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Volumn 227, Issue 11, 2002, Pages 969-980

Mechanism of action of progesterone antagonists

Author keywords

Progesterone; Progesterone receptor; RU486, nonsteroidal antagonists; Steroidal antagonists

Indexed keywords

11BETA [4 (DIMETHYLAMINO)PHENYL] 4',5' DIHYDRO 6BETA METHYLSPIRO[ESTRA 4,9 DIENE 17BETA,2'(3'H) FURAN] 3 ONE; 8 BROMO CYCLIC AMP; ANDROGEN RECEPTOR; ANTIGESTAGEN; CP 8400; CP 8401; DNA; ESTROGEN RECEPTOR; GLUCOCORTICOID RECEPTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LG 001447; LG 100127; LG 120753; LG 120830; MIFEPRISTONE; ONAPRISTONE; ORG 31806; ORG 33628; PF 1092C; PROMEGESTONE; PYRIDAZINE DERIVATIVE; RTI 012; RTI 022; RWJ 26329; TETRAHYDROPYRIDAZINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1; UNCLASSIFIED DRUG;

EID: 0036917921     PISSN: 00379727     EISSN: None     Source Type: Journal    
DOI: 10.1177/153537020222701104     Document Type: Short Survey
Times cited : (142)

References (74)
  • 2
    • 0031051692 scopus 로고    scopus 로고
    • RU486 (Mifepristone): Mechanisms of action and clinical uses
    • Cadepond F, Ulmann A, Baulieu E-E. RU486 (Mifepristone): Mechanisms of action and clinical uses. Annu Rev Med 48:129-156, 1997.
    • (1997) Annu Rev Med , vol.48 , pp. 129-156
    • Cadepond, F.1    Ulmann, A.2    Baulieu, E.-E.3
  • 3
    • 0024470651 scopus 로고
    • Contragestion and other clinical applications of RU 486, an antiprogesterone at the receptor
    • Baulieu E-E. Contragestion and other clinical applications of RU486, an antiprogesterone at the receptor. Science 245:1351-1357, 1989.
    • (1989) Science , vol.245 , pp. 1351-1357
    • Baulieu, E.-E.1
  • 4
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 14:121-141, 2000.
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 5
    • 0032617352 scopus 로고    scopus 로고
    • Coregulatory proteins in nuclear receptor action
    • Edwards DP. Coregulatory proteins in nuclear receptor action. Vitam Horm 55:165-218, 1999.
    • (1999) Vitam Horm , vol.55 , pp. 165-218
    • Edwards, D.P.1
  • 6
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna NJ, O'Malley BW. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108:465-474, 2002.
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 9
    • 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. 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.
    • (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
  • 10
    • 0037085303 scopus 로고    scopus 로고
    • Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells
    • Richer JK, Jacobsen BM, Manning NG, Abel MG, Wolf DM, Horwitz KB. Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells. J Biol Chem 277:5209-5218, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 5209-5218
    • Richer, J.K.1    Jacobsen, B.M.2    Manning, N.G.3    Abel, M.G.4    Wolf, D.M.5    Horwitz, K.B.6
  • 11
    • 0033374783 scopus 로고    scopus 로고
    • The A B isoforms of the human progesterone receptor: Two functionally different transcription factors encoded by a single gene
    • Giangrande PH, McDonnell DP. The A and B isoforms of the human progesterone receptor: Two functionally different transcription factors encoded by a single gene. Rec Prog Horm Res 54:291-313, 1999.
    • (1999) Rec Prog Horm Res , vol.54 , pp. 291-313
    • Giangrande, P.H.1    McDonnell, D.P.2
  • 12
    • 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. 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.
    • (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
  • 13
    • 0033669231 scopus 로고    scopus 로고
    • Progesterone receptors in reproduction: Functional impact of the A and B isoforms
    • Conneely OM, Lydon JP. Progesterone receptors in reproduction: Functional impact of the A and B isoforms. Steroids 65:571-577, 2000.
    • (2000) Steroids , vol.65 , pp. 571-577
    • Conneely, O.M.1    Lydon, J.P.2
  • 14
    • 0035919191 scopus 로고    scopus 로고
    • Reproductive functions of the progesterone receptor isoforms: Lessons from knock-out mice
    • Conneely OM, Mulac-Jericevic B, Lydon JP, DeMayo FJ. Reproductive functions of the progesterone receptor isoforms: Lessons from knock-out mice. Mol Cell Endocrinol 179:97-103, 2001.
    • (2001) Mol Cell Endocrinol , vol.179 , pp. 97-103
    • Conneely, O.M.1    Mulac-Jericevic, B.2    Lydon, J.P.3    DeMayo, F.J.4
  • 15
    • 0031906819 scopus 로고    scopus 로고
    • Transgenic mice carrying an imbalance in the native ratio of A to B forms of progesterone receptor exhibit developmental abnormalities in mammary glands
    • Shyamala G, Yang X, Silberstein G, Barcellos-Hoff MH, Dale E. Transgenic mice carrying an imbalance in the native ratio of A to B forms of progesterone receptor exhibit developmental abnormalities in mammary glands. Proc Natl Acad Sci USA 95:696-701, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 696-701
    • Shyamala, G.1    Yang, X.2    Silberstein, G.3    Barcellos-Hoff, M.H.4    Dale, E.5
  • 16
    • 0034463399 scopus 로고    scopus 로고
    • Molecular chaperone interactions with steroid receptors: An update
    • Cheung J, Smith DF. Molecular chaperone interactions with steroid receptors: An update. Mol Endocrinol 14:939-946, 2000.
    • (2000) Mol Endocrinol , vol.14 , pp. 939-946
    • Cheung, J.1    Smith, D.F.2
  • 17
    • 0032524634 scopus 로고    scopus 로고
    • The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF 2 domains of steroid receptors
    • Onate SA, Boonyaratanakornkit V, Spencer TE, Tsai SY, Tsai M-J, Edwards DP, O'Malley BW. The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J Biol Chem 273:12101-12108, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 12101-12108
    • Onate, S.A.1    Boonyaratanakornkit, V.2    Spencer, T.E.3    Tsai, S.Y.4    Tsai, M.-J.5    Edwards, D.P.6    O'Malley, B.W.7
  • 18
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonist of this alteration by tamoxifen
    • Shiau A, Barstad D, Loria P, Cheng L, Kushner P, Agard D, Greene G. The structural basis of estrogen receptor/coactivator recognition and the antagonist of this alteration by tamoxifen. Cell 7:927-937, 1999.
    • (1999) Cell , vol.7 , pp. 927-937
    • Shiau, A.1    Barstad, D.2    Loria, P.3    Cheng, L.4    Kushner, P.5    Agard, D.6    Greene, G.7
  • 19
    • 0032549744 scopus 로고    scopus 로고
    • Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene
    • Xu J, Qiu Y, DeMayo FJ, Tsai SY, Tsai M-J, O'Malley B. Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene. Science 279:1922-1925, 1998.
    • (1998) Science , vol.279 , pp. 1922-1925
    • Xu, J.1    Qiu, Y.2    DeMayo, F.J.3    Tsai, S.Y.4    Tsai, M.-J.5    O'Malley, B.6
  • 20
    • 0034612264 scopus 로고    scopus 로고
    • The steroid receptor coactivator SRC-3 (pCIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development
    • Xu J, Liao L, Ning G, Yoshida-Komiya H, Deng C, O'Malley B. The steroid receptor coactivator SRC-3 (pCIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development. Proc Natl Acad Sci USA 97:6379-6384, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6379-6384
    • Xu, J.1    Liao, L.2    Ning, G.3    Yoshida-Komiya, H.4    Deng, C.5    O'Malley, B.6
  • 22
    • 0036135671 scopus 로고    scopus 로고
    • Genetic ablation of the steroid receptor coactivatorubiquitin ligase, E6-AP, results in tissue-selective steroid hormone resistance and defects in reproduction
    • Smith CL, DeVera DG, Lamb DJ, Nawaz Z, Jiang YH, Beaudet AL, O'Malley B. Genetic ablation of the steroid receptor coactivatorubiquitin ligase, E6-AP, results in tissue-selective steroid hormone resistance and defects in reproduction. Mol Cell Biol 2:525-535, 2002.
    • (2002) Mol Cell Biol , vol.2 , pp. 525-535
    • Smith, C.L.1    DeVera, D.G.2    Lamb, D.J.3    Nawaz, Z.4    Jiang, Y.H.5    Beaudet, A.L.6    O'Malley, B.7
  • 23
    • 0029855010 scopus 로고    scopus 로고
    • Steroid hormone receptors and their regulation by phosphorylation
    • Weigel N. Steroid hormone receptors and their regulation by phosphorylation. Biochem J 319:657-667, 1996.
    • (1996) Biochem J , vol.319 , pp. 657-667
    • Weigel, N.1
  • 24
    • 0035896651 scopus 로고    scopus 로고
    • Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites
    • Knotts T, Orkiszewski R, Cook R, Edwards D, Weigel N. Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites. J Biol Chem 276:8475-8483, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 8475-8483
    • Knotts, T.1    Orkiszewski, R.2    Cook, R.3    Edwards, D.4    Weigel, N.5
  • 25
    • 0033967491 scopus 로고    scopus 로고
    • Phosphorylation of human progesterone receptors at set-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome
    • Lange CA, Shen T, Horwitz KB. Phosphorylation of human progesterone receptors at set-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome. Proc Natl Acad Sci 97:1032-1037, 2000.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 1032-1037
    • Lange, C.A.1    Shen, T.2    Horwitz, K.B.3
  • 26
    • 0026653659 scopus 로고
    • The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor
    • Vegeto E, Allan GF, Schrader WT, Tsai M-J, McDonnell DP, O'Malley BW. The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor. Cell 69:703-713, 1992.
    • (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
  • 28
    • 0026445459 scopus 로고
    • Effects of the steroid antagonist RU 486 on dimerization of the human progesterone receptor
    • DeMarzo AM, Onate SA, Nordeen SK, Edwards DP. Effects of the steroid antagonist RU486 on dimerization of the human progesterone receptor. Biochemistry 31:10491-10501, 1992.
    • (1992) Biochemistry , vol.31 , pp. 10491-10501
    • DeMarzo, A.M.1    Onate, S.A.2    Nordeen, S.K.3    Edwards, D.P.4
  • 29
    • 0026322726 scopus 로고
    • Differences in the binding mechanism of RU 486 and progesterone to the progesterone receptor
    • Skafar D. Differences in the binding mechanism of RU486 and progesterone to the progesterone receptor. Biochemistry 30:10829-10832, 1991.
    • (1991) Biochemistry , vol.30 , pp. 10829-10832
    • Skafar, D.1
  • 30
    • 0024806349 scopus 로고
    • Mapping contacts between unpurified human progesterone receptor and the hormone response element of mouse mammary tumor virus
    • Kuhnel B, El Ashry D, Edwards DP, Nordeen SK. Mapping contacts between unpurified human progesterone receptor and the hormone response element of mouse mammary tumor virus. DNA 10:703-713, 1989.
    • (1989) DNA , vol.10 , pp. 703-713
    • Kuhnel, B.1    El Ashry, D.2    Edwards, D.P.3    Nordeen, S.K.4
  • 31
    • 0023938276 scopus 로고
    • Differential gene activation by glucocorticoids and progestins through the hormone regulatory element of mouse mammary tumor virus
    • Chalepakis G, Arnemann J, Slater E, Bruller HJ, Gross B, Beato M. Differential gene activation by glucocorticoids and progestins through the hormone regulatory element of mouse mammary tumor virus. Cell 53:371-382, 1988.
    • (1988) Cell , vol.53 , pp. 371-382
    • Chalepakis, G.1    Arnemann, J.2    Slater, E.3    Bruller, H.J.4    Gross, B.5    Beato, M.6
  • 32
    • 0027195589 scopus 로고
    • In vivo evidence against the existence of antiprogestins disrupting receptor binding to DNA
    • Delabre K, Guiochon-Mantel A, Milgorm E. In vivo evidence against the existence of antiprogestins disrupting receptor binding to DNA. Proc Natl Acad Sci USA 90:4421-4425, 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4421-4425
    • Delabre, K.1    Guiochon-Mantel, A.2    Milgorm, E.3
  • 33
    • 0031763999 scopus 로고    scopus 로고
    • The antagonists RU 486 and ZK98299 stimulate progesterone receptor binding to DNA in vitro and in vivo but have distinct effects on receptor conformation
    • Gass EK, Leonhardt SA, Nordeen SK, Edwards DP. The antagonists RU486 and ZK98299 stimulate progesterone receptor binding to DNA in vitro and in vivo but have distinct effects on receptor conformation. Endocrinol 139:1905-1919, 1998.
    • (1998) Endocrinol , vol.139 , pp. 1905-1919
    • Gass, E.K.1    Leonhardt, S.A.2    Nordeen, S.K.3    Edwards, D.P.4
  • 34
    • 0026096890 scopus 로고
    • Two types of antiprogestins identified by their differential action in transcriptionally active extracts from T 47D cells
    • Klein-Hitpass L, Cato ACB, Henderson D, Ryffel G. Two types of antiprogestins identified by their differential action in transcriptionally active extracts from T47D cells. Nucl Acids Res 19:1227-1234, 1991.
    • (1991) Nucl Acids Res , vol.19 , pp. 1227-1234
    • Klein-Hitpass, L.1    Cato, A.C.B.2    Henderson, D.3    Ryffel, G.4
  • 35
    • 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. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354-1357, 1995.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 36
    • 0024434594 scopus 로고
    • Human progesterone receptor complexed with the antagonist RU 486 binds to hormone response elements in a structurally altered form
    • El-Ashry D, Oñate SO. K. NS, Edwards DP. Human progesterone receptor complexed with the antagonist RU486 binds to hormone response elements in a structurally altered form. Mol Endocrinol 3:1545-1558, 1989.
    • (1989) Mol Endocrinol , vol.3 , pp. 1545-1558
    • El-Ashry, D.1    Oñate, S.O.2    Edwards, D.P.3
  • 37
    • 0025053671 scopus 로고
    • Agonistic and antagonistic activities of RU 486 on the functions of the human progesterone receptor
    • Meyer M-E, Pornon A, Ji J, Bocquel M-T, Chambon P, Gronemeyer H. Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor. EMBO J 9:3923-3932, 1990.
    • (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
  • 38
    • 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. Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation. J Biol Chem 267:19513-19520, 1992.
    • (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
  • 39
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • Williams SP, Sigler PB. Atomic structure of progesterone complexed with its receptor. Nature 393:392-396, 1998.
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 40
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tanebaum D, Wang Y, Williams S, Sigler P. Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci USA 95:5998-6003, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5998-6003
    • Tanebaum, D.1    Wang, Y.2    Williams, S.3    Sigler, P.4
  • 41
    • 0029616211 scopus 로고
    • Ligand-dependent, transcriptionally productive association of the amino- and carboxylterminal regions of a steroid hormone nuclear receptor
    • Kraus WL, McInerney EM, Katzenellenbogen BS. Ligand-dependent, transcriptionally productive association of the amino- and carboxylterminal regions of a steroid hormone nuclear receptor. Proc Natl Acad Sci USA 92:12314-12318, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12314-12318
    • Kraus, W.L.1    McInerney, E.M.2    Katzenellenbogen, B.S.3
  • 42
    • 0034725648 scopus 로고    scopus 로고
    • FXXLF and WXXLF sequences mediate the NH2-terminal interaction with the ligand binding domain of the androgen receptor
    • He B, Kemppainen JA, Wilson EM. FXXLF and WXXLF sequences mediate the NH2-terminal interaction with the ligand binding domain of the androgen receptor. J Biol Chem 275:22986-22994, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 22986-22994
    • He, B.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 43
    • 0033305373 scopus 로고    scopus 로고
    • Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo
    • Tetel MJ, Giangrande PH, Leonhardt SA, McDonnell DP, Edwards DP. Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo. Mol Endocrinol 13:910-924, 1999.
    • (1999) Mol Endocrinol , vol.13 , pp. 910-924
    • Tetel, M.J.1    Giangrande, P.H.2    Leonhardt, S.A.3    McDonnell, D.P.4    Edwards, D.P.5
  • 44
    • 0029982567 scopus 로고    scopus 로고
    • Modulation of AP-1 activity by the human progesterone receptor in endometrial adenocarcinoma cells
    • Bamberger A-M, Bamberger C, Gellersen B, Schulte HM. Modulation of AP-1 activity by the human progesterone receptor in endometrial adenocarcinoma cells. Proc Natl Acad Sci USA 93:6169-6174, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6169-6174
    • Bamberger, A.-M.1    Bamberger, C.2    Gellersen, B.3    Schulte, H.M.4
  • 45
    • 0029939162 scopus 로고    scopus 로고
    • Negative interaction between the RelA(p65) subunit of NF-κB and the progesterone receptor
    • Kalkhoven E, Wissink S, van der Saag PT, van der Burg B. Negative interaction between the RelA(p65) subunit of NF-κB and the progesterone receptor. J Biol Chem 271:6217-6224, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 6217-6224
    • Kalkhoven, E.1    Wissink, S.2    Van der Saag, P.T.3    Van der Burg, B.4
  • 46
    • 0036139766 scopus 로고    scopus 로고
    • Functional association of PR and CCAAT/Enhancer-binding protein β isoforms: Promoter-dependent cooperation between PR-B and liver-enriched inhibitory protein, or liver-enriched activatory protein and PR-A in human endometrial stromal cells
    • Christian M, Pohnke Y, Kempf R, Gellersen B, Brosens JJ. Functional association of PR and CCAAT/Enhancer-binding protein β isoforms: Promoter-dependent cooperation between PR-B and liver-enriched inhibitory protein, or liver-enriched activatory protein and PR-A in human endometrial stromal cells. Mol Endocrinol 16:141-154, 2002.
    • (2002) Mol Endocrinol , vol.16 , pp. 141-154
    • Christian, M.1    Pohnke, Y.2    Kempf, R.3    Gellersen, B.4    Brosens, J.J.5
  • 47
    • 1942471552 scopus 로고    scopus 로고
    • Novel mechanisms of progesterone antagonists and progesterone receptor
    • Edwards DP, Leonhardt SA, Gass-Handel E. Novel mechanisms of progesterone antagonists and progesterone receptor. J Soc Gynecol Invest 7:22-24, 2000.
    • (2000) J Soc Gynecol Invest , vol.7 , pp. 22-24
    • Edwards, D.P.1    Leonhardt, S.A.2    Gass-Handel, E.3
  • 49
    • 0031725634 scopus 로고    scopus 로고
    • Agonist and antagonists induce homodimerization and mixed ligand heterodimerization of human progesterone receptors in vivo by a mammalian two-hybrid assay
    • Leonhardt SA, Altmann M, Edwards DP. Agonist and antagonists induce homodimerization and mixed ligand heterodimerization of human progesterone receptors in vivo by a mammalian two-hybrid assay. Mol Endocrinol 12:1914-1930, 1998.
    • (1998) Mol Endocrinol , vol.12 , pp. 1914-1930
    • Leonhardt, S.A.1    Altmann, M.2    Edwards, D.P.3
  • 50
    • 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 corepressors N-CoR or SMRT
    • Jackson TA, Richer JK, Bain DL, Takimoto GS, Tung L, Horwitz KB. The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the corepressors N-CoR or SMRT. Mol Endocrinol 11:693-705, 1997.
    • (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
  • 51
    • 0032230289 scopus 로고    scopus 로고
    • A nuclear receptor corepressor modulates transcriptional activity of antagonist-occupied steroid hormone receptor
    • Zhang X, Jeyakumar M, Petukhov S, Bagchi MK. A nuclear receptor corepressor modulates transcriptional activity of antagonist-occupied steroid hormone receptor. Mol Endocrinol 12:513-524, 1998.
    • (1998) Mol Endocrinol , vol.12 , pp. 513-524
    • Zhang, X.1    Jeyakumar, M.2    Petukhov, S.3    Bagchi, M.K.4
  • 52
    • 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. 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.
    • (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
    • 0034000089 scopus 로고    scopus 로고
    • The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding
    • Giangrande PH, Kimbrel ER, Edwards DP, McDonnell DP. The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding. Mol Cell Biol 20:3102-3115, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 3102-3115
    • Giangrande, P.H.1    Kimbrel, E.R.2    Edwards, D.P.3    McDonnell, D.P.4
  • 55
    • 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 MK, Hoeffler JP, Takimoto GS, Horwitz KB. Antagonist-occupied human progesterone B-receptors activate transcription without binding to progesterone response elements and are dominantly inhibited by A-receptors. Mol Endocrinol 7:1256-1265, 1993.
    • (1993) Mol Endocrinol , vol.7 , pp. 1256-1265
    • Tung, L.1    Mohamed, M.K.2    Hoeffler, J.P.3    Takimoto, G.S.4    Horwitz, K.B.5
  • 56
    • 0027191140 scopus 로고
    • The progesterone antagonist RU 486 acquires agonist activity upon stimulation of cAMP signaling pathways
    • Beck CA, Weigel NL, Moyer ML, Nordeen SK, Edwards DP. The progesterone antagonist RU486 acquires agonist activity upon stimulation of cAMP signaling pathways. Proc Natl Acad Sci USA 90:4441-4445, 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4441-4445
    • Beck, C.A.1    Weigel, N.L.2    Moyer, M.L.3    Nordeen, S.K.4    Edwards, D.P.5
  • 57
    • 0027156480 scopus 로고
    • Antagonist-occupied human progesterone receptors bound to DNA are functionally switched to transcriptional agonists by cAMP
    • Sartorius CA, Tung L, Takimoto GS, Horwitz KB. Antagonist-occupied human progesterone receptors bound to DNA are functionally switched to transcriptional agonists by cAMP. J Biol Chem 268:9262-9266, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 9262-9266
    • Sartorius, C.A.1    Tung, L.2    Takimoto, G.S.3    Horwitz, K.B.4
  • 58
    • 0034460313 scopus 로고    scopus 로고
    • 8-Bromo-cyclic AMP induces phosphorylation of two sites in SRC-1 that facilitate ligand-independent activation of the chicken progesterone receptor and are critical for functional cooperation between SRC-1 and CREB binding protein
    • Rowan BG, Garrison N, Weigel N, O'Malley B. 8-Bromo-cyclic AMP induces phosphorylation of two sites in SRC-1 that facilitate ligand-independent activation of the chicken progesterone receptor and are critical for functional cooperation between SRC-1 and CREB binding protein. Mol Cell Biol 23:8720-8730, 2000.
    • (2000) Mol Cell Biol , vol.23 , pp. 8720-8730
    • Rowan, B.G.1    Garrison, N.2    Weigel, N.3    O'Malley, B.4
  • 60
    • 0036311098 scopus 로고    scopus 로고
    • Jun dimerization protein-2 (JDP-2) functions as a progesterone receptor N-terminal domain coactivator
    • Wardell SE, Boonyaratanakornkit V, Adelman JS, Aronheim A, Edwards DP. Jun dimerization protein-2 (JDP-2) functions as a progesterone receptor N-terminal domain coactivator. Mol Cell Biol 22: 5451-5466, 2002.
    • (2002) Mol Cell Biol , vol.22 , pp. 5451-5466
    • Wardell, S.E.1    Boonyaratanakornkit, V.2    Adelman, J.S.3    Aronheim, A.4    Edwards, D.P.5
  • 62
    • 0026684499 scopus 로고
    • Novel antiprogestins ORG 31806 and 31710: Interaction with mammalian progesterone receptor and DNA binding of antisteroid receptor complexes
    • Mizutani T, Bhakta A, Kloosterboer HJ, Moudgil VK. Novel antiprogestins ORG 31806 and 31710: Interaction with mammalian progesterone receptor and DNA binding of antisteroid receptor complexes. J Steroid Biochem Mol Biol 42:695-704, 1992.
    • (1992) J Steroid Biochem Mol Biol , vol.42 , pp. 695-704
    • Mizutani, T.1    Bhakta, A.2    Kloosterboer, H.J.3    Moudgil, V.K.4
  • 65
    • 0032959038 scopus 로고    scopus 로고
    • The novel progesterone receptor antagonists RTI 3021-012 and RTI 3021-022 exhibit complex glucocorticoid receptor antagonist activities: Implications for the development of dissociated antiprogestins
    • Wagner BL, Pollio G, Giangrande P, Webster JC, Breslin M, Mais DE, Cook CE, Vedeckis WV, Cidlowski JA, McDonnell DP. The novel progesterone receptor antagonists RTI 3021-012 and RTI 3021-022 exhibit complex glucocorticoid receptor antagonist activities: Implications for the development of dissociated antiprogestins. Endocrinol 140:1449-1458, 1999.
    • (1999) Endocrinol , vol.140 , pp. 1449-1458
    • Wagner, B.L.1    Pollio, G.2    Giangrande, P.3    Webster, J.C.4    Breslin, M.5    Mais, D.E.6    Cook, C.E.7    Vedeckis, W.V.8    Cidlowski, J.A.9    McDonnell, D.P.10
  • 70
    • 0028805303 scopus 로고
    • Nonsteroidal progesterone receptor ligands. 1. 3-Aryl-1-benzoyl-1,4,5,6-tetrahydropyridazines
    • Combs DW, Reese K, Phillips A. Nonsteroidal progesterone receptor ligands. 1. 3-Aryl-1-benzoyl-1,4,5,6-tetrahydropyridazines. J Med Chem 38:4878-4879, 1995.
    • (1995) J Med Chem , vol.38 , pp. 4878-4879
    • Combs, D.W.1    Reese, K.2    Phillips, A.3
  • 72
    • 0035798402 scopus 로고    scopus 로고
    • Fungal metabolites, PF1092 compounds and their derivatives, are nonsteroidal and selective progesterone receptor modulators
    • Tabata Y, Iizulka J, Masuda NT, Shinei R, Kurihara K-I, Okonogi T, Hoshiko S, Kurata Y. Fungal metabolites, PF1092 compounds and their derivatives, are nonsteroidal and selective progesterone receptor modulators. Eur J Pharm 430:159-165, 2001.
    • (2001) Eur J Pharm , vol.430 , pp. 159-165
    • Tabata, Y.1    Iizulka, J.2    Masuda, N.T.3    Shinei, R.4    Kurihara, K.-I.5    Okonogi, T.6    Hoshiko, S.7    Kurata, Y.8


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