메뉴 건너뛰기




Volumn 348, Issue 2, 2012, Pages 418-429

Structural and functional analysis of domains of the progesterone receptor

Author keywords

Amino terminal domain (NTD); Carboxyl terminal extension (CTE); High mobility group B (HMGB) protein; Intrinsic disorder; Jun dimerization protein 2 (JDP 2); Progesterone receptor

Indexed keywords

CELL NUCLEUS RECEPTOR; DNA; HIGH MOBILITY GROUP B PROTEIN; JUN DIMERIZATION PROTEIN 2; PROGESTERONE RECEPTOR; REGULATOR PROTEIN; STEROID RECEPTOR; UNCLASSIFIED DRUG;

EID: 82655172410     PISSN: 03037207     EISSN: 18728057     Source Type: Journal    
DOI: 10.1016/j.mce.2011.07.017     Document Type: Review
Times cited : (67)

References (141)
  • 1
    • 66149124844 scopus 로고    scopus 로고
    • Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation
    • Abdel-Hafiz H., Dudevoir M.L., Horwitz K.B. Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation. J. Biol. Chem. 2009, 284:9099-9108.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9099-9108
    • Abdel-Hafiz, H.1    Dudevoir, M.L.2    Horwitz, K.B.3
  • 2
    • 0037072795 scopus 로고    scopus 로고
    • The inhibitory function in human progesterone receptor N termini binds SUMO-1 protein to regulate autoinhibition and transrepression
    • Abdel-Hafiz H., Takimoto G.S., Tung L., Horwitz K.B. The inhibitory function in human progesterone receptor N termini binds SUMO-1 protein to regulate autoinhibition and transrepression. J. Biol. Chem. 2002, 277:33950-33956.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33950-33956
    • Abdel-Hafiz, H.1    Takimoto, G.S.2    Tung, L.3    Horwitz, K.B.4
  • 3
    • 15944375439 scopus 로고    scopus 로고
    • GR and HMGB1 interact only within chromatin and influence each other's residence time
    • Agresti A., Scaffidi P., Riva A., Caiolfa V.R., Bianchi M.E. GR and HMGB1 interact only within chromatin and influence each other's residence time. Mol. Cell 2005, 18:109-121.
    • (2005) Mol. Cell , vol.18 , pp. 109-121
    • Agresti, A.1    Scaffidi, P.2    Riva, A.3    Caiolfa, V.R.4    Bianchi, M.E.5
  • 4
    • 0026726806 scopus 로고
    • Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation
    • Allan G.F., Leng X., Tsai S.Y., Weigel N.L., Edwards D.P., Tsai M.J., O'Malley B.W. Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation. J. Biol. Chem. 1992, 267:19513-19520.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19513-19520
    • Allan, G.F.1    Leng, X.2    Tsai, S.Y.3    Weigel, N.L.4    Edwards, D.P.5    Tsai, M.J.6    O'Malley, B.W.7
  • 5
    • 0030923133 scopus 로고    scopus 로고
    • Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions
    • Aronheim A., Zandi E., Hennemann H., Elledge S.J., Karin M. Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions. Mol. Cell. Biol. 1997, 17:3094-3102.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3094-3102
    • Aronheim, A.1    Zandi, E.2    Hennemann, H.3    Elledge, S.J.4    Karin, M.5
  • 6
    • 0034629344 scopus 로고    scopus 로고
    • The N-terminal region of the human progesterone A-receptor. Structural analysis and the influence of the DNA binding domain
    • Bain D.L., Franden M.A., McManaman J.L., Takimoto G.S., Horwitz K.B. The N-terminal region of the human progesterone A-receptor. Structural analysis and the influence of the DNA binding domain. J. Biol. Chem. 2000, 275:7313-7320.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7313-7320
    • Bain, D.L.1    Franden, M.A.2    McManaman, J.L.3    Takimoto, G.S.4    Horwitz, K.B.5
  • 7
    • 0035968162 scopus 로고    scopus 로고
    • The N-terminal region of human progesterone B-receptors: biophysical and biochemical comparison to A-receptors
    • Bain D.L., Franden M.A., McManaman J.L., Takimoto G.S., Horwitz K.B. The N-terminal region of human progesterone B-receptors: biophysical and biochemical comparison to A-receptors. J. Biol. Chem. 2001, 276:23825-23831.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23825-23831
    • Bain, D.L.1    Franden, M.A.2    McManaman, J.L.3    Takimoto, G.S.4    Horwitz, K.B.5
  • 8
    • 0037371863 scopus 로고    scopus 로고
    • Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c-Src/Erk pathway in mammalian cells
    • Ballare C., Uhrig M., Bechtold T., Sancho E., Di Domenico M., Migliaccio A., Auricchio F., Beato M. Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c-Src/Erk pathway in mammalian cells. Mol. Cell. Biol. 2003, 23:1994-2008.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1994-2008
    • Ballare, C.1    Uhrig, M.2    Bechtold, T.3    Sancho, E.4    Di Domenico, M.5    Migliaccio, A.6    Auricchio, F.7    Beato, M.8
  • 9
    • 0034129679 scopus 로고    scopus 로고
    • Steroid hormone receptors: an update
    • Beato M., Klug J. Steroid hormone receptors: an update. Hum. Reprod. Update 2000, 6:225-236.
    • (2000) Hum. Reprod. Update , vol.6 , pp. 225-236
    • Beato, M.1    Klug, J.2
  • 10
    • 24344498241 scopus 로고    scopus 로고
    • HMG proteins: dynamic players in gene regulation and differentiation
    • Bianchi M.E., Agresti A. HMG proteins: dynamic players in gene regulation and differentiation. Curr. Opin. Genet. Dev. 2005, 15:496-506.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 496-506
    • Bianchi, M.E.1    Agresti, A.2
  • 12
    • 33846581488 scopus 로고    scopus 로고
    • The role of extranuclear signaling actions of progesterone receptor in mediating progesterone regulation of gene expression and the cell cycle
    • Boonyaratanakornkit V., McGowan E., Sherman L., Mancini M.A., Cheskis B.J., Edwards D.P. The role of extranuclear signaling actions of progesterone receptor in mediating progesterone regulation of gene expression and the cell cycle. Mol. Endocrinol. 2007, 21:359-375.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 359-375
    • Boonyaratanakornkit, V.1    McGowan, E.2    Sherman, L.3    Mancini, M.A.4    Cheskis, B.J.5    Edwards, D.P.6
  • 14
    • 0034852802 scopus 로고    scopus 로고
    • Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases
    • Boonyaratanakornkit V., Scott M.P., Ribon V., Sherman L., Anderson S.M., Maller J.L., Miller W.T., Edwards D.P. Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases. Mol. Cell 2001, 8:269-280.
    • (2001) Mol. Cell , vol.8 , pp. 269-280
    • Boonyaratanakornkit, V.1    Scott, M.P.2    Ribon, V.3    Sherman, L.4    Anderson, S.M.5    Maller, J.L.6    Miller, W.T.7    Edwards, D.P.8
  • 15
    • 0034306499 scopus 로고    scopus 로고
    • Nuclear receptor ligand-binding domains: three-dimensional structures, molecular interactions and pharmacological implications
    • Bourguet W., Germain P., Gronemeyer H. Nuclear receptor ligand-binding domains: three-dimensional structures, molecular interactions and pharmacological implications. Trends Pharmacol. Sci. 2000, 21:381-388.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 381-388
    • Bourguet, W.1    Germain, P.2    Gronemeyer, H.3
  • 17
    • 0033052037 scopus 로고    scopus 로고
    • The lack of chromosomal protein Hmg1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice
    • Calogero S., Grassi F., Aguzzi A., Voigtlander T., Ferrier P., Ferrari S., Bianchi M.E. The lack of chromosomal protein Hmg1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice. Nat. Genet. 1999, 22:276-280.
    • (1999) Nat. Genet. , vol.22 , pp. 276-280
    • Calogero, S.1    Grassi, F.2    Aguzzi, A.3    Voigtlander, T.4    Ferrier, P.5    Ferrari, S.6    Bianchi, M.E.7
  • 19
    • 33747860031 scopus 로고    scopus 로고
    • The role of the general transcription factor IIF in androgen receptor-dependent transcription
    • Choudhry M.A., Ball A., McEwan I.J. The role of the general transcription factor IIF in androgen receptor-dependent transcription. Mol. Endocrinol. 2006, 20:2052-2061.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 2052-2061
    • Choudhry, M.A.1    Ball, A.2    McEwan, I.J.3
  • 21
    • 0034463134 scopus 로고    scopus 로고
    • Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody
    • Clemm D.L., Sherman L., Boonyaratanakornkit V., Schrader W.T., Weigel N.L., Edwards D.P. Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody. Mol. Endocrinol. 2000, 14:52-65.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 52-65
    • Clemm, D.L.1    Sherman, L.2    Boonyaratanakornkit, V.3    Schrader, W.T.4    Weigel, N.L.5    Edwards, D.P.6
  • 22
    • 33750715148 scopus 로고    scopus 로고
    • Hydrodynamic analysis of the human progesterone receptor A-isoform reveals that self-association occurs in the micromolar range
    • Connaghan-Jones K.D., Heneghan A.F., Miura M.T., Bain D.L. Hydrodynamic analysis of the human progesterone receptor A-isoform reveals that self-association occurs in the micromolar range. Biochemistry 2006, 45:12090-12099.
    • (2006) Biochemistry , vol.45 , pp. 12090-12099
    • Connaghan-Jones, K.D.1    Heneghan, A.F.2    Miura, M.T.3    Bain, D.L.4
  • 23
    • 33847792712 scopus 로고    scopus 로고
    • Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function
    • Connaghan-Jones K.D., Heneghan A.F., Miura M.T., Bain D.L. Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function. Proc. Natl .Acad. Sci. USA 2007, 104:2187-2192.
    • (2007) Proc. Natl .Acad. Sci. USA , vol.104 , pp. 2187-2192
    • Connaghan-Jones, K.D.1    Heneghan, A.F.2    Miura, M.T.3    Bain, D.L.4
  • 24
    • 40849140749 scopus 로고    scopus 로고
    • Thermodynamic dissection of progesterone receptor interactions at the mouse mammary tumor virus promoter: monomer binding and strong cooperativity dominate the assembly reaction
    • Connaghan-Jones K.D., Heneghan A.F., Miura M.T., Bain D.L. Thermodynamic dissection of progesterone receptor interactions at the mouse mammary tumor virus promoter: monomer binding and strong cooperativity dominate the assembly reaction. J. Mol. Biol. 2008, 377:1144-1160.
    • (2008) J. Mol. Biol. , vol.377 , pp. 1144-1160
    • Connaghan-Jones, K.D.1    Heneghan, A.F.2    Miura, M.T.3    Bain, D.L.4
  • 25
    • 33744492845 scopus 로고    scopus 로고
    • Activation function 1 of glucocorticoid receptor binds TATA-binding protein in vitro and in vivo
    • Copik A.J., Webb M.S., Miller A.L., Wang Y., Kumar R., Thompson E.B. Activation function 1 of glucocorticoid receptor binds TATA-binding protein in vitro and in vivo. Mol. Endocrinol. 2006, 20:1218-1230.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1218-1230
    • Copik, A.J.1    Webb, M.S.2    Miller, A.L.3    Wang, Y.4    Kumar, R.5    Thompson, E.B.6
  • 26
    • 78049332125 scopus 로고    scopus 로고
    • The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention
    • Daniel A.R., Gaviglio A.L., Czaplicki L.M., Hillard C.J., Housa D., Lange C.A. The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. Mol. Endocrinol. 2010, 24:2126-2138.
    • (2010) Mol. Endocrinol. , vol.24 , pp. 2126-2138
    • Daniel, A.R.1    Gaviglio, A.L.2    Czaplicki, L.M.3    Hillard, C.J.4    Housa, D.5    Lange, C.A.6
  • 27
    • 70149092341 scopus 로고    scopus 로고
    • Protein kinases mediate ligand-independent derepression of sumoylated progesterone receptors in breast cancer cells
    • Daniel A.R., Lange C.A. Protein kinases mediate ligand-independent derepression of sumoylated progesterone receptors in breast cancer cells. Proc. Natl. Acad. Sci. USA 2009, 106:14287-14292.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14287-14292
    • Daniel, A.R.1    Lange, C.A.2
  • 28
    • 33847058518 scopus 로고    scopus 로고
    • Linkage of progestin and epidermal growth factor signaling: phosphorylation of progesterone receptors mediates transcriptional hypersensitivity and increased ligand-independent breast cancer cell growth
    • Daniel A.R., Qiu M., Faivre E.J., Ostrander J.H., Skildum A., Lange C.A. Linkage of progestin and epidermal growth factor signaling: phosphorylation of progesterone receptors mediates transcriptional hypersensitivity and increased ligand-independent breast cancer cell growth. Steroids 2007, 72:188-201.
    • (2007) Steroids , vol.72 , pp. 188-201
    • Daniel, A.R.1    Qiu, M.2    Faivre, E.J.3    Ostrander, J.H.4    Skildum, A.5    Lange, C.A.6
  • 29
    • 8344226092 scopus 로고    scopus 로고
    • High mobility group B proteins facilitate strong estrogen receptor binding to classical and half-site estrogen response elements and relax binding selectivity
    • Das D., Peterson R.C., Scovell W.M. High mobility group B proteins facilitate strong estrogen receptor binding to classical and half-site estrogen response elements and relax binding selectivity. Mol. Endocrinol. 2004, 18:2616-2632.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 2616-2632
    • Das, D.1    Peterson, R.C.2    Scovell, W.M.3
  • 30
    • 0035980151 scopus 로고    scopus 로고
    • The binding interaction of HMG-1 with the TATA-binding protein/TATA complex
    • Das D., Scovell W.M. The binding interaction of HMG-1 with the TATA-binding protein/TATA complex. J. Biol. Chem. 2001, 276:32597-32605.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32597-32605
    • Das, D.1    Scovell, W.M.2
  • 32
    • 0036510607 scopus 로고    scopus 로고
    • HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences
    • Dintilhac A., Bernues J. HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences. J. Biol. Chem. 2002, 277:7021-7028.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7021-7028
    • Dintilhac, A.1    Bernues, J.2
  • 33
    • 3042814763 scopus 로고    scopus 로고
    • Intramolecular interactions between the AF3 domain and the C-terminus of the human progesterone receptor are mediated through two LXXLL motifs
    • Dong X., Challis J.R., Lye S.J. Intramolecular interactions between the AF3 domain and the C-terminus of the human progesterone receptor are mediated through two LXXLL motifs. J. Mol. Endocrinol. 2004, 32:843-857.
    • (2004) J. Mol. Endocrinol. , vol.32 , pp. 843-857
    • Dong, X.1    Challis, J.R.2    Lye, S.J.3
  • 34
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005, 6:197-208.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 35
    • 0038657687 scopus 로고    scopus 로고
    • Progesterone receptor interacting coregulatory proteins and cross talk with cell signaling pathways
    • Edwards D.P., Wardell S.E., Boonyaratanakornkit V. Progesterone receptor interacting coregulatory proteins and cross talk with cell signaling pathways. J. Steroid Biochem. Mol. Biol. 2002, 83:173-186.
    • (2002) J. Steroid Biochem. Mol. Biol. , vol.83 , pp. 173-186
    • Edwards, D.P.1    Wardell, S.E.2    Boonyaratanakornkit, V.3
  • 36
    • 33750316364 scopus 로고    scopus 로고
    • Post-translational modifications of steroid receptors
    • Faus H., Haendler B. Post-translational modifications of steroid receptors. Biomed. Pharmacother. 2006, 60:520-528.
    • (2006) Biomed. Pharmacother. , vol.60 , pp. 520-528
    • Faus, H.1    Haendler, B.2
  • 38
    • 33748258328 scopus 로고    scopus 로고
    • A practical overview of protein disorder prediction methods
    • Ferron F., Longhi S., Canard B., Karlin D. A practical overview of protein disorder prediction methods. Proteins 2006, 65:1-14.
    • (2006) Proteins , vol.65 , pp. 1-14
    • Ferron, F.1    Longhi, S.2    Canard, B.3    Karlin, D.4
  • 40
    • 0034617058 scopus 로고    scopus 로고
    • P300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation
    • Fu M., Wang C., Reutens A.T., Wang J., Angeletti R.H., Siconolfi-Baez L., Ogryzko V., Avantaggiati M.L., Pestell R.G. p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation. J. Biol. Chem. 2000, 275:20853-20860.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20853-20860
    • Fu, M.1    Wang, C.2    Reutens, A.T.3    Wang, J.4    Angeletti, R.H.5    Siconolfi-Baez, L.6    Ogryzko, V.7    Avantaggiati, M.L.8    Pestell, R.G.9
  • 41
    • 73549096417 scopus 로고    scopus 로고
    • Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor
    • Garza A.M., Khan S.H., Kumar R. Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. Mol. Cell. Biol. 2010, 30:220-230.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 220-230
    • Garza, A.M.1    Khan, S.H.2    Kumar, R.3
  • 42
    • 0037418634 scopus 로고    scopus 로고
    • Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition
    • Gearhart M.D., Holmbeck S.M., Evans R.M., Dyson H.J., Wright P.E. Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition. J. Mol. Biol. 2003, 327:819-832.
    • (2003) J. Mol. Biol. , vol.327 , pp. 819-832
    • Gearhart, M.D.1    Holmbeck, S.M.2    Evans, R.M.3    Dyson, H.J.4    Wright, P.E.5
  • 43
    • 0029010368 scopus 로고
    • The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex
    • Gewirth D.T., Sigler P.B. The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex. Nat. Struct. Biol. 1995, 2:386-394.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 386-394
    • Gewirth, D.T.1    Sigler, P.B.2
  • 44
    • 33646066806 scopus 로고    scopus 로고
    • Synergistic functions of SII and p300 in productive activator-dependent transcription of chromatin templates
    • Guermah M., Palhan V.B., Tackett A.J., Chait B.T., Roeder R.G. Synergistic functions of SII and p300 in productive activator-dependent transcription of chromatin templates. Cell 2006, 125:275-286.
    • (2006) Cell , vol.125 , pp. 275-286
    • Guermah, M.1    Palhan, V.B.2    Tackett, A.J.3    Chait, B.T.4    Roeder, R.G.5
  • 45
    • 34249307492 scopus 로고    scopus 로고
    • The hinge region regulates DNA binding, nuclear translocation, and transactivation of the androgen receptor
    • Haelens A., Tanner T., Denayer S., Callewaert L., Claessens F. The hinge region regulates DNA binding, nuclear translocation, and transactivation of the androgen receptor. Cancer Res. 2007, 67:4514-4523.
    • (2007) Cancer Res. , vol.67 , pp. 4514-4523
    • Haelens, A.1    Tanner, T.2    Denayer, S.3    Callewaert, L.4    Claessens, F.5
  • 46
    • 0037263134 scopus 로고    scopus 로고
    • DNA recognition by the androgen receptor: evidence for an alternative DNA-dependent dimerization, and an active role of sequences flanking the response element on transactivation
    • Haelens A., Verrijdt G., Callewaert L., Christiaens V., Schauwaers K., Peeters B., Rombauts W., Claessens F. DNA recognition by the androgen receptor: evidence for an alternative DNA-dependent dimerization, and an active role of sequences flanking the response element on transactivation. Biochem. J. 2003, 369:141-151.
    • (2003) Biochem. J. , vol.369 , pp. 141-151
    • Haelens, A.1    Verrijdt, G.2    Callewaert, L.3    Christiaens, V.4    Schauwaers, K.5    Peeters, B.6    Rombauts, W.7    Claessens, F.8
  • 47
    • 0036185782 scopus 로고    scopus 로고
    • Allosteric regulation of estrogen receptor structure, function, and coactivator recruitment by different estrogen response elements
    • Hall J.M., McDonnell D.P., Korach K.S. Allosteric regulation of estrogen receptor structure, function, and coactivator recruitment by different estrogen response elements. Mol. Endocrinol. 2002, 16:469-486.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 469-486
    • Hall, J.M.1    McDonnell, D.P.2    Korach, K.S.3
  • 49
    • 21844477014 scopus 로고    scopus 로고
    • Self-association energetics of an intact, full-length nuclear receptor: the B-isoform of human progesterone receptor dimerizes in the micromolar range
    • Heneghan A.F., Berton N., Miura M.T., Bain D.L. Self-association energetics of an intact, full-length nuclear receptor: the B-isoform of human progesterone receptor dimerizes in the micromolar range. Biochemistry 2005, 44:9528-9537.
    • (2005) Biochemistry , vol.44 , pp. 9528-9537
    • Heneghan, A.F.1    Berton, N.2    Miura, M.T.3    Bain, D.L.4
  • 50
    • 33644855967 scopus 로고    scopus 로고
    • Cooperative DNA binding by the B-isoform of human progesterone receptor: thermodynamic analysis reveals strongly favorable and unfavorable contributions to assembly
    • Heneghan A.F., Connaghan-Jones K.D., Miura M.T., Bain D.L. Cooperative DNA binding by the B-isoform of human progesterone receptor: thermodynamic analysis reveals strongly favorable and unfavorable contributions to assembly. Biochemistry 2006, 45:3285-3296.
    • (2006) Biochemistry , vol.45 , pp. 3285-3296
    • Heneghan, A.F.1    Connaghan-Jones, K.D.2    Miura, M.T.3    Bain, D.L.4
  • 51
    • 34848844722 scopus 로고    scopus 로고
    • Coactivator assembly at the promoter: efficient recruitment of SRC2 is coupled to cooperative DNA binding by the progesterone receptor
    • Heneghan A.F., Connaghan-Jones K.D., Miura M.T., Bain D.L. Coactivator assembly at the promoter: efficient recruitment of SRC2 is coupled to cooperative DNA binding by the progesterone receptor. Biochemistry 2007, 46:11023-11032.
    • (2007) Biochemistry , vol.46 , pp. 11023-11032
    • Heneghan, A.F.1    Connaghan-Jones, K.D.2    Miura, M.T.3    Bain, D.L.4
  • 52
    • 69949146216 scopus 로고    scopus 로고
    • A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain
    • Hill K.K., Roemer S.C., Jones D.N., Churchill M.E., Edwards D.P. A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain. J. Biol. Chem. 2009, 284:24415-24424.
    • (2009) J. Biol. Chem. , vol.284 , pp. 24415-24424
    • Hill, K.K.1    Roemer, S.C.2    Jones, D.N.3    Churchill, M.E.4    Edwards, D.P.5
  • 53
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser V.J., Thompson E.B. Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc. Natl. Acad. Sci. USA 2007, 104:8311-8315.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 54
    • 33846804545 scopus 로고    scopus 로고
    • HMG chromosomal proteins in development and disease
    • Hock R., Furusawa T., Ueda T., Bustin M. HMG chromosomal proteins in development and disease. Trends Cell Biol. 2007, 17:72-79.
    • (2007) Trends Cell Biol. , vol.17 , pp. 72-79
    • Hock, R.1    Furusawa, T.2    Ueda, T.3    Bustin, M.4
  • 55
    • 24344451969 scopus 로고    scopus 로고
    • Modulation of the expression and transactivation of androgen receptor by the basic helix-loop-helix transcription factor Pod-1 through recruitment of histone deacetylase 1
    • Hong C.Y., Gong E.Y., Kim K., Suh J.H., Ko H.M., Lee H.J., Choi H.S., Lee K. Modulation of the expression and transactivation of androgen receptor by the basic helix-loop-helix transcription factor Pod-1 through recruitment of histone deacetylase 1. Mol. Endocrinol. 2005, 19:2245-2257.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 2245-2257
    • Hong, C.Y.1    Gong, E.Y.2    Kim, K.3    Suh, J.H.4    Ko, H.M.5    Lee, H.J.6    Choi, H.S.7    Lee, K.8
  • 57
    • 0033534163 scopus 로고    scopus 로고
    • Characterization of unique DNA-binding and transcriptional-activation functions in the carboxyl-terminal extension of the zinc finger region in the human vitamin D receptor
    • Hsieh J.C., Whitfield G.K., Oza A.K., Dang H.T., Price J.N., Galligan M.A., Jurutka P.W., Thompson P.D., Haussler C.A., Haussler M.R. Characterization of unique DNA-binding and transcriptional-activation functions in the carboxyl-terminal extension of the zinc finger region in the human vitamin D receptor. Biochemistry 1999, 38:16347-16358.
    • (1999) Biochemistry , vol.38 , pp. 16347-16358
    • Hsieh, J.C.1    Whitfield, G.K.2    Oza, A.K.3    Dang, H.T.4    Price, J.N.5    Galligan, M.A.6    Jurutka, P.W.7    Thompson, P.D.8    Haussler, C.A.9    Haussler, M.R.10
  • 59
    • 0346656463 scopus 로고    scopus 로고
    • Androgen receptor corepressor-19kDa (ARR19), a leucine-rich protein that represses the transcriptional activity of androgen receptor through recruitment of histone deacetylase
    • Jeong B.C., Hong C.Y., Chattopadhyay S., Park J.H., Gong E.Y., Kim H.J., Chun S.Y., Lee K. Androgen receptor corepressor-19kDa (ARR19), a leucine-rich protein that represses the transcriptional activity of androgen receptor through recruitment of histone deacetylase. Mol. Endocrinol. 2004, 18:13-25.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 13-25
    • Jeong, B.C.1    Hong, C.Y.2    Chattopadhyay, S.3    Park, J.H.4    Gong, E.Y.5    Kim, H.J.6    Chun, S.Y.7    Lee, K.8
  • 61
    • 0036272787 scopus 로고    scopus 로고
    • JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells
    • Jin C., Li H., Murata T., Sun K., Horikoshi M., Chiu R., Yokoyama K.K. JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells. Mol. Cell. Biol. 2002, 22:4815-4826.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4815-4826
    • Jin, C.1    Li, H.2    Murata, T.3    Sun, K.4    Horikoshi, M.5    Chiu, R.6    Yokoyama, K.K.7
  • 62
    • 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. 1990, 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
  • 63
    • 0035369335 scopus 로고    scopus 로고
    • Nuclear-receptor interactions on DNA-response elements
    • Khorasanizadeh S., Rastinejad F. Nuclear-receptor interactions on DNA-response elements. Trends Biochem. Sci. 2001, 26:384-390.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 384-390
    • Khorasanizadeh, S.1    Rastinejad, F.2
  • 64
    • 33745658056 scopus 로고    scopus 로고
    • Acetylation of estrogen receptor alpha by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor
    • Kim M.Y., Woo E.M., Chong Y.T., Homenko D.R., Kraus W.L. Acetylation of estrogen receptor alpha by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor. Mol. Endocrinol. 2006, 20:1479-1493.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1479-1493
    • Kim, M.Y.1    Woo, E.M.2    Chong, Y.T.3    Homenko, D.R.4    Kraus, W.L.5
  • 65
    • 0036132913 scopus 로고    scopus 로고
    • Identification and characterization of a tissue-specific coactivator, GT198, that interacts with the DNA-binding domains of nuclear receptors
    • Ko L., Cardona G.R., Henrion-Caude A., Chin W.W. Identification and characterization of a tissue-specific coactivator, GT198, that interacts with the DNA-binding domains of nuclear receptors. Mol. Cell. Biol. 2002, 22:357-369.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 357-369
    • Ko, L.1    Cardona, G.R.2    Henrion-Caude, A.3    Chin, W.W.4
  • 67
    • 1542743970 scopus 로고    scopus 로고
    • Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF
    • Kumar R., Betney R., Li J., Thompson E.B., McEwan I.J. Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. Biochemistry 2004, 43:3008-3013.
    • (2004) Biochemistry , vol.43 , pp. 3008-3013
    • Kumar, R.1    Betney, R.2    Li, J.3    Thompson, E.B.4    McEwan, I.J.5
  • 68
    • 0037245786 scopus 로고    scopus 로고
    • Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions
    • Kumar R., Thompson E.B. Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions. Mol. Endocrinol. 2003, 17:1-10.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1-10
    • Kumar, R.1    Thompson, E.B.2
  • 69
    • 9344227341 scopus 로고    scopus 로고
    • TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain
    • Kumar R., Volk D.E., Li J., Lee J.C., Gorenstein D.G., Thompson E.B. TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain. Proc. Natl. Acad. Sci. USA 2004, 101:16425-16430.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16425-16430
    • Kumar, R.1    Volk, D.E.2    Li, J.3    Lee, J.C.4    Gorenstein, D.G.5    Thompson, E.B.6
  • 70
    • 34248649845 scopus 로고    scopus 로고
    • The human androgen receptor AF1 transactivation domain: interactions with transcription factor IIF and molten-globule-like structural characteristics
    • Lavery D.N., McEwan I.J. The human androgen receptor AF1 transactivation domain: interactions with transcription factor IIF and molten-globule-like structural characteristics. Biochem. Soc. Trans. 2006, 34:1054-1057.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 1054-1057
    • Lavery, D.N.1    McEwan, I.J.2
  • 72
    • 0027222793 scopus 로고
    • Structure of the retinoid X receptor alpha DNA binding domain: a helix required for homodimeric DNA binding
    • Lee M.S., Kliewer S.A., Provencal J., Wright P.E., Evans R.M. Structure of the retinoid X receptor alpha DNA binding domain: a helix required for homodimeric DNA binding. Science 1993, 260:1117-1121.
    • (1993) Science , vol.260 , pp. 1117-1121
    • Lee, M.S.1    Kliewer, S.A.2    Provencal, J.3    Wright, P.E.4    Evans, R.M.5
  • 73
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin J.A., Yamamoto K.R. Allosteric effects of DNA on transcriptional regulators. Nature 1998, 392:885-888.
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 74
    • 28144433667 scopus 로고    scopus 로고
    • Recruitment of histone deacetylase 4 to the N-terminal region of estrogen receptor alpha
    • Leong H., Sloan J.R., Nash P.D., Greene G.L. Recruitment of histone deacetylase 4 to the N-terminal region of estrogen receptor alpha. Mol. Endocrinol. 2005, 19:2930-2942.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 2930-2942
    • Leong, H.1    Sloan, J.R.2    Nash, P.D.3    Greene, G.L.4
  • 75
    • 0141891343 scopus 로고    scopus 로고
    • Unfolding the action of progesterone receptors
    • Li X., O'Malley B.W. Unfolding the action of progesterone receptors. J. Biol. Chem. 2003, 278:39261-39264.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39261-39264
    • Li, X.1    O'Malley, B.W.2
  • 79
    • 34548252291 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: judges, juries, and executioners of cellular regulation
    • Lonard D.M., O'Malley B.W. Nuclear receptor coregulators: judges, juries, and executioners of cellular regulation. Mol. Cell 2007, 27:691-700.
    • (2007) Mol. Cell , vol.27 , pp. 691-700
    • Lonard, D.M.1    O'Malley, B.W.2
  • 80
    • 0025780755 scopus 로고
    • Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    • Luisi B.F., Xu W.X., Otwinowski Z., Freedman L.P., Yamamoto K.R., Sigler P.B. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature 1991, 352:497-505.
    • (1991) Nature , vol.352 , pp. 497-505
    • Luisi, B.F.1    Xu, W.X.2    Otwinowski, Z.3    Freedman, L.P.4    Yamamoto, K.R.5    Sigler, P.B.6
  • 83
    • 33750968212 scopus 로고    scopus 로고
    • PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus
    • Man J.H., Li H.Y., Zhang P.J., Zhou T., He K., Pan X., Liang B., Li A.L., Zhao J., Gong W.L., et al. PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus. Nucleic Acids Res. 2006, 34:5552-5566.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 5552-5566
    • Man, J.H.1    Li, H.Y.2    Zhang, P.J.3    Zhou, T.4    He, K.5    Pan, X.6    Liang, B.7    Li, A.L.8    Zhao, J.9    Gong, W.L.10
  • 84
  • 85
    • 34249667205 scopus 로고    scopus 로고
    • Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors
    • McEwan I.J., Lavery D., Fischer K., Watt K. Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors. Nucl. Recept. Signal. 2007, 5:e001.
    • (2007) Nucl. Recept. Signal. , vol.5
    • McEwan, I.J.1    Lavery, D.2    Fischer, K.3    Watt, K.4
  • 86
    • 65249167505 scopus 로고    scopus 로고
    • DNA binding site sequence directs glucocorticoid receptor structure and activity
    • Meijsing S.H., Pufall M.A., So A.Y., Bates D.L., Chen L., Yamamoto K.R. DNA binding site sequence directs glucocorticoid receptor structure and activity. Science 2009, 324:407-410.
    • (2009) Science , vol.324 , pp. 407-410
    • Meijsing, S.H.1    Pufall, M.A.2    So, A.Y.3    Bates, D.L.4    Chen, L.5    Yamamoto, K.R.6
  • 87
    • 2442530463 scopus 로고    scopus 로고
    • The role of the C-terminal extension (CTE) of the estrogen receptor alpha and beta DNA binding domain in DNA binding and interaction with HMGB
    • Melvin V.S., Harrell C., Adelman J.S., Kraus W.L., Churchill M., Edwards D.P. The role of the C-terminal extension (CTE) of the estrogen receptor alpha and beta DNA binding domain in DNA binding and interaction with HMGB. J. Biol. Chem. 2004, 279:14763-14771.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14763-14771
    • Melvin, V.S.1    Harrell, C.2    Adelman, J.S.3    Kraus, W.L.4    Churchill, M.5    Edwards, D.P.6
  • 88
    • 0037067664 scopus 로고    scopus 로고
    • The C-terminal extension (CTE) of the nuclear hormone receptor DNA binding domain determines interactions and functional response to the HMGB-1/-2 co-regulatory proteins
    • Melvin V.S., Roemer S.C., Churchill M.E., Edwards D.P. The C-terminal extension (CTE) of the nuclear hormone receptor DNA binding domain determines interactions and functional response to the HMGB-1/-2 co-regulatory proteins. J. Biol. Chem. 2002, 277:25115-25124.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25115-25124
    • Melvin, V.S.1    Roemer, S.C.2    Churchill, M.E.3    Edwards, D.P.4
  • 89
    • 0034740164 scopus 로고    scopus 로고
    • Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains
    • Metivier R., Penot G., Flouriot G., Pakdel F. Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains. Mol. Endocrinol. 2001, 15:1953-1970.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1953-1970
    • Metivier, R.1    Penot, G.2    Flouriot, G.3    Pakdel, F.4
  • 90
    • 0025053671 scopus 로고
    • Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor
    • Meyer M.E., Pornon A., Ji J.W., Bocquel M.T., Chambon P., Gronemeyer H. Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor. EMBO J. 1990, 9:3923-3932.
    • (1990) EMBO J. , vol.9 , pp. 3923-3932
    • Meyer, M.E.1    Pornon, A.2    Ji, J.W.3    Bocquel, M.T.4    Chambon, P.5    Gronemeyer, H.6
  • 91
    • 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. A limiting factor mediates the differential activation of promoters by the human progesterone receptor isoforms. J. Biol. Chem. 1992, 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
  • 92
    • 0033328138 scopus 로고    scopus 로고
    • Colocalization of progesterone receptors A and B by dual immunofluorescent histochemistry in human endometrium during the menstrual cycle
    • Mote P.A., Balleine R.L., McGowan E.M., Clarke C.L. Colocalization of progesterone receptors A and B by dual immunofluorescent histochemistry in human endometrium during the menstrual cycle. J. Clin. Endocrinol. Metab. 1999, 84:2963-2971.
    • (1999) J. Clin. Endocrinol. Metab. , vol.84 , pp. 2963-2971
    • Mote, P.A.1    Balleine, R.L.2    McGowan, E.M.3    Clarke, C.L.4
  • 93
    • 0036112855 scopus 로고    scopus 로고
    • Loss of co-ordinate expression of progesterone receptors A and B is an early event in breast carcinogenesis
    • Mote P.A., Bartow S., Tran N., Clarke C.L. Loss of co-ordinate expression of progesterone receptors A and B is an early event in breast carcinogenesis. Breast Cancer Res. Treat. 2002, 72:163-172.
    • (2002) Breast Cancer Res. Treat. , vol.72 , pp. 163-172
    • Mote, P.A.1    Bartow, S.2    Tran, N.3    Clarke, C.L.4
  • 94
    • 82655176365 scopus 로고    scopus 로고
    • Protein induced folding of the intrinsically disordered amino-terminal domain of progesterone receptor controls transcriptional activity of AF1. In Annual Endocrine Society Meetings (Washington, DC)
    • Moure, M.C., Callaway, C., Kumar, R., Edwards, D.P., 2009. Protein induced folding of the intrinsically disordered amino-terminal domain of progesterone receptor controls transcriptional activity of AF1. In Annual Endocrine Society Meetings (Washington, DC).
    • (2009)
    • Moure, M.C.1    Callaway, C.2    Kumar, R.3    Edwards, D.P.4
  • 95
    • 16244382046 scopus 로고    scopus 로고
    • Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity
    • Narayanan R., Edwards D.P., Weigel N.L. Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity. Mol. Cell. Biol. 2005, 25:2885-2898.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2885-2898
    • Narayanan, R.1    Edwards, D.P.2    Weigel, N.L.3
  • 97
    • 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 AF2 domains of steroid receptors
    • Onate S.A., Boonyaratanakornkit V., Spencer T.E., Tsai S.Y., Tsai M.J., Edwards D.P., O'Malley B.W. 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. 1998, 273:12101-12108.
    • (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
  • 98
    • 0030995770 scopus 로고    scopus 로고
    • DNA bending is induced by binding of the glucocorticoid receptor DNA binding domain and progesterone receptors to their response element
    • Petz L.N., Nardulli A.M., Kim J., Horwitz K.B., Freedman L.P., Shapiro D.J. DNA bending is induced by binding of the glucocorticoid receptor DNA binding domain and progesterone receptors to their response element. J. Steroid Biochem. Mol. Biol. 1997, 60:31-41.
    • (1997) J. Steroid Biochem. Mol. Biol. , vol.60 , pp. 31-41
    • Petz, L.N.1    Nardulli, A.M.2    Kim, J.3    Horwitz, K.B.4    Freedman, L.P.5    Shapiro, D.J.6
  • 99
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka H., Karvonen U., Janne O.A., Palvimo J.J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. USA 2000, 97:14145-14150.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 100
    • 0033829607 scopus 로고    scopus 로고
    • The RING finger protein SNURF modulates nuclear trafficking of the androgen receptor
    • Poukka H., Karvonen U., Yoshikawa N., Tanaka H., Palvimo J.J., Janne O.A. The RING finger protein SNURF modulates nuclear trafficking of the androgen receptor. J. Cell Sci. 2000, 113(Pt 17):2991-3001.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 17 , pp. 2991-3001
    • Poukka, H.1    Karvonen, U.2    Yoshikawa, N.3    Tanaka, H.4    Palvimo, J.J.5    Janne, O.A.6
  • 101
    • 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., Edwards D.P. Progesterone receptor-induced bending of its target DNA: distinct effects of the A and B receptor forms. Mol. Endocrinol. 1996, 10:393-407.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 393-407
    • Prendergast, P.1    Pan, Z.2    Edwards, D.P.3
  • 103
    • 0032404179 scopus 로고    scopus 로고
    • The role of the T-box for the function of the vitamin D receptor on different types of response elements
    • Quack M., Szafranski K., Rouvinen J., Carlberg C. The role of the T-box for the function of the vitamin D receptor on different types of response elements. Nucleic Acids Res. 1998, 26:5372-5378.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5372-5378
    • Quack, M.1    Szafranski, K.2    Rouvinen, J.3    Carlberg, C.4
  • 104
    • 67749148919 scopus 로고    scopus 로고
    • The X-ray structure of RU486 bound to the progesterone receptor in a destabilized agonistic conformation
    • Raaijmakers H.C., Versteegh J.E., Uitdehaag J.C. The X-ray structure of RU486 bound to the progesterone receptor in a destabilized agonistic conformation. J. Biol. Chem. 2009, 284:19572-19579.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19572-19579
    • Raaijmakers, H.C.1    Versteegh, J.E.2    Uitdehaag, J.C.3
  • 105
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • Rastinejad F., Perlmann T., Evans R.M., Sigler P.B. Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature 1995, 375:203-211.
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 106
    • 0037205522 scopus 로고    scopus 로고
    • Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions
    • Reid J., Kelly S.M., Watt K., Price N.C., McEwan I.J. Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. J. Biol. Chem. 2002, 277:20079-20086.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20079-20086
    • Reid, J.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    McEwan, I.J.5
  • 107
    • 0037085303 scopus 로고    scopus 로고
    • Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells
    • Richer J.K., Jacobsen B.M., Manning N.G., Abel M.G., Wolf D.M., Horwitz K.B. Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells. J. Biol. Chem. 2002, 277:5209-5218.
    • (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
  • 108
    • 46349086564 scopus 로고    scopus 로고
    • Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding
    • Roemer S.C., Adelman J., Churchill M.E., Edwards D.P. Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding. Nucleic Acids Res. 2008, 36:3655-3666.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3655-3666
    • Roemer, S.C.1    Adelman, J.2    Churchill, M.E.3    Edwards, D.P.4
  • 109
    • 33751551165 scopus 로고    scopus 로고
    • Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements
    • Roemer S.C., Donham D.C., Sherman L., Pon V.H., Edwards D.P., Churchill M.E. Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements. Mol. Endocrinol. 2006, 20:3042-3052.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 3042-3052
    • Roemer, S.C.1    Donham, D.C.2    Sherman, L.3    Pon, V.H.4    Edwards, D.P.5    Churchill, M.E.6
  • 110
    • 26844491712 scopus 로고    scopus 로고
    • Medroxyprogesterone acetate induces cell proliferation through up-regulation of cyclin D1 expression via phosphatidylinositol 3-kinase/Akt/nuclear factor-kappaB cascade in human breast cancer cells
    • Saitoh M., Ohmichi M., Takahashi K., Kawagoe J., Ohta T., Doshida M., Takahashi T., Igarashi H., Mori-Abe A., Du B., et al. Medroxyprogesterone acetate induces cell proliferation through up-regulation of cyclin D1 expression via phosphatidylinositol 3-kinase/Akt/nuclear factor-kappaB cascade in human breast cancer cells. Endocrinology 2005, 146:4917-4925.
    • (2005) Endocrinology , vol.146 , pp. 4917-4925
    • Saitoh, M.1    Ohmichi, M.2    Takahashi, K.3    Kawagoe, J.4    Ohta, T.5    Doshida, M.6    Takahashi, T.7    Igarashi, H.8    Mori-Abe, A.9    Du, B.10
  • 111
    • 56649089874 scopus 로고    scopus 로고
    • Isolation of novel coregulatory protein networks associated with DNA-bound estrogen receptor alpha
    • Schultz-Norton J.R., Ziegler Y.S., Likhite V.S., Yates J.R., Nardulli A.M. Isolation of novel coregulatory protein networks associated with DNA-bound estrogen receptor alpha. BMC Mol. Biol. 2008, 9:97.
    • (2008) BMC Mol. Biol. , vol.9 , pp. 97
    • Schultz-Norton, J.R.1    Ziegler, Y.S.2    Likhite, V.S.3    Yates, J.R.4    Nardulli, A.M.5
  • 112
    • 0037040967 scopus 로고    scopus 로고
    • Differential modulation of DNA conformation by estrogen receptors alpha and beta
    • Schultz J.R., Loven M.A., Melvin V.M., Edwards D.P., Nardulli A.M. Differential modulation of DNA conformation by estrogen receptors alpha and beta. J. Biol. Chem. 2002, 277:8702-8707.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8702-8707
    • Schultz, J.R.1    Loven, M.A.2    Melvin, V.M.3    Edwards, D.P.4    Nardulli, A.M.5
  • 113
    • 0030789691 scopus 로고    scopus 로고
    • NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region is unstructured in the free form of the protein
    • Sem D.S., Casimiro D.R., Kliewer S.A., Provencal J., Evans R.M., Wright P.E. NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region is unstructured in the free form of the protein. J. Biol. Chem. 1997, 272:18038-18043.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18038-18043
    • Sem, D.S.1    Casimiro, D.R.2    Kliewer, S.A.3    Provencal, J.4    Evans, R.M.5    Wright, P.E.6
  • 114
    • 0036566396 scopus 로고    scopus 로고
    • Structural basis of VDR-DNA interactions on direct repeat response elements
    • Shaffer P.L., Gewirth D.T. Structural basis of VDR-DNA interactions on direct repeat response elements. EMBO J. 2002, 21:2242-2252.
    • (2002) EMBO J. , vol.21 , pp. 2242-2252
    • Shaffer, P.L.1    Gewirth, D.T.2
  • 116
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., Greene G.L. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 1998, 95:927-937.
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6    Greene, G.L.7
  • 117
    • 13544276888 scopus 로고    scopus 로고
    • Progesterone receptors induce cell cycle progression via activation of mitogen-activated protein kinases
    • Skildum A., Faivre E., Lange C.A. Progesterone receptors induce cell cycle progression via activation of mitogen-activated protein kinases. Mol. Endocrinol. 2005, 19:327-339.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 327-339
    • Skildum, A.1    Faivre, E.2    Lange, C.A.3
  • 120
    • 0033305373 scopus 로고    scopus 로고
    • Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo
    • Tetel M.J., Giangrande P.H., Leonhardt S.A., McDonnell D.P., Edwards D.P. Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo. Mol. Endocrinol. 1999, 13:910-924.
    • (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
  • 121
    • 33751538254 scopus 로고    scopus 로고
    • Progesterone receptors (PR)-B and -A regulate transcription by different mechanisms: AF-3 exerts regulatory control over coactivator binding to PR-B
    • Tung L., Abdel-Hafiz H., Shen T., Harvell D.M., Nitao L.K., Richer J.K., Sartorius C.A., Takimoto G.S., Horwitz K.B. Progesterone receptors (PR)-B and -A regulate transcription by different mechanisms: AF-3 exerts regulatory control over coactivator binding to PR-B. Mol. Endocrinol. 2006, 20:2656-2670.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 2656-2670
    • Tung, L.1    Abdel-Hafiz, H.2    Shen, T.3    Harvell, D.M.4    Nitao, L.K.5    Richer, J.K.6    Sartorius, C.A.7    Takimoto, G.S.8    Horwitz, K.B.9
  • 122
    • 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., Horwitz K.B. Antagonist-occupied human progesterone B-receptors activate transcription without binding to progesterone response elements and are dominantly inhibited by A-receptors. Mol. Endocrinol. 1993, 7:1256-1265.
    • (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
  • 123
    • 0035955734 scopus 로고    scopus 로고
    • Mapping the unique activation function 3 in the progesterone B-receptor upstream segment. Two LXXLL motifs and a tryptophan residue are required for activity
    • Tung L., Shen T., Abel M.G., Powell R.L., Takimoto G.S., Sartorius C.A., Horwitz K.B. Mapping the unique activation function 3 in the progesterone B-receptor upstream segment. Two LXXLL motifs and a tryptophan residue are required for activity. J. Biol. Chem. 2001, 276:39843-39851.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39843-39851
    • Tung, L.1    Shen, T.2    Abel, M.G.3    Powell, R.L.4    Takimoto, G.S.5    Sartorius, C.A.6    Horwitz, K.B.7
  • 124
    • 0024337858 scopus 로고
    • Determinants of target gene specificity for steroid/thyroid hormone receptors
    • Umesono K., Evans R.M. Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell 1989, 57:1139-1146.
    • (1989) Cell , vol.57 , pp. 1139-1146
    • Umesono, K.1    Evans, R.M.2
  • 125
    • 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 G.F., Schrader W.T., Tsai M.J., McDonnell D.P., O'Malley B.W. The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor. Cell 1992, 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
  • 126
    • 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., McDonnell D.P. Human progesterone receptor A form is a cell- and promoter-specific repressor of human progesterone receptor B function. Mol. Endocrinol. 1993, 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
  • 127
    • 0036177576 scopus 로고    scopus 로고
    • Comparative analysis of the influence of the high-mobility group box 1 protein on DNA binding and transcriptional activation by the androgen, glucocorticoid, progesterone and mineralocorticoid receptors
    • Verrijdt G., Haelens A., Schoenmakers E., Rombauts W., Claessens F. Comparative analysis of the influence of the high-mobility group box 1 protein on DNA binding and transcriptional activation by the androgen, glucocorticoid, progesterone and mineralocorticoid receptors. Biochem. J. 2002, 361:97-103.
    • (2002) Biochem. J. , vol.361 , pp. 97-103
    • Verrijdt, G.1    Haelens, A.2    Schoenmakers, E.3    Rombauts, W.4    Claessens, F.5
  • 128
    • 73349085238 scopus 로고    scopus 로고
    • Steroid receptor phosphorylation: assigning function to site-specific phosphorylation
    • Ward R.D., Weigel N.L. Steroid receptor phosphorylation: assigning function to site-specific phosphorylation. Biofactors 2009, 35:528-536.
    • (2009) Biofactors , vol.35 , pp. 528-536
    • Ward, R.D.1    Weigel, N.L.2
  • 130
    • 26444526919 scopus 로고    scopus 로고
    • Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism
    • Wardell S.E., Kwok S.C., Sherman L., Hodges R.S., Edwards D.P. Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism. Mol. Cell. Biol. 2005, 25:8792-8808.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8792-8808
    • Wardell, S.E.1    Kwok, S.C.2    Sherman, L.3    Hodges, R.S.4    Edwards, D.P.5
  • 131
    • 75149130096 scopus 로고    scopus 로고
    • Partial agonist activity of the progesterone receptor antagonist RU486 mediated by an amino-terminal domain coactivator and phosphorylation of serine400
    • Wardell S.E., Narayanan R., Weigel N.L., Edwards D.P. Partial agonist activity of the progesterone receptor antagonist RU486 mediated by an amino-terminal domain coactivator and phosphorylation of serine400. Mol. Endocrinol. 2010, 24:335-345.
    • (2010) Mol. Endocrinol. , vol.24 , pp. 335-345
    • Wardell, S.E.1    Narayanan, R.2    Weigel, N.L.3    Edwards, D.P.4
  • 132
    • 0035824562 scopus 로고    scopus 로고
    • The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties
    • Warnmark A., Wikstrom A., Wright A.P., Gustafsson J.A., Hard T. The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. J. Biol. Chem. 2001, 276:45939-45944.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45939-45944
    • Warnmark, A.1    Wikstrom, A.2    Wright, A.P.3    Gustafsson, J.A.4    Hard, T.5
  • 134
    • 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 N.L., Beck C.A., Estes P.A., Prendergast P., Altmann M., Christensen K., Edwards D.P. Ligands induce conformational changes in the carboxyl-terminus of progesterone receptors which are detected by a site-directed antipeptide monoclonal antibody. Mol. Endocrinol. 1992, 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
  • 135
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • Williams S.P., Sigler P.B. Atomic structure of progesterone complexed with its receptor. Nature 1998, 393:392-396.
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 136
    • 0034969440 scopus 로고    scopus 로고
    • Allosteric modulation of estrogen receptor conformation by different estrogen response elements
    • Wood J.R., Likhite V.S., Loven M.A., Nardulli A.M. Allosteric modulation of estrogen receptor conformation by different estrogen response elements. Mol. Endocrinol. 2001, 15:1114-1126.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1114-1126
    • Wood, J.R.1    Likhite, V.S.2    Loven, M.A.3    Nardulli, A.M.4
  • 137
    • 0029970860 scopus 로고    scopus 로고
    • The extreme C terminus of progesterone receptor contains a transcriptional repressor domain that functions through a putative corepressor
    • Xu J., Nawaz Z., Tsai S.Y., Tsai M.J., O'Malley B.W. The extreme C terminus of progesterone receptor contains a transcriptional repressor domain that functions through a putative corepressor. Proc. Natl. Acad. Sci. USA 1996, 93:12195-12199.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12195-12199
    • Xu, J.1    Nawaz, Z.2    Tsai, S.Y.3    Tsai, M.J.4    O'Malley, B.W.5
  • 138
    • 27144480681 scopus 로고    scopus 로고
    • Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1)
    • Yi P., Wu R.C., Sandquist J., Wong J., Tsai S.Y., Tsai M.J., Means A.R., O'Malley B.W. Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1). Mol. Cell. Biol. 2005, 25:9687-9699.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9687-9699
    • Yi, P.1    Wu, R.C.2    Sandquist, J.3    Wong, J.4    Tsai, S.Y.5    Tsai, M.J.6    Means, A.R.7    O'Malley, B.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.