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Volumn 9, Issue 9, 1998, Pages 2527-2543

Activation of androgen receptor function by a novel nuclear protein kinase

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN RECEPTOR; GENE PRODUCT; NUCLEAR PROTEIN; PROTEIN SERINE THREONINE KINASE; RECEPTOR PROTEIN; ZINC FINGER PROTEIN;

EID: 0031717887     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.9.2527     Document Type: Article
Times cited : (100)

References (91)
  • 1
    • 0027484532 scopus 로고
    • A single-base substitution in exon 6 of the androgen receptor gene causing complete androgen insensitivity: The mutated receptor fails to transactivate but binds to DNA in vitro
    • Adeyemo, O., Kallio, P.J., Palvimo, J.J., Kontula, K., and Jänne, O.A. (1993). A single-base substitution in exon 6 of the androgen receptor gene causing complete androgen insensitivity: the mutated receptor fails to transactivate but binds to DNA in vitro. Hum. Mol. Genet. 2, 1809-1812.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1809-1812
    • Adeyemo, O.1    Kallio, P.J.2    Palvimo, J.J.3    Kontula, K.4    Jänne, O.A.5
  • 2
    • 0027340548 scopus 로고
    • Modulation by vitamin B6 of glucocorticoid receptor-mediated gene expression requires transcription factors in addition to the glucocorticoid receptor
    • Allgood, V.E., Oakley, R.H., and Cidlowski, J.A. (1993). Modulation by vitamin B6 of glucocorticoid receptor-mediated gene expression requires transcription factors in addition to the glucocorticoid receptor. J. Biol. Chem. 268, 20870-20876.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20870-20876
    • Allgood, V.E.1    Oakley, R.H.2    Cidlowski, J.A.3
  • 5
    • 0031036099 scopus 로고    scopus 로고
    • Estradiol-binding mechanism and binding capacity of the human receptor is regulated by tyrosine phosphorylation
    • Arnold, S.F., Melamed, M., Vorojeikina, D.P., Notides, A.C., and Sasson, S. (1997). Estradiol-binding mechanism and binding capacity of the human receptor is regulated by tyrosine phosphorylation. Mol. Endocrinol. 11, 48-53.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 48-53
    • Arnold, S.F.1    Melamed, M.2    Vorojeikina, D.P.3    Notides, A.C.4    Sasson, S.5
  • 6
    • 0019023345 scopus 로고
    • Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA
    • Auffray, C., and Rougeon, F. (1980). Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA. Eur. J. Biochem. 107, 303-314.
    • (1980) Eur. J. Biochem. , vol.107 , pp. 303-314
    • Auffray, C.1    Rougeon, F.2
  • 8
    • 0030936243 scopus 로고    scopus 로고
    • Differential phosphorylation of chicken progesterone receptor in hormone-dependent and ligand-independent activation
    • Bai, W., Rowan, B.G., Allgood, V.E., O'Malley, B.W., and Weigel, N.L. (1997). Differential phosphorylation of chicken progesterone receptor in hormone-dependent and ligand-independent activation. J. Biol. Chem. 272, 10457-10463.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10457-10463
    • Bai, W.1    Rowan, B.G.2    Allgood, V.E.3    O'Malley, B.W.4    Weigel, N.L.5
  • 9
    • 0028291992 scopus 로고
    • Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction
    • Barratt, M.J., Hazzalin, C.A., Cano, E., and Mahadevan, L.C. (1994). Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction. Proc. Natl. Acad. Sci. USA 91, 4781-4785.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4781-4785
    • Barratt, M.J.1    Hazzalin, C.A.2    Cano, E.3    Mahadevan, L.C.4
  • 11
    • 0030731040 scopus 로고    scopus 로고
    • Identification and sequence of human PKY, a putative kinase with increased expression in multidrug-resistant cells, with homology to yeast protein kinase Yak1
    • Begley, D.A., Berkenpas, M.B., Sampson, K.E., and Abraham, I. (1997). Identification and sequence of human PKY, a putative kinase with increased expression in multidrug-resistant cells, with homology to yeast protein kinase Yak1. Gene 200, 35-43.
    • (1997) Gene , vol.200 , pp. 35-43
    • Begley, D.A.1    Berkenpas, M.B.2    Sampson, K.E.3    Abraham, I.4
  • 12
    • 0029618368 scopus 로고
    • Steroid hormone receptors: Many actors in search of a plot
    • Beato, M., Herrlich, P., and Schütz, G. (1995). Steroid hormone receptors: many actors in search of a plot. Cell 83, 851-857.
    • (1995) Cell , vol.83 , pp. 851-857
    • Beato, M.1    Herrlich, P.2    Schütz, G.3
  • 13
    • 0030451142 scopus 로고    scopus 로고
    • Interaction of steroid hormone receptors with the transcription initiation complex
    • Beato, M., and Sanchez-Pacheco, A. (1996). Interaction of steroid hormone receptors with the transcription initiation complex. Endocr. Rev. 17, 587-609.
    • (1996) Endocr. Rev. , vol.17 , pp. 587-609
    • Beato, M.1    Sanchez-Pacheco, A.2
  • 14
    • 0026642483 scopus 로고
    • Effects of hormone and cellular modulators of protein phosphorylation on transcriptional activity, DNA binding, and phosphorylation of human progesterone receptors
    • Beck, C.A., Weigel, N.L., and Edwards, D.P. (1992). Effects of hormone and cellular modulators of protein phosphorylation on transcriptional activity, DNA binding, and phosphorylation of human progesterone receptors. Mol. Endocrinol. 6, 607-620.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 607-620
    • Beck, C.A.1    Weigel, N.L.2    Edwards, D.P.3
  • 16
    • 0032539993 scopus 로고    scopus 로고
    • Foskolin-induced dephosphorylation of the androgen receptor impairs ligand binding
    • Blok, L.J., de Ruiter, P.E., and Brinkmann, A.O. (1998). Foskolin-induced dephosphorylation of the androgen receptor impairs ligand binding. Biochemistry 37, 3850-3857.
    • (1998) Biochemistry , vol.37 , pp. 3850-3857
    • Blok, L.J.1    De Ruiter, P.E.2    Brinkmann, A.O.3
  • 17
    • 0002830140 scopus 로고
    • Modulation of steroid receptor signal transduction by heat shock protein
    • ed. R. Morimoto, A. Tissieres, and C. Georgopoulos, Cold Spring Harbor, NY: Cold Spring Harbor Press
    • Bohen, S.P., and Yamamoto, K.R. (1993). Modulation of steroid receptor signal transduction by heat shock protein. In: The Biology of Heat Shock Proteins and Molecular Chaperones, ed. R. Morimoto, A. Tissieres, and C. Georgopoulos, Cold Spring Harbor, NY: Cold Spring Harbor Press, 313-334.
    • (1993) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 313-334
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 18
    • 0029877913 scopus 로고    scopus 로고
    • Activation of the unliganded estrogen receptor involves the MAP kinase pathway and direct phosphorylation
    • Bunone, G., Briand, P.-A., Miksicek, R.J., and Picard, D. (1996). Activation of the unliganded estrogen receptor involves the MAP kinase pathway and direct phosphorylation. EMBO J. 15, 2174-2183.
    • (1996) EMBO J. , vol.15 , pp. 2174-2183
    • Bunone, G.1    Briand, P.-A.2    Miksicek, R.J.3    Picard, D.4
  • 19
  • 21
    • 0027509872 scopus 로고
    • Synergistic activation of estrogen receptor-mediated transcription by estradiol and protein kinase activators
    • Cho, H., and Katzenellenbogen, B.S. (1993). Synergistic activation of estrogen receptor-mediated transcription by estradiol and protein kinase activators. Mol. Endocrinol. 7, 441-452.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 441-452
    • Cho, H.1    Katzenellenbogen, B.S.2
  • 22
    • 0028113415 scopus 로고
    • Androgen receptor activation in prostatic tumor cell lines by insulin-like growth factor-I, keratinocyte growth factor, and epidermal growth factor
    • Culig, Z., Hobish, A., Cronauer, M., Radmayr, C., Trapman, J., Hittmair, A., Bartsch, G., and Klocker, H. (1994). Androgen receptor activation in prostatic tumor cell lines by insulin-like growth factor-I, keratinocyte growth factor, and epidermal growth factor. Cancer Res. 54, 5474-5478.
    • (1994) Cancer Res. , vol.54 , pp. 5474-5478
    • Culig, Z.1    Hobish, A.2    Cronauer, M.3    Radmayr, C.4    Trapman, J.5    Hittmair, A.6    Bartsch, G.7    Klocker, H.8
  • 23
    • 0025697567 scopus 로고
    • Regulation of progesterone receptor-mediated transcription by phosphorylation
    • Denner, L.A., Weigel, N.L., Maxwell, B.L., Schrader, W.T., and O'Malley, B.W. (1990). Regulation of progesterone receptor-mediated transcription by phosphorylation. Science 250, 1740-1743.
    • (1990) Science , vol.250 , pp. 1740-1743
    • Denner, L.A.1    Weigel, N.L.2    Maxwell, B.L.3    Schrader, W.T.4    O'Malley, B.W.5
  • 24
    • 0001543270 scopus 로고
    • An improvement to the novel rapid assay for chloramphenicol acetyltransferase gene expression
    • Eastman, A. (1987). An improvement to the novel rapid assay for chloramphenicol acetyltransferase gene expression. Biotechniques 5, 73.
    • (1987) Biotechniques , vol.5 , pp. 73
    • Eastman, A.1
  • 25
    • 0029985050 scopus 로고    scopus 로고
    • Hsp90 regulates androgen receptor hormone binding affinity in vivo
    • Fang, Y., Fliss, A.E., Robins, D.M., and Caplan, A.J. (1996). Hsp90 regulates androgen receptor hormone binding affinity in vivo. J. Biol. Chem. 271, 28697-28702.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28697-28702
    • Fang, Y.1    Fliss, A.E.2    Robins, D.M.3    Caplan, A.J.4
  • 26
    • 0030659844 scopus 로고    scopus 로고
    • Differential in vivo regulation of steroid hormone receptor by Cdc37p
    • Fliss, A.E., Fang, Y., Boschelli, F., and Caplan, A.J. (1997). Differential in vivo regulation of steroid hormone receptor by Cdc37p. Mol. Biol. Cell 8, 2501-2509.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2501-2509
    • Fliss, A.E.1    Fang, Y.2    Boschelli, F.3    Caplan, A.J.4
  • 27
    • 0024723687 scopus 로고
    • Loss of Ras activity in Saccharomyces cerevisiae is suppressed by disruptions of a new kinase gene, YAK1, whose product may act downstream of the cAMP-dependent protein kinase
    • Garrett, S., and Broach, J.R. (1989). Loss of Ras activity in Saccharomyces cerevisiae is suppressed by disruptions of a new kinase gene, YAK1, whose product may act downstream of the cAMP-dependent protein kinase. Genes Dev. 3, 1336-1348.
    • (1989) Genes Dev. , vol.3 , pp. 1336-1348
    • Garrett, S.1    Broach, J.R.2
  • 28
    • 0025851170 scopus 로고
    • The Saccharomyces cerevisiae YAK1 gene encodes a protein kinase that is induced by arrest early in the cell cycle
    • Garrett, S., Menold, M.M., and Broach, J.R. (1991). The Saccharomyces cerevisiae YAK1 gene encodes a protein kinase that is induced by arrest early in the cell cycle. Mol. Cell. Biol. 11, 4045-4052.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4045-4052
    • Garrett, S.1    Menold, M.M.2    Broach, J.R.3
  • 29
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W., and Roeder, R.G. (1997). Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 30
    • 0029044001 scopus 로고
    • A 10-amino acid sequence in the N-terminal A/B domain of thyroid hormone receptor a is essential for transcriptional activation and interaction with the general transcription factor TFIIB
    • Hadzig, E., Desai-Yajnik, V., Helmer, E., Guo, S., Wu, S., Koudinova, N., Casanova, J., Raaka, B.M., and Samuels, H.H. (1995). A 10-amino acid sequence in the N-terminal A/B domain of thyroid hormone receptor a is essential for transcriptional activation and interaction with the general transcription factor TFIIB. Mol. Cell. Biol. 15, 4507-4517.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4507-4517
    • Hadzig, E.1    Desai-Yajnik, V.2    Helmer, E.3    Guo, S.4    Wu, S.5    Koudinova, N.6    Casanova, J.7    Raaka, B.M.8    Samuels, H.H.9
  • 31
    • 0029020282 scopus 로고
    • The eucaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S.K., and Hunter, T. (1995). The eucaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 32
    • 0026345394 scopus 로고
    • The protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks, S.K., and Quinn, A.M (1991). The protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200, 38-62.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 34
    • 0028897113 scopus 로고
    • Transcriptional regulation by extracellular signals: Mechanisms and specificity
    • Hill, C., and Treisman, R. (1995). Transcriptional regulation by extracellular signals: mechanisms and specificity. Cell 80, 199-211.
    • (1995) Cell , vol.80 , pp. 199-211
    • Hill, C.1    Treisman, R.2
  • 35
    • 0029018708 scopus 로고
    • Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system
    • Hollenberg, S.M., Sternglanz, R., Cheng, P.F., and Weintraub, H. (1995). Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol. Cell. Biol. 15, 3813-3822.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3813-3822
    • Hollenberg, S.M.1    Sternglanz, R.2    Cheng, P.F.3    Weintraub, H.4
  • 36
    • 0029978605 scopus 로고    scopus 로고
    • GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors
    • Hong, H., Kohli, K., Trivedi, A., Johnson, D.L., and Stallcup, M.R. (1996). GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proc. Natl. Acad. Sci. USA 93, 4948-4952.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4948-4952
    • Hong, H.1    Kohli, K.2    Trivedi, A.3    Johnson, D.L.4    Stallcup, M.R.5
  • 38
    • 0026636883 scopus 로고
    • Regulation of transcription by phosphorylation
    • Hunter, T., and Karin, M. (1992). Regulation of transcription by phosphorylation. Cell 70, 375-385.
    • (1992) Cell , vol.70 , pp. 375-385
    • Hunter, T.1    Karin, M.2
  • 39
    • 0030669765 scopus 로고    scopus 로고
    • Interaction between amino- and carboxyl-terminal regions of rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators
    • Ikonen, T., Palvimo, J.J., and Jänne, O.A. (1997). Interaction between amino- and carboxyl-terminal regions of rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators. J. Biol. Chem. 272, 29821-29828.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29821-29828
    • Ikonen, T.1    Palvimo, J.J.2    Jänne, O.A.3
  • 40
    • 0027994209 scopus 로고
    • Stimulation of androgen-regulated transactivation by modulators of protein phosphorylation
    • Ikonen, T., Palvimo, J.J., Kallio, P.J., Reinikainen, P., and Jänne, O.A. (1994). Stimulation of androgen-regulated transactivation by modulators of protein phosphorylation. Endocrinology 135, 1359-1366.
    • (1994) Endocrinology , vol.135 , pp. 1359-1366
    • Ikonen, T.1    Palvimo, J.J.2    Kallio, P.J.3    Reinikainen, P.4    Jänne, O.A.5
  • 41
    • 0026722537 scopus 로고
    • Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II)
    • Ing, N.H., Beekman, J.M., Tsai, S.Y., Tsai, M.-J., and O'Malley, B.W. (1992). Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II). J. Biol. Chem. 267, 17617-17623.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17617-17623
    • Ing, N.H.1    Beekman, J.M.2    Tsai, S.Y.3    Tsai, M.-J.4    O'Malley, B.W.5
  • 42
    • 0028170036 scopus 로고
    • II30 is present in a distinct TFIID complex and is required for transcriptional activation by the estrogen receptor
    • II30 is present in a distinct TFIID complex and is required for transcriptional activation by the estrogen receptor. Cell 79, 107-117.
    • (1994) Cell , vol.79 , pp. 107-117
    • Jacq, X.1    Brou, C.2    Lutz, Y.3    Davidson, I.4    Chambon, P.5    Tora, L.6
  • 43
    • 0027483936 scopus 로고
    • Optimization of the resolution of phosphoamino acids by one-dimensional thin-layer electrophoresis
    • Jelinek, T., and Weber, M.J. (1993). Optimization of the resolution of phosphoamino acids by one-dimensional thin-layer electrophoresis. Biotechniques 15, 629-630.
    • (1993) Biotechniques , vol.15 , pp. 629-630
    • Jelinek, T.1    Weber, M.J.2
  • 44
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L.N., Noble, M.E.M., and Owen, D.J. (1996). Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 45
    • 0029098252 scopus 로고
    • Androgen receptor mediated transcriptional regulation in the absence of direct interaction with a specific DNA element
    • Kallio, P.J., Poukka, H., Moilanen, A., Jänne, O.A., and Palvimo, J.J. (1995). Androgen receptor mediated transcriptional regulation in the absence of direct interaction with a specific DNA element. Mol. Endocrinol. 9, 1017-1028.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 1017-1028
    • Kallio, P.J.1    Poukka, H.2    Moilanen, A.3    Jänne, O.A.4    Palvimo, J.J.5
  • 46
    • 0242587820 scopus 로고    scopus 로고
    • A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors
    • Kamei, Y., et al. (1996). A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85, 403-414.
    • (1996) Cell , vol.85 , pp. 403-414
    • Kamei, Y.1
  • 47
    • 0030904753 scopus 로고    scopus 로고
    • Interaction of androgen receptors with androgen response elements in intact cells: Roles of amino- and carboxyl-terminal regions and the ligand
    • Karvonen, U., Kallio, P.J., Jänne, O.A., and Palvimo, J.J. (1997). Interaction of androgen receptors with androgen response elements in intact cells: roles of amino- and carboxyl-terminal regions and the ligand. J. Biol. Chem. 272, 15973-15979.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15973-15979
    • Karvonen, U.1    Kallio, P.J.2    Jänne, O.A.3    Palvimo, J.J.4
  • 48
    • 0028886694 scopus 로고
    • Activation of estrogen receptor through phosphorylation by mitogen-activated protein kinase
    • Kato, S., et al. (1995). Activation of estrogen receptor through phosphorylation by mitogen-activated protein kinase. Science 270, 1491-1494.
    • (1995) Science , vol.270 , pp. 1491-1494
    • Kato, S.1
  • 49
    • 0030022273 scopus 로고    scopus 로고
    • Dyrk, a dual specificity protein kinase with unique structural features whose activity is dependent on tyrosine residues between subdomains VII and VIII
    • Kentrup, H., Becker, W., Heukelbach, J., Wilmes, A., Schürmann, A., Huppertz, C., Kainulainen, H., and Joost, H.-G. (1996). Dyrk, a dual specificity protein kinase with unique structural features whose activity is dependent on tyrosine residues between subdomains VII and VIII. J. Biol. Chem. 271, 3488-3495.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3488-3495
    • Kentrup, H.1    Becker, W.2    Heukelbach, J.3    Wilmes, A.4    Schürmann, A.5    Huppertz, C.6    Kainulainen, H.7    Joost, H.-G.8
  • 50
    • 0030998260 scopus 로고    scopus 로고
    • Mitogen-activated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor
    • Krstic, M.D., Rogatsky, I., Yamamoto, K.R., and Garabedian M.J. (1997). Mitogen-activated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor. Mol. Cell. Biol. 17, 3947-3954.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3947-3954
    • Krstic, M.D.1    Rogatsky, I.2    Yamamoto, K.R.3    Garabedian, M.J.4
  • 51
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 22, 680-685.
    • (1970) Nature , vol.22 , pp. 680-685
    • Laemmli, U.K.1
  • 52
    • 0029030016 scopus 로고
    • The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18
    • Le Douarin, B., Zechel, C., Garnier, J.-M., Lutz, Y., Tora, L., Pierrat, P., Heery, D., Gronemeyer, H., Chambon, P., and Losson, R. (1995). The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. EMBO J. 14, 2020-2033.
    • (1995) EMBO J. , vol.14 , pp. 2020-2033
    • Le Douarin, B.1    Zechel, C.2    Garnier, J.-M.3    Lutz, Y.4    Tora, L.5    Pierrat, P.6    Heery, D.7    Gronemeyer, H.8    Chambon, P.9    Losson, R.10
  • 53
    • 0028890361 scopus 로고
    • Interaction of thyroid hormone receptor with a conserved transcriptional mediator
    • Lee, J.W., Ryan, F., Swaffield, S.A., Johnston, S.A., and Moore, D.D. (1995). Interaction of thyroid hormone receptor with a conserved transcriptional mediator. Nature 374, 91-94.
    • (1995) Nature , vol.374 , pp. 91-94
    • Lee, J.W.1    Ryan, F.2    Swaffield, S.A.3    Johnston, S.A.4    Moore, D.D.5
  • 54
    • 0031555477 scopus 로고    scopus 로고
    • Identification of functional surfaces of the zinc binding domains of intracellular receptors
    • Lichtarge, O., Yamamoto, K.R., and Cohen, F.E. (1997). Identification of functional surfaces of the zinc binding domains of intracellular receptors. J. Mol. Biol. 274, 325-337.
    • (1997) J. Mol. Biol. , vol.274 , pp. 325-337
    • Lichtarge, O.1    Yamamoto, K.R.2    Cohen, F.E.3
  • 55
    • 0030790495 scopus 로고    scopus 로고
    • Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF
    • McEwan, I.J., and Gustafsson, J.-Å. (1997). Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF. Proc. Natl. Acad. Sci. USA 94, 8485-8490.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8485-8490
    • McEwan, I.J.1    Gustafsson, J.-Å.2
  • 56
    • 0031010721 scopus 로고    scopus 로고
    • II135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells
    • II135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells. Genes Dev. 11, 1381-1395.
    • (1997) Genes Dev. , vol.11 , pp. 1381-1395
    • Mengus, G.1    May, M.2    Carré, L.3    Chambon, P.4    Davidson, I.5
  • 57
    • 0031812159 scopus 로고    scopus 로고
    • Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription
    • in press
    • Moilanen, A.-M., Poukka, H., Karvonen, U., Häkli, M., Jänne, O.A., and Palvimo, J.J. (1998). Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription. Mol. Cell. Biol. (in press).
    • (1998) Mol. Cell. Biol.
    • Moilanen, A.-M.1    Poukka, H.2    Karvonen, U.3    Häkli, M.4    Jänne, O.A.5    Palvimo, J.J.6
  • 58
    • 0030763084 scopus 로고    scopus 로고
    • The presence of a transcription activation function in the hormone-binding domain of androgen receptor is revealed by studies in yeast cells
    • Moilanen, A.-M., Rouleau, N., Ikonen, T., Palvimo, J.J., and Jänne, O.A. (1997). The presence of a transcription activation function in the hormone-binding domain of androgen receptor is revealed by studies in yeast cells. FEBS Lett. 412, 355-358.
    • (1997) FEBS Lett. , vol.412 , pp. 355-358
    • Moilanen, A.-M.1    Rouleau, N.2    Ikonen, T.3    Palvimo, J.J.4    Jänne, O.A.5
  • 59
    • 0031565538 scopus 로고    scopus 로고
    • Something new to hang your HAT on
    • Montminy, M. (1997). Something new to hang your HAT on. Nature 387, 654-655.
    • (1997) Nature , vol.387 , pp. 654-655
    • Montminy, M.1
  • 60
    • 0027378364 scopus 로고
    • Modulation of cell signalling pathways can enhance or impair glucocorticoid-induced gene expression without altering the state of receptor phosphorylation
    • Moyer, M.L., Borror, K.C., Bona, B.J., DeFranco, D.B., and Nordeen, S.K. (1993). Modulation of cell signalling pathways can enhance or impair glucocorticoid-induced gene expression without altering the state of receptor phosphorylation. J. Biol. Chem. 268, 22933-22940.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22933-22940
    • Moyer, M.L.1    Borror, K.C.2    Bona, B.J.3    DeFranco, D.B.4    Nordeen, S.K.5
  • 61
    • 0029814415 scopus 로고    scopus 로고
    • Activation of the human androgen receptor through a protein kinase a signalling pathway
    • Nazareth, V.L., and Weigel, N.L. (1996). Activation of the human androgen receptor through a protein kinase A signalling pathway. J. Biol. Chem. 271, 19900-19907.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19900-19907
    • Nazareth, V.L.1    Weigel, N.L.2
  • 62
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Oñate, S.A., Tsai, S.Y., Tsai, M.-J., and O'Malley, B.W. (1995). Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270, 1354-1357.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Oñate, S.A.1    Tsai, S.Y.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 63
    • 0027482359 scopus 로고
    • Dominant negative regulation of trans-activation by the rat androgen receptor: Roles of the N-terminal domain and heterodimer formation
    • Palvimo, J.J., Kallio, P.J., Ikonen, T., Mehto, M., and Jänne, O.A. (1993). Dominant negative regulation of trans-activation by the rat androgen receptor: roles of the N-terminal domain and heterodimer formation. Mol. Endocrinol. 7, 1399-1028.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1399-11028
    • Palvimo, J.J.1    Kallio, P.J.2    Ikonen, T.3    Mehto, M.4    Jänne, O.A.5
  • 64
    • 0024299063 scopus 로고
    • Binding of high-mobility-group proteins HMG 14 and HMG 17 to DNA and histone H1 as influenced by phosphorylation
    • Palvimo, J., and Mäenpää, P.H. (1988). Binding of high-mobility-group proteins HMG 14 and HMG 17 to DNA and histone H1 as influenced by phosphorylation. Biochim. Biophys. Acta 952, 172-180.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 172-180
    • Palvimo, J.1    Mäenpää, P.H.2
  • 65
    • 0029778727 scopus 로고    scopus 로고
    • Characterization of a cell specific modulatory element in the murine ornithine decarboxylase promoter
    • Palvimo, J.J., Partanen, M., and Jänne, O.A. (1996). Characterization of a cell specific modulatory element in the murine ornithine decarboxylase promoter. Biochem. J. 316, 993-998.
    • (1996) Biochem. J. , vol.316 , pp. 993-998
    • Palvimo, J.J.1    Partanen, M.2    Jänne, O.A.3
  • 67
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription
    • Pazin, M.J., and Kadonaga, J.T. (1997). What's up and down with histone deacetylation and transcription. Cell 89, 325-328.
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 68
    • 0030787871 scopus 로고    scopus 로고
    • Nuclear receptors in Sicily: All in the famiglia
    • Perlmann, T., and Evans, R.M. (1997). Nuclear receptors in Sicily: all in the famiglia. Cell 90, 391-397.
    • (1997) Cell , vol.90 , pp. 391-397
    • Perlmann, T.1    Evans, R.M.2
  • 69
    • 0026317212 scopus 로고
    • Dopaminergic and ligand-independent activation of steroid hormone receptors
    • Power, R.F., Mani, S.K., Codina, J., Conneely, O.M., and O'Malley, B.W. (1991). Dopaminergic and ligand-independent activation of steroid hormone receptors. Science 254, 1636-1639.
    • (1991) Science , vol.254 , pp. 1636-1639
    • Power, R.F.1    Mani, S.K.2    Codina, J.3    Conneely, O.M.4    O'Malley, B.W.5
  • 71
    • 0032478254 scopus 로고    scopus 로고
    • Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase
    • Rogatsky, I., Logan, S.K., and Garabedian M.J. (1998). Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase. Proc. Natl. Acad. Sci. USA 95, 2050-2055.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2050-2055
    • Rogatsky, I.1    Logan, S.K.2    Garabedian, M.J.3
  • 72
    • 0023078285 scopus 로고
    • Identification of regulatory elements of cloned genes with functional assays
    • Rosenthal, N. (1987). Identification of regulatory elements of cloned genes with functional assays. Methods Enzymol. 152, 704-720.
    • (1987) Methods Enzymol. , vol.152 , pp. 704-720
    • Rosenthal, N.1
  • 73
    • 0024744568 scopus 로고
    • Mutations in the glucocorticoid receptor zinc finger region that distinguish interdigitated DNA binding and transcriptional enhancement activities
    • Schena, M., Freedman, L.P., and Yamamoto, K.R. (1989). Mutations in the glucocorticoid receptor zinc finger region that distinguish interdigitated DNA binding and transcriptional enhancement activities. Genes Dev. 3, 1590-1601.
    • (1989) Genes Dev. , vol.3 , pp. 1590-1601
    • Schena, M.1    Freedman, L.P.2    Yamamoto, K.R.3
  • 74
    • 0029085038 scopus 로고
    • Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation
    • Schulman, I.G., Chakravarti, D., Juguilon, H., Romo, A., and Evans, R.M. (1995). Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation. Proc. Natl. Acad. Sci. USA 92, 8288-8292.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8288-8292
    • Schulman, I.G.1    Chakravarti, D.2    Juguilon, H.3    Romo, A.4    Evans, R.M.5
  • 76
    • 0030570719 scopus 로고    scopus 로고
    • Cloning of a human homolog of the Drosophila Minibrain/rat Dyrk gene from "the Down syndrome critical region" of chromosome 21
    • Shindoh, N., Kudoh, J., Hideto, M., Yamaki, A., Minoshima, M., Shimizu, Y., and Shimizu, N. (1996). Cloning of a human homolog of the Drosophila Minibrain/rat Dyrk gene from "the Down syndrome critical region" of chromosome 21. Biochem. Biophys. Res. Commun. 225, 92-99.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 92-99
    • Shindoh, N.1    Kudoh, J.2    Hideto, M.3    Yamaki, A.4    Minoshima, M.5    Shimizu, Y.6    Shimizu, N.7
  • 77
    • 0030915187 scopus 로고    scopus 로고
    • Functional screening of 2 Mb of human chromosome 21q22.2 in transgenic mice implicates minibrain in learning defects associated with Down syndrome
    • Smith, D.J., et al. (1997). Functional screening of 2 Mb of human chromosome 21q22.2 in transgenic mice implicates minibrain in learning defects associated with Down syndrome. Nat. Genet. 16, 28-36.
    • (1997) Nat. Genet. , vol.16 , pp. 28-36
    • Smith, D.J.1
  • 78
    • 0026608983 scopus 로고
    • Effects of okadaic acid, a protein phosphatase inhibitor, on glucocorticoid receptor mediated enhancement
    • Somers, J.P., and DeFranco, D.B. (1992). Effects of okadaic acid, a protein phosphatase inhibitor, on glucocorticoid receptor mediated enhancement. Mol. Endocrinol. 6, 26-34.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 26-34
    • Somers, J.P.1    Defranco, D.B.2
  • 79
    • 0031584810 scopus 로고    scopus 로고
    • The murine Dyrk protein maps to chromosome 16, localizes to the nucleus, and can form multimers
    • Song, W.-J., Chung, S.-H., and Kurnit, D.M. (1997). The murine Dyrk protein maps to chromosome 16, localizes to the nucleus, and can form multimers. Biochem. Biophys. Res. Commun. 231, 640-644.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 640-644
    • Song, W.-J.1    Chung, S.-H.2    Kurnit, D.M.3
  • 80
    • 0029894563 scopus 로고    scopus 로고
    • Intracellular receptors use a common mechanism to interpret signaling information at response elements
    • Starr, D.B., Matsui, W., Thomas, J.R., and Yamamoto, K.R. (1996). Intracellular receptors use a common mechanism to interpret signaling information at response elements. Genes Dev. 10, 1271-1283.
    • (1996) Genes Dev. , vol.10 , pp. 1271-1283
    • Starr, D.B.1    Matsui, W.2    Thomas, J.R.3    Yamamoto, K.R.4
  • 81
    • 0030786270 scopus 로고    scopus 로고
    • TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1
    • Takeshita, A., Cardona, G.R., Koibuchi, N., Suen, C.S., and Chin, W.W. (1997). TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J. Biol. Chem. 272, 27629-27634.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27629-27634
    • Takeshita, A.1    Cardona, G.R.2    Koibuchi, N.3    Suen, C.S.4    Chin, W.W.5
  • 83
    • 0028337542 scopus 로고
    • Transcriptional activation: A complex puzzle with few easy pieces
    • Tjian, R., and Maniatis, T. (1994). Transcriptional activation: a complex puzzle with few easy pieces. Cell 77, 5-8.
    • (1994) Cell , vol.77 , pp. 5-8
    • Tjian, R.1    Maniatis, T.2
  • 84
    • 0029954339 scopus 로고    scopus 로고
    • TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel, J.J., Hiene, M.J.S., Zechel, C., Chambon, P., and 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    Hiene, M.J.S.2    Zechel, C.3    Chambon, P.4    Gronemeyer, H.5
  • 85
    • 0012316186 scopus 로고    scopus 로고
    • Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and putative transcriptional intermediary factors mSUG1 and TIF1
    • vom Baur, E., Zechel, C., Heery, D., Heine, M.J.S., Garnier, J.M., Vivat, V., Le Douarin, B., Gronemeyer, H., Chambon, P., and Losson, R. (1996). Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and putative transcriptional intermediary factors mSUG1 and TIF1. EMBO J. 15, 110-124.
    • (1996) EMBO J. , vol.15 , pp. 110-124
    • Vom Baur, E.1    Zechel, C.2    Heery, D.3    Heine, M.J.S.4    Garnier, J.M.5    Vivat, V.6    Le Douarin, B.7    Gronemeyer, H.8    Chambon, P.9    Losson, R.10
  • 86
    • 0029855010 scopus 로고    scopus 로고
    • Steroid hormone receptors and their regulation by phosphorylation
    • Weigel, N.L. (1996). Steroid hormone receptors and their regulation by phosphorylation. Biochem. J. 319, 657-667.
    • (1996) Biochem. J. , vol.319 , pp. 657-667
    • Weigel, N.L.1
  • 87
    • 0342547258 scopus 로고    scopus 로고
    • Ligand-independent activation of the oestrogen receptor by mutation of a conserved tyrosine
    • White R., Sjöberg, M., Kalkhoven, E., and Parker, M.G. (1997). Ligand-independent activation of the oestrogen receptor by mutation of a conserved tyrosine. EMBO J. 16, 1427-1435.
    • (1997) EMBO J. , vol.16 , pp. 1427-1435
    • White, R.1    Sjöberg, M.2    Kalkhoven, E.3    Parker, M.G.4
  • 88
    • 0028295681 scopus 로고
    • 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans
    • Wilson, R. et al. (1994). 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 368, 32-38.
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1
  • 89
    • 0029951486 scopus 로고    scopus 로고
    • 70, for the androgen receptor in human prostate cells
    • 70, for the androgen receptor in human prostate cells. Proc. Natl. Acad. Sci. USA 93, 5517-5521.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5517-5521
    • Yeh, S.1    Chang, C.2
  • 90
    • 0029041681 scopus 로고
    • Identification of three proline-directed phosphorylation sites in the human androgen receptor
    • Zhou, Z.-X., Lane, V.M., Kemppainen, J.A., and Wilson, E.M. (1995). Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol. Endocrinol. 9, 605-615.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 605-615
    • Zhou, Z.-X.1    Lane, V.M.2    Kemppainen, J.A.3    Wilson, E.M.4


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