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Volumn 59, Issue 5-6, 1996, Pages 413-429

Stability of the ligand-estrogen receptor interaction depends on estrogen response element flanking sequences and cellular factors

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYTAMOXIFEN; ANTIESTROGEN; ESTROGEN RECEPTOR; TAMOXIFEN AZIRIDINE;

EID: 0030479144     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-0760(96)00129-X     Document Type: Article
Times cited : (35)

References (58)
  • 2
    • 0025855110 scopus 로고
    • Synergistic transcriptional activation by CTF/NF-I and the estrogen receptor involved stabilized interactions with a limiting target factor
    • 2. Martinez E., Dusserre Y., Wahli W. and Mermod N.: Synergistic transcriptional activation by CTF/NF-I and the estrogen receptor involved stabilized interactions with a limiting target factor. Molec. Cell. Biol. 11 (1991) 2937-2945.
    • (1991) Molec. Cell. Biol. , vol.11 , pp. 2937-2945
    • Martinez, E.1    Dusserre, Y.2    Wahli, W.3    Mermod, N.4
  • 3
    • 0028580550 scopus 로고
    • Multiple Pit-1-binding sites facilitate estrogen responsiveness of the prolactin gene
    • 3. Nowakowski B. E. and Maurer R. A.: Multiple Pit-1-binding sites facilitate estrogen responsiveness of the prolactin gene. Molec. Endocr. 8 (1994) 1742-1749.
    • (1994) Molec. Endocr. , vol.8 , pp. 1742-1749
    • Nowakowski, B.E.1    Maurer, R.A.2
  • 4
    • 0028233383 scopus 로고
    • Estrogen receptor-associated proteins: Possible mediators of hormone-induced transcription
    • 4. Halachmi S., Marden E., Martin G., MacKay H., Abbondanza C. and Brown M.: Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription. Science 264 (1994) 1455-1458.
    • (1994) Science , vol.264 , pp. 1455-1458
    • Halachmi, S.1    Marden, E.2    Martin, G.3    MacKay, H.4    Abbondanza, C.5    Brown, M.6
  • 5
    • 0029121358 scopus 로고
    • Nuclear factor RIP 140 modulates transcriptional activation by the estrogen receptor
    • 5. Cavailles V., Dauvois S., L'Horst F., Lopez G., Hoare S., Kushner P. J. and Parker M. G.: Nuclear factor RIP 140 modulates transcriptional activation by the estrogen receptor. EMBO J. 14 (1995) 3741-3751.
    • (1995) EMBO J. , vol.14 , pp. 3741-3751
    • Cavailles, V.1    Dauvois, S.2    L'Horst, F.3    Lopez, G.4    Hoare, S.5    Kushner, P.J.6    Parker, M.G.7
  • 6
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • 6. Onate S. A., Tsai S. Y., Tsai M.-J. and O'Malley B. W.: Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270 (1995) 1354-1357.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 8
    • 0029030016 scopus 로고
    • The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18
    • 8. LeDouarin B., Zechel C., Garnier J.-M., Lutz Y., Tora L., Pierrat B., Heery D., Gronemeyer H., Chambon P. and Losson R.: The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. EMBO J. 14 (1995) 2020-2033.
    • (1995) EMBO J. , vol.14 , pp. 2020-2033
    • LeDouarin, B.1    Zechel, C.2    Garnier, J.-M.3    Lutz, Y.4    Tora, L.5    Pierrat, B.6    Heery, D.7    Gronemeyer, H.8    Chambon, P.9    Losson, R.10
  • 9
    • 0024518991 scopus 로고
    • Human progesterone receptor binding to mouse mammary tumor virus deoxyribonuecleic acid: Dependence on hormone and nonreceptor nuclear factors
    • 9. Edwards D. P., Kuhnel B., Estes P. A. and Nordeen S. K.: Human progesterone receptor binding to mouse mammary tumor virus deoxyribonuecleic acid: dependence on hormone and nonreceptor nuclear factors. Molec. Endocr. 3 (1989) 381-391.
    • (1989) Molec. Endocr. , vol.3 , pp. 381-391
    • Edwards, D.P.1    Kuhnel, B.2    Estes, P.A.3    Nordeen, S.K.4
  • 10
    • 0025317798 scopus 로고
    • A nuclear factor that enhances binding of thyroid hormone receptors to thyroid hormone response elements
    • 10. Burnside J., Darling D. A. and Chin W. W.: A nuclear factor that enhances binding of thyroid hormone receptors to thyroid hormone response elements. J. Biol. Chem. 265 (1990) 2500-2504.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2500-2504
    • Burnside, J.1    Darling, D.A.2    Chin, W.W.3
  • 11
    • 0028890361 scopus 로고
    • Interaction of thyroid hormone receptor with a conserved transcriptional mediator
    • 11. Lee J. W., Ryan F., Swaffield J. C., Johnston S. A. and Moore D. D.: Interaction of thyroid hormone receptor with a conserved transcriptional mediator. Nature 374 (1995) 91-94.
    • (1995) Nature , vol.374 , pp. 91-94
    • Lee, J.W.1    Ryan, F.2    Swaffield, J.C.3    Johnston, S.A.4    Moore, D.D.5
  • 12
    • 0024465135 scopus 로고
    • Positive and negative regulation of gene transcription by a retinoic acid-thyroid hormone receptor heterodimer
    • 12. Glass C. K., Lipkin S. M., Devary O. V. and Rosenfeld M. G.: Positive and negative regulation of gene transcription by a retinoic acid-thyroid hormone receptor heterodimer. Cell 59 (1989) 697-708.
    • (1989) Cell , vol.59 , pp. 697-708
    • Glass, C.K.1    Lipkin, S.M.2    Devary, O.V.3    Rosenfeld, M.G.4
  • 13
    • 0025172266 scopus 로고
    • A single-stranded DNA-binding protein promotes the binding of the purified oestrogen receptor to its responsive element
    • 13. Mukherjee R. and Chambon P.: A single-stranded DNA-binding protein promotes the binding of the purified oestrogen receptor to its responsive element. Nucl. Acids Res. 18 (1990) 5713-5716.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 5713-5716
    • Mukherjee, R.1    Chambon, P.2
  • 14
    • 0026378317 scopus 로고
    • Phosphate-sensitive binding of the estrogen receptor to its response elements
    • 14. Koszewski N. J. and Notides A. C.: Phosphate-sensitive binding of the estrogen receptor to its response elements. Molec. Endocr. 5 (1991) 1129-1136.
    • (1991) Molec. Endocr. , vol.5 , pp. 1129-1136
    • Koszewski, N.J.1    Notides, A.C.2
  • 15
    • 0028036401 scopus 로고
    • The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins
    • 15. Landel C. C., Kushner P. J. and Greene G. L.: The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins. Molec. Endocr. 8 (1994) 1407-1419.
    • (1994) Molec. Endocr. , vol.8 , pp. 1407-1419
    • Landel, C.C.1    Kushner, P.J.2    Greene, G.L.3
  • 16
    • 0023448601 scopus 로고
    • Interaction of two nonhistone proteins with the estradiol response element of the avian vitellogenin gene modulates the binding of estradiol-receptor complex
    • 16. Feavers I. M., Jiricny J., Moncharmont B., Saluz H. P. and Jost J.R .: Interaction of two nonhistone proteins with the estradiol response element of the avian vitellogenin gene modulates the binding of estradiol-receptor complex. Proc. Natn. Acad. Sci. U.S.A. 84 (1987) 7453-7457.
    • (1987) Proc. Natn. Acad. Sci. U.S.A. , vol.84 , pp. 7453-7457
    • Feavers, I.M.1    Jiricny, J.2    Moncharmont, B.3    Saluz, H.P.4    Jost, J.R.5
  • 17
    • 0026803415 scopus 로고
    • Multiple forms of affinity-labeled estrogen receptors in rat distinct pituitary cells
    • 17. Geffroy-Roisne S., Duval J. and Thieulant M. L.: Multiple forms of affinity-labeled estrogen receptors in rat distinct pituitary cells. Endocrinology 131 (1992) 1503-1510.
    • (1992) Endocrinology , vol.131 , pp. 1503-1510
    • Geffroy-Roisne, S.1    Duval, J.2    Thieulant, M.L.3
  • 18
    • 0026589273 scopus 로고
    • Cooperative estrogen receptor interaction with consensus or variant estrogen responsive elements in vitro
    • 18. Klinge C. M., Peale F. V. Jr, Hilf R., Bambara R. A. and Zain S.: Cooperative estrogen receptor interaction with consensus or variant estrogen responsive elements in vitro. Cancer Res. 52 (1992) 1073-1081.
    • (1992) Cancer Res. , vol.52 , pp. 1073-1081
    • Klinge, C.M.1    Peale F.V., Jr.2    Hilf, R.3    Bambara, R.A.4    Zain, S.5
  • 19
    • 0027752932 scopus 로고
    • Differential impact of flanking sequences on estradiol-versus 4-hydroxytamoxifen-liganded estrogen receptor binding to estrogen responsive element DNA
    • 19. Anolik J. H., Klinge C. M., Bambara R. A. and Hilf R.: Differential impact of flanking sequences on estradiol-versus 4-hydroxytamoxifen-liganded estrogen receptor binding to estrogen responsive element DNA. J. Steroid Biochem. Molec. Biol. 46 (1993) 713-730.
    • (1993) J. Steroid Biochem. Molec. Biol. , vol.46 , pp. 713-730
    • Anolik, J.H.1    Klinge, C.M.2    Bambara, R.A.3    Hilf, R.4
  • 20
    • 0028908885 scopus 로고
    • Cooperative binding of estrogen receptor to DNA depends on spacing of binding sites, flanking sequence, and ligand
    • 20. Anolik J. H., Klinge C. M., Hilf R. and Bambara R. A.: Cooperative binding of estrogen receptor to DNA depends on spacing of binding sites, flanking sequence, and ligand. Biochemistry 34 (1995) 2511-2520.
    • (1995) Biochemistry , vol.34 , pp. 2511-2520
    • Anolik, J.H.1    Klinge, C.M.2    Hilf, R.3    Bambara, R.A.4
  • 21
    • 0029873531 scopus 로고    scopus 로고
    • Dissociation of 4-hydroxytamoxifen, but not estradiol or tamoxifen aziridine, from the estrogen receptor when the receptor binds estrogen response element DNA
    • 21. Klinge C. M., Traish A. M., Bambara R. A. and Hilf R.: Dissociation of 4-hydroxytamoxifen, but not estradiol or tamoxifen aziridine, from the estrogen receptor when the receptor binds estrogen response element DNA. J. Steroid Biochem. Molec. Biol. 57 (1996) 51-66.
    • (1996) J. Steroid Biochem. Molec. Biol. , vol.57 , pp. 51-66
    • Klinge, C.M.1    Traish, A.M.2    Bambara, R.A.3    Hilf, R.4
  • 22
    • 0029994081 scopus 로고    scopus 로고
    • Site-directed estrogen receptor antibodies stabilize 4-hydroxytamoxifen ligand, but not estradiol, and indicate ligand-specific differences in the recognition of estrogen response element DNA in vitro
    • 22. Klinge C. M., Traish A. M., Driscoll M. D., Hilf R. and Bambara R. A.: Site-directed estrogen receptor antibodies stabilize 4-hydroxytamoxifen ligand, but not estradiol, and indicate ligand-specific differences in the recognition of estrogen response element DNA in vitro. Steroids 61 (1996) 278-289.
    • (1996) Steroids , vol.61 , pp. 278-289
    • Klinge, C.M.1    Traish, A.M.2    Driscoll, M.D.3    Hilf, R.4    Bambara, R.A.5
  • 23
    • 0026968942 scopus 로고
    • What differentiates antiestrogen-liganded versus estradiol-liganded estrogen receptor action?
    • 23. Klinge C. M., Bambara R. A. and Hilf R.: What differentiates antiestrogen-liganded versus estradiol-liganded estrogen receptor action?. Oncol. Res. 4 (1992) 137-144.
    • (1992) Oncol. Res. , vol.4 , pp. 137-144
    • Klinge, C.M.1    Bambara, R.A.2    Hilf, R.3
  • 24
    • 0026726491 scopus 로고
    • Antiestrogen-liganded estrogen receptor interaction with estrogen responsive element DNA in vitro
    • 24. Klinge C. M., Bambara R. A. and Hilf R.: Antiestrogen-liganded estrogen receptor interaction with estrogen responsive element DNA in vitro. J. Steroid Biochem. Molec. Biol. 43 (1992) 249-262.
    • (1992) J. Steroid Biochem. Molec. Biol. , vol.43 , pp. 249-262
    • Klinge, C.M.1    Bambara, R.A.2    Hilf, R.3
  • 25
    • 0030130436 scopus 로고    scopus 로고
    • Footprint analysis of estrogen receptor binding to adjacent estrogen response elements
    • 25. Driscoll M. D., Klinge C. M., Hilf R. and Bambara R. A.: Footprint analysis of estrogen receptor binding to adjacent estrogen response elements. J. Steroid Biochem. Molec. Biol. 58 (1996) 45-61.
    • (1996) J. Steroid Biochem. Molec. Biol. , vol.58 , pp. 45-61
    • Driscoll, M.D.1    Klinge, C.M.2    Hilf, R.3    Bambara, R.A.4
  • 28
    • 0017127061 scopus 로고
    • Hydroxylapatite "batch" assay for estrogen receptor: Increased sensitivity over present receptor assays
    • 28. Pavlik E. J. and Coulson P. B.: Hydroxylapatite "batch" assay for estrogen receptor: increased sensitivity over present receptor assays. J. Steroid Biochem. 7 (1976) 357-368.
    • (1976) J. Steroid Biochem. , vol.7 , pp. 357-368
    • Pavlik, E.J.1    Coulson, P.B.2
  • 29
    • 0024450125 scopus 로고
    • Rapid purification of the estrogen receptor by sequence-specific DNA affinity chromatography
    • 29. Peale F. V. Jr., Ishibe Y., Klinge C. M., Zain S., Hilf R. and Bambara R. A.: Rapid purification of the estrogen receptor by sequence-specific DNA affinity chromatography. Biochemistry 28 (1989) 8671-8675.
    • (1989) Biochemistry , vol.28 , pp. 8671-8675
    • Peale F.V., Jr.1    Ishibe, Y.2    Klinge, C.M.3    Zain, S.4    Hilf, R.5    Bambara, R.A.6
  • 30
    • 0027322696 scopus 로고
    • Hormone-and DNA-binding mechanisms of the recombinant human estrogen receptor
    • 30. Obourn J. D., Koszewski N. J. and Notides A. C.: Hormone-and DNA-binding mechanisms of the recombinant human estrogen receptor. Biochemistry 32 (1993) 6229-6236.
    • (1993) Biochemistry , vol.32 , pp. 6229-6236
    • Obourn, J.D.1    Koszewski, N.J.2    Notides, A.C.3
  • 32
    • 0025077241 scopus 로고
    • A microtiter well assay for quantitative measurement of estrogen receptor binding to estrogen-responsive elements
    • 32. Ludwig L. B., Klinge C. M., Peale F. V. Jr., Bambara R. A., Zain S. and Hilf R.: A microtiter well assay for quantitative measurement of estrogen receptor binding to estrogen-responsive elements. Molec. Endocr. 4 (1990) 1027-1033.
    • (1990) Molec. Endocr. , vol.4 , pp. 1027-1033
    • Ludwig, L.B.1    Klinge, C.M.2    Peale F.V., Jr.3    Bambara, R.A.4    Zain, S.5    Hilf, R.6
  • 33
    • 0029127987 scopus 로고
    • Identification of structurally-altered estrogen receptors in human breast cancer by site-directed monoclonal antibodies
    • 33. Traish A. M., Al-Fadhli S., Klinge C. M., Kounine M. and Quick T. C.: Identification of structurally-altered estrogen receptors in human breast cancer by site-directed monoclonal antibodies. Steroids 60 (1995) 467-474.
    • (1995) Steroids , vol.60 , pp. 467-474
    • Traish, A.M.1    Al-Fadhli, S.2    Klinge, C.M.3    Kounine, M.4    Quick, T.C.5
  • 34
    • 0026500078 scopus 로고
    • DNA allosterically modulates the steroid binding domain of the estrogen receptor
    • 34. Fritsch M., Welch R. D., Murdoch F. E., Anderson I. and Gorski J.: DNA allosterically modulates the steroid binding domain of the estrogen receptor. J. Biol. Chem. 267 (1992) 1823-1828.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1823-1828
    • Fritsch, M.1    Welch, R.D.2    Murdoch, F.E.3    Anderson, I.4    Gorski, J.5
  • 35
    • 0029394774 scopus 로고
    • Major molecular weight heterogeneity of estrogen receptor from breast cancer is not related to neoplasia
    • 35. Maaroufi Y., Trivedi S. and LeClercq G.: Major molecular weight heterogeneity of estrogen receptor from breast cancer is not related to neoplasia. Cancer Biochem. Biophys. 15 (1995) 67-78.
    • (1995) Cancer Biochem. Biophys. , vol.15 , pp. 67-78
    • Maaroufi, Y.1    Trivedi, S.2    LeClercq, G.3
  • 36
    • 0026509582 scopus 로고
    • Increasing the activity of affinity-purified DNA-binding proteins by adding high concentrations of nonspecific proteins
    • 36. Zhang X. Y., Asiedu C. K., Supakar P. C. and Ehrlich M.: Increasing the activity of affinity-purified DNA-binding proteins by adding high concentrations of nonspecific proteins. Analyt. Biochem. 201 (1992) 366-374.
    • (1992) Analyt. Biochem. , vol.201 , pp. 366-374
    • Zhang, X.Y.1    Asiedu, C.K.2    Supakar, P.C.3    Ehrlich, M.4
  • 37
    • 0028021514 scopus 로고
    • Mutational analysis of cysteine residues within the hormone-binding domain of the human estrogen receptor identifies mutants that are defective in both DNA-binding and subcellular distribution
    • 37. Neff S., Sadowski C. and Kiksicek R. J.: Mutational analysis of cysteine residues within the hormone-binding domain of the human estrogen receptor identifies mutants that are defective in both DNA-binding and subcellular distribution. Molec. Endocr. 8 (1994) 1215-1223.
    • (1994) Molec. Endocr. , vol.8 , pp. 1215-1223
    • Neff, S.1    Sadowski, C.2    Kiksicek, R.J.3
  • 39
    • 0027235507 scopus 로고
    • High affinity binding of the estrogen receptor to a DNA response element does not require homodimer formation or estrogen
    • 39. Furlow J. D., Murdoch F. E. and Gorski J.: High affinity binding of the estrogen receptor to a DNA response element does not require homodimer formation or estrogen. J. Biol. Chem. 268 (1993) 12519-12525.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12519-12525
    • Furlow, J.D.1    Murdoch, F.E.2    Gorski, J.3
  • 40
    • 0023878971 scopus 로고
    • Mechanism of the estrogen receptor interaction with 4-hydroxytamoxifen
    • 40. Sasson S. and Notides A. C.: Mechanism of the estrogen receptor interaction with 4-hydroxytamoxifen. Molec. Endocr. 2 (1988) 307-312.
    • (1988) Molec. Endocr. , vol.2 , pp. 307-312
    • Sasson, S.1    Notides, A.C.2
  • 41
    • 0028275296 scopus 로고
    • The side chains responsible for the dimerization of the estradiol receptor by ionic bonds are lost in a 17 kDa fragment extending downstream from aa303
    • 41. Thole H. H.: The side chains responsible for the dimerization of the estradiol receptor by ionic bonds are lost in a 17 kDa fragment extending downstream from aa303. J. Steroid Biochem. Molec. Biol. 48 (1994) 463-466.
    • (1994) J. Steroid Biochem. Molec. Biol. , vol.48 , pp. 463-466
    • Thole, H.H.1
  • 42
    • 0025329841 scopus 로고
    • Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor
    • 42. Fawell S. E., Lees J. A., White R. and Parker M. G.: Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor. Cell 60 (1990) 953-962.
    • (1990) Cell , vol.60 , pp. 953-962
    • Fawell, S.E.1    Lees, J.A.2    White, R.3    Parker, M.G.4
  • 43
    • 0028809317 scopus 로고
    • Specificity of ligand-dependent androgen receptor stabiization: Receptor domain interactions influence ligand dissociation and receptor stability
    • 43. Zhou Z.-X., Lane M. S., Kemppainen J. A., French F. S. and Wilson E. M.: Specificity of ligand-dependent androgen receptor stabiization: receptor domain interactions influence ligand dissociation and receptor stability. Molec. Endocr. 9 (1995) 208-218.
    • (1995) Molec. Endocr. , vol.9 , pp. 208-218
    • Zhou, Z.-X.1    Lane, M.S.2    Kemppainen, J.A.3    French, F.S.4    Wilson, E.M.5
  • 44
    • 0024578739 scopus 로고
    • AT-rich sequences may lower the activation energy of cruciform extrusion in supercoiled DNA
    • 44. Wang Y. and Sauerbier W.: AT-rich sequences may lower the activation energy of cruciform extrusion in supercoiled DNA. Biochem. Biophys. Res. Commun. 158 (1989) 423-431.
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 423-431
    • Wang, Y.1    Sauerbier, W.2
  • 45
    • 0027289302 scopus 로고
    • Analysis of estrogen receptor interaction with tertiary-structured estrogen responsive elements
    • 45. Lannigan D. A., Tamashek J. J., Obourn J. D. and Notides A. C.: Analysis of estrogen receptor interaction with tertiary-structured estrogen responsive elements. Biochem. Pharm. 45 (1993) 1921-1928.
    • (1993) Biochem. Pharm. , vol.45 , pp. 1921-1928
    • Lannigan, D.A.1    Tamashek, J.J.2    Obourn, J.D.3    Notides, A.C.4
  • 46
    • 0027474989 scopus 로고
    • Multiple transitions to non-B-DNA structures occur in the distal regulatory region of the rat prolactin gene
    • 46. Kladde M. P., D'Cunha J. and Gorski J.: Multiple transitions to non-B-DNA structures occur in the distal regulatory region of the rat prolactin gene. J. Molec. Biol. 229 (1993) 344-367.
    • (1993) J. Molec. Biol. , vol.229 , pp. 344-367
    • Kladde, M.P.1    D'Cunha, J.2    Gorski, J.3
  • 47
    • 3042978947 scopus 로고
    • Estrogen receptor selectively binds the "coding strand" of an estrogen responsive element
    • 47. Lannigan D. A. and Notides A. C.: Estrogen receptor selectively binds the "coding strand" of an estrogen responsive element. Proc. Natn. Acad. Sci. U.S.A. 86 (1989) 863-867.
    • (1989) Proc. Natn. Acad. Sci. U.S.A. , vol.86 , pp. 863-867
    • Lannigan, D.A.1    Notides, A.C.2
  • 49
    • 0028068422 scopus 로고
    • Novel estrogen response elements identified by genetic selection in yeast are differentially responsive to estogens and antiestrognes in mammalian cells
    • 49. Dana S. L., Hoener P. A., Wheeler D. A., Lawrence C. B. and McDonnell D. P.: Novel estrogen response elements identified by genetic selection in yeast are differentially responsive to estogens and antiestrognes in mammalian cells. Molec. Endocr. 8 (1994) 1193-1207.
    • (1994) Molec. Endocr. , vol.8 , pp. 1193-1207
    • Dana, S.L.1    Hoener, P.A.2    Wheeler, D.A.3    Lawrence, C.B.4    McDonnell, D.P.5
  • 50
    • 0024066404 scopus 로고
    • A cell-specific activator in the Xenopus A2 vitellogenin gene: Promoter elements functioning with rat liver nuclear extracts
    • 50. Dobbeling U., Rob K., Klein-Hitpass L., Morley C., Wagner U. and Ryffel G. U.: A cell-specific activator in the Xenopus A2 vitellogenin gene: promoter elements functioning with rat liver nuclear extracts. EMBO J. 7 (1988) 2495-2501.
    • (1988) EMBO J. , vol.7 , pp. 2495-2501
    • Dobbeling, U.1    Rob, K.2    Klein-Hitpass, L.3    Morley, C.4    Wagner, U.5    Ryffel, G.U.6
  • 51
    • 0026704585 scopus 로고
    • Binding of the estrogen receptor DNA-binding domain to the estrogen response element induces DNA bending
    • 51. Nardulli A. M. and Shapiro D. J.: Binding of the estrogen receptor DNA-binding domain to the estrogen response element induces DNA bending. Molec. Cell. Biol. 12 (1992) 2037-2042.
    • (1992) Molec. Cell. Biol. , vol.12 , pp. 2037-2042
    • Nardulli, A.M.1    Shapiro, D.J.2
  • 52
    • 0029161482 scopus 로고
    • Estrogen receptor-induced DNA bending: Orientation of the bend and replacement of an estrogen response element with an intrinsic DNA bending sequence
    • 52. Nardulli A. M., Grobner C. and Cotter D.: Estrogen receptor-induced DNA bending: orientation of the bend and replacement of an estrogen response element with an intrinsic DNA bending sequence. Molec. Endocr. 9 (1995) 1064-1076.
    • (1995) Molec. Endocr. , vol.9 , pp. 1064-1076
    • Nardulli, A.M.1    Grobner, C.2    Cotter, D.3
  • 53
    • 0026766290 scopus 로고
    • Protein-induced bending and DNA cyclization
    • 53. Kahn J. D. and Crothers D. M.: Protein-induced bending and DNA cyclization. Proc. Natn. Acad. Sci. U.S.A. 89 (1989) 6343-6347.
    • (1989) Proc. Natn. Acad. Sci. U.S.A. , vol.89 , pp. 6343-6347
    • Kahn, J.D.1    Crothers, D.M.2
  • 55
    • 0028266504 scopus 로고
    • Nuclear accessory factors enhance the binding of progesterone receptor to specific target DNA
    • 55. Prendergast P., Onate S. A., Christensen K. and Edwards D.: Nuclear accessory factors enhance the binding of progesterone receptor to specific target DNA. J. Steroid Biochem. Molec. Biol. 48 (1994) 1-13.
    • (1994) J. Steroid Biochem. Molec. Biol. , vol.48 , pp. 1-13
    • Prendergast, P.1    Onate, S.A.2    Christensen, K.3    Edwards, D.4
  • 56
    • 0029026719 scopus 로고
    • Poly(dA:dT), a ubiquitous promoter element that stimulates transcription via its intrinsic DNA structure
    • 56. Iyer V. and Struhl K.: Poly(dA:dT), a ubiquitous promoter element that stimulates transcription via its intrinsic DNA structure. EMBO J. 14 (1995) 2570-2579.
    • (1995) EMBO J. , vol.14 , pp. 2570-2579
    • Iyer, V.1    Struhl, K.2
  • 57
    • 0024197289 scopus 로고
    • Cell-specific activity of a GGTCA half-palindromic oestrogen-responsive element in the chicken ovalbumin gene promoter
    • 57. Tora L., Gaub M. P., Mader S., Dierich A., Bellard M. and Chambon P.: Cell-specific activity of a GGTCA half-palindromic oestrogen-responsive element in the chicken ovalbumin gene promoter. EMBO J. 7 (1988) 3771-3778.
    • (1988) EMBO J. , vol.7 , pp. 3771-3778
    • Tora, L.1    Gaub, M.P.2    Mader, S.3    Dierich, A.4    Bellard, M.5    Chambon, P.6
  • 58
    • 0027267497 scopus 로고
    • Receptor accessory factor enhances specific DNA binding of androgen and glucocorticoid receptor
    • 58. Kupfer S. R., Marshke K. B., Wilson E. M. and French F. S.: Receptor accessory factor enhances specific DNA binding of androgen and glucocorticoid receptor. J. Biol. Chem. 268 (1993) 17519-17527.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17519-17527
    • Kupfer, S.R.1    Marshke, K.B.2    Wilson, E.M.3    French, F.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.