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Volumn 173, Issue 1-2, 1997, Pages 59-69

Hydrogen peroxide-induced expression of the proto-oncogenes, c-jun, c-fos and c-myc in rabbit lens epithelial cells

Author keywords

Gene expression; Hydrogen peroxide; Lens epithelial cells; N acetylcysteine; Oxidative stress; Pyrrolidine dithiocarbamate

Indexed keywords

ACETYLCYSTEINE; DITHIOCARBAMIC ACID DERIVATIVE; HYDROGEN PEROXIDE; MESSENGER RNA; PYRROLIDINE DERIVATIVE; TRANSCRIPTION FACTOR AP 1;

EID: 0030844854     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006828402225     Document Type: Article
Times cited : (76)

References (76)
  • 1
    • 0029151027 scopus 로고
    • Oxidative stress-induced cataract: Mechanism of action
    • Spector A: Oxidative stress-induced cataract: Mechanism of action. FASEB J 9: 1173-1182, 1995
    • (1995) FASEB J , vol.9 , pp. 1173-1182
    • Spector, A.1
  • 2
    • 0019843761 scopus 로고
    • Hydrogen peroxide and human cataract
    • Spector A, Garner WH: Hydrogen peroxide and human cataract. Exp Eye Res 33: 673-681, 1981
    • (1981) Exp Eye Res , vol.33 , pp. 673-681
    • Spector, A.1    Garner, W.H.2
  • 3
    • 0001331063 scopus 로고
    • Light induced damage to ocular lens pump. Prevention by vitamin C
    • Varma SD, Kumar S, Richards RD: Light induced damage to ocular lens pump. Prevention by vitamin C. Proc Natl Acad Sci USA 76: 3504-3506, 1979
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 3504-3506
    • Varma, S.D.1    Kumar, S.2    Richards, R.D.3
  • 5
    • 0022257613 scopus 로고
    • The effect of oxygen radicals generated in the medium on lenses in organ culture, inhibition of damage by chelated iron
    • Zigler JS Jr, Jernigan HM, Garland D, Reddy VN: The effect of oxygen radicals generated in the medium on lenses in organ culture, inhibition of damage by chelated iron. Arch Biochem Biophys 241: 163-172, 1985
    • (1985) Arch Biochem Biophys , vol.241 , pp. 163-172
    • Zigler Jr., J.S.1    Jernigan, H.M.2    Garland, D.3    Reddy, V.N.4
  • 6
    • 0023192764 scopus 로고
    • Peroxide-induced effects on lens cation transport following inhibition of glutathione reductase activity in vitro
    • Giblin FJ, McCready JP, Schrimscher L, Reddy VN: Peroxide-induced effects on lens cation transport following inhibition of glutathione reductase activity in vitro. Exp Eye Res 45: 77-91, 1987
    • (1987) Exp Eye Res , vol.45 , pp. 77-91
    • Giblin, F.J.1    McCready, J.P.2    Schrimscher, L.3    Reddy, V.N.4
  • 7
    • 0027228162 scopus 로고
    • Photochemically induced cataract in rat lenses can be prevented by AL-3823A, a glutathione peroxidase mimic
    • Spector A, Wang GM, Wang RR: Photochemically induced cataract in rat lenses can be prevented by AL-3823A, a glutathione peroxidase mimic. Proc Natl Acad Sci USA 90: 7845-7849, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7845-7849
    • Spector, A.1    Wang, G.M.2    Wang, R.R.3
  • 9
    • 0029986646 scopus 로고    scopus 로고
    • Lens epithelial cell apoptosis is an early event during UVB induced cataract formation
    • Li W-C, Spector A: Lens epithelial cell apoptosis is an early event during UVB induced cataract formation. Free Radic Biol Med 20: 301-311, 1996
    • (1996) Free Radic Biol Med , vol.20 , pp. 301-311
    • Li, W.-C.1    Spector, A.2
  • 10
    • 0025021892 scopus 로고
    • Hydrogen peroxide induced DNA damage in bovine lens epithelial cells
    • Kleiman NJ, Wang RR, Spector A: Hydrogen peroxide induced DNA damage in bovine lens epithelial cells. Mutat Res 240: 35-45, 1990
    • (1990) Mutat Res , vol.240 , pp. 35-45
    • Kleiman, N.J.1    Wang, R.R.2    Spector, A.3
  • 11
    • 0000324675 scopus 로고
    • Studies on the oxidation of cysteine to cysteine in lens proteins during cataract formation
    • Dische Z, Zil, H: Studies on the oxidation of cysteine to cysteine in lens proteins during cataract formation. Am J Ophthalmol 34: 104-113, 1951
    • (1951) Am J Ophthalmol , vol.34 , pp. 104-113
    • Dische, Z.1    Zil, H.2
  • 12
    • 0015257846 scopus 로고
    • The nature and origin of the urea-insoluble protein of the human lens
    • Harding JJ: The nature and origin of the urea-insoluble protein of the human lens. Exp Eye Res 13: 33-40, 1972
    • (1972) Exp Eye Res , vol.13 , pp. 33-40
    • Harding, J.J.1
  • 13
    • 84918314440 scopus 로고
    • Glycosylation of lens proteins and its relationship to cataract
    • SK Srivastava (ed). Elsevier North Holland, New York
    • Spector A, Garner WH: Glycosylation of lens proteins and its relationship to cataract. In: SK Srivastava (ed). The Red Blood Cell and Lens Metabolism. Elsevier North Holland, New York, 1980, pp 233-236
    • (1980) The Red Blood Cell and Lens Metabolism , pp. 233-236
    • Spector, A.1    Garner, W.H.2
  • 14
    • 0017656881 scopus 로고
    • Regulation of hydrogen peroxide in eye humors: Effects of 3-amino-111- 1,2,4-triazole on catalase and glutathione peroxidase of rabbit eye
    • Bhuyan D K, Bhuyan KC: Regulation of hydrogen peroxide in eye humors: Effects of 3-amino-111- 1,2,4-triazole on catalase and glutathione peroxidase of rabbit eye. Biochem Biophys Acta 497: 641-651, 1977
    • (1977) Biochem Biophys Acta , vol.497 , pp. 641-651
    • Bhuyan, D.K.1    Bhuyan, K.C.2
  • 16
    • 0027981492 scopus 로고
    • The redox active components H2O2 and N-acetyl-L-cysteine regulate expression of c-jun and c-fos in lens systems
    • Li W-C, Wang G-M, Wang R-R, Spector A: The redox active components H2O2 and N-acetyl-L-cysteine regulate expression of c-jun and c-fos in lens systems. Exp Eye Res 59: 179-190, 1994
    • (1994) Exp Eye Res , vol.59 , pp. 179-190
    • Li, W.-C.1    Wang, G.-M.2    Wang, R.-R.3    Spector, A.4
  • 19
    • 0025721047 scopus 로고
    • Redox Redux: The control of oxidative stress response
    • Demple B, Amabile-Cuevas CF: Redox Redux: The control of oxidative stress response. Cell 67: 837-839, 1991
    • (1991) Cell , vol.67 , pp. 837-839
    • Demple, B.1    Amabile-Cuevas, C.F.2
  • 20
    • 0027090115 scopus 로고
    • Mammalian genes induced by radiation; Activation of genes associated with growth control
    • Fornace AJ Jr: Mammalian genes induced by radiation; Activation of genes associated with growth control. Annu Rev Genet 26: 507-526, 1992
    • (1992) Annu Rev Genet , vol.26 , pp. 507-526
    • Fornace Jr., A.J.1
  • 21
    • 0026970404 scopus 로고
    • Nuclear factor κB: An oxidative stress-responsive transcription factor of eukaryotic cells
    • Schreck R, Albermann K, Baeuerle PA: Nuclear factor κB: An oxidative stress-responsive transcription factor of eukaryotic cells (a review). Free Radic Res Commun 17: 221-237, 1992
    • (1992) Free Radic Res Commun , vol.17 , pp. 221-237
    • Schreck, R.1    Albermann, K.2    Baeuerle, P.A.3
  • 22
    • 0023924345 scopus 로고
    • Induction of DNA replication and expression of proto-oncogene c-myc and c-fos in quiescent Balb/3T3 cells by xanthine/xanthine oxidase
    • 1988
    • Shibanuma M, Kuroki T, Nose K: (1988). Induction of DNA replication and expression of proto-oncogene c-myc and c-fos in quiescent Balb/3T3 cells by xanthine/xanthine oxidase. Oncogene 3: 17-21, 1988
    • (1988) Oncogene , vol.3 , pp. 17-21
    • Shibanuma, M.1    Kuroki, T.2    Nose, K.3
  • 23
    • 0023941812 scopus 로고
    • Oxidant stress induces the protooncogenes c-fos and c-myc in mouse epidermal cells
    • Crawford D, Zbinden I, Amstad P, Cerutti P: Oxidant stress induces the protooncogenes c-fos and c-myc in mouse epidermal cells. Oncogene 3: 27-32, 1988
    • (1988) Oncogene , vol.3 , pp. 27-32
    • Crawford, D.1    Zbinden, I.2    Amstad, P.3    Cerutti, P.4
  • 24
    • 0024582832 scopus 로고
    • Induction of fos RNA by DNA-damaging agents
    • Hollander MC, Fornace AJ Jr: Induction of fos RNA by DNA-damaging agents. Cancer Res 49: 1687-1692, 1989
    • (1989) Cancer Res , vol.49 , pp. 1687-1692
    • Hollander, M.C.1    Fornace Jr., A.J.2
  • 25
    • 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, 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
  • 26
    • 0026341905 scopus 로고
    • Rapid and preferential activation of the c-jun gene during the mammalian UV response
    • Devary Y, Gottlieb RA, Lau LF, Karin M: Rapid and preferential activation of the c-jun gene during the mammalian UV response. Mol Cell Biol 11: 2804-2811, 1991
    • (1991) Mol Cell Biol , vol.11 , pp. 2804-2811
    • Devary, Y.1    Gottlieb, R.A.2    Lau, L.F.3    Karin, M.4
  • 29
    • 0027269781 scopus 로고
    • 2 and antioxidants have opposite effects on activation of NF-κB and AP-1 in intact cells: AP-1 As a secondary antioxidant-responsive factor
    • 2 and antioxidants have opposite effects on activation of NF-κB and AP-1 in intact cells: AP-1 As a secondary antioxidant-responsive factor. EMBO J 12: 2005-2115, 1993
    • (1993) EMBO J , vol.12 , pp. 2005-2115
    • Meyer, M.1    Schreck, R.2    Baeuerle, P.A.3
  • 30
    • 0025720735 scopus 로고
    • The role of Jun, Fos and the AP-1 complex in cell-proliferation and Transformation
    • Angel P, 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
  • 31
    • 0001817670 scopus 로고
    • Dangerous liaisons: Fos and Jun, oncogenic transcription factors
    • SL Mcknight and KR Yamamoto (eds). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Curran T, Vogt PK: Dangerous liaisons: Fos and Jun, oncogenic transcription factors. In: SL Mcknight and KR Yamamoto (eds). Transcriptional Regulation. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1992, pp 797-831
    • (1992) Transcriptional Regulation , pp. 797-831
    • Curran, T.1    Vogt, P.K.2
  • 35
    • 0025953899 scopus 로고
    • Myc family oncogenes in the development of normal and neoplastic cells
    • Depinho RA, Schreiber-Agus N, Alt FW: Myc family oncogenes in the development of normal and neoplastic cells. Adv Cancer Res 57: 1-46, 1991
    • (1991) Adv Cancer Res , vol.57 , pp. 1-46
    • Depinho, R.A.1    Schreiber-Agus, N.2    Alt, F.W.3
  • 36
    • 0021041054 scopus 로고
    • Cell-specific regulation of the c-myc gene by lymphocyte mitogens and platelet-derived growth factor
    • Kelly K, Cochran BH, Stiles CD, Leder P: Cell-specific regulation of the c-myc gene by lymphocyte mitogens and platelet-derived growth factor. Cell 35: 603-610, 1983
    • (1983) Cell , vol.35 , pp. 603-610
    • Kelly, K.1    Cochran, B.H.2    Stiles, C.D.3    Leder, P.4
  • 37
    • 0024393228 scopus 로고
    • Regulation of expression of c-myc protooncogene in aclonal line of mouse lens epithelial cells by serum growth factors
    • Rao GN, Church RL: Regulation of expression of c-myc protooncogene in aclonal line of mouse lens epithelial cells by serum growth factors. Exp Cell Res 183: 140-148, 1989
    • (1989) Exp Cell Res , vol.183 , pp. 140-148
    • Rao, G.N.1    Church, R.L.2
  • 38
    • 0025286079 scopus 로고    scopus 로고
    • Regulation of expression of c-myc protooncogenes c-fos and c-myc expression by protein tyrosine kinase, protein kinase C, and cyclic AMP mitogenic pathways in dog primary thymocites: A positive and negative control by cyclic AMP on c-myc expression
    • Reuse S, Maenhaut C, Dumont JE: Regulation of expression of c-myc protooncogenes c-fos and c-myc expression by protein tyrosine kinase, protein kinase C, and cyclic AMP mitogenic pathways in dog primary thymocites: A positive and negative control by cyclic AMP on c-myc expression. Exp Cell Res 189: 33-44
    • Exp Cell Res , vol.189 , pp. 33-44
    • Reuse, S.1    Maenhaut, C.2    Dumont, J.E.3
  • 39
    • 0026588089 scopus 로고
    • Expression of c-fos and c-jun mRNA in the developing chicken lens: Relationship to cell proliferation, quiescence, and differentiation
    • Rinaudo JAS, Zelenka PS: Expression of c-fos and c-jun mRNA in the developing chicken lens: Relationship to cell proliferation, quiescence, and differentiation. Exp Cell Res 199: 147-153, 1992
    • (1992) Exp Cell Res , vol.199 , pp. 147-153
    • Rinaudo, J.A.S.1    Zelenka, P.S.2
  • 40
    • 0029070755 scopus 로고
    • Effects of c-jun and a negative dominant mutation of c jun on differentiation and gene expression in lens epithelial cell cells
    • Rinaudo JAS, Vachiano E, Zelenka PS: Effects of c-jun and a negative dominant mutation of c jun on differentiation and gene expression in lens epithelial cell cells. J Cell Biochem 58: 237-247, 1995
    • (1995) J Cell Biochem , vol.58 , pp. 237-247
    • Rinaudo, J.A.S.1    Vachiano, E.2    Zelenka, P.S.3
  • 41
    • 0023097070 scopus 로고
    • C-myc mRNA is elevated as differentiating lens cells withdraw from cell cycle
    • Nath P, Getzenberg R, Beebe D, Pallansch L, Zelenka P: c-myc mRNA is elevated as differentiating lens cells withdraw from cell cycle. Exp Cell Res. 169: 215-222, 1987
    • (1987) Exp Cell Res , vol.169 , pp. 215-222
    • Nath, P.1    Getzenberg, R.2    Beebe, D.3    Pallansch, L.4    Zelenka, P.5
  • 42
    • 0026646876 scopus 로고
    • Contrasting pattern of c-myc and N-myc expression in proliferating, quiescent, and differentiating cells of the embryonic chicken lens
    • Harris LL, Talian JC, Zelenka PZ: Contrasting pattern of c-myc and N-myc expression in proliferating, quiescent, and differentiating cells of the embryonic chicken lens. Development 115: 813-820, 1992
    • (1992) Development , vol.115 , pp. 813-820
    • Harris, L.L.1    Talian, J.C.2    Zelenka, P.Z.3
  • 43
    • 0026623167 scopus 로고
    • Expression of c-myc protooncogene in rat lens cells during development, maturation and reversal of galactose cataracts
    • Wen Y, Shu S, Unakar NJ, Bekhor I: Expression of c-myc protooncogene in rat lens cells during development, maturation and reversal of galactose cataracts. Mol Cell Biochem 112: 73-79, 1992
    • (1992) Mol Cell Biochem , vol.112 , pp. 73-79
    • Wen, Y.1    Shu, S.2    Unakar, N.J.3    Bekhor, I.4
  • 44
    • 0026708227 scopus 로고
    • Differential expression of c-myc and N-myc during oral organogenesis of the mouse embryo
    • Yamada S, Ikeda M, Eto K: Differential expression of c-myc and N-myc during oral organogenesis of the mouse embryo. Dev Growth Differ 34: 239-251, 1992
    • (1992) Dev Growth Differ , vol.34 , pp. 239-251
    • Yamada, S.1    Ikeda, M.2    Eto, K.3
  • 47
    • 0023631879 scopus 로고
    • Isolation and characterization of the c-fos (rat) cDNA and analysis of post-translational modification in vitro
    • Curran T, Gordon MB, Rubino KL, Sambucetti LC: Isolation and characterization of the c-fos (rat) cDNA and analysis of post-translational modification in vitro. Oncogene 2: 79-84, 1987
    • (1987) Oncogene , vol.2 , pp. 79-84
    • Curran, T.1    Gordon, M.B.2    Rubino, K.L.3    Sambucetti, L.C.4
  • 48
    • 0025217198 scopus 로고
    • Direct cloning of leucine zipper proteins: Jun binds cooperatively to the CRE with CRE-BP1
    • Macgregor PF, Abate C, Curran T: Direct cloning of leucine zipper proteins: Jun binds cooperatively to the CRE with CRE-BP1. Oncogene 5: 451-458, 1990
    • (1990) Oncogene , vol.5 , pp. 451-458
    • Macgregor, P.F.1    Abate, C.2    Curran, T.3
  • 49
    • 0021162032 scopus 로고
    • Nucleotide sequence comparison of normal and translocated murine c-myc genes
    • Stanton LW, Fahrlander PD, Tesser PM, Marcu KB: Nucleotide sequence comparison of normal and translocated murine c-myc genes. Nature 310: 423-425, 1984
    • (1984) Nature , vol.310 , pp. 423-425
    • Stanton, L.W.1    Fahrlander, P.D.2    Tesser, P.M.3    Marcu, K.B.4
  • 50
    • 0022423245 scopus 로고
    • Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: Genomic complexity and molecular evolution of the gene
    • Tso JY, Sun XH, Kao TH, Reece KS, Wu R: Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: Genomic complexity and molecular evolution of the gene. Nucleic Acids Res 13: 2485-2502, 1985
    • (1985) Nucleic Acids Res , vol.13 , pp. 2485-2502
    • Tso, J.Y.1    Sun, X.H.2    Kao, T.H.3    Reece, K.S.4    Wu, R.5
  • 52
    • 0020793569 scopus 로고
    • A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity
    • Feinberg AP, Vogelstein B: A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 132: 6-13, 1983
    • (1983) Anal Biochem , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 53
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162, 156-159, 1987
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 54
    • 0019061278 scopus 로고
    • Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose
    • Thomas PS : Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci USA 77: 5201-5205, 1980
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5201-5205
    • Thomas, P.S.1
  • 55
    • 0028033585 scopus 로고
    • The two duplicated insecticyanin genes, ins-a and ins-b are differentially expressed in the tobacco hornworm, Manduca sexta
    • Li W-C, Riddiford LM: The two duplicated insecticyanin genes, ins-a and ins-b are differentially expressed in the tobacco hornworm, Manduca sexta. Nucl Acids Res 22: 2945-2950, 1994
    • (1994) Nucl Acids Res , vol.22 , pp. 2945-2950
    • Li, W.-C.1    Riddiford, L.M.2
  • 56
    • 0023947899 scopus 로고
    • Evidence for positive and negative regulation in the promoter of the chicken δ-crystallin gene
    • Borras T, Peterson CA, Piatigorsky J: Evidence for positive and negative regulation in the promoter of the chicken δ-crystallin gene. Dev Biol 127, 209-219, 1988
    • (1988) Dev Biol , vol.127 , pp. 209-219
    • Borras, T.1    Peterson, C.A.2    Piatigorsky, J.3
  • 57
    • 0023392945 scopus 로고
    • High efficiency transformation of mammalian cells by plasmid DNA
    • Chen C, Okayama H: High efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7: 2745-2752, 1987
    • (1987) Mol Cell Biol , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 58
    • 0024829771 scopus 로고
    • Optimized use of the firefly luciferase assay as a reporter gene in mammalian cell lines
    • Brasier AR, Tate JE, Habener JF: Optimized use of the firefly luciferase assay as a reporter gene in mammalian cell lines. BioTechniques 7: 1116-1122, 1989
    • (1989) BioTechniques , vol.7 , pp. 1116-1122
    • Brasier, A.R.1    Tate, J.E.2    Habener, J.F.3
  • 60
    • 0023135497 scopus 로고
    • Interaction between two different regulatory elements activates the murine αA-crystallin gene promoter in explanted lens epithelia
    • Cheplinsky AB, Sommer B, Piatigorsky J: Interaction between two different regulatory elements activates the murine αA-crystallin gene promoter in explanted lens epithelia. Mol Cell Biol 7: 1807-1814, 1987
    • (1987) Mol Cell Biol , vol.7 , pp. 1807-1814
    • Cheplinsky, A.B.1    Sommer, B.2    Piatigorsky, J.3
  • 61
    • 0026343403 scopus 로고
    • Glutathione deficiency produced by inhibition of its synthesis and its reversal, applications in research and therapy
    • Meister A: Glutathione deficiency produced by inhibition of its synthesis and its reversal, applications in research and therapy. Pharmacol Therap 51: 155-194, 1991
    • (1991) Pharmacol Therap , vol.51 , pp. 155-194
    • Meister, A.1
  • 62
    • 0024497521 scopus 로고
    • Heine oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA-radiation, hydrogen peroxide and sodium arsenate
    • Keyse SM, Tyrrell RM: Heine oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA-radiation, hydrogen peroxide and sodium arsenate. Proc Natl Acad Sci USA 86: 99-103, 1989
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 63
    • 0025105624 scopus 로고
    • Oxidant stress leads to transcriptional activation of the human heme oxygenase gene in cultured skin fibroblasts
    • Keyse SM, Applegate LA, Tromvoukis Y, Tyrrell RM: Oxidant stress leads to transcriptional activation of the human heme oxygenase gene in cultured skin fibroblasts. Mol Cell Biol 10: 4967-4868, 1990
    • (1990) Mol Cell Biol , vol.10 , pp. 4967-14868
    • Keyse, S.M.1    Applegate, L.A.2    Tromvoukis, Y.3    Tyrrell, R.M.4
  • 65
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1
    • Schreck R, Albermann K, Baeuerle PA: Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J 10: 2247-2258, 1991
    • (1991) EMBO J , vol.10 , pp. 2247-2258
    • Schreck, R.1    Albermann, K.2    Baeuerle, P.A.3
  • 66
    • 0345371234 scopus 로고
    • Up-regulation of antioxidative gene expression in the lenses of emory mice subjected to oxidative stress
    • Bhuyan DK, Li W-C, Kuriakose G, Spector A, Bhuyan KC: Up-regulation of antioxidative gene expression in the lenses of emory mice subjected to oxidative stress. Invest Ophthalmol Vis Sci 36: S409, 1995
    • (1995) Invest Ophthalmol Vis Sci , vol.36
    • Bhuyan, D.K.1    Li, W.-C.2    Kuriakose, G.3    Spector, A.4    Bhuyan, K.C.5
  • 67
    • 0000117979 scopus 로고
    • Transcription regulation of crystallin genes: Cis elements, trans-factors, and signal transduction systems in the lens
    • Piatigorsky J, Zelenka PS: Transcription regulation of crystallin genes: Cis elements, trans-factors, and signal transduction systems in the lens. Adv Dev Biochem 1: 211-256, 1992
    • (1992) Adv Dev Biochem , vol.1 , pp. 211-256
    • Piatigorsky, J.1    Zelenka, P.S.2
  • 68
    • 0026695184 scopus 로고
    • Structure and lens expression of the gene encoding chicken βA3/A1-crystallin
    • McDermott JB, Paterson CA, Piatigorsky J: Structure and lens expression of the gene encoding chicken βA3/A1-crystallin. Gene 117: 193-200, 1992
    • (1992) Gene , vol.117 , pp. 193-200
    • McDermott, J.B.1    Paterson, C.A.2    Piatigorsky, J.3
  • 69
    • 0023625870 scopus 로고
    • Complete nucleotide sequence of the chicken αA-crystallin gene and its 5 flank sequence
    • Thompson MA, Hawkins JW, Piatigorsky J: Complete nucleotide sequence of the chicken αA-crystallin gene and its 5 flank sequence Gene 56: 173-184, 1987
    • (1987) Gene , vol.56 , pp. 173-184
    • Thompson, M.A.1    Hawkins, J.W.2    Piatigorsky, J.3
  • 70
    • 0027999510 scopus 로고
    • A complex array of positive and negative elements regulates the chicken αA-crystallin gene: Involvement of Pax-6, USF, CREB and/or CREM, and AP-1 proteins
    • Cvekl A, Sax CM, Brensnick EH, Piatigorsky J: A complex array of positive and negative elements regulates the chicken αA-crystallin gene: Involvement of Pax-6, USF, CREB and/or CREM, and AP-1 proteins. Mol Cell Biol 14: 7363-7376, 1994
    • (1994) Mol Cell Biol , vol.14 , pp. 7363-7376
    • Cvekl, A.1    Sax, C.M.2    Brensnick, E.H.3    Piatigorsky, J.4
  • 72
    • 0025077481 scopus 로고
    • Redox regulation of Fos and Jun DNA binding activity in vitro
    • Abate C, Patel L, Rauscher III FJ, 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 III, F.J.3    Curran, T.4
  • 73
    • 0026714672 scopus 로고
    • Redox-activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S, Miao G, Wang F, Pan YC, Curran T: Redox-activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO 111: 3323-3335, 1992
    • (1992) EMBO , vol.111 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 74
    • 0027324056 scopus 로고
    • Identification of residues in the human DNA repair enzyme HAP1 (Ref. [1]) that are essential for redox regulation of Jun DNA binding
    • Walker L J, Robson CN, Black E, Gillespie D, Hickson ID: Identification of residues in the human DNA repair enzyme HAP1 (Ref. [1]) that are essential for redox regulation of Jun DNA binding. Mol Cell Biol 13: 5370-5376, 1993
    • (1993) Mol Cell Biol , vol.13 , pp. 5370-5376
    • Walker, L.J.1    Robson, C.N.2    Black, E.3    Gillespie, D.4    Hickson, I.D.5
  • 75
    • 0028879873 scopus 로고
    • Myc but not Fos rescue of PDGF signaling blockage caused by kinase-inactive Src
    • Barone MV, Courtneidge SA: Myc but not Fos rescue of PDGF signaling blockage caused by kinase-inactive Src. Nature 378: 509-512, 1995
    • (1995) Nature , vol.378 , pp. 509-512
    • Barone, M.V.1    Courtneidge, S.A.2
  • 76
    • 0028982274 scopus 로고
    • ras as a common signaling target of reactive free radicals and cellular redox stress
    • ras as a common signaling target of reactive free radicals and cellular redox stress. J Biol Chem 270: 21195-21198, 1995
    • (1995) J Biol Chem , vol.270 , pp. 21195-21198
    • Lander, H.M.1    Ogiste, J.S.2    Teng, K.K.3    Novogrodsky, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.