메뉴 건너뛰기




Volumn 16, Issue 3, 1996, Pages 1035-1046

Physical and functional sensitivity of zinc finger transcription factors to redox change

Author keywords

[No Author keywords available]

Indexed keywords

TRANSCRIPTION FACTOR; ZINC FINGER PROTEIN;

EID: 0030042987     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.3.1035     Document Type: Article
Times cited : (183)

References (94)
  • 1
    • 0025077481 scopus 로고
    • Redox regulation of Fos and Jun DNA-binding activity in vitro
    • Abate, C., L. Patel, F. J. Rauscher, and T. Curran. 1990. Redox regulation of Fos and Jun DNA-binding activity in vitro. Science 249:1157-1161.
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher, F.J.3    Curran, T.4
  • 2
    • 0028061405 scopus 로고
    • Multiple elements within the 5′ distal enhancer of the mouse heme oxygenase-1 gene mediate induction by heavy metals
    • Alam, J. 1994. Multiple elements within the 5′ distal enhancer of the mouse heme oxygenase-1 gene mediate induction by heavy metals. J. Biol. Chem 269:25049-25056.
    • (1994) J. Biol. Chem , vol.269 , pp. 25049-25056
    • Alam, J.1
  • 3
    • 0027968491 scopus 로고
    • The DNA-binding efficiency of Sp1 is affected by redox changes
    • Ammendola, R., M. Mesuraca, T. Russo, and F. Cimino. 1994. The DNA-binding efficiency of Sp1 is affected by redox changes. Eur J Biochem. 225: 483-489.
    • (1994) Eur J Biochem. , vol.225 , pp. 483-489
    • Ammendola, R.1    Mesuraca, M.2    Russo, T.3    Cimino, F.4
  • 4
    • 0028006612 scopus 로고
    • Separation of oxidant-initiated and redox-regulated steps in the NF-κB signal transduction pathway
    • Anderson, M. T., F. J. T. Staal, C. Gitler, and L. A. Herzenberg. 1994 Separation of oxidant-initiated and redox-regulated steps in the NF-κB signal transduction pathway. Proc. Natl. Acad. Sci. USA 91:11527-11531
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11527-11531
    • Anderson, M.T.1    Staal, F.J.T.2    Gitler, C.3    Herzenberg, L.A.4
  • 5
    • 0025825989 scopus 로고
    • Redox regulation of a protein tyrosine kinase in the endoplasmic reticulum
    • Bauskin, A. R., I. Alkalay, and Y. Ben-Neriah. 1991. Redox regulation of a protein tyrosine kinase in the endoplasmic reticulum Cell 66:685-696.
    • (1991) Cell , vol.66 , pp. 685-696
    • Bauskin, A.R.1    Alkalay, I.2    Ben-Neriah, Y.3
  • 6
    • 0026497472 scopus 로고
    • Sp1 and the subfamily of zinc finger proteins with guanine-rich binding sites
    • Berg, J. M. 1992. Sp1 and the subfamily of zinc finger proteins with guanine-rich binding sites. Proc. Natl. Acad. Sci. USA 89:11109-11110.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11109-11110
    • Berg, J.M.1
  • 7
    • 0028008680 scopus 로고
    • Intracellular glutathione levels regulate Fos/Jun induction and activation of glutathione S-transferase gene expression
    • Bergelson, S., R. Pinkus, and V. Daniel. 1994. Intracellular glutathione levels regulate Fos/Jun induction and activation of glutathione S-transferase gene expression. Cancer Res. 54:36-40.
    • (1994) Cancer Res. , vol.54 , pp. 36-40
    • Bergelson, S.1    Pinkus, R.2    Daniel, V.3
  • 8
    • 9044253374 scopus 로고
    • Positive regulation of the skeletal α-actin gene by Fos and Jun
    • Bishopric, N. H., B. Sato, and K. A. Webster. 1992. Positive regulation of the skeletal α-actin gene by Fos and Jun. J. Biol. Chem 270:2567-2573.
    • (1992) J. Biol. Chem , vol.270 , pp. 2567-2573
    • Bishopric, N.H.1    Sato, B.2    Webster, K.A.3
  • 9
    • 0025889742 scopus 로고
    • Mithramycin inhibits Sp1 binding and selectively inhibits transcriptional activity of the dihydrofolate reductase gene in vitro and in vivo
    • Blume, S. W., R. C. Snyder, R. Ray, S. Thomas, C. A. Koller, and D. M. Miller. 1991. Mithramycin inhibits Sp1 binding and selectively inhibits transcriptional activity of the dihydrofolate reductase gene in vitro and in vivo J Clin Invest. 88:1613-1621.
    • (1991) J Clin Invest. , vol.88 , pp. 1613-1621
    • Blume, S.W.1    Snyder, R.C.2    Ray, R.3    Thomas, S.4    Koller, C.A.5    Miller, D.M.6
  • 10
    • 0027448981 scopus 로고
    • Three clustered Sp1 sites are required for efficient transcription of the TATA-less promoter of the gene for insulin-like growth factor-binding protein-2 from the rat
    • Boisclair, Y. R., A. L. Brown, S. Casola, and M. M. Rechler. 1993. Three clustered Sp1 sites are required for efficient transcription of the TATA-less promoter of the gene for insulin-like growth factor-binding protein-2 from the rat. J. Biol. Chem. 268:24892-24901.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24892-24901
    • Boisclair, Y.R.1    Brown, A.L.2    Casola, S.3    Rechler, M.M.4
  • 11
    • 0024205855 scopus 로고
    • Thiol/disulfide exchange between 3-hydroxy-3-methyglutaryl-CoA reductase and glutathione
    • Cappel, R. E., and H. F. Gilbert. 1988. Thiol/disulfide exchange between 3-hydroxy-3-methyglutaryl-CoA reductase and glutathione. J. Biol. Chem. 263:12204-12212.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12204-12212
    • Cappel, R.E.1    Gilbert, H.F.2
  • 12
    • 0027416753 scopus 로고
    • The Sp1 transcription factor binds the CD11b promoter specifically in myeloid cells in vivo and is essential for myeloid-specific promoter activity
    • Chen, H., H. L. Pahl, R. J. Scheibe, D. Zhang, and D. G. Tenen. 1993 The Sp1 transcription factor binds the CD11b promoter specifically in myeloid cells in vivo and is essential for myeloid-specific promoter activity. J. Biol Chem. 268:8230-8239
    • (1993) J. Biol Chem. , vol.268 , pp. 8230-8239
    • Chen, H.1    Pahl, H.L.2    Scheibe, R.J.3    Zhang, D.4    Tenen, D.G.5
  • 13
    • 0024811686 scopus 로고
    • Synergistic activation by the glutamine-rich domains of human transcription factor Sp1
    • Courey, A. J., D. A. Holtzman, S. P. Jackson, and R. Tjian. 1989. Synergistic activation by the glutamine-rich domains of human transcription factor Sp1 Cell 59:827-836.
    • (1989) Cell , vol.59 , pp. 827-836
    • Courey, A.J.1    Holtzman, D.A.2    Jackson, S.P.3    Tjian, R.4
  • 14
    • 0024276524 scopus 로고
    • Analysis of Sp1 in vivo reveals multiple transcriptional domains, including a novel glutamine-rich activation motif
    • Courey, A. J., and R. Tjian. 1988. Analysis of Sp1 in vivo reveals multiple transcriptional domains, including a novel glutamine-rich activation motif. Cell 55:887-898.
    • (1988) Cell , vol.55 , pp. 887-898
    • Courey, A.J.1    Tjian, R.2
  • 15
    • 0027771175 scopus 로고
    • Identification of oxygen regulatory elements in the 5′ flanking region of the human glutathione peroxidase gene
    • Cowan, D. B., R. D. Weisel, W. G. Williams, and D. A. Mickle. 1993 Identification of oxygen regulatory elements in the 5′ flanking region of the human glutathione peroxidase gene. J. Biol. Chem. 268:26904-26910.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26904-26910
    • Cowan, D.B.1    Weisel, R.D.2    Williams, W.G.3    Mickle, D.A.4
  • 16
    • 0026751187 scopus 로고
    • The regulation of glutathione peroxidase expression by oxygen tension in cultured human cardiomyocytes
    • Cowan, D. B., R. D. Weisel, W. G. Williams, and D. A. G. Mickle. 1992 The regulation of glutathione peroxidase expression by oxygen tension in cultured human cardiomyocytes. J. Mol. Cell Cardiol. 24:423-433.
    • (1992) J. Mol. Cell Cardiol. , vol.24 , pp. 423-433
    • Cowan, D.B.1    Weisel, R.D.2    Williams, W.G.3    Mickle, D.A.G.4
  • 17
    • 0025756918 scopus 로고
    • Enzymic mechanisms of superoxide production
    • Cross, A. R., and O. T. G. Jones. 1991. Enzymic mechanisms of superoxide production. Biochim. Biophys. Acta 1057:281-298.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 281-298
    • Cross, A.R.1    Jones, O.T.G.2
  • 18
    • 0026577610 scopus 로고
    • Regulation of tyrosine hydroxylase gene expression in the rat carotid body by hypoxia
    • Czyzyk-Krzeska, M., D. A. Bayliss, E. E. Lawson, and D. E. Millhorn. 1992. Regulation of tyrosine hydroxylase gene expression in the rat carotid body by hypoxia. J. Neurochem. 58:1538-1546.
    • (1992) J. Neurochem. , vol.58 , pp. 1538-1546
    • Czyzyk-Krzeska, M.1    Bayliss, D.A.2    Lawson, E.E.3    Millhorn, D.E.4
  • 19
    • 0028593507 scopus 로고
    • Transcriptional induction of the mouse metallothionine-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., R. D. Palmiter, and G. K. Andrews. 1994. Transcriptional induction of the mouse metallothionine-1 gene in hydrogen peroxide-treated Hepa cells involves a composite major late transcription factor/antioxidant response element and metal response promoter elements. Nucleic Acids Res. 22:5016-5023.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5016-5023
    • Dalton, T.1    Palmiter, R.D.2    Andrews, G.K.3
  • 20
    • 0024372988 scopus 로고
    • Regulation of the expression of the L-type pyruvate kinase gene in adult rat hepatocytes in primary culture
    • Decaux, J., B. Antoine, and A. Kahn. 1989. Regulation of the expression of the L-type pyruvate kinase gene in adult rat hepatocytes in primary culture. J. Biol. Chem. 264:11584-11590.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11584-11590
    • Decaux, J.1    Antoine, B.2    Kahn, A.3
  • 21
    • 0025721047 scopus 로고
    • Redox redux: The control of oxidative stress responses
    • Demple, B., and C. F. Amabile-Cuevas. 1991. Redox redux: the control of oxidative stress responses. Cell 67:837-839.
    • (1991) Cell , vol.67 , pp. 837-839
    • Demple, B.1    Amabile-Cuevas, C.F.2
  • 22
    • 0026742626 scopus 로고
    • Toward rules relating zinc finger protein sequences and DNA binding site preferences
    • Desjarlais, J. R., and J. M. Berg. 1992. Toward rules relating zinc finger protein sequences and DNA binding site preferences. Proc. Natl. Acad. Sci. USA 89:7345-7349.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7345-7349
    • Desjarlais, J.R.1    Berg, J.M.2
  • 23
    • 0026341905 scopus 로고
    • Rapid and preferential activation of the c-jun gene during the mammalian UV response
    • Devary, Y., R. A. Gottlieb, L. F. Lau, and M. Karin. 1991. Rapid and preferential activation of the c-jun gene during the mammalian UV response. Mol. Cell. Biol. 11:2804-2811.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2804-2811
    • Devary, Y.1    Gottlieb, R.A.2    Lau, L.F.3    Karin, M.4
  • 24
    • 0027049804 scopus 로고
    • The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases
    • Devary, Y., R. A. Gottlieb, T. Smeal, and M. Karin. 1992. The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases. Cell 71: 1081-1091.
    • (1992) Cell , vol.71 , pp. 1081-1091
    • Devary, Y.1    Gottlieb, R.A.2    Smeal, T.3    Karin, M.4
  • 25
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., R. M. Lebovitz, and R. Roeder. 1983 Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei Nucleic Acids Res. 11:1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.3
  • 26
    • 0023857830 scopus 로고
    • Zinc fingers: Guilt by association
    • Evans, R. M., and S. M. Hollenberg. 1988. Zinc fingers: guilt by association. Cell 52:1-3.
    • (1988) Cell , vol.52 , pp. 1-3
    • Evans, R.M.1    Hollenberg, S.M.2
  • 27
    • 0027238681 scopus 로고
    • Two different, overlapping pathways of transcription initiation are active on the TATA-less human androgen receptor promoter
    • Faber, P. W., H. C. J. van Rooij, H. J. Schipper, A. O. Brinkmann, and J. Trapman. 1993. Two different, overlapping pathways of transcription initiation are active on the TATA-less human androgen receptor promoter. J. Biol Chem. 268:9296-9301.
    • (1993) J. Biol Chem. , vol.268 , pp. 9296-9301
    • Faber, P.W.1    Van Rooij, H.C.J.2    Schipper, H.J.3    Brinkmann, A.O.4    Trapman, J.5
  • 28
    • 0028359320 scopus 로고
    • Oxygen-regulated control elements in the phosphoglycerate kinase and lactate dehydrogenase A genes: Similarities with the erythropoietin 3′ enhancer
    • Firth, J. D., B. L. Ebert, C. W. Pugh, and P. J. Ratclifle. 1994. Oxygen-regulated control elements in the phosphoglycerate kinase and lactate dehydrogenase A genes: similarities with the erythropoietin 3′ enhancer. Proc. Natl. Acad. Sci. USA 91:6496-6500.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6496-6500
    • Firth, J.D.1    Ebert, B.L.2    Pugh, C.W.3    Ratclifle, P.J.4
  • 29
    • 0348230014 scopus 로고
    • Reactive oxygen species and antioxidant vitamins: Mechanisms of action
    • Frei, B. 1994. Reactive oxygen species and antioxidant vitamins: mechanisms of action. Am. J. Med. 97(Suppl. 3A):5S-13S.
    • (1994) Am. J. Med. , vol.97 , Issue.SUPPL. 3A
    • Frei, B.1
  • 30
    • 0027185251 scopus 로고
    • Cooperative DNA binding of the human HoxB5 (Hox-2 1) protein is under redox regulation in vitro
    • Galang, C. K., and C. A. Hauser. 1993. Cooperative DNA binding of the human HoxB5 (Hox-2 1) protein is under redox regulation in vitro. Mol. Cell. Biol. 13:4609-4617.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4609-4617
    • Galang, C.K.1    Hauser, C.A.2
  • 31
    • 0028036190 scopus 로고
    • II110 component of the Drosophila TFIID complex and mediates transcriptional activation
    • II110 component of the Drosophila TFIID complex and mediates transcriptional activation. Proc. Natl. Acad. Sci. USA 91:192-196.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 192-196
    • Gill, G.1    Pascal, E.2    Tseng, Z.H.3    Tjian, R.4
  • 34
    • 0027361046 scopus 로고
    • Redox modulation of p53 conformation and sequence-specific DNA binding in vitro
    • Hainaut, P., and J. Milner. 1993. Redox modulation of p53 conformation and sequence-specific DNA binding in vitro. Cancer Res. 53:4469-4473.
    • (1993) Cancer Res. , vol.53 , pp. 4469-4473
    • Hainaut, P.1    Milner, J.2
  • 35
    • 0024516594 scopus 로고
    • Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction
    • Hentze, M. W., T. A. Rouault, J. B. Harford, and R. D. Klausner. 1989. Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction. Science 244:357-359.
    • (1989) Science , vol.244 , pp. 357-359
    • Hentze, M.W.1    Rouault, T.A.2    Harford, J.B.3    Klausner, R.D.4
  • 36
    • 0028167278 scopus 로고
    • The degradation of phosphoenolpyruvate carboxykinase (GTP) mRNA is regulated by cyclic AMP but not by dexamethasone
    • Hod, Y. 1994. The degradation of phosphoenolpyruvate carboxykinase (GTP) mRNA is regulated by cyclic AMP but not by dexamethasone. Arch. Biochem Biophys. 308:82-88.
    • (1994) Arch. Biochem Biophys. , vol.308 , pp. 82-88
    • Hod, Y.1
  • 37
    • 0027456704 scopus 로고
    • Characterization of the DNA-binding properties of the early growth response-1 (Egr-1) transcription factor: Evidence for modulation by a redox mechanism
    • Huang, R., and E. D. Adamson. 1993. Characterization of the DNA-binding properties of the early growth response-1 (Egr-1) transcription factor: evidence for modulation by a redox mechanism. DNA Cell Biol. 12:265-273.
    • (1993) DNA Cell Biol. , vol.12 , pp. 265-273
    • Huang, R.1    Adamson, E.D.2
  • 38
    • 0028023597 scopus 로고
    • Antioxidant response element
    • Jaiswal, A. K. 1994. Antioxidant response element. Biochem. Pharmacol. 28: 439-444.
    • (1994) Biochem. Pharmacol. , vol.28 , pp. 439-444
    • Jaiswal, A.K.1
  • 39
    • 0023066977 scopus 로고
    • Spectrophotometric assay of thiols
    • Jocelyn, P. C. 1987 Spectrophotometric assay of thiols. Methods Enzymol. 143:44-50.
    • (1987) Methods Enzymol. , vol.143 , pp. 44-50
    • Jocelyn, P.C.1
  • 41
    • 0023663884 scopus 로고
    • Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain
    • Kadonaga, J. T., K. R. Carner, F. R. Masiarz, and R. Tjian. 1987. Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain. Cell 51:1079-1090.
    • (1987) Cell , vol.51 , pp. 1079-1090
    • Kadonaga, J.T.1    Carner, K.R.2    Masiarz, F.R.3    Tjian, R.4
  • 42
    • 0019932125 scopus 로고
    • Human metallothionine genes, primary structure of the metallothionine-II gene and a related processed gene
    • Karin, M., and R. I. Richard. 1982. Human metallothionine genes, primary structure of the metallothionine-II gene and a related processed gene. Nature (London) 299:797-802.
    • (1982) Nature (London) , vol.299 , pp. 797-802
    • Karin, M.1    Richard, R.I.2
  • 43
    • 0025959037 scopus 로고
    • Fnr mutants that activate gene expression in the presence of oxygen
    • Kiley, P. J., and W. S. Resnikoff. 1991. Fnr mutants that activate gene expression in the presence of oxygen. J. Bacteriol. 173:16-22.
    • (1991) J. Bacteriol. , vol.173 , pp. 16-22
    • Kiley, P.J.1    Resnikoff, W.S.2
  • 45
    • 0026086319 scopus 로고
    • Ishemic induction of protooncogene expression in gerbil brain
    • Kindy, M. S., J. P. Carney, R. J. Dempsey, and J. M. Carney. 1991. Ishemic induction of protooncogene expression in gerbil brain. J. Mol. Neurosci. 2: 217-228.
    • (1991) J. Mol. Neurosci. , vol.2 , pp. 217-228
    • Kindy, M.S.1    Carney, J.P.2    Dempsey, R.J.3    Carney, J.M.4
  • 46
    • 0026756135 scopus 로고
    • Cloning of GT box-binding proteins: A novel Sp1 multigene family regulating T-cell receptor gene expression
    • Kingsley, C., and A. Winoto. 1992. Cloning of GT box-binding proteins: a novel Sp1 multigene family regulating T-cell receptor gene expression. Mol. Cell Biol. 12:4251-4261.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 4251-4261
    • Kingsley, C.1    Winoto, A.2
  • 47
    • 0024326951 scopus 로고
    • Cis-trans models for post-transcriptional gene regulation
    • Klausner, R. D., and J. B. Harford. 1989. Cis-trans models for post-transcriptional gene regulation. Science 246:870-872.
    • (1989) Science , vol.246 , pp. 870-872
    • Klausner, R.D.1    Harford, J.B.2
  • 48
    • 0028290479 scopus 로고
    • Role of zinc-coordination and the glutathione redox couple in the redox susceptibility of human transcription factor Sp1
    • Knoepfel, L., C. Steinkuhler, M. Carri, and G. Rotilio. 1994 Role of zinc-coordination and the glutathione redox couple in the redox susceptibility of human transcription factor Sp1. Biochem. Biophys. Res. Commun. 201: 871-877.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 871-877
    • Knoepfel, L.1    Steinkuhler, C.2    Carri, M.3    Rotilio, G.4
  • 49
    • 0026754698 scopus 로고
    • Sequence-specific recognition of DNA by zinc-finger peptides derived from the transcription factor Sp1
    • Kriwachi, R. W., S. C. Schultz, T. A. Steitz, and J. P. Caradonna. 1992. Sequence-specific recognition of DNA by zinc-finger peptides derived from the transcription factor Sp1. Proc. Natl Acad. Sci. USA 89:9759-9763.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9759-9763
    • Kriwachi, R.W.1    Schultz, S.C.2    Steitz, T.A.3    Caradonna, J.P.4
  • 50
    • 0021259402 scopus 로고
    • Dihydrofolate reductase gene expression in cultured mouse cells is regulated by transcript stabilization in the nucleus
    • Leys, E. J., G. F. Crouse, and R. E. Kellems. 1984. Dihydrofolate reductase gene expression in cultured mouse cells is regulated by transcript stabilization in the nucleus J. Cell Biol. 99:180-187.
    • (1984) J. Cell Biol. , vol.99 , pp. 180-187
    • Leys, E.J.1    Crouse, G.F.2    Kellems, R.E.3
  • 51
    • 0027466893 scopus 로고
    • Transcriptional regulation of the pyruvate kinase erythroid-specific promoter
    • Max-Audit, I., J. Eleouet, and P. Romeo. 1993. Transcriptional regulation of the pyruvate kinase erythroid-specific promoter. J. Biol. Chem. 268:5431-5437
    • (1993) J. Biol. Chem. , vol.268 , pp. 5431-5437
    • Max-Audit, I.1    Eleouet, J.2    Romeo, P.3
  • 52
    • 0027461553 scopus 로고
    • Inducible operation of the erythropoietin 3′ enhancer in multiple cell lines: Evidence for a wide-spread oxygen-sensing mechanism
    • Maxwell, P. H., C. W. Pugh, and P. J. Ratcliffe. 1993. Inducible operation of the erythropoietin 3′ enhancer in multiple cell lines: evidence for a wide-spread oxygen-sensing mechanism Proc. Natl. Acad. Sci. USA 90:2423-2427.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2423-2427
    • Maxwell, P.H.1    Pugh, C.W.2    Ratcliffe, P.J.3
  • 53
    • 0026774217 scopus 로고
    • Conserved cysteine residue in the DNA-binding domain of the bovine papillomavirus type 1 E2 protein confers redox regulation of the DNA-binding activity in vitro
    • McBride, A. A., R. D. Klausner, and P. M. Howley. 1992. Conserved cysteine residue in the DNA-binding domain of the bovine papillomavirus type 1 E2 protein confers redox regulation of the DNA-binding activity in vitro. Proc. Natl Acad. Sci. USA 89:7531-7535.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7531-7535
    • McBride, A.A.1    Klausner, R.D.2    Howley, P.M.3
  • 54
    • 0023277174 scopus 로고
    • Oxygen-derived free radicals: A link between reperfusion injury and inflammation
    • McCord, J. M. 1987. Oxygen-derived free radicals: a link between reperfusion injury and inflammation Fed. Proc. 46:2401-2406.
    • (1987) Fed. Proc. , vol.46 , pp. 2401-2406
    • McCord, J.M.1
  • 55
    • 0028283186 scopus 로고
    • Transcription factor GATA-4 regulates cardiac muscle-specific expression of the alpha-myosin heavy-chain gene
    • Molkentin, J. D., D. V. Kahakolanu, and B. E. Markham. 1994. Transcription factor GATA-4 regulates cardiac muscle-specific expression of the alpha-myosin heavy-chain gene. Mol. Cell. Biol. 14:4947-4957.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4947-4957
    • Molkentin, J.D.1    Kahakolanu, D.V.2    Markham, B.E.3
  • 56
    • 0028077621 scopus 로고
    • Metallothionine IIA is up-regulated by hypoxia in human A431 squamous carcinoma cells
    • Murphy, B. J., K. R. Laderoute, R. J. Chin, and R. M. Sutherland. 1994. Metallothionine IIA is up-regulated by hypoxia in human A431 squamous carcinoma cells. Cancer Res. 54:5808-5810.
    • (1994) Cancer Res. , vol.54 , pp. 5808-5810
    • Murphy, B.J.1    Laderoute, K.R.2    Chin, R.J.3    Sutherland, R.M.4
  • 57
    • 0025305575 scopus 로고
    • Polymerase chain reaction based assay to detect allelic loss in human DNA
    • Neubauer, A., B. Neubauer, and E. Liu. 1991. Polymerase chain reaction based assay to detect allelic loss in human DNA. Nucleic Acids Res. 18: 993-998
    • (1991) Nucleic Acids Res. , vol.18 , pp. 993-998
    • Neubauer, A.1    Neubauer, B.2    Liu, E.3
  • 58
    • 0025906411 scopus 로고
    • Cerebral ischemia induces transient intracellular redistribution and intranuclear translocation of the raf proto-oncogene product in hippocampal pyramidal cells
    • Olah, Z., S. Komoly, N. Nagashima, F. Joo, U. R. Rapp, and W. B. Anderson. 1991. Cerebral ischemia induces transient intracellular redistribution and intranuclear translocation of the raf proto-oncogene product in hippocampal pyramidal cells. Exp. Brain Res. 84:403-410.
    • (1991) Exp. Brain Res. , vol.84 , pp. 403-410
    • Olah, Z.1    Komoly, S.2    Nagashima, N.3    Joo, F.4    Rapp, U.R.5    Anderson, W.B.6
  • 59
    • 0025853524 scopus 로고
    • Molecular structure of the human muscle-specific enolase gene (ENO3)
    • Peshavaria, M., and I. N. M. Day. 1991. Molecular structure of the human muscle-specific enolase gene (ENO3). Biochem. J. 275:427-433.
    • (1991) Biochem. J. , vol.275 , pp. 427-433
    • Peshavaria, M.1    Day, I.N.M.2
  • 60
    • 0026473086 scopus 로고
    • The helix-loop-helix repeat transcription factor USF can be functionally regulated in a redox-dependent manner
    • Pognonec, P., H. Kato, and R. G. Roeder. 1992. The helix-loop-helix repeat transcription factor USF can be functionally regulated in a redox-dependent manner. J. Biol Chem 267:24563-24567.
    • (1992) J. Biol Chem , vol.267 , pp. 24563-24567
    • Pognonec, P.1    Kato, H.2    Roeder, R.G.3
  • 61
    • 0025228088 scopus 로고
    • Mithramycin selectively inhibits the transcriptional activity of a transfected c-myc gene
    • Ray, R., S. Thomas, and D. M. Miller. 1990. Mithramycin selectively inhibits the transcriptional activity of a transfected c-myc gene. Am J. Med. Sci 299: 203-208
    • (1990) Am J. Med. Sci , vol.299 , pp. 203-208
    • Ray, R.1    Thomas, S.2    Miller, D.M.3
  • 62
    • 0027547987 scopus 로고
    • Zinc fingers
    • Rhodes, D., and A. Klug. 1993. Zinc fingers Sci. Am. 268:56-65.
    • (1993) Sci. Am. , vol.268 , pp. 56-65
    • Rhodes, D.1    Klug, A.2
  • 65
    • 0027301258 scopus 로고
    • Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor-a and immunoglobulin G
    • Satriano, J. A., M. Shuldiner, K. Hora, Y. Xing, Z. Shan, and D. Schlondorff. 1993. Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor-a and immunoglobulin G. J. Clin. Invest. 92:1564-1571.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1564-1571
    • Satriano, J.A.1    Shuldiner, M.2    Hora, K.3    Xing, Y.4    Shan, Z.5    Schlondorff, D.6
  • 66
    • 0028344541 scopus 로고
    • Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-κB and AP-1
    • Schenk, H., M. Klein, W. Erdbrugger, W. Droge, and K. Schulze-Osthoff. 1994. Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-κB and AP-1. Proc. Natl. Acad. Sci. USA 91:1672-1676.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1672-1676
    • Schenk, H.1    Klein, M.2    Erdbrugger, W.3    Droge, W.4    Schulze-Osthoff, K.5
  • 67
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NK-κB transcription factor and HIV-1
    • Schreck, R., P. Rieber, and P. A. Baeuerle. 1991. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NK-κB transcription factor and HIV-1. EMBO J. 10:2247-2258.
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 68
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1
    • Semenza, G. L., P. H. Roth, H.-M. Fang, and G. L. Wang. 1994 Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1. J Biol. Chem. 269:23757-23763
    • (1994) J Biol. Chem. , vol.269 , pp. 23757-23763
    • Semenza, G.L.1    Roth, P.H.2    Fang, H.-M.3    Wang, G.L.4
  • 69
    • 0027373948 scopus 로고
    • Interaction between transcription factors Sp1 and YY1
    • Seto, E., B. Lewis, and T. Shenk. 1993. Interaction between transcription factors Sp1 and YY1. Nature (London) 365:462-464
    • (1993) Nature (London) , vol.365 , pp. 462-464
    • Seto, E.1    Lewis, B.2    Shenk, T.3
  • 70
    • 0027056464 scopus 로고
    • Oxygen modulates prostacyclin synthesis in ovine fetal pulmonary arteries by an effect on cyclooxygenase
    • Shaul, P. W., W. B. Campbell, M. A. Farrar, and R. R. Magness. 1992. Oxygen modulates prostacyclin synthesis in ovine fetal pulmonary arteries by an effect on cyclooxygenase. J. Clin. Invest. 90:2147-2155.
    • (1992) J. Clin. Invest. , vol.90 , pp. 2147-2155
    • Shaul, P.W.1    Campbell, W.B.2    Farrar, M.A.3    Magness, R.R.4
  • 71
    • 0021361028 scopus 로고
    • Rapid action of insulin and cyclic AMP in the regulation of functional messenger RNA coding for glucokinase in rat liver
    • Sibrowski, W., and H. J. Seitz. 1984. Rapid action of insulin and cyclic AMP in the regulation of functional messenger RNA coding for glucokinase in rat liver J. Biol. Chem. 259:343-346.
    • (1984) J. Biol. Chem. , vol.259 , pp. 343-346
    • Sibrowski, W.1    Seitz, H.J.2
  • 72
    • 0019877708 scopus 로고
    • Electrostatic influence of local cysteine environments on disulfide exchange kinetics
    • Snyder, G. H., M. J. Cennerazzo, A. J. Karalis, and D. Field. 1981 Electrostatic influence of local cysteine environments on disulfide exchange kinetics. Biochemistry 20:6509-6518.
    • (1981) Biochemistry , vol.20 , pp. 6509-6518
    • Snyder, G.H.1    Cennerazzo, M.J.2    Karalis, A.J.3    Field, D.4
  • 73
    • 0025214474 scopus 로고
    • Transcriptional regulation of oxidative stress-inducible genes: Direct activation by oxidation
    • Storz, G., L. A. Tartaglia, and B. N. Ames. 1990. Transcriptional regulation of oxidative stress-inducible genes: direct activation by oxidation. Science 248:189-194.
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 74
    • 0024404661 scopus 로고
    • Functional analysis of GC element binding and transcription in the hamster dihydrofolate reductase gene promoter
    • Swick, A. G., M. C. Blake, J. W. Kahn, and J. C. Azizkhan. 1989 Functional analysis of GC element binding and transcription in the hamster dihydrofolate reductase gene promoter. Nucleic Acids. Res. 17:9291-9304.
    • (1989) Nucleic Acids. Res. , vol.17 , pp. 9291-9304
    • Swick, A.G.1    Blake, M.C.2    Kahn, J.W.3    Azizkhan, J.C.4
  • 75
    • 0028842013 scopus 로고
    • Regulation of the myoblast-specific expression of the human β-enolase gene
    • Taylor, J. M., J. D. Davies, and C. A. Peterson. 1995. Regulation of the myoblast-specific expression of the human β-enolase gene. J. Biol. Chem. 270:2535-2540.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2535-2540
    • Taylor, J.M.1    Davies, J.D.2    Peterson, C.A.3
  • 77
    • 0028023175 scopus 로고
    • Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: A mechanism for differential promoter selection
    • Toledano, M. B., I. Kullik, F. Trinh, P. T. Baird, T. D. Schneider, and G. Storz. 1994. Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection. Cell 78:897-909.
    • (1994) Cell , vol.78 , pp. 897-909
    • Toledano, M.B.1    Kullik, I.2    Trinh, F.3    Baird, P.T.4    Schneider, T.D.5    Storz, G.6
  • 78
    • 0025852479 scopus 로고
    • Modulation of transcription factor NF-κB binding activity by oxidation-reduction in vitro
    • Toledano, M. B., and W. J. Leonard. 1991. Modulation of transcription factor NF-κB binding activity by oxidation-reduction in vitro. Proc. Natl. Acad. Sci. USA 88:4328-4332.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4328-4332
    • Toledano, M.B.1    Leonard, W.J.2
  • 79
    • 0027287614 scopus 로고
    • The proximal promoter region of the human heme oxygenase gene contains elements involved in stimulation of transcriptional activity by a variety of agents including oxidants
    • Tyrrell, R. M., L. A. Appelgate, and Y. Tromvoukis. 1993 The proximal promoter region of the human heme oxygenase gene contains elements involved in stimulation of transcriptional activity by a variety of agents including oxidants. Carcinogenesis 14:1-6.
    • (1993) Carcinogenesis , vol.14 , pp. 1-6
    • Tyrrell, R.M.1    Appelgate, L.A.2    Tromvoukis, Y.3
  • 80
    • 0028227648 scopus 로고
    • Cellular thiols as a determinant of responsiveness to menadione in cardiomyocytes
    • Tzeng, W., T. Chiou, C. Wang, J. Lee, and Y. Chen. 1994 Cellular thiols as a determinant of responsiveness to menadione in cardiomyocytes. J. Mol. Cell Cardiol. 26:889-897
    • (1994) J. Mol. Cell Cardiol. , vol.26 , pp. 889-897
    • Tzeng, W.1    Chiou, T.2    Wang, C.3    Lee, J.4    Chen, Y.5
  • 81
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee, B. L., and D. S. Auld. 1990 Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29:5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 82
    • 0027210562 scopus 로고
    • General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia
    • Wang, G. L., and G. L. Semenza. 1993. General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia Proc. Natl. Acad. Sci. USA 90:4304-4308.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4304-4308
    • Wang, G.L.1    Semenza, G.L.2
  • 83
    • 0023405817 scopus 로고
    • Regulation of glycolytic enzyme RNA transcriptional rates by oxygen availability in skeletal muscle cells Mol
    • Webster, K. A. 1987. Regulation of glycolytic enzyme RNA transcriptional rates by oxygen availability in skeletal muscle cells Mol. Cell. Biochem. 77: 19-28.
    • (1987) Cell. Biochem. , vol.77 , pp. 19-28
    • Webster, K.A.1
  • 84
    • 0027257482 scopus 로고
    • Induction and nuclear accumulation of fos and jun proto-oncogenes in hypoxia cardiac myocytes
    • Webster, K. A., D. Discher, and N. H. Bishopric. 1993. Induction and nuclear accumulation of fos and jun proto-oncogenes in hypoxia cardiac myocytes. J Biol. Chem. 258:16852-16859.
    • (1993) J Biol. Chem. , vol.258 , pp. 16852-16859
    • Webster, K.A.1    Discher, D.2    Bishopric, N.H.3
  • 85
    • 0010728074 scopus 로고
    • Regulation of fos and jun immediate-early genes by redox or metabolic stress in cardiac myocytes
    • Webster, K. A., D. J. Discher, and N. H. Bishopric. 1994. Regulation of fos and jun immediate-early genes by redox or metabolic stress in cardiac myocytes. Circ. Res. 75:361-371.
    • (1994) Circ. Res. , vol.75 , pp. 361-371
    • Webster, K.A.1    Discher, D.J.2    Bishopric, N.H.3
  • 86
    • 0025272210 scopus 로고
    • The c-fos cyclic AMP-responsive element conveys constitutive expression to a tissue-specific promoter
    • Webster, K. A., and L. Kedes. 1990. The c-fos cyclic AMP-responsive element conveys constitutive expression to a tissue-specific promoter. Mol Cell Biol. 10:2402-2406.
    • (1990) Mol Cell Biol. , vol.10 , pp. 2402-2406
    • Webster, K.A.1    Kedes, L.2
  • 87
    • 0023939652 scopus 로고
    • Adenovirus E1A products suppress myogenic differentiation and inhibit transcription from muscle-specific promoters
    • Webster, K. A., G. E. O. Muscat, and L. Kedes. 1988 Adenovirus E1A products suppress myogenic differentiation and inhibit transcription from muscle-specific promoters. Nature (London) 332:553-561.
    • (1988) Nature (London) , vol.332 , pp. 553-561
    • Webster, K.A.1    Muscat, G.E.O.2    Kedes, L.3
  • 88
    • 0025248740 scopus 로고
    • Free radicals and ischemic tissue injury
    • Werns, S. W., and R. Lucchesi. 1990. Free radicals and ischemic tissue injury Trends Physiol. Sci. 11:161-166.
    • (1990) Trends Physiol. Sci. , vol.11 , pp. 161-166
    • Werns, S.W.1    Lucchesi, R.2
  • 89
    • 15844370979 scopus 로고
    • Zinc fingers are redox sensors during acute oxidative stress
    • Wu, X., et al. 1994. Zinc fingers are redox sensors during acute oxidative stress. Circulation 90:I-250.
    • (1994) Circulation , vol.90
    • Wu, X.1
  • 90
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis, S., G. Miao, F. Wang, Y. E. Pan, and T. Curran. 1992. Redox activation of Fos-Jun binding activity is mediated by a DNA repair enzyme EMBO J. 11:3323-3335.
    • (1992) EMBO J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.E.4    Curran, T.5
  • 91
    • 0028058086 scopus 로고
    • The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains
    • Xanthoudakis, S., G. G. Miao, and T. Curran. 1994. The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains. Proc Natl. Acad. Sci. USA 91:23-27.
    • (1994) Proc Natl. Acad. Sci. USA , vol.91 , pp. 23-27
    • Xanthoudakis, S.1    Miao, G.G.2    Curran, T.3
  • 92
    • 0027338196 scopus 로고
    • T3 receptor suppression of Sp-1-dependent transcription from the epidermal growth factor receptor promoter via overlapping DNA-binding sites
    • Xu, J., K. L. Thompson, L. B. Shephard, L. G. Hudson, and G. N. Gill. 1993 T3 receptor suppression of Sp-1-dependent transcription from the epidermal growth factor receptor promoter via overlapping DNA-binding sites. J. Biol Chem. 268:16065-16073.
    • (1993) J. Biol Chem. , vol.268 , pp. 16065-16073
    • Xu, J.1    Thompson, K.L.2    Shephard, L.B.3    Hudson, L.G.4    Gill, G.N.5
  • 93
    • 0017361716 scopus 로고
    • A myogenic cell line with altered serum requirements for differentiation
    • Yaffe, D., and O. Saxel. 1977. A myogenic cell line with altered serum requirements for differentiation. Differentiation 7:159-166
    • (1977) Differentiation , vol.7 , pp. 159-166
    • Yaffe, D.1    Saxel, O.2
  • 94
    • 0025976912 scopus 로고
    • Thionein can modulate DNA binding and transcription activation by zinc finger containing factor Sp1
    • Zeng, J., R. Heuchel, W. Schaffner, and J. H. R. Kagi. 1991. Thionein can modulate DNA binding and transcription activation by zinc finger containing factor Sp1. FEBS Lett. 279:310-312.
    • (1991) FEBS Lett. , vol.279 , pp. 310-312
    • Zeng, J.1    Heuchel, R.2    Schaffner, W.3    Kagi, J.H.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.