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Volumn 11, Issue 3, 1997, Pages 379-389

At least three subdomains of v-erbA are involved in its silencing function

Author keywords

[No Author keywords available]

Indexed keywords

THYROID HORMONE;

EID: 0031049397     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/mend.11.3.9903     Document Type: Article
Times cited : (23)

References (36)
  • 2
    • 0024336324 scopus 로고
    • Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist
    • Damm K, Thompson CC, Evans RM 1989 Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist. Nature 339:593-597
    • (1989) Nature , vol.339 , pp. 593-597
    • Damm, K.1    Thompson, C.C.2    Evans, R.M.3
  • 3
    • 0025311121 scopus 로고
    • Transcriptional repression in eukaryotes
    • Renkawitz R 1990 Transcriptional repression in eukaryotes. Trends Genet 6:192-197
    • (1990) Trends Genet , vol.6 , pp. 192-197
    • Renkawitz, R.1
  • 4
    • 0025336820 scopus 로고
    • Modular structure of a chicken lysozyme silencer: Involvement of an unusual thyroid hormone receptor binding site
    • Baniahmad A, Steiner C, Koehne AJ, Renkawitz R 1990 Modular structure of a chicken lysozyme silencer: involvement of an unusual thyroid hormone receptor binding site. Cell 61:505-514
    • (1990) Cell , vol.61 , pp. 505-514
    • Baniahmad, A.1    Steiner, C.2    Koehne, A.J.3    Renkawitz, R.4
  • 5
    • 0026557594 scopus 로고
    • A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor
    • Baniahmad A, Koehne AC, Renkawitz R 1992 A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor. EMBO J 11:1015-1023
    • (1992) EMBO J , vol.11 , pp. 1015-1023
    • Baniahmad, A.1    Koehne, A.C.2    Renkawitz, R.3
  • 6
    • 0028578074 scopus 로고
    • Two silencing sub-domains of v-erbA synergize with each other, but not with RXR
    • Martin B, Renkawitz R, Muller M 1994 Two silencing sub-domains of v-erbA synergize with each other, but not with RXR. Nucleic Acid Res 22:4898-4905
    • (1994) Nucleic Acid Res , vol.22 , pp. 4898-4905
    • Martin, B.1    Renkawitz, R.2    Muller, M.3
  • 7
    • 0027435514 scopus 로고
    • Interaction of human thyroid hormone receptor-beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone
    • Baniahmad A, Ha I, Reinberg D, Tsai S, Tsai M-J, O'Malley BW 1993 Interaction of human thyroid hormone receptor-beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone. Proc Natl Acad Sci USA 90:8832-8836
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8832-8836
    • Baniahmad, A.1    Ha, I.2    Reinberg, D.3    Tsai, S.4    Tsai, M.-J.5    O'Malley, B.W.6
  • 9
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD, Evans RM 1995 A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377:454-457
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 11
    • 0027240151 scopus 로고
    • Unliganded thyroid hormone receptor inhibits formation of a functional preinitiation complex: Implications for active repression
    • Fondell JD, Roy AL, Roeder RG 1993 Unliganded thyroid hormone receptor inhibits formation of a functional preinitiation complex: implications for active repression. Genes Dev 7:1400-1410
    • (1993) Genes Dev , vol.7 , pp. 1400-1410
    • Fondell, J.D.1    Roy, A.L.2    Roeder, R.G.3
  • 12
    • 0028970198 scopus 로고
    • Ligand modulates the interaction of thyroid hormone receptor β with the basal transcription machinery
    • Tong G-X, Tanen MR, Bagchi MK 1995 Ligand modulates the interaction of thyroid hormone receptor β with the basal transcription machinery. J Biol Chem 270:10601-10611
    • (1995) J Biol Chem , vol.270 , pp. 10601-10611
    • Tong, G.-X.1    Tanen, M.R.2    Bagchi, M.K.3
  • 13
    • 0029656208 scopus 로고    scopus 로고
    • Unliganded thyroid hormone receptor a can target TATA-binding protein for transcriptional repression
    • Fondell JD, Brunel F, Hisatake K, Roeder RG 1996 Unliganded thyroid hormone receptor a can target TATA-binding protein for transcriptional repression. Mol Cell Biol 16:281-287
    • (1996) Mol Cell Biol , vol.16 , pp. 281-287
    • Fondell, J.D.1    Brunel, F.2    Hisatake, K.3    Roeder, R.G.4
  • 14
    • 0028988482 scopus 로고
    • The τ4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing
    • Baniahmad A, Leng X, Burris TP, Tsai SY, Tsai M-J, O'Malley BW 1995 The τ4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing. Mol Cell Biol 15:76-86
    • (1995) Mol Cell Biol , vol.15 , pp. 76-86
    • Baniahmad, A.1    Leng, X.2    Burris, T.P.3    Tsai, S.Y.4    Tsai, M.-J.5    O'Malley, B.W.6
  • 15
    • 0027375518 scopus 로고
    • Identification of a domain required for oncogenic activity and transcriptional suppression by v-erbA and thyroid-hormone receptor α
    • Damm K, Evans RM 1993 Identification of a domain required for oncogenic activity and transcriptional suppression by v-erbA and thyroid-hormone receptor α. Proc Natl Acad Sci USA 90:10668-10672
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10668-10672
    • Damm, K.1    Evans, R.M.2
  • 17
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet W, Ruff M, Chambon P, Gronemeyer H 1995 Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 375:377-382
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4
  • 18
    • 0028894022 scopus 로고
    • Genetic dissection of thyroid hormone receptor α: Identification of mutations that separate hormone binding and transcriptional activation
    • Uppaluri R, Towle HC 1995 Genetic dissection of thyroid hormone receptor α: identification of mutations that separate hormone binding and transcriptional activation. Mol Cell Biol 15:1499-1512
    • (1995) Mol Cell Biol , vol.15 , pp. 1499-1512
    • Uppaluri, R.1    Towle, H.C.2
  • 19
    • 0024021255 scopus 로고
    • Mutations that alter both localization and production of a yeast nuclear protein
    • Silver PA, Chiang A, Sadler I 1988 Mutations that alter both localization and production of a yeast nuclear protein. Genes Dev 2:707-717
    • (1988) Genes Dev , vol.2 , pp. 707-717
    • Silver, P.A.1    Chiang, A.2    Sadler, I.3
  • 21
    • 0027204754 scopus 로고
    • Characterization of the transcription activation function and the DNA binding domain of transcriptional enhancer factor-1
    • Hwang JJ, Chambon P, Davidson I 1993 Characterization of the transcription activation function and the DNA binding domain of transcriptional enhancer factor-1. EMBO J 12:2337-2348
    • (1993) EMBO J , vol.12 , pp. 2337-2348
    • Hwang, J.J.1    Chambon, P.2    Davidson, I.3
  • 22
    • 0024317270 scopus 로고
    • The human estrogen receptor has two independent nonacidic transcriptional activation functions
    • Tora L, White J, Brou C, Tasset D, Webster N, Scheer E, Chambon P 1989 The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 59:477-487
    • (1989) Cell , vol.59 , pp. 477-487
    • Tora, L.1    White, J.2    Brou, C.3    Tasset, D.4    Webster, N.5    Scheer, E.6    Chambon, P.7
  • 23
    • 0029587601 scopus 로고
    • Specific mutations in the ligand binding domain selectively abolish the silencing function of human thyroid hormone receptor β
    • Nawaz Z, Tsai M-J, O'Malley BW 1995 Specific mutations in the ligand binding domain selectively abolish the silencing function of human thyroid hormone receptor β. Proc Natl Acad Sci USA 92:11691-11695
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11691-11695
    • Nawaz, Z.1    Tsai, M.-J.2    O'Malley, B.W.3
  • 24
    • 0026048274 scopus 로고
    • Ligand-binding and heterodimerization activities of a conserved region in the ligand-binding domain of the thyroid hormone receptor
    • Spanjaard RA, Darling DS, Chin WW 1991 Ligand-binding and heterodimerization activities of a conserved region in the ligand-binding domain of the thyroid hormone receptor. Proc Natl Acad Sci USA 88:8587-8591
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8587-8591
    • Spanjaard, R.A.1    Darling, D.S.2    Chin, W.W.3
  • 25
    • 0027219428 scopus 로고
    • The conserved ninth C-terminal heptad in thyroid hormone and retinoic acid receptors mediates diverse responses by affecting heterodimer but not homodimer formation
    • Au-Fliegner M, Helmer E, Casanova J, Raaka BM, Samuels HH 1993 The conserved ninth C-terminal heptad in thyroid hormone and retinoic acid receptors mediates diverse responses by affecting heterodimer but not homodimer formation. Mol Cell Biol 13:5725-5737
    • (1993) Mol Cell Biol , vol.13 , pp. 5725-5737
    • Au-Fliegner, M.1    Helmer, E.2    Casanova, J.3    Raaka, B.M.4    Samuels, H.H.5
  • 26
    • 0028832067 scopus 로고
    • The ligand-binding domains of the thyroid hormone/retinoid receptor gene superfamily function in vivo to mediate heterodimerization, gene silencing, and transactivation
    • Qi J-C, Desai-Yajnik V, Greene ME, Raaka BM, Samuels HH 1995 The ligand-binding domains of the thyroid hormone/retinoid receptor gene superfamily function in vivo to mediate heterodimerization, gene silencing, and transactivation. Mol Cell Biol 15:1817-1825
    • (1995) Mol Cell Biol , vol.15 , pp. 1817-1825
    • Qi, J.-C.1    Desai-Yajnik, V.2    Greene, M.E.3    Raaka, B.M.4    Samuels, H.H.5
  • 28
  • 29
    • 0027941792 scopus 로고
    • Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: Presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity
    • Durand B, Saunders M, Gaudon C, Roy B, Losson R, Chambon P 1994 Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity. EMBO J 13:5370-82
    • (1994) EMBO J , vol.13 , pp. 5370-5382
    • Durand, B.1    Saunders, M.2    Gaudon, C.3    Roy, B.4    Losson, R.5    Chambon, P.6
  • 30
    • 0028305554 scopus 로고
    • A highly conserved region in the hormone binding domain of the human estrogen receptor functions as an efficient transactivation domain in yeast
    • Pierrat B, Heery DM, Chambon P, Losson R 1994 A highly conserved region in the hormone binding domain of the human estrogen receptor functions as an efficient transactivation domain in yeast. Gene 143:193-200
    • (1994) Gene , vol.143 , pp. 193-200
    • Pierrat, B.1    Heery, D.M.2    Chambon, P.3    Losson, R.4
  • 31
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA, Roberts JD, Zakour RA 1987 Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154:367-382
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 32
    • 45249130610 scopus 로고
    • An automated method for calcium-mediated gene transfer
    • Steiner C, Kaltschmidt C 1989 An automated method for calcium-mediated gene transfer. Trends Genet 5:138
    • (1989) Trends Genet , vol.5 , pp. 138
    • Steiner, C.1    Kaltschmidt, C.2
  • 33
    • 0024280908 scopus 로고
    • Developmental regulation of β-globin gene switching
    • Choi O-B, Engel JD 1988 Developmental regulation of β-globin gene switching. Cell 55:17-26
    • (1988) Cell , vol.55 , pp. 17-26
    • Choi, O.-B.1    Engel, J.D.2
  • 34
    • 0018751062 scopus 로고
    • Depletion of L-3,5,3′-triiodothyronine and L-thyroxine in euthyroid calf serum for use in cell culture studies of the action of thyroid hormone
    • Samuels HH, Frederick S, Casanova J 1979 Depletion of L-3,5,3′-triiodothyronine and L-thyroxine in euthyroid calf serum for use in cell culture studies of the action of thyroid hormone. Endocrinology 105:80-85
    • (1979) Endocrinology , vol.105 , pp. 80-85
    • Samuels, H.H.1    Frederick, S.2    Casanova, J.3
  • 35
    • 0020435972 scopus 로고
    • Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells
    • Gorman CM, Moffat LF, Howard BH 1982 Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Mol Cell Biol 2:1044-1051
    • (1982) Mol Cell Biol , vol.2 , pp. 1044-1051
    • Gorman, C.M.1    Moffat, L.F.2    Howard, B.H.3
  • 36
    • 0023808861 scopus 로고
    • The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer
    • Kumar V, Chambon P 1988 The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell 55:145-156
    • (1988) Cell , vol.55 , pp. 145-156
    • Kumar, V.1    Chambon, P.2


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