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Volumn 21, Issue 3, 1996, Pages 335-348

Redox regulation of transcriptional activators

Author keywords

AP 1; Free radicals; NF B; p53; Redox regulation; Transcription factors activators

Indexed keywords

AROMATIC HYDROCARBON RECEPTOR; GLUCOCORTICOID RECEPTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; ONCOPROTEIN; OXIDIZING AGENT; PROTEIN P53; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR SP1;

EID: 0029760957     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/0891-5849(96)00109-8     Document Type: Review
Times cited : (633)

References (133)
  • 1
    • 0025158520 scopus 로고
    • Transcription regulating proteins and their recognition sequences
    • 1. Wingender, E. Transcription regulating proteins and their recognition sequences. Eukaryotic Gene Exp. 1:11-48; 1990.
    • (1990) Eukaryotic Gene Exp. , vol.1 , pp. 11-48
    • Wingender, E.1
  • 2
    • 0028291252 scopus 로고
    • The basics of basal transcription by RNA polymerase II
    • 2. Buratowski, S. The basics of basal transcription by RNA polymerase II. Cell 77:1-3; 1994.
    • (1994) Cell , vol.77 , pp. 1-3
    • Buratowski, S.1
  • 3
    • 0027354762 scopus 로고
    • Initiation of transcription by RNA polymerase II: A multi-step process
    • 3. Zawel, L.; Reinberg, D. Initiation of transcription by RNA polymerase II: A multi-step process. Prog. Nucleic Acid Res. Mol. Biol. 44:67-108; 1993.
    • (1993) Prog. Nucleic Acid Res. Mol. Biol. , vol.44 , pp. 67-108
    • Zawel, L.1    Reinberg, D.2
  • 4
    • 0025865317 scopus 로고
    • The inducible transcription activator NF-κB: Regulation by distinct protein subunits
    • 4. Baeuerle, P. A. The inducible transcription activator NF-κB: Regulation by distinct protein subunits. Biochim. Biophys. Acta 1072:63-80; 1991.
    • (1991) Biochim. Biophys. Acta , vol.1072 , pp. 63-80
    • Baeuerle, P.A.1
  • 5
    • 0026559568 scopus 로고
    • Regulating transcription factor activity by phosphorylation
    • 5. Jackson, S. P. Regulating transcription factor activity by phosphorylation. Trends Cell Biol. 2:104-108; 1992.
    • (1992) Trends Cell Biol. , vol.2 , pp. 104-108
    • Jackson, S.P.1
  • 6
    • 0025126386 scopus 로고
    • Jun: Oncogene and transcription factor
    • 6. Vogt, P. K.; Bos, T. J. Jun: Oncogene and transcription factor. Adv. Cancer Res. 55:1-35; 1990.
    • (1990) Adv. Cancer Res. , vol.55 , pp. 1-35
    • Vogt, P.K.1    Bos, T.J.2
  • 7
    • 0025720735 scopus 로고
    • The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation
    • 7. Angel, P.; Karin, M. The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation. Biochim. Biophys. Acta 1072:129-157; 1991.
    • (1991) Biochim. Biophys. Acta , vol.1072 , pp. 129-157
    • Angel, P.1    Karin, M.2
  • 8
    • 0021616838 scopus 로고
    • UV irradiation stimulates levels of p53 cellular tumor antigen in nontransformed mouse cells
    • 8. Maltzman, W.; Czyzyk, L. UV irradiation stimulates levels of p53 cellular tumor antigen in nontransformed mouse cells. Mol. Cell. Biol. 4:1689-1694; 1984.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1689-1694
    • Maltzman, W.1    Czyzyk, L.2
  • 10
    • 0025806587 scopus 로고
    • Ha-Ras augments c-Jun activity and stimulates phophorylation of its activation domain
    • 10. Binetruy, B.; Smeal, T.; Karin, M. Ha-Ras augments c-Jun activity and stimulates phophorylation of its activation domain. Nature 351:122-127; 1991.
    • (1991) Nature , vol.351 , pp. 122-127
    • Binetruy, B.1    Smeal, T.2    Karin, M.3
  • 11
    • 0025788098 scopus 로고
    • Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serine 63 and 73
    • 11. Smeal, T.; Binetruy, B.; Mercola, D. A.; Birrer, M.; Karin, M. Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serine 63 and 73. Nature 354:494-496; 1991.
    • (1991) Nature , vol.354 , pp. 494-496
    • Smeal, T.1    Binetruy, B.2    Mercola, D.A.3    Birrer, M.4    Karin, M.5
  • 12
    • 0026039676 scopus 로고
    • The retinoblastoma protein is phosphorylated on multiple sites by human cdc2
    • 12. Lees, J. A.; Buchkovich, K. J.; Marshak, D. R.; Anderson, C. W.; Harlow, E. The retinoblastoma protein is phosphorylated on multiple sites by human cdc2. EMBO J. 10:4279-4290; 1991.
    • (1991) EMBO J. , vol.10 , pp. 4279-4290
    • Lees, J.A.1    Buchkovich, K.J.2    Marshak, D.R.3    Anderson, C.W.4    Harlow, E.5
  • 13
    • 0028066283 scopus 로고
    • Postranslational regulation of p53 tumor suppressor protein function
    • 13. Maxwell, S. A.; Roth, J. A. Postranslational regulation of p53 tumor suppressor protein function. Crit. Rev. Oncog. 5:23-57; 1994.
    • (1994) Crit. Rev. Oncog. , vol.5 , pp. 23-57
    • Maxwell, S.A.1    Roth, J.A.2
  • 14
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress-inducible genes: Direct activation by oxidation
    • 14. Storz, G.; Tartaglia, L. A.; Ames, B. N. Transcriptional regulator of oxidative stress-inducible genes; Direct activation by oxidation. Science 248:189-194; 1990.
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 15
    • 0027363665 scopus 로고
    • Redox control of transcription: Sensors, response regulators, activators and repressors
    • 15. Allen, F. Redox control of transcription: Sensors, response regulators, activators and repressors. FEBS Lett. 332:203-207; 1993.
    • (1993) FEBS Lett. , vol.332 , pp. 203-207
    • Allen, F.1
  • 16
    • 0028049068 scopus 로고
    • An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein
    • 16. Hidalgo, E.; Demple, B. An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein. EMBO J. 13:138-146; 1994.
    • (1994) EMBO J. , vol.13 , pp. 138-146
    • Hidalgo, E.1    Demple, B.2
  • 17
    • 0025721047 scopus 로고
    • Redox redux: The control of oxidative stress responses
    • 17. Demple, B.; Amábile-Cuevas, C. F. Redox redux: The control of oxidative stress responses. Cell 67:837-839; 1991.
    • (1991) Cell , vol.67 , pp. 837-839
    • Demple, B.1    Amábile-Cuevas, C.F.2
  • 18
    • 0027294788 scopus 로고
    • PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator
    • 18. Ostrovsky de Spicer, P.; Maloy, S. PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator. Proc. Natl. Acad. Sci. USA 90:4295-4298; 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4295-4298
    • Ostrovsky de Spicer, P.1    Maloy, S.2
  • 20
    • 0028124528 scopus 로고
    • P53 and human cancers
    • 20. Lane, D. P. P53 and human cancers. Br. Med. Bull. 50:582-599; 1994.
    • (1994) Br. Med. Bull. , vol.50 , pp. 582-599
    • Lane, D.P.1
  • 22
    • 0025040233 scopus 로고
    • Suppression of human colorectal carcinoma cell growth by wildtype p53
    • 22. Baker, S. J.; Markowitz, S.; Fearon, E. R.; Willson, J. K.; Vogelstein, B. Suppression of human colorectal carcinoma cell growth by wildtype p53. Science 249:912-915; 1990.
    • (1990) Science , vol.249 , pp. 912-915
    • Baker, S.J.1    Markowitz, S.2    Fearon, E.R.3    Willson, J.K.4    Vogelstein, B.5
  • 23
    • 0027109075 scopus 로고
    • P53, guardian of the genome
    • 23. Land, D. P. P53, guardian of the genome. Nature 358:15-16; 1992.
    • (1992) Nature , vol.358 , pp. 15-16
    • Land, D.P.1
  • 24
    • 0026452949 scopus 로고
    • Defects in a cell cycle checkpoint may be responsible for the genomic instability of cancer cells
    • 24. Hartwell, L. Defects in a cell cycle checkpoint may be responsible for the genomic instability of cancer cells. Cell 71:543-546; 1992.
    • (1992) Cell , vol.71 , pp. 543-546
    • Hartwell, L.1
  • 25
    • 0028071555 scopus 로고
    • Mutations in the p53 suppressor gene: Clues to cancer etiology and molecular pathogenesis
    • 25. Greenblatt, M. S.; Bennett, W. P.; Hollstein, M.; Harris, C. C. Mutations in the p53 suppressor gene: Clues to cancer etiology and molecular pathogenesis. Cancer Res. 54:4855-4878; 1994.
    • (1994) Cancer Res. , vol.54 , pp. 4855-4878
    • Greenblatt, M.S.1    Bennett, W.P.2    Hollstein, M.3    Harris, C.C.4
  • 26
    • 0022067728 scopus 로고
    • Human p53 cellular tumor antigen: cDNA sequence and expression in COS cells
    • 26. Zakut-Houri, R.; Bienz-Tadmor, B.; Givol, D.; Oren, M. Human p53 cellular tumor antigen: cDNA sequence and expression in COS cells. EMBO J. 4:1251-1255; 1985.
    • (1985) EMBO J. , vol.4 , pp. 1251-1255
    • Zakut-Houri, R.1    Bienz-Tadmor, B.2    Givol, D.3    Oren, M.4
  • 28
    • 0029984305 scopus 로고    scopus 로고
    • Database of mutations in the p53 and APC tumor suppressor genes designed to facilitate molecular epidemiological analyses
    • 28. De Vries, E. M.; Ricke, D. O.; De Vries, T. N.; Hartmann, A.; Blaszyk, H.; Liao, D.; Soussi, T.; Kovach, J. S.; Sommer, S. Database of mutations in the p53 and APC tumor suppressor genes designed to facilitate molecular epidemiological analyses. Hum. Mutat. 7:202-213; 1996.
    • (1996) Hum. Mutat. , vol.7 , pp. 202-213
    • De Vries, E.M.1    Ricke, D.O.2    De Vries, T.N.3    Hartmann, A.4    Blaszyk, H.5    Liao, D.6    Soussi, T.7    Kovach, J.S.8    Sommer, S.9
  • 29
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • 29. Cho, Y.; Gorina, S.; Jeffrey, P. D.; Pavletich, N. P. Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations. Science 265:346-355; 1994.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 30
    • 0027361046 scopus 로고
    • Redox modulation of p53 conformation and sequence-specific DNA binding in vitro
    • 30. Hainaut, P.; Milner, J. Redox modulation of p53 conformation and sequence-specific DNA binding in vitro. Cancer Res. 53:4469-4473: 1993.
    • (1993) Cancer Res. , vol.53 , pp. 4469-4473
    • Hainaut, P.1    Milner, J.2
  • 31
    • 0028830748 scopus 로고
    • Modulation by copper of p53 conformation and sequence-specific DNA binding: Role for Cu(II)/Cu(I) redox mechanism
    • 31. Hainaut, P.; Rolley, N.; Davies, M.; Milner, J. Modulation by copper of p53 conformation and sequence-specific DNA binding: Role for Cu(II)/Cu(I) redox mechanism. Oncogene 10:27-32; 1995.
    • (1995) Oncogene , vol.10 , pp. 27-32
    • Hainaut, P.1    Rolley, N.2    Davies, M.3    Milner, J.4
  • 32
    • 0027269545 scopus 로고
    • A structural role of metal ions in the "wild-type" conformation of the tumor suppressor protein p53
    • 32. Hainaut, P.; Milner, J. A structural role of metal ions in the "wild-type" conformation of the tumor suppressor protein p53. Cancer Res. 53:1739-1742: 1993.
    • (1993) Cancer Res. , vol.53 , pp. 1739-1742
    • Hainaut, P.1    Milner, J.2
  • 33
    • 0028349874 scopus 로고
    • Increased salt concentration reversibly destabilizes p53 quaternary structure and sequence-specific DNA binding
    • 33. Butcher, S.; Hainaut, P.; Milner, J. Increased salt concentration reversibly destabilizes p53 quaternary structure and sequence-specific DNA binding. Biochem. J. 298:513-516; 1994.
    • (1994) Biochem. J. , vol.298 , pp. 513-516
    • Butcher, S.1    Hainaut, P.2    Milner, J.3
  • 34
    • 0028838002 scopus 로고
    • Temperature sensitivity for conformation is an intrinsic property of wild type p53
    • 34. Hainaut, P.; Butcher, S.; Milner, J. Temperature sensitivity for conformation is an intrinsic property of wild type p53. Br. J. Cancer 71:227-231; 1995.
    • (1995) Br. J. Cancer , vol.71 , pp. 227-231
    • Hainaut, P.1    Butcher, S.2    Milner, J.3
  • 35
    • 0027250493 scopus 로고
    • Activation of the cryptic DNA binding function of mutant form of p53
    • 35. Hupp, T. R.; Meek, D. W.; Midgley, C. A.; Lane, D. P. Activation of the cryptic DNA binding function of mutant form of p53. Nucleic Acids Res. 21:3167-3174; 1993.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3167-3174
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 36
    • 0027385992 scopus 로고
    • Sequence-specific interaction of a conformational domain of p53 with DNA
    • 36. Srinivasan, R.; Roth, J. A.; Maxwell, S. A. Sequence-specific interaction of a conformational domain of p53 with DNA. Cancer Res. 53:5361-5364; 1993.
    • (1993) Cancer Res. , vol.53 , pp. 5361-5364
    • Srinivasan, R.1    Roth, J.A.2    Maxwell, S.A.3
  • 37
    • 0027771333 scopus 로고
    • The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spot
    • 37. Pavletich, N. P.; Chambers, K. A.; Pabo, C. O. The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spot. Genes Dev. 7:2556-2564; 1993.
    • (1993) Genes Dev. , vol.7 , pp. 2556-2564
    • Pavletich, N.P.1    Chambers, K.A.2    Pabo, C.O.3
  • 39
    • 0025289049 scopus 로고
    • Free radicals, antioxidant enzymes and carcinogenesis
    • 39. Sun, Y. Free radicals, antioxidant enzymes and carcinogenesis. Free Radic. Biol. Med. 8:583-599; 1990.
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 583-599
    • Sun, Y.1
  • 40
    • 0027501841 scopus 로고
    • Wild type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene
    • 40. Juven, T.; Barak, Y.; Zauberman, A.; George, D. L.; Oren, M. Wild type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene. Oncogene 8:3411-3416; 1993.
    • (1993) Oncogene , vol.8 , pp. 3411-3416
    • Juven, T.1    Barak, Y.2    Zauberman, A.3    George, D.L.4    Oren, M.5
  • 43
    • 0027160694 scopus 로고
    • No point mutation of Ha-ras or p53 genes expressed in preneoplastic-to-neoplastic progression as modeled in mouse JB6 cell variants
    • 43. Sun, Y.; Nakamura, K.; Hegamyer, G. A.; Dong, Z.; Colburn, N. H. No point mutation of Ha-ras or p53 genes expressed in preneoplastic-to-neoplastic progression as modeled in mouse JB6 cell variants. Mol. Carcinog. 8:49-57; 1993.
    • (1993) Mol. Carcinog. , vol.8 , pp. 49-57
    • Sun, Y.1    Nakamura, K.2    Hegamyer, G.A.3    Dong, Z.4    Colburn, N.H.5
  • 44
    • 0027137919 scopus 로고
    • Alterations of the p53 tumor suppressor gene in transformed mouse liver cells
    • 44. Sun, Y.; Hegamyer, G.; Nakamura, K.; Kim, H.; Oberley, L. W.; Colburn, N. H. Alterations of the p53 tumor suppressor gene in transformed mouse liver cells. Int. J. Cancer 55:952-956; 1993.
    • (1993) Int. J. Cancer , vol.55 , pp. 952-956
    • Sun, Y.1    Hegamyer, G.2    Nakamura, K.3    Kim, H.4    Oberley, L.W.5    Colburn, N.H.6
  • 45
    • 0027474057 scopus 로고
    • Progression toward tumor cell phenotype is enhanced by overexpression of a mutant p53 tumor suppressor gene isolated from nasopharyngeal carcinoma
    • 45. Sun, Y.; Nakamura, K.; Wendel, E.; Colburn, N. H. Progression toward tumor cell phenotype is enhanced by overexpression of a mutant p53 tumor suppressor gene isolated from nasopharyngeal carcinoma. Proc. Natl. Acad. Sci. USA 90:2827-2831; 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2827-2831
    • Sun, Y.1    Nakamura, K.2    Wendel, E.3    Colburn, N.H.4
  • 46
    • 0027291957 scopus 로고
    • Dosage dependent dominace over wild type p53 of a mutant p53 isolated from nasopharyngeal carcinoma
    • 46. Sun, Y.; Dong, Z.; Nakamura, K.; Colburn, N. H. Dosage dependent dominace over wild type p53 of a mutant p53 isolated from nasopharyngeal carcinoma. FASEB J. 7:944-950; 1993.
    • (1993) FASEB J. , vol.7 , pp. 944-950
    • Sun, Y.1    Dong, Z.2    Nakamura, K.3    Colburn, N.H.4
  • 47
    • 0028342913 scopus 로고
    • Regulation of the transcription factors NF-κB and AP-1 by redox changes
    • 47. Meyer, M.; Pahl, H. L.; Baeuerle, P. A. Regulation of the transcription factors NF-κB and AP-1 by redox changes. Chem. Biol. Interact. 91:91-100; 1994.
    • (1994) Chem. Biol. Interact. , vol.91 , pp. 91-100
    • Meyer, M.1    Pahl, H.L.2    Baeuerle, P.A.3
  • 48
    • 0025091890 scopus 로고
    • Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: Both Fos and Jun contact DNA directly
    • 48. Abate, C.; Luk, D.; Gentz, R.; Rauscher, F. J., , III; Curran, T. Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly. Proc. Natl. Acad. Sci. USA 87:1032-1036; 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1032-1036
    • Abate, C.1    Luk, D.2    Gentz, R.3    Rauscher F.J. III4    Curran, T.5
  • 49
    • 0025077481 scopus 로고
    • Redox regulation of Fos and Jun DNA-binding activity in vitro
    • 49. Abate, C.; Patel, L.; Rauscher, F. J., III; 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. III3    Curran, T.4
  • 50
    • 0025852479 scopus 로고
    • Modulation of transcription factor NF-κB binding activity by oxidation-reduction in vitro
    • 50. Toledano, M. B.; Leonard, W. J. Modulation of transcription factor NF-κB binding activity by oxidation-reduction in vitro. Proc. Natl. Acad. Sci. USA 88:4328-4332; 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4328-4332
    • Toledano, M.B.1    Leonard, W.J.2
  • 51
    • 0028348239 scopus 로고
    • Distinct effects of glutathione disulphide on the nuclear transcripton factor κB and the activator protein-1
    • 51. Galter, D.; Mihm, S.; Droge, W. Distinct effects of glutathione disulphide on the nuclear transcripton factor κB and the activator protein-1. Eur. J. Biochem. 221:639-648; 1994.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 639-648
    • Galter, D.1    Mihm, S.2    Droge, W.3
  • 52
    • 0025887817 scopus 로고
    • In vitro DNA binding activity of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes
    • 52. Bannister, A. J.; Cook, A.; Kouzarides, T. In vitro DNA binding activity of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes. Onogene 6:1243-1250; 1991.
    • (1991) Onogene , vol.6 , pp. 1243-1250
    • Bannister, A.J.1    Cook, A.2    Kouzarides, T.3
  • 53
    • 0029048919 scopus 로고
    • Inhibition of AP-1 binding and transcription by gold and selenium involving conseved cysteine residues in Jun and Fos
    • 53. Handel, M. L.; Watts, C. K. W.; DeFazio, A.; Day, R. O.; Sutherland, R. L. Inhibition of AP-1 binding and transcription by gold and selenium involving conseved cysteine residues in Jun and Fos. Proc. Natl. Acad. Sci. USA 92:4497-4501; 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4497-4501
    • Handel, M.L.1    Watts, C.K.W.2    DeFazio, A.3    Day, R.O.4    Sutherland, R.L.5
  • 54
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, nuclear protein that facilitates AP-1 DNA-binding activily
    • 54. Xanthoudakis, S.; Curran, T. Identification and characterization of Ref-1, nuclear protein that facilitates AP-1 DNA-binding activily. EMBO J. 11:653-665; 1992.
    • (1992) EMBO J. , vol.11 , pp. 653-665
    • Xanthoudakis, S.1    Curran, T.2
  • 55
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • 55. Xanthoudakis, S.; Miao, G.; Wang, F.; Pan, Y. E.; Curran, T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11:3323-3335; 1992.
    • (1992) EMBO J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.E.4    Curran, T.5
  • 56
    • 0025936119 scopus 로고
    • Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. Coli xth (exonuclease III) mutants
    • 56. Robson, C. N.; Hickson, I. D. Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. Coli xth (exonuclease III) mutants. Nucleic Acids Res. 19:5519-5523; 1991.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5519-5523
    • Robson, C.N.1    Hickson, I.D.2
  • 57
    • 0026323008 scopus 로고
    • Cloning and expression of APE. The cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes
    • 57. Demple, B.; Herman, T.; Chen, D. S. Cloning and expression of APE. the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes. Proc. Natl. Acad. Sci. USA 88:11450-11454; 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 58
    • 0028058086 scopus 로고
    • The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains
    • 58. Xanthoudakis, S.; Miao, G. G.; Curran, T. The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains. Proc. Natl. Acad. Sci. USA 91:23-27; 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 23-27
    • Xanthoudakis, S.1    Miao, G.G.2    Curran, T.3
  • 59
    • 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
    • 59. Walker, L. J.; Robson, C. N.; Black, E.; Gillespie, D.; Hickson, I. D. 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
  • 60
    • 0027981492 scopus 로고
    • 2 and N-acetyl-L-cysteine regulate expression of c-jun and c-fos in lens systems
    • 2 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
  • 61
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • 61. Holmgren, A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264:13963-13966; 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 62
    • 0028344541 scopus 로고
    • Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-κB and AP-1
    • 62. Schenk, H.; Klein, M.; Erdbrugger, W.; Dröge, W; Schulze-Osthoff, K. 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.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1672-1676
    • Schenk, H.1    Klein, M.2    Erdbrugger, W.3    Dröge, W.4    Schulze-Osthoff, K.5
  • 63
    • 0028008680 scopus 로고
    • Intracellular glutathione levels regulate Fos/Jun induction and activation of glutathione S-transferase gene expression
    • 63. Bergelson, S.; Pinkus, R.; Daniel, V. Intracellular glutathione levels regulate Fos/Jun induction and activation of glutathione S-transferase gene expression. Cancer Res. 54:36-40; 1994.
    • (1994) Cancer Res. , vol.54 , pp. 36-40
    • Bergelson, S.1    Pinkus, R.2    Daniel, V.3
  • 64
    • 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
  • 66
    • 0027506460 scopus 로고
    • Escape from redox regulation enhances the transforming activity of Fos
    • 66. Okuno, H.; Akahori, A.; Sato, H.; Xanthoudakis, S.; Curran, T.; Iba, H. Escape from redox regulation enhances the transforming activity of Fos. Oncogene 8:695-701; 1993.
    • (1993) Oncogene , vol.8 , pp. 695-701
    • Okuno, H.1    Akahori, A.2    Sato, H.3    Xanthoudakis, S.4    Curran, T.5    Iba, H.6
  • 67
    • 0029039420 scopus 로고
    • 2 is directly related to increased proliferation and transformation of tracheal epithelial cells
    • 2 is directly related to increased proliferation and transformation of tracheal epithelial cells. Cancer Res. 55:2723-2726; 1995.
    • (1995) Cancer Res. , vol.55 , pp. 2723-2726
    • Timblin, C.R.1    Janssen, Y.W.M.2    Mossman, B.T.3
  • 68
    • 0000315372 scopus 로고
    • Gene regulation by active oxygen and other stress inducers: Role in tumor promotion and progression
    • Spatz, L.; Bloom, A. D. eds. London: Oxford University Press; 1992
    • 68. Colburn, N. H. Gene regulation by active oxygen and other stress inducers: Role in tumor promotion and progression. In: Spatz, L.; Bloom, A. D. eds. Biological consequences of oxidative stress: Implications for cardiovascular disease and carcinogenesis. London: Oxford University Press; 1992; 1992:121-137.
    • (1992) Biological Consequences of Oxidative Stress: Implications for Cardiovascular Disease and Carcinogenesis , pp. 121-137
    • Colburn, N.H.1
  • 69
    • 0028989492 scopus 로고
    • C-jun and multi-stage carcinogenesis: Association of overexpression of introduced c-jun with progression toward a neoplastic endpoint in mouse JB6 cells sensitive to tumor promoter-induced transformation
    • 69. Watts, R. G.; Ben-Ari, E. T.; Bernstein, L. R.; Birrer, M. J.; Winterstein, D.; Wendel, E.; Colburn, N. H. C-jun and multi-stage carcinogenesis: Association of overexpression of introduced c-jun with progression toward a neoplastic endpoint in mouse JB6 cells sensitive to tumor promoter-induced transformation. Mol. Carcinog. 13:27-36; 1995.
    • (1995) Mol. Carcinog. , vol.13 , pp. 27-36
    • Watts, R.G.1    Ben-Ari, E.T.2    Bernstein, L.R.3    Birrer, M.J.4    Winterstein, D.5    Wendel, E.6    Colburn, N.H.7
  • 70
    • 0029000906 scopus 로고
    • Antitumor promotion by phenolic antioxidants: Inhibition of AP-1 activity through induction of Fra expression
    • 70. Yoshioka, K.; Deng, T.; Cavigelli, M.; Karin, M. Antitumor promotion by phenolic antioxidants: Inhibition of AP-1 activity through induction of Fra expression. Proc. Natl. Acad. Sci. USA 92:4972-4976; 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4972-4976
    • Yoshioka, K.1    Deng, T.2    Cavigelli, M.3    Karin, M.4
  • 71
    • 0025149657 scopus 로고
    • Cloning of a mitogen-inducible gene encoding a κB DNA-binding protein with homology to the rel oncogene and to cell-cycle motifs
    • 71. Bours, V.; Villalobos, J.; Burd, P. R.; Kelly, K.; Siebenlist, U. Cloning of a mitogen-inducible gene encoding a κB DNA-binding protein with homology to the rel oncogene and to cell-cycle motifs. Nature 348:76-80; 1990.
    • (1990) Nature , vol.348 , pp. 76-80
    • Bours, V.1    Villalobos, J.2    Burd, P.R.3    Kelly, K.4    Siebenlist, U.5
  • 73
    • 0025078530 scopus 로고
    • Cloning of the p50 DNA binding subunit of NF-κB: Homology to rel and dorsal
    • 73. Ghosh, S.; Gifford, A. M.; Riviere, L. R.; Tempst, P.; Nolan, G. P.; Baltimore, D. Cloning of the p50 DNA binding subunit of NF-κB: Homology to rel and dorsal.. Cell 62:1019-1029; 1990.
    • (1990) Cell , vol.62 , pp. 1019-1029
    • Ghosh, S.1    Gifford, A.M.2    Riviere, L.R.3    Tempst, P.4    Nolan, G.P.5    Baltimore, D.6
  • 74
    • 0025184764 scopus 로고
    • The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain
    • 74. Bull, P.; Morley, K. L.; Hoekstra, M. F.; Hunter, T.; Verma, I. M. The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain. Mol. Cell. Biol. 10:5473-5485; 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5473-5485
    • Bull, P.1    Morley, K.L.2    Hoekstra, M.F.3    Hunter, T.4    Verma, I.M.5
  • 75
    • 0023724778 scopus 로고
    • IκB: A specific inhibitor of the NF-κB transcription factor
    • 75. Baeuerle, P. A.; Baltimore, D. IκB: A specific inhibitor of the NF-κB transcription factor. Science 242:540-546; 1988.
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 76
    • 0028170265 scopus 로고
    • Activation of NF-κB in vivo is regulated by multiple phosphorylations
    • 76. Naumann, M.; Scheidereit, C. Activation of NF-κB in vivo is regulated by multiple phosphorylations. EMBO J. 13:4597-4607; 1994.
    • (1994) EMBO J. , vol.13 , pp. 4597-4607
    • Naumann, M.1    Scheidereit, C.2
  • 77
    • 0027369661 scopus 로고
    • Identification of a new serine kinase that activates NF-κB by direct phosphorylation
    • 77. Hayashi, T.; Sekine, T.; Okamoto, T. Identification of a new serine kinase that activates NF-κB by direct phosphorylation. J. Biol. Chem. 268:26790-26795; 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26790-26795
    • Hayashi, T.1    Sekine, T.2    Okamoto, T.3
  • 78
    • 0027176524 scopus 로고
    • Rapid proteolysis of IκB-α is necessary for activation of transcription factor NF-κB
    • 78. Henkel, T.; Machleidt, T.; Alkalay, I.; Kronke, M.; Ben-Neriah, Y.; Baeuerle, P. A. Rapid proteolysis of IκB-α is necessary for activation of transcription factor NF-κB. Nature 365:182-185; 1993.
    • (1993) Nature , vol.365 , pp. 182-185
    • Henkel, T.1    Machleidt, T.2    Alkalay, I.3    Kronke, M.4    Ben-Neriah, Y.5    Baeuerle, P.A.6
  • 79
    • 0028174061 scopus 로고
    • Function and activation of NF-kappa B in the immune system
    • 79. Baeuerle, P. A.; Henkel, T. Function and activation of NF-kappa B in the immune system. Annu. Rev. Immunol. 12:141-179; 1994.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 81
    • 0027521580 scopus 로고
    • Potential involvement of the transcription factor NF-kappa B in neurological disorders
    • 81. Kaltschmidt, B.; Baeuerle, P. A.; Kaltschmidt, C. Potential involvement of the transcription factor NF-kappa B in neurological disorders. Mol. Aspects Med. 14:171-190; 1993.
    • (1993) Mol. Aspects Med. , vol.14 , pp. 171-190
    • Kaltschmidt, B.1    Baeuerle, P.A.2    Kaltschmidt, C.3
  • 82
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-κB by reduction of a disulphide bond involving cysteine 62
    • 82. Matthews, J. R.; Wakasugi, N.; Virelizier, J. L; Yodoi, J.; Hay, R. T. Thioredoxin regulates the DNA binding activity of NF-κB by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res. 20:3821-3830; 1992.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3821-3830
    • Matthews, J.R.1    Wakasugi, N.2    Virelizier, J.L.3    Yodoi, J.4    Hay, R.T.5
  • 83
    • 0027963233 scopus 로고
    • Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-κB in vitro
    • 83. Mitomo, K.; Nakayama, K.; Fujimoto, K.; Sun, X.; Seki, S.; Yamamoto, K. Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-κB in vitro. Gene 145:197-203; 1994.
    • (1994) Gene , vol.145 , pp. 197-203
    • Mitomo, K.1    Nakayama, K.2    Fujimoto, K.3    Sun, X.4    Seki, S.5    Yamamoto, K.6
  • 84
    • 0027217531 scopus 로고
    • Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin
    • 84. Hayashi, T.; Ueno, Y.; Okamoto, T. Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin. J. Biol. Chem. 268:11380-11388; 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11380-11388
    • Hayashi, T.1    Ueno, Y.2    Okamoto, T.3
  • 85
    • 0026652879 scopus 로고
    • The RxxRxRxxC motif conserved in all Rel/κB proteins is essential for the DNA binding activity and redox regulation of the v-Rel oncoprotein
    • 85. Kumar, S.; Rabson, A. B.; Gelinas, C. The RxxRxRxxC motif conserved in all Rel/κB proteins is essential for the DNA binding activity and redox regulation of the v-Rel oncoprotein. Mol. Cell. Biol. 12:3094-3106; 1992.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3094-3106
    • Kumar, S.1    Rabson, A.B.2    Gelinas, C.3
  • 86
    • 0026741597 scopus 로고
    • Human thioredoxin/adult T cell leukemia-derived factor activates the enhancer binding protein of human immunodeficiency virus type 1 by thiol redox control mechanism
    • 86. Okamoto, T.; Ogiwara, H.; Hayashi, T.; Mitsui, A.; Kawabe, T.; Yodoi, J. Human thioredoxin/adult T cell leukemia-derived factor activates the enhancer binding protein of human immunodeficiency virus type 1 by thiol redox control mechanism. Int. Immunol. 4:811-819; 1992.
    • (1992) Int. Immunol. , vol.4 , pp. 811-819
    • Okamoto, T.1    Ogiwara, H.2    Hayashi, T.3    Mitsui, A.4    Kawabe, T.5    Yodoi, J.6
  • 87
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor κB activation in intact cells
    • 87. Schreck, R.; Meier, B.; Mannel, D. N.; Droge, W.; Baeuerle, P. A. Dithiocarbamates as potent inhibitors of nuclear factor 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.N.3    Droge, W.4    Baeuerle, P.A.5
  • 88
    • 0026467248 scopus 로고
    • Redox status of cells influences constitutive or induced NF-kappa B translocation and HIV long terminal activity in human T and monocytic cell lines
    • 88. Israel, N.; Gougerol-Pocidalo, M. A.; Aillet, F.; Virelizier, J. L. Redox status of cells influences constitutive or induced NF-kappa B translocation and HIV long terminal activity in human T and monocytic cell lines. J. Immunol. 149:3386-3393; 1992.
    • (1992) J. Immunol , vol.149 , pp. 3386-3393
    • Israel, N.1    Gougerol-Pocidalo, M.A.2    Aillet, F.3    Virelizier, J.L.4
  • 89
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1
    • 89. Schreck, F.; Rieber, P.; Baeuerle, P. A. 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, F.1    Rieber, P.2    Baeuerle, P.A.3
  • 90
    • 0025677250 scopus 로고
    • Intracellular thiols regulate activation of nuclear factor κB and transcription of human immunodeficiency virus
    • 90. Staal, F. J. T.; Roederer, M.; Herzenberg, L. A.; Herzenberg, L. A. Intracellular thiols regulate activation of nuclear factor κB and transcription of human immunodeficiency virus. Proc. Natl. Acad. Sci. USA 87:9943-9947; 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9943-9947
    • Staal, F.J.T.1    Roederer, M.2    Herzenberg, L.A.3    Herzenberg, L.A.4
  • 92
    • 0028006612 scopus 로고
    • Separation of oxidant-initiated and redox-regulated steps in the NF-κB signal transduction pathway
    • 92. Anderson, M. T.; Staal, F. J. T.; Gitler, C.; Hersenberg, L. A.; Hersenberg. L. A. Separation of oxidant-initiated and redox-regulated steps in the NF-κB signal transduction pathway. Proc. Natl. Acad. Sci. USA 91:11527-11531; 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11527-11531
    • Anderson, M.T.1    Staal, F.J.T.2    Gitler, C.3    Hersenberg, L.A.4    Hersenberg, L.A.5
  • 93
    • 0027521838 scopus 로고
    • Differential induction of nuclear NF-κB by protein phosphatase inhibitors in primary and transformed human cells: Requirement for both oxidation and phosphorylation in nuclear translocation
    • 93. Menon, S. D.; Qin, S.; Guy, G. R.; Tan, T. H. Differential induction of nuclear NF-κB by protein phosphatase inhibitors in primary and transformed human cells: Requirement for both oxidation and phosphorylation in nuclear translocation. J. Biol. Chem. 268:26805-26812; 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26805-26812
    • Menon, S.D.1    Qin, S.2    Guy, G.R.3    Tan, T.H.4
  • 95
  • 98
    • 0027433604 scopus 로고
    • DNA and redox state induced conformational changes in the DNA-binding domain of the Myb oncoprotein
    • 98. Myrset, A. H.; Bostad, A.; Jamin, N.; Lirsac, P. N.; Toma, F.; Gabrielsen, O. S. DNA and redox state induced conformational changes in the DNA-binding domain of the Myb oncoprotein. EMBO J. 12:4625-1633; 1993.
    • (1993) EMBO J. , vol.12 , pp. 4625-11633
    • Myrset, A.H.1    Bostad, A.2    Jamin, N.3    Lirsac, P.N.4    Toma, F.5    Gabrielsen, O.S.6
  • 99
    • 0026510719 scopus 로고
    • A highly conserved cysteine in the v-Myb DNA binding domain is essential for transformation and transcriptional trans-activation
    • 99. Grasser, F. A.; LaMontagne, K.; Whittaker, L.; Stohr, S.; Lipsick. J. S. A highly conserved cysteine in the v-Myb DNA binding domain is essential for transformation and transcriptional trans-activation. Oncogene 7:1005-1009; 1992.
    • (1992) Oncogene , vol.7 , pp. 1005-1009
    • Grasser, F.A.1    LaMontagne, K.2    Whittaker, L.3    Stohr, S.4    Lipsick, J.S.5
  • 100
    • 0027458366 scopus 로고
    • The Ets family of transcription factors
    • 100. Wasylyk, B.; Hahn, S. L.; Giovane, A. The Ets family of transcription factors. Eur. J. Biochem. 211:7-18; 1993.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 7-18
    • Wasylyk, B.1    Hahn, S.L.2    Giovane, A.3
  • 101
    • 0025334775 scopus 로고
    • The c-ets proto-oncogenes encode transcription factors that cooperate with c-Fos and c-Jun for transcriptional activation
    • 101. Wasylyk, B.; Wasylyk, C.; Flores, P.; Begue, A.; Leprince, D.; Stehelin, D. The c-ets proto-oncogenes encode transcription factors that cooperate with c-Fos and c-Jun for transcriptional activation. Nature 346:191-193; 1990.
    • (1990) Nature , vol.346 , pp. 191-193
    • Wasylyk, B.1    Wasylyk, C.2    Flores, P.3    Begue, A.4    Leprince, D.5    Stehelin, D.6
  • 102
    • 0027252929 scopus 로고
    • Oncogenic conversion of Ets affects redox regulation in vivo and in vitro
    • 102. Wasylyk, C.; Wasylyk, B. Oncogenic conversion of Ets affects redox regulation in vivo and in vitro. Nucleic Acids Res. 21:523-529; 1993.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 523-529
    • Wasylyk, C.1    Wasylyk, B.2
  • 104
    • 0023663884 scopus 로고
    • Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain
    • 104. Kadonaga, J. T.; Garner, K. R.; Masiarz, F. R.; Tjian, R. Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain. Cell 51:1079-1090; 1987.
    • (1987) Cell , vol.51 , pp. 1079-1090
    • Kadonaga, J.T.1    Carner, K.R.2    Masiarz, F.R.3    Tjian, R.4
  • 105
    • 0023920195 scopus 로고
    • Heavy metal ions in transcription factors from HeLa cells:Sp1, but not octamer transcription factor requires zinc for DNA binding and for activator function
    • 105. Westin, G.; Schaffner, W. Heavy metal ions in transcription factors from HeLa cells:Sp1, but not octamer transcription factor requires zinc for DNA binding and for activator function. Nucleic Acids Res. 16:5771-5781; 1988.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 5771-5781
    • Westin, G.1    Schaffner, W.2
  • 106
    • 0028290479 scopus 로고
    • Role of zinc-coordination and of the glutathione redox couple in the redox susceptibility of human transcription factor SP1
    • 106. Knoepfel, L.; Steinkühler, C.; Carrì, M.-T.; Rotilio, G. Role of zinc-coordination and of the glutathione redox couple in the redox susceptibility of human transcription factor SP1. Biochem. Biophys. Res. Commun. 201:871-877; 1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 871-877
    • Knoepfel, L.1    Steinkühler, C.2    Carrì, M.-T.3    Rotilio, G.4
  • 107
    • 0026644408 scopus 로고
    • Sp1 DNA binding efficiency is highly reduced in nuclear extracts from aged rat tissues
    • 107. Ammendola, R.; Mesuraca, M.; Russo, T.; Cimino, F. Sp1 DNA binding efficiency is highly reduced in nuclear extracts from aged rat tissues. J. Biol. Chem. 267:17944-17948; 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17944-17948
    • Ammendola, R.1    Mesuraca, M.2    Russo, T.3    Cimino, F.4
  • 108
    • 0027968491 scopus 로고
    • The DNA-binding efficiency of Sp1 is affected by redox changes
    • 108. Ammendola, R.; Mesuraca, M.; Russo, T.; Cimino, F. The DNA-binding efficiency of Sp1 is affected by redox changes. Eur. J. Biochem. 225:483-489; 1994.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 483-489
    • Ammendola, R.1    Mesuraca, M.2    Russo, T.3    Cimino, F.4
  • 109
    • 0021087686 scopus 로고
    • Sequence-specific binding of glucocorticoid receptor to MTV DNA at sites within and upstream of the transcribed region
    • 109. Payvar, F.; DeFranco, D.; Firestone, G. L.; Edgar, B.; Wrange, O.; Okret, S.; Gustafsson, J.-A.; Yamamoto, K. R. Sequence-specific binding of glucocorticoid receptor to MTV DNA at sites within and upstream of the transcribed region. Cell 35:381-392; 1983.
    • (1983) Cell , vol.35 , pp. 381-392
    • Payvar, F.1    DeFranco, D.2    Firestone, G.L.3    Edgar, B.4    Wrange, O.5    Okret, S.6    Gustafsson, J.-A.7    Yamamoto, K.R.8
  • 110
    • 0023769378 scopus 로고
    • The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain
    • 110. Freedman, L. F.; Luisi, B. F.; Korszun, Z. R.; Basavappa, R.; Sigler, P. B.; Yamamoto, K. R. The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain. Nature 334:543-546; 1988.
    • (1988) Nature , vol.334 , pp. 543-546
    • Freedman, L.F.1    Luisi, B.F.2    Korszun, Z.R.3    Basavappa, R.4    Sigler, P.B.5    Yamamoto, K.R.6
  • 111
    • 0015526424 scopus 로고
    • Investigations on the glucocorticoid-binding protein from rat thymocytes: II. Stability, kinetics and specificity of binding of steroids
    • 111. Schaumburg, B. P. Investigations on the glucocorticoid-binding protein from rat thymocytes: II. Stability, kinetics and specificity of binding of steroids. Biochim. Biophys. Acta 261:219-235: 1972.
    • (1972) Biochim. Biophys. Acta , vol.261 , pp. 219-235
    • Schaumburg, B.P.1
  • 112
    • 0021962337 scopus 로고
    • Proof that the endogenous, heat-stable glucocorticoid receptor-activating factor is thioredoxin
    • 112. Grippo, J. F.; Holmgren, A.; Pratt, W. B. Proof that the endogenous, heat-stable glucocorticoid receptor-activating factor is thioredoxin. J. Biol. Chem. 260:93-97; 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 93-97
    • Grippo, J.F.1    Holmgren, A.2    Pratt, W.B.3
  • 113
    • 0021130138 scopus 로고
    • Evidence for distinct sulfhydryl groups associated with steroid-and DNA-binding domains of rat thymus glucocorticoid receptors
    • 113. Bodwell, J. E.; Holbrook, N. J.; Munck, A. Evidence for distinct sulfhydryl groups associated with steroid-and DNA-binding domains of rat thymus glucocorticoid receptors. Biochemistry 23:4237-4242; 1984.
    • (1984) Biochemistry , vol.23 , pp. 4237-4242
    • Bodwell, J.E.1    Holbrook, N.J.2    Munck, A.3
  • 114
    • 0023664439 scopus 로고
    • The role of sulfhydryl groups in permitting transformation and DNA binding of the glucocorticoid receptor
    • 114. Tienrungroj, W.; Meshinchi, S.; Sanchez, E. R.; Pratt, S. E.; Grippo, J. F.; Holmgren, A.; Pratt, W. B. The role of sulfhydryl groups in permitting transformation and DNA binding of the glucocorticoid receptor. J. Biol. Chem. 262:6992-7000; 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6992-7000
    • Tienrungroj, W.1    Meshinchi, S.2    Sanchez, E.R.3    Pratt, S.E.4    Grippo, J.F.5    Holmgren, A.6    Pratt, W.B.7
  • 115
    • 0028795795 scopus 로고
    • DNA binding activity of the glucocorticoid receptor is sensitive to redox changes in intact cells
    • 115. Esposio, F.; Cuccovillo, F.; Morra, F.; Russo, T.; Cimino, F. DNA binding activity of the glucocorticoid receptor is sensitive to redox changes in intact cells. Biochim. Biophys. Acta 1260:308-314; 1995.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 308-314
    • Esposio, F.1    Cuccovillo, F.2    Morra, F.3    Russo, T.4    Cimino, F.5
  • 116
    • 0018771944 scopus 로고
    • Dissociation of glucocorticoid inhibition of glucose transport and metabolism by increase in adipocyte age and/or size
    • 116. Roth, G. S.; Livingston, J. N. Dissociation of glucocorticoid inhibition of glucose transport and metabolism by increase in adipocyte age and/or size. Endocrinology 104:423-428; 1979.
    • (1979) Endocrinology , vol.104 , pp. 423-428
    • Roth, G.S.1    Livingston, J.N.2
  • 118
    • 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
    • 118. Huang, R.-P.; Adamson, E. D. 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.
    • (1993) DNA Cell Biol. , vol.12 , pp. 265-273
    • Huang, R.-P.1    Adamson, E.D.2
  • 119
    • 0028136950 scopus 로고
    • Inhibition of the differentiation of human myeloid cell lines by redox changes induced through glutathione depletion
    • 119. Esposito, F.; Agosti, V.; Morrone, G.; Morra, F.; Cuomo, C.; Russo, T.; Venuta, S.; Cimino, F. Inhibition of the differentiation of human myeloid cell lines by redox changes induced through glutathione depletion. Biochem. J. 301:649-653; 1994.
    • (1994) Biochem. J. , vol.301 , pp. 649-653
    • Esposito, F.1    Agosti, V.2    Morrone, G.3    Morra, F.4    Cuomo, C.5    Russo, T.6    Venuta, S.7    Cimino, F.8
  • 120
    • 0028998576 scopus 로고
    • The DNA binding activity and the dimerization ability of the thyroid transcription factor I are redox regulated
    • 120. Arnone, M. I.; Zannini, M.; Di Lauro, R. The DNA binding activity and the dimerization ability of the thyroid transcription factor I are redox regulated. J. Biol. Chem. 270:12048-12055; 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12048-12055
    • Arnone, M.I.1    Zannini, M.2    Di Lauro, R.3
  • 121
    • 0028568429 scopus 로고
    • Purification and characterization of thyroid transcription factor 2
    • 121. Civitareale, D.; Saiardi, A.; Falasca, P. Purification and characterization of thyroid transcription factor 2. Biochem. J. 304:981-985; 1994.
    • (1994) Biochem. J. , vol.304 , pp. 981-985
    • Civitareale, D.1    Saiardi, A.2    Falasca, P.3
  • 122
    • 0025989240 scopus 로고
    • Recombinant 43-kDa USF binds to DNA and activates transcription in a manner indistinguishable from that of natural 43/44-kDa USF
    • 122. Pognonec, P.; Roeder, R. G. Recombinant 43-kDa USF binds to DNA and activates transcription in a manner indistinguishable from that of natural 43/44-kDa USF. Mol. Cell. Biol. 11:5125-5136; 1991.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5125-5136
    • Pognonec, P.1    Roeder, R.G.2
  • 123
    • 0026473086 scopus 로고
    • The Helix-Loop-Helix/ Leucine repeat transcription fractor USF can be functionally regulated in a redox-dependent manner
    • 123. Pognonec, P.; Kato, H.; Roeder, R. G. The Helix-Loop-Helix/ Leucine repeat transcription fractor USF can be functionally regulated in a redox-dependent manner. J. Biol. Chem. 267:24563-24567; 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24563-24567
    • Pognonec, P.1    Kato, H.2    Roeder, R.G.3
  • 124
    • 0027922810 scopus 로고
    • Role of the Ah receptor and the dioxin-inducible [Ah] gene battery in toxicity, cancer, and signal transduction
    • 124. Nebert, D. W.; Puga, A.; Vasiliou, S. Role of the Ah receptor and the dioxin-inducible [Ah] gene battery in toxicity, cancer, and signal transduction. Ann. NY Acad. Sci. 685:624-640; 1993.
    • (1993) Ann. NY Acad. Sci. , vol.685 , pp. 624-640
    • Nebert, D.W.1    Puga, A.2    Vasiliou, S.3
  • 125
    • 0026625037 scopus 로고
    • Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor
    • 125. Reyes, H.; Reisz-Porszasz, S.; Hankinson, O. Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. Science 256:1193-1195; 1992.
    • (1992) Science , vol.256 , pp. 1193-1195
    • Reyes, H.1    Reisz-Porszasz, S.2    Hankinson, O.3
  • 126
    • 0027532636 scopus 로고
    • Analysis of protein-DNA interactions at a dioxin-responsive enhancer
    • 126. Lusska, A.; Shen, E.; Whitlock, J. P., Jr. Analysis of protein-DNA interactions at a dioxin-responsive enhancer. J. Biol. Chem. 268:680-685; 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 680-685
    • Lusska, A.1    Shen, E.2    Whitlock J.P., Jr.3
  • 127
    • 0024829409 scopus 로고
    • The Ah locus: Genetic differences in toxicity, cancer, mutation, and birth defects
    • 127. Nebert, D. W. The Ah locus: Genetic differences in toxicity, cancer, mutation, and birth defects. Crit. Rev. Toxicol. 20:153-174; 1989.
    • (1989) Crit. Rev. Toxicol. , vol.20 , pp. 153-174
    • Nebert, D.W.1
  • 128
    • 0029042132 scopus 로고
    • The DNA binding of purified Ah receptor heterodimer is regulated by redox conditions
    • 128. Ireland, R. C.; Li, S.-Y.; Dougherty, J. J. The DNA binding of purified Ah receptor heterodimer is regulated by redox conditions. Arch. Biochem. Biophys. 319:470-480; 1995.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 470-480
    • Ireland, R.C.1    Li, S.-Y.2    Dougherty, J.J.3
  • 130
    • 0027994037 scopus 로고
    • Analysis of the most representative tumour-derived p53 mutants reveals that changes in protein conformation are not correlated with loss of transactivation or inhibition of cell proliferation
    • 130. Ory, K.; Legros, Y.; Auguin, C.; Soussi, T. Analysis of the most representative tumour-derived p53 mutants reveals that changes in protein conformation are not correlated with loss of transactivation or inhibition of cell proliferation. EMBO J. 13:3496-3504; 1994.
    • (1994) EMBO J. , vol.13 , pp. 3496-3504
    • Ory, K.1    Legros, Y.2    Auguin, C.3    Soussi, T.4
  • 131
    • 0027224017 scopus 로고
    • Cross-coupling of the NF-κB p65 and Fos/Jun transcription factors produces potentiated biological function
    • 131. Stein, B.; Baldwin, A. S., Jr.; Ballard, D. W.; Greene, W. C.; Angel, P.; Herrlich, P. Cross-coupling of the NF-κB p65 and Fos/Jun transcription factors produces potentiated biological function. EMBO J. 12:3879-3891; 1993.
    • (1993) EMBO J. , vol.12 , pp. 3879-3891
    • Stein, B.1    Baldwin A.S., Jr.2    Ballard, D.W.3    Greene, W.C.4    Angel, P.5    Herrlich, P.6
  • 132
    • 0028366089 scopus 로고
    • Repression of AP-1 -stimulated transcription by c-Ets-1
    • 132. Goldberg, Y.; Treier, M.; Ghysdael, J.; Bohmann, D. Repression of AP-1 -stimulated transcription by c-Ets-1. J. Biol. Chem. 269:16566-16573; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16566-16573
    • Goldberg, Y.1    Treier, M.2    Ghysdael, J.3    Bohmann, D.4
  • 133
    • 0026526269 scopus 로고
    • Transcriptional cross-talk: Nuclear factor CREM and CREB bind to AP-1 sites and inhibit activation by Jun
    • 133. Masquilier, D.; Sassone-Corsi, P. Transcriptional cross-talk: Nuclear factor CREM and CREB bind to AP-1 sites and inhibit activation by Jun. J. Biol. Chem. 267:22460-22466; 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22460-22466
    • Masquilier, D.1    Sassone-Corsi, P.2


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