Research 2011 711 1-2 193 201 2-s2.0-79956191022 10.1016/j.mrfmmm.2010.12.016
    • (2011) Mutation Research , vol.711 , Issue.1-2 , pp. 193-201
    • Kryston, T.B.1    Georgiev, A.B.2    Pissis, P.3    Georgakilas, A.G.4
  • 13
    • 0032558424 scopus 로고    scopus 로고
    • Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8- dihydroguanosine triphosphate incorporation and extension by replicative and repair DNA polymerases
    • DOI 10.1021/bi981346d
    • Einolf H. J., Schnetz-Boutaud N., Guengerich F. P., Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8- dihydroguanosine triphosphate incorporation and extension by replicative and repair DNA polymerases. Biochemistry 1998 37 38 13300 13312 2-s2.0-0032558424 10.1021/bi981346d (Pubitemid 28449575)
    • (1998) Biochemistry , vol.37 , Issue.38 , pp. 13300-13312
    • Einolf, H.J.1    Schnetz-Boutaud, N.2    Guengerich, F.P.3
  • 14
    • 0038799736 scopus 로고    scopus 로고
    • Oxidative DNA damage: Mechanisms, mutation, and disease
    • DOI 10.1096/fj.02-0752rev
    • Cooke M. S., Evans M. D., Dizdaroglu M., Lunec J., Oxidative DNA damage: mechanisms, mutation, and disease. The FASEB Journal 2003 17 10 1195 1214 2-s2.0-0038799736 10.1096/fj.02-0752rev (Pubitemid 36775767)
    • (2003) FASEB Journal , vol.17 , Issue.10 , pp. 1195-1214
    • Cooke, M.S.1    Evans, M.D.2    Dizdaroglu, M.3    Lunec, J.4
  • 15
    • 0028341311 scopus 로고
    • Major oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil, exhibit sequence context-dependent mispairing in vitro
    • Purmal A. A., Kow Y. W., Wallace S. S., Major oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil, exhibit sequence context-dependent mispairing in vitro. Nucleic Acids Research 1994 22 1 72 78 2-s2.0-0028341311 (Pubitemid 24157436)
    • (1994) Nucleic Acids Research , vol.22 , Issue.1 , pp. 72-78
    • Purmal, A.A.1    Kow, Y.W.2    Wallace, S.S.3
  • 16
    • 70350518538 scopus 로고    scopus 로고
    • Creating context for the use of DNA adduct data in cancer risk assessment: II. Overview of methods of identification and quantitation of DNA damage Analysis of DNA damage
    • 2-s2.0-70350518538 10.1080/10408440903164163
    • Himmelstein M. W., Boogaard P. J., Cadet J., Farmer P. B., Kim J. H., Martin E. A., Persaud R., Shuker D. E. G., Creating context for the use of DNA adduct data in cancer risk assessment: II. Overview of methods of identification and quantitation of DNA damage Analysis of DNA damage. Critical Reviews in Toxicology 2009 39 8 679 694 2-s2.0-70350518538 10.1080/10408440903164163
    • (2009) Critical Reviews in Toxicology , vol.39 , Issue.8 , pp. 679-694
    • Himmelstein, M.W.1    Boogaard, P.J.2    Cadet, J.3    Farmer, P.B.4    Kim, J.H.5    Martin, E.A.6    Persaud, R.7    Shuker, D.E.G.8
  • 17
    • 47849100494 scopus 로고    scopus 로고
    • Mechanism of oxidative DNA damage repair and relevance to human pathology
    • 2-s2.0-47849100494 10.1016/j.mrrev.2007.10.003
    • D'Errico M., Parlanti E., Dogliotti E., Mechanism of oxidative DNA damage repair and relevance to human pathology. Mutation Research 2008 659 1-2 4 14 2-s2.0-47849100494 10.1016/j.mrrev.2007.10.003
    • (2008) Mutation Research , vol.659 , Issue.1-2 , pp. 4-14
    • D'Errico, M.1    Parlanti, E.2    Dogliotti, E.3
  • 18
    • 0030818650 scopus 로고    scopus 로고
    • Kinetics of excision of purine lesions from DNA by Escherichia coli Fpg protein
    • DOI 10.1093/nar/25.3.474
    • Karakaya A., Jaruga P., Bohr V. A., Grollman A. P., Dizdaroglu M., Kinetics of excision of purine lesions from DNA by Escherichia coli Fpg protein. Nucleic Acids Research 1997 25 3 474 479 2-s2.0-0030818650 10.1093/nar/25.3.474 (Pubitemid 27298226)
    • (1997) Nucleic Acids Research , vol.25 , Issue.3 , pp. 474-479
    • Karakaya, A.1    Jaruga, P.2    Bohr, V.A.3    Grollman, A.P.4    Dizdaroglu, M.5
  • 19
    • 0345448169 scopus 로고    scopus 로고
    • Substrate specificities and excision kinetics of DNA glycosylases involved in base-excision repair of oxidative DNA damage
    • DOI 10.1016/j.mrfmmm.2003.07.003
    • Dizdaroglu M., Substrate specificities and excision kinetics of DNA glycosylases involved in base-excision repair of oxidative DNA damage. Mutation Research 2003 531 1-2 109 126 2-s2.0-0345448169 10.1016/j.mrfmmm.2003.07.003 (Pubitemid 37456726)
    • (2003) Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis , vol.531 , Issue.1-2 , pp. 109-126
    • Dizdaroglu, M.1
  • 20
    • 27844495699 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage by DNA glycosylases
    • DOI 10.1016/j.mrfmmm.2005.01.033, PII S0027510705002782, Mechanistic Approaches to Chemoprevention of Mutation and Cancer
    • Dizdaroglu M., Base-excision repair of oxidative DNA damage by DNA glycosylases. Mutation Research 2005 591 1-2 45 59 2-s2.0-27844495699 10.1016/j.mrfmmm.2005.01.033 (Pubitemid 41654839)
    • (2005) Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis , vol.591 , Issue.1-2 , pp. 45-59
    • Dizdaroglu, M.1
  • 21
    • 0027375157 scopus 로고
    • Direct enzymic detection of endogenous oxidative base damage in human lymphocyte DNA
    • Collins A. R., Duthie S. J., Dobson V. L., Direct enzymic detection of endogenous oxidative base damage in human lymphocyte DNA. Carcinogenesis 1993 14 9 1733 1735 2-s2.0-0027375157 (Pubitemid 23290881)
    • (1993) Carcinogenesis , vol.14 , Issue.9 , pp. 1733-1735
    • Collins, A.R.1    Duthie, S.J.2    Dobson, V.L.3
  • 22
    • 0036628726 scopus 로고    scopus 로고
    • Biological consequences of free radical-damaged DNA bases
    • DOI 10.1016/S0891-5849(02)00827-4, PII S0891584902008274
    • Wallace S. S., Biological consequences of free radical-damaged DNA bases. Free Radical Biology and Medicine 2002 33 1 1 14 2-s2.0-0036628726 10.1016/S0891-5849(02)00827-4 (Pubitemid 34681001)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.1 , pp. 1-14
    • Wallace, S.S.1
  • 23
    • 0037215540 scopus 로고    scopus 로고
    • The stalling of transcription at abasic sites is highly mutagenic
    • DOI 10.1128/MCB.23.1.382-388.2003
    • Yu S. L., Lee S. K., Johnson R. E., Prakash L., Prakash S., The stalling of transcription at abasic sites is highly mutagenic. Molecular and Cellular Biology 2003 23 1 382 388 2-s2.0-0037215540 10.1128/MCB.23.1.382-388.2003 (Pubitemid 36008528)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.1 , pp. 382-388
    • Yu, S.-L.1    Lee, S.-K.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5
  • 24
    • 4344577088 scopus 로고    scopus 로고
    • Role of p53 in sensing oxidative DNA damage in response to reactive oxygen species-generating agents
    • DOI 10.1158/0008-5472.CAN-04-0494
    • Achanta G., Huang P., Role of p53 in sensing oxidative DNA damage in response to reactive oxygen species-generating agents. Cancer Research 2004 64 17 6233 6239 2-s2.0-4344577088 10.1158/0008-5472.CAN-04-0494 (Pubitemid 39129425)
    • (2004) Cancer Research , vol.64 , Issue.17 , pp. 6233-6239
    • Achanta, G.1    Huang, P.2
  • 25
    • 33645459044 scopus 로고    scopus 로고
    • Biomarkers of oxidative damage in human disease
    • 2-s2.0-33645459044 10.1373/clinchem.2005.061408
    • Dalle-Donne I., Rossi R., Colombo R., Giustarini D., Milzani A., Biomarkers of oxidative damage in human disease. Clinical Chemistry 2006 52 4 601 623 2-s2.0-33645459044 10.1373/clinchem.2005.061408
    • (2006) Clinical Chemistry , vol.52 , Issue.4 , pp. 601-623
    • Dalle-Donne, I.1    Rossi, R.2    Colombo, R.3    Giustarini, D.4    Milzani, A.5
  • 26
    • 0025240126 scopus 로고
    • Investigation of the adducts formed by reaction of malondialdehyde with adenosine
    • Stone K., Ksebati M. B., Marnett L. J., Investigation of the adducts formed by reaction of malondialdehyde with adenosine. Chemical Research in Toxicology 1990 3 1 33 38 2-s2.0-0025240126 (Pubitemid 20128626)
    • (1990) Chemical Research in Toxicology , vol.3 , Issue.1 , pp. 33-38
    • Stone, K.1    Ksebati, M.B.2    Marnett, L.J.3
  • 27
    • 0041731614 scopus 로고    scopus 로고
    • Malondialdehyde, a product of lipid peroxidation, is mutagenic in human cells
    • DOI 10.1074/jbc.M212549200
    • Niedernhofer L. J., Daniels J. S., Rouzer C. A., Greene R. E., Marnett L. J., Malondialdehyde, a product of lipid peroxidation, is mutagenic in human cells. The Journal of Biological Chemistry 2003 278 33 31426 31433 2-s2.0-0041731614 10.1074/jbc.M212549200 (Pubitemid 36994664)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31426-31433
    • Niedernhofer, L.J.1    Daniels, J.S.2    Rouzer, C.A.3    Greene, R.E.4    Marnett, L.J.5
  • 28
    • 79951518607 scopus 로고    scopus 로고
    • Molecular targets of oxidative stress
    • 2-s2.0-79951518607 10.1042/BJ20101695
    • Avery S. V., Molecular targets of oxidative stress. Biochemical Journal 2011 434 2 201 210 2-s2.0-79951518607 10.1042/BJ20101695
    • (2011) Biochemical Journal , vol.434 , Issue.2 , pp. 201-210
    • Avery, S.V.1
  • 29
    • 34248165632 scopus 로고    scopus 로고
    • Lipid peroxidation, oxidative stress genes and dietary factors in breast cancer protection: A hypothesis
    • ARTICLE 201 2-s2.0-34248165632
    • Gago-Dominguez M., Jiang X., Castelao J. E., Lipid peroxidation, oxidative stress genes and dietary factors in breast cancer protection: a hypothesis. Breast Cancer Research 2007 9 1, article 201 2-s2.0-34248165632
    • (2007) Breast Cancer Research , vol.9 , Issue.1
    • Gago-Dominguez, M.1    Jiang, X.2    Castelao, J.E.3
  • 30
    • 13244258258 scopus 로고    scopus 로고
    • Lipid peroxidation in diabetes mellitus
    • DOI 10.1089/ars.2005.7.256
    • Davì G., Falco A., Patrono C., Lipid peroxidation in diabetes mellitus. Antioxidants and Redox Signaling 2005 7 1-2 256 268 2-s2.0-13244258258 10.1089/ars.2005.7.256 (Pubitemid 40187942)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.1-2 , pp. 256-268
    • Davi, G.1    Falco, A.2    Patrono, C.3
  • 31
    • 0021833156 scopus 로고
    • Lipid peroxidation and acute lung injury after thermal trauma to skin. Evidence of a role for hydroxyl radical
    • Till G. O., Hatherill J. R., Tourtellotte W. W., Lipid peroxidation and acute lung injury after thermal trauma to skin. Evidence of a role for hydroxyl radical. American Journal of Pathology 1985 119 3 376 384 2-s2.0-0021833156 (Pubitemid 15051886)
    • (1985) American Journal of Pathology , vol.119 , Issue.3 , pp. 376-384
    • Till, G.O.1    Hatherill, J.R.2    Tourtellotte, W.W.3
  • 33
    • 0022978476 scopus 로고
    • Lipid peroxidation and Parkinson's disease
    • Pall H. S., Williams A. C., Blake D. R., Lipid peroxidation and Parkinson's disease. The Lancet 1986 2 8511 870 871 2-s2.0-0022978476 (Pubitemid 17178075)
    • (1986) Lancet , vol.2 , Issue.8511 , pp. 870-871
    • Pall, H.S.1    Williams, A.C.2    Blake, D.R.3
  • 34
    • 4644310560 scopus 로고    scopus 로고
    • Role of oxidative modifications in atherosclerosis
    • DOI 10.1152/physrev.00047.2003
    • Stocker R., Keaney J. F., Role of oxidative modifications in atherosclerosis. Physiological Reviews 2004 84 4 1381 1478 2-s2.0-4644310560 10.1152/physrev.00047.2003 (Pubitemid 39302636)
    • (2004) Physiological Reviews , vol.84 , Issue.4 , pp. 1381-1478
    • Stocker, R.1    Keaney Jr., J.F.2
  • 35
    • 80053513183 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatases by reversible oxidation
    • 2-s2.0-80053513183 10.1093/jb/mvr104
    • Östman A., Frijhoff J., Sandin Å., Böhmer F.-D., Regulation of protein tyrosine phosphatases by reversible oxidation. Journal of Biochemistry 2011 150 4 345 356 2-s2.0-80053513183 10.1093/jb/mvr104
    • (2011) Journal of Biochemistry , vol.150 , Issue.4 , pp. 345-356
    • Östman, A.1    Frijhoff, J.2    Sandin, Å.3    Böhmer, F.-D.4
  • 37
    • 0028139041 scopus 로고
    • Identification of a conserved oxidation-sensitive cysteine residue in the NFI family of DNA-binding proteins
    • Bandyopadhyay S., Gronostajski R. M., Identification of a conserved oxidation-sensitive cysteine residue in the NFI family of DNA-binding proteins. The Journal of Biological Chemistry 1994 269 47 29949 29955 2-s2.0-0028139041 (Pubitemid 24365164)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.47 , pp. 29949-29955
    • Bandyopadhyay, S.1    Gronostajski, R.M.2
  • 38
    • 50249175909 scopus 로고    scopus 로고
    • Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins
    • 2-s2.0-50249175909 10.1083/jcb.200803022
    • Medicherla B., Goldberg A. L., Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins. Journal of Cell Biology 2008 182 4 663 673 2-s2.0-50249175909 10.1083/jcb.200803022
    • (2008) Journal of Cell Biology , vol.182 , Issue.4 , pp. 663-673
    • Medicherla, B.1    Goldberg, A.L.2
  • 39
    • 0042666797 scopus 로고    scopus 로고
    • Ascorbate-induced oxidation of glyceraldehyde-3-phosphate dehydrogenase
    • DOI 10.1016/S0006-291X(03)01421-9
    • Schmalhausen E. V., Pleten' A. P., Muronetz V. I., Ascorbate-induced oxidation of glyceraldehyde-3-phosphate dehydrogenase. Biochemical and Biophysical Research Communications 2003 308 3 492 496 2-s2.0-0042666797 10.1016/S0006-291X(03)01421-9 (Pubitemid 36945519)
    • (2003) Biochemical and Biophysical Research Communications , vol.308 , Issue.3 , pp. 492-496
    • Schmalhausen, E.V.1    Pleten, A.P.2    Muronetz, V.I.3
  • 40
    • 0023852405 scopus 로고
    • Increase of enzyme activities following the in vitro peroxidation of normal human red blood cells
    • Vives Corrons J. L., Pujades M. A., Colomer D., Increase of enzyme activities following the in vitro peroxidation of normal human red blood cells. Enzyme 1988 39 1 1 7 2-s2.0-0023852405 (Pubitemid 18038661)
    • (1988) Enzyme , vol.39 , Issue.1 , pp. 1-7
    • Vives Corrons, J.L.1    Pujades, M.A.2    Colomer, D.3
  • 41
    • 84864186763 scopus 로고    scopus 로고
    • Nuclear transport: A switch for the oxidative stresssignaling circuit?
    • 208650 10.1155/2012/208650
    • Kodiha M., Vol. 2012, pp. 1-18, 2012, Stochaj U., Nuclear transport: a switch for the oxidative stresssignaling circuit? Journal of Signal Transduction 2012 2012 18 208650 10.1155/2012/208650
    • (2012) Journal of Signal Transduction , vol.2012 , pp. 18
    • Kodiha, M.1    Stochaj, U.2
  • 42
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of krebs cycle enzymes by hydrogen peroxide: A key role of α-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress
    • Tretter L., Adam-Vizi V., Inhibition of krebs cycle enzymes by hydrogen peroxide: a key role of α -ketoglutarate dehydrogenase in limiting NADH production under oxidative stress. Journal of Neuroscience 2000 20 24 8972 8979 2-s2.0-0034671429 (Pubitemid 32042897)
    • (2000) Journal of Neuroscience , vol.20 , Issue.24 , pp. 8972-8979
    • Tretter, L.1    Adam-Vizi, V.2
  • 44
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • DOI 10.1007/s00726-003-0011-2
    • Stadtman E. R., Levine R. L., Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 2003 25 3-4 207 218 2-s2.0-0346100345 10.1007/s00726-003-0011-2 (Pubitemid 38043943)
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 45
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • DOI 10.1074/jbc.272.33.20313
    • Berlett B. S., Stadtman E. R., Protein oxidation in aging, disease, and oxidative stress. The Journal of Biological Chemistry 1997 272 33 20313 20316 2-s2.0-0030841350 10.1074/jbc.272.33.20313 (Pubitemid 27355575)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 46
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • DOI 10.1074/jbc.M206279200
    • Shringarpure R., Grune T., Mehlhase J., Davies K. J. A., Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. The Journal of Biological Chemistry 2003 278 1 311 318 2-s2.0-0037414834 10.1074/jbc.M206279200 (Pubitemid 36043578)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.A.4
  • 47
    • 0033938817 scopus 로고    scopus 로고
    • Protein oxidative damage
    • Shacter E., Protein oxidative damage. Methods in Enzymology 2000 319 428 436 2-s2.0-0033938817 (Pubitemid 30448062)
    • (2000) Methods in Enzymology , vol.319 , pp. 428-436
    • Shacter, E.1
  • 49
    • 0034714355 scopus 로고    scopus 로고
    • Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria-dependent caspase activation
    • 2-s2.0-0034714355 10.1074/jbc.M003412200
    • Hatai T., Matsuzawa A., Inoshita S., Mochida Y., Kuroda T., Sakamaki K., Kuida K., Yonehara S., Ichijo H., Takeda K., Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria- dependent caspase activation. The Journal of Biological Chemistry 2000 275 34 26576 26581 2-s2.0-0034714355 10.1074/jbc.M003412200
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.34 , pp. 26576-26581
    • Hatai, T.1    Matsuzawa, A.2    Inoshita, S.3    Mochida, Y.4    Kuroda, T.5    Sakamaki, K.6    Kuida, K.7    Yonehara, S.8    Ichijo, H.9    Takeda, K.10
  • 50
    • 14444281569 scopus 로고    scopus 로고
    • Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways
    • DOI 10.1126/science.275.5296.90
    • Ichijo H., Nishida E., Irie K., Ten Dijke P., Saitoh M., Moriguchi T., Takagi M., Matsumoto K., Miyazono K., Gotoh Y., Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 1997 275 5296 90 94 2-s2.0-14444281569 10.1126/science.275.5296.90 (Pubitemid 27020316)
    • (1997) Science , vol.275 , Issue.5296 , pp. 90-94
    • Ichijo, H.1    Nishida, E.2    Irie, K.3    Ten Dijke, P.4    Saitoh, M.5    Moriguchi, T.6    Takagi, M.7    Matsumoto, K.8    Miyazono, K.9    Gotoh, Y.10
  • 51
    • 54249119561 scopus 로고    scopus 로고
    • JNK signaling in apoptosis
    • 2-s2.0-54249119561 10.1038/onc.2008.301
    • Dhanasekaran D. N., Reddy E. P., JNK signaling in apoptosis. Oncogene 2008 27 48 6245 6251 2-s2.0-54249119561 10.1038/onc.2008.301
    • (2008) Oncogene , vol.27 , Issue.48 , pp. 6245-6251
    • Dhanasekaran, D.N.1    Reddy, E.P.2
  • 52
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three akts
    • 2-s2.0-0032752063 10.1101/gad.13.22.2905
    • Datta S. R., Brunet A., Greenberg M. E., Cellular survival: a play in three akts. Genes and Development 1999 13 22 2905 2927 2-s2.0-0032752063 10.1101/gad.13.22.2905
    • (1999) Genes and Development , vol.13 , Issue.22 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 53
    • 79960716001 scopus 로고    scopus 로고
    • Akt signalling in health and disease
    • 2-s2.0-79960716001 10.1016/j.cellsig.2011.05.004
    • Hers I., Vincent E. E., Tavaré J. M., Akt signalling in health and disease. Cellular Signalling 2011 23 10 1515 1527 2-s2.0-79960716001 10.1016/j.cellsig.2011.05.004
    • (2011) Cellular Signalling , vol.23 , Issue.10 , pp. 1515-1527
    • Hers, I.1    Vincent, E.E.2    Tavaré, J.M.3
  • 54
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell- intrinsic death machinery
    • DOI 10.1016/S0092-8674(00)80405-5
    • Datta S. R., Dudek H., Xu T., Masters S., Haian F., Gotoh Y., Greenberg M. E., Akt phosphorylation of BAD couples survival signals to the cell- intrinsic death machinery. Cell 1997 91 2 231 241 2-s2.0-0030702123 10.1016/S0092-8674(00)80405-5 (Pubitemid 27456390)
    • (1997) Cell , vol.91 , Issue.2 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Xu, T.3    Masters, S.4    Haian, F.5    Gotoh, Y.6    Greenberg, M.E.7
  • 56
    • 0035369623 scopus 로고    scopus 로고
    • Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway
    • DOI 10.1016/S0959-4388(00)00211-7
    • Brunet A., Datta S. R., Greenberg M. E., Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway. Current Opinion in Neurobiology 2001 11 3 297 305 2-s2.0-0035369623 10.1016/S0959-4388(00)00211-7 (Pubitemid 32524094)
    • (2001) Current Opinion in Neurobiology , vol.11 , Issue.3 , pp. 297-305
    • Brunet, A.1    Datta, S.R.2    Greenberg, M.E.3
  • 57
    • 84859624232 scopus 로고    scopus 로고
    • The cytoprotective effect of butin against oxidative stress is mediated by the up-regulation of manganese superoxide dismutase expression through a PI3K/Akt/Nrf2-dependent pathway
    • 2-s2.0-84859624232 10.1002/jcb.24068
    • Zhang R., Chae S., Lee J. H., Hyun J. W., The cytoprotective effect of butin against oxidative stress is mediated by the up-regulation of manganese superoxide dismutase expression through a PI3K/Akt/Nrf2-dependent pathway. Journal of Cellular Biochemistry 2012 113 6 1987 1997 2-s2.0-84859624232 10.1002/jcb.24068
    • (2012) Journal of Cellular Biochemistry , vol.113 , Issue.6 , pp. 1987-1997
    • Zhang, R.1    Chae, S.2    Lee, J.H.3    Hyun, J.W.4
  • 58
    • 0036279441 scopus 로고    scopus 로고
    • Drug-induced cutaneous photosensitivity: Incidence, mechanism, prevention and management
    • Moore D. E., Drug-induced cutaneous photosensitivity: incidence, mechanism, prevention and management. Drug Safety 2002 25 5 345 372 2-s2.0-0036279441 (Pubitemid 34634272)
    • (2002) Drug Safety , vol.25 , Issue.5 , pp. 345-372
    • Moore, D.E.1
  • 59
    • 0033006172 scopus 로고    scopus 로고
    • A critical evaluation of the mechanisms of action proposed for the antitumor effects of the anthracycline antibiotics adriamycin and daunorubicin
    • DOI 10.1016/S0006-2952(98)00307-4, PII S0006295298003074
    • Gewirtz D. A., A critical evaluation of the mechanisms of action proposed for the antitumor effects of the anthracycline antibiotics adriamycin and daunorubicin. Biochemical Pharmacology 1999 57 7 727 741 2-s2.0-0033006172 10.1016/S0006-2952(98)00307-4 (Pubitemid 29094544)
    • (1999) Biochemical Pharmacology , vol.57 , Issue.7 , pp. 727-741
    • Gewirtz, D.A.1
  • 60
    • 0033628701 scopus 로고    scopus 로고
    • Topoisomerase II as a target for anticancer drugs: When enzymes stop being nice
    • 2-s2.0-0033628701
    • Fortune J. M., Osheroff N., Topoisomerase II as a target for anticancer drugs: when enzymes stop being nice. Progress in Nucleic Acid Research and Molecular Biology 2000 64 221 253 2-s2.0-0033628701
    • (2000) Progress in Nucleic Acid Research and Molecular Biology , vol.64 , pp. 221-253
    • Fortune, J.M.1    Osheroff, N.2
  • 61
    • 0025850827 scopus 로고
    • Cardiac toxicity 4 to 20 years after completing anthracycline therapy
    • 2-s2.0-0025850827 10.1001/jama.266.12.1672
    • Steinherz L. J., Steinherz P. G., Tan C. T. C., Heller G., Murphy M. L., Cardiac toxicity 4 to 20 years after completing anthracycline therapy. JAMA 1991 266 12 1672 1677 2-s2.0-0025850827 10.1001/jama.266.12.1672
    • (1991) JAMA , vol.266 , Issue.12 , pp. 1672-1677
    • Steinherz, L.J.1    Steinherz, P.G.2    Tan, C.T.C.3    Heller, G.4    Murphy, M.L.5
  • 62
    • 66949171305 scopus 로고    scopus 로고
    • Anthracycline-induced cardiotoxicity: Overview of studies examining the roles of oxidative stress and free cellular iron
    • 2-s2.0-66949171305
    • Šimůnek T., Štěrba M., Popelová O., Adamcová M., Hrdina R., Gerši V., Anthracycline-induced cardiotoxicity: overview of studies examining the roles of oxidative stress and free cellular iron. Pharmacological Reports 2009 61 1 154 171 2-s2.0-66949171305
    • (2009) Pharmacological Reports , vol.61 , Issue.1 , pp. 154-171
    • Šimůnek, T.1    Štěrba, M.2    Popelová, O.3    Adamcová, M.4    Hrdina, R.5    Gerši, V.6
  • 63
    • 34548301536 scopus 로고    scopus 로고
    • An introduction to the metabolic determinants of anthracycline cardiotoxicity
    • DOI 10.1007/s12012-007-0011-7
    • Menna P., Recalcati S., Cairo G., Minotti G., An introduction to the metabolic determinants of anthracycline cardiotoxicity. Cardiovascular Toxicology 2007 7 2 80 85 2-s2.0-34548301536 10.1007/s12012-007-0011-7 (Pubitemid 47339872)
    • (2007) Cardiovascular Toxicology , vol.7 , Issue.2 , pp. 80-85
    • Menna, P.1    Recalcati, S.2    Cairo, G.3    Minotti, G.4
  • 64
    • 0022967083 scopus 로고
    • Redox cycling of anthracyclines by cardiac mitochondria. I. Anthracycline radical formation by NADH dehydrogenase
    • Davies K. J. A., Doroshow J. H., Redox cycling of anthracyclines by cardiac mitochondria. I. Anthracycline radical formation by NADH dehydrogenase. The Journal of Biological Chemistry 1986 261 7 3060 3067 2-s2.0-0022967083 (Pubitemid 17204909)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.7 , pp. 3060-3067
    • Davies, K.J.A.1    Doroshow, J.H.2
  • 65
    • 0023028913 scopus 로고
    • Redox cycling of anthracyclines by cardiac mitochondria. II. Formation of superoxide anion, hydrogen peroxide, and hydroxyl radical
    • Doroshow J. H., Davies K. J. A., Redox cycling of anthracyclines by cardiac mitochondria. II. Formation of superoxide anion, hydrogen peroxide, and hydroxyl radical. The Journal of Biological Chemistry 1986 261 7 3068 3074 2-s2.0-0023028913 (Pubitemid 17204910)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.7 , pp. 3068-3074
    • Doroshow, J.H.1    Davies, K.J.A.2
  • 66
    • 70349734337 scopus 로고    scopus 로고
    • Chronic doxorubicin cardiotoxicity is mediated by oxidative DNA damage-ATM-p53-apoptosis pathway and attenuated by pitavastatin through the inhibition of Rac1 activity
    • 2-s2.0-70349734337 10.1016/j.yjmcc.2009.07.024
    • Yoshida M., Shiojima I., Ikeda H., Komuro I., Chronic doxorubicin cardiotoxicity is mediated by oxidative DNA damage-ATM-p53-apoptosis pathway and attenuated by pitavastatin through the inhibition of Rac1 activity. Journal of Molecular and Cellular Cardiology 2009 47 5 698 705 2-s2.0-70349734337 10.1016/j.yjmcc.2009.07.024
    • (2009) Journal of Molecular and Cellular Cardiology , vol.47 , Issue.5 , pp. 698-705
    • Yoshida, M.1    Shiojima, I.2    Ikeda, H.3    Komuro, I.4
  • 67
    • 0019221914 scopus 로고
    • Evidence of a specific complex between adriamycin and negatively-charged phospholipids
    • Goormaghtigh E., Chatelain P., Caspers J., Ruysschaert J. M., Evidence of a specific complex between adriamycin and negatively-charged phospholipids. Biochimica et Biophysica Acta 1980 597 1 1 14 2-s2.0-0019221914 (Pubitemid 10120606)
    • (1980) Biochimica et Biophysica Acta , vol.597 , Issue.1 , pp. 1-14
    • Goormaghtigh, E.1    Chatelain, P.2    Caspers, J.3    Ruysschaert, J.M.4
  • 68
    • 80052226370 scopus 로고    scopus 로고
    • Drug-induced cardiac mitochondrial toxicity and protection: From doxorubicin to carvedilol
    • 2-s2.0-80052226370 10.2174/138161211796904812
    • Pereira G. C., Silva A. M., Diogo C. V., Carvalho F. S., Monteiro P., Oliveira P. J., Drug-induced cardiac mitochondrial toxicity and protection: from doxorubicin to carvedilol. Current Pharmaceutical Design 2011 17 20 2113 2129 2-s2.0-80052226370 10.2174/138161211796904812
    • (2011) Current Pharmaceutical Design , vol.17 , Issue.20 , pp. 2113-2129
    • Pereira, G.C.1    Silva, A.M.2    Diogo, C.V.3    Carvalho, F.S.4    Monteiro, P.5    Oliveira, P.J.6
  • 69
    • 34250375254 scopus 로고    scopus 로고
    • Mitochondrial and nuclear p53 localization in cardiomyocytes: Redox modulation by doxorubicin (Adriamycin)?
    • DOI 10.1089/ars.2007.1632
    • Nithipongvanitch R., Ittarat W., Cole M. P., Tangpong J., Clair D. K. S., Oberley T. D., Mitochondrial and nuclear p53 localization in cardiomyocytes: redox modulation by doxorubicin (Adriamycin)? Antioxidants and Redox Signaling 2007 9 7 1001 1008 2-s2.0-34250375254 10.1089/ars.2007.1632 (Pubitemid 46919601)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.7 , pp. 1001-1008
    • Nithipongvanitch, R.1    Ittarat, W.2    Cole, M.P.3    Tangpong, J.4    St. Clair, D.K.5    Oberley, T.D.6
  • 70
    • 34548299678 scopus 로고    scopus 로고
    • Adriamycin-induced interference with cardiac mitochondrial calcium homeostasis
    • DOI 10.1007/s12012-007-0008-2
    • Wallace K. B., Adriamycin-induced interference with cardiac mitochondrial calcium homeostasis. Cardiovascular Toxicology 2007 7 2 101 107 2-s2.0-34548299678 10.1007/s12012-007-0008-2 (Pubitemid 47339855)
    • (2007) Cardiovascular Toxicology , vol.7 , Issue.2 , pp. 101-107
    • Wallace, K.B.1
  • 71
    • 70450260555 scopus 로고    scopus 로고
    • Cardiomyocyte death in doxorubicin-induced cardiotoxicity
    • 2-s2.0-70450260555 10.1007/s00005-009-0051-8
    • Zhang Y. W., Shi J., Li Y. J., Wei L., Cardiomyocyte death in doxorubicin-induced cardiotoxicity. Archivum Immunologiae et Therapiae Experimentalis 2009 57 6 435 445 2-s2.0-70450260555 10.1007/s00005-009-0051-8
    • (2009) Archivum Immunologiae et Therapiae Experimentalis , vol.57 , Issue.6 , pp. 435-445
    • Zhang, Y.W.1    Shi, J.2    Li, Y.J.3    Wei, L.4
  • 72
    • 0037102148 scopus 로고    scopus 로고
    • Doxorubicin treatment in vivo causes cytochrome c release and cardiomyocyte apoptosis, as well as increased mitochondrial efficiency, superoxide dismutase activity, and Bcl-2:Bax ratio
    • 2-s2.0-0037102148
    • Childs A. C., Phaneuf S. L., Dirks A. J., Phillips T., Leeuwenburgh C., Doxorubicin treatment in vivo causes cytochrome c release and cardiomyocyte apoptosis, as well as increased mitochondrial efficiency, superoxide dismutase activity, and Bcl-2:Bax ratio. Cancer Research 2002 62 16 4592 4598 2-s2.0-0037102148
    • (2002) Cancer Research , vol.62 , Issue.16 , pp. 4592-4598
    • Childs, A.C.1    Phaneuf, S.L.2    Dirks, A.J.3    Phillips, T.4    Leeuwenburgh, C.5
  • 73
    • 84856049297 scopus 로고    scopus 로고
    • Heart to heart with trastuzumab: A review on cardiac toxicity
    • 2-s2.0-84856049297 10.1007/s11523-011-0203-8
    • Di Cosimo S., Heart to heart with trastuzumab: a review on cardiac toxicity. Targeted Oncology 2011 6 4 189 195 2-s2.0-84856049297 10.1007/s11523-011-0203-8
    • (2011) Targeted Oncology , vol.6 , Issue.4 , pp. 189-195
    • Di Cosimo, S.1
  • 75
    • 67349248085 scopus 로고    scopus 로고
    • Cardiac toxicity with anti-HER-2 therapies-what have we learned so far?
    • 2-s2.0-67349248085 10.1007/s11523-009-0112-2
    • De Azambuja E., Bedard P. L., Suter T., Piccart-Gebhart M., Cardiac toxicity with anti-HER-2 therapies-what have we learned so far? Targeted Oncology 2009 4 2 77 88 2-s2.0-67349248085 10.1007/s11523-009-0112-2
    • (2009) Targeted Oncology , vol.4 , Issue.2 , pp. 77-88
    • De Azambuja, E.1    Bedard, P.L.2    Suter, T.3    Piccart-Gebhart, M.4
  • 76
    • 0033551890 scopus 로고    scopus 로고
    • Protective effects of carvedilol against doxorubicin-induced cardiomyopathy in rats
    • DOI 10.1016/S0024-3205(99)00362-8, PII S0024320599003628
    • Matsui H., Morishima I., Numaguchi Y., Toki Y., Okumura K., Hayakawa T., Protective effects of carvedilol against doxorubicin-induced cardiomyopathy in rats. Life Sciences 1999 65 12 1265 1274 2-s2.0-0033551890 10.1016/S0024- 3205(99)00362-8 (Pubitemid 29425963)
    • (1999) Life Sciences , vol.65 , Issue.12 , pp. 1265-1274
    • Matsui, H.1    Morishima, I.2    Numaguchi, Y.3    Toki, Y.4    Okumura, K.5    Hayakawa, T.6
  • 77
    • 0019414005 scopus 로고
    • Prevention of doxorubicin cardiac toxicity in the mouse by N-acetylcysteine
    • Doroshow J. H., Locker G. Y., Ifrim I., Myers C. E., Prevention of doxorubicin cardiac toxicity in the mouse by N-acetylcysteine. The Journal of Clinical Investigation 1981 68 4 1053 1064 2-s2.0-0019414005 (Pubitemid 11023534)
    • (1981) Journal of Clinical Investigation , vol.68 , Issue.4 , pp. 1053-1064
    • Doroshow, J.H.1    Locker, G.Y.2    Ifrim, I.3    Myers, C.E.4
  • 78
    • 84855734341 scopus 로고    scopus 로고
    • Propofol ameliorates doxorubicin-induced oxidative stress and cellular apoptosis in rat cardiomyocytes
    • 2-s2.0-84855734341 10.1016/j.taap.2011.10.001
    • Lai H. C., Yeh Y. C., Wang L. C., Ting C. T., Lee W. L., Lee H. W., Wang K. Y., Wu A., Su C. S., Liu T. J., Propofol ameliorates doxorubicin-induced oxidative stress and cellular apoptosis in rat cardiomyocytes. Toxicology and Applied Pharmacology 2011 257 3 437 448 2-s2.0-84855734341 10.1016/j.taap.2011. 10.001
    • (2011) Toxicology and Applied Pharmacology , vol.257 , Issue.3 , pp. 437-448
    • Lai, H.C.1    Yeh, Y.C.2    Wang, L.C.3    Ting, C.T.4    Lee, W.L.5    Lee, H.W.6    Wang, K.Y.7    Wu, A.8    Su, C.S.9    Liu, T.J.10
  • 80
    • 0034523687 scopus 로고    scopus 로고
    • The cardioprotective effect of the iron chelator dexrazoxane (ICRF-187) on anthracycline-mediated cardiotoxicity
    • DOI 10.1179/135100000101535898
    • Kwok J. C., Richardson D. R., The cardioprotective effect of the iron chelator dexrazoxane (ICRF-187) on anthracycline-mediated cardiotoxicity. Redox Report 2000 5 6 317 324 2-s2.0-0034523687 10.1179/135100000101535898 (Pubitemid 32040825)
    • (2000) Redox Report , vol.5 , Issue.6 , pp. 317-324
    • Kwok, J.C.1    Richardson, D.R.2
  • 81
    • 18744377282 scopus 로고    scopus 로고
    • Dexrazoxane: A review of its use for cardioprotection during anthracycline chemotherapy
    • DOI 10.2165/00003495-200565070-00008
    • Cvetković R. S., Scott L. J., Dexrazoxane: a review of its use for cardioprotection during anthracycline chemotherapy. Drugs 2005 65 7 1005 1024 2-s2.0-18744377282 10.2165/00003495-200565070-00008 (Pubitemid 40667518)
    • (2005) Drugs , vol.65 , Issue.7 , pp. 1005-1024
    • Cvetkovic, R.S.1    Scott, L.J.2
  • 82
    • 73549103358 scopus 로고    scopus 로고
    • The development of antiretroviral therapy and its impact on the HIV-1/AIDS pandemic
    • 2-s2.0-73549103358 10.1016/j.antiviral.2009.10.002
    • Broder S., The development of antiretroviral therapy and its impact on the HIV-1/AIDS pandemic. Antiviral Research 2010 85 1 1 18 2-s2.0-73549103358 10.1016/j.antiviral.2009.10.002
    • (2010) Antiviral Research , vol.85 , Issue.1 , pp. 1-18
    • Broder, S.1
  • 84
    • 0031003145 scopus 로고    scopus 로고
    • Cellular and mitochondrial toxicity of zidovudine (AZT), didanosine (ddI) and zalcitabine (ddC) on cultured human muscle cells
    • DOI 10.1016/S0022-510X(97)05376-8, PII S0022510X97053768
    • Benbrik E., Chariot P., Bonavaud S., Ammi-Saïd M., Frisdal E., Rey C., Gherardi R., Barlovatz-Meimon G., Cellular and mitochondrial toxicity of zidovudine (AZT), didanosine (ddI) and zalcitabine (ddC) on cultured human muscle cells. Journal of the Neurological Sciences 1997 149 1 19 25 2-s2.0-0031003145 10.1016/S0022-510X(97)05376-8 (Pubitemid 27196376)
    • (1997) Journal of the Neurological Sciences , vol.149 , Issue.1 , pp. 19-25
    • Benbrik, E.1    Chariot, P.2    Bonavaud, S.3    Ammi-Said, M.4    Frisdal, E.5    Rey, C.6    Gherardi, R.7    Barlovatz-Meimon, G.8
  • 85
    • 75749123458 scopus 로고    scopus 로고
    • Pro-oxidant properties of AZT and other thymidine analogues in macrophages: Implication of the azido moiety in oxidative stress
    • 2-s2.0-75749123458 10.1002/cmdc.200900464
    • Amatore C., Arbault S., Jaouen G., Koh A. C. W., Leong W. K., Top S., Valleron M. A., Woo C. H., Pro-oxidant properties of AZT and other thymidine analogues in macrophages: implication of the azido moiety in oxidative stress. ChemMedChem 2010 5 2 296 301 2-s2.0-75749123458 10.1002/cmdc.200900464
    • (2010) ChemMedChem , vol.5 , Issue.2 , pp. 296-301
    • Amatore, C.1    Arbault, S.2    Jaouen, G.3    Koh, A.C.W.4    Leong, W.K.5    Top, S.6    Valleron, M.A.7    Woo, C.H.8
  • 88
    • 33847772869 scopus 로고    scopus 로고
    • Renal proximal tubule segment-specific nephrotoxicity: An overview on biomarkers and histopathology
    • DOI 10.1080/01926230601187430, PII 772662810
    • Cristofori P., Zanetti E., Fregona D., Piaia A., Trevisan A., Renal proximal tubule segment-specific nephrotoxicity: an overview on biomarkers and histopathology. Toxicologic Pathology 2007 35 2 270 275 2-s2.0-33847772869 10.1080/01926230601187430 (Pubitemid 46393079)
    • (2007) Toxicologic Pathology , vol.35 , Issue.2 , pp. 270-275
    • Cristofori, P.1    Zanetti, E.2    Fregona, D.3    Piaia, A.4    Trevisan, A.5
  • 90
    • 70349440952 scopus 로고    scopus 로고
    • Contribution of organic cation transporter 2 (OCT2) to cisplatin-induced nephrotoxicity
    • 2-s2.0-70349440952 10.1038/clpt.2009.139
    • Filipski K. K., Mathijssen R. H., Mikkelsen T. S., Schinkel A. H., Sparreboom A., Contribution of organic cation transporter 2 (OCT2) to cisplatin-induced nephrotoxicity. Clinical Pharmacology and Therapeutics 2009 86 4 396 402 2-s2.0-70349440952 10.1038/clpt.2009.139
    • (2009) Clinical Pharmacology and Therapeutics , vol.86 , Issue.4 , pp. 396-402
    • Filipski, K.K.1    Mathijssen, R.H.2    Mikkelsen, T.S.3    Schinkel, A.H.4    Sparreboom, A.5
  • 91
    • 0027965261 scopus 로고
    • Cisplatin generates superoxide anion by interaction with DNA in a cell-free system
    • DOI 10.1006/bbrc.1994.2306
    • Masuda H., Tanaka T., Takahama U., Cisplatin generates superoxide anion by interaction with DNA in a cell-free system. Biochemical and Biophysical Research Communications 1994 203 2 1175 1180 2-s2.0-0027965261 10.1006/bbrc.1994.2306 (Pubitemid 24304953)
    • (1994) Biochemical and Biophysical Research Communications , vol.203 , Issue.2 , pp. 1175-1180
    • Masuda, H.1    Tanaka, T.2    Takahama, U.3
  • 93
    • 67349112401 scopus 로고    scopus 로고
    • Role of oxidative and nitrosative stress in cisplatin-induced nephrotoxicity
    • 2-s2.0-67349112401 10.1016/j.etp.2008.09.003
    • Chirino Y. I., Pedraza-Chaverri J., Role of oxidative and nitrosative stress in cisplatin-induced nephrotoxicity. Experimental and Toxicologic Pathology 2009 61 3 223 242 2-s2.0-67349112401 10.1016/j.etp.2008.09.003
    • (2009) Experimental and Toxicologic Pathology , vol.61 , Issue.3 , pp. 223-242
    • Chirino, Y.I.1    Pedraza-Chaverri, J.2
  • 94
    • 34347352096 scopus 로고    scopus 로고
    • Cisplatin-induced nephrotoxicity is associated with oxidative stress, redox state unbalance, impairment of energetic metabolism and apoptosis in rat kidney mitochondria
    • DOI 10.1007/s00204-006-0173-2
    • Santos N. A. G., Catão C. S., Martins N. M., Curti C., Bianchi M. L. P., Santos A. C., Cisplatin-induced nephrotoxicity is associated with oxidative stress, redox state unbalance, impairment of energetic metabolism and apoptosis in rat kidney mitochondria. Archives of Toxicology 2007 81 7 495 504 2-s2.0-34347352096 10.1007/s00204-006-0173-2 (Pubitemid 47012464)
    • (2007) Archives of Toxicology , vol.81 , Issue.7 , pp. 495-504
    • Santos, N.A.G.1    Catao, C.S.2    Martins, N.M.3    Curti, C.4    Bianchi, M.L.P.5    Santos, A.C.6
  • 95
    • 20444446307 scopus 로고    scopus 로고
    • The cochlear targets of cisplatin: An electrophysiological and morphological time-sequence study
    • DOI 10.1016/j.heares.2005.03.023, PII S0378595505001115
    • Van Ruijven M. W. M., De Groot J. C. M. J., Klis S. F. L., Smoorenburg G. F., The cochlear targets of cisplatin: an electrophysiological and morphological time-sequence study. Hearing Research 2005 205 1-2 241 248 2-s2.0-20444446307 10.1016/j.heares.2005.03.023 (Pubitemid 40813286)
    • (2005) Hearing Research , vol.205 , Issue.1-2 , pp. 241-248
    • Van Ruijven, M.W.M.1    De Groot, J.C.M.J.2    Klis, S.F.L.3    Smoorenburg, G.F.4
  • 96
    • 0031760577 scopus 로고    scopus 로고
    • A semiquantitative analysis of the effects of cisplatin on the rat stria vascularis
    • DOI 10.1016/S0378-5955(98)00116-6, PII S0378595598001166
    • Meech R. P., Campbell K. C. M., Hughes L. P., Rybak L. P., A semiquantitative analysis of the effects of cisplatin on the rat stria vascularis. Hearing Research 1998 124 1-2 44 59 2-s2.0-0031760577 10.1016/S0378-5955(98)00116-6 (Pubitemid 28483064)
    • (1998) Hearing Research , vol.124 , Issue.1-2 , pp. 44-59
    • Meech, R.P.1    Campbell, K.C.M.2    Hughes, L.P.3    Rybak, L.P.4
  • 97
    • 77949699981 scopus 로고    scopus 로고
    • Roles of NADPH oxidases in cisplatin-induced reactive oxygen species generation and ototoxicity
    • 2-s2.0-77949699981 10.1523/JNEUROSCI.6054-09.2010
    • Kim H. J., Lee J. H., Kim S. J., Oh G. S., Moon H. D., Kwon K. B., Park C., Park B. H., Lee H. K., Chung S. Y., Park R., So H. S., Roles of NADPH oxidases in cisplatin-induced reactive oxygen species generation and ototoxicity. Journal of Neuroscience 2010 30 11 3933 3946 2-s2.0-77949699981 10.1523/JNEUROSCI.6054-09.2010
    • (2010) Journal of Neuroscience , vol.30 , Issue.11 , pp. 3933-3946
    • Kim, H.J.1    Lee, J.H.2    Kim, S.J.3    Oh, G.S.4    Moon, H.D.5    Kwon, K.B.6    Park, C.7    Park, B.H.8    Lee, H.K.9    Chung, S.Y.10    Park, R.11    So, H.S.12
  • 98
    • 0029012886 scopus 로고
    • Mechanism of cisplatin ototoxicity: Antioxidant system
    • 2-s2.0-0029012886
    • Ravi R., Somani S. M., Rybak L. P., Mechanism of cisplatin ototoxicity: antioxidant system. Pharmacology and Toxicology 1995 76 6 386 394 2-s2.0-0029012886
    • (1995) Pharmacology and Toxicology , vol.76 , Issue.6 , pp. 386-394
    • Ravi, R.1    Somani, S.M.2    Rybak, L.P.3
  • 99
    • 33746007179 scopus 로고    scopus 로고
    • Future opportunities in preventing cisplatin induced ototoxicity
    • DOI 10.1016/j.ctrv.2006.04.011, PII S0305737206000971
    • van den Berg J. H., Beijnen J. H., Balm A. J. M., Schellens J. H. M., Future opportunities in preventing cisplatin induced ototoxicity. Cancer Treatment Reviews 2006 32 5 390 397 2-s2.0-33746007179 10.1016/j.ctrv.2006.04. 011 (Pubitemid 44063878)
    • (2006) Cancer Treatment Reviews , vol.32 , Issue.5 , pp. 390-397
    • Van Den Berg, J.H.1    Beijnen, J.H.2    Balm, A.J.M.3    Schellens, J.H.M.4
  • 100
    • 0032775070 scopus 로고    scopus 로고
    • Randomized study of a short course of weekly cisplatin with or without amifostine in advanced head and neck cancer
    • DOI 10.1023/A:1008353505916
    • Planting A. S. T., Catimel G., De Mulder P. H. M., De Graeff A., Höppener F., Verweij J., Oster W., Vermorken J. B., Randomized study of a short course of weekly cisplatin with or without amifostine in advanced head and neck cancer. Annals of Oncology 1999 10 6 693 700 2-s2.0-0032775070 10.1023/A:1008353505916 (Pubitemid 29342375)
    • (1999) Annals of Oncology , vol.10 , Issue.6 , pp. 693-700
    • Planting, A.S.T.1    Catimel, G.2    De Mulder, P.H.M.3    De Graeff, A.4    Hoppener, F.5    Verweij, J.6    Oster, W.7    Vermorken, J.B.8
  • 101
    • 4644262696 scopus 로고    scopus 로고
    • High-dose cisplatin with amifostine: Ototoxicity and pharmacokinetics
    • DOI 10.1097/00005537-200409000-00030
    • Ekborn A., Hansson J., Ehrsson H., Eksborg S., Wallin I., Wagenius G., Laurell G., High-dose cisplatin with amifostine: ototoxicity and pharmacokinetics. Laryngoscope 2004 114 9 1660 1667 2-s2.0-4644262696 10.1097/00005537-200409000-00030 (Pubitemid 39278890)
    • (2004) Laryngoscope , vol.114 , Issue.I9 , pp. 1660-1667
    • Ekborn, A.1    Hansson, J.2    Ehrsson, H.3    Eksborg, S.4    Wallin, I.5    Wagenius, G.6    Laurell, G.7
  • 102
    • 46549087839 scopus 로고    scopus 로고
    • Reactive oxygen species assay-based risk assessment of drug-induced phototoxicity: Classification criteria and application to drug candidates
    • 2-s2.0-46549087839 10.1016/j.jpba.2008.03.026
    • Onoue S., Kawamura K., Igarashi N., Zhou Y., Fujikawa M., Yamada H., Tsuda Y., Seto Y., Yamada S., Reactive oxygen species assay-based risk assessment of drug-induced phototoxicity: classification criteria and application to drug candidates. Journal of Pharmaceutical and Biomedical Analysis 2008 47 4-5 967 972 2-s2.0-46549087839 10.1016/j.jpba.2008.03.026
    • (2008) Journal of Pharmaceutical and Biomedical Analysis , vol.47 , Issue.4-5 , pp. 967-972
    • Onoue, S.1    Kawamura, K.2    Igarashi, N.3    Zhou, Y.4    Fujikawa, M.5    Yamada, H.6    Tsuda, Y.7    Seto, Y.8    Yamada, S.9
  • 104
    • 33947590154 scopus 로고    scopus 로고
    • Cisplatin-induced long-term hearing impairment is associated with specific glutathione S-transferase genotypes in testicular cancer survivors
    • DOI 10.1200/JCO.2006.08.9599
    • Oldenburg J., Kraggerud S. M., Cvancarova M., Lothe R. A., Fossa S. D., Cisplatin-induced long-term hearing impairment is associated with specific glutathione S-transferase genotypes in testicular cancer survivors. Journal of Clinical Oncology 2007 25 6 708 714 2-s2.0-33947590154 10.1200/JCO.2006.08.9599 (Pubitemid 350002927)
    • (2007) Journal of Clinical Oncology , vol.25 , Issue.6 , pp. 708-714
    • Oldenburg, J.1    Kraggerud, S.M.2    Cvancarova, M.3    Lothe, R.A.4    Fossa, S.D.5
  • 105
    • 79960807006 scopus 로고    scopus 로고
    • Pharmacogenomics of cisplatin-induced ototoxicity
    • 2-s2.0-79960807006 10.2217/pgs.11.48
    • Mukherjea D., Rybak L. P., Pharmacogenomics of cisplatin-induced ototoxicity. Pharmacogenomics 2011 12 7 1039 1050 2-s2.0-79960807006 10.2217/pgs.11.48
    • (2011) Pharmacogenomics , vol.12 , Issue.7 , pp. 1039-1050
    • Mukherjea, D.1    Rybak, L.P.2
  • 106
    • 77949539805 scopus 로고    scopus 로고
    • Influence of pharmacogenetics on response and toxicity in breast cancer patients treated with doxorubicin and cyclophosphamide
    • 2-s2.0-77949539805 10.1038/sj.bjc.6605587
    • Bray J., Sludden J., Griffin M. J., Cole M., Verrill M., Jamieson D., Boddy A. V., Influence of pharmacogenetics on response and toxicity in breast cancer patients treated with doxorubicin and cyclophosphamide. British Journal of Cancer 2010 102 6 1003 1009 2-s2.0-77949539805 10.1038/sj.bjc.6605587
    • (2010) British Journal of Cancer , vol.102 , Issue.6 , pp. 1003-1009
    • Bray, J.1    Sludden, J.2    Griffin, M.J.3    Cole, M.4    Verrill, M.5    Jamieson, D.6    Boddy, A.V.7
  • 108
    • 80052980622 scopus 로고    scopus 로고
    • Pharmacogenetics of genes across the doxorubicin pathway
    • 2-s2.0-80052980622 10.1517/17425255.2011.610180
    • Jamieson D., Boddy A. V., Pharmacogenetics of genes across the doxorubicin pathway. Expert Opinion on Drug Metabolism and Toxicology 2011 7 10 1201 1210 2-s2.0-80052980622 10.1517/17425255.2011.610180
    • (2011) Expert Opinion on Drug Metabolism and Toxicology , vol.7 , Issue.10 , pp. 1201-1210
    • Jamieson, D.1    Boddy, A.V.2
  • 110
    • 28644448262 scopus 로고    scopus 로고
    • Savior and slayer: The two faces of p53
    • DOI 10.1038/nm1205-1278
    • Bensaad K., Vousden K. H., Savior and slayer: the two faces of p53. Nature Medicine 2005 11 12 1278 1279 2-s2.0-28644448262 10.1038/nm1205-1278 (Pubitemid 41752901)
    • (2005) Nature Medicine , vol.11 , Issue.12 , pp. 1278-1279
    • Bensaad, K.1    Vousden, K.H.2
  • 111
    • 77955906955 scopus 로고    scopus 로고
    • Mechanisms of anthracycline cardiac injury: Can we identify strategies for cardioprotection?
    • 2-s2.0-77955906955 10.1016/j.pcad.2010.06.007
    • Sawyer D. B., Peng X., Chen B., Pentassuglia L., Lim C. C., Mechanisms of anthracycline cardiac injury: can we identify strategies for cardioprotection? Progress in Cardiovascular Diseases 2010 53 2 105 113 2-s2.0-77955906955 10.1016/j.pcad.2010.06.007
    • (2010) Progress in Cardiovascular Diseases , vol.53 , Issue.2 , pp. 105-113
    • Sawyer, D.B.1    Peng, X.2    Chen, B.3    Pentassuglia, L.4    Lim, C.C.5
  • 112
    • 77249101995 scopus 로고    scopus 로고
    • Anticancer drugs and cardiotoxicity: Insights and perspectives in the era of targeted therapy
    • 2-s2.0-77249101995 10.1016/j.pharmthera.2009.10.002
    • Raschi E., Vasina V., Ursino M. G., Boriani G., Martoni A., de Ponti F., Anticancer drugs and cardiotoxicity: insights and perspectives in the era of targeted therapy. Pharmacology and Therapeutics 2010 125 2 196 218 2-s2.0-77249101995 10.1016/j.pharmthera.2009.10.002
    • (2010) Pharmacology and Therapeutics , vol.125 , Issue.2 , pp. 196-218
    • Raschi, E.1    Vasina, V.2    Ursino, M.G.3    Boriani, G.4    Martoni, A.5    De Ponti, F.6
  • 113
    • 67649861056 scopus 로고    scopus 로고
    • Transgenic mitochondrial superoxide dismutase and mitochondrially targeted catalase prevent antiretroviral-induced oxidative stress and cardiomyopathy
    • 2-s2.0-67649861056 10.1038/labinvest.2009.39
    • Kohler J. J., Cucoranu I., Fields E., Green E., He S., Hoying A., Russ R., Abuin A., Johnson D., Hosseini S. H., Raper C. M., Lewis W., Transgenic mitochondrial superoxide dismutase and mitochondrially targeted catalase prevent antiretroviral-induced oxidative stress and cardiomyopathy. Laboratory Investigation 2009 89 7 782 790 2-s2.0-67649861056 10.1038/labinvest.2009.39
    • (2009) Laboratory Investigation , vol.89 , Issue.7 , pp. 782-790
    • Kohler, J.J.1    Cucoranu, I.2    Fields, E.3    Green, E.4    He, S.5    Hoying, A.6    Russ, R.7    Abuin, A.8    Johnson, D.9    Hosseini, S.H.10    Raper, C.M.11    Lewis, W.12
  • 114
    • 0035879827 scopus 로고    scopus 로고
    • Diclofenac induced in vivo nephrotoxicity may involve oxidative stress-mediated massive genomic DNA fragmentation and apoptotic cell death
    • DOI 10.1016/S0891-5849(01)00560-3, PII S0891584901005603
    • Hickey E. J., Raje R. R., Reid V. E., Gross S. M., Ray S. D., Diclofenac induced in vivo nephrotoxicity may involve oxidative stress-mediated massive genomic DNA fragmentation and apoptotic cell death. Free Radical Biology and Medicine 2001 31 2 139 152 2-s2.0-0035879827 10.1016/S0891-5849(01)00560-3 (Pubitemid 32607581)
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.2 , pp. 139-152
    • Hickey, E.J.1    Raje, R.R.2    Reid, V.E.3    Gross, S.M.4    Ray, S.D.5
  • 115
    • 0142219774 scopus 로고    scopus 로고
    • Diclofenac-induced liver injury: A paradigm of idiosyncratic drug toxicity
    • DOI 10.1016/S0041-008X(03)00368-5
    • Boelsterli U. A., Diclofenac-induced liver injury: a paradigm of idiosyncratic drug toxicity. Toxicology and Applied Pharmacology 2003 192 3 307 322 2-s2.0-0142219774 10.1016/S0041-008X(03)00368-5 (Pubitemid 37311346)
    • (2003) Toxicology and Applied Pharmacology , vol.192 , Issue.3 , pp. 307-322
    • Boelsterli, U.A.1
  • 116
    • 78650604361 scopus 로고    scopus 로고
    • Liver injury caused by drugs: An update
    • 2-s2.0-78650604361 10.4414/smw.2010.13080
    • Stirnimann G., Kessebohm K., Lauterburg B., Liver injury caused by drugs: an update. Swiss Medical Weekly 2010 140 18 24 2-s2.0-78650604361 10.4414/smw.2010.13080
    • (2010) Swiss Medical Weekly , vol.140 , pp. 18-24
    • Stirnimann, G.1    Kessebohm, K.2    Lauterburg, B.3
  • 117
    • 0024350380 scopus 로고
    • Cisplatin nephrotoxicity. A review
    • DOI 10.1007/BF00694330
    • Daugaard G., Abildgaard U., Cisplatin nephrotoxicity. A review. Cancer Chemotherapy and Pharmacology 1989 25 1 1 9 2-s2.0-0024350380 10.1007/BF00694330 (Pubitemid 20000790)
    • (1989) Cancer Chemotherapy and Pharmacology , vol.25 , Issue.1 , pp. 1-9
    • Daugaard, G.1    Abildgaard, U.2


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