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Volumn 141, Issue 1-2, 2002, Pages 63-76

DNA binding and protein interactions of the AHR/ARNT heterodimer that facilitate gene activation

Author keywords

AHR ARNT heterodimer; DNA binding; Gene activation; Protein interactions

Indexed keywords

AMINO ACID; AROMATIC HYDROCARBON RECEPTOR; HELIX LOOP HELIX PROTEIN; HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR; NUCLEOTIDE; RECEPTOR; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0037145010     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00066-2     Document Type: Article
Times cited : (127)

References (84)
  • 2
    • 0026725943 scopus 로고
    • Cloning of the Ah-receptor cDNA reveals a distinctive ligand activated transcription factor
    • Burbach K.M., Poland A., Bradfield C.A. Cloning of the Ah-receptor cDNA reveals a distinctive ligand activated transcription factor. Proc. Natl. Acad. Sci. USA. 89:1992;8185-8189.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8185-8189
    • Burbach, K.M.1    Poland, A.2    Bradfield, C.A.3
  • 3
    • 0028118685 scopus 로고
    • Getting a grip on DNA recognition: Structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains
    • Ellenberger T. Getting a grip on DNA recognition: structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains. Curr. Opin. Struct. Biol. 4:1995;12-21.
    • (1995) Curr. Opin. Struct. Biol. , vol.4 , pp. 12-21
    • Ellenberger, T.1
  • 4
    • 0031041307 scopus 로고    scopus 로고
    • Two murine homologs of the drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein
    • Probst M.R., Fan C.-M., Tessier-Lavigne M., Hankinson O. Two murine homologs of the drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein. J. Biol. Chem. 272:1997;4451-4457.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4451-4457
    • Probst, M.R.1    Fan, C.-M.2    Tessier-Lavigne, M.3    Hankinson, O.4
  • 5
    • 0028865103 scopus 로고
    • DNA binding specificities and pairing rules of the Ah receptor, ARNT, and SIM proteins
    • Swanson H.I., Chan W.K., Bradfield C.A. DNA binding specificities and pairing rules of the Ah receptor, ARNT, and SIM proteins. J. Biol. Chem. 270:1995;26292-26302.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26292-26302
    • Swanson, H.I.1    Chan, W.K.2    Bradfield, C.A.3
  • 7
    • 0030887045 scopus 로고    scopus 로고
    • Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway
    • Hogenesch J.B., Chan W.K., Jackiw V.H., Brown R.C., Gu Y.-Z., Pray-Grant M., Perdew G.H., Bradfield C.A. Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. J. Biol. Chem. 272:1997;8581-8593.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8581-8593
    • Hogenesch, J.B.1    Chan, W.K.2    Jackiw, V.H.3    Brown, R.C.4    Gu, Y.-Z.5    Pray-Grant, M.6    Perdew, G.H.7    Bradfield, C.A.8
  • 8
    • 0034011764 scopus 로고    scopus 로고
    • Cardiovascular basic helix loop helix factor 1, a novel transcriptional repressor expressed preferentially in the developing and adult cardiovascular system
    • Chin M.T., Maemura K., Fukumoto S., Jain M.K., Layne M.D., Watanabe M., Hsieh C.-M., Lee M.-E. Cardiovascular basic helix loop helix factor 1, a novel transcriptional repressor expressed preferentially in the developing and adult cardiovascular system. J. Biol. Chem. 275:2000;6381-6397.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6381-6397
    • Chin, M.T.1    Maemura, K.2    Fukumoto, S.3    Jain, M.K.4    Layne, M.D.5    Watanabe, M.6    Hsieh, C.-M.7    Lee, M.-E.8
  • 9
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian H., McNight S.L., Russell D.W. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev. 11:1997;72-82.
    • (1997) Genes Dev. , vol.11 , pp. 72-82
    • Tian, H.1    McNight, S.L.2    Russell, D.W.3
  • 11
    • 0024210678 scopus 로고
    • The DNA recognition site for the dioxin-Ah receptor complex
    • Denison M.S., Fisher J.M., Whitlock J.P. Jr. The DNA recognition site for the dioxin-Ah receptor complex. J. Biol. Chem. 263:1988;17221-17224.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17221-17224
    • Denison, M.S.1    Fisher, J.M.2    Whitlock J.P., Jr.3
  • 12
    • 0028908504 scopus 로고
    • Orientation of the heterodimeric aryl hydrocarbon (dioxin) receptor complex on its asymmetric DNA recognition sequence
    • Bacsi S.G., Reisz-Porszasz S., Hankinson O. Orientation of the heterodimeric aryl hydrocarbon (dioxin) receptor complex on its asymmetric DNA recognition sequence. Mol. Pharmacol. 47:1995;432-438.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 432-438
    • Bacsi, S.G.1    Reisz-Porszasz, S.2    Hankinson, O.3
  • 15
    • 0031834838 scopus 로고    scopus 로고
    • Role of the PAS domain in regulation of dimerization and DNA binding specificity of the dioxin receptor
    • Pongratz I., Antonsson C., Whitelaw M.L., Poellinger L. Role of the PAS domain in regulation of dimerization and DNA binding specificity of the dioxin receptor. Mol. Cell. Biol. 18:1998;4079-4088.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4079-4088
    • Pongratz, I.1    Antonsson, C.2    Whitelaw, M.L.3    Poellinger, L.4
  • 17
    • 0029789568 scopus 로고    scopus 로고
    • Functional interference between hypoxia and dioxin signal transduction pathways: Competition for recruitment of the Arnt transcription factor
    • Gradin K., McGuire J., Wenger R.H., Kvietikova I., Whitelaw M.L., Toftgard R., Gassmann M., Poellinger L. Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor. Mol. Cell. Biol. 16:1996;5221-5231.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5221-5231
    • Gradin, K.1    McGuire, J.2    Wenger, R.H.3    Kvietikova, I.4    Whitelaw, M.L.5    Toftgard, R.6    Gassmann, M.7    Poellinger, L.8
  • 18
    • 0033597313 scopus 로고    scopus 로고
    • Cross-talk between the aryl hydrocarbon receptor and hypoxia inducible factor signaling pathways
    • Chan W.K., Yao G., Gu Y.-Z., Bradfield C.A. Cross-talk between the aryl hydrocarbon receptor and hypoxia inducible factor signaling pathways. J. Biol. Chem. 274:1999;12115-12123.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12115-12123
    • Chan, W.K.1    Yao, G.2    Gu, Y.-Z.3    Bradfield, C.A.4
  • 19
    • 0032731702 scopus 로고    scopus 로고
    • Analysis of aryl hydrocarbon receptor-mediated signaling during physiological hypoxia reveals lack of competition for the aryl hydrocarbon nuclear translocator transcription factor
    • Pollenz R.S., Davarinos N.A., Shearer T.P. Analysis of aryl hydrocarbon receptor-mediated signaling during physiological hypoxia reveals lack of competition for the aryl hydrocarbon nuclear translocator transcription factor. Mol. Pharmacol. 56:1999;1127-1137.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1127-1137
    • Pollenz, R.S.1    Davarinos, N.A.2    Shearer, T.P.3
  • 20
    • 0035089346 scopus 로고    scopus 로고
    • Function of the c-Myc oncoprotein in chromatin remodeling and transcription
    • Amati B., Frank S.R., Donjerkovic D., Taubert S. Function of the c-Myc oncoprotein in chromatin remodeling and transcription. Biochim. Biophys. Acta. 1471:2001;M135-M145.
    • (2001) Biochim. Biophys. Acta , vol.1471
    • Amati, B.1    Frank, S.R.2    Donjerkovic, D.3    Taubert, S.4
  • 21
    • 0032899367 scopus 로고    scopus 로고
    • Identification of a novel mechanism of regulation of Ah (dioxin) receptor function
    • Mimura J., Ema M., Sogawa K., Fujii-Kuriyama Y. Identification of a novel mechanism of regulation of Ah (dioxin) receptor function. Genes Dev. 13:1999;20-25.
    • (1999) Genes Dev. , vol.13 , pp. 20-25
    • Mimura, J.1    Ema, M.2    Sogawa, K.3    Fujii-Kuriyama, Y.4
  • 22
    • 0039107897 scopus 로고    scopus 로고
    • Repression of dioxin signal transduction in fibroblasts
    • Gradin K., Toftgard R., Poellinger L., Berghard A. Repression of dioxin signal transduction in fibroblasts. J. Biol. Chem. 274:1999;13511-13518.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13511-13518
    • Gradin, K.1    Toftgard, R.2    Poellinger, L.3    Berghard, A.4
  • 24
    • 0026643609 scopus 로고
    • DNA sequence determinants for binding of transformed Ah receptor to a dioxin-responsive enhancer
    • Yao E.F., Denison M.S. DNA sequence determinants for binding of transformed Ah receptor to a dioxin-responsive enhancer. Biochemistry. 31:1992;5060-5067.
    • (1992) Biochemistry , vol.31 , pp. 5060-5067
    • Yao, E.F.1    Denison, M.S.2
  • 26
    • 0033178263 scopus 로고    scopus 로고
    • Specificity of DNA binding of the c-Myc/Max and ARNT/ARNT dimers at the CACGTG recognition site
    • Swanson H.I., Yang J.-H. Specificity of DNA binding of the c-Myc/Max and ARNT/ARNT dimers at the CACGTG recognition site. Nucleic Acids Res. 27:1999;3205-3212.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3205-3212
    • Swanson, H.I.1    Yang, J.-H.2
  • 27
    • 0027169125 scopus 로고
    • In vitro analysis of Ah receptor domain involved in ligand-activated DNA recognition
    • Dolwick K.M., Swanson H.I., Bradfield C.A. In vitro analysis of Ah receptor domain involved in ligand-activated DNA recognition. Proc. Natl. Acad. Sci. USA. 90:1993;8566-8570.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8566-8570
    • Dolwick, K.M.1    Swanson, H.I.2    Bradfield, C.A.3
  • 28
    • 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., Hankinson O. Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT). Mol. Cell. Biol. 14:1994;6075-6086.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6075-6086
    • Reisz-Porszasz, S.1    Probst, M.R.2    Fukunaga, B.N.3    Hankinson, O.4
  • 29
    • 0029932754 scopus 로고    scopus 로고
    • DNA binding by the heterodimeric Ah receptor
    • Dong L., Ma Q., Whitlock J.P. Jr. DNA binding by the heterodimeric Ah receptor. J. Biol. Chem. 271:1996;7942-7948.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7942-7948
    • Dong, L.1    Ma, Q.2    Whitlock J.P., Jr.3
  • 30
    • 0029947626 scopus 로고    scopus 로고
    • Functional characterization of DNA-binding domains of the subunits of heterodimeric aryl hydrocarbon receptor complex imputing novel and canonical basic helix-loop-helix protein-DNA interactions
    • Bacsi S.G., Hankinson O. Functional characterization of DNA-binding domains of the subunits of heterodimeric aryl hydrocarbon receptor complex imputing novel and canonical basic helix-loop-helix protein-DNA interactions. J. Biol. Chem. 271:1996;8843-8850.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8843-8850
    • Bacsi, S.G.1    Hankinson, O.2
  • 31
    • 0029859749 scopus 로고    scopus 로고
    • Mapping the protein/DNA contact sites of the Ah receptor and Ah receptor nuclear translocator
    • Swanson H.I., Yang J.-H. Mapping the protein/DNA contact sites of the Ah receptor and Ah receptor nuclear translocator. J. Biol. Chem. 271:1996;31657-31665.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31657-31665
    • Swanson, H.I.1    Yang, J.-H.2
  • 32
    • 0033673463 scopus 로고    scopus 로고
    • A tetratricopeptide repeat half-site in the aryl hydrocarbon receptor is important for DNA binding and trans-activation potential
    • Levine S.L., Petrulis J.R., Dubil A., Perdew G.H. A tetratricopeptide repeat half-site in the aryl hydrocarbon receptor is important for DNA binding and trans-activation potential. Mol. Pharmacol. 58:2000;1517-1524.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1517-1524
    • Levine, S.L.1    Petrulis, J.R.2    Dubil, A.3    Perdew, G.H.4
  • 33
    • 0031451924 scopus 로고    scopus 로고
    • A mutation in the aryl hydrocarbon receptor (AHR) in a cultured mammalian cell line identifies a novel region of AHR that affects DNA binding
    • Sun W., Zhang J., Hankinson O. A mutation in the aryl hydrocarbon receptor (AHR) in a cultured mammalian cell line identifies a novel region of AHR that affects DNA binding. J. Biol. Chem. 272:1997;31845-31854.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31845-31854
    • Sun, W.1    Zhang, J.2    Hankinson, O.3
  • 34
    • 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.L., 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. USA. 89:1992;599-602.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 599-602
    • Dang, C.V.1    Dolde, C.2    Gillison, M.L.3    Kato, G.J.4
  • 35
    • 0031008399 scopus 로고    scopus 로고
    • A natural classification of the basic helix-loop-helix class of transcription factors
    • Atchley W.R., Fitch W.M. A natural classification of the basic helix-loop-helix class of transcription factors. Proc. Natl. Acad. Sci. USA. 94:1997;5172-5176.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5172-5176
    • Atchley, W.R.1    Fitch, W.M.2
  • 36
    • 0033977832 scopus 로고    scopus 로고
    • Correlations among amino acid sites in bHLH protein domains: An information theoretic analysis
    • Atchley W.R., Wollenberg K.R., Fitch W.M., Terhalle W., Dress A.W. Correlations among amino acid sites in bHLH protein domains: an information theoretic analysis. Mol. Biol. Evol. 17:2000;164-178.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 164-178
    • Atchley, W.R.1    Wollenberg, K.R.2    Fitch, W.M.3    Terhalle, W.4    Dress, A.W.5
  • 37
    • 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., Burley S.K. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature. 363:1993;38-45.
    • (1993) Nature , vol.363 , pp. 38-45
    • Ferre-D'Amare, A.R.1    Prendergast, G.C.2    Ziff, E.B.3    Burley, S.K.4
  • 39
    • 0028329080 scopus 로고
    • Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer
    • Ellenberger T., Fass D., Arnaud M., Harrison S.C. Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer. Genes Dev. 8:1994;970-980.
    • (1994) Genes Dev. , vol.8 , pp. 970-980
    • Ellenberger, T.1    Fass, D.2    Arnaud, M.3    Harrison, S.C.4
  • 41
    • 0035798677 scopus 로고    scopus 로고
    • The basic helix-loop-helix domain of the aryl hydrocarbon receptor nuclear transporter (ARNT) can oligomerize and bind E-box DNA specifically
    • Huffman J.L., Mokashi A., Bachinger H.P., Brennan R.G. The basic helix-loop-helix domain of the aryl hydrocarbon receptor nuclear transporter (ARNT) can oligomerize and bind E-box DNA specifically. J. Biol. Chem. 276:2001;40537-40544.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40537-40544
    • Huffman, J.L.1    Mokashi, A.2    Bachinger, H.P.3    Brennan, R.G.4
  • 42
    • 0033845842 scopus 로고    scopus 로고
    • Regulation of transcription factor function by phosphorylation
    • Whitmarsh A.J., Davis R.J. Regulation of transcription factor function by phosphorylation. Cell. Mol. Life Sci. 57:2000;1172-1183.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1172-1183
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 43
    • 0025352117 scopus 로고
    • Analysis of photoaffinity-labeled aryl hydrocarbon receptor heterogeneity by two-dimensional gel electrophoresis
    • Perdew G.H., Hollenback C.E. Analysis of photoaffinity-labeled aryl hydrocarbon receptor heterogeneity by two-dimensional gel electrophoresis. Biochemistry. 29:1990;6210-6214.
    • (1990) Biochemistry , vol.29 , pp. 6210-6214
    • Perdew, G.H.1    Hollenback, C.E.2
  • 44
    • 0028943250 scopus 로고
    • Ah receptor phosphorylation: Localization of phosphorylation sites to the c-terminal half of the protein
    • Mahon M.J., Gasiewicz T.A. Ah receptor phosphorylation: localization of phosphorylation sites to the c-terminal half of the protein. Arch. Biochem. Biophys. 318:1995;166-174.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 166-174
    • Mahon, M.J.1    Gasiewicz, T.A.2
  • 45
    • 0030811298 scopus 로고    scopus 로고
    • Ah receptor nuclear translocator protein heterogeneity is altered after heterodimerization with the Ah receptor
    • Tsai J.-C., Perdew G.H. Ah receptor nuclear translocator protein heterogeneity is altered after heterodimerization with the Ah receptor. Biochemistry. 36:1997;9066-9072.
    • (1997) Biochemistry , vol.36 , pp. 9066-9072
    • Tsai, J.-C.1    Perdew, G.H.2
  • 46
    • 0026056609 scopus 로고
    • Inhibition of the specific DNA binding activity of the dioxin receptor by phosphatase treatment
    • Pongratz I., Stomstedt P.E., Mason G.G., Poellinger L. Inhibition of the specific DNA binding activity of the dioxin receptor by phosphatase treatment. J. Biol. Chem. 266:1991;16813-16817.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16813-16817
    • Pongratz, I.1    Stomstedt, P.E.2    Mason, G.G.3    Poellinger, L.4
  • 47
    • 0026559509 scopus 로고
    • Dioxin dependent activation of murine Cyp1a-1 gene transcription requires protein kinase C-dependent phosphorylation
    • Carrier F., Owens R.A., Nebert D.W., Puga A. Dioxin dependent activation of murine Cyp1a-1 gene transcription requires protein kinase C-dependent phosphorylation. Mol. Cell. Biol. 12:1992;1856-1863.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1856-1863
    • Carrier, F.1    Owens, R.A.2    Nebert, D.W.3    Puga, A.4
  • 48
    • 0028016159 scopus 로고
    • A tyrosine kinase-dependent pathway regulates ligand-dependent activation of the dioxin receptor in human keratinocytes
    • Gradin K., Whitelaw M.L., Toftgard R., Poellinger L., Berghard A. A tyrosine kinase-dependent pathway regulates ligand-dependent activation of the dioxin receptor in human keratinocytes. J. Biol. Chem. 269:1994;23800-23807.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23800-23807
    • Gradin, K.1    Whitelaw, M.L.2    Toftgard, R.3    Poellinger, L.4    Berghard, A.5
  • 49
    • 0031127715 scopus 로고    scopus 로고
    • Inhibitors of serine/threonine-specific protein phosphatases stimulate transcription by the Ah receptor/Arnt dimer by affecting a step subsequent to XRE binding
    • Li S.-Y., Dougherty J.J. Inhibitors of serine/threonine-specific protein phosphatases stimulate transcription by the Ah receptor/Arnt dimer by affecting a step subsequent to XRE binding. Arch. Biochem. Biophys. 340:1997;73-82.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 73-82
    • Li, S.-Y.1    Dougherty, J.J.2
  • 50
    • 0034664685 scopus 로고    scopus 로고
    • Regulation of DNA binding activity of the ligand-activated aryl hydrocarbon receptor by tyrosine phosphorylation
    • Park S., Henry E.C., Gasiewicz T.A. Regulation of DNA binding activity of the ligand-activated aryl hydrocarbon receptor by tyrosine phosphorylation. Arch. Biochem. Biophys. 381:2000;302-312.
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 302-312
    • Park, S.1    Henry, E.C.2    Gasiewicz, T.A.3
  • 51
    • 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., 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. 13:1993;677-689.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 677-689
    • Berghard, A.1    Gradin, K.2    Pongratz, I.3    Whitelaw, M.4    Poellinger, L.5
  • 52
    • 0011123644 scopus 로고    scopus 로고
    • Structural role of tyrosine 9 in maintaining proper conformation of the Ah receptor DNA binding domain
    • Minsavage G.D., Park S., Henry E.C., Gasiewicz T.A. Structural role of tyrosine 9 in maintaining proper conformation of the Ah receptor DNA binding domain. Toxicologist. 60:2001;1724.
    • (2001) Toxicologist , vol.60 , pp. 1724
    • Minsavage, G.D.1    Park, S.2    Henry, E.C.3    Gasiewicz, T.A.4
  • 53
    • 0035126508 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor (AhR)/AhR nuclear translocator (ARNT) activity is unaltered by phosphorylation of a periodicity/ARNT/single-minded (PAS)-region serine residue
    • Levine S.L., Perdew G.H. Aryl hydrocarbon receptor (AhR)/AhR nuclear translocator (ARNT) activity is unaltered by phosphorylation of a periodicity/ARNT/single-minded (PAS)-region serine residue. Mol. Pharmacol. 59:2001;557-566.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 557-566
    • Levine, S.L.1    Perdew, G.H.2
  • 54
    • 0026669306 scopus 로고
    • Phorbol esters inhibit the dioxin receptor-mediated transcriptional activation of the mouse Cyp1a-1 and Cyp1a-2 genes by 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Okino S.T., Pendurthi U.R., Tukey R.H. Phorbol esters inhibit the dioxin receptor-mediated transcriptional activation of the mouse Cyp1a-1 and Cyp1a-2 genes by 2,3,7,8-tetrachlorodibenzo-p-dioxin. J. Biol. Chem. 267:1992;6991-6998.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6991-6998
    • Okino, S.T.1    Pendurthi, U.R.2    Tukey, R.H.3
  • 55
    • 0029967886 scopus 로고    scopus 로고
    • Protein kinase C modulates regulation of the CYP1A1 gene by the aryl hydrocarbon receptor
    • Chen Y.-H., Tukey R.H. Protein kinase C modulates regulation of the CYP1A1 gene by the aryl hydrocarbon receptor. J. Biol. Chem. 271:1996;26261-26266.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26261-26266
    • Chen, Y.-H.1    Tukey, R.H.2
  • 57
    • 0031958368 scopus 로고    scopus 로고
    • Protein kinase C activity is required for aryl hydrocarbon receptor pathway-mediated signal transduction
    • Long W.P., Pray-Grant M., Tsai J.-C., Perdew G.H. Protein kinase C activity is required for aryl hydrocarbon receptor pathway-mediated signal transduction. Mol. Pharmacol. 53:1998;691-700.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 691-700
    • Long, W.P.1    Pray-Grant, M.2    Tsai, J.-C.3    Perdew, G.H.4
  • 58
    • 0033617298 scopus 로고    scopus 로고
    • Protein kinase C modulates aryl hydrocarbon receptor nuclear translocator protein-mediated transactivation potential in a dimer context
    • Long W.P., Chen X., Perdew G.H. Protein kinase C modulates aryl hydrocarbon receptor nuclear translocator protein-mediated transactivation potential in a dimer context. J. Biol. Chem. 274:1999;12391-12400.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12391-12400
    • Long, W.P.1    Chen, X.2    Perdew, G.H.3
  • 59
    • 0033571467 scopus 로고    scopus 로고
    • Lack of an absolute requirement for the native aryl hydrocarbon receptor (AhR) and AhR nuclear translocator transactivation domains in protein kinase C-mediated modulation of the AhR pathway
    • Long W.P., Perdew G.H. Lack of an absolute requirement for the native aryl hydrocarbon receptor (AhR) and AhR nuclear translocator transactivation domains in protein kinase C-mediated modulation of the AhR pathway. Arch. Biochem. Biophys. 371:1999;246-259.
    • (1999) Arch. Biochem. Biophys. , vol.371 , pp. 246-259
    • Long, W.P.1    Perdew, G.H.2
  • 60
    • 0029042132 scopus 로고
    • The DNA binding of purified Ah receptor heterodimer is regulated by redox conditions
    • Ireland R.C., Li S.-Y., Dougherty J.J. The DNA binding of purified Ah receptor heterodimer is regulated by redox conditions. Arch. Biochem. Biophys. 319:1995;470-480.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 470-480
    • Ireland, R.C.1    Li, S.-Y.2    Dougherty, J.J.3
  • 61
    • 0032189606 scopus 로고    scopus 로고
    • DNA binding activity of the aryl hydrocarbon receptor is sensitive to redox changes in intact cells
    • Xu C., Siu C.-S., Pasco D.S. DNA binding activity of the aryl hydrocarbon receptor is sensitive to redox changes in intact cells. Arch. Biochem. Biophys. 358:1998;149-156.
    • (1998) Arch. Biochem. Biophys. , vol.358 , pp. 149-156
    • Xu, C.1    Siu, C.-S.2    Pasco, D.S.3
  • 62
    • 0033815334 scopus 로고    scopus 로고
    • Nitrosation and oxidation in the regulation of gene expression
    • Marshall H.E., Merchant K., Stamler J.S. Nitrosation and oxidation in the regulation of gene expression. FASEB J. 14:2000;1889-1900.
    • (2000) FASEB J. , vol.14 , pp. 1889-1900
    • Marshall, H.E.1    Merchant, K.2    Stamler, J.S.3
  • 63
    • 0033650023 scopus 로고    scopus 로고
    • Cellular thiols and redox-regulated signal transduction
    • Sen C.K. Cellular thiols and redox-regulated signal transduction. Curr. Topics Cell. Reg. 36:2000;1-30.
    • (2000) Curr. Topics Cell. Reg. , vol.36 , pp. 1-30
    • Sen, C.K.1
  • 64
    • 0032957695 scopus 로고    scopus 로고
    • Ah receptor and NF-kappaB interactions, a potential mechanism for dioxin toxicity
    • Tian Y., Ke S., Denison M.S., Rabson A.B., Gallo M.A. Ah receptor and NF-kappaB interactions, a potential mechanism for dioxin toxicity. J. Biol. Chem. 274:1999;510-515.
    • (1999) J. Biol. Chem. , vol.274 , pp. 510-515
    • Tian, Y.1    Ke, S.2    Denison, M.S.3    Rabson, A.B.4    Gallo, M.A.5
  • 65
    • 0032575589 scopus 로고    scopus 로고
    • A direct interaction between the aryl hydrocarbon receptor and retinoblastoma protein. Linking dioxin signaling to the cell cycle
    • Ge N., Elferink C.J. A direct interaction between the aryl hydrocarbon receptor and retinoblastoma protein. Linking dioxin signaling to the cell cycle. J. Biol. Chem. 273:1998;22708-22713.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22708-22713
    • Ge, N.1    Elferink, C.J.2
  • 66
    • 0033958620 scopus 로고    scopus 로고
    • The aryl hydrocarbon receptor interacts with estrogen receptor alpha and orphan receptors COUP-TFI and ERRalpha1
    • Klinge C.M., Kau K., Swanson H.I. The aryl hydrocarbon receptor interacts with estrogen receptor alpha and orphan receptors COUP-TFI and ERRalpha1. Arch. Biochem. Biophys. 373:2000;163-174.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 163-174
    • Klinge, C.M.1    Kau, K.2    Swanson, H.I.3
  • 67
    • 0031727376 scopus 로고    scopus 로고
    • The aryl hydrocarbon receptor interacts with transcription factor IIB
    • Swanson H.I., Yang J.-H. The aryl hydrocarbon receptor interacts with transcription factor IIB. Mol. Pharmacol. 54:1998;671-677.
    • (1998) Mol. Pharmacol. , vol.54 , pp. 671-677
    • Swanson, H.I.1    Yang, J.-H.2
  • 68
    • 0029810168 scopus 로고    scopus 로고
    • Trans-activation by the human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins: Direct interactions with basal transcription factors
    • Rowlands J.C., McEwan I.J., Gustafsson J.-A. Trans-activation by the human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins: direct interactions with basal transcription factors. Mol. Pharmacol. 50:1996;538-548.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 538-548
    • Rowlands, J.C.1    McEwan, I.J.2    Gustafsson, J.-A.3
  • 69
    • 0033324251 scopus 로고    scopus 로고
    • Nuclear receptor coactivator SRC-1 interacts with the Q-rich subdomain of the AhR and modulates its transactivation potential
    • Kumar M.B., Perdew G.H. Nuclear receptor coactivator SRC-1 interacts with the Q-rich subdomain of the AhR and modulates its transactivation potential. Gene Expr. 8:1999;273-286.
    • (1999) Gene Expr. , vol.8 , pp. 273-286
    • Kumar, M.B.1    Perdew, G.H.2
  • 70
    • 0033529692 scopus 로고    scopus 로고
    • Differential recruitment of coactivator RIP140 by Ah and estrogen receptors. Absence of a role for LXXLL motifs
    • Kumar M.B., Tarpey R.W., Perdew G.H. Differential recruitment of coactivator RIP140 by Ah and estrogen receptors. Absence of a role for LXXLL motifs. J. Biol. Chem. 274:1999;22155-22164.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22155-22164
    • Kumar, M.B.1    Tarpey, R.W.2    Perdew, G.H.3
  • 71
    • 0033566197 scopus 로고    scopus 로고
    • Interactions of nuclear receptor coactivator/corepressor proteins with the aryl hydrocarbon receptor complex
    • Nguyen T.A., Hovik D., Lee J.-E., Safe S. Interactions of nuclear receptor coactivator/corepressor proteins with the aryl hydrocarbon receptor complex. Arch. Biochem. Biophys. 367:1999;250-257.
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 250-257
    • Nguyen, T.A.1    Hovik, D.2    Lee, J.-E.3    Safe, S.4
  • 72
    • 0030667728 scopus 로고    scopus 로고
    • CBP/p300 functions as a possible transcriptional coactivator of Ah receptor nuclear translocator (Arnt)
    • Kobayashi A., Numayama-Tsuruta K., Sogawa K., Fujii-Kuriyama Y. CBP/p300 functions as a possible transcriptional coactivator of Ah receptor nuclear translocator (Arnt). J. Biochem. 122:1997;703-710.
    • (1997) J. Biochem. , vol.122 , pp. 703-710
    • Kobayashi, A.1    Numayama-Tsuruta, K.2    Sogawa, K.3    Fujii-Kuriyama, Y.4
  • 73
    • 0033802958 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor is required for p300-mediated induction of DNA synthesis by adenovirus E1A
    • Tohkin M., Fukuhara M., Elizondo G., Tomita S., Gonzalez F.J. Aryl hydrocarbon receptor is required for p300-mediated induction of DNA synthesis by adenovirus E1A. Mol. Pharmacol. 58:2000;845-851.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 845-851
    • Tohkin, M.1    Fukuhara, M.2    Elizondo, G.3    Tomita, S.4    Gonzalez, F.J.5
  • 74
    • 0011107798 scopus 로고    scopus 로고
    • GRIP1 enhances AHR signaling in Hepa1c1c7 cells
    • Rushing S., Jones C., Denison M. GRIP1 enhances AHR signaling in Hepa1c1c7 cells. Toxicologist. 66:2002;1068.
    • (2002) Toxicologist , vol.66 , pp. 1068
    • Rushing, S.1    Jones, C.2    Denison, M.3
  • 75
    • 0037023766 scopus 로고    scopus 로고
    • Functional involvement of the brahma/SWI2-related gene 1 protein in cytochrome P4501A1 transcription mediated by the aryl hydrocarbon receptor complex
    • Wang S., Hankinson O. Functional involvement of the brahma/SWI2-related gene 1 protein in cytochrome P4501A1 transcription mediated by the aryl hydrocarbon receptor complex. J. Biol. Chem. 277:2002;11821-11827.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11821-11827
    • Wang, S.1    Hankinson, O.2
  • 76
    • 15844389899 scopus 로고    scopus 로고
    • Cooperative interaction between AhR-Arnt and Sp1 for the drug-inducible expression of CYP1A1 gene
    • Kobayashi A., Sogawa K., Fujii-Kuriyama Y. Cooperative interaction between AhR-Arnt and Sp1 for the drug-inducible expression of CYP1A1 gene. J. Biol. Chem. 271:1996;12310-12316.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12310-12316
    • Kobayashi, A.1    Sogawa, K.2    Fujii-Kuriyama, Y.3
  • 77
    • 0033621035 scopus 로고    scopus 로고
    • Regulation of constitutive gene expression through interactions of Sp1 protein with the nuclear aryl hydrocarbon receptor complex
    • Wang F., Wang W., Safe S. Regulation of constitutive gene expression through interactions of Sp1 protein with the nuclear aryl hydrocarbon receptor complex. Biochemistry. 38:1999;11490-11500.
    • (1999) Biochemistry , vol.38 , pp. 11490-11500
    • Wang, F.1    Wang, W.2    Safe, S.3
  • 78
    • 27244462253 scopus 로고    scopus 로고
    • Short heterodimeric partner (SHP) orphan nuclear receptor inhibits the transcriptional activity of aryl hydrocarbon receptor (AHR)/AHR nuclear translocator (ARNT)
    • Klinge C.M., Jernigan S.C., Risinger K.E., Lee J.E., Tyulmenkov V.V., Falkner K.C., Prough R.A. Short heterodimeric partner (SHP) orphan nuclear receptor inhibits the transcriptional activity of aryl hydrocarbon receptor (AHR)/AHR nuclear translocator (ARNT). Arch. Biochem. Biophys. 390:2001;64-70.
    • (2001) Arch. Biochem. Biophys. , vol.390 , pp. 64-70
    • Klinge, C.M.1    Jernigan, S.C.2    Risinger, K.E.3    Lee, J.E.4    Tyulmenkov, V.V.5    Falkner, K.C.6    Prough, R.A.7
  • 80
    • 0035962669 scopus 로고    scopus 로고
    • Nuclear receptors coordinate the activities of chromatin remodeling complexes and coactivators to facilitate initiation of transcription
    • Dilworth F.J., Chambon P. Nuclear receptors coordinate the activities of chromatin remodeling complexes and coactivators to facilitate initiation of transcription. Oncogene. 20:2001;3047-3054.
    • (2001) Oncogene , vol.20 , pp. 3047-3054
    • Dilworth, F.J.1    Chambon, P.2
  • 81
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang Y., Hu X., DiRenzo J., Lazar M.A., Brown M. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell. 103:2000;843-852.
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    DiRenzo, J.3    Lazar, M.A.4    Brown, M.5
  • 83
    • 0035838460 scopus 로고    scopus 로고
    • Eukaryotic transcription: The core of eukaryotic gene activation
    • Johnson K.M., Mitsouras K., Carey M. Eukaryotic transcription: The core of eukaryotic gene activation. Curr. Biol. 11:2001;R510-R513.
    • (2001) Curr. Biol. , vol.11
    • Johnson, K.M.1    Mitsouras, K.2    Carey, M.3
  • 84
    • 0037040543 scopus 로고    scopus 로고
    • Unlocking the gates to gene expression
    • Fry C.J., Peterson C.L. Unlocking the gates to gene expression. Science. 295:2002;1847-1848.
    • (2002) Science , vol.295 , pp. 1847-1848
    • Fry, C.J.1    Peterson, C.L.2


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