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Volumn 27, Issue 2, 1997, Pages 109-134

Aryl hydrocarbon receptor-mediated signal transduction

Author keywords

ARNT; Basic helix loop helix (bHLH) protein; Dioxin receptor; Halogenated aromatic hydrocarbon; PAS domain; Transcription factor

Indexed keywords

AROMATIC HYDROCARBON RECEPTOR; CARRIER PROTEIN; POLYCYCLIC AROMATIC HYDROCARBON;

EID: 0030888748     PISSN: 10408444     EISSN: None     Source Type: Journal    
DOI: 10.3109/10408449709021615     Document Type: Review
Times cited : (445)

References (223)
  • 2
    • 0027285549 scopus 로고
    • Environmental toxicology of polychlorinated dibenzo-p-dioxins and polychlorinated dibenzofurans
    • Vanden Heuvel, J. P. and Lucier, G., Environmental toxicology of polychlorinated dibenzo-p-dioxins and polychlorinated dibenzofurans, Environ. Health Perspect., 100, 189, 1983.
    • (1983) Environ. Health Perspect. , vol.100 , pp. 189
    • Vanden Heuvel, J.P.1    Lucier, G.2
  • 3
    • 0021637059 scopus 로고
    • Polychlorinated biphenyls (PCBs) and polybrominated biphenyls (PBBs): Biochemistry, toxicology and mechanism of action
    • Safe, S., Polychlorinated biphenyls (PCBs) and polybrominated biphenyls (PBBs): biochemistry, toxicology and mechanism of action, CRC Crit. Rev. Toxicol., 13, 319, 1984.
    • (1984) CRC Crit. Rev. Toxicol. , vol.13 , pp. 319
    • Safe, S.1
  • 4
    • 84965851166 scopus 로고
    • Polychlorinated dibenzo-p-dioxins and polychlorinated dibenzofurans: The risk to human health. A review
    • Skene, S. A., Dewhurst, I. C., and Greenber, M., Polychlorinated dibenzo-p-dioxins and polychlorinated dibenzofurans: the risk to human health. A review, Human Toxicol., 8, 173, 1989.
    • (1989) Human Toxicol. , vol.8 , pp. 173
    • Skene, S.A.1    Dewhurst, I.C.2    Greenber, M.3
  • 7
    • 0003317494 scopus 로고
    • Bioacumulation and toxicity of TCDD and related compounds in aquatic ecosystems
    • Gallo, M. A., Scheuplein, R. J., and Van Der Heijden, K. A., Eds., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Cook, P. M., W., K. D., Walker, M. K., and Peterson, R. E., Bioacumulation and toxicity of TCDD and related compounds in aquatic ecosystems, in: Banbury Report 35: Biological Basis for Risk Assessment of Dioxins and Related Compounds, Gallo, M. A., Scheuplein, R. J., and Van Der Heijden, K. A., Eds., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1991, 143.
    • (1991) Banbury Report 35: Biological Basis for Risk Assessment of Dioxins and Related Compounds , pp. 143
    • Cook, P.M.1    W., K.D.2    Walker, M.K.3    Peterson, R.E.4
  • 8
    • 0020010617 scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin and related halogenated aromatic hydrocarbons: Examination of the mechanism of toxicity
    • Poland, A. and Knutson, J. C., 2,3,7,8-Tetrachlorodibenzo-p-dioxin and related halogenated aromatic hydrocarbons: examination of the mechanism of toxicity, Annu. Rev. Pharmacol. Toxicol., 22, 517, 1982.
    • (1982) Annu. Rev. Pharmacol. Toxicol. , vol.22 , pp. 517
    • Poland, A.1    Knutson, J.C.2
  • 9
    • 0022555425 scopus 로고
    • Comparative toxicology and mechanism of action of polychlorinated dibenzo-p-dioxins and dibenzofurans
    • Safe, S. H., Comparative toxicology and mechanism of action of polychlorinated dibenzo-p-dioxins and dibenzofurans, Annu. Rev. Pharmacol. Toxicol., 26, 371, 1986.
    • (1986) Annu. Rev. Pharmacol. Toxicol. , vol.26 , pp. 371
    • Safe, S.H.1
  • 10
    • 0000539634 scopus 로고
    • Mechanism of action and structure-activity relationships for the chlorinated dibenzo-p-dioxins and related compounds
    • Kimbrough, R. D. and Jensen, A. A., Eds., Elsevier-North Holland, Amsterdam
    • Goldstein, J. A. and Safe, S., Mechanism of action and structure-activity relationships for the chlorinated dibenzo-p-dioxins and related compounds, in: Halogented Biphenyls, Naphthalenes, Dibenzodioxins and Related Compounds, Kimbrough, R. D. and Jensen, A. A., Eds., Elsevier-North Holland, Amsterdam, 1989.
    • (1989) Halogented Biphenyls, Naphthalenes, Dibenzodioxins and Related Compounds
    • Goldstein, J.A.1    Safe, S.2
  • 11
    • 0026522195 scopus 로고
    • The dioxin and peroxisome proliferator-activated receptors: Nuclear receptors in search of endogenous ligands
    • Poellinger, L., Göttlicher, M., and Gustafsson, J.-Å., The dioxin and peroxisome proliferator-activated receptors: nuclear receptors in search of endogenous ligands, TiPS, 13, 241, 1992.
    • (1992) TiPS , vol.13 , pp. 241
    • Poellinger, L.1    Göttlicher, M.2    Gustafsson, J.-Å.3
  • 12
    • 0022555426 scopus 로고
    • The regulation of cytochrome P-450 gene expression
    • Whitlock, J. P., The regulation of cytochrome P-450 gene expression, Annu. Rev. Pharmacol. Toxicol., 26, 333, 1986.
    • (1986) Annu. Rev. Pharmacol. Toxicol. , vol.26 , pp. 333
    • Whitlock, J.P.1
  • 13
    • 0023251208 scopus 로고
    • The regulation of gene expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Whitlock, J. P., The regulation of gene expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin, Pharmacol. Rev., 39, 147, 1987.
    • (1987) Pharmacol. Rev. , vol.39 , pp. 147
    • Whitlock, J.P.1
  • 14
    • 0026725943 scopus 로고
    • Cloning of the Ah receptor cDNA reveals a distinctive ligand-activated transcription factor
    • Burbach, K. M., Poland, A., and Bradfield, C. A., Cloning of the Ah receptor cDNA reveals a distinctive ligand-activated transcription factor, Proc. Natl. Acad. Sci. U.S.A., 89, 8185, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8185
    • Burbach, K.M.1    Poland, A.2    Bradfield, C.A.3
  • 15
    • 0028033592 scopus 로고
    • Tissue specific expression of the rat Ah-receptor and ARNT mRNAs
    • Carver, L. A., Hogenesch, J. B., and Bradfield, C. A., Tissue specific expression of the rat Ah-receptor and ARNT mRNAs, Nucleic Acids Res., 22, 3038, 1994.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3038
    • Carver, L.A.1    Hogenesch, J.B.2    Bradfield, C.A.3
  • 17
    • 0026068698 scopus 로고
    • Role of the ligand in intracellular receptor function: Receptor affinity determines activation in vitro of the latent dioxin receptor to a DNA-binding form
    • Cuthill, S., Wilhelmsson, A., and Poellinger, L., Role of the ligand in intracellular receptor function: receptor affinity determines activation in vitro of the latent dioxin receptor to a DNA-binding form. Mol. Cell Biol., 11, 401, 1991.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 401
    • Cuthill, S.1    Wilhelmsson, A.2    Poellinger, L.3
  • 18
    • 0025959728 scopus 로고
    • Characterization of polyclonal antibodies to the Ah receptor prepared by immunization with a synthetic peptide hupten
    • Poland, A., Glover, E., and Bradfield, C., Characterization of polyclonal antibodies to the Ah receptor prepared by immunization with a synthetic peptide hupten, Mol. Pharmacol., 39, 20, 1991.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 20
    • Poland, A.1    Glover, E.2    Bradfield, C.3
  • 20
    • 0015528243 scopus 로고
    • Aryl hydrocarbon hydroxylase induction by polycyclic hydrocarbons is a simple autosomal dominant trait in the mouse
    • Nebert, D. W., Goujon, F. M., and Gielen, J. E., Aryl hydrocarbon hydroxylase induction by polycyclic hydrocarbons is a simple autosomal dominant trait in the mouse, Nature New Biol., 236, 107, 1972.
    • (1972) Nature New Biol. , vol.236 , pp. 107
    • Nebert, D.W.1    Goujon, F.M.2    Gielen, J.E.3
  • 21
    • 0015323626 scopus 로고
    • The genetics of aryl hydrocarbon hydroxylase induction in mice: A single gene difference between C57BL/6J and DBA/2J
    • Thomas, P. E., Kouri, R. E., and Hutton, J. J., The genetics of aryl hydrocarbon hydroxylase induction in mice: a single gene difference between C57BL/6J and DBA/2J, Biochem. Genet., 6, 157, 1972.
    • (1972) Biochem. Genet. , vol.6 , pp. 157
    • Thomas, P.E.1    Kouri, R.E.2    Hutton, J.J.3
  • 22
    • 0014590169 scopus 로고
    • The in vivo and in vitro induction of aryl hydrocarbon hydroxylase in mammalian cells of different species, tissues, strains, and developmental and hormonal states
    • Nebert, D. W. and Gelboin, H. V., The in vivo and in vitro induction of aryl hydrocarbon hydroxylase in mammalian cells of different species, tissues, strains, and developmental and hormonal states, Arch. of Biochem. Biophys., 134, 76, 1969.
    • (1969) Arch. of Biochem. Biophys. , vol.134 , pp. 76
    • Nebert, D.W.1    Gelboin, H.V.2
  • 23
    • 0015814427 scopus 로고
    • Nomenclature of genetically determined biochemical variants in mice
    • Green, M. C., Nomenclature of genetically determined biochemical variants in mice, Biochem. Genet., 9, 369, 1973.
    • (1973) Biochem. Genet. , vol.9 , pp. 369
    • Green, M.C.1
  • 24
    • 0015722751 scopus 로고
    • Chlorinated dibenzo-p-dioxins: Potent inducers of d-aminolevulinic acid synthetase and aryl hydrocarbon hydroxylase. II. A study of the structure activity relationship
    • Poland, A. and Glover, E., Chlorinated dibenzo-p-dioxins: potent inducers of d-aminolevulinic acid synthetase and aryl hydrocarbon hydroxylase. II. A study of the structure activity relationship, Mol. Pharmacol., 9, 737, 1973.
    • (1973) Mol. Pharmacol. , vol.9 , pp. 737
    • Poland, A.1    Glover, E.2
  • 25
    • 0018805844 scopus 로고
    • Studies on the mechanism of action of the chlorinated dibenzo-p-dioxins and related compounds
    • Poland, A., Greenlee, W. F., and Kende, A. S., Studies on the mechanism of action of the chlorinated dibenzo-p-dioxins and related compounds, Ann. N.Y. Acad. Sci., 30, 214, 1979.
    • (1979) Ann. N.Y. Acad. Sci. , vol.30 , pp. 214
    • Poland, A.1    Greenlee, W.F.2    Kende, A.S.3
  • 26
    • 0017145975 scopus 로고
    • Stereospecific, high-affinity binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin by hepatic cytosol
    • Poland, A., Glover, E., and Kende, A. S., Stereospecific, high-affinity binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin by hepatic cytosol, J. Biol. Chem., 251, 4936, 1976.
    • (1976) J. Biol. Chem. , vol.251 , pp. 4936
    • Poland, A.1    Glover, E.2    Kende, A.S.3
  • 27
    • 0025875527 scopus 로고
    • The Ah receptor and the mechanism of dioxin toxicity
    • Landers, J. P. and Bunce, N. J., The Ah receptor and the mechanism of dioxin toxicity, Biochem. J., 276, 273, 1991.
    • (1991) Biochem. J. , vol.276 , pp. 273
    • Landers, J.P.1    Bunce, N.J.2
  • 28
    • 0025719532 scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) and related compounds as antiestrogens: Characterization and mechanism of action
    • Safe, S., Astroff, B., Harris, M., Zacharewski, T., Dickerson, R., Romkes, M., and Biegel, L., 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) and related compounds as antiestrogens: characterization and mechanism of action, Pharmacol. Toxicol., 69, 400, 1991.
    • (1991) Pharmacol. Toxicol. , vol.69 , pp. 400
    • Safe, S.1    Astroff, B.2    Harris, M.3    Zacharewski, T.4    Dickerson, R.5    Romkes, M.6    Biegel, L.7
  • 29
    • 0027314196 scopus 로고
    • Characterization of the aryl hydrocarbon receptor and aryl hydrocarbon responsiveness in human ovarian carcinoma cell lines
    • Rowlands, C., Krishnan, V., Wang, X., Santostefano, M., Safe, S., Miller, W. R., and Langdon, S., Characterization of the aryl hydrocarbon receptor and aryl hydrocarbon responsiveness in human ovarian carcinoma cell lines, Cancer Res., 53, 1802, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 1802
    • Rowlands, C.1    Krishnan, V.2    Wang, X.3    Santostefano, M.4    Safe, S.5    Miller, W.R.6    Langdon, S.7
  • 31
    • 0016706001 scopus 로고
    • Genetic expression of aryl hydrocarbon hydroxylase by 2,3,7,8-tetrachlorodibenzo-p-dioxin: Evidence for a receptor mutation in genetically non-responsive mice
    • Poland, A. and Glover, E., Genetic expression of aryl hydrocarbon hydroxylase by 2,3,7,8-tetrachlorodibenzo-p-dioxin: evidence for a receptor mutation in genetically non-responsive mice, Mol. Pharmacol., 11, 389, 1975.
    • (1975) Mol. Pharmacol. , vol.11 , pp. 389
    • Poland, A.1    Glover, E.2
  • 32
    • 0024829409 scopus 로고
    • The Ah locus: Genetic differences in toxicity, cancer, mutation, and birth defects
    • Nebert, D. W., The Ah locus: genetic differences in toxicity, cancer, mutation, and birth defects, CRC Crit. Rev. Toxicol., 20, 153, 1989.
    • (1989) CRC Crit. Rev. Toxicol. , vol.20 , pp. 153
    • Nebert, D.W.1
  • 33
    • 0011397027 scopus 로고
    • The receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin: Similarities and dissimilarities with steroid hormone receptors
    • Moudgil, V. K., Ed., Walter de Gruyter & Co., Berlin
    • Poellinger, L., Lund, J., Gillner, M., and Gustafsson, J.-Å., The receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin: similarities and dissimilarities with steroid hormone receptors, in: Molecular Mechanisms of Steroid Hormone Action, Moudgil, V. K., Ed., Walter de Gruyter & Co., Berlin, 1985.
    • (1985) Molecular Mechanisms of Steroid Hormone Action
    • Poellinger, L.1    Lund, J.2    Gillner, M.3    Gustafsson, J.-Å.4
  • 35
    • 0026625037 scopus 로고
    • Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor
    • Reyes, H., Reiz-Porszasz, S., and 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, 1992.
    • (1992) Science , vol.256 , pp. 1193
    • Reyes, H.1    Reiz-Porszasz, S.2    Hankinson, O.3
  • 36
    • 0027184569 scopus 로고
    • PAS is a dimerization domain common to Drosophila Period and several transcription factors
    • Huang, Z. J., Edery, J. I., and Robash, M., PAS is a dimerization domain common to Drosophila Period and several transcription factors, Nature, 364, 259, 1993.
    • (1993) Nature , vol.364 , pp. 259
    • Huang, Z.J.1    Edery, J.I.2    Robash, M.3
  • 37
    • 0026314893 scopus 로고
    • The Drosophila single-minded gene encodes a helix-loop-helix protein that acts as a master regulator of CNS midline development
    • Nambu, J. R., Lewis, J. O., Wharton, K. A., and Crews, S. T., The Drosophila single-minded gene encodes a helix-loop-helix protein that acts as a master regulator of CNS midline development, Cell, 67, 1157, 1991.
    • (1991) Cell , vol.67 , pp. 1157
    • Nambu, J.R.1    Lewis, J.O.2    Wharton, K.A.3    Crews, S.T.4
  • 38
    • 0026798829 scopus 로고
    • Helix-loop-helix proteins in the regulation of immunoglobulin gene transcription
    • Kadesch, T., Helix-loop-helix proteins in the regulation of immunoglobulin gene transcription, Immun. Today, 13, 31, 1992.
    • (1992) Immun. Today , vol.13 , pp. 31
    • Kadesch, T.1
  • 39
    • 0027208834 scopus 로고
    • Consequences of heteromeric interactions among helix-loop-helix proteins
    • Kadesch, T., Consequences of heteromeric interactions among helix-loop-helix proteins, Cell Growth Diff., 4, 49, 1993.
    • (1993) Cell Growth Diff. , vol.4 , pp. 49
    • Kadesch, T.1
  • 40
    • 0028679626 scopus 로고
    • Transcription factors 2: Helix-loop-helix
    • Littlewood, T. D. and Evan, G. I., Transcription factors 2: helix-loop-helix, Protein Profile, 1, 639, 1994.
    • (1994) Protein Profile , vol.1 , pp. 639
    • Littlewood, T.D.1    Evan, G.I.2
  • 41
    • 0027439511 scopus 로고
    • Helix-loop-helix proteins as regulators of muscle-specific transcription
    • Edmondson, D. G. and Olson, E. N., Helix-loop-helix proteins as regulators of muscle-specific transcription, J. Biol. Chem., 268, 755, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 755
    • Edmondson, D.G.1    Olson, E.N.2
  • 44
    • 0028207310 scopus 로고
    • The aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator protein show distinct subcellular localizations in Hepa 1c1c7 cells by immunofluorescence microscopy
    • Pollenz, R. S., Sattler, C. A., and Poland, A., The aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator protein show distinct subcellular localizations in Hepa 1c1c7 cells by immunofluorescence microscopy, Mol. Pharmacol., 45, 428, 1994.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 428
    • Pollenz, R.S.1    Sattler, C.A.2    Poland, A.3
  • 45
    • 0026492934 scopus 로고
    • Circadian clock genes are ticking
    • Takahashi, J. S., Circadian clock genes are ticking, Science, 258, 238, 1992.
    • (1992) Science , vol.258 , pp. 238
    • Takahashi, J.S.1
  • 46
    • 0028816847 scopus 로고
    • Purification and characterization of hypoxia-inducible factor 1
    • Wang, G. L. and Semenza, G. L., Purification and characterization of hypoxia-inducible factor 1, J. Biol. Chem., 270, 1230, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1230
    • Wang, G.L.1    Semenza, G.L.2
  • 47
    • 0024458989 scopus 로고
    • Characterization of the gene for a protein kinase which phosphorylates the sporulation-regulatory proteins Spo0A and Spo0F of Bacillus subtilis
    • Perego, M., Cole, S. P., Burbulys, D., Trach, K., and Hoch, J. A., Characterization of the gene for a protein kinase which phosphorylates the sporulation-regulatory proteins Spo0A and Spo0F of Bacillus subtilis, J. Bacteriol., 171, 6187, 1989.
    • (1989) J. Bacteriol. , vol.171 , pp. 6187
    • Perego, M.1    Cole, S.P.2    Burbulys, D.3    Trach, K.4    Hoch, J.A.5
  • 48
    • 0023937550 scopus 로고
    • The aryl hydrocarbon (Ah) receptor
    • Safe, S. H., The aryl hydrocarbon (Ah) receptor, ISI Atlas Sci. Pharmacol., 2, 78, 1988.
    • (1988) ISI Atlas Sci. Pharmacol. , vol.2 , pp. 78
    • Safe, S.H.1
  • 49
    • 0028006520 scopus 로고
    • The Ah receptor: Mediator of the toxicity of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and related compounds
    • Okey, A. B., The Ah receptor: mediator of the toxicity of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and related compounds, Toxicol. Lett., 70, 1, 1994.
    • (1994) Toxicol. Lett. , vol.70 , pp. 1
    • Okey, A.B.1
  • 50
    • 0021088018 scopus 로고
    • Physiochemical characterization of specific and nonspecific polyaromatic hydrocarbon binders in rat and mouse liver cytosol
    • Poellinger, L., Lund, J., Gillner, M., Hansson, L.-A., and Gustafsson, J.-Å., Physiochemical characterization of specific and nonspecific polyaromatic hydrocarbon binders in rat and mouse liver cytosol, J. Biol. Chem., 258, 13535, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13535
    • Poellinger, L.1    Lund, J.2    Gillner, M.3    Hansson, L.-A.4    Gustafsson, J.-Å.5
  • 51
    • 0023653349 scopus 로고
    • Variation in the molecular mass of the Ah receptor among vertabrate species and strains of rats
    • Poland, A. and Glover, E., Variation in the molecular mass of the Ah receptor among vertabrate species and strains of rats, Biochem. Biophys. Res. Commun., 146, 1439, 1987.
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 1439
    • Poland, A.1    Glover, E.2
  • 52
    • 0021200784 scopus 로고
    • Cytosolic receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Evidence for a homologous nature among various mammalian species
    • Gasiewicz, T. A. and Rucci, G., Cytosolic receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Evidence for a homologous nature among various mammalian species, Mol. Pharmacol., 26, 90, 1984.
    • (1984) Mol. Pharmacol. , vol.26 , pp. 90
    • Gasiewicz, T.A.1    Rucci, G.2
  • 53
    • 0023654310 scopus 로고
    • The receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin in the mouse hepatoma cell line Hepa 1c1c7. A comparison with the glucocorticoid receptor and the mouse and rat hepatic dioxin receptors
    • Cuthill, S., Poellinger, L., and Gustafsson, J.-Å., The receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin in the mouse hepatoma cell line Hepa 1c1c7. A comparison with the glucocorticoid receptor and the mouse and rat hepatic dioxin receptors, J. Biol. Chem., 262, 3477, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3477
    • Cuthill, S.1    Poellinger, L.2    Gustafsson, J.-Å.3
  • 54
    • 0023033162 scopus 로고
    • Structure and function of the Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Species differences in the molecular properties of the receptors from mouse and rat hepatic cytosols
    • Denison, M. S., Vella, L. M., and Okey, A. B., Structure and function of the Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Species differences in the molecular properties of the receptors from mouse and rat hepatic cytosols, J. Biol. Chem., 261, 3987 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3987
    • Denison, M.S.1    Vella, L.M.2    Okey, A.B.3
  • 55
    • 0022975576 scopus 로고
    • Polyanionic properties of the receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Wilhelmsson, A., Wikström, A.-C., and Poellinger, L., Polyanionic properties of the receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin, J. Biol. Chem., 261, 13456, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13456
    • Wilhelmsson, A.1    Wikström, A.-C.2    Poellinger, L.3
  • 56
    • 0025220130 scopus 로고
    • The hepatic Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Species differences in subunit dissociation
    • Denison, M. and Vella, L., The hepatic Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Species differences in subunit dissociation, Arch. Biochem. Biophys., 277, 382, 1990.
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 382
    • Denison, M.1    Vella, L.2
  • 57
    • 0024400769 scopus 로고
    • Characterization of multiple forms of the Ah receptor: Comparison of species and tissues
    • Henry, E. C., Rucci, G., and Gasiewicz, T. A., Characterization of multiple forms of the Ah receptor: comparison of species and tissues, Biochemistry, 28, 6430, 1989.
    • (1989) Biochemistry , vol.28 , pp. 6430
    • Henry, E.C.1    Rucci, G.2    Gasiewicz, T.A.3
  • 58
    • 0024207289 scopus 로고
    • Physicochemical characterization of the nuclear form of Ah receptor from mouse hepatoma cells exposed in culture to 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Prokipcak, R. D. and Okey, A. B., Physicochemical characterization of the nuclear form of Ah receptor from mouse hepatoma cells exposed in culture to 2,3,7,8-tetrachlorodibenzo-p-dioxin, Arch. Biochem. Biophys., 267, 811, 1988.
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 811
    • Prokipcak, R.D.1    Okey, A.B.2
  • 59
    • 0025647768 scopus 로고
    • Nuclear Ah receptor from mouse hepatoma cells: Effect of partial proteolysis on relative molecular mass and DNA-binding properties
    • Prokipcak, R. D., Denison, M. S., and Okey, A. B., Nuclear Ah receptor from mouse hepatoma cells: effect of partial proteolysis on relative molecular mass and DNA-binding properties, Arch. Biochem. Biophys., 283, 476, 1990.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 476
    • Prokipcak, R.D.1    Denison, M.S.2    Okey, A.B.3
  • 60
    • 0023742858 scopus 로고
    • Association of the Ah receptor with the 90-kDa heat shock protein
    • Perdew, G. H., Association of the Ah receptor with the 90-kDa heat shock protein., J. Biol. Chem., 263, 13802, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13802
    • Perdew, G.H.1
  • 61
    • 0023741595 scopus 로고
    • Association of the dioxin receptor with the Mr 90,000 heat shock protein: A structural kinship with the glucocorticoid receptor
    • Denis, M., Cuthill, S., Wikstrom, A. C., Poellinger, L., and Gustafsson, J.-Å., Association of the dioxin receptor with the Mr 90,000 heat shock protein: a structural kinship with the glucocorticoid receptor. Biochem. Biophys. Res. Commun., 155, 801, 1988.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 801
    • Denis, M.1    Cuthill, S.2    Wikstrom, A.C.3    Poellinger, L.4    Gustafsson, J.-Å.5
  • 62
    • 0027970550 scopus 로고
    • Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex
    • Chen, H. S. and Perdew, G. H., Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex, J. Biol. Chem., 269, 27554, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27554
    • Chen, H.S.1    Perdew, G.H.2
  • 63
    • 0019829563 scopus 로고
    • Regulatory gene product of the Ah complex. Comparison of 2,3,7,8-tetrachlorodibenzo-p-dioxin and 3-methylcholanthrene binding to several moiteies in mouse liver cytosol
    • Hannah, R. R., Nebert, D. W., and Eisen, H. J., Regulatory gene product of the Ah complex. Comparison of 2,3,7,8-tetrachlorodibenzo-p-dioxin and 3-methylcholanthrene binding to several moiteies in mouse liver cytosol, J. Biol. Chem., 256, 4584, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4584
    • Hannah, R.R.1    Nebert, D.W.2    Eisen, H.J.3
  • 64
    • 0019291033 scopus 로고
    • Temperature-dependent cytosol-to-nucleus translocation of the Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin in continuous cell culture
    • Okey, A. B., Bondy, G. P., Mason, M. E., Nebert, D. W., Forster-Gibson, C. J., and Dufresne, M. J., Temperature-dependent cytosol-to-nucleus translocation of the Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin in continuous cell culture, J. Biol. Chem., 255, 11415, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11415
    • Okey, A.B.1    Bondy, G.P.2    Mason, M.E.3    Nebert, D.W.4    Forster-Gibson, C.J.5    Dufresne, M.J.6
  • 65
    • 0021324451 scopus 로고
    • 2.3,7,8-Tetrachlorodibenzo-p-dioxin receptors in wild type and variant mouse hepatoma cells. Nuclear location and strength of nuclear binding
    • Whitlock, J., Jr. and Galeazzi, D. R., 2.3,7,8-Tetrachlorodibenzo-p-dioxin receptors in wild type and variant mouse hepatoma cells. Nuclear location and strength of nuclear binding, J. Biol. Chem., 259, 980, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 980
    • Whitlock Jr., J.1    Galeazzi, D.R.2
  • 66
    • 0022472821 scopus 로고
    • Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Codistribution of unoccupied receptor with cytosolic marker enzymes during fractionation of mouse liver, rat liver, and cultured Hepa 1c1c7 cells
    • Denison, M. S., Harper, P. A., and Okey, A. B., Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Codistribution of unoccupied receptor with cytosolic marker enzymes during fractionation of mouse liver, rat liver, and cultured Hepa 1c1c7 cells, Eur. J. Biochem., 155, 223, 1986.
    • (1986) Eur. J. Biochem. , vol.155 , pp. 223
    • Denison, M.S.1    Harper, P.A.2    Okey, A.B.3
  • 68
    • 0027944707 scopus 로고
    • Physicochemical and immunocytochemical analysis of the aryl hydrocarbon receptor nuclear translocator: Characterization of two monoclonal antibodies to the aryl hydrocarbon receptor nuclear translocator
    • Hord, N. G. and Perdew, G. H., Physicochemical and immunocytochemical analysis of the aryl hydrocarbon receptor nuclear translocator: characterization of two monoclonal antibodies to the aryl hydrocarbon receptor nuclear translocator, Mol. Pharmacol., 46, 618, 1994.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 618
    • Hord, N.G.1    Perdew, G.H.2
  • 69
    • 0018603346 scopus 로고
    • Nuclear uptake of 2,3,7,8-tetrachlorodibenzo-p-dioxin in C57B1/6J and DBA/2J mice
    • Greenlee, W. F. and Poland, A., Nuclear uptake of 2,3,7,8-tetrachlorodibenzo-p-dioxin in C57B1/6J and DBA/2J mice, J. Biol. Chem., 254, 9814, 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9814
    • Greenlee, W.F.1    Poland, A.2
  • 70
    • 0027403810 scopus 로고
    • Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor
    • Whitelaw, M., Pongratz, I., Wilhelmsson, A., Gustafsson, J.-Å., and Poellinger, L., Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor, Mol. Cell. Biol., 13, 2504, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2504
    • Whitelaw, M.1    Pongratz, I.2    Wilhelmsson, A.3    Gustafsson, J.-Å.4    Poellinger, L.5
  • 71
    • 0025969240 scopus 로고
    • Characterization of the interaction of transformed rat hepatic cytosolic Ah receptor with a dioxin responsive transcriptional enhancer
    • Denison, M. S. and Yao, E. F., Characterization of the interaction of transformed rat hepatic cytosolic Ah receptor with a dioxin responsive transcriptional enhancer, Arch. Biochem. Biophys., 284, 158, 1991.
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 158
    • Denison, M.S.1    Yao, E.F.2
  • 72
    • 0025157272 scopus 로고
    • The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein
    • Wilhelmsson, A., Cuthill, S., Denis, M., Wikström, A. C., Gustafsson, J.-Å., and Poellinger, L., The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein, EMBO J., 9, 69, 1990.
    • (1990) EMBO J. , vol.9 , pp. 69
    • Wilhelmsson, A.1    Cuthill, S.2    Denis, M.3    Wikström, A.C.4    Gustafsson, J.-Å.5    Poellinger, L.6
  • 73
    • 0025815731 scopus 로고
    • Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000
    • Perdew, G. H. and Whitelaw, M. L., Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000, J. Biol. Chem., 266, 6708, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6708
    • Perdew, G.H.1    Whitelaw, M.L.2
  • 74
    • 0028296576 scopus 로고
    • A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor
    • McGuire, J., Whitelaw, M. L., Pongratz, I., Gustafsson, J.-Å., and Poellinger, L., A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor, Mol. Cell. Biol., 14, 2438, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2438
    • McGuire, J.1    Whitelaw, M.L.2    Pongratz, I.3    Gustafsson, J.-Å.4    Poellinger, L.5
  • 75
    • 0023061373 scopus 로고
    • P450 genes: Structure, evolution and regulation
    • Nebert, D. W. and Gonzalez, F. J., P450 genes: structure, evolution and regulation. Annu. Rev. Biochem., 56, 945, 1987.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 945
    • Nebert, D.W.1    Gonzalez, F.J.2
  • 76
    • 0020448952 scopus 로고
    • The Ah locus: Correlation of intranuclear appearance of inducer-receptor complex with induction of cytochrome P-450 mRNA
    • Tukey, R. H., Hannah, R. R., Negishi, M., Nebert, D. W., and Eisen, H. J., The Ah locus: correlation of intranuclear appearance of inducer-receptor complex with induction of cytochrome P-450 mRNA, Cell, 31, 275, 1982.
    • (1982) Cell , vol.31 , pp. 275
    • Tukey, R.H.1    Hannah, R.R.2    Negishi, M.3    Nebert, D.W.4    Eisen, H.J.5
  • 77
    • 0021289379 scopus 로고
    • Regulation of cytochrome P1-450 gene transcription by 2,3,7,8-tetrachlorodibezo-p-dioxin in wild type and variant mouse hepatoma cells
    • Israel, D. I. and Whitlock, J. P., Jr., Regulation of cytochrome P1-450 gene transcription by 2,3,7,8-tetrachlorodibezo-p-dioxin in wild type and variant mouse hepatoma cells, J. Biol. Chem., 259, 5400, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5400
    • Israel, D.I.1    Whitlock Jr., J.P.2
  • 78
    • 0347393109 scopus 로고
    • Location of regulatory elements responsible for drug induction in the rat cytochrome P-450c gene
    • Sogawa, K., Fujisawa-Sehara, A., Yamane, M., and Fuji-Kuriyama, Y., Location of regulatory elements responsible for drug induction in the rat cytochrome P-450c gene, Proc. Natl. Acad. Sci. U.S.A., 83, 8044, 1986.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8044
    • Sogawa, K.1    Fujisawa-Sehara, A.2    Yamane, M.3    Fuji-Kuriyama, Y.4
  • 79
    • 0024210678 scopus 로고
    • The DNA recognition site for the dioxin-Ah receptor complex
    • Denison, M. S., Fisher, J. M., and Whitlock, J. P., Jr., The DNA recognition site for the dioxin-Ah receptor complex, J. Biol. Chem., 263, 17221, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17221
    • Denison, M.S.1    Fisher, J.M.2    Whitlock Jr., J.P.3
  • 80
    • 0021060932 scopus 로고
    • Induction of mRNA specific for cytochrome P1-450 in wild type and variant mouse hepatoma cells
    • Israel, D. I. and Whitlock, J. P., Jr., Induction of mRNA specific for cytochrome P1-450 in wild type and variant mouse hepatoma cells, J. Biol. Chem., 258, 10390, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10390
    • Israel, D.I.1    Whitlock Jr., J.P.2
  • 81
    • 0023665615 scopus 로고
    • Characterization of xenobiotic responsive elements upstream from the drug-metabolizing cytochrome P-450c gene. A similarity to glucocorticoid regulatory elements
    • Fujisawa-Sehara, A., Sogawa, K., Yamane, M., and Fuji-Kuriyama, Y., Characterization of xenobiotic responsive elements upstream from the drug-metabolizing cytochrome P-450c gene. A similarity to glucocorticoid regulatory elements, Nucleic Acids Res., 15, 4179, 1987.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 4179
    • Fujisawa-Sehara, A.1    Sogawa, K.2    Yamane, M.3    Fuji-Kuriyama, Y.4
  • 82
    • 0022432447 scopus 로고
    • Autoregulation plus upstream positive and negative control regions associated with transcriptional activation of the mouse cytochrome P1-450 gene
    • Gonzalez, F. J. and Nebert, D. W., Autoregulation plus upstream positive and negative control regions associated with transcriptional activation of the mouse cytochrome P1-450 gene, Nucleic Acids Res., 13, 7269, 1985.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 7269
    • Gonzalez, F.J.1    Nebert, D.W.2
  • 83
    • 0021895358 scopus 로고
    • Control of cytochrome P1-450 gene expression by dioxin
    • Jones, P. B., Galeazzi, D. R., Fisher, J. M., and Whitlock, J. P., Jr., Control of cytochrome P1-450 gene expression by dioxin. Science, 227, 1499, 1985.
    • (1985) Science , vol.227 , pp. 1499
    • Jones, P.B.1    Galeazzi, D.R.2    Fisher, J.M.3    Whitlock Jr., J.P.4
  • 84
    • 0022721693 scopus 로고
    • Control of cytochrome P1-450 gene expression: Analysis of a dioxin-responsive enhancer system
    • Jones, P. B. C., Durrin, L. K., Galeazzi, D. R. and Whitlock, J. P., Jr., Control of cytochrome P1-450 gene expression: Analysis of a dioxin-responsive enhancer system, Proc. Natl. Acad. Sci. U.S.A., 83, 2802, 1986.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 2802
    • Jones, P.B.C.1    Durrin, L.K.2    Galeazzi, D.R.3    Whitlock Jr., J.P.4
  • 85
    • 0024462025 scopus 로고
    • Protein-DNA interaction at recognition sites for the dioxin-Ah receptor complex
    • Denison, M. S., Fisher, J. M., and Whitlock, J. P., Jr., Protein-DNA interaction at recognition sites for the dioxin-Ah receptor complex, J. Biol. Chem., 264, 16478, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16478
    • Denison, M.S.1    Fisher, J.M.2    Whitlock Jr., J.P.3
  • 86
    • 0028556386 scopus 로고
    • Purification to homogeneity of the heteromeric DNA-binding form of the aryl hydrocarbon receptor from rat liver
    • Henry, E. C., Rucci, G., and Gasiewicz, T. A., Purification to homogeneity of the heteromeric DNA-binding form of the aryl hydrocarbon receptor from rat liver, Mol. Pharmacol., 46, 1022, 1994.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 1022
    • Henry, E.C.1    Rucci, G.2    Gasiewicz, T.A.3
  • 87
    • 0029042132 scopus 로고
    • The DNA binding of purified Ah receptor heterodimer is regulated by redox conditions
    • Ireland, R. C., Li, S. Y., and Dougherty, J. J., The DNA binding of purified Ah receptor heterodimer is regulated by redox conditions, Arch. Biochem. Biophys., 319, 470, 1995.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 470
    • Ireland, R.C.1    Li, S.Y.2    Dougherty, J.J.3
  • 88
    • 0028510057 scopus 로고
    • Dioxin-dependent, DNA sequence-specific binding of a multiprotein complex containing the Ah receptor
    • Elferink, C. J. and Whitlock, J., Jr., Dioxin-dependent, DNA sequence-specific binding of a multiprotein complex containing the Ah receptor. Receptor, 4, 157, 1994.
    • (1994) Receptor , vol.4 , pp. 157
    • Elferink, C.J.1    Whitlock Jr., J.2
  • 89
    • 33751385798 scopus 로고
    • Binding of transformed Ah receptor complex to a dioxin responsive transcriptional enhancer: Evidence for two distinct heteromeric DNA-binding forms
    • Swanson, H. I., Tullis, K., and Denison, M. S., Binding of transformed Ah receptor complex to a dioxin responsive transcriptional enhancer: evidence for two distinct heteromeric DNA-binding forms, Biochemistry, 32, 12841, 1993.
    • (1993) Biochemistry , vol.32 , pp. 12841
    • Swanson, H.I.1    Tullis, K.2    Denison, M.S.3
  • 90
    • 0027467437 scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin induces the nuclear translocation of two XRE binding proteins in mice
    • Okino, S. T., Pendurthi, U. R., and Tukey, R. H., 2,3,7,8-Tetrachlorodibenzo-p-dioxin induces the nuclear translocation of two XRE binding proteins in mice, Pharmacogenetics, 3, 101, 1993.
    • (1993) Pharmacogenetics , vol.3 , pp. 101
    • Okino, S.T.1    Pendurthi, U.R.2    Tukey, R.H.3
  • 91
    • 0029283558 scopus 로고
    • Evidence for two functionally distinct forms of the human Ah receptor
    • Perdew, G. H. and Holenback, C. E., Evidence for two functionally distinct forms of the human Ah receptor, J. Biochem. Toxicol., 10, 95, 1995.
    • (1995) J. Biochem. Toxicol. , vol.10 , pp. 95
    • Perdew, G.H.1    Holenback, C.E.2
  • 92
    • 0027973453 scopus 로고
    • Baculovirus expression of the Ah receptor and Ah receptor nuclear translocator - Evidence for additional dioxin responsive element-binding species and factors required for signaling
    • Chan, W. K., Chu, R. Y., Jain, S., Reddy, J. K., and Bradfield, C. A., Baculovirus expression of the Ah receptor and Ah receptor nuclear translocator - evidence for additional dioxin responsive element-binding species and factors required for signaling. J. Biol. Chem., 269, 26464, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26464
    • Chan, W.K.1    Chu, R.Y.2    Jain, S.3    Reddy, J.K.4    Bradfield, C.A.5
  • 93
    • 0023803055 scopus 로고
    • Identification of multiple regulatory elements on the human cytochrome P450IA1 gene
    • Hines, R. N., Mathis, J. M., and Jacob, C. S., Identification of multiple regulatory elements on the human cytochrome P450IA1 gene, Carcinogenesis, 9, 1599, 1988.
    • (1988) Carcinogenesis , vol.9 , pp. 1599
    • Hines, R.N.1    Mathis, J.M.2    Jacob, C.S.3
  • 94
    • 0026644794 scopus 로고
    • Protein-DNA interactions at the dioxin-responsive enhancer
    • Shen, E. S. and Whitlock, J. P., Jr., Protein-DNA interactions at the dioxin-responsive enhancer, J. Biol. Chem., 267, 6815, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6815
    • Shen, E.S.1    Whitlock Jr., J.P.2
  • 95
    • 0027532636 scopus 로고
    • Protein-DNA interactions at a dioxin-responsive enhancer. Analysis of six bona fide DNA-binding sites for the liganded Ah receptor
    • Lusska, A., Shen, E., and Whitlock, J., Jr., Protein-DNA interactions at a dioxin-responsive enhancer. Analysis of six bona fide DNA-binding sites for the liganded Ah receptor, J. Biol. Chem., 268, 6575, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6575
    • Lusska, A.1    Shen, E.2    Whitlock Jr., J.3
  • 96
    • 0026643609 scopus 로고
    • DNA sequence determinants for binding of transformed Ah receptor to a dioxin-responsive enhancer
    • Yao, E. F. and Denison, M. S., DNA sequence determinants for binding of transformed Ah receptor to a dioxin-responsive enhancer. Biochemistry, 31, 5060, 1992.
    • (1992) Biochemistry , vol.31 , pp. 5060
    • Yao, E.F.1    Denison, M.S.2
  • 97
    • 0024467620 scopus 로고
    • The potential role of DNA methylution in the response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Shen, E. S. and Whitlock, J. P., Jr., The potential role of DNA methylution in the response to 2,3,7,8-tetrachlorodibenzo-p-dioxin, J. Biol. Chem., 264, 17754, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17754
    • Shen, E.S.1    Whitlock Jr., J.P.2
  • 98
    • 0025307742 scopus 로고
    • Genetic and molecular aspects of 2,3,7,8-tetrachlorodibenzo-p-dioxin action
    • Whitlock, J. P., Jr., Genetic and molecular aspects of 2,3,7,8-tetrachlorodibenzo-p-dioxin action, Annu. Rev. Pharmacol. Toxicol., 30, 251, 1990.
    • (1990) Annu. Rev. Pharmacol. Toxicol. , vol.30 , pp. 251
    • Whitlock Jr., J.P.1
  • 99
    • 0026052405 scopus 로고
    • Diversity and specificity in transcriptional regulation: The benefits of heterotypic dimerization
    • Lamb, P. and McKnight, S. L., Diversity and specificity in transcriptional regulation: the benefits of heterotypic dimerization. Trends Biol. Sci., 16, 417, 1991.
    • (1991) Trends Biol. Sci. , vol.16 , pp. 417
    • Lamb, P.1    McKnight, S.L.2
  • 100
    • 0028908504 scopus 로고
    • Orientation of the heterodimeric aryl hydrocarbon (dioxin) receptor complex on its asymmetric DNA recognition sequence
    • Bacsi, S. G., Reiszporszasz, S., and Hankinson, O., Orientation of the heterodimeric aryl hydrocarbon (dioxin) receptor complex on its asymmetric DNA recognition sequence, Mol. Pharmacol., 47, 432, 1995.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 432
    • Bacsi, S.G.1    Reiszporszasz, S.2    Hankinson, O.3
  • 101
    • 0028865103 scopus 로고
    • DNA binding specificities and pairing rules of the Ah receptor, ARNT, and SIM proteins
    • Swanson, H. I., Chan, W. K., and Bradfield, C. A., DNA binding specificities and pairing rules of the Ah receptor, ARNT, and SIM proteins, J. Biol. Chem., 270, 26292, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26292
    • Swanson, H.I.1    Chan, W.K.2    Bradfield, C.A.3
  • 102
    • 0025675615 scopus 로고
    • Serum and extracellular calcium modulate induction of cytochrome P-450IA1 in human keratinocytes
    • Berghard, A., Gradin, K., and Toftgard, R., Serum and extracellular calcium modulate induction of cytochrome P-450IA1 in human keratinocytes, J. Biol. Chem., 265, 21086, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21086
    • Berghard, A.1    Gradin, K.2    Toftgard, R.3
  • 103
    • 0026669306 scopus 로고
    • Phorbol esters inhibit the dioxin receptor-mediated transcriptional activation of the mouse CypIa-1 and CypIa-2 genes by 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Okino, S. T., Pendurthi, U. R., and Tukey, R. H., Phorbol esters inhibit the dioxin receptor-mediated transcriptional activation of the mouse CypIa-1 and CypIa-2 genes by 2,3,7,8-tetrachlorodibenzo-p-dioxin, J. Biol. Chem., 267, 6991, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6991
    • Okino, S.T.1    Pendurthi, U.R.2    Tukey, R.H.3
  • 104
    • 0026559509 scopus 로고
    • Dioxin-dependent activation of murine Cypla-1 gene transcription requires protein kinase C-dependent phosphorylation
    • Carrier, F., Owens, R. A., Nebert, D. W., and Puga, A., Dioxin-dependent activation of murine Cypla-1 gene transcription requires protein kinase C-dependent phosphorylation, Mol. Cell. Biol., 12, 1856, 1992.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1856
    • Carrier, F.1    Owens, R.A.2    Nebert, D.W.3    Puga, A.4
  • 105
    • 0027473240 scopus 로고
    • Cross-coupling of signal transduction pathways: The dioxin receptor mediates induction of cytochrome P-450IA1 expression via a protein kinase C-dependent mechanism
    • Berghard, A., Gradin, K., Pongratz, I., Whitelaw, M., and Poellinger, L., Cross-coupling of signal transduction pathways: the dioxin receptor mediates induction of cytochrome P-450IA1 expression via a protein kinase C-dependent mechanism, Mol. Cell. Biol., 13, 677, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 677
    • Berghard, A.1    Gradin, K.2    Pongratz, I.3    Whitelaw, M.4    Poellinger, L.5
  • 106
    • 0026056609 scopus 로고
    • Inhibition of the specific DNA binding activity of the dioxin receptor by phosphatase treatment
    • Pongratz, I., Stromstedt, P. E., Mason, G. G., and Poellinger, L., Inhibition of the specific DNA binding activity of the dioxin receptor by phosphatase treatment, J. Biol. Chem., 266, 16813, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16813
    • Pongratz, I.1    Stromstedt, P.E.2    Mason, G.G.3    Poellinger, L.4
  • 108
    • 0027169125 scopus 로고
    • In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition
    • Dolwick, K. M., Swanson, H. I., and Bradfield, C. A., In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition, Proc. Natl. Acad. Sci. U.S.A., 90, 8566, 1993.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8566
    • Dolwick, K.M.1    Swanson, H.I.2    Bradfield, C.A.3
  • 109
    • 0028943250 scopus 로고
    • Ah receptor phosphorylation - Localization of phosphorylation sites to the c-terminal half of the protein
    • Mahon, M. J. and Gasiewicz, T. A., Ah receptor phosphorylation - localization of phosphorylation sites to the c-terminal half of the protein, Arch. Biochem. Biophys., 318, 166, 1995.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 166
    • Mahon, M.J.1    Gasiewicz, T.A.2
  • 110
    • 0025217856 scopus 로고
    • The MyoD DNA binding domain contains a recognition code tor muscle-specific gene activation
    • Davis, R. L., Cheng, P.-F., Lasser, A. B., and Weintraub, H., The MyoD DNA binding domain contains a recognition code tor muscle-specific gene activation, Cell, 60, 733, 1990.
    • (1990) Cell , vol.60 , pp. 733
    • Davis, R.L.1    Cheng, P.-F.2    Lasser, A.B.3    Weintraub, H.4
  • 111
    • 0025341295 scopus 로고
    • Mutations that disrupt DNA binding and dimer formation in the E47 helix-loop-helix protein map to distinct domains
    • Voronova, A. and Baltimore, D., Mutations that disrupt DNA binding and dimer formation in the E47 helix-loop-helix protein map to distinct domains, Proc. Natl. Acad. Sci. U.S.A., 87, 4722, 1990.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4722
    • Voronova, A.1    Baltimore, D.2
  • 113
    • 0028144972 scopus 로고
    • Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT)
    • Reisz-Porszasz, S., Probst, M. R., Fukunaga, B. N., and Hankinson, O., Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT), Mol. Cell. Biol., 14, 6075, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6075
    • Reisz-Porszasz, S.1    Probst, M.R.2    Fukunaga, B.N.3    Hankinson, O.4
  • 114
    • 0028858813 scopus 로고
    • Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains
    • Antonsson, C., Whitelaw, M. L., McGuire, J., Gustafsson, J.-Å., and Poellinger, L., Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains, Mol. Cell. Biol. 15, 756, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 756
    • Antonsson, C.1    Whitelaw, M.L.2    McGuire, J.3    Gustafsson, J.-Å.4    Poellinger, L.5
  • 115
    • 0029017976 scopus 로고
    • Protein-protein interaction via pas domains - Role of the pas domain in positive and negative regulation of the bhlh/pas dioxin receptor-arnt transcription factor complex
    • Lindebro, M. C., Poellinger, L., and Whitelaw, M. L., Protein-protein interaction via pas domains - role of the pas domain in positive and negative regulation of the bhlh/pas dioxin receptor-arnt transcription factor complex, EMBO J., 14, 3528, 1995.
    • (1995) EMBO J. , vol.14 , pp. 3528
    • Lindebro, M.C.1    Poellinger, L.2    Whitelaw, M.L.3
  • 116
    • 0027522075 scopus 로고
    • Definition of a novel ligand binding domain of a nuclear bHLH receptor: Co-localization of ligand and hsp90 binding activities within the regulable inactivation domain of the dioxin receptor
    • Whitelaw, M. L., Göttlicher, M., Gustafsson, J.-Å., and Poellinger, L., Definition of a novel ligand binding domain of a nuclear bHLH receptor: co-localization of ligand and hsp90 binding activities within the regulable inactivation domain of the dioxin receptor, EMBO J, 12, 4169, 1993.
    • (1993) EMBO J , vol.12 , pp. 4169
    • Whitelaw, M.L.1    Göttlicher, M.2    Gustafsson, J.-Å.3    Poellinger, L.4
  • 117
    • 0028823398 scopus 로고
    • Definition of a minimal domain of the dioxin receptor that is associated with hsp90 and maintains wild type ligand binding affinity and specificity
    • Coumailleau, P., Poellinger, L., Gustafsson, J.-Å., and Whitelaw, M. L., Definition of a minimal domain of the dioxin receptor that is associated with hsp90 and maintains wild type ligand binding affinity and specificity, J. Biol. Chem., 270, 25291, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25291
    • Coumailleau, P.1    Poellinger, L.2    Gustafsson, J.-Å.3    Whitelaw, M.L.4
  • 118
    • 0025763419 scopus 로고
    • Max: A helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc
    • Blackwood, E. M. and Eisenman, R. N., Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc, Science, 251, 1211, 1991.
    • (1991) Science , vol.251 , pp. 1211
    • Blackwood, E.M.1    Eisenman, R.N.2
  • 120
    • 0022384065 scopus 로고
    • Interactions of indoles with specific binding sites for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver
    • Gillner, M., Bergman, J., Cambillan, C., Fernstrom, B., and Gustafsson, J.-A., Interactions of indoles with specific binding sites for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver, Mol. Pharmacol., 28, 357, 1985.
    • (1985) Mol. Pharmacol. , vol.28 , pp. 357
    • Gillner, M.1    Bergman, J.2    Cambillan, C.3    Fernstrom, B.4    Gustafsson, J.-A.5
  • 121
    • 0026693657 scopus 로고
    • In vitro activation of the dioxin receptor to a DNA-binding form by food-borne heterocyclic amines
    • Kleman, M. I., Overvik, E., Mason, G. G., and Gustafsson, J.-Å., In vitro activation of the dioxin receptor to a DNA-binding form by food-borne heterocyclic amines, Carcinogenesis, 13, 1619, 1992.
    • (1992) Carcinogenesis , vol.13 , pp. 1619
    • Kleman, M.I.1    Overvik, E.2    Mason, G.G.3    Gustafsson, J.-Å.4
  • 122
    • 0023616773 scopus 로고
    • Certain photooxidized derivatives of tryptophan bind with very high affinity to the Ah receptor and are likely to be endogenous signal substances
    • Rannug, A., Rannug, U., Rosenkranz, H. S., Winqvist, L., Westerholm, R., Agurell, E., and Grafstrom, A.-K., Certain photooxidized derivatives of tryptophan bind with very high affinity to the Ah receptor and are likely to be endogenous signal substances, J. Biol. Chem., 262, 15422, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15422
    • Rannug, A.1    Rannug, U.2    Rosenkranz, H.S.3    Winqvist, L.4    Westerholm, R.5    Agurell, E.6    Grafstrom, A.-K.7
  • 123
    • 0024566306 scopus 로고
    • Interactions of rutaecarpine alkaloids with specific binding sites for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver
    • Gillner, M., Bergman, J., Cambillau, C., and Gustafsson, J.-Å., Interactions of rutaecarpine alkaloids with specific binding sites for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver, Carcinogenesis, 10, 651, 1989.
    • (1989) Carcinogenesis , vol.10 , pp. 651
    • Gillner, M.1    Bergman, J.2    Cambillau, C.3    Gustafsson, J.-Å.4
  • 124
    • 0019203127 scopus 로고
    • Keratinization of mouse teratoma cell line XB produced by 2,3,7,8-tetrachlorodibenzo-p-dioxin: An in vitro model of toxicity
    • Knutson, J. C. and Poland, A., Keratinization of mouse teratoma cell line XB produced by 2,3,7,8-tetrachlorodibenzo-p-dioxin: an in vitro model of toxicity, Cell, 22, 27, 1980.
    • (1980) Cell , vol.22 , pp. 27
    • Knutson, J.C.1    Poland, A.2
  • 125
    • 0027521742 scopus 로고
    • Mechanistic aspects of dioxin action
    • Whitlock, J., Jr., Mechanistic aspects of dioxin action., Chem. Res. Toxicol., 6: 754, 1993.
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 754
    • Whitlock Jr., J.1
  • 127
    • 0021755245 scopus 로고
    • Regulation of mouse cytochrome P3-450 by the Ah receptor. Studies with a P3-450 cDNA clone
    • Tukey, R. H. and Nebert, D. W., Regulation of mouse cytochrome P3-450 by the Ah receptor. Studies with a P3-450 cDNA clone, Biochemistry, 23, 6003, 1984.
    • (1984) Biochemistry , vol.23 , pp. 6003
    • Tukey, R.H.1    Nebert, D.W.2
  • 128
    • 0021140707 scopus 로고
    • Synthesis and characterization of twenty-two purified polychlorinated dibenzofuran congeners
    • Safe, S. and Safe, L., Synthesis and characterization of twenty-two purified polychlorinated dibenzofuran congeners, J. Agric. Food Chem., 32, 68, 1984.
    • (1984) J. Agric. Food Chem. , vol.32 , pp. 68
    • Safe, S.1    Safe, L.2
  • 129
    • 0022969614 scopus 로고
    • The cytosolic binding affinities and AHH induction potencies of 29 polynuclear aromatic hydrocarbons
    • Piskorska-Pliszczynska, J., Keys, B., Safe, S., and Newman, M. S., The cytosolic binding affinities and AHH induction potencies of 29 polynuclear aromatic hydrocarbons., Toxicol.Lett., 34, 67, 1986.
    • (1986) Toxicol.Lett. , vol.34 , pp. 67
    • Piskorska-Pliszczynska, J.1    Keys, B.2    Safe, S.3    Newman, M.S.4
  • 130
    • 0027295906 scopus 로고
    • Interactions of indolo[3,2-b] carbazoles and related polycyclic aromatic hydrocarbons with specific binding sites for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver
    • Gillner, M., Bergman, J., Cambillau, C., Alexandersson, M., Fernstrom, B., and Gustafsson, J.-Å., Interactions of indolo[3,2-b] carbazoles and related polycyclic aromatic hydrocarbons with specific binding sites for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver, Mol. Pharmacol., 44, 336, 1993.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 336
    • Gillner, M.1    Bergman, J.2    Cambillau, C.3    Alexandersson, M.4    Fernstrom, B.5    Gustafsson, J.-Å.6
  • 131
    • 0028978788 scopus 로고
    • Three-dimensional quantitative structure-activity relationships of dioxins and dioxin-like compounds - Model validation and Ah receptor characterization
    • Waller, C. L. and Mckinney, J. D., Three-dimensional quantitative structure-activity relationships of dioxins and dioxin-like compounds - model validation and Ah receptor characterization, Chem. Res. Toxicol., 8, 847, 1995.
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 847
    • Waller, C.L.1    Mckinney, J.D.2
  • 132
    • 0027944549 scopus 로고
    • Analysis of the four alleles of the murine aryl hydrocarbon receptor
    • Poland, A., Palen, D., and Glover, E., Analysis of the four alleles of the murine aryl hydrocarbon receptor, Mol. Pharmacol., 46, 915, 1994.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 915
    • Poland, A.1    Palen, D.2    Glover, E.3
  • 133
    • 0015955055 scopus 로고
    • Comparison of 2,3,7,8-tetrachlorodibenzo-p-dioxin, a potent inducer of aryl hydrocarbon hydroxylase, with 3-methylcholanthrene
    • Poland, A. and Glover, E., Comparison of 2,3,7,8-tetrachlorodibenzo-p-dioxin, a potent inducer of aryl hydrocarbon hydroxylase, with 3-methylcholanthrene, Mol. Pharmacol., 10, 349, 1974.
    • (1974) Mol. Pharmacol. , vol.10 , pp. 349
    • Poland, A.1    Glover, E.2
  • 134
    • 0024337946 scopus 로고
    • Detection and characterization of a low affinity form of cytosolic Ah receptor in livers of mice nonresponsive to induction of cytochrome P1-450 by 3-methylcholanthrene
    • Okey, A. B., Vella, L. M., and Harper, P. A., Detection and characterization of a low affinity form of cytosolic Ah receptor in livers of mice nonresponsive to induction of cytochrome P1-450 by 3-methylcholanthrene, Mol. Pharmacol., 35, 823, 1989.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 823
    • Okey, A.B.1    Vella, L.M.2    Harper, P.A.3
  • 135
    • 0028034621 scopus 로고
    • Dioxin binding activities of polymorphic forms of mouse and human aryl hydrocarbon receptors
    • Ema, M., Ohe, N., Suzuki, M., Mimura, J., Sogawa, K., Ikawa, S., and Fujii-Kuriyama, Y., Dioxin binding activities of polymorphic forms of mouse and human aryl hydrocarbon receptors, J. Biol. Chem., 269, 27337, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27337
    • Ema, M.1    Ohe, N.2    Suzuki, M.3    Mimura, J.4    Sogawa, K.5    Ikawa, S.6    Fujii-Kuriyama, Y.7
  • 136
    • 0023885681 scopus 로고
    • Characterization of the Ah receptor and aryl hydrocarbon hydroxylase induction by 2,3,7,8-tetrachlorodibenzo-p-dioxin and benz(a)anthracene in the human A431 squamous cell carcinoma line
    • Harper, P. A., Golas, C. L., and Okey, A. B., Characterization of the Ah receptor and aryl hydrocarbon hydroxylase induction by 2,3,7,8-tetrachlorodibenzo-p-dioxin and benz(a)anthracene in the human A431 squamous cell carcinoma line, Cancer Research, 48, 2388, 1988.
    • (1988) Cancer Research , vol.48 , pp. 2388
    • Harper, P.A.1    Golas, C.L.2    Okey, A.B.3
  • 137
    • 0027447541 scopus 로고
    • Steroid receptors and their associated proteins
    • Smith, D. F. and Toft, D. O., Steroid receptors and their associated proteins., Mol. Endocrinol., 7, 4, 1993.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 4
    • Smith, D.F.1    Toft, D.O.2
  • 138
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt, W. B., The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor, J. Biol. Chem., 268, 21455, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21455
    • Pratt, W.B.1
  • 139
    • 0026631538 scopus 로고
    • Dual roles of the 90-kDa heat shock protein hsp90 in modulating functional activities of the dioxin receptor. Evidence that the dioxin receptor functionally belongs to a subclass of nuclear receptors which require hsp90 both for ligand binding activity and repression of intrinsic DNA binding activity
    • Pongratz, I., Mason, G. G., and Poellinger, L., Dual roles of the 90-kDa heat shock protein hsp90 in modulating functional activities of the dioxin receptor. Evidence that the dioxin receptor functionally belongs to a subclass of nuclear receptors which require hsp90 both for ligand binding activity and repression of intrinsic DNA binding activity, J. Biol. Chem., 267, 13728, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13728
    • Pongratz, I.1    Mason, G.G.2    Poellinger, L.3
  • 141
    • 0028077887 scopus 로고
    • The 90-kda heat shock protein is essential for Ah receptor signaling in a yeast expression system
    • Carver, L. A., Jackiw, V., and Bradfield, C. A., The 90-kda heat shock protein is essential for Ah receptor signaling in a yeast expression system, J. Biol. Chem., 269, 30109, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30109
    • Carver, L.A.1    Jackiw, V.2    Bradfield, C.A.3
  • 142
    • 0027942089 scopus 로고
    • Identification of transactivation and repression functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: Inducible versus constitutive modes of regulation
    • Whitelaw, M. L., Gustafsson, J.-Å., and Poellinger, L., Identification of transactivation and repression functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: inducible versus constitutive modes of regulation. Mol. Cell. Biol., 14, 8343, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8343
    • Whitelaw, M.L.1    Gustafsson, J.-Å.2    Poellinger, L.3
  • 143
    • 0028113007 scopus 로고
    • Transcriptional activation function of the mouse Ah receptor nuclear translocator
    • Li, H., Dong, L. Q., and Whitlock, J. P., Transcriptional activation function of the mouse Ah receptor nuclear translocator, J. Biol. Chem., 269, 28098, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28098
    • Li, H.1    Dong, L.Q.2    Whitlock, J.P.3
  • 144
    • 0028079988 scopus 로고
    • Potent transactivation domains of the Ah receptor and the Ah receptor nuclear translocator map to their carboxyl termini
    • Jain, S., Dolwick, K. M., Schmidt, J. V., and Bradfield, C. A., Potent transactivation domains of the Ah receptor and the Ah receptor nuclear translocator map to their carboxyl termini, J. Biol. Chem., 269, 31518, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31518
    • Jain, S.1    Dolwick, K.M.2    Schmidt, J.V.3    Bradfield, C.A.4
  • 145
    • 0029019489 scopus 로고
    • Transcriptional activation by the mouse Ah receptor - Interplay between multiple stimulatory and inhibitory functions
    • Ma, Q., Dong, L. Q., and Whitlock, J. P., Transcriptional activation by the mouse Ah receptor - interplay between multiple stimulatory and inhibitory functions, J. Biol. Chem., 270, 12697, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12697
    • Ma, Q.1    Dong, L.Q.2    Whitlock, J.P.3
  • 146
    • 0029810168 scopus 로고    scopus 로고
    • Transactivation by the human dioxin receptor and ARNT proteins: Direct interactions with basal transcription factors
    • Rowlands, J. C., McEwan, I. J., and Gustafsson, J.-Å., Transactivation by the human dioxin receptor and ARNT proteins: direct interactions with basal transcription factors. Mol. Pharmacol., 50, 538, 1996.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 538
    • Rowlands, J.C.1    McEwan, I.J.2    Gustafsson, J.-Å.3
  • 147
    • 0028808111 scopus 로고
    • Transcriptional activation domains of the Ah receptor and Ah receptor nuclear translocator
    • Sogawa, K., Iwabuchi, K., Abe, H., and Fujiikuriyama, Y., Transcriptional activation domains of the Ah receptor and Ah receptor nuclear translocator, J. Cancer Res. Clin. Oncol. 121, 612, 1995.
    • (1995) J. Cancer Res. Clin. Oncol. , vol.121 , pp. 612
    • Sogawa, K.1    Iwabuchi, K.2    Abe, H.3    Fujiikuriyama, Y.4
  • 148
    • 0023683667 scopus 로고
    • How eukaryotic transcriptional activators work
    • Ptashne, M., How eukaryotic transcriptional activators work, Nature, 335, 683, 1988.
    • (1988) Nature , vol.335 , pp. 683
    • Ptashne, M.1
  • 149
    • 0028337542 scopus 로고
    • Transcriptional activation: A complex puzzle with few easy pieces
    • Tjian, R. and Maniatis, T., Transcriptional activation: a complex puzzle with few easy pieces, Cell, 77, 5, 1994.
    • (1994) Cell , vol.77 , pp. 5
    • Tjian, R.1    Maniatis, T.2
  • 150
    • 0027619276 scopus 로고
    • Role of chromatin structure in the regulation of transcription by RNA polymerase II
    • Croston, G. E. and Kadonaga, J. T., Role of chromatin structure in the regulation of transcription by RNA polymerase II, Curr. Opin. Cell Biol., 5, 417, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 417
    • Croston, G.E.1    Kadonaga, J.T.2
  • 151
    • 0027413988 scopus 로고
    • Histones, nucleosomes and transcription
    • Svaren, J. and Hörz, W., Histones, nucleosomes and transcription, Curr. Opin. Genet. Dev., 3, 219, 1993.
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 219
    • Svaren, J.1    Hörz, W.2
  • 152
    • 0023394004 scopus 로고
    • In situ protein-DNA interactions at a dioxin-responsive enhancer associated with the cytochrome P1-450 gene
    • Durrin, L. K. and Whitlock, J. P., Jr., In situ protein-DNA interactions at a dioxin-responsive enhancer associated with the cytochrome P1-450 gene, Mol. Cell. Biol., 7, 3008, 1987.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3008
    • Durrin, L.K.1    Whitlock Jr., J.P.2
  • 153
    • 0025201536 scopus 로고
    • Protein-DNA interactions at a dioxin-responsive enhancer: Evidence that the transformed Ah receptor is heteromeric
    • Elferink, C. J., Gasiewicz, T. A., and Whitlock, J. P., Jr., Protein-DNA interactions at a dioxin-responsive enhancer: evidence that the transformed Ah receptor is heteromeric, J. Biol. Chem., 265, 20708, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20708
    • Elferink, C.J.1    Gasiewicz, T.A.2    Whitlock Jr., J.P.3
  • 154
    • 0026457834 scopus 로고
    • Transcription-dependent and transcription-independent nucleosome disruption induced by dioxin
    • Morgan, J. E. and Whitlock, J., Jr., Transcription-dependent and transcription-independent nucleosome disruption induced by dioxin, Proc. Natl. Acad. Sci. U.S.A., 89, 11622, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 11622
    • Morgan, J.E.1    Whitlock Jr., J.2
  • 155
    • 0027255780 scopus 로고
    • Mechanism of dioxin action: Receptor-enhancer interactions in intact cells
    • Wu, L. and Whitlock, J., Jr., Mechanism of dioxin action: receptor-enhancer interactions in intact cells, Nucleic Acids Res., 21, 119, 1993.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 119
    • Wu, L.1    Whitlock Jr., J.2
  • 156
    • 0026653368 scopus 로고
    • Mechanism of dioxin action: Ah receptor-mediated increase in promoter accessibility in vivo
    • Wu, L. and Whitlock, J., Jr., Mechanism of dioxin action: Ah receptor-mediated increase in promoter accessibility in vivo. Proc. Natl. Acad. Sci. U.S.A., 89, 4811, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4811
    • Wu, L.1    Whitlock Jr., J.2
  • 157
    • 0029034448 scopus 로고
    • Dioxin induces localized, graded changes in chromatin structure - Implications for cyplal gene transcription
    • Okino, S. T. and Whitlock, J. P., Dioxin induces localized, graded changes in chromatin structure - implications for cyplal gene transcription, Mol. Cell. Biol., 15, 3714, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3714
    • Okino, S.T.1    Whitlock, J.P.2
  • 158
  • 159
    • 0029042392 scopus 로고
    • Common themes in assembly and function of eukaryotic transcription complexes
    • Zawel, L. and Reinberg, D., Common themes in assembly and function of eukaryotic transcription complexes, Annu. Rev. Biochem., 64, 533, 1995.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 533
    • Zawel, L.1    Reinberg, D.2
  • 160
    • 0028289788 scopus 로고
    • TBP-TAF complexes: Selectivity factors for eukaryotic transcription
    • Goodrich, J. A. and Tjian, R., TBP-TAF complexes: selectivity factors for eukaryotic transcription, Curr. Opin. Cell Biol., 6, 403, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 403
    • Goodrich, J.A.1    Tjian, R.2
  • 161
    • 0026452218 scopus 로고
    • Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae
    • Sayre, M. H., Tschochner, H., and Kornberg, R. D., Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae, J. Biol. Chem., 267, 23376, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23376
    • Sayre, M.H.1    Tschochner, H.2    Kornberg, R.D.3
  • 162
    • 0027529830 scopus 로고
    • Direct interaction of the tau 1 transactivation domain of the human glucocorticoid receptor with the basal transcriptional machinery
    • McEwan, I. J., Wright, A. P., Dahlman-Wright, K., Carlstedt-Duke, J., and Gustafsson, J.-A., Direct interaction of the tau 1 transactivation domain of the human glucocorticoid receptor with the basal transcriptional machinery, Mol. Cell. Biol., 13, 399, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 399
    • McEwan, I.J.1    Wright, A.P.2    Dahlman-Wright, K.3    Carlstedt-Duke, J.4    Gustafsson, J.-A.5
  • 163
    • 0027946057 scopus 로고
    • The glucocorticoid receptor functions at multiple steps during transcription initiation by RNA polymerase II
    • McEwan, I. J., Almlof, T., Wikstrom, A. C., Dahlman-Wright, K., Wright, A. P., and Gustafsson, J.-A., The glucocorticoid receptor functions at multiple steps during transcription initiation by RNA polymerase II, J. Biol. Chem., 269, 25629, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25629
    • McEwan, I.J.1    Almlof, T.2    Wikstrom, A.C.3    Dahlman-Wright, K.4    Wright, A.P.5    Gustafsson, J.-A.6
  • 164
    • 0028242365 scopus 로고
    • Aryl hydrocarbon-induced interactions at multiple DNA elements of diverse sequence - A multicomponent mechanism for activation of cytochrome P4501A1 (CYP1A1) gene transcription
    • Robertson, R. W., Zhang, L., Pasco, D. S., and Fagan, J. B., Aryl hydrocarbon-induced interactions at multiple DNA elements of diverse sequence - a multicomponent mechanism for activation of cytochrome P4501A1 (CYP1A1) gene transcription, Nucleic Acids Res., 22, 1741, 1994.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1741
    • Robertson, R.W.1    Zhang, L.2    Pasco, D.S.3    Fagan, J.B.4
  • 165
    • 0025051172 scopus 로고
    • Functional analysis of the transcriptional promoter for the CYPIA1 gene
    • Jones, K. W. and Whitlock, J. P., Jr., Functional analysis of the transcriptional promoter for the CYPIA1 gene, Mol. Cell. Biol., 10, 5098, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5098
    • Jones, K.W.1    Whitlock Jr., J.P.2
  • 166
    • 0026688421 scopus 로고
    • Dioxin- and Ah receptor-dependent protein binding to xenobiotic responsive elements and G-rich DNA studied by in vivo footprinting
    • Watson, A., J. and Hankinson, O., Dioxin- and Ah receptor-dependent protein binding to xenobiotic responsive elements and G-rich DNA studied by in vivo footprinting, J. Biol. Chem., 266, 6874, 1992.
    • (1992) J. Biol. Chem. , vol.266 , pp. 6874
    • Watson, A.J.1    Hankinson, O.2
  • 167
    • 0025324530 scopus 로고
    • Organization and function of a dioxin-responsive enhancer
    • Fisher, J. M., Wu, L., Denison, M. S., and Whitlock, J. P., Jr., Organization and function of a dioxin-responsive enhancer, J. Biol. Chem., 265, 9676, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9676
    • Fisher, J.M.1    Wu, L.2    Denison, M.S.3    Whitlock Jr., J.P.4
  • 168
    • 0029131399 scopus 로고
    • Partial characterization of the human CYP1A1 negatively acting transcription factor and mutational analysis of its cognate DNA recognition sequence
    • Boucher, P. D., Piechocki, M. P., and Hines, R. N., Partial characterization of the human CYP1A1 negatively acting transcription factor and mutational analysis of its cognate DNA recognition sequence, Mol. Cell. Biol., 15, 5144, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5144
    • Boucher, P.D.1    Piechocki, M.P.2    Hines, R.N.3
  • 169
    • 0027317353 scopus 로고
    • Rat CYP1A1 negative regulatory element: Biological activity and interaction with a protein from liver and hepatoma cells
    • Sterling, K., Weaver, J., Ho, K. L., Xu, L. C., and Bresnick, E., Rat CYP1A1 negative regulatory element: biological activity and interaction with a protein from liver and hepatoma cells, Mol. Pharmacol., 44, 560, 1993.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 560
    • Sterling, K.1    Weaver, J.2    Ho, K.L.3    Xu, L.C.4    Bresnick, E.5
  • 170
    • 0027503107 scopus 로고
    • Nonnresponsiveness of normal human fibroblasts to dioxin correlates with the presence of a constitutive xenobiotic response element-binding factor
    • Gradin, K., Wilhelmsson, A., Poellinger, L., and Berghard, A., Nonnresponsiveness of normal human fibroblasts to dioxin correlates with the presence of a constitutive xenobiotic response element-binding factor, J. Biol. Chem., 268, 4061, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4061
    • Gradin, K.1    Wilhelmsson, A.2    Poellinger, L.3    Berghard, A.4
  • 172
    • 0027943255 scopus 로고
    • Interaction of the regulatory domains of the murine Cyp1a1 gene with two DNA-binding proteins in addition to the Ah receptor and the Ah receptor nuclear translocator (ARNT)
    • Carrier, F., Chang, C. Y., Duh, J. L., Nebert, D. W., and Puga, A., Interaction of the regulatory domains of the murine Cyp1a1 gene with two DNA-binding proteins in addition to the Ah receptor and the Ah receptor nuclear translocator (ARNT), Biochem. Pharmacol., 48, 1767, 1994.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1767
    • Carrier, F.1    Chang, C.Y.2    Duh, J.L.3    Nebert, D.W.4    Puga, A.5
  • 174
    • 0028318179 scopus 로고
    • The human CYP1A2 gene and induction by 3-methylcholanthrene
    • Quattrochi, L. C., Vu, T., and Tukey, R. H., The human CYP1A2 gene and induction by 3-methylcholanthrene, J. Biol. Chem., 269, 6949, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6949
    • Quattrochi, L.C.1    Vu, T.2    Tukey, R.H.3
  • 175
    • 0024362285 scopus 로고
    • The human cytochrome Cyp1A2 gene contains regulatory elements responsive to 3-methyleholanthrene
    • Quattrochi, L. C. and Tukey, R. H., The human cytochrome Cyp1A2 gene contains regulatory elements responsive to 3-methyleholanthrene, Mol. Pharmacol., 36, 66, 1989.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 66
    • Quattrochi, L.C.1    Tukey, R.H.2
  • 176
    • 0030071214 scopus 로고    scopus 로고
    • Increased oxidative DNA damage in livers of 2,3,7,8-tetrachlorodibenzo-p-dioxin treated intact but not ovariectomized rats
    • Tritscher, A. M., Seacat, A. M., Yager, J. D., Groopman, J. D., Miller, B. D., Bell, D., Sutter, T. R., and Lucier, G. W., Increased oxidative DNA damage in livers of 2,3,7,8-tetrachlorodibenzo-p-dioxin treated intact but not ovariectomized rats, Cancer Lett., 98, 219, 1996.
    • (1996) Cancer Lett. , vol.98 , pp. 219
    • Tritscher, A.M.1    Seacat, A.M.2    Yager, J.D.3    Groopman, J.D.4    Miller, B.D.5    Bell, D.6    Sutter, T.R.7    Lucier, G.W.8
  • 177
    • 0028276386 scopus 로고
    • Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2
    • Sutter, T. R., Tang, Y. M., Hayes, C. L., Wo, Y. Y., Jabs, E. W., Li, X., Yin, H., Cody, C. W., and Greenlee, W. F., Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2, J. Biol. Chem., 269, 13092, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13092
    • Sutter, T.R.1    Tang, Y.M.2    Hayes, C.L.3    Wo, Y.Y.4    Jabs, E.W.5    Li, X.6    Yin, H.7    Cody, C.W.8    Greenlee, W.F.9
  • 178
    • 0028339108 scopus 로고
    • Mouse cytochrome P-450EF, representative of a new 1B subfamily of cytochrome P-450s. Cloning, sequence determination, and tissue expression
    • Savas, U., Bhattacharyya, K. K., Christou, M., Alexander, D. L., and Jefcoate, C. R., Mouse cytochrome P-450EF, representative of a new 1B subfamily of cytochrome P-450s. Cloning, sequence determination, and tissue expression, J. Biol. Chem., 269, 14905, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14905
    • Savas, U.1    Bhattacharyya, K.K.2    Christou, M.3    Alexander, D.L.4    Jefcoate, C.R.5
  • 179
    • 0029009343 scopus 로고
    • Identification of a rat adrenal cytochrome P450 active in polycyclic hydrocarbon metabolism as rat CYP1B1. Demonstration of a unique tissue-specific pattern of hormonal and aryl hydrocarbon receptor-linked regulation
    • Bhattacharyya, K. K., Brake, P. B., Eltom, S. E., Otto, S. A., and Jefcoate, C. R., Identification of a rat adrenal cytochrome P450 active in polycyclic hydrocarbon metabolism as rat CYP1B1. Demonstration of a unique tissue-specific pattern of hormonal and aryl hydrocarbon receptor-linked regulation, J. Biol. Chem., 270, 11595, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11595
    • Bhattacharyya, K.K.1    Brake, P.B.2    Eltom, S.E.3    Otto, S.A.4    Jefcoate, C.R.5
  • 180
    • 0029048701 scopus 로고
    • Rat cyp1b1 - An adrenal cytochrome p450 that exhibits sexdependent expression in livers and kidneys of tcdd-treated animals
    • Walker, N. J., Gastel, J. A., Costa, L. T., Clark, G. C., Lucier, G. W., and Sutter, T. R., Rat cyp1b1 - an adrenal cytochrome p450 that exhibits sexdependent expression in livers and kidneys of tcdd-treated animals, Carcinogenesis, 16, 1319, 1995.
    • (1995) Carcinogenesis , vol.16 , pp. 1319
    • Walker, N.J.1    Gastel, J.A.2    Costa, L.T.3    Clark, G.C.4    Lucier, G.W.5    Sutter, T.R.6
  • 181
    • 0025368036 scopus 로고
    • Regulation of glutathione S-transferase Ya subunit gene expression: Identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds
    • Rushmore, T. H., King, R. G., Paulson, K. E., and Pickett, C. B., Regulation of glutathione S-transferase Ya subunit gene expression: identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds, Proc. Natl. Acad. Sci. U.S.A., 87, 3826, 1990.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3826
    • Rushmore, T.H.1    King, R.G.2    Paulson, K.E.3    Pickett, C.B.4
  • 182
    • 0024997241 scopus 로고
    • Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants
    • Rushmore, T. H. and Pickett, C. B., Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants, J. Biol. Chem., 265, 14648, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14648
    • Rushmore, T.H.1    Pickett, C.B.2
  • 183
    • 0025268888 scopus 로고
    • Analysis of the upstream elements of the xenobiotic compound-inducible and positionally regulated glutathione S-transferase Ya gene
    • Paulson, K. E., Darnell, J., Jr., Rushmore, T., and Pickett, C. B., Analysis of the upstream elements of the xenobiotic compound-inducible and positionally regulated glutathione S-transferase Ya gene, Mol. Cell. Biol., 10, 1841, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1841
    • Paulson, K.E.1    Darnell Jr., J.2    Rushmore, T.3    Pickett, C.B.4
  • 184
    • 0027256085 scopus 로고
    • Dioxin receptor and C/EBP regulate the function of the glutatione S-transferase Ya gene xenobiotic response element
    • Pimentai, R. A., Liang, B., Yee, G. K., Wilhelmsson, A., Poellinger, L., and Paulson, K. E., Dioxin receptor and C/EBP regulate the function of the glutatione S-transferase Ya gene xenobiotic response element, Mol. Cell. Biol., 13, 4365, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4365
    • Pimentai, R.A.1    Liang, B.2    Yee, G.K.3    Wilhelmsson, A.4    Poellinger, L.5    Paulson, K.E.6
  • 185
    • 0026571238 scopus 로고
    • Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene
    • Friling, R. S., Bergelson, S., and Daniel, V., Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene, Proc. Natl. Acad. Sci. U.S.A., 89, 668, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 668
    • Friling, R.S.1    Bergelson, S.2    Daniel, V.3
  • 186
    • 0028364075 scopus 로고
    • Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate
    • Nguyen, T., Rushmore, T. H., and Pickett, C. B., Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate, J. Biol. Chem., 269, 13656, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13656
    • Nguyen, T.1    Rushmore, T.H.2    Pickett, C.B.3
  • 187
    • 0029076781 scopus 로고
    • Regulation of the Ah gene battery via Ah receptor-dependent and independent processes in cultured adult rat hepatocytes
    • Xiao, G. H., Pinaire, J. A., Rodrigues, A. D., and Prough, R. A., Regulation of the Ah gene battery via Ah receptor-dependent and independent processes in cultured adult rat hepatocytes, Drug Metab. Dispos., 23, 642, 1995.
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 642
    • Xiao, G.H.1    Pinaire, J.A.2    Rodrigues, A.D.3    Prough, R.A.4
  • 188
    • 0026453420 scopus 로고
    • Regulation of 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible expression of aldehyde dehydrogenase in hepatoma cells
    • Takimoto, K., Lindahl, R., and Pilot, H. C., Regulation of 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible expression of aldehyde dehydrogenase in hepatoma cells, Arch. Biochem. Biophys., 298, 493, 1992.
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 493
    • Takimoto, K.1    Lindahl, R.2    Pilot, H.C.3
  • 189
    • 0024549056 scopus 로고
    • Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: Distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria
    • Hempel, J., Harper, K., and Lindahl, R., Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria, Biochemistry, 28, 1160, 1989.
    • (1989) Biochemistry , vol.28 , pp. 1160
    • Hempel, J.1    Harper, K.2    Lindahl, R.3
  • 190
    • 0027982711 scopus 로고
    • Structure of the 5′ flanking region of class 3 aldehyde dehydrogenase in the rat
    • Takimoto, K., Lindahl, R., Dunn, T. J., and Pilot, H. C., Structure of the 5′ flanking region of class 3 aldehyde dehydrogenase in the rat, Arch. Biochem. Biophys., 312,: 539, 1994.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 539
    • Takimoto, K.1    Lindahl, R.2    Dunn, T.J.3    Pilot, H.C.4
  • 191
    • 0017364249 scopus 로고
    • Genetic differences in induction of cytosol reduced-NAD(P):menadione oxidoreductase and microsomal aryl hydrocarbon hydroxylase in the mouse
    • Kumaki, K., Jensen, N. M., Shire, J. G., and Nebert, D. W., Genetic differences in induction of cytosol reduced-NAD(P):menadione oxidoreductase and microsomal aryl hydrocarbon hydroxylase in the mouse, J. Biol. Chem., 252, 157, 1977.
    • (1977) J. Biol. Chem. , vol.252 , pp. 157
    • Kumaki, K.1    Jensen, N.M.2    Shire, J.G.3    Nebert, D.W.4
  • 192
    • 0021457972 scopus 로고
    • Rat liver DT-diaphorase: Regulation of functional mRNA levels by 3-methylcholanthrene, transstilbene oxide, and phenobarbital
    • Williams, J. B., Wang, R., Lu, A. Y., and Pickett, C. B., Rat liver DT-diaphorase: regulation of functional mRNA levels by 3-methylcholanthrene, transstilbene oxide, and phenobarbital, Arch. Biochem. Biophys., 232, 408, 1984.
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 408
    • Williams, J.B.1    Wang, R.2    Lu, A.Y.3    Pickett, C.B.4
  • 193
    • 0025806510 scopus 로고
    • Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Identification of regulatory elements controlling basal level expression and inducible expression by planar aromatic compounds and phenolic antioxidants
    • Favreau, L. V. and Pickett, C. B., Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Identification of regulatory elements controlling basal level expression and inducible expression by planar aromatic compounds and phenolic antioxidants, J. Biol. Chem., 266, 4556, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4556
    • Favreau, L.V.1    Pickett, C.B.2
  • 194
    • 0027185397 scopus 로고
    • Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Characterization of a DNA-protein interaction at the antioxidant responsive element and induction by 12-O-tetradecanoylphorbol 13-acetate
    • Favreau, L. V. and Pickett, C. B., Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Characterization of a DNA-protein interaction at the antioxidant responsive element and induction by 12-O-tetradecanoylphorbol 13-acetate, J. Biol. Chem., 268, 19875, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19875
    • Favreau, L.V.1    Pickett, C.B.2
  • 195
    • 0025934316 scopus 로고
    • Targets for dioxin: Genes for plasminogen activator inhibitor-2 and interleukin-1 beta
    • Sutter, T. R., Guzman, K., Dold, K. M., and Greenlee, W. F., Targets for dioxin: genes for plasminogen activator inhibitor-2 and interleukin-1 beta, Science, 254, 415, 1991.
    • (1991) Science , vol.254 , pp. 415
    • Sutter, T.R.1    Guzman, K.2    Dold, K.M.3    Greenlee, W.F.4
  • 196
    • 0025775491 scopus 로고
    • Regulatory elements involved in constitutive and phorbol ester-inducible expression of the plasminogen activator inhibitor type 2 gene promoter
    • Cousin, E., Medcalf, R. L., Bergonzelli, G. E. and Kruithof, E. K., Regulatory elements involved in constitutive and phorbol ester-inducible expression of the plasminogen activator inhibitor type 2 gene promoter, Nucleic Acids Res., 19, 3881, 1991.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3881
    • Cousin, E.1    Medcalf, R.L.2    Bergonzelli, G.E.3    Kruithof, E.K.4
  • 198
    • 0026496895 scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin-dependent regulation of transforming growth factors-alpha and -beta 2 expression in a human keratinocyte cell line involves both transcriptional and post-transcriptional control
    • Gaido, K. W., Maness, S. C., Leonard, L. S. and Greenlee, W. F., 2,3,7,8-Tetrachlorodibenzo-p-dioxin-dependent regulation of transforming growth factors-alpha and -beta 2 expression in a human keratinocyte cell line involves both transcriptional and post-transcriptional control, J. Biol. Chem., 267, 24591, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24591
    • Gaido, K.W.1    Maness, S.C.2    Leonard, L.S.3    Greenlee, W.F.4
  • 199
    • 0026648792 scopus 로고
    • Dioxin induces expression of c-fos and c-jun proto-oncogenes and a large increase in transcription factor AP-1, DM4
    • Puga, A., Nebert, D. W., and Carrier, F., Dioxin induces expression of c-fos and c-jun proto-oncogenes and a large increase in transcription factor AP-1, DM4 Cell Biol., 11, 269, 1992.
    • (1992) Cell Biol. , vol.11 , pp. 269
    • Puga, A.1    Nebert, D.W.2    Carrier, F.3
  • 200
    • 0029118684 scopus 로고
    • Modulation of gene expression and endocrine response pathways by 2,3,7,8-tetrachlorodibenzo-p-dioxin and related compounds
    • Safe, S. H., Modulation of gene expression and endocrine response pathways by 2,3,7,8-tetrachlorodibenzo-p-dioxin and related compounds, Pharmacol. Therap., 67, 247, 1995.
    • (1995) Pharmacol. Therap. , vol.67 , pp. 247
    • Safe, S.H.1
  • 201
    • 0027205024 scopus 로고
    • Estradiol increases and anti-estrogens antagonize the growth factor-induced activator protein-1 activity in MCF-7 breast cancer cells without affecting c-fos and c-jun synthesis
    • Philips, A., Chalbos, D., and Rochefort, H., Estradiol increases and anti-estrogens antagonize the growth factor-induced activator protein-1 activity in MCF-7 breast cancer cells without affecting c-fos and c-jun synthesis, J. Biol. Chem., 268, 14103, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14103
    • Philips, A.1    Chalbos, D.2    Rochefort, H.3
  • 202
    • 0028285855 scopus 로고
    • Antiestrogenic effect of 2,3,7,8-tetrachlorodibenzo-p-dioxin on 17 beta-estradiol-induced pS2 expression
    • Zacharewski, T. R., Bondy, K. L., McDonell, P., and Wu, Z. F., Antiestrogenic effect of 2,3,7,8-tetrachlorodibenzo-p-dioxin on 17 beta-estradiol-induced pS2 expression, Cancer Res., 54, 2707, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 2707
    • Zacharewski, T.R.1    Bondy, K.L.2    McDonell, P.3    Wu, Z.F.4
  • 203
    • 0028884592 scopus 로고
    • Molecular mechanism of inhibition of estrogen-induced cathepsin D gene expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in MCF-7 cells
    • Krishnan, V., Porter, W., Santostefano, M., Wang, X. H., and Safe, S., Molecular mechanism of inhibition of estrogen-induced cathepsin D gene expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in MCF-7 cells, Mol. Cell. Biol., 15, 6710, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6710
    • Krishnan, V.1    Porter, W.2    Santostefano, M.3    Wang, X.H.4    Safe, S.5
  • 204
    • 0028287546 scopus 로고
    • Estrogen receptor-Spl complexes mediate estrogen-induced cathepsin D gene expression in MCF-7 human breast cancer cells
    • Krishnan, V., Wang, X., and Safe, S., Estrogen receptor-Spl complexes mediate estrogen-induced cathepsin D gene expression in MCF-7 human breast cancer cells, J. Biol. Chem., 269, 15912, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15912
    • Krishnan, V.1    Wang, X.2    Safe, S.3
  • 205
    • 0024454741 scopus 로고
    • The 5′ flanking region of the pS2 gene contains a complex enhancer region responsive to oestrogens, epidermal growth factor, a tumor promoter (TPA), the c-Ha-ras oncoprotein and the c-jun protein
    • Nunez, A., Berry, M., Imler, J. and Chambon, P., The 5′ flanking region of the pS2 gene contains a complex enhancer region responsive to oestrogens, epidermal growth factor, a tumor promoter (TPA), the c-Ha-ras oncoprotein and the c-jun protein, EMBO J., 8, 823, 1989.
    • (1989) EMBO J. , vol.8 , pp. 823
    • Nunez, A.1    Berry, M.2    Imler, J.3    Chambon, P.4
  • 206
    • 8244261975 scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin inhibition of nuclear AP-1 binding in MCF-7 human breast cancer cells
    • Rowlands, J. C., Wang, X., and Safe, S., 2,3,7,8-Tetrachlorodibenzo-p-dioxin inhibition of nuclear AP-1 binding in MCF-7 human breast cancer cells, Organohalogen Compounds, 10, 201, 1992.
    • (1992) Organohalogen Compounds , vol.10 , pp. 201
    • Rowlands, J.C.1    Wang, X.2    Safe, S.3
  • 207
    • 0025774929 scopus 로고
    • Inhibition of 17β-estradiol-induced and constitutive expression of the cellular protooncogene c-Fos by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in the female rat uterus
    • Astroff, B., Eldridge, B., and Safe, S., Inhibition of 17β-estradiol-induced and constitutive expression of the cellular protooncogene c-Fos by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in the female rat uterus, Toxicol. Lett., 56, 305, 1991.
    • (1991) Toxicol. Lett. , vol.56 , pp. 305
    • Astroff, B.1    Eldridge, B.2    Safe, S.3
  • 208
    • 0025120750 scopus 로고
    • MyoD family: A paradigm for development?
    • Olson, E. N., MyoD family: a paradigm for development?, Genes Dev., 4, 1454, 1990.
    • (1990) Genes Dev. , vol.4 , pp. 1454
    • Olson, E.N.1
  • 210
    • 0025612795 scopus 로고
    • Myogenesis and development control genes
    • Emerson, C. P., Myogenesis and development control genes, Curr. Opin. Cell Biol., 2, 1065, 1990.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 1065
    • Emerson, C.P.1
  • 211
    • 0025572707 scopus 로고
    • Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection
    • Blackwell, T. K. and Weintraub, H., Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection, Science, 250, 1104, 1990.
    • (1990) Science , vol.250 , pp. 1104
    • Blackwell, T.K.1    Weintraub, H.2
  • 212
    • 0025822948 scopus 로고
    • Cyclic amplification and selection of targets (CASTing) for the myogenin consensus binding site
    • Wright, W. E., Binder, M., and Funk, W., Cyclic amplification and selection of targets (CASTing) for the myogenin consensus binding site, Mol. Cell. Biol., 11, 4104, 1991.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4104
    • Wright, W.E.1    Binder, M.2    Funk, W.3
  • 213
    • 0026534215 scopus 로고
    • Predicted structural similarities of the DNA binding domains of c-Myc and endonuclease Eco R1
    • Halazonetis, T. D. and Kandil, A. N., Predicted structural similarities of the DNA binding domains of c-Myc and endonuclease Eco R1, Science, 255, 464, 1992.
    • (1992) Science , vol.255 , pp. 464
    • Halazonetis, T.D.1    Kandil, A.N.2
  • 214
    • 0026546825 scopus 로고
    • Discrimination between related DNA sites by a single amino acid residue of Myc-related basic helix-loop-helix proteins
    • Dang, C. V., Dolde, C., Gillison, M. C., and Kato, G. J., Discrimination between related DNA sites by a single amino acid residue of Myc-related basic helix-loop-helix proteins, Proc. Natl. Acad. Sci. U.S.A., 89, 559, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 559
    • Dang, C.V.1    Dolde, C.2    Gillison, M.C.3    Kato, G.J.4
  • 215
    • 0026670518 scopus 로고
    • Single amino acid substitutions alter helix-loop-helix protein specificity for bases flanking the core CANNTG motif
    • Fisher, F. and Goding, C. R., Single amino acid substitutions alter helix-loop-helix protein specificity for bases flanking the core CANNTG motif, EMBO J, 11, 4103, 1992.
    • (1992) EMBO J , vol.11 , pp. 4103
    • Fisher, F.1    Goding, C.R.2
  • 216
    • 0027910469 scopus 로고
    • Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
    • Ferre-D'Amare, A. R., Prendergast, G. C., Ziff, E. B., and Burley, S. K., Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain, Nature, 363, 38, 1993.
    • (1993) Nature , vol.363 , pp. 38
    • Ferre-D'Amare, A.R.1    Prendergast, G.C.2    Ziff, E.B.3    Burley, S.K.4
  • 218
    • 0025084602 scopus 로고
    • The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer
    • Gregor, P., Sawadogo, M., and Roeder, R. G., The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer, Genes Dev., 4, 1730, 1990.
    • (1990) Genes Dev. , vol.4 , pp. 1730
    • Gregor, P.1    Sawadogo, M.2    Roeder, R.G.3
  • 219
    • 0028998310 scopus 로고
    • Constitutive function of the basic helix-loop-helix/PAS factor Arnt. Regulation of target promoters via the e box motif
    • Antonsson, C., Arulampalam, V., Whitelaw, M. L., Pettersson, S., and Poellinger, L., Constitutive function of the basic helix-loop-helix/PAS factor Arnt. Regulation of target promoters via the E box motif, J. Biol. Chem., 270, 13968, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13968
    • Antonsson, C.1    Arulampalam, V.2    Whitelaw, M.L.3    Pettersson, S.4    Poellinger, L.5
  • 221
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1
    • Semenza, G. L., Roth, P. H., Fang, H. M., and Wang, G. L., Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1, J. Biol. Chem., 269, 23757, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23757
    • Semenza, G.L.1    Roth, P.H.2    Fang, H.M.3    Wang, G.L.4
  • 222
    • 0028937378 scopus 로고
    • Overexpressed max is not oncogenic and attenuates myc-induced lymphoproliferation and lymphomagenesis in transgenic mice
    • Lindeman, G. J., Harris, A. W., Bath, M. L., Eisenman, R. N., and Adams, J. M., Overexpressed max is not oncogenic and attenuates myc-induced lymphoproliferation and lymphomagenesis in transgenic mice, Oncogene, 10, 1013, 1995.
    • (1995) Oncogene , vol.10 , pp. 1013
    • Lindeman, G.J.1    Harris, A.W.2    Bath, M.L.3    Eisenman, R.N.4    Adams, J.M.5
  • 223
    • 0028318949 scopus 로고
    • Suppression of Myc, but not E1a, transformation activity by Max-associated proteins, Mad and Mxil
    • Lahoz, E. G., Xu, L., Schreiber-Agus, N., and DePinho, R. A., Suppression of Myc, but not E1a, transformation activity by Max-associated proteins, Mad and Mxil, Proc. Natl. Acad. Sci. U.S.A., 91, 5503, 1994.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5503
    • Lahoz, E.G.1    Xu, L.2    Schreiber-Agus, N.3    DePinho, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.