메뉴 건너뛰기




Volumn 12, Issue 12, 1998, Pages 1914-1930

Agonist and antagonists induce homodimerization and mixed ligand heterodimerization of human progesterone receptors in vivo by a mammalian two-hybrid assay

Author keywords

[No Author keywords available]

Indexed keywords

11BETA (4 ACETYLPHENYL) 17BETA HYDROXY 17ALPHA (1 PROPYNYL)ESTRA 4,9 DIEN 3 ONE; MIFEPRISTONE; ONAPRISTONE; PROGESTERONE RECEPTOR;

EID: 0031725634     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/mend.12.12.0210     Document Type: Article
Times cited : (36)

References (65)
  • 1
    • 0025239785 scopus 로고
    • Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B
    • Kastner P, Krust A, Turcotte B, Stropp U, Tora L, Gronemeyer H, Chambon P 1990 Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B. EMBO J 9:1603-1614
    • (1990) EMBO J , vol.9 , pp. 1603-1614
    • Kastner, P.1    Krust, A.2    Turcotte, B.3    Stropp, U.4    Tora, L.5    Gronemeyer, H.6    Chambon, P.7
  • 2
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interaction with heat shock proteins and immunophilin chaperones
    • Pratt WB, Toft DO 1997 Steroid receptor interaction with heat shock proteins and immunophilin chaperones. Endocr Rev 18:306-360
    • (1997) Endocr Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 3
    • 0027249002 scopus 로고
    • Steroid hormone receptors and interaction with DNA and transcription factors
    • Truss M, Beato M 1993 Steroid hormone receptors and interaction with DNA and transcription factors. Endocr Rev 14:459-479
    • (1993) Endocr Rev , vol.14 , pp. 459-479
    • Truss, M.1    Beato, M.2
  • 4
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptors superfamily members
    • Tsai M-J, O'Malley BW 1994 Molecular mechanisms of action of steroid/thyroid receptors superfamily members. Annu Rev Biochem 63:451-86
    • (1994) Annu Rev Biochem , vol.63 , pp. 451-486
    • Tsai, M.-J.1    O'Malley, B.W.2
  • 5
    • 0029954339 scopus 로고    scopus 로고
    • TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel JJ, Heine MJS, Zechel C, Chambon P, Gronemeyer H 1996 TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J 15:3667-3675
    • (1996) EMBO J , vol.15 , pp. 3667-3675
    • Voegel, J.J.1    Heine, M.J.S.2    Zechel, C.3    Chambon, P.4    Gronemeyer, H.5
  • 6
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate SA, Tsai SY, Tsai M-J, O'Malley BW 1995 Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354-1357
    • (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
    • 0025329841 scopus 로고
    • Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor
    • Fawell SE, Lees JA, White R, Parker MG 1990 Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor. Cell 60:953-962
    • (1990) Cell , vol.60 , pp. 953-962
    • Fawell, S.E.1    Lees, J.A.2    White, R.3    Parker, M.G.4
  • 9
    • 0024372113 scopus 로고
    • Mechanisms of nuclear localization of the progesterone receptor: Evidence for interaction between monomers
    • Guiochon-Mantel A, Loosfelt H, Lescop P, Sar S, Atger M, Perrot-Applanat M, Milgorm E 1989 Mechanisms of nuclear localization of the progesterone receptor: evidence for interaction between monomers. Cell 57:1147-1154
    • (1989) Cell , vol.57 , pp. 1147-1154
    • Guiochon-Mantel, A.1    Loosfelt, H.2    Lescop, P.3    Sar, S.4    Atger, M.5    Perrot-Applanat, M.6    Milgorm, E.7
  • 10
    • 0024518991 scopus 로고
    • Human progesterone receptor binding to mouse mammary tumor virus deoxyribonucleic acid: Dependence on hormone and nonreceptor nuclear factor(s)
    • Edwards DP, Kuhnel B, Estes PA, Nordeen SK 1989 Human progesterone receptor binding to mouse mammary tumor virus deoxyribonucleic acid: dependence on hormone and nonreceptor nuclear factor(s). Mol Endocrinol 3:381-391
    • (1989) Mol Endocrinol , vol.3 , pp. 381-391
    • Edwards, D.P.1    Kuhnel, B.2    Estes, P.A.3    Nordeen, S.K.4
  • 11
    • 0024434594 scopus 로고
    • Human progesterone receptor complexed with the antagonist RU486 binds to hormone response elements in a structurally altered form
    • El-Ashry D, Oñate SO, Nordeen SK, Edwards DP 1989 Human progesterone receptor complexed with the antagonist RU486 binds to hormone response elements in a structurally altered form. Mol Endocrinol 3:1545-1558
    • (1989) Mol Endocrinol , vol.3 , pp. 1545-1558
    • El-Ashry, D.1    Oñate, S.O.2    Nordeen, S.K.3    Edwards, D.P.4
  • 12
    • 0025053671 scopus 로고
    • Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor
    • Meyer M-E, Pornon A, Ji J, Bocquel M-T, Chambon P, Gronemeyer H 1990 Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor. EMBO J 9:3923-3932
    • (1990) EMBO J , vol.9 , pp. 3923-3932
    • Meyer, M.-E.1    Pornon, A.2    Ji, J.3    Bocquel, M.-T.4    Chambon, P.5    Gronemeyer, H.6
  • 13
    • 0026096890 scopus 로고
    • Two types of antiprogestins identified by their differential action in transcriptionally active extracts from T47D cells
    • Klein-Hitpass L, Cato ACB, Henderson D, Ryffel G 1991 Two types of antiprogestins identified by their differential action in transcriptionally active extracts from T47D cells. Nucleic Acids Res 19:1227-1234
    • (1991) Nucleic Acids Res , vol.19 , pp. 1227-1234
    • Klein-Hitpass, L.1    Cato, A.C.B.2    Henderson, D.3    Ryffel, G.4
  • 14
    • 0029586681 scopus 로고
    • Steroid receptor heterodimerization demonstrated in vitro and in vivo
    • Liu W, Wang J, Sauter NK, Pearce D 1995 Steroid receptor heterodimerization demonstrated in vitro and in vivo. Proc Natl Acad Sci USA 92:12480-12484
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12480-12484
    • Liu, W.1    Wang, J.2    Sauter, N.K.3    Pearce, D.4
  • 15
    • 0028588118 scopus 로고
    • Heterodimerization between mineralocorticoid and glucocorticoid receptor: A new principle of glucocorticoid action in the CNS
    • Trapp T, Rupprecht R, Castren M, Reul JM, Holsboer F 1994 Heterodimerization between mineralocorticoid and glucocorticoid receptor: a new principle of glucocorticoid action in the CNS. Neuron 13:1457-1462
    • (1994) Neuron , vol.13 , pp. 1457-1462
    • Trapp, T.1    Rupprecht, R.2    Castren, M.3    Reul, J.M.4    Holsboer, F.5
  • 16
    • 15644372928 scopus 로고    scopus 로고
    • Mouse estrogen receptor in vivo evidence against the existence of antiprogestins disrupting receptor binding to DNA
    • Pettersson, K, K Grandien, GGJ M Kuiper, J-A Gustafsson 1997 Mouse estrogen receptor In vivo evidence against the existence of antiprogestins disrupting receptor binding to DNA. Proc Natl Acad Sci USA 90:4421-4425
    • (1997) Proc Natl Acad Sci USA , vol.90 , pp. 4421-4425
    • Pettersson, K.1    Grandien, K.2    Kuiper, G.G.J.M.3    Gustafsson, J.-A.4
  • 17
    • 0029584593 scopus 로고
    • Nonsteroid nuclear receptors: What are genetic studies telling us about their role in real life?
    • Kastner P, Mark M, Chambon P 1995 Nonsteroid nuclear receptors: what are genetic studies telling us about their role in real life? Cell 83:859-869
    • (1995) Cell , vol.83 , pp. 859-869
    • Kastner, P.1    Mark, M.2    Chambon, P.3
  • 19
    • 0028332036 scopus 로고
    • Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers
    • Glass CK 1994 Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers. Endocr Rev 15:391-407
    • (1994) Endocr Rev , vol.15 , pp. 391-407
    • Glass, C.K.1
  • 20
    • 0028853067 scopus 로고
    • Modulation of DNA-binding specificity within the nuclear receptor family by substitutions at a single amino acid position
    • Zilliacus J, Wright APH, Carlstedt-Duke J, Nilsson L, Gustafsson J-A 1995 Modulation of DNA-binding specificity within the nuclear receptor family by substitutions at a single amino acid position. Proteins 21:57-67
    • (1995) Proteins , vol.21 , pp. 57-67
    • Zilliacus, J.1    Wright, A.P.H.2    Carlstedt-Duke, J.3    Nilsson, L.4    Gustafsson, J.-A.5
  • 21
    • 0023808861 scopus 로고
    • The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer
    • Kumar V, Chambon P 1988 The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell 55:145-156
    • (1988) Cell , vol.55 , pp. 145-156
    • Kumar, V.1    Chambon, P.2
  • 22
    • 0029120606 scopus 로고
    • An antiestrogen: A phosphotyrosyl peptide that blocks dimerization of the human estrogen receptor
    • Arnold SF, Nodtides AC 1995 An antiestrogen: a phosphotyrosyl peptide that blocks dimerization of the human estrogen receptor. Proc Natl Acad Sci USA 92:7475-7479
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7475-7479
    • Arnold, S.F.1    Nodtides, A.C.2
  • 23
    • 0027161982 scopus 로고
    • Steroid requirement for androgen receptor dimerization and DNA binding
    • Wong C-I, Zhou Z-X, Sar M, Wilson EM 1993 Steroid requirement for androgen receptor dimerization and DNA binding. J Biol Chem 268:19004-19012
    • (1993) J Biol Chem , vol.268 , pp. 19004-19012
    • Wong, C.-I.1    Zhou, Z.-X.2    Sar, M.3    Wilson, E.M.4
  • 24
    • 85047678506 scopus 로고    scopus 로고
    • 3H]progesterone to the human progesterone receptor: Differences between individual and mixed isoforms
    • 3H]progesterone to the human progesterone receptor: differences between individual and mixed isoforms. Endocrinology 137:2339-2346
    • (1996) Endocrinology , vol.137 , pp. 2339-2346
    • Carbajo, P.1    Christensen, K.2    Edwards, D.P.3    Skafar, D.F.4
  • 25
    • 0026756271 scopus 로고
    • Determinants of high-affinity DNA binding by the glucocorticoid receptor: Evaluation of receptor domains outside the DNA-binding domain
    • Dahlman-Wright K, Wright APH, Gustafsson J-A 1992 Determinants of high-affinity DNA binding by the glucocorticoid receptor: evaluation of receptor domains outside the DNA-binding domain. Biochemistry 31:9040-9044
    • (1992) Biochemistry , vol.31 , pp. 9040-9044
    • Dahlman-Wright, K.1    Wright, A.P.H.2    Gustafsson, J.-A.3
  • 26
    • 0028289947 scopus 로고
    • Analysis of androgen receptor-DNA interactions with receptor proteins produced in insect cells
    • Kallio PJ, Palvimo JJ, Mehto M, Janne OA 1994 Analysis of androgen receptor-DNA interactions with receptor proteins produced in insect cells. J Biol Chem 269: 11514-11522
    • (1994) J Biol Chem , vol.269 , pp. 11514-11522
    • Kallio, P.J.1    Palvimo, J.J.2    Mehto, M.3    Janne, O.A.4
  • 27
    • 0030062631 scopus 로고    scopus 로고
    • Glucocorticoid receptor dimerization investigated by analysis of receptor binding to glucocorticoid responsive elements using a monomer-dimer equilibrium model
    • Segard-Maurel I, Rajkowski K, Jibard N, Schweizwer-Groyer G, Baulieu E-E, Cadepond F 1996 Glucocorticoid receptor dimerization investigated by analysis of receptor binding to glucocorticoid responsive elements using a monomer-dimer equilibrium model. Biochemistry 35:1634-1642
    • (1996) Biochemistry , vol.35 , pp. 1634-1642
    • Segard-Maurel, I.1    Rajkowski, K.2    Jibard, N.3    Schweizwer-Groyer, G.4    Baulieu, E.-E.5    Cadepond, F.6
  • 28
    • 0030955767 scopus 로고    scopus 로고
    • Hinge and amino-terminal sequences contribute to solution dimerization of human progesterone receptor
    • Tetel MJ, Jung S, Carbajo P, Ladtkow T, Skafar DF, Edwards DP 1997 Hinge and amino-terminal sequences contribute to solution dimerization of human progesterone receptor. Mol Endocrinol 11:1114-1128
    • (1997) Mol Endocrinol , vol.11 , pp. 1114-1128
    • Tetel, M.J.1    Jung, S.2    Carbajo, P.3    Ladtkow, T.4    Skafar, D.F.5    Edwards, D.P.6
  • 29
    • 0027195589 scopus 로고
    • In vivo evidence against the existence of antiprogestins disrupting receptor binding to DNA
    • Delabre K, Guiochon-Mantel A, Milgorm E 1993 in vivo evidence against the existence of antiprogestins disrupting receptor binding to DNA. Proc Natl Acad Sci USA 90:4421-4425
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4421-4425
    • Delabre, K.1    Guiochon-Mantel, A.2    Milgorm, E.3
  • 30
    • 0031763999 scopus 로고    scopus 로고
    • The antagonists RU486 and ZK98299 stimulate progesterone receptor binding to DNA in vitro and in vivo but have distinct effects on receptor conformation
    • Gass, EK, SA Leonhardt, SK Nordeen, DP Edwards 1998 The antagonists RU486 and ZK98299 stimulate progesterone receptor binding to DNA in vitro and in vivo but have distinct effects on receptor conformation. Endocrinology 139:1905-1919
    • (1998) Endocrinology , vol.139 , pp. 1905-1919
    • Gass, E.K.1    Leonhardt, S.A.2    Nordeen, S.K.3    Edwards, D.P.4
  • 31
    • 0026726806 scopus 로고
    • Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation
    • Allan GF, Leng X, Tsai SF, Weigel NL, Edwards DP, Tsai M-J, O'Malley BW 1992 Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation. J Biol Chem 267:19513-19520
    • (1992) J Biol Chem , vol.267 , pp. 19513-19520
    • Allan, G.F.1    Leng, X.2    Tsai, S.F.3    Weigel, N.L.4    Edwards, D.P.5    Tsai, M.-J.6    O'Malley, B.W.7
  • 32
    • 0026786105 scopus 로고
    • Ligands induce conformational changes in the carboxyl-terminus of progesterone receptors which are detected by a site-directed antipeptide monoclonal antibody
    • Weigel NL, Beck CA, Estes PA, Prendergast P, Altmann M, Christensen K, Edwards DP 1992 Ligands induce conformational changes in the carboxyl-terminus of progesterone receptors which are detected by a site-directed antipeptide monoclonal antibody. Mol Endocrinol 6:1585-1597
    • (1992) Mol Endocrinol , vol.6 , pp. 1585-1597
    • Weigel, N.L.1    Beck, C.A.2    Estes, P.A.3    Prendergast, P.4    Altmann, M.5    Christensen, K.6    Edwards, D.P.7
  • 33
    • 0026653659 scopus 로고
    • The mechanism of RU486 antagonism is dependent on the conformation of the carboxyterminal tail of the human progesterone receptor
    • Vegeto E, Allan GF, Schrader WT, Tsai M-J, McDonnell DP, O'Malley BW 1992 The mechanism of RU486 antagonism is dependent on the conformation of the carboxyterminal tail of the human progesterone receptor. Cell 69:703-713
    • (1992) Cell , vol.69 , pp. 703-713
    • Vegeto, E.1    Allan, G.F.2    Schrader, W.T.3    Tsai, M.-J.4    McDonnell, D.P.5    O'Malley, B.W.6
  • 35
    • 0029038986 scopus 로고
    • Analysis of estrogen receptor function in vitro reveals three distinct classes of antiestrogens
    • McDonnell DP, Clemm DL, Hermann T, Goldman ME, Pike JW 1995 Analysis of estrogen receptor function in vitro reveals three distinct classes of antiestrogens. Mol Endocrinol 9:659-669
    • (1995) Mol Endocrinol , vol.9 , pp. 659-669
    • McDonnell, D.P.1    Clemm, D.L.2    Hermann, T.3    Goldman, M.E.4    Pike, J.W.5
  • 37
    • 0029026914 scopus 로고
    • Definition of the critical cellular components which distinguish between hormone and antihormone activated progesterone receptor
    • Clemm DL, Macy BL, Santiso-Mere D, McDonnell DP 1995 Definition of the critical cellular components which distinguish between hormone and antihormone activated progesterone receptor. J Steroid Biochem Mol Biol 53:487-495
    • (1995) J Steroid Biochem Mol Biol , vol.53 , pp. 487-495
    • Clemm, D.L.1    Macy, B.L.2    Santiso-Mere, D.3    McDonnell, D.P.4
  • 39
    • 0028124463 scopus 로고
    • The two-hybrid system: An assay for protein-protein interactions
    • Fields S, Sternglanz R 1994 The two-hybrid system: an assay for protein-protein interactions. Trends Genet 10:286-292
    • (1994) Trends Genet , vol.10 , pp. 286-292
    • Fields, S.1    Sternglanz, R.2
  • 40
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S, Song OK 1989 A novel genetic system to detect protein-protein interactions. Nature 340:245-246
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.K.2
  • 41
    • 0027518430 scopus 로고
    • Detection and modulation in vivo of helix-loop-helix protein-protein interactions
    • Finkel T, Duc J, Fearon ER, Dang CV, Tomaselli GF 1993 Detection and modulation in vivo of helix-loop-helix protein-protein interactions. J Biol Chem 268:5-8
    • (1993) J Biol Chem , vol.268 , pp. 5-8
    • Finkel, T.1    Duc, J.2    Fearon, E.R.3    Dang, C.V.4    Tomaselli, G.F.5
  • 42
    • 0028786569 scopus 로고
    • Yeast two-hybrid system demonstrates that estrogen receptor dimerization is ligand-dependent in vivo
    • Wang H, Peters GA, Zeng X, Tang M, Ip W, Khan SA 1995 Yeast two-hybrid system demonstrates that estrogen receptor dimerization is ligand-dependent in vivo. J Biol Chem 270:23322-23329
    • (1995) J Biol Chem , vol.270 , pp. 23322-23329
    • Wang, H.1    Peters, G.A.2    Zeng, X.3    Tang, M.4    Ip, W.5    Khan, S.A.6
  • 43
    • 0029560494 scopus 로고
    • Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer
    • Langley E, Zhou Z, Wilson EM 1995 Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer. J Biol Chem 270:29983-29990
    • (1995) J Biol Chem , vol.270 , pp. 29983-29990
    • Langley, E.1    Zhou, Z.2    Wilson, E.M.3
  • 45
    • 0026445459 scopus 로고
    • Effects of the steroid antagonist RU486 on dimerization of the human progesterone receptor
    • DeMarzo AM, Onate SA, Nordeen SK, Edwards DP 1992 Effects of the steroid antagonist RU486 on dimerization of the human progesterone receptor. Biochemistry 31:10491-10501
    • (1992) Biochemistry , vol.31 , pp. 10491-10501
    • DeMarzo, A.M.1    Onate, S.A.2    Nordeen, S.K.3    Edwards, D.P.4
  • 46
    • 0025965909 scopus 로고
    • Dimerization of mammalian progesterone receptors occurs in the absence of DNA and is related to the release of the 90-kDa heat shock protein
    • DeMarzo AM, Beck CA, Onate SA, Edwards DP 1991 Dimerization of mammalian progesterone receptors occurs in the absence of DNA and is related to the release of the 90-kDa heat shock protein. Proc Natl Acad Sci USA 88:72-76
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 72-76
    • DeMarzo, A.M.1    Beck, C.A.2    Onate, S.A.3    Edwards, D.P.4
  • 47
    • 0027300145 scopus 로고
    • Specific binding of progesterone receptor to progesterone-responsive elements does not require prior dimerization
    • Cohen-Solal K, Bailly A, Rauch C, Quesne M, Milgrom E 1993 Specific binding of progesterone receptor to progesterone-responsive elements does not require prior dimerization. Eur J Biochem 214:189-195
    • (1993) Eur J Biochem , vol.214 , pp. 189-195
    • Cohen-Solal, K.1    Bailly, A.2    Rauch, C.3    Quesne, M.4    Milgrom, E.5
  • 48
    • 0025697436 scopus 로고
    • Dimerization of the chicken progesterone receptor in vitro can occur in the absence of hormone and DNA
    • Rodriguez R, Weigel NL, O'Malley BW, Schrader WT 1990 Dimerization of the chicken progesterone receptor in vitro can occur in the absence of hormone and DNA. Mol Endocrinol 4:1782-1790
    • (1990) Mol Endocrinol , vol.4 , pp. 1782-1790
    • Rodriguez, R.1    Weigel, N.L.2    O'Malley, B.W.3    Schrader, W.T.4
  • 49
    • 0028073682 scopus 로고
    • A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B-isoform
    • Sartorius CA, Melville MY, Hovland AR, Tung L, Takimoto GS, Horwitz KB 1994 A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B-isoform. Mol Endocrinol 8:1347-1360
    • (1994) Mol Endocrinol , 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
  • 50
    • 0026768322 scopus 로고
    • A limiting factor mediates the differential activation of promoters by the human progesterone receptor isoforms
    • Meyer M-E, Quirin-Stricker C, Lerouge T, Bocquel M-T, Gronemeyer H 1992 A limiting factor mediates the differential activation of promoters by the human progesterone receptor isoforms. J Biol Chem 267:10882-10887
    • (1992) J Biol Chem , vol.267 , pp. 10882-10887
    • Meyer, M.-E.1    Quirin-Stricker, C.2    Lerouge, T.3    Bocquel, M.-T.4    Gronemeyer, H.5
  • 51
    • 0028033988 scopus 로고
    • The A and B isoforms of the human progesterone receptor operate through distinct signaling pathways within target cells
    • Wen DX, Xu Y-F, Mais DE, Goldman ME, McDonnell DP 1994 The A and B isoforms of the human progesterone receptor operate through distinct signaling pathways within target cells. Mol Cell Biol 14:8356-8364
    • (1994) Mol Cell Biol , vol.14 , pp. 8356-8364
    • Wen, D.X.1    Xu, Y.-F.2    Mais, D.E.3    Goldman, M.E.4    McDonnell, D.P.5
  • 52
    • 0027427216 scopus 로고
    • Human progesterone receptor a form is a cell- and promoter-specific repressor of human progesterone receptor B function
    • Vegeto E, Shahbaz MM, Wen DX, Goldman ME, O'Malley BW, McDonnell DP 1993 Human progesterone receptor A form is a cell- and promoter-specific repressor of human progesterone receptor B function. Mol Endocrinol 7:1244-1255
    • (1993) Mol Endocrinol , 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
  • 53
    • 0031910827 scopus 로고    scopus 로고
    • The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor
    • Wagner BL, Norris JD, Knotts TA, Weigel NL, McDonnell DP 1998 The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor. Mol Cell Biol 18:1369-1378
    • (1998) Mol Cell Biol , vol.18 , pp. 1369-1378
    • Wagner, B.L.1    Norris, J.D.2    Knotts, T.A.3    Weigel, N.L.4    McDonnell, D.P.5
  • 54
    • 0030946198 scopus 로고    scopus 로고
    • Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen
    • Smith CL, Nawaz Z, O'Malley BW 1997 Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol Endocrinol 11:657-666
    • (1997) Mol Endocrinol , vol.11 , pp. 657-666
    • Smith, C.L.1    Nawaz, Z.2    O'Malley, B.W.3
  • 55
    • 0030998328 scopus 로고    scopus 로고
    • The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPa and the core-pressors N-Cor or SMRT
    • Jackson TA, Richer JK, Bain DL, Takimoto GS, Tung L, Horwitz KB 1997 The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the core-pressors N-CoR or SMRT. Mol Endocrinol 11:693-705
    • (1997) Mol Endocrinol , vol.11 , pp. 693-705
    • Jackson, T.A.1    Richer, J.K.2    Bain, D.L.3    Takimoto, G.S.4    Tung, L.5    Horwitz, K.B.6
  • 57
    • 0030933291 scopus 로고    scopus 로고
    • Yeast hormone response element assays detect and characterize GRIP1 coactivator-dependent activation of transcription by thyroid and retinoid nuclear receptors
    • Walfish PG, Yoganathan T, Yang Y-F, Hong H, Butt TR, Stallcup MR 1997 Yeast hormone response element assays detect and characterize GRIP1 coactivator-dependent activation of transcription by thyroid and retinoid nuclear receptors. Proc Natl Acad Sci USA 94:3697-3702
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3697-3702
    • Walfish, P.G.1    Yoganathan, T.2    Yang, Y.-F.3    Hong, H.4    Butt, T.R.5    Stallcup, M.R.6
  • 59
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • Williams SP, Sigler PB 1998 Atomic structure of progesterone complexed with its receptor. Nature 393:392-396
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 60
    • 0023640541 scopus 로고
    • Immunological analysis of human breast cancer progesterone receptors. 1. Immunoaffinity purification of transformed receptors and production of monoclonal antibodies
    • Estes PA, Suba EJ, Lawler-Heavner J, Elashry-Stowers D, Wei LL, Toft DO, Sullivan WP, Horwitz KB, Edwards DP 1987 Immunological analysis of human breast cancer progesterone receptors. 1. Immunoaffinity purification of transformed receptors and production of monoclonal antibodies. Biochemistry 26:6250-6262
    • (1987) Biochemistry , vol.26 , pp. 6250-6262
    • Estes, P.A.1    Suba, E.J.2    Lawler-Heavner, J.3    Elashry-Stowers, D.4    Wei, L.L.5    Toft, D.O.6    Sullivan, W.P.7    Horwitz, K.B.8    Edwards, D.P.9
  • 61
    • 0024571802 scopus 로고
    • Transcriptional activation by the adenovirus E1b protein
    • Lillie JW, Green MR 1989 Transcriptional activation by the adenovirus E1b protein. Nature 338:39-44
    • (1989) Nature , vol.338 , pp. 39-44
    • Lillie, J.W.1    Green, M.R.2
  • 62
    • 0031021312 scopus 로고    scopus 로고
    • Analysis of chicken progesterone receptor function and phosphorylation using an adenovirus-mediated procedure for high-efficiency DNA transfer
    • Allgood VE, Zhang Y, O'Malley BW, Weigel NL 1997 Analysis of chicken progesterone receptor function and phosphorylation using an adenovirus-mediated procedure for high-efficiency DNA transfer. Biochemistry 36:224-232
    • (1997) Biochemistry , vol.36 , pp. 224-232
    • Allgood, V.E.1    Zhang, Y.2    O'Malley, B.W.3    Weigel, N.L.4
  • 63
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:28-254
    • (1976) Anal Biochem , vol.72 , pp. 28-254
    • Bradford, M.M.1
  • 64
    • 0023127059 scopus 로고
    • A rapid, sensitive, and inexpensive assay for chloramphenicol acetyltransferase
    • Nordeen SK, Green PP, Fowlkes DM 1987 A rapid, sensitive, and inexpensive assay for chloramphenicol acetyltransferase. DNA 6:173-178
    • (1987) DNA , vol.6 , pp. 173-178
    • Nordeen, S.K.1    Green, P.P.2    Fowlkes, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.