메뉴 건너뛰기




Volumn 20, Issue 3, 1997, Pages 151-163

New directions for studying the role of free radicals in aging

Author keywords

Overexpression and deletion of genes; Oxidative stress; Signal transduction; Transcription factors, Antioxidant defense, Transgenic mice

Indexed keywords

CATALASE; FREE RADICAL; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR AP 1;

EID: 0031545015     PISSN: 01619152     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11357-997-0014-0     Document Type: Article
Times cited : (5)

References (106)
  • 1
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman, D., Aging: A theory based on free radical and radiation chemistry. J. Gerontol., 11: 298-300, 1956.
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 2
    • 0027457521 scopus 로고
    • The free radical hypothesis of aging: An appraisal of the current status
    • Sohal, R.S : The free radical hypothesis of aging: an appraisal of the current status. Aging Clin. Exp. Res., 5: 3-17, 1993.
    • (1993) Aging Clin. Exp. Res. , vol.5 , pp. 3-17
    • Sohal, R.S.1
  • 3
    • 0027217874 scopus 로고
    • Involvement of free radicals in aging: A consequence or cause of senescence
    • Nohl, H.: Involvement of free radicals in aging: a consequence or cause of senescence. Brit Med. Bull., 40: 653-667, 1993.
    • (1993) Brit Med. Bull. , vol.40 , pp. 653-667
    • Nohl, H.1
  • 4
    • 0021741506 scopus 로고
    • Free radical theory of aging: The free radical diseases
    • Harman, D.: Free radical theory of aging: the free radical diseases. Age, 7: 111-131, 1984.
    • (1984) Age , vol.7 , pp. 111-131
    • Harman, D.1
  • 5
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymic function for erythrocuprein (neurocuprein)
    • McCord, J.M , and Fridovich, I.: Superoxide dismutase: An enzymic function for erythrocuprein (neurocuprein) J Biol., Chem., 244: 6049-6055, 1969.
    • (1969) J Biol., Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 6
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance, B., Sies, H , and Boveris, A.: Hydroperoxide metabolism in mammalian organs. Physiol. Rev., 62: 527-605, 1979.
    • (1979) Physiol. Rev. , vol.62 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 7
    • 0025787017 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase is the 18 kDa selenoprotein expressed in human tumor cell lines
    • Maiorino, M., Chu, F.F., Ursini, F., Davies, K., Dorshaw, J.H., and Esworthy, R.S., Phospholipid hydroperoxide glutathione peroxidase is the 18 kDa selenoprotein expressed in human tumor cell lines. J. Biol. Chem., 255: 7728-7732, 1991.
    • (1991) J. Biol. Chem. , vol.255 , pp. 7728-7732
    • Maiorino, M.1    Chu, F.F.2    Ursini, F.3    Davies, K.4    Dorshaw, J.H.5    Esworthy, R.S.6
  • 8
    • 0022684839 scopus 로고
    • Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: Extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation
    • Elroy-Stein, O , Bernstein, Y., and Groner, Y.: Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation. EMBO J . 5: 615-622, 1986.
    • (1986) EMBO J. , vol.5 , pp. 615-622
    • Elroy-Stein, O.1    Bernstein, Y.2    Groner, Y.3
  • 9
    • 0026589727 scopus 로고
    • Relationship of resistance to oxygen free radicals to CuZn-superoxide dismutase activity in transgenic, transfected. and trisomic cells
    • Huang, T.T., Carlson. E.J., Leadon, S.A., and Epstein, C J.: Relationship of resistance to oxygen free radicals to CuZn-superoxide dismutase activity in transgenic, transfected. and trisomic cells. FASEB J., 6: 03-910, 1992.
    • (1992) FASEB J. , vol.6 , pp. 03-910
    • Huang, T.T.1    Carlson, E.J.2    Leadon, S.A.3    Epstein, C.J.4
  • 10
    • 0023901508 scopus 로고
    • Superoxide mediates the toxicity of paraquat for cultured mammalian cells
    • Krall, J., Bagley. A.C., Mullenbach. G T., Hallewell, R.A . and Lynch, R E : Superoxide mediates the toxicity of paraquat for cultured mammalian cells. J. Biol. Chem . 263: 1910-1914, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1910-1914
    • Krall, J.1    Bagley, A.C.2    Mullenbach, G.T.3    Hallewell, R.A.4    Lynch, R.E.5
  • 11
    • 0028945710 scopus 로고
    • Transfection with human copper-zinc Superoxide dismutase induces bidirectional alterations in other antioxidant enzymes, proteins, growth factor response, and paraquat resistance
    • Keiner, M.J., Bagnell, R., Montoya. M., Estes, L. Uglik, S.F., and Cerutti P.: Transfection with human copper-zinc Superoxide dismutase induces bidirectional alterations in other antioxidant enzymes, proteins, growth factor response, and paraquat resistance. Free Rad Biol. Med , 18: 497-506, 1995
    • (1995) Free Rad Biol. Med , vol.18 , pp. 497-506
    • Keiner, M.J.1    Bagnell, R.2    Montoya, M.3    Estes, L.4    Uglik, S.F.5    Cerutti, P.6
  • 12
  • 13
    • 0023848325 scopus 로고
    • Impaired neurotransmitter uptake in PC-12 cells overexpressing human CuZn-superoxide dismutase-implication for gene dosage effects in Down Syndrome
    • Elroy-Stein, O , and Groner, Y.: Impaired neurotransmitter uptake in PC-12 cells overexpressing human CuZn-superoxide dismutase-implication for gene dosage effects in Down Syndrome. Cell, 52: 259-267, 1988.
    • (1988) Cell , vol.52 , pp. 259-267
    • Elroy-Stein, O.1    Groner, Y.2
  • 14
    • 0025316007 scopus 로고
    • Cytotoxic effects of expression of human Superoxide dismutase in bovine adrenocortical cells
    • Morris, K.H., and Homsby, P.J.: Cytotoxic effects of expression of human Superoxide dismutase in bovine adrenocortical cells. Mutat. Res , 237: 95-106, 1990.
    • (1990) Mutat. Res , vol.237 , pp. 95-106
    • Morris, K.H.1    Homsby, P.J.2
  • 15
    • 0025940313 scopus 로고
    • The balance between Cu/Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress
    • Amstad, P., Peskin, A., Shah, G., Mirault, M.-E, Moret, R , Zbinden, I., and Cerutti, P.: The balance between Cu/Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress. Biochemistry, 30: 9305-9313, 1991.
    • (1991) Biochemistry , vol.30 , pp. 9305-9313
    • Amstad, P.1    Peskin, A.2    Shah, G.3    Mirault, M.-E.4    Moret, R.5    Zbinden, I.6    Cerutti, P.7
  • 16
    • 0027174021 scopus 로고
    • Protection of human endothelial cells from oxidant injury by adenovirus-mediated transfer of the human catalase cDNA
    • Erzurum, S C., Lemarchand, P., Rosenfeld, M.A., Yoo, J -H., Crystal, R G.: Protection of human endothelial cells from oxidant injury by adenovirus-mediated transfer of the human catalase cDNA. Nucleic Acids Res., 21: 1607-1612, 1993.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1607-1612
    • Erzurum, S.C.1    Lemarchand, P.2    Rosenfeld, M.A.3    Yoo, J.H.4    Crystal, R.G.5
  • 18
    • 0024428198 scopus 로고
    • Manganous Superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor
    • Wong, G.H W., Elwell, J.H , Oberley, LW., and Goeddel, D.V. Manganous Superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor. Cell, 58 923-931, 1989.
    • (1989) Cell , vol.58 , pp. 923-931
    • Wong, G.H.W.1    Elwell, J.H.2    Oberley, L.W.3    Goeddel, D.V.4
  • 19
    • 0027394553 scopus 로고
    • Overexpression of mitochondrial manganese Superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs, and ionizing radiation
    • Hirose, K., Longo, D.L., Oppenheim, J J , and Matsushima, K.: Overexpression of mitochondrial manganese Superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs, and ionizing radiation. FASEB J., 7: 361-368, 1993.
    • (1993) FASEB J. , vol.7 , pp. 361-368
    • Hirose, K.1    Longo, D.L.2    Oppenheim, J.J.3    Matsushima, K.4
  • 20
    • 0028457620 scopus 로고
    • Role of manganese Superoxide dismutase in radioprotection using gene transfer studies
    • Suresh, A., Tung, F., Moreb, J., and Zucali. J.R.: Role of manganese Superoxide dismutase in radioprotection using gene transfer studies. Cancer Gene Therapy 1: 85-90, 1994
    • (1994) Cancer Gene Therapy , vol.1 , pp. 85-90
    • Suresh, A.1    Tung, F.2    Moreb, J.3    Zucali, J.R.4
  • 21
    • 0026048173 scopus 로고
    • Overproduction of human Mn-superoxide dismutase modulates paraquat-mediated toxicity in mammalian cells
    • St.Clair, D.K., Oberley, T D., and Ho, Y.-S Overproduction of human Mn-superoxide dismutase modulates paraquat-mediated toxicity in mammalian cells. FEBS Lett , 293: 199-203. 1991.
    • (1991) FEBS Lett , vol.293 , pp. 199-203
    • St.Clair, D.K.1    Oberley, T.D.2    Ho, Y.-S.3
  • 22
    • 0027298244 scopus 로고
    • Expression of human Mn SOD in Chinese hamster ovary cells confers protection from oxidant injury
    • Warner. B , Papes. R . Heile. M., Spitz. D., and Wispe. J Expression of human Mn SOD in Chinese hamster ovary cells confers protection from oxidant injury. Am. J Physiol., 264 L598-L605, 1993.
    • (1993) Am. J Physiol. , vol.264
    • Warner, B.1    Papes, R.2    Heile, M.3    Spitz, D.4    Wispe, J.5
  • 23
    • 0028027824 scopus 로고
    • Overexpression of manganous superoxide dismutase (MnSOD) in pulmonary endothelial cells confers resistance to hyperoxia
    • Lindau-Shepard. B., Shaffer. J B . and Del Vecchio, P J: Overexpression of manganous superoxide dismutase (MnSOD) in pulmonary endothelial cells confers resistance to hyperoxia. J. Cell. Physiol.. 161. 237-242 1994.
    • (1994) J. Cell. Physiol. , vol.161 , pp. 237-242
    • Lindau-Shepard, B.1    Shaffer, J.B.2    Del Vecchio, P.J.3
  • 24
    • 0027093827 scopus 로고
    • Suppression of radiation-induced neoplastic transformation by overexpression of mitochondrial superoxide dismutase
    • St. Clair. D.K , Wan. X S., Oberley, T D . Muse, K.E., and St. Clair, W.H : Suppression of radiation-induced neoplastic transformation by overexpression of mitochondrial superoxide dismutase. Mol. Carcinog., 6: 238-242, 1992.
    • (1992) Mol. Carcinog. , vol.6 , pp. 238-242
    • St. Clair, D.K.1    Wan, X.S.2    Oberley, T.D.3    Muse, K.E.4    St. Clair, W.H.5
  • 25
    • 0028329155 scopus 로고
    • Expression of manganese superoxide dismutase promotes cellular differentiation
    • St. Clair, D.K., Oberley, T.D., Muse, K.E . and St. Clair, W.H.: Expression of manganese superoxide dismutase promotes cellular differentiation. Free Radic. Biol. Med., 16: 275-282, 1994.
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 275-282
    • St. Clair, D.K.1    Oberley, T.D.2    Muse, K.E.3    St. Clair, W.H.4
  • 27
    • 0029032567 scopus 로고
    • Phenotypic changes induced in human breast cancer cells by overexpression of manganese-containing superoxide dismutase
    • Li, J.J., Oberley, L.W., St Clair, D.K.. Ridnour, L.A., and Oberley, T.D : Phenotypic changes induced in human breast cancer cells by overexpression of manganese-containing superoxide dismutase. Oncogene, 10: 1989-2000, 1995.
    • (1995) Oncogene , vol.10 , pp. 1989-2000
    • Li, J.J.1    Oberley, L.W.2    St Clair, D.K.3    Ridnour, L.A.4    Oberley, T.D.5
  • 28
    • 0025786654 scopus 로고
    • Overexpression of selenogluthathione peroxidase by gene transfer enhances the resistance of T47D human breast cells to clastogenic oxidants
    • Mirault. M.E , Tremblay, A., Beaudoin, N., and Tremblay, M.: Overexpression of selenogluthathione peroxidase by gene transfer enhances the resistance of T47D human breast cells to clastogenic oxidants J. Biol. Chem., 266: 20752-20760, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20752-20760
    • Mirault, M.E.1    Tremblay, A.2    Beaudoin, N.3    Tremblay, M.4
  • 29
    • 0027270922 scopus 로고
    • Glutathione peroxidase protects cultured mammalian cells from the toxicity of adriamycin and paraquat
    • Taylor. S.D., Davenport, L.D , Speranza, M.J., Mullenbach. G.T., and Lynch, R.E: Glutathione peroxidase protects cultured mammalian cells from the toxicity of adriamycin and paraquat Arch. Biochem Biophys , 305: 600-605, 1993
    • (1993) Arch. Biochem Biophys , vol.305 , pp. 600-605
    • Taylor, S.D.1    Davenport, L.D.2    Speranza, M.J.3    Mullenbach, G.T.4    Lynch, R.E.5
  • 30
    • 0025362247 scopus 로고
    • Overexpression of Cu-Zn superoxide dismutase in Drosophila does not affect life-span
    • Seto, N.O , Hayashi. S., and Tener G.M : Overexpression of Cu-Zn superoxide dismutase in Drosophila does not affect life-span Proc. Natl Acad. Sci. USA, 87: 4270-4274, 1990.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4270-4274
    • Seto, N.O.1    Hayashi, S.2    Tener, G.M.3
  • 31
    • 0027293919 scopus 로고
    • Effects of Cu-Zn superoxide dismutase overexpression on life span and resistance to oxidative stress in transgenic Drosophila melanogaster
    • Orr, W C , and Sohal, R S : Effects of Cu-Zn superoxide dismutase overexpression on life span and resistance to oxidative stress in transgenic Drosophila melanogaster. Arch. Biochem. Biophys., 301. 4-40 1993
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 4-40
    • Orr, W.C.1    Sohal, R.S.2
  • 32
    • 0025977719 scopus 로고
    • Expression of bovine superoxide dismutase in Drosophila melanogaster augments resistance to oxidative stress
    • Reveillaud, I., Niedzwiecki. A., Bensch, K.G., and Fleming. J.E.: Expression of bovine superoxide dismutase in Drosophila melanogaster augments resistance to oxidative stress Mol. Biol. Cell, 11: 632-640, 1991.
    • (1991) Mol. Biol. Cell , vol.11 , pp. 632-640
    • Reveillaud, I.1    Niedzwiecki, A.2    Bensch, K.G.3    Fleming, J.E.4
  • 33
    • 0028809224 scopus 로고
    • Age-related activity of catalase in different genotypes of Drosophila melanogaster
    • Durusoy. M., Dinl, N., and Bozcuk. A.: Age-related activity of catalase in different genotypes of Drosophila melanogaster. Exp. Gerontol., 30: 77-86. 1995.
    • (1995) Exp. Gerontol. , vol.30 , pp. 77-86
    • Durusoy, M.1    Dinl, N.2    Bozcuk, A.3
  • 35
    • 0026629397 scopus 로고
    • Superoxide dismutase, catalase. and glutathione peroxidase activities in copper/zinc-superoxide dismutase transgenic mice
    • Przedborski, S., Jackson-Lewis, V., Kostic, V., Carlson, E., Epstein. C.J., and Cadet. J.L., Superoxide dismutase, catalase. and glutathione peroxidase activities in copper/zinc-superoxide dismutase transgenic mice. J. Neurochem , 58: 1760-1767, 1992
    • (1992) J. Neurochem , vol.58 , pp. 1760-1767
    • Przedborski, S.1    Jackson-Lewis, V.2    Kostic, V.3    Carlson, E.4    Epstein, C.J.5    Cadet, J.L.6
  • 36
    • 0025942842 scopus 로고
    • Transgenic mice with expression of elevated levels of copper-zinc superoxide dismutase in the lungs are resistant to pulmonary oxygen toxicity
    • White, C.W., Avraham, K.B., Shanley, P.F, and Groner, Y: Transgenic mice with expression of elevated levels of copper-zinc superoxide dismutase in the lungs are resistant to pulmonary oxygen toxicity. J. Clin. Invest., 87: 2162-2168, 1991.
    • (1991) J. Clin. Invest. , vol.87 , pp. 2162-2168
    • White, C.W.1    Avraham, K.B.2    Shanley, P.F.3    Groner, Y.4
  • 37
    • 0026345023 scopus 로고
    • Attenuation of focal cerebral ischemic injury in transgenic mice overexpressing CuZn superoxide dismutase
    • Kinouchi, H., Epstein, C.J., Mizui, T., Carlson, E., Chen, S.F., and Chan, P.H.: Attenuation of focal cerebral ischemic injury in transgenic mice overexpressing CuZn superoxide dismutase. Proc. Natl. Acad Sci. USA, 88: 11158-11162, 1991.
    • (1991) Proc. Natl. Acad Sci. USA , vol.88 , pp. 11158-11162
    • Kinouchi, H.1    Epstein, C.J.2    Mizui, T.3    Carlson, E.4    Chen, S.F.5    Chan, P.H.6
  • 38
    • 0025911148 scopus 로고
    • Cold-induced brain edema and infarction are reduced in transgenic mice overexpressing CuZn-superoxide dismutase
    • Chan, P.H , Yang, G.Y., Chen, S.F., Carlson, E., and Epstein, C.J.: Cold-induced brain edema and infarction are reduced in transgenic mice overexpressing CuZn-superoxide dismutase. Ann. Neurol , 29: 482-486, 1991.
    • (1991) Ann. Neurol , vol.29 , pp. 482-486
    • Chan, P.H.1    Yang, G.Y.2    Chen, S.F.3    Carlson, E.4    Epstein, C.J.5
  • 39
    • 0025513984 scopus 로고
    • Reduced neurotoxicity in transgenic mice overexpressing human copper-zinc-superoxide dismutase
    • Chan. P.H., Chu, L., Chen, S.F., Carlson, E.J., and Epstein, C.J: Reduced neurotoxicity in transgenic mice overexpressing human copper-zinc-superoxide dismutase. Stroke, 21: 80-82, 1990.
    • (1990) Stroke , vol.21 , pp. 80-82
    • Chan, P.H.1    Chu, L.2    Chen, S.F.3    Carlson, E.J.4    Epstein, C.J.5
  • 40
    • 0026583465 scopus 로고
    • Transgenic mice with increased Cu/Zn-superoxide dismutase activity are resistant to N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine- induced neurotoxicity
    • Przedborski, S., Kostic, V., Jackson-Lewis, V., Naini, A.B., Simonetti. S , Fahn, S., Carlson, E., Epstein, C J., and Cadet, J.L: Transgenic mice with increased Cu/Zn-superoxide dismutase activity are resistant to N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine- induced neurotoxicity. J. Neurosci., 12: 1658-1667, 1992.
    • (1992) J. Neurosci. , vol.12 , pp. 1658-1667
    • Przedborski, S.1    Kostic, V.2    Jackson-Lewis, V.3    Naini, A.B.4    Simonetti, S.5    Fahn, S.6    Carlson, E.7    Epstein, C.J.8    Cadet, J.L.9
  • 41
    • 0023809302 scopus 로고
    • Down's syndrome: Abnormal neuromuscular junction in tongue of transgenic mice with elevated levels of human Cu/ Zn-superoxidedismutase
    • Avraham, K.B., Schickler, M., Sapoznikov, D., Yarom, R., and Groner, Y: Down's syndrome: abnormal neuromuscular junction in tongue of transgenic mice with elevated levels of human Cu/ Zn-superoxidedismutase. Cell. 54: 823-829, 1988.
    • (1988) Cell , vol.54 , pp. 823-829
    • Avraham, K.B.1    Schickler, M.2    Sapoznikov, D.3    Yarom, R.4    Groner, Y.5
  • 42
    • 0026096819 scopus 로고
    • Down's syndrome: Morphological remodeling and increased complexity in the neuromuscular junction of transgenic CuZn-superoxide dismutase mice
    • Avraham. K.B , Sugarman, H., Rotshenker S., and Groner. Y.: Down's syndrome: morphological remodeling and increased complexity in the neuromuscular junction of transgenic CuZn-superoxide dismutase mice. J Neurocytol., 20: 208-215, 1991.
    • (1991) J Neurocytol. , vol.20 , pp. 208-215
    • Avraham, K.B.1    Sugarman, H.2    Rotshenker, S.3    Groner, Y.4
  • 43
    • 0024366919 scopus 로고
    • Diminished serotonin uptake in platelets of transgenic mice with increased Cu/Zn-superoxide dismutase activity
    • Schickler. M., Knobler H , Avraham, K.B , Elroy-Stein. O., and Groner. Y.: Diminished serotonin uptake in platelets of transgenic mice with increased Cu/Zn-superoxide dismutase activity EMBO J , 8. 1385-1392. 1989.
    • (1989) EMBO J , vol.8 , pp. 1385-1392
    • Schickler, M.1    Knobler, H.2    Avraham, K.B.3    Elroy-Stein, O.4    Groner, Y.5
  • 44
    • 0025861601 scopus 로고
    • Gene dosage of CuZnSOD and Down's syndrome: Diminished prostaglandin synthesis in human trisomy 21, transfected cells and transgenic mice
    • Minc-Golomb, D., Knobler. H., and Groner. Y.: Gene dosage of CuZnSOD and Down's syndrome: diminished prostaglandin synthesis in human trisomy 21, transfected cells and transgenic mice. EMBO J., 10: 119-2124, 1991.
    • (1991) EMBO J. , vol.10 , pp. 119-2124
    • Minc-Golomb, D.1    Knobler, H.2    Groner, Y.3
  • 45
    • 0029983348 scopus 로고    scopus 로고
    • Transgenic mice overexpressing the human CuZn-SOD gene: Ultrastructural studies of a premature thymic involution model of Down's Syndrome (Trisomy 21)
    • Nabarra, B., Casanova, M., Paris, D., Nicole, A., Toyama, K., Sinet, P., Ceballos, I., and London, J.: Transgenic mice overexpressing the human CuZn-SOD gene: ultrastructural studies of a premature thymic involution model of Down's Syndrome (Trisomy 21). Laboratory Investigation, 74: 617-626, 1996.
    • (1996) Laboratory Investigation , vol.74 , pp. 617-626
    • Nabarra, B.1    Casanova, M.2    Paris, D.3    Nicole, A.4    Toyama, K.5    Sinet, P.6    Ceballos, I.7    London, J.8
  • 46
    • 0030022578 scopus 로고    scopus 로고
    • Effect of overexpression of human Cu,Zn superoxide dismutase in transgenic mice on macrophage functions
    • Mirochnitchenko, O., and Inouye, M.: Effect of overexpression of human Cu,Zn superoxide dismutase in transgenic mice on macrophage functions. J. Immunol., 156: 1578-1586, 1996.
    • (1996) J. Immunol. , vol.156 , pp. 1578-1586
    • Mirochnitchenko, O.1    Inouye, M.2
  • 48
    • 0028303783 scopus 로고
    • Transgenic models for the study of lung biology and disease
    • Ho, Y.S., Transgenic models for the study of lung biology and disease. Am. J. Physiol., 266: L319-L353, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Ho, Y.S.1
  • 50
    • 0028827252 scopus 로고
    • Dilated cardiomopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • Li, Y., Huang, T., Carlson, E., Yoshimura, M , Berger, C., Chan. P., Wallace, D., and Epstein, C : Dilated cardiomopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat. Genet , 11: 376-381, 1995.
    • (1995) Nat. Genet , vol.11 , pp. 376-381
    • Li, Y.1    Huang, T.2    Carlson, E.3    Yoshimura, M.4    Berger, C.5    Chan, P.6    Wallace, D.7    Epstein, C.8
  • 51
    • 0029838063 scopus 로고    scopus 로고
    • Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice
    • Lebovitz, R M., Zhang, H., Vogel, H., Cartwright, J., Dionne, L., Lu, N , Huang, S., and Matzuk, M.: Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc. Natl Acad. Sci USA, 93: 9782-9787, 1996.
    • (1996) Proc. Natl Acad. Sci USA , vol.93 , pp. 9782-9787
    • Lebovitz, R.M.1    Zhang, H.2    Vogel, H.3    Cartwright, J.4    Dionne, L.5    Lu, N.6    Huang, S.7    Matzuk, M.8
  • 52
    • 0027269781 scopus 로고
    • 2 and antioxidants have opposite effects on activation of NF-κB and AP-1 in intact cells. AP-1 as secondary antioxidant-responsive factor
    • 2 and antioxidants have opposite effects on activation of NF-κB and AP-1 in intact cells. AP-1 as secondary antioxidant-responsive factor. EMBO J., 12: 2005-2015, 1993.
    • (1993) EMBO J. , vol.12 , pp. 2005-2015
    • Meyer, M.1    Schreck, R.2    Baeuerle, P.A.3
  • 53
    • 0028593507 scopus 로고
    • Transcriptional induction of the mouse metallothionein-1 gene in hydrogen peroxide-treated Hepa cells involves a composite major late transcription factor/antioxidant response element and metal response promoter elements
    • Dalton, T. Palmer, R.D., and Andrews. G K.: Transcriptional induction of the mouse metallothionein-1 gene in hydrogen peroxide-treated Hepa cells involves a composite major late transcription factor/antioxidant response element and metal response promoter elements Nucleic Acid Res., 22: 5016-5023, 1994
    • (1994) Nucleic Acid Res. , vol.22 , pp. 5016-5023
    • Dalton, T.1    Palmer, R.D.2    Andrews, G.K.3
  • 55
    • 0018223827 scopus 로고
    • Biological function of metallothionin V. Its induction in rats by various stresses
    • Oh, S. H., Deagen, J.T., Whanger, P.D., and Werving, P.H., Biological function of metallothionin V. Its induction in rats by various stresses. Am. J. Physiol., 234: E282-E305, 1978.
    • (1978) Am. J. Physiol. , vol.234
    • Oh, S.H.1    Deagen, J.T.2    Whanger, P.D.3    Werving, P.H.4
  • 56
    • 0002798521 scopus 로고
    • Acute Phase Reactants
    • A.C. Allison, (ed.), New York, Plenum Publishing Corp.
    • Koj, A.: Acute Phase Reactants. in: Structure and Function of Plasma Proteins. A.C. Allison, (ed.), New York, Plenum Publishing Corp., 1985, 73-125.
    • (1985) Structure and Function of Plasma Proteins , pp. 73-125
    • Koj, A.1
  • 57
    • 0023724778 scopus 로고
    • LκB: A specific inhibitor of the NF-kappa B transcription factor
    • Baeuerle, P.A., and Baltimore, D.: lκB: A specific inhibitor of the NF-kappa B transcription factor. Science, 242: 540-546, 1988
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 58
    • 0025903780 scopus 로고
    • Differential expression of the mouse alpha 1-acid glycoprotein genes during inflammation
    • Carter, K.C., Post, D.G., and Papaconstantinou, J.: Differential expression of the mouse alpha 1-acid glycoprotein genes during inflammation. Biochem. Biophys. Acta., 1089: 197-205, 1991
    • (1991) Biochem. Biophys. Acta , vol.1089 , pp. 197-205
    • Carter, K.C.1    Post, D.G.2    Papaconstantinou, J.3
  • 59
    • 0024359486 scopus 로고
    • Attenuated induction of heat shock gene expression in aging fibroblast
    • Liu, A., Lin, Y.C., Chio, H.S., Sarhage, F., and Li, B.: Attenuated induction of heat shock gene expression in aging fibroblast. J. Biol. Chem, 264: 12037-12045, 1989.
    • (1989) J. Biol. Chem , vol.264 , pp. 12037-12045
    • Liu, A.1    Lin, Y.C.2    Chio, H.S.3    Sarhage, F.4    Li, B.5
  • 60
    • 0026378375 scopus 로고
    • The effect of aging on constitutive mRNA levels and lipopolysaccharide inducibility of acute phase genes
    • Post, D.J , Carter, K.C., and Papaconstantinou, J.: The effect of aging on constitutive mRNA levels and lipopolysaccharide inducibility of acute phase genes. N. Y. Acad. Sci., 621: 66-77, 1991.
    • (1991) N. Y. Acad. Sci. , vol.621 , pp. 66-77
    • Post, D.J.1    Carter, K.C.2    Papaconstantinou, J.3
  • 61
    • 0027154719 scopus 로고
    • Expression of heat shock protein 70 is altered by age and diet at the level of transcription
    • Heydari, A R., Wu, B., Takahashi, R., Strong, R, and Richardson, A.: Expression of heat shock protein 70 is altered by age and diet at the level of transcription. Mol. Cell. Biol., 13: 2909-2918, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2909-2918
    • Heydari, A.R.1    Wu, B.2    Takahashi, R.3    Strong, R.4    Richardson, A.5
  • 62
    • 0029032361 scopus 로고
    • The expression of heat shock protein 70 decreases with age in ymphocytes from rats and rhesus monkeys
    • Pahlavani, M. A., Denny, M., Moore, S. A., Weindruch, R., and Richardson, A: The expression of heat shock protein 70 decreases with age in ymphocytes from rats and rhesus monkeys. Exp. Cell Res., 218: 310-318, 1995.
    • (1995) Exp. Cell Res. , vol.218 , pp. 310-318
    • Pahlavani, M.A.1    Denny, M.2    Moore, S.A.3    Weindruch, R.4    Richardson, A.5
  • 64
    • 0026335852 scopus 로고
    • Regulation of bacterial oxidative stress genes
    • Demple, B . Regulation of bacterial oxidative stress genes. Annu Rev Genet, 25: 315-337. 1991
    • (1991) Annu Rev Genet , vol.25 , pp. 315-337
    • Demple, B.1
  • 65
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of NF-κB activation in intact cells
    • Schreck, R., Meier, B., Mannel, D , Droge, W., and Baeuerle, P. A.: Dithiocarbamates as potent inhibitors of NF-κB activation in intact cells. J. Exp.Med., 175: 1181-1194, 1992.
    • (1992) J. Exp.Med. , vol.175 , pp. 1181-1194
    • Schreck, R.1    Meier, B.2    Mannel, D.3    Droge, W.4    Baeuerle, P.A.5
  • 66
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kB transcription factor and HIV-1
    • Schreck, R., Rieber, P., and Baeuerle, P.A.: Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kB transcription factor and HIV-1 EMBO J., 10 2247-2258, 1991
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 68
    • 0025865317 scopus 로고
    • The inducible transcription activator NF-κB: Regulation by distinct protein subunits
    • Baeuerle, P.A.: The inducible transcription activator NF-κB: Regulation by distinct protein subunits. Biochem Biophys. Acta. 1072: 63-80, 1991.
    • (1991) Biochem Biophys. Acta , vol.1072 , pp. 63-80
    • Baeuerle, P.A.1
  • 69
    • 0025865317 scopus 로고
    • The inducible transcription activator NF-κB: Regulation by distinct protein subunits
    • Baeuerle, P A.: The inducible transcription activator NF-κB: Regulation by distinct protein subunits. Biochem Biophys Acta, 1072: 63-80, 1991
    • (1991) Biochem Biophys Acta , vol.1072 , pp. 63-80
    • Baeuerle, P.A.1
  • 70
    • 0025916445 scopus 로고
    • Transcriptional activation of early-response genes by hydrogen peroxide in a mouse osteoblastic cell line
    • Nose K., Shibanuma, M., Kikuchi. K., Kageyama, H., Sakiyama. S., and Kuroki, T.: Transcriptional activation of early-response genes by hydrogen peroxide in a mouse osteoblastic cell line. Eur. J. Biochem, 201: 99-106, 1991.
    • (1991) Eur. J. Biochem , vol.201 , pp. 99-106
    • Nose, K.1    Shibanuma, M.2    Kikuchi, K.3    Kageyama, H.4    Sakiyama, S.5    Kuroki, T.6
  • 71
    • 0026753708 scopus 로고
    • Mechanisms of c-fos induction by active oxygen
    • Amstad, P.A., Krupitza, G., and Cerutti, P A.: Mechanisms of c-fos induction by active oxygen. Cancer Res., 52: 3952-3960, 1992.
    • (1992) Cancer Res. , vol.52 , pp. 3952-3960
    • Amstad, P.A.1    Krupitza, G.2    Cerutti, P.A.3
  • 72
    • 0026970404 scopus 로고
    • Nuclear factor κB: An oxidative stress-response transcription factor of eukaryotic cells
    • Schreck, R , Albermann, K., and Baeuerle, P.A.: Nuclear factor κB: an oxidative stress-response transcription factor of eukaryotic cells. Free Rad. Res. Commun., 17: 221-237, 1992.
    • (1992) Free Rad. Res. Commun. , vol.17 , pp. 221-237
    • Schreck, R.1    Albermann, K.2    Baeuerle, P.A.3
  • 73
    • 0026606650 scopus 로고
    • Leukotriene B4 stimulates c-fos and c-jun transcription and AP-1 binding activity in human monocytes
    • Stankova, J., and Pleszczynski, M.: Leukotriene B4 stimulates c-fos and c-jun transcription and AP-1 binding activity in human monocytes. Biochem. J., 282: 625-629, 1992.
    • (1992) Biochem. J. , vol.282 , pp. 625-629
    • Stankova, J.1    Pleszczynski, M.2
  • 75
    • 0026530158 scopus 로고
    • IL-1 induces protein tyrosine phosphorylation in T cells
    • Munoz, E., Zubiaga, A.M., Huang, C., and Huber, B T.: IL-1 induces protein tyrosine phosphorylation in T cells Eur J. Immunol., 22: 1391-1396, 1992
    • (1992) Eur J. Immunol. , vol.22 , pp. 1391-1396
    • Munoz, E.1    Zubiaga, A.M.2    Huang, C.3    Huber, B.T.4
  • 76
    • 0027049804 scopus 로고
    • The mammalian ultraviolet response is triggered by activation of Sre tyrosine kinases
    • Devary, Y., Gottlieb, R.A., Smeal, T., and Karin, M.: The mammalian ultraviolet response is triggered by activation of Sre tyrosine kinases. Cell, 71: 1081-1092. 1992.
    • (1992) Cell , vol.71 , pp. 1081-1092
    • Devary, Y.1    Gottlieb, R.A.2    Smeal, T.3    Karin, M.4
  • 78
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA binding activity in vitro
    • Abate. C., Patel. L, Rauscher. F.J., and Curran, T.: Redox regulation of fos and jun DNA binding activity in vitro Science, 249: 1157-1161, 1990.
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher, F.J.3    Curran, T.4
  • 80
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter, T. and Kann, M.: The regulation of transcription by phosphorylation. Cell. 70: 375-387, 1992
    • (1992) Cell , vol.70 , pp. 375-387
    • Hunter, T.1    Kann, M.2
  • 81
    • 0026696360 scopus 로고
    • Mitogen-activated protein kinases: Versatile transducers for cell signaling
    • Pelech. S.L and Sanghera. J.S.: Mitogen-activated protein kinases: Versatile transducers for cell signaling Trends in Biochem. Sci., 17: 233-238. 1992.
    • (1992) Trends in Biochem. Sci. , vol.17 , pp. 233-238
    • Pelech, S.L.1    Sanghera, J.S.2
  • 82
    • 0028366023 scopus 로고
    • Unifying model of the programmed and stochastic theories of aging. Stress response genes. signal transduction-redox pathways and aging
    • Papaconstantinou, J . Unifying model of the programmed and stochastic theories of aging. Stress response genes. signal transduction-redox pathways and aging. Ann. New York Acad. Sci., 719: 195-211, 1994
    • (1994) Ann. New York Acad. Sci. , vol.719 , pp. 195-211
    • Papaconstantinou, J.1
  • 83
    • 0026456536 scopus 로고
    • DNA damage inducing gene expression: Signal transduction and relation to growth factor signaling
    • Herrlich. P , Ponta. H., and Rahmsdorf, H J : DNA damage inducing gene expression: Signal transduction and relation to growth factor signaling. Rev. Physiol. Biochem Pharmacol., 119: 187-223, 1992
    • (1992) Rev. Physiol. Biochem Pharmacol. , vol.119 , pp. 187-223
    • Herrlich, P.1    Ponta, H.2    Rahmsdorf, H.J.3
  • 84
    • 0025583152 scopus 로고
    • Fos and Jun: Two into one will go
    • Woodgette, J.R.: Fos and Jun: Two into one will go. Seminar in Cancer Biology, 4: 389-397, 1990.
    • (1990) Seminar in Cancer Biology , vol.4 , pp. 389-397
    • Woodgette, J.R.1
  • 85
    • 0025720735 scopus 로고
    • The role of Jun, Fos, and the AP-1 complex in cell proliferation and transformation
    • Angel. P. and Karin, M: The role of Jun, Fos, and the AP-1 complex in cell proliferation and transformation. Biochem. Biophys. Acta., 1072: 129-157, 1991.
    • (1991) Biochem. Biophys. Acta , vol.1072 , pp. 129-157
    • Angel, P.1    Karin, M.2
  • 86
    • 0028786336 scopus 로고
    • Transcriptional Regulation by MAP kinases
    • Davis, R.J : Transcriptional Regulation by MAP kinases. Mol. Reprod Dev. 42: 459-567, 1995.
    • (1995) Mol. Reprod Dev. , vol.42 , pp. 459-567
    • Davis, R.J.1
  • 87
    • 0029010944 scopus 로고
    • Protein tyrosine in signal transduction
    • Conrad, A. C., and Steck, P.A.: Protein tyrosine in signal transduction. The Cancer Bulletin, 47: 125-133, 1995.
    • (1995) The Cancer Bulletin , vol.47 , pp. 125-133
    • Conrad, A.C.1    Steck, P.A.2
  • 88
    • 0028291767 scopus 로고
    • A family of mitogen-activated protein kinase-related proteins interacts in vivo with activator protein-1 transcription factor
    • Bernstein, L.R , Ferris, D.K., Colburn, N.H., and Sobel, M.E.: A family of mitogen-activated protein kinase-related proteins interacts in vivo with activator protein-1 transcription factor. J. Biol. Chem., 269: 9401-411, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9401-9411
    • Bernstein, L.R.1    Ferris, D.K.2    Colburn, N.H.3    Sobel, M.E.4
  • 89
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger, R., and Krebs, E.G.: The MAPK signaling cascade FASEB J., 9: 726-732, 1995.
    • (1995) FASEB J. , vol.9 , pp. 726-732
    • Seger, R.1    Krebs, E.G.2
  • 90
    • 0028291525 scopus 로고
    • JNK is involves in signal integration during costimulation of T lymphocytes
    • Su, B , Jacinto, E., Hibi, M., Kallunki, T., Karin, M., and Neriah, Y.: JNK is involves in signal integration during costimulation of T lymphocytes. Cell, 77 726-735, 1994.
    • (1994) Cell , vol.77 , pp. 726-735
    • Su, B.1    Jacinto, E.2    Hibi, M.3    Kallunki, T.4    Karin, M.5    Neriah, Y.6
  • 91
    • 0028229012 scopus 로고
    • The stress-activated protein kinase subfamily of c-jun kinases
    • Kyriakis. J M., Banerjee, P , and Nikolakaki. E.: The stress-activated protein kinase subfamily of c-jun kinases. Nature, 369. 156-160, 1994.
    • (1994) Nature , vol.369 , pp. 156-160
    • Kyriakis, J.M.1    Banerjee, P.2    Nikolakaki, E.3
  • 92
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras taht binds and phosphorylates the c-jun activation domain
    • D'erijard, B., Hibi, M., and Wu, I.H.: JNK1: A protein kinase stimulated by UV light and Ha-Ras taht binds and phosphorylates the c-jun activation domain. Cell. 76: 1025-1037, 1994.
    • (1994) Cell , vol.76 , pp. 1025-1037
    • D'erijard, B.1    Hibi, M.2    Wu, I.H.3
  • 93
    • 0028558986 scopus 로고
    • SAP/ ERK kinase-1 (SEK1) defines the SAP pathway regulating c-Jun N-terminal phosphorylation
    • Sanchez, I., Hughes, R., and Mayer, B.: SAP/ ERK kinase-1 (SEK1) defines the SAP pathway regulating c-Jun N-terminal phosphorylation. Nature. 372: 794-798. 1994
    • (1994) Nature , vol.372 , pp. 794-798
    • Sanchez, I.1    Hughes, R.2    Mayer, B.3
  • 94
    • 0028670788 scopus 로고
    • MEKK1 activates the stress activated protein kinase (SAPK) in vivo, not MAP kinase, via direct phosphorylation of the SAPK activator SEK1
    • Yan. M., Dai, T., Dek. J., Kyriakis, J., Zon, L , Woodgett, J., and Templeton, D.: MEKK1 activates the stress activated protein kinase (SAPK) in vivo, not MAP kinase, via direct phosphorylation of the SAPK activator SEK1. Nature. 372: 798-800. 1994.
    • (1994) Nature , vol.372 , pp. 798-800
    • Yan, M.1    Dai, T.2    Dek, J.3    Kyriakis, J.4    Zon, L.5    Woodgett, J.6    Templeton, D.7
  • 95
    • 0027946514 scopus 로고
    • The stress-activated protein kinases (SAPKs) are major c-Jun amino terminal kinases actiated by ischemia and reperfusion
    • Pombo. C.M , Bonventre. J.V., Woodgett. J R., Kyriakis. J. M., and Force. T. The stress-activated protein kinases (SAPKs) are major c-Jun amino terminal kinases actiated by ischemia and reperfusion. J. Biol. Chem., 269: 26546-26550, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26546-26550
    • Pombo, C.M.1    Bonventre, J.V.2    Woodgett, J.R.3    Kyriakis, J.M.4    Force, T.5
  • 97
    • 0027392874 scopus 로고
    • Co-purification of mitogen-activated protein kinases with phorbol ester-induced c-Jun kinase in U937 leukaemic cells
    • Pulverer, B , Hughes, K., Franklin, C., Kraft, A., Leevers. S., and Woodgett. J.: Co-purification of mitogen-activated protein kinases with phorbol ester-induced c-Jun kinase in U937 leukaemic cells. Oncogene, 8. 407-415. 1993.
    • (1993) Oncogene , vol.8 , pp. 407-415
    • Pulverer, B.1    Hughes, K.2    Franklin, C.3    Kraft, A.4    Leevers, S.5    Woodgett, J.6
  • 98
    • 0027049804 scopus 로고
    • The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases
    • Devary, Y., Gottlieb, R., Smeal, T., and Karin, M.: The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases. Cell, 71. 1081-1091, 1992.
    • (1992) Cell , vol.71 , pp. 1081-1091
    • Devary, Y.1    Gottlieb, R.2    Smeal, T.3    Karin, M.4
  • 99
    • 0025024263 scopus 로고
    • Endotoxin induction of murine metallothionein gene expression
    • De, S.K., McMaster, M.T., and Andrews, G.K.: Endotoxin induction of murine metallothionein gene expression. J. Biol. Chem., 265. 15267-15274, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15267-15274
    • De, S.K.1    McMaster, M.T.2    Andrews, G.K.3
  • 101
    • 0024523351 scopus 로고
    • Inhibition of hydroxyl-radical generated DNA degradation by metallothionein
    • Abel, J., and de Ruiter, N.: Inhibition of hydroxyl-radical generated DNA degradation by metallothionein. Toxicol. Lett., 47: 191-196, 1989.
    • (1989) Toxicol. Lett. , vol.47 , pp. 191-196
    • Abel, J.1    De Ruiter, N.2
  • 102
    • 0021944046 scopus 로고
    • Possible role of metallothionein in protection against radiation-induced oxidative stress
    • Thornalley, P.J., and Vasak, M.: Possible role of metallothionein in protection against radiation-induced oxidative stress. Biochem. Biophys. Acta, 827. 36-44, 1985.
    • (1985) Biochem. Biophys. Acta , vol.827 , pp. 36-44
    • Thornalley, P.J.1    Vasak, M.2
  • 103
    • 0025948113 scopus 로고
    • The antioxidant responsive element. Activation by oxidative stress and identification of DNA consensus sequence required for functional activity
    • Rushmore, T.H., Morton, M.R , and Pickett, C.B.: The antioxidant responsive element. Activation by oxidative stress and identification of DNA consensus sequence required for functional activity. J. Biol. Chem , 266: 11632-11639, 1991.
    • (1991) J. Biol. Chem , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 104
    • 0028364075 scopus 로고
    • Transcriptional regulation of a rat liver glutathione-S-transferase Ya subunit gene
    • Nguyen, T, Rushmore, T.H., and Pickett, C B.: Transcriptional regulation of a rat liver glutathione-S-transferase Ya subunit gene. J. Biol. Chem., 269 13656-13662, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13656-13662
    • Nguyen, T.1    Rushmore, T.H.2    Pickett, C.B.3
  • 105
    • 0027414642 scopus 로고
    • The transcription factor MTF-I is essential for basal and heavy metal-induced metallothionein gene expression
    • Radtke, F , Heuchel, R , Georgiev, O., Hergersberg. M., Gariglio. M., Dembic, Z., and Schaffner, W.: The transcription factor MTF-I is essential for basal and heavy metal-induced metallothionein gene expression EMBO J , 12: 1355-1362, 1993.
    • (1993) EMBO J , vol.12 , pp. 1355-1362
    • Radtke, F.1    Heuchel, R.2    Georgiev, O.3    Hergersberg, M.4    Gariglio, M.5    Dembic, Z.6    Schaffner, W.7
  • 106
    • 0028125990 scopus 로고
    • Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor MTF-I
    • Palmiter, R.D.: Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor MTF-I. Proc. Natl Acad. Sci. USA, 91: 1219-1223, 1994.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1219-1223
    • Palmiter, R.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.