메뉴 건너뛰기




Volumn 60, Issue 1-2, 1997, Pages 31-41

DNA bending is induced by binding of the glucocorticoid receptor DNA binding domain and progesterone receptors to their response element

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOCORTICOID RECEPTOR; PROGESTERONE RECEPTOR;

EID: 0030995770     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-0760(96)00171-9     Document Type: Article
Times cited : (32)

References (54)
  • 1
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai M.-J. and O'Malley B. W.: Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63 (1994) 451-486.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 451-486
    • Tsai, M.-J.1    O'Malley, B.W.2
  • 2
    • 0022447855 scopus 로고
    • Gene regulation by proteins acting nearby and at a distance
    • Ptashne M.: Gene regulation by proteins acting nearby and at a distance. Nature 322 (1989) 697-701.
    • (1989) Nature , vol.322 , pp. 697-701
    • Ptashne, M.1
  • 3
    • 0021320555 scopus 로고
    • Torsional rigidity of DNA and lenght dependence of the free energy of DNA supercoiling
    • Horowitz D. and Wang J. C.: Torsional rigidity of DNA and lenght dependence of the free energy of DNA supercoiling. J. Molec. Biol. 173 (1984) 75-91.
    • (1984) J. Molec. Biol. , vol.173 , pp. 75-91
    • Horowitz, D.1    Wang, J.C.2
  • 4
    • 0024814234 scopus 로고
    • Bending of DNA by gene-regulatory proteins: Construction and use of a DNA bending vector
    • Kim J., Zwieb C., Wu C. and Adhya S.: Bending of DNA by gene-regulatory proteins: construction and use of a DNA bending vector. Gene 85 (1989) 15-23.
    • (1989) Gene , vol.85 , pp. 15-23
    • Kim, J.1    Zwieb, C.2    Wu, C.3    Adhya, S.4
  • 5
    • 0021268779 scopus 로고
    • The locus of sequence-directed and protein-induced DNA bending
    • Wu H.-M. and Crothers D. M.: The locus of sequence-directed and protein-induced DNA bending. Nature 308 (1984) 509-513.
    • (1984) Nature , vol.308 , pp. 509-513
    • Wu, H.-M.1    Crothers, D.M.2
  • 6
    • 0027349270 scopus 로고
    • Bending of DNA by transcription factors
    • van der Vliet P. C. and Verrijzer C. P.: Bending of DNA by transcription factors. BioEssays 15 (1993) 25-32.
    • (1993) BioEssays , vol.15 , pp. 25-32
    • Van Der Vliet, P.C.1    Verrijzer, C.P.2
  • 7
    • 0026704585 scopus 로고
    • Binding of the estrogen receptor DNA-binding domain to the estrogen response element induces DNA bending
    • 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
  • 8
    • 0027462304 scopus 로고
    • Human estrogen receptor bound to an estrogen response element bends DNA
    • Nardulli A. M., Greene G. L. and Shapiro D. J.: Human estrogen receptor bound to an estrogen response element bends DNA. Molec. Endocr. 7 (1993) 331-340.
    • (1993) Molec. Endocr. , vol.7 , pp. 331-340
    • Nardulli, A.M.1    Greene, G.L.2    Shapiro, D.J.3
  • 9
    • 0026653078 scopus 로고
    • Estrogen receptor-induced bending of the Xenopus vitellogenin A2 gene hormone response element
    • Sabbah M., Le Ricousse S., Redeuilh G. and Baulieu E.-E.: Estrogen receptor-induced bending of the Xenopus vitellogenin A2 gene hormone response element. Biochem. Biophys. Res. Commun. 185 (1992) 944-952.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 944-952
    • Sabbah, M.1    Le Ricousse, S.2    Redeuilh, G.3    Baulieu, E.-E.4
  • 10
    • 0027509352 scopus 로고
    • Thyroid hormone receptor-induced bending of specific DNA sequences is modified by an accessory factor
    • King I. N., Soyza T. d., Catanzaro D. F. and Lavin T. N.: Thyroid hormone receptor-induced bending of specific DNA sequences is modified by an accessory factor. J. Biol. Chem. 286 (1993) 495-501.
    • (1993) J. Biol. Chem. , vol.286 , pp. 495-501
    • King, I.N.1    Soyza, T.D.2    Catanzaro, D.F.3    Lavin, T.N.4
  • 11
    • 0028937343 scopus 로고
    • DNA bending by thyroid hormone receptor: Influence of half-site spacing and RXR
    • Shulemovich K., Dimaculangan D. D., Katz D. and Lazar M. A.: DNA bending by thyroid hormone receptor: influence of half-site spacing and RXR. Nucl. Acids Res. 23 (1995) 811-818.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 811-818
    • Shulemovich, K.1    Dimaculangan, D.D.2    Katz, D.3    Lazar, M.A.4
  • 12
    • 0027371181 scopus 로고
    • DNA bending by retinoid X receptor-containing retinoid and thyroid hormone receptor complexes
    • Lu X. P., Eberhardt N. L. and Pfahl M.: DNA bending by retinoid X receptor-containing retinoid and thyroid hormone receptor complexes. Molec. Cell. Biol. 13 (1993) 6509-6519.
    • (1993) Molec. Cell. Biol. , vol.13 , pp. 6509-6519
    • Lu, X.P.1    Eberhardt, N.L.2    Pfahl, M.3
  • 13
    • 0026502765 scopus 로고
    • Thyroid hormone responsiveness in human growth hormone-related genes: Possible correlation with receptor-induced DNA conformational changes
    • Leidig F., Shepard A. R., Zhang W., Stelter A., Cattini P. A., Baxter J. D. and Eberhardt N. L.: Thyroid hormone responsiveness in human growth hormone-related genes: possible correlation with receptor-induced DNA conformational changes. J. Biol. Chem. 267 (1992) 913-921.
    • (1992) J. Biol. Chem. , vol.267 , pp. 913-921
    • Leidig, F.1    Shepard, A.R.2    Zhang, W.3    Stelter, A.4    Cattini, P.A.5    Baxter, J.D.6    Eberhardt, N.L.7
  • 14
    • 0029560318 scopus 로고
    • Protein sculptors that help turn on genes
    • Wickelgren I.: Protein sculptors that help turn on genes. Science 270 (1995) 1587-1588.
    • (1995) Science , vol.270 , pp. 1587-1588
    • Wickelgren, I.1
  • 15
    • 0027314409 scopus 로고
    • Protein-induced bending as a transcriptional switch
    • Pérez-Martin J. and Espinosa M.: Protein-induced bending as a transcriptional switch. Science 260 (1993) 805-807.
    • (1993) Science , vol.260 , pp. 805-807
    • Pérez-Martin, J.1    Espinosa, M.2
  • 16
    • 0028897104 scopus 로고
    • Intrinsically bent DNA in a eukaryotic transcription factor recognition sequence potentiates transcription activation
    • Kim J., Klooster S. and Shapiro D. J.: Intrinsically bent DNA in a eukaryotic transcription factor recognition sequence potentiates transcription activation. J. Biol. Chem. 270 (1995) 1282-1288.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1282-1288
    • Kim, J.1    Klooster, S.2    Shapiro, D.J.3
  • 17
    • 0029993518 scopus 로고    scopus 로고
    • The human glucocorticoid receptor B isoform
    • Oakley R. H., Sar M. and Cidlowski J. A.: The human glucocorticoid receptor B isoform. J. Biol. Chem. 271 (1996) 9550-9559.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9550-9559
    • Oakley, R.H.1    Sar, M.2    Cidlowski, J.A.3
  • 18
    • 0015499899 scopus 로고
    • Progesterone-binding components of chick oviduct: Characterization of purified subunits
    • Schrader W. T. and O'Malley B. W.: Progesterone-binding components of chick oviduct: characterization of purified subunits. J. Biol. Chem. 247 (1972) 51-59.
    • (1972) J. Biol. Chem. , vol.247 , pp. 51-59
    • Schrader, W.T.1    O'Malley, B.W.2
  • 19
    • 0021070493 scopus 로고
    • In situ photolinked nuclear progesterone receptors of human breast cancer cells: Subunit molecular weights after transformation and translocation
    • Horwitz K. B. and Alexander P. S.: In situ photolinked nuclear progesterone receptors of human breast cancer cells: subunit molecular weights after transformation and translocation. Endocrinology 113 (1983) 2195-2201.
    • (1983) Endocrinology , vol.113 , pp. 2195-2201
    • Horwitz, K.B.1    Alexander, P.S.2
  • 20
    • 0027427216 scopus 로고
    • Human progesterone receptor A form is a cell- and promoter-specific repressor of human progesterone receptor B function
    • Vegeto E., Shahbaz M. M., Wen D. X., Goldman M. E., O'Malley B. W. and McDonnell D. P.: Human progesterone receptor A form is a cell- and promoter-specific repressor of human progesterone receptor B function. Molec. Endocr. 7 (1993) 1244-1255.
    • (1993) Molec. Endocr. , vol.7 , pp. 1244-1255
    • Vegeto, E.1    Shahbaz, M.M.2    Wen, D.X.3    Goldman, M.E.4    O'Malley, B.W.5    McDonnell, D.P.6
  • 21
    • 0027494065 scopus 로고
    • Antagonist-occupied human progesterone B-receptors activate transcription without binding to progesterone response elements and are dominantly inhibited by A-receptors
    • Tung L., Mohamed M. K., Hoeffler J. P., Takimoto G. S. and Horwitz K. B.: Antagonist-occupied human progesterone B-receptors activate transcription without binding to progesterone response elements and are dominantly inhibited by A-receptors. Molec. Endocr. 7 (1993) 1256-1265.
    • (1993) Molec. Endocr. , vol.7 , pp. 1256-1265
    • Tung, L.1    Mohamed, M.K.2    Hoeffler, J.P.3    Takimoto, G.S.4    Horwitz, K.B.5
  • 22
    • 0028601260 scopus 로고
    • The leucine zippers of c-fos and c-jun for progesterone receptor dimerization: A-dominance in the A/B heterodimer
    • Mohamed M. K., Tung L., Takimoto G. S. and Horwitz K. B.: The leucine zippers of c-fos and c-jun for progesterone receptor dimerization: A-dominance in the A/B heterodimer. J. Steroid Biochem. Molec. Biol. 51 (1994) 241-250.
    • (1994) J. Steroid Biochem. Molec. Biol. , vol.51 , pp. 241-250
    • Mohamed, M.K.1    Tung, L.2    Takimoto, G.S.3    Horwitz, K.B.4
  • 23
    • 0024365823 scopus 로고
    • The chicken progesterone receptor A and B isoforms are products of an alternate translation initiation event
    • Conneely O. M., Kettelberger D. M., Tsai J. J., Schrader W. T. and O'Malley B. W.: The chicken progesterone receptor A and B isoforms are products of an alternate translation initiation event. J. Biol. Chem. 264 (1989) 14062-14064.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14062-14064
    • Conneely, O.M.1    Kettelberger, D.M.2    Tsai, J.J.3    Schrader, W.T.4    O'Malley, B.W.5
  • 24
    • 0025239785 scopus 로고
    • Two distinct estrogen-regulated promoters generate transcripts encoding two functionally different human progesterone receptor forms A and B
    • Kastner P., Kurst A., Turcotte B., Stropp U., Tora L., Gronemeyer H. and Chambon P.: Two distinct estrogen-regulated promoters generate transcripts encoding two functionally different human progesterone receptor forms A and B. EMBO J. 9 (1990) 1603-1614.
    • (1990) EMBO J. , vol.9 , pp. 1603-1614
    • Kastner, P.1    Kurst, A.2    Turcotte, B.3    Stropp, U.4    Tora, L.5    Gronemeyer, H.6    Chambon, P.7
  • 25
    • 0028073682 scopus 로고
    • A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B isoform
    • Sartorius C. A., Melville M. Y., Hovland A. R., Tung L., Takimoto G. S. and Horwitz K. B.: A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B isoform. Molec. Endocr. 8 (1994) 1347-1360.
    • (1994) Molec. Endocr. , vol.8 , pp. 1347-1360
    • Sartorius, C.A.1    Melville, M.Y.2    Hovland, A.R.3    Tung, L.4    Takimoto, G.S.5    Horwitz, K.B.6
  • 27
    • 0025780755 scopus 로고
    • Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    • Luisi V. F., Xu W. X., Otwinowski Z., Freedman L. P., Yamamoto K. R. and Sigler P. B.: Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature 352 (1991) 497-505.
    • (1991) Nature , vol.352 , pp. 497-505
    • Luisi, V.F.1    Xu, W.X.2    Otwinowski, Z.3    Freedman, L.P.4    Yamamoto, K.R.5    Sigler, P.B.6
  • 28
    • 0028026693 scopus 로고
    • New T47D breast cell lines for the independent study of progesterone B- and A-receptors: Only antiprogestin-occupied B-receptors are switched to transcriptional agonist by cAMP
    • Sartorius C. A., Groshong S. D., Miller L. A., Powell R. L., Tung L., Takimoto G. S. and Horwitz K. B.: New T47D breast cell lines for the independent study of progesterone B- and A-receptors: only antiprogestin-occupied B-receptors are switched to transcriptional agonist by cAMP. Cancer Res. 54 (1994) 3868-3877.
    • (1994) Cancer Res. , vol.54 , pp. 3868-3877
    • Sartorius, C.A.1    Groshong, S.D.2    Miller, L.A.3    Powell, R.L.4    Tung, L.5    Takimoto, G.S.6    Horwitz, K.B.7
  • 30
    • 0026588023 scopus 로고
    • DNA binding analysis of glucocorticoid receptor specificity mutants
    • Alroy I. and Freedman L. P.: DNA binding analysis of glucocorticoid receptor specificity mutants. Nucl. Acids Res. 20 (1992) 1045-1052.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 1045-1052
    • Alroy, I.1    Freedman, L.P.2
  • 31
    • 0026354989 scopus 로고
    • Purified estrogen receptor DNA binding domain expressed in Escherichia coli activates transcription of an estrogen-responsive promoter in cultured cells
    • Nardulli A. M., Lew D., Erijman L. and Shapiro D. J.: Purified estrogen receptor DNA binding domain expressed in Escherichia coli activates transcription of an estrogen-responsive promoter in cultured cells. J. Biol. Chem. 266 (1991) 24070-24076.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24070-24076
    • Nardulli, A.M.1    Lew, D.2    Erijman, L.3    Shapiro, D.J.4
  • 32
    • 0000435320 scopus 로고
    • Mobility shift DNA-binding assay using gel electrophoresis
    • (Edited by Ausubel F. M., Brent R., Kingston R. E., Moore D. D., Seidman J. G., Smith J. A. and Struhl K.). Greene Publishing Associates and Wiley Interscience, New York
    • Chodosh L. A.: Mobility shift DNA-binding assay using gel electrophoresis. In Current Protocols in Molecular Biology (Edited by Ausubel F. M., Brent R., Kingston R. E., Moore D. D., Seidman J. G., Smith J. A. and Struhl K.). Greene Publishing Associates and Wiley Interscience, New York (1989) pp. 12.2.1-12.2.10.
    • (1989) Current Protocols in Molecular Biology , pp. 1221-12210
    • Chodosh, L.A.1
  • 33
    • 0023771741 scopus 로고
    • Empirical estimation of protein-induced DNA bending angles: Applications to λ site-specific recombination complexes
    • Thompson J. F. and Landy A.: Empirical estimation of protein-induced DNA bending angles: applications to λ site-specific recombination complexes. Nucl. Acids Res. 16 (1988) 9687-9705.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 9687-9705
    • Thompson, J.F.1    Landy, A.2
  • 36
    • 0025228644 scopus 로고
    • Determination of the extent of DNA binding by an adenine-thymine tract
    • Koo H.-S., Drak J., Rice J. A. and Crothers D. M.: Determination of the extent of DNA binding by an adenine-thymine tract. Biochem. J. 29 (1990) 4227-4234.
    • (1990) Biochem. J. , vol.29 , pp. 4227-4234
    • Koo, H.-S.1    Drak, J.2    Rice, J.A.3    Crothers, D.M.4
  • 37
    • 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
    • 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
  • 38
    • 0029934522 scopus 로고    scopus 로고
    • Estrogen receptor affinity and location of consensus and imperfect estrogen response elements influence transcription activation of simplified promoters
    • Nardulli A. M., Romine L. E., Carpo C., Greene G. L. and Rainish B.: Estrogen receptor affinity and location of consensus and imperfect estrogen response elements influence transcription activation of simplified promoters. Molec. Endocr. 10 (1996) 694-704.
    • (1996) Molec. Endocr. , vol.10 , pp. 694-704
    • Nardulli, A.M.1    Romine, L.E.2    Carpo, C.3    Greene, G.L.4    Rainish, B.5
  • 39
    • 0024300174 scopus 로고
    • DNA sequence determinants of CAP-induced bending and protein binding affinity
    • Gartenberg M. R. and Crothers D. M.: DNA sequence determinants of CAP-induced bending and protein binding affinity. Nature 333 (1988) 824-831.
    • (1988) Nature , vol.333 , pp. 824-831
    • Gartenberg, M.R.1    Crothers, D.M.2
  • 40
    • 0030025260 scopus 로고    scopus 로고
    • Molecular dynamics study of glucocorticoid receptor-DNA binding
    • Bishop T. C. and Schulten K.: Molecular dynamics study of glucocorticoid receptor-DNA binding. PROTEINS: Struct. Funct. Genet. 24 (1996) 115-133.
    • (1996) PROTEINS: Struct. Funct. Genet. , vol.24 , pp. 115-133
    • Bishop, T.C.1    Schulten, K.2
  • 41
    • 0029757625 scopus 로고
    • Effects of wild type and mutant estrogen receptors on DNA flexibility, DNA bending, and transcription activation
    • Potthoff S. J., Romine L. R. and Nardulli A. M.: Effects of wild type and mutant estrogen receptors on DNA flexibility, DNA bending, and transcription activation. Molec. Endocr. 10 (1966) 1095-1106.
    • (1966) Molec. Endocr. , vol.10 , pp. 1095-1106
    • Potthoff, S.J.1    Romine, L.R.2    Nardulli, A.M.3
  • 42
    • 0029879137 scopus 로고    scopus 로고
    • Progesterone receptor-induced bending of its target DNA: Distinct effects of the A and B receptor forms
    • Prendergast P., Pan Z. and Edwards D. P.: Progesterone receptor-induced bending of its target DNA: distinct effects of the A and B receptor forms. Molec. Endocr. 10 (1996) 393-407.
    • (1996) Molec. Endocr. , vol.10 , pp. 393-407
    • Prendergast, P.1    Pan, Z.2    Edwards, D.P.3
  • 43
    • 0024340266 scopus 로고
    • The interaction of E. Coli IHF protein with its specific binding sites
    • Yang C. C. and Nash H. A.: The interaction of E. coli IHF protein with its specific binding sites. Cell 57 (1989) 869-880.
    • (1989) Cell , vol.57 , pp. 869-880
    • Yang, C.C.1    Nash, H.A.2
  • 44
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90°
    • Schultz S. C., Shields G. C. and Steitz T. A.: Crystal structure of a CAP-DNA complex: the DNA is bent by 90°. Science 253 (1991) 1001-1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 46
    • 0025902328 scopus 로고
    • Fos-Jun heterodimers and Jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity
    • Kerppola T. K. and Curran T.: Fos-Jun heterodimers and Jun homodimers bend DNA in opposite orientations: implications for transcription factor cooperativity. Cell 66 (1991) 317-326.
    • (1991) Cell , vol.66 , pp. 317-326
    • Kerppola, T.K.1    Curran, T.2
  • 48
    • 0026643104 scopus 로고
    • The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structures
    • Giese K., Cox J. and Grosschedl R.: The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structures. Cell 69 (1992) 185-195.
    • (1992) Cell , vol.69 , pp. 185-195
    • Giese, K.1    Cox, J.2    Grosschedl, R.3
  • 49
    • 0029131298 scopus 로고
    • Structural basis for DNA bending by the architectural transcription factor LEF-1
    • Love J. J., Li X., Case D. A., Giese K., Grosschedl R. and Wright P. E.: Structural basis for DNA bending by the architectural transcription factor LEF-1. Nature 376 (1995) 791-795.
    • (1995) Nature , vol.376 , pp. 791-795
    • Love, J.J.1    Li, X.2    Case, D.A.3    Giese, K.4    Grosschedl, R.5    Wright, P.E.6
  • 50
    • 0028919503 scopus 로고
    • Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor
    • Parvin J. D., McCormick R. J., Sharp P. A. and Fisher D. E.: Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor. Nature 373 (1995) 724-727.
    • (1995) Nature , vol.373 , pp. 724-727
    • Parvin, J.D.1    McCormick, R.J.2    Sharp, P.A.3    Fisher, D.E.4
  • 51
    • 0029149889 scopus 로고
    • Bending DNA can repress a eukaryotic basal promoter and inhibit TFIID binding
    • Ten A. H. and Biggin M. D.: Bending DNA can repress a eukaryotic basal promoter and inhibit TFIID binding. Molec. Cell. Biol. 15 (1995) 5492-5498.
    • (1995) Molec. Cell. Biol. , vol.15 , pp. 5492-5498
    • Ten, A.H.1    Biggin, M.D.2
  • 52
    • 0028359441 scopus 로고
    • Retinoblastoma protein reverses DNA bending by transcription factor E2F
    • Huber H. E., Goodhart P. J. and Huang P. S.: Retinoblastoma protein reverses DNA bending by transcription factor E2F. J. Biol. Chem. 269 (1994) 6999-7005.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6999-7005
    • Huber, H.E.1    Goodhart, P.J.2    Huang, P.S.3
  • 53
    • 0029584901 scopus 로고
    • Analysis of mechanisms that determine dominant negative estrogen receptor effectiveness
    • Schodin D. J., Zhuang Y., Shapiro D. J. and Katzenellenbogen B. S.: Analysis of mechanisms that determine dominant negative estrogen receptor effectiveness. J. Biol. Chem. 270 (1995) 31163-31171.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31163-31171
    • Schodin, D.J.1    Zhuang, Y.2    Shapiro, D.J.3    Katzenellenbogen, B.S.4
  • 54
    • 0023808861 scopus 로고
    • The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer
    • Kumar V. and Chambon P.: The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell 55 (1988) 145-156.
    • (1988) Cell , vol.55 , pp. 145-156
    • Kumar, V.1    Chambon, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.