메뉴 건너뛰기




Volumn 88, Issue 11, 2006, Pages 1549-1559

Cadmium: cellular effects, modifications of biomolecules, modulation of DNA repair and genotoxic consequences (a review)

Author keywords

Cadmium; DNA damage; DNA repair; Oxidative stress

Indexed keywords

CADMIUM;

EID: 33751002324     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.10.001     Document Type: Article
Times cited : (839)

References (141)
  • 4
    • 0000349342 scopus 로고
    • Berrylium, cadmium, mercury and exposures in the glass manufacturing industry
    • International Agency for Research on Cancer, IARC Scientific Publications, Lyon
    • International Agency for Research on Cancer. Berrylium, cadmium, mercury and exposures in the glass manufacturing industry. International Agency for Research on Cancer Monographs on the Evaluation of Carcinogenic Risks to Humans, vol. 58 (1993), IARC Scientific Publications, Lyon 119-237
    • (1993) International Agency for Research on Cancer Monographs on the Evaluation of Carcinogenic Risks to Humans, vol. 58 , pp. 119-237
  • 6
    • 17944381040 scopus 로고    scopus 로고
    • Renal dysfunction of cadmium-exposed workers residing in a cadmium-polluted environment
    • Jin T., Kong Q., Ye T., Wu X., and Nordberg G.F. Renal dysfunction of cadmium-exposed workers residing in a cadmium-polluted environment. Biometals 17 (2004) 513-518
    • (2004) Biometals , vol.17 , pp. 513-518
    • Jin, T.1    Kong, Q.2    Ye, T.3    Wu, X.4    Nordberg, G.F.5
  • 7
    • 0031690143 scopus 로고    scopus 로고
    • Toxicokinetics and biochemistry of cadmium with special emphasis on the role of metallothioneins
    • Jin T., Lu J., and Nordberg M. Toxicokinetics and biochemistry of cadmium with special emphasis on the role of metallothioneins. Neurotoxicology 19 (1998) 529-535
    • (1998) Neurotoxicology , vol.19 , pp. 529-535
    • Jin, T.1    Lu, J.2    Nordberg, M.3
  • 8
    • 0345708255 scopus 로고    scopus 로고
    • Cadmium carcinogenesis
    • Waalkes M.P. Cadmium carcinogenesis. Mutat. Res. 533 (2003) 107-120
    • (2003) Mutat. Res. , vol.533 , pp. 107-120
    • Waalkes, M.P.1
  • 11
    • 14044254161 scopus 로고    scopus 로고
    • Cadmium-induced malignant transformation in rat liver cells: role of aberrant oncogene expression and minimal role of oxidative stress
    • Qu W., Diwan B.A., Reece J.M., Bortner C.D., Pi J., Liu J., and Waalkes M.P. Cadmium-induced malignant transformation in rat liver cells: role of aberrant oncogene expression and minimal role of oxidative stress. Int. J. Cancer 114 (2005) 346-355
    • (2005) Int. J. Cancer , vol.114 , pp. 346-355
    • Qu, W.1    Diwan, B.A.2    Reece, J.M.3    Bortner, C.D.4    Pi, J.5    Liu, J.6    Waalkes, M.P.7
  • 13
    • 0031424866 scopus 로고    scopus 로고
    • Induction and repair inhibition of oxidative DNA damage by nickel(II) and cadmium(II) in mammalian cells
    • Dally H., and Hartwig A. Induction and repair inhibition of oxidative DNA damage by nickel(II) and cadmium(II) in mammalian cells. Carcinogenesis 18 (1997) 1021-1026
    • (1997) Carcinogenesis , vol.18 , pp. 1021-1026
    • Dally, H.1    Hartwig, A.2
  • 15
    • 0038419826 scopus 로고    scopus 로고
    • Cancer, cadmium and genome integrity
    • McMurray C.T., and Tainer J.A. Cancer, cadmium and genome integrity. Nat. Genet. 34 (2003) 239-241
    • (2003) Nat. Genet. , vol.34 , pp. 239-241
    • McMurray, C.T.1    Tainer, J.A.2
  • 16
    • 0031172562 scopus 로고    scopus 로고
    • Cadmium, gene regulation, and cellular signalling in mammalian cells
    • Beyersmann D., and Hechtenberg S. Cadmium, gene regulation, and cellular signalling in mammalian cells. Toxicol. Appl. Pharmacol. 144 (1997) 247-261
    • (1997) Toxicol. Appl. Pharmacol. , vol.144 , pp. 247-261
    • Beyersmann, D.1    Hechtenberg, S.2
  • 17
    • 0142219722 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of cadmium carcinogenesis
    • Waisberg M., Joseph P., Hale B., and Beyersmann D. Molecular and cellular mechanisms of cadmium carcinogenesis. Toxicology 192 (2003) 95-117
    • (2003) Toxicology , vol.192 , pp. 95-117
    • Waisberg, M.1    Joseph, P.2    Hale, B.3    Beyersmann, D.4
  • 18
    • 28544447373 scopus 로고    scopus 로고
    • Cadmium toxicity in plants: is there any analogy to its carcinogenic effect in mammalian cells
    • Deckert J. Cadmium toxicity in plants: is there any analogy to its carcinogenic effect in mammalian cells. Biometals 18 (2005) 475-481
    • (2005) Biometals , vol.18 , pp. 475-481
    • Deckert, J.1
  • 19
    • 0037102720 scopus 로고    scopus 로고
    • Cadmium affects genes involved in growth regulation during two-stage transformation of Balb/3T3 cells
    • Fang M.Z., Mar W., and Cho M.H. Cadmium affects genes involved in growth regulation during two-stage transformation of Balb/3T3 cells. Toxicology 177 (2002) 253-265
    • (2002) Toxicology , vol.177 , pp. 253-265
    • Fang, M.Z.1    Mar, W.2    Cho, M.H.3
  • 20
    • 6344226159 scopus 로고    scopus 로고
    • Effect of cadmium on cell cycle progression in Chinese hamster ovary cells
    • Yang P.M., Chiu S.J., Lin K.A., and Lin L.Y. Effect of cadmium on cell cycle progression in Chinese hamster ovary cells. Chem. Biol. Interact. 149 (2004) 125-136
    • (2004) Chem. Biol. Interact. , vol.149 , pp. 125-136
    • Yang, P.M.1    Chiu, S.J.2    Lin, K.A.3    Lin, L.Y.4
  • 21
    • 0034815483 scopus 로고    scopus 로고
    • Cadmium-induced apoptosis and phenotypic changes in mouse thymocytes
    • Dong S., Shen H.M., and Ong C.N. Cadmium-induced apoptosis and phenotypic changes in mouse thymocytes. Mol. Cell. Biochem. 222 (2001) 11-20
    • (2001) Mol. Cell. Biochem. , vol.222 , pp. 11-20
    • Dong, S.1    Shen, H.M.2    Ong, C.N.3
  • 22
    • 33646126929 scopus 로고    scopus 로고
    • A rapid and transient ROS generation by cadmium triggers apoptosis via caspase-dependent pathway in HepG2 cells and this is inhibited through N-acetylcysteine-mediated catalase upregulation
    • Oh S.H., and Lim S.C. A rapid and transient ROS generation by cadmium triggers apoptosis via caspase-dependent pathway in HepG2 cells and this is inhibited through N-acetylcysteine-mediated catalase upregulation. Toxicol. Appl. Pharmacol. 212 (2006) 212-223
    • (2006) Toxicol. Appl. Pharmacol. , vol.212 , pp. 212-223
    • Oh, S.H.1    Lim, S.C.2
  • 23
    • 0141741479 scopus 로고    scopus 로고
    • Induction of mitogenic signalling in the 1LN prostate cell line on exposure to submicromolar concentrations of cadmium+
    • Misra U.K., Gawdi G., and Pizzo S.V. Induction of mitogenic signalling in the 1LN prostate cell line on exposure to submicromolar concentrations of cadmium+. Cell. Signal. 15 (2003) 1059-1070
    • (2003) Cell. Signal. , vol.15 , pp. 1059-1070
    • Misra, U.K.1    Gawdi, G.2    Pizzo, S.V.3
  • 26
    • 0025164630 scopus 로고
    • Cadmium induces transcription of proto-oncogenes c-jun and c-myc in rat L6 myoblasts
    • Jin P., and Ringertz N.R. Cadmium induces transcription of proto-oncogenes c-jun and c-myc in rat L6 myoblasts. J. Biol. Chem. 265 (1990) 14061-14064
    • (1990) J. Biol. Chem. , vol.265 , pp. 14061-14064
    • Jin, P.1    Ringertz, N.R.2
  • 27
    • 0037021805 scopus 로고    scopus 로고
    • Transient induction of metallothionein isoform 3 (MT-3), c-fos, c-jun and c-myc in human proximal tubule cells exposed to cadmium
    • Garrett S.H., Phillips V., Somji S., Sens M.A., Dutta R., Park S., Kim D., and Sens D.A. Transient induction of metallothionein isoform 3 (MT-3), c-fos, c-jun and c-myc in human proximal tubule cells exposed to cadmium. Toxicol. Lett. 126 (2002) 69-80
    • (2002) Toxicol. Lett. , vol.126 , pp. 69-80
    • Garrett, S.H.1    Phillips, V.2    Somji, S.3    Sens, M.A.4    Dutta, R.5    Park, S.6    Kim, D.7    Sens, D.A.8
  • 28
    • 0742324326 scopus 로고    scopus 로고
    • Up-regulation of expression of translation factors-a novel molecular mechanism for cadmium carcinogenesis
    • Joseph P., Lei Y.X., and Ong T.M. Up-regulation of expression of translation factors-a novel molecular mechanism for cadmium carcinogenesis. Mol. Cell. Biochem. 255 (2004) 93-101
    • (2004) Mol. Cell. Biochem. , vol.255 , pp. 93-101
    • Joseph, P.1    Lei, Y.X.2    Ong, T.M.3
  • 30
    • 0033990794 scopus 로고    scopus 로고
    • Regulation of metallothionein gene expression by oxidative stress and metal ions.Biochem
    • Andrews G.K. Regulation of metallothionein gene expression by oxidative stress and metal ions.Biochem. Pharmacol. 59 (2000) 95-104
    • (2000) Pharmacol. , vol.59 , pp. 95-104
    • Andrews, G.K.1
  • 31
    • 26944485546 scopus 로고    scopus 로고
    • Two major branches of anti-cadmium defense in the mouse: MTF-1/metallothioneins and glutathione
    • Wimmer U., Wang Y., Georgiev O., and Schaffner W. Two major branches of anti-cadmium defense in the mouse: MTF-1/metallothioneins and glutathione. Nucleic Acids Res. 33 (2005) 5715-5727
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5715-5727
    • Wimmer, U.1    Wang, Y.2    Georgiev, O.3    Schaffner, W.4
  • 32
    • 27944457297 scopus 로고    scopus 로고
    • Basal and zinc-induced metallothionein in resistance to cadmium, cisplatin, zinc, and tertbutyl hydroperoxide: studies using MT knockout and antisense-downregulated MT in mammalian cells
    • Kennette W., Collins O.M., Zalups R.K., and Koropatnick J. Basal and zinc-induced metallothionein in resistance to cadmium, cisplatin, zinc, and tertbutyl hydroperoxide: studies using MT knockout and antisense-downregulated MT in mammalian cells. Toxicol. Sci. 88 (2005) 602-613
    • (2005) Toxicol. Sci. , vol.88 , pp. 602-613
    • Kennette, W.1    Collins, O.M.2    Zalups, R.K.3    Koropatnick, J.4
  • 33
    • 25444455321 scopus 로고    scopus 로고
    • Effect of metallothionein on cell viability and its interactions with cadmium and zinc in HEK293 cells
    • Li J., Liu Y., and Ru B. Effect of metallothionein on cell viability and its interactions with cadmium and zinc in HEK293 cells. Cell Biol. Int. 29 (2005) 843-848
    • (2005) Cell Biol. Int. , vol.29 , pp. 843-848
    • Li, J.1    Liu, Y.2    Ru, B.3
  • 34
    • 20444431515 scopus 로고    scopus 로고
    • Effects of exogenous metallothionein on acute cadmium toxicity in rats
    • Kara H., Karatas F., Canatan H., and Servi K. Effects of exogenous metallothionein on acute cadmium toxicity in rats. Biol. Trace Elem. Res. 104 (2005) 223-232
    • (2005) Biol. Trace Elem. Res. , vol.104 , pp. 223-232
    • Kara, H.1    Karatas, F.2    Canatan, H.3    Servi, K.4
  • 35
    • 0035198895 scopus 로고    scopus 로고
    • Induction of apoptosis in cells by cadmium: quantitative negative correlation between basal or induced metallothionein concentration and apoptotic rate
    • Shimoda R., Nagamine T., Takagi H., Mori M., and Waalkes M.P. Induction of apoptosis in cells by cadmium: quantitative negative correlation between basal or induced metallothionein concentration and apoptotic rate. Toxicol. Sci. 64 (2001) 208-215
    • (2001) Toxicol. Sci. , vol.64 , pp. 208-215
    • Shimoda, R.1    Nagamine, T.2    Takagi, H.3    Mori, M.4    Waalkes, M.P.5
  • 36
    • 33745132699 scopus 로고    scopus 로고
    • Metallothionein 1 isoform gene expression induced by cadmium in human peripheral blood lymphocytes
    • Chang X.L., Jin T.Y., and Zhou Y.F. Metallothionein 1 isoform gene expression induced by cadmium in human peripheral blood lymphocytes. Biomed. Environ. Sci. 19 (2006) 104-109
    • (2006) Biomed. Environ. Sci. , vol.19 , pp. 104-109
    • Chang, X.L.1    Jin, T.Y.2    Zhou, Y.F.3
  • 38
    • 0030014643 scopus 로고    scopus 로고
    • Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death
    • Mehlen P., Schulze-Osthoff K., and Arrigo A.P. Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J. Biol. Chem. 271 28 (1996) 16510-16514
    • (1996) J. Biol. Chem. , vol.271 , Issue.28 , pp. 16510-16514
    • Mehlen, P.1    Schulze-Osthoff, K.2    Arrigo, A.P.3
  • 40
    • 0033971311 scopus 로고    scopus 로고
    • Implication of free radicals and glutathione in the mechanism of cadmium-induced expression of stress proteins in the A549 human lung cell-line
    • Gaubin Y., Vaissade F., Croute F., Beau B., Soleilhavoup J., and Murat J. Implication of free radicals and glutathione in the mechanism of cadmium-induced expression of stress proteins in the A549 human lung cell-line. Biochim. Biophys. Acta 1495 (2000) 4-13
    • (2000) Biochim. Biophys. Acta , vol.1495 , pp. 4-13
    • Gaubin, Y.1    Vaissade, F.2    Croute, F.3    Beau, B.4    Soleilhavoup, J.5    Murat, J.6
  • 41
    • 0036818754 scopus 로고    scopus 로고
    • Differential heat shock gene hsp70-1 response to toxicants revealed by in vivo study of lungs in transgenic mice
    • Wirth D., Christians E., Munaut C., Dessy C., Foidart J.M., and Gustin P. Differential heat shock gene hsp70-1 response to toxicants revealed by in vivo study of lungs in transgenic mice. Cell Stress Chaperones 7 (2002) 387-395
    • (2002) Cell Stress Chaperones , vol.7 , pp. 387-395
    • Wirth, D.1    Christians, E.2    Munaut, C.3    Dessy, C.4    Foidart, J.M.5    Gustin, P.6
  • 42
    • 0037166041 scopus 로고    scopus 로고
    • Upregulation of stress response mRNAs in COS-7 cells exposed to cadmium
    • Lee M.J., Nishio H., Ayaki H., Yamamoto M., and Sumino K. Upregulation of stress response mRNAs in COS-7 cells exposed to cadmium. Toxicology 174 (2002) 109-117
    • (2002) Toxicology , vol.174 , pp. 109-117
    • Lee, M.J.1    Nishio, H.2    Ayaki, H.3    Yamamoto, M.4    Sumino, K.5
  • 44
    • 0036804354 scopus 로고    scopus 로고
    • Induction of apoptosis in mammalian cells by cadmium and zinc
    • Watjen W., Haase H., Biagioli M., and Beyersmann D. Induction of apoptosis in mammalian cells by cadmium and zinc. Environ. Health Perspect. 110 Suppl. 5 (2002) 865-867
    • (2002) Environ. Health Perspect. , vol.110 , Issue.SUPPL. 5 , pp. 865-867
    • Watjen, W.1    Haase, H.2    Biagioli, M.3    Beyersmann, D.4
  • 46
    • 0036159106 scopus 로고    scopus 로고
    • Cadmium-induced apoptosis in C6 glioma cells: mediation by caspase 9-activation
    • Watjen W., Cox M., Biagioli M., and Beyersmann D. Cadmium-induced apoptosis in C6 glioma cells: mediation by caspase 9-activation. Biometals 15 (2002) 15-25
    • (2002) Biometals , vol.15 , pp. 15-25
    • Watjen, W.1    Cox, M.2    Biagioli, M.3    Beyersmann, D.4
  • 47
    • 33645117749 scopus 로고    scopus 로고
    • Single and combination toxic metal exposures induce apoptosis in cultured mutine podocytes exclusively via the extrinsic caspase 8 pathway
    • Eichler T., Ma Q., Kelly C., Mishra J., Parikh S., Ransom R.F., Devarajan P., and Smoyer W.F. Single and combination toxic metal exposures induce apoptosis in cultured mutine podocytes exclusively via the extrinsic caspase 8 pathway. Toxicol. Sci. 90 (2006) 392-399
    • (2006) Toxicol. Sci. , vol.90 , pp. 392-399
    • Eichler, T.1    Ma, Q.2    Kelly, C.3    Mishra, J.4    Parikh, S.5    Ransom, R.F.6    Devarajan, P.7    Smoyer, W.F.8
  • 48
    • 33751007596 scopus 로고    scopus 로고
    • Activation of iniator caspases: history, hypotheses, and perspectives
    • Shi Y. Activation of iniator caspases: history, hypotheses, and perspectives. J. Cancer Mol. 1 (2005) 9-18
    • (2005) J. Cancer Mol. , vol.1 , pp. 9-18
    • Shi, Y.1
  • 49
    • 32044458623 scopus 로고    scopus 로고
    • Protection of betulin against cadmium-induced apoptosis in hepatoma cells
    • Oh S.-H., Choi J.-E., and Lim S.-C. Protection of betulin against cadmium-induced apoptosis in hepatoma cells. Toxicology 220 (2006) 1-12
    • (2006) Toxicology , vol.220 , pp. 1-12
    • Oh, S.-H.1    Choi, J.-E.2    Lim, S.-C.3
  • 50
  • 52
    • 4644320547 scopus 로고    scopus 로고
    • Cadmium induces apoptotic cell death in WI 38 cells via caspase-dependent Bid cleavage and calpain-mediated mitochondrial Bax cleavage by Bcl-2-independent pathway
    • Oh S.H., Lee B.H., and Lim S.C. Cadmium induces apoptotic cell death in WI 38 cells via caspase-dependent Bid cleavage and calpain-mediated mitochondrial Bax cleavage by Bcl-2-independent pathway. Biochem. Pharmacol. 68 (2004) 1845-1855
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1845-1855
    • Oh, S.H.1    Lee, B.H.2    Lim, S.C.3
  • 53
    • 5144220858 scopus 로고    scopus 로고
    • Mediating of caspase-independent apoptosis by cadmium through the mitochondria-ROS pathway in MRC-5 fibroblasts
    • Shih C.M., Ko W.C., Wu J.S., Wei Y.H., Wang L.F., Chang E.E., Lo T.Y., Cheng H.H., and Chen C.T. Mediating of caspase-independent apoptosis by cadmium through the mitochondria-ROS pathway in MRC-5 fibroblasts. J. Cell. Biochem. 91 (2004) 384-397
    • (2004) J. Cell. Biochem. , vol.91 , pp. 384-397
    • Shih, C.M.1    Ko, W.C.2    Wu, J.S.3    Wei, Y.H.4    Wang, L.F.5    Chang, E.E.6    Lo, T.Y.7    Cheng, H.H.8    Chen, C.T.9
  • 55
    • 0344845135 scopus 로고    scopus 로고
    • Metal-induced apoptosis: mechanisms
    • Pulido M.D., and Parrish A.R. Metal-induced apoptosis: mechanisms. Mutat. Res. 533 (2003) 227-241
    • (2003) Mutat. Res. , vol.533 , pp. 227-241
    • Pulido, M.D.1    Parrish, A.R.2
  • 56
    • 0033992478 scopus 로고    scopus 로고
    • p53 and human cancer: the first ten thousand mutations
    • Hainaut P., and Hollstein M. p53 and human cancer: the first ten thousand mutations. Adv. Cancer Res. 77 (2000) 81-137
    • (2000) Adv. Cancer Res. , vol.77 , pp. 81-137
    • Hainaut, P.1    Hollstein, M.2
  • 57
    • 0036208657 scopus 로고    scopus 로고
    • Cadmium-induced apoptosis of primary epithelial lung cells: involvement of Bax and p53, but not of oxidative stress
    • Lag M., Westly S., Lerstad T., Bjornsrud C., Refsnes M., and Schwarze P.E. Cadmium-induced apoptosis of primary epithelial lung cells: involvement of Bax and p53, but not of oxidative stress. Cell Biol. Toxicol. 18 (2002) 29-42
    • (2002) Cell Biol. Toxicol. , vol.18 , pp. 29-42
    • Lag, M.1    Westly, S.2    Lerstad, T.3    Bjornsrud, C.4    Refsnes, M.5    Schwarze, P.E.6
  • 58
    • 0034193451 scopus 로고    scopus 로고
    • Cadmium induces c-myc, p53, and c-jun expression in normal human prostate epithelial cells as a prelude to apoptosis
    • Achanzar W.E., Achanzar K.B., Lewis J.G., Webber M.M., and Waalkes M.P. Cadmium induces c-myc, p53, and c-jun expression in normal human prostate epithelial cells as a prelude to apoptosis. Toxicol. Appl. Pharmacol. 164 (2000) 291-300
    • (2000) Toxicol. Appl. Pharmacol. , vol.164 , pp. 291-300
    • Achanzar, W.E.1    Achanzar, K.B.2    Lewis, J.G.3    Webber, M.M.4    Waalkes, M.P.5
  • 59
    • 0034805815 scopus 로고    scopus 로고
    • Cadmium induces phosphorylation of p53 at serine 15 in MCF-7 cells, Biochem
    • Matsuoka M., and Igisu H. Cadmium induces phosphorylation of p53 at serine 15 in MCF-7 cells, Biochem. Biophys. Res.Commun. 282 (2001) 1120-1125
    • (2001) Biophys. Res.Commun. , vol.282 , pp. 1120-1125
    • Matsuoka, M.1    Igisu, H.2
  • 60
    • 0039136305 scopus 로고    scopus 로고
    • Cadmium induces conformational modifications of wild-type p53 and suppresses p53 response to DNA damage in cultured cells
    • Meplan C., Mann K., and Hainaut P. Cadmium induces conformational modifications of wild-type p53 and suppresses p53 response to DNA damage in cultured cells. J. Biol. Chem. 274 (1999) 31663-31670
    • (1999) J. Biol. Chem. , vol.274 , pp. 31663-31670
    • Meplan, C.1    Mann, K.2    Hainaut, P.3
  • 61
    • 0034859507 scopus 로고    scopus 로고
    • Zinc binding and redox control of p53 structure and function
    • Hainaut P., and Mann K. Zinc binding and redox control of p53 structure and function. Antioxid. Redox Signal. 3 (2001) 611-623
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 611-623
    • Hainaut, P.1    Mann, K.2
  • 62
    • 32044431692 scopus 로고    scopus 로고
    • Oxidative stress and apoptotic changes in murine splenocytes exposed to cadmium
    • Pathak N., and Khandelwal S. Oxidative stress and apoptotic changes in murine splenocytes exposed to cadmium. Toxicology 220 (2006) 26-36
    • (2006) Toxicology , vol.220 , pp. 26-36
    • Pathak, N.1    Khandelwal, S.2
  • 63
    • 0031959845 scopus 로고    scopus 로고
    • Evaluation of the direct genotoxic potential of cadmium in four different rodent cell lines
    • Misra R.R., Smith G.T., and Waalkes M.P. Evaluation of the direct genotoxic potential of cadmium in four different rodent cell lines. Toxicology 126 (1998) 103-114
    • (1998) Toxicology , vol.126 , pp. 103-114
    • Misra, R.R.1    Smith, G.T.2    Waalkes, M.P.3
  • 64
    • 0033964480 scopus 로고    scopus 로고
    • DNA damage in arsenite- and cadmium-treated bovine aortic endothelial cells
    • Liu F., and Jan K.Y. DNA damage in arsenite- and cadmium-treated bovine aortic endothelial cells. Free Radic. Biol. Med. 28 (2000) 55-63
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 55-63
    • Liu, F.1    Jan, K.Y.2
  • 65
    • 8144220011 scopus 로고    scopus 로고
    • A comparative investigation of DNA strand breaks, sister chromatid exchanges and K-ras gene mutations induced by cadmium salts in cultured human cells
    • Mouron S.A., Grillo C.A., Dulout F.N., and Golijow C.D. A comparative investigation of DNA strand breaks, sister chromatid exchanges and K-ras gene mutations induced by cadmium salts in cultured human cells. Mutat. Res. 568 (2004) 221-231
    • (2004) Mutat. Res. , vol.568 , pp. 221-231
    • Mouron, S.A.1    Grillo, C.A.2    Dulout, F.N.3    Golijow, C.D.4
  • 66
    • 17044395830 scopus 로고    scopus 로고
    • Cadmium chloride-induced DNA and lysosomal damage in a hepatoma cell line
    • Fotakis G., Cemeli E., Anderson D., and Timbrell J.A. Cadmium chloride-induced DNA and lysosomal damage in a hepatoma cell line. Toxicol. In Vitro 19 (2005) 481-489
    • (2005) Toxicol. In Vitro , vol.19 , pp. 481-489
    • Fotakis, G.1    Cemeli, E.2    Anderson, D.3    Timbrell, J.A.4
  • 67
    • 0031149665 scopus 로고    scopus 로고
    • Cadmium inhibits DNA strand break rejoining in methyl methanesulfonate-treated CHO-K1 cells
    • Lynn S., Lai H.T., Kao S.M., Lai J., and Jan K.Y. Cadmium inhibits DNA strand break rejoining in methyl methanesulfonate-treated CHO-K1 cells. Toxicol. Appl. Pharmacol. 144 (1997) 171-176
    • (1997) Toxicol. Appl. Pharmacol. , vol.144 , pp. 171-176
    • Lynn, S.1    Lai, H.T.2    Kao, S.M.3    Lai, J.4    Jan, K.Y.5
  • 68
    • 0042009730 scopus 로고    scopus 로고
    • Cadmium inhibits repair of UV-, methyl methanesulfonate- and N-methyl-N-nitrosourea-induced DNA damage in Chinese hamster ovary cells
    • Fatur T., Lah T.T., and Filipic M. Cadmium inhibits repair of UV-, methyl methanesulfonate- and N-methyl-N-nitrosourea-induced DNA damage in Chinese hamster ovary cells. Mutat. Res. 529 (2003) 109-116
    • (2003) Mutat. Res. , vol.529 , pp. 109-116
    • Fatur, T.1    Lah, T.T.2    Filipic, M.3
  • 69
    • 1642322044 scopus 로고    scopus 로고
    • Effects of cadmium(II) on (+/-)-anti-benzo[a]pyrene-7,8-diol-9,10-epoxide-induced DNA damage response in human fibroblasts and DNA repair: a possible mechanism of cadmium's cogenotoxicity
    • Mukherjee J.J., Gupta S.K., Kumar S., and Sikka H.C. Effects of cadmium(II) on (+/-)-anti-benzo[a]pyrene-7,8-diol-9,10-epoxide-induced DNA damage response in human fibroblasts and DNA repair: a possible mechanism of cadmium's cogenotoxicity. Chem. Res. Toxicol. 17 (2004) 287-293
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 287-293
    • Mukherjee, J.J.1    Gupta, S.K.2    Kumar, S.3    Sikka, H.C.4
  • 70
    • 0021179711 scopus 로고
    • In vitro cadmium-DNA interactions: cooperativity of cadmium binding and competitive antagonism by calcium, magnesium, and zinc
    • Waalkes M.P., and Poirier L.A. In vitro cadmium-DNA interactions: cooperativity of cadmium binding and competitive antagonism by calcium, magnesium, and zinc. Toxicol. Appl. Pharmacol. 75 (1984) 539-546
    • (1984) Toxicol. Appl. Pharmacol. , vol.75 , pp. 539-546
    • Waalkes, M.P.1    Poirier, L.A.2
  • 71
    • 0030938045 scopus 로고    scopus 로고
    • Cadmium-induced 8-hydroxydeoxyguanosine formation, DNA strand breaks and antioxidant enzyme activities in lymphoblastoid cells
    • Mikhailova M.V., Littlefield N.A., Hass B.S., Poirier L.A., and Chou M.W. Cadmium-induced 8-hydroxydeoxyguanosine formation, DNA strand breaks and antioxidant enzyme activities in lymphoblastoid cells. Cancer Lett. 115 (1997) 141-148
    • (1997) Cancer Lett. , vol.115 , pp. 141-148
    • Mikhailova, M.V.1    Littlefield, N.A.2    Hass, B.S.3    Poirier, L.A.4    Chou, M.W.5
  • 72
    • 0033769575 scopus 로고    scopus 로고
    • Effect of cadmium on the relationship between replicative and repair DNA synthesis in synchronized CHO cells
    • Banfalvi G., Littlefield N., Hass B., Mikhailova M., Csuka I., Szepessy E., and Chou M.W. Effect of cadmium on the relationship between replicative and repair DNA synthesis in synchronized CHO cells. Eur. J. Biochem. 267 (2000) 6580-6585
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6580-6585
    • Banfalvi, G.1    Littlefield, N.2    Hass, B.3    Mikhailova, M.4    Csuka, I.5    Szepessy, E.6    Chou, M.W.7
  • 73
    • 0030566884 scopus 로고    scopus 로고
    • Mechanism of cadmium-induced cytotoxicity in rat hepatocytes: cadmium-induced active oxygen-related permeability changes of the plasma membrane
    • Koizumi T., Shirakura H., Kumagai H., Tatsumoto H., and Suzuki K.T. Mechanism of cadmium-induced cytotoxicity in rat hepatocytes: cadmium-induced active oxygen-related permeability changes of the plasma membrane. Toxicology 114 (1996) 125-134
    • (1996) Toxicology , vol.114 , pp. 125-134
    • Koizumi, T.1    Shirakura, H.2    Kumagai, H.3    Tatsumoto, H.4    Suzuki, K.T.5
  • 74
    • 1342267699 scopus 로고    scopus 로고
    • Cadmium-induced mitochondrial membrane-potential dissipation does not necessarily require cytosolic oxidative stress: studies using rhodamine-123 fluorescence unquenching
    • Bolduc J.S., Denizeau F., and Jumarie C. Cadmium-induced mitochondrial membrane-potential dissipation does not necessarily require cytosolic oxidative stress: studies using rhodamine-123 fluorescence unquenching. Toxicol. Sci. 77 (2004) 299-306
    • (2004) Toxicol. Sci. , vol.77 , pp. 299-306
    • Bolduc, J.S.1    Denizeau, F.2    Jumarie, C.3
  • 75
    • 27544490827 scopus 로고    scopus 로고
    • Cadmium chloride-induced oxidative stress in skeletal muscle cells in vitro
    • Yano C.L., and Marcondes M.C. Cadmium chloride-induced oxidative stress in skeletal muscle cells in vitro. Free Radic. Biol. Med. 39 (2005) 1378-1384
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 1378-1384
    • Yano, C.L.1    Marcondes, M.C.2
  • 76
    • 0033508131 scopus 로고    scopus 로고
    • Influence of cadmium intoxication on hepatic lipid peroxidation, glutathione level, and glutathione S-transferase and gamma-glutamyl transpeptidase activities: correlation with chromosome aberrations in bone marrow cells
    • Karmakar R., Banerjee A., Datta S., and Chatterjee M. Influence of cadmium intoxication on hepatic lipid peroxidation, glutathione level, and glutathione S-transferase and gamma-glutamyl transpeptidase activities: correlation with chromosome aberrations in bone marrow cells. J. Environ. Pathol. Toxicol. Oncol. 18 (1999) 277-287
    • (1999) J. Environ. Pathol. Toxicol. Oncol. , vol.18 , pp. 277-287
    • Karmakar, R.1    Banerjee, A.2    Datta, S.3    Chatterjee, M.4
  • 77
    • 28844506092 scopus 로고    scopus 로고
    • Acute cadmium intoxication induces alpha-class glutathione S-transferase protein synthesis and enzyme activity in rat liver
    • Casalino E., Sblano C., Calzaretti G., and Landriscina C. Acute cadmium intoxication induces alpha-class glutathione S-transferase protein synthesis and enzyme activity in rat liver. Toxicology 217 (2006) 240-245
    • (2006) Toxicology , vol.217 , pp. 240-245
    • Casalino, E.1    Sblano, C.2    Calzaretti, G.3    Landriscina, C.4
  • 78
    • 16644361891 scopus 로고    scopus 로고
    • Response of antioxidant enzymes and redox metabolites to cadmium-induced oxidative stress in CRL-1439 normal rat liver cells
    • Ikediobi C.O., Badisa V.L., Ayuk-Takem L.T., Latinwo L.M., and West J. Response of antioxidant enzymes and redox metabolites to cadmium-induced oxidative stress in CRL-1439 normal rat liver cells. Int. J. Mol. Med. 14 (2004) 87-92
    • (2004) Int. J. Mol. Med. , vol.14 , pp. 87-92
    • Ikediobi, C.O.1    Badisa, V.L.2    Ayuk-Takem, L.T.3    Latinwo, L.M.4    West, J.5
  • 79
    • 0032557581 scopus 로고    scopus 로고
    • Disruption of the intracellular sulfhydryl homeostasis by cadmium-induced oxidative stress leads to protein thiolation and ubiquitination in neuronal cells
    • Figueiredo-Pereira M.E., Yakushin S., and Cohen G. Disruption of the intracellular sulfhydryl homeostasis by cadmium-induced oxidative stress leads to protein thiolation and ubiquitination in neuronal cells. J. Biol. Chem. 273 (1998) 12703-12709
    • (1998) J. Biol. Chem. , vol.273 , pp. 12703-12709
    • Figueiredo-Pereira, M.E.1    Yakushin, S.2    Cohen, G.3
  • 81
    • 0002847975 scopus 로고
    • Introduction
    • Spatz L., and Bloom A.D. (Eds), Oxford University Press, New York
    • Spatz L. Introduction. In: Spatz L., and Bloom A.D. (Eds). Biological Consequences of Oxidative Stress (1992), Oxford University Press, New York 3-22
    • (1992) Biological Consequences of Oxidative Stress , pp. 3-22
    • Spatz, L.1
  • 82
    • 0033061893 scopus 로고    scopus 로고
    • Glutathione depletion and oxidative damage in mitochondria following exposure to cadmium in rat liver and kidney
    • Nigam D., Shukla G.S., and Agarwal A.K. Glutathione depletion and oxidative damage in mitochondria following exposure to cadmium in rat liver and kidney. Toxicol. Lett. 106 (1999) 151-157
    • (1999) Toxicol. Lett. , vol.106 , pp. 151-157
    • Nigam, D.1    Shukla, G.S.2    Agarwal, A.K.3
  • 83
    • 0022348627 scopus 로고
    • The effect of ferric iron complex on isolated rat liver mitochondria. I. Respiratory and electrochemical responses
    • Masini A., Trenti T., Ceccarelli-Stanzani D., and Ventura E. The effect of ferric iron complex on isolated rat liver mitochondria. I. Respiratory and electrochemical responses. Biochim. Biophys. Acta 810 (1985) 20-26
    • (1985) Biochim. Biophys. Acta , vol.810 , pp. 20-26
    • Masini, A.1    Trenti, T.2    Ceccarelli-Stanzani, D.3    Ventura, E.4
  • 84
    • 0023685030 scopus 로고
    • Lipid peroxidation in mitochondria
    • Bindoli A. Lipid peroxidation in mitochondria. Free Radic. Biol. Med. 5 (1988) 247-261
    • (1988) Free Radic. Biol. Med. , vol.5 , pp. 247-261
    • Bindoli, A.1
  • 86
    • 0036343634 scopus 로고    scopus 로고
    • Role of the mitochondrial permeability transition and cytochrome C release in hydrogen peroxide-induced apoptosis
    • Takeyama N., Miki S., Hirakawa A., and Tanaka T. Role of the mitochondrial permeability transition and cytochrome C release in hydrogen peroxide-induced apoptosis. Exp. Cell Res. 274 (2002) 16-24
    • (2002) Exp. Cell Res. , vol.274 , pp. 16-24
    • Takeyama, N.1    Miki, S.2    Hirakawa, A.3    Tanaka, T.4
  • 87
    • 17244382315 scopus 로고    scopus 로고
    • 17beta-estradiol suppresses ROS-induced apoptosis of CHO cells through inhibition of lipid peroxidation-coupled membrane permeability transition
    • Miyaguchi C., Muranaka S., Kanno T., Fujita H., Akiyama J., Yoshioka T., and Yasuda T. 17beta-estradiol suppresses ROS-induced apoptosis of CHO cells through inhibition of lipid peroxidation-coupled membrane permeability transition. Physiol. Chem. Phys. Med. NMR 36 (2004) 21-35
    • (2004) Physiol. Chem. Phys. Med. NMR , vol.36 , pp. 21-35
    • Miyaguchi, C.1    Muranaka, S.2    Kanno, T.3    Fujita, H.4    Akiyama, J.5    Yoshioka, T.6    Yasuda, T.7
  • 89
    • 22044450545 scopus 로고    scopus 로고
    • Cadmium toxicity toward caspase-independent apoptosis through the mitochondria-calcium pathway in mtDNA-depleted cells
    • Shih Y.L., Lin C.J., Hsu S.W., Wang S.H., Chen W.L., Lee M.T., Wei Y.H., and Shih C.M. Cadmium toxicity toward caspase-independent apoptosis through the mitochondria-calcium pathway in mtDNA-depleted cells. Ann. N. Y. Acad. Sci. 1042 (2005) 497-505
    • (2005) Ann. N. Y. Acad. Sci. , vol.1042 , pp. 497-505
    • Shih, Y.L.1    Lin, C.J.2    Hsu, S.W.3    Wang, S.H.4    Chen, W.L.5    Lee, M.T.6    Wei, Y.H.7    Shih, C.M.8
  • 90
    • 2342646206 scopus 로고    scopus 로고
    • Cadmium inhibits the electron transfer chain and induces reactive oxygen species
    • Wang Y., Fang J., Leonard S.S., and Rao K.M. Cadmium inhibits the electron transfer chain and induces reactive oxygen species. Free Radic. Biol. Med. 36 (2004) 1434-1443
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1434-1443
    • Wang, Y.1    Fang, J.2    Leonard, S.S.3    Rao, K.M.4
  • 92
    • 0030702781 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical formation during reductive and oxidative stress to intact hepatocytes
    • Lemasters J.J., and Nieminen A.L. Mitochondrial oxygen radical formation during reductive and oxidative stress to intact hepatocytes. Biosci. Rep. 17 (1997) 281-291
    • (1997) Biosci. Rep. , vol.17 , pp. 281-291
    • Lemasters, J.J.1    Nieminen, A.L.2
  • 93
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers J.H. Genome maintenance mechanisms for preventing cancer. Nature 411 (2001) 366-374
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 94
    • 33645322935 scopus 로고    scopus 로고
    • Signalling cell cycle arrest and cell death through the MMR system
    • O'brien V., and Brown R. Signalling cell cycle arrest and cell death through the MMR system. Carcinogenesis 27 (2006) 682-692
    • (2006) Carcinogenesis , vol.27 , pp. 682-692
    • O'brien, V.1    Brown, R.2
  • 96
    • 11144230352 scopus 로고    scopus 로고
    • Cadmium inhibits the functions of eukaryotic MutS complexes
    • Clark A.B., and Kunkel T.A. Cadmium inhibits the functions of eukaryotic MutS complexes. J. Biol. Chem. 279 (2004) 53903-53906
    • (2004) J. Biol. Chem. , vol.279 , pp. 53903-53906
    • Clark, A.B.1    Kunkel, T.A.2
  • 97
    • 14544292921 scopus 로고    scopus 로고
    • Cadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complex
    • Banerjee S., and Flores-Rozas H. Cadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complex. Nucleic Acids Res. 33 (2005) 1410-1419
    • (2005) Nucleic Acids Res. , vol.33 , pp. 1410-1419
    • Banerjee, S.1    Flores-Rozas, H.2
  • 98
    • 17344395338 scopus 로고    scopus 로고
    • Carcinogenicity of metal compounds: possible role of DNA repair inhibition
    • Hartwig A. Carcinogenicity of metal compounds: possible role of DNA repair inhibition. Toxicol. Lett. 102-103 (1998) 35-239
    • (1998) Toxicol. Lett. , vol.102-103 , pp. 35-239
    • Hartwig, A.1
  • 99
    • 0030723714 scopus 로고    scopus 로고
    • The DNA damage-recognition problem in human and other eukaryotic cells: the XPA damage binding protein
    • Cleaver J.E., and States J.C. The DNA damage-recognition problem in human and other eukaryotic cells: the XPA damage binding protein. Biochem. J. 328 (1997) 1-12
    • (1997) Biochem. J. , vol.328 , pp. 1-12
    • Cleaver, J.E.1    States, J.C.2
  • 100
    • 0026625629 scopus 로고
    • Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein. Identification of essential domains for nuclear localization and DNA excision repair
    • Miyamoto I., Miura N., Niwa H., Miyazaki J., and Tanaka K. Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein. Identification of essential domains for nuclear localization and DNA excision repair. J. Biol. Chem. 267 (1992) 12182-12187
    • (1992) J. Biol. Chem. , vol.267 , pp. 12182-12187
    • Miyamoto, I.1    Miura, N.2    Niwa, H.3    Miyazaki, J.4    Tanaka, K.5
  • 102
    • 0032102927 scopus 로고    scopus 로고
    • Structural features of the minimal DNA binding domain (M98-F219) of human nucleotide excision repair protein XPA
    • Buchko G.W., Ni S., Thrall B.D., and Kennedy M.A. Structural features of the minimal DNA binding domain (M98-F219) of human nucleotide excision repair protein XPA. Nucleic Acids Res. 26 (1998) 2779-2788
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2779-2788
    • Buchko, G.W.1    Ni, S.2    Thrall, B.D.3    Kennedy, M.A.4
  • 103
    • 0031843623 scopus 로고    scopus 로고
    • Disturbance of DNA damage recognition after UV-irradiation by nickel(II) and cadmium(II) in mammalian cells
    • Hartmann M., and Hartwig A. Disturbance of DNA damage recognition after UV-irradiation by nickel(II) and cadmium(II) in mammalian cells. Carcinogenesis 19 (1998) 617-621
    • (1998) Carcinogenesis , vol.19 , pp. 617-621
    • Hartmann, M.1    Hartwig, A.2
  • 105
    • 0033743112 scopus 로고    scopus 로고
    • Differential effects of toxic metal compounds on the activities of Fpg and XPA, two zinc finger proteins involved in DNA repair
    • Asmuss M., Mullenders L.H., Eker A., and Hartwig A. Differential effects of toxic metal compounds on the activities of Fpg and XPA, two zinc finger proteins involved in DNA repair. Carcinogenesis 21 (2000) 2097-2104
    • (2000) Carcinogenesis , vol.21 , pp. 2097-2104
    • Asmuss, M.1    Mullenders, L.H.2    Eker, A.3    Hartwig, A.4
  • 106
    • 8844270071 scopus 로고    scopus 로고
    • Co(II) and Cd(II) substitute for Zn(II) in the zinc finger derived from the DNA repair protein XPA, demonstrating a variety of potential mechanisms of toxicity
    • Kopera E., Schwerdtle T., Hartwig A., and Bal W. Co(II) and Cd(II) substitute for Zn(II) in the zinc finger derived from the DNA repair protein XPA, demonstrating a variety of potential mechanisms of toxicity. Chem. Res. Toxicol. 17 (2004) 1452-1458
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 1452-1458
    • Kopera, E.1    Schwerdtle, T.2    Hartwig, A.3    Bal, W.4
  • 107
    • 0025802822 scopus 로고
    • Site-specific mutagenesis using a gapped duplex vector: a study of translation synthesis past 8-oxodeoxyguanosine in E. coli
    • Moriya M., Ou C., Bodepudi V., Johnson F., Takeshita M., and Grollman A.P. Site-specific mutagenesis using a gapped duplex vector: a study of translation synthesis past 8-oxodeoxyguanosine in E. coli. Mutat. Res. 254 (1991) 281-288
    • (1991) Mutat. Res. , vol.254 , pp. 281-288
    • Moriya, M.1    Ou, C.2    Bodepudi, V.3    Johnson, F.4    Takeshita, M.5    Grollman, A.P.6
  • 108
    • 0027462131 scopus 로고
    • Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role
    • O'Connor T.R., Graves R.J., de Murcia G., Castaing B., and Laval J. Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role. J. Biol. Chem. 268 (1993) 9063-9070
    • (1993) J. Biol. Chem. , vol.268 , pp. 9063-9070
    • O'Connor, T.R.1    Graves, R.J.2    de Murcia, G.3    Castaing, B.4    Laval, J.5
  • 109
    • 0037416096 scopus 로고    scopus 로고
    • Cadmium exposure down-regulates 8-oxoguanine DNA glycosylase expression in rat lung and alveolar epithelial cells
    • Potts R.J., Watkin R.D., and Hart B.A. Cadmium exposure down-regulates 8-oxoguanine DNA glycosylase expression in rat lung and alveolar epithelial cells. Toxicology 184 (2003) 189-202
    • (2003) Toxicology , vol.184 , pp. 189-202
    • Potts, R.J.1    Watkin, R.D.2    Hart, B.A.3
  • 111
    • 0037416094 scopus 로고    scopus 로고
    • Mechanisms regulating the cadmium-mediated suppression of Sp1 transcription factor activity in alveolar epithelial cells
    • Watkin R.D., Nawrot T., Potts R.J., and Hart B.A. Mechanisms regulating the cadmium-mediated suppression of Sp1 transcription factor activity in alveolar epithelial cells. Toxicology 184 (2003) 157-178
    • (2003) Toxicology , vol.184 , pp. 157-178
    • Watkin, R.D.1    Nawrot, T.2    Potts, R.J.3    Hart, B.A.4
  • 112
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: enzymology and biology
    • Demple B., and Harrison L. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63 (1994) 915-948
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 114
    • 0026662651 scopus 로고
    • The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity
    • Schreiber V., Molinete M., Boeuf H., de Murcia G., and Menissier-de Murcia J. The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity. EMBO J. 11 (1992) 3263-3269
    • (1992) EMBO J. , vol.11 , pp. 3263-3269
    • Schreiber, V.1    Molinete, M.2    Boeuf, H.3    de Murcia, G.4    Menissier-de Murcia, J.5
  • 116
    • 0032496235 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions
    • Malanga M., Pleschke J.M., Kleczkowska H.E., and Althaus F.R. Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions. J. Biol. Chem. 273 (1998) 11839-11843
    • (1998) J. Biol. Chem. , vol.273 , pp. 11839-11843
    • Malanga, M.1    Pleschke, J.M.2    Kleczkowska, H.E.3    Althaus, F.R.4
  • 118
    • 19444374556 scopus 로고    scopus 로고
    • Mediation of cell death by poly(ADP-ribose) polymerase-1
    • Koh D.W., Dawson T.M., and Dawson V.L. Mediation of cell death by poly(ADP-ribose) polymerase-1. Pharmacol. Res. 52 (2005) 5-14
    • (2005) Pharmacol. Res. , vol.52 , pp. 5-14
    • Koh, D.W.1    Dawson, T.M.2    Dawson, V.L.3
  • 119
    • 24744447821 scopus 로고    scopus 로고
    • The role of poly(ADP-ribose) in the DNA damage signaling network
    • Malanga M., and Althaus F.R. The role of poly(ADP-ribose) in the DNA damage signaling network. Biochem. Cell Biol. 83 (2005) 354-364
    • (2005) Biochem. Cell Biol. , vol.83 , pp. 354-364
    • Malanga, M.1    Althaus, F.R.2
  • 120
    • 0042632806 scopus 로고    scopus 로고
    • Physical and functional interaction between DNA ligase IIIalpha and poly(ADP-Ribose) polymerase 1 in DNA single-strand break repair
    • Leppard J.B., Dong Z., Mackey Z.B., and Tomkinson A.E. Physical and functional interaction between DNA ligase IIIalpha and poly(ADP-Ribose) polymerase 1 in DNA single-strand break repair. Mol. Cell. Biol. 23 (2003) 5919-5927
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5919-5927
    • Leppard, J.B.1    Dong, Z.2    Mackey, Z.B.3    Tomkinson, A.E.4
  • 121
    • 32644432644 scopus 로고    scopus 로고
    • Damage of zinc fingers in DNA repair proteins, a novel molecular mechanism in carcinogenesis
    • Witkiewicz-Kucharczyk A., and Bal W. Damage of zinc fingers in DNA repair proteins, a novel molecular mechanism in carcinogenesis. Toxicol. Lett. 162 (2006) 29-42
    • (2006) Toxicol. Lett. , vol.162 , pp. 29-42
    • Witkiewicz-Kucharczyk, A.1    Bal, W.2
  • 122
    • 26944485546 scopus 로고    scopus 로고
    • Two major branches of anti-cadmium defense in the mouse: MTF-1/metallothioneins and glutathione
    • Wimmer U., Wang Y., Georgiev O., and Schaffner W. Two major branches of anti-cadmium defense in the mouse: MTF-1/metallothioneins and glutathione. Nucleic Acids Res. 33 (2005) 5715-5727
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5715-5727
    • Wimmer, U.1    Wang, Y.2    Georgiev, O.3    Schaffner, W.4
  • 123
    • 3042739151 scopus 로고    scopus 로고
    • Induction of metallothionein I by phenolic antioxidants requires metal-activated transcription factor 1 (MTF-1) and zinc
    • Bi Y., Palmiter R.D., Wood K.M., and Ma Q. Induction of metallothionein I by phenolic antioxidants requires metal-activated transcription factor 1 (MTF-1) and zinc. Biochem. J. 380 (2004) 695-703
    • (2004) Biochem. J. , vol.380 , pp. 695-703
    • Bi, Y.1    Palmiter, R.D.2    Wood, K.M.3    Ma, Q.4
  • 124
    • 0028358324 scopus 로고
    • The transcription factor MTF-1 is essential for basal and heavy metal-induced metallothionein gene expression
    • Heuchel R., Radtke F., Georgiev O., Stark G., Aguet M., and Schaffner W. The transcription factor MTF-1 is essential for basal and heavy metal-induced metallothionein gene expression. EMBO J. 13 (1994) 2870-2875
    • (1994) EMBO J. , vol.13 , pp. 2870-2875
    • Heuchel, R.1    Radtke, F.2    Georgiev, O.3    Stark, G.4    Aguet, M.5    Schaffner, W.6
  • 125
    • 0034859756 scopus 로고    scopus 로고
    • Metal response element (MRE)-binding transcription factor-1 (MTF-1): structure, function, and regulation
    • Giedroc D.P., Chen X., and Apuy J.L. Metal response element (MRE)-binding transcription factor-1 (MTF-1): structure, function, and regulation. Antioxid. Redox Signal. 3 (2001) 577-596
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 577-596
    • Giedroc, D.P.1    Chen, X.2    Apuy, J.L.3
  • 126
    • 0034711045 scopus 로고    scopus 로고
    • Functional characterization of zinc-finger motif in redox regulation of RPA-ssDNA interaction
    • You J.S., Wang M., and Lee S.H. Functional characterization of zinc-finger motif in redox regulation of RPA-ssDNA interaction. Biochemistry 39 (2000) 12953-12958
    • (2000) Biochemistry , vol.39 , pp. 12953-12958
    • You, J.S.1    Wang, M.2    Lee, S.H.3
  • 127
    • 0026333726 scopus 로고
    • Primary structure of the catalytic subunit of human DNA polymerase delta and chromosomal location of the gene
    • Chung D.W., Zhang J.A., Tan C.K., Davie E.W., So A.G., and Downey K.M. Primary structure of the catalytic subunit of human DNA polymerase delta and chromosomal location of the gene. Proc. Natl. Acad. Sci. USA 88 (1991) 11197-11201
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11197-11201
    • Chung, D.W.1    Zhang, J.A.2    Tan, C.K.3    Davie, E.W.4    So, A.G.5    Downey, K.M.6
  • 128
    • 4344678213 scopus 로고    scopus 로고
    • Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIalpha
    • Kulczyk A.W., Yang J.C., and Neuhaus D. Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIalpha. J. Mol. Biol. 341 (2004) 723-738
    • (2004) J. Mol. Biol. , vol.341 , pp. 723-738
    • Kulczyk, A.W.1    Yang, J.C.2    Neuhaus, D.3
  • 130
  • 131
    • 0036231641 scopus 로고    scopus 로고
    • ATP-dependent DNA ligases
    • reviews 3005.1 - 3005.7
    • Martin I.V., and MacNeill S.A. ATP-dependent DNA ligases. Genome Biol. 3 (2002) reviews 3005.1 - 3005.7
    • (2002) Genome Biol. , vol.3
    • Martin, I.V.1    MacNeill, S.A.2
  • 132
    • 0035853789 scopus 로고    scopus 로고
    • Role of ATM in oxidative stress-mediated c-Jun phosphorylation in response to ionizing radiation and CdCl2
    • Lee S.A., Dritschilo A., and Jung M. Role of ATM in oxidative stress-mediated c-Jun phosphorylation in response to ionizing radiation and CdCl2. J. Biol. Chem. 276 (2000) 11783-11790
    • (2000) J. Biol. Chem. , vol.276 , pp. 11783-11790
    • Lee, S.A.1    Dritschilo, A.2    Jung, M.3
  • 133
    • 19444363740 scopus 로고    scopus 로고
    • ATM-dependent phosphorylation of ATF2 is required for the DNA damage response
    • Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N., and Ronai Z. ATM-dependent phosphorylation of ATF2 is required for the DNA damage response. Mol. Cell 18 (2005) 577-587
    • (2005) Mol. Cell , vol.18 , pp. 577-587
    • Bhoumik, A.1    Takahashi, S.2    Breitweiser, W.3    Shiloh, Y.4    Jones, N.5    Ronai, Z.6
  • 134
    • 0031572856 scopus 로고    scopus 로고
    • Enzyme activity alteration by cadmium administration to rats: the possibility of iron involvement in lipid peroxidation
    • Casalino E., Sblano C., and Landriscina C. Enzyme activity alteration by cadmium administration to rats: the possibility of iron involvement in lipid peroxidation. Arch. Biochem. Biophys. 346 (1997) 171-179
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 171-179
    • Casalino, E.1    Sblano, C.2    Landriscina, C.3
  • 135
    • 0026452185 scopus 로고
    • DNA damaging activity of cadmium in Leydig cells, a target cell population for cadmium carcinogenesis in the rat testis
    • Koizumi T., Li Z.G., and Tatsumoto H. DNA damaging activity of cadmium in Leydig cells, a target cell population for cadmium carcinogenesis in the rat testis. Toxicol. Lett. 63 (1992) 211-220
    • (1992) Toxicol. Lett. , vol.63 , pp. 211-220
    • Koizumi, T.1    Li, Z.G.2    Tatsumoto, H.3
  • 136
    • 1342323673 scopus 로고    scopus 로고
    • Oxidative stress, toxicology, and pharmacology of CYP2E1
    • Caro A.A., and Cederbaum A.I. Oxidative stress, toxicology, and pharmacology of CYP2E1. Annu. Rev. Pharmacol. Toxicol. 44 (2004) 27-42
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 27-42
    • Caro, A.A.1    Cederbaum, A.I.2
  • 137
    • 25844520458 scopus 로고    scopus 로고
    • Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism
    • Jezek P., and Hlavata L. Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism. Int. J. Biochem. Cell Biol. 37 (2005) 2478-2503
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 2478-2503
    • Jezek, P.1    Hlavata, L.2
  • 138
    • 8644221211 scopus 로고    scopus 로고
    • Mammalian peroxisomes and reactive oxygen species
    • Schrader M., and Fahimi H.D. Mammalian peroxisomes and reactive oxygen species. Histochem. Cell Biol. 122 (2004) 383-393
    • (2004) Histochem. Cell Biol. , vol.122 , pp. 383-393
    • Schrader, M.1    Fahimi, H.D.2
  • 139
    • 0028803293 scopus 로고
    • Induction of peroxisome proliferation and increase of catalase activity in yeast, Candida albicans, by cadmium
    • Chen T., Li W., Schulz P.J., Furst A., and Chien P.K. Induction of peroxisome proliferation and increase of catalase activity in yeast, Candida albicans, by cadmium. Biol. Trace Elem. Res. 50 (1995) 125-133
    • (1995) Biol. Trace Elem. Res. , vol.50 , pp. 125-133
    • Chen, T.1    Li, W.2    Schulz, P.J.3    Furst, A.4    Chien, P.K.5
  • 141
    • 0036148249 scopus 로고    scopus 로고
    • Interactive effects of benzo(a)pyrene and cadmium and effects of di(2-ethylhexyl) phthalate on antioxidant and peroxisomal enzymes and peroxisomal volume density in the digestive gland of mussel Mytilus galloprovincialis Lmk
    • Orbea A., Ortiz-Zarragoitia M., and Cajaraville M.P. Interactive effects of benzo(a)pyrene and cadmium and effects of di(2-ethylhexyl) phthalate on antioxidant and peroxisomal enzymes and peroxisomal volume density in the digestive gland of mussel Mytilus galloprovincialis Lmk. Biomarkers 7 (2002) 33-48
    • (2002) Biomarkers , vol.7 , pp. 33-48
    • Orbea, A.1    Ortiz-Zarragoitia, M.2    Cajaraville, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.