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Volumn 6, Issue 5, 1996, Pages 567-574

Retinoid receptors in transcriptional regulation

Author keywords

[No Author keywords available]

Indexed keywords

VITAMIN RECEPTOR;

EID: 0030271711     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(96)80085-2     Document Type: Article
Times cited : (59)

References (67)
  • 2
    • 0028419153 scopus 로고
    • The retinoid signaling pathway: Molecular and genetic analyses
    • Chambon P. The retinoid signaling pathway: molecular and genetic analyses. Semin Cell Biol. 5:1994;115-125.
    • (1994) Semin Cell Biol , vol.5 , pp. 115-125
    • Chambon, P.1
  • 3
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangeldorf DJ, Evans RM. The RXR heterodimers and orphan receptors. Cell. 83:1995;841-850.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangeldorf, D.J.1    Evans, R.M.2
  • 7
    • 0028332036 scopus 로고
    • Differential recognition of target genes by nuclear receptors monomers, dimers and heterodimers
    • Glass CK. Differential recognition of target genes by nuclear receptors monomers, dimers and heterodimers. Endocrinol Rev. 15:1994;391-407.
    • (1994) Endocrinol Rev , vol.15 , pp. 391-407
    • Glass, C.K.1
  • 8
    • 0029115655 scopus 로고
    • 9-cis retinoic acid signaling: Changing partners causes some excitement
    • Leblanc B, Stunnenberg HG. 9-cis retinoic acid signaling: changing partners causes some excitement. Genes Dev. 9:1995;1811-1816.
    • (1995) Genes Dev , vol.9 , pp. 1811-1816
    • Leblanc, B.1    Stunnenberg, H.G.2
  • 9
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai M-J, O'Malley BW. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu Rev Biochem. 63:1994;451-486.
    • (1994) Annu Rev Biochem , vol.63 , pp. 451-486
    • Tsai M-J1    O'Malley, B.W.2
  • 10
    • 0029618368 scopus 로고
    • Steroid hormone receptors: Many actors in search of a plot
    • Beato M, Herrlich P, Schütz G. Steroid hormone receptors: many actors in search of a plot. Cell. 83:1995;851-857.
    • (1995) Cell , vol.83 , pp. 851-857
    • Beato, M.1    Herrlich, P.2    Schütz, G.3
  • 11
    • 0029584593 scopus 로고
    • Nonsteroid nuclear receptors: What are genetic studies telling us about their roles in real life?
    • Kastner P, Mark M, Chambon P. Nonsteroid nuclear receptors: what are genetic studies telling us about their roles in real life? Cell. 83:1995;859-871.
    • (1995) Cell , vol.83 , pp. 859-871
    • Kastner, P.1    Mark, M.2    Chambon, P.3
  • 12
    • 0011864472 scopus 로고
    • Retinoic acid receptors
    • Bäuerle P.A. Boston: Birkhäuser
    • Keaveney M, Stunnenberg H. Retinoic acid receptors. Bäuerle PA. Inducible Gene Expression. 1995;187-242 Birkhäuser, Boston.
    • (1995) Inducible Gene Expression , pp. 187-242
    • Keaveney, M.1    Stunnenberg, H.2
  • 14
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • of outstanding interest. The paper reports the X-ray structure of apo-RXR LBD, with the novel folding shown for the LBD. As further analyzed in [17], it seems likely that this fold, like that for the DBD, is common throughout the nuclear receptor family.
    • Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α of outstanding interest Nature. 375:1995;377-382 The paper reports the X-ray structure of apo-RXR LBD, with the novel folding shown for the LBD. As further analyzed in [17], it seems likely that this fold, like that for the DBD, is common throughout the nuclear receptor family.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 15
    • 0029643780 scopus 로고
    • Crystal structure of the RARγ ligand binding domain bound to all-trans retinoic acid
    • of outstanding interest. This paper shows the X-ray structure of holo-RARγ LBD. By comparing the structure of the previously resolved holo-RXR LDB, the authors propose that, upon ligand binding, the carboxy-terminal part (AF-2) folds back to the core of the LDB.
    • Renaud J-P, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D. Crystal structure of the RARγ ligand binding domain bound to all-trans retinoic acid. of outstanding interest Nature. 378:1995;681-690 This paper shows the X-ray structure of holo-RARγ LBD. By comparing the structure of the previously resolved holo-RXR LDB, the authors propose that, upon ligand binding, the carboxy-terminal part (AF-2) folds back to the core of the LDB.
    • (1995) Nature , vol.378 , pp. 681-690
    • Renaud J-P1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 16
    • 0029643769 scopus 로고
    • A structural role for hormone in the thyroid hormone receptor
    • of outstanding interest. This paper reports the X-ray structure of holo-TRα LDB, revealing a number of shared features with that of holo-RARγ.
    • Wagner RL, Apriletti JW, McGrath ME, West BL, Baxter JD, Fletterick RJ. A structural role for hormone in the thyroid hormone receptor. of outstanding interest Nature. 378:1995;690-697 This paper reports the X-ray structure of holo-TRα LDB, revealing a number of shared features with that of holo-RARγ.
    • (1995) Nature , vol.378 , pp. 690-697
    • Wagner, R.L.1    Apriletti, J.W.2    McGrath, M.E.3    West, B.L.4    Baxter, J.D.5    Fletterick, R.J.6
  • 17
    • 0030056997 scopus 로고    scopus 로고
    • A canonical structure for the ligand-binding domain of nuclear receptors
    • of outstanding interest. of special interest. By extensive sequence analysis, the authors propose the preence of a common fold for the nuclear receptor LBD (see also [14, 16]).
    • of outstanding interest Wurtz JM, Bourguet W, Renaud JP, Vivat V, Chambon P, Moras D, Gronemeyer H. A canonical structure for the ligand-binding domain of nuclear receptors. of special interest Nat Struct Biol. 3:1996;87-94 By extensive sequence analysis, the authors propose the preence of a common fold for the nuclear receptor LBD (see also [14, 16]).
    • (1996) Nat Struct Biol , vol.3 , pp. 87-94
    • Wurtz, J.M.1    Bourguet, W.2    Renaud, J.P.3    Vivat, V.4    Chambon, P.5    Moras, D.6    Gronemeyer, H.7
  • 18
    • 0030113441 scopus 로고    scopus 로고
    • How nuclear receptors get turned on
    • Schwabe JWR. How nuclear receptors get turned on. Curr Biol. 6:1996;372-374.
    • (1996) Curr Biol , vol.6 , pp. 372-374
    • Schwabe, J.W.R.1
  • 19
    • 0026726806 scopus 로고
    • Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation
    • Allan GF, Leng X, Tsai SY, Weigel NL, Edwards DP, Tsai M-J, O'Malley BW. Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation. J Biol Chem. 267:1992;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-J6    O'Malley, B.W.7
  • 20
    • 0027754125 scopus 로고
    • Ligand-dependent conformational changes in thyroid hormone and retinoic acid receptors are potentially enhanced by heterodimerization with retinoic X receptor
    • Len X, Tsai SY, O'Malley BW, Tsai MJ. Ligand-dependent conformational changes in thyroid hormone and retinoic acid receptors are potentially enhanced by heterodimerization with retinoic X receptor. J Steroid Biochem Molec Biol. 46:1993;643-661.
    • (1993) J Steroid Biochem Molec Biol , vol.46 , pp. 643-661
    • Len, X.1    Tsai, S.Y.2    O'Malley, B.W.3    Tsai, M.J.4
  • 21
    • 0028012039 scopus 로고
    • Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping
    • Keidel S, LeMotte P, Apfel C. Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping. Mol Cell Biol. 14:1994;287-298.
    • (1994) Mol Cell Biol , vol.14 , pp. 287-298
    • Keidel, S.1    LeMotte, P.2    Apfel, C.3
  • 22
    • 0028336807 scopus 로고
    • Ligand-induced alteration of the protease sensitivity of retinoid X receptor alpha
    • Leid M. Ligand-induced alteration of the protease sensitivity of retinoid X receptor alpha. J Biol Chem. 269:1994;14175-14181.
    • (1994) J Biol Chem , vol.269 , pp. 14175-14181
    • Leid, M.1
  • 23
    • 0028961189 scopus 로고
    • Mouse retinoid X receptor β contains a separable ligand-binding and transactivation domain in its E region
    • Leng X, Blanco J, Tsai SY, Ozato K, O'Malley BW, Tsai M-J. Mouse retinoid X receptor β contains a separable ligand-binding and transactivation domain in its E region. Mol Cell Biol. 15:1995;255-263.
    • (1995) Mol Cell Biol , vol.15 , pp. 255-263
    • Leng, X.1    Blanco, J.2    Tsai, S.Y.3    Ozato, K.4    O'Malley, B.W.5    Tsai M-J6
  • 24
    • 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. 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. 13:1994;5370-5382.
    • (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
  • 26
    • 0029002298 scopus 로고
    • Unique response pathways are established by allosteric interactions among nuclear hormone receptors
    • of outstanding interest. Another report investigating the ligand binding properties of RXR in several heterodimeric contexts. It is shown that RXR-selective ligands can activate RXR/NURR1 heterodimers, suggesting the existence of novel retinoid pathways.
    • Forman BM, Umesono K, Chen J, Evans RM. Unique response pathways are established by allosteric interactions among nuclear hormone receptors. of outstanding interest Cell. 81:1995;541-550 Another report investigating the ligand binding properties of RXR in several heterodimeric contexts. It is shown that RXR-selective ligands can activate RXR/NURR1 heterodimers, suggesting the existence of novel retinoid pathways.
    • (1995) Cell , vol.81 , pp. 541-550
    • Forman, B.M.1    Umesono, K.2    Chen, J.3    Evans, R.M.4
  • 27
    • 0029947425 scopus 로고    scopus 로고
    • Individual subunits of heterodimers comprised of retinoic acid and retinoid X receptors interact with their ligands independently
    • of outstanding interest. Using fluorescence-based methods, the authors show that RXR and RAR, when heterodimerized, are both able to bind to their respective ligands either in solution or when bound to target DNA. These findings are in contrast to other reports [25, 26] where (by using different methods, i.e. GST-receptor ligand pull-down assays) binding of a synthetic ligand to RXR was inhibited by RAR in the presence of target DNA.
    • Kersten S, Dawson MI, Lewis BA, Noy N. Individual subunits of heterodimers comprised of retinoic acid and retinoid X receptors interact with their ligands independently. of outstanding interest Biochemistry. 35:1996;3816-3824 Using fluorescence-based methods, the authors show that RXR and RAR, when heterodimerized, are both able to bind to their respective ligands either in solution or when bound to target DNA. These findings are in contrast to other reports [25, 26] where (by using different methods, i.e. GST-receptor ligand pull-down assays) binding of a synthetic ligand to RXR was inhibited by RAR in the presence of target DNA.
    • (1996) Biochemistry , vol.35 , pp. 3816-3824
    • Kersten, S.1    Dawson, M.I.2    Lewis, B.A.3    Noy, N.4
  • 28
    • 0029587448 scopus 로고
    • Enhancement of HL-60 differentiation by a new class of retinoids with selective affinity on retinoid X receptor
    • Apfel C, Kamber M, Klaus M, Mohr P, Keidel S, LeMotte PK. Enhancement of HL-60 differentiation by a new class of retinoids with selective affinity on retinoid X receptor. J Biol Chem. 270:1995;30765-30772.
    • (1995) J Biol Chem , vol.270 , pp. 30765-30772
    • Apfel, C.1    Kamber, M.2    Klaus, M.3    Mohr, P.4    Keidel, S.5    LeMotte, P.K.6
  • 29
    • 0028894263 scopus 로고
    • Enhanced efficiency of combinations of retinoic acid and retinoid X receptor-selective retinoids and α-interferon in inhibition of cervical carcinoma cell proliferation
    • Lotan R, Dawson MI, Zou C-C, Jong L, Lotan D, Zou C-P. Enhanced efficiency of combinations of retinoic acid and retinoid X receptor-selective retinoids and α-interferon in inhibition of cervical carcinoma cell proliferation. Cancer Res. 55:1995;232-236.
    • (1995) Cancer Res , vol.55 , pp. 232-236
    • Lotan, R.1    Dawson, M.I.2    Zou C-C3    Jong, L.4    Lotan, D.5    Zou C-P6
  • 31
    • 0028811341 scopus 로고
    • Synergistic activation of retinoic acid (RA)-responsive genes and induction of embryonal carcinoma cell differentiation by an RA receptor α(RARα)-, RARβ-, or RARγ-selective ligand in combination with a retinoid X receptor-specific ligand
    • Roy B, Taneja R, Chambon P. Synergistic activation of retinoic acid (RA)-responsive genes and induction of embryonal carcinoma cell differentiation by an RA receptor α(RARα)-, RARβ-, or RARγ-selective ligand in combination with a retinoid X receptor-specific ligand. Mol Cell Biol. 15:1995;6481-6487.
    • (1995) Mol Cell Biol , vol.15 , pp. 6481-6487
    • Roy, B.1    Taneja, R.2    Chambon, P.3
  • 32
    • 0028796740 scopus 로고
    • Endogenous RAR/RXR heterodimers are the major functional forms regulating retinoid-responsive elements in adult human keratinocytes
    • Xiao J-H, Durand B, Chambon P, Voorhees JJ. Endogenous RAR/RXR heterodimers are the major functional forms regulating retinoid-responsive elements in adult human keratinocytes. J Biol Chem. 270:1995;3001-3011.
    • (1995) J Biol Chem , vol.270 , pp. 3001-3011
    • Xiao J-H1    Durand, B.2    Chambon, P.3    Voorhees, J.J.4
  • 33
    • 0029097645 scopus 로고
    • Efficient inhibition of activation-induced Fas ligand up-regulation and T cell apoptosis by retinoids requires occupancy of both retinoid X receptors and retinoic acid receptors
    • Yang Y, Minucci S, Ozato K, Heyman RA, Ashwell JD. Efficient inhibition of activation-induced Fas ligand up-regulation and T cell apoptosis by retinoids requires occupancy of both retinoid X receptors and retinoic acid receptors. J Biol Chem. 270:1995;18672-18677.
    • (1995) J Biol Chem , vol.270 , pp. 18672-18677
    • Yang, Y.1    Minucci, S.2    Ozato, K.3    Heyman, R.A.4    Ashwell, J.D.5
  • 34
    • 0030031227 scopus 로고    scopus 로고
    • Myeloid differentiation and retinoblastoma phosphorylation changes in HL-60 cells induced by retinoic acid receptor- and retinoid X receptor-selective retinoic acid analogs
    • Brooks SC III, Kazmer S, Levin AA, Yen A. Myeloid differentiation and retinoblastoma phosphorylation changes in HL-60 cells induced by retinoic acid receptor- and retinoid X receptor-selective retinoic acid analogs. Blood. 87:1996;227-237.
    • (1996) Blood , vol.87 , pp. 227-237
    • Brooks S.C. III1    Kazmer, S.2    Levin, A.A.3    Yen, A.4
  • 35
    • 0029793892 scopus 로고    scopus 로고
    • RAR and RXR selective ligands cooperatively induce apoptosis and neuronal differentiation in P19 embryonal carcinoma cells
    • Horn V, Minucci S, Ogryzko V, Adamson E, Howard B, Levin A, Ozato K. RAR and RXR selective ligands cooperatively induce apoptosis and neuronal differentiation in P19 embryonal carcinoma cells. FASEB J. 10:1996;1071-1077.
    • (1996) FASEB J , vol.10 , pp. 1071-1077
    • Horn, V.1    Minucci, S.2    Ogryzko, V.3    Adamson, E.4    Howard, B.5    Levin, A.6    Ozato, K.7
  • 36
    • 0026705751 scopus 로고
    • Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors
    • Kliewer SA, Umesono K, Noonan DJ, Heyman RA, Evans RM. Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors. Nature. 358:1992;771-774.
    • (1992) Nature , vol.358 , pp. 771-774
    • Kliewer, S.A.1    Umesono, K.2    Noonan, D.J.3    Heyman, R.A.4    Evans, R.M.5
  • 37
    • 0028946634 scopus 로고
    • A novel pathway for Vitamin A signaling mediated by RXR heterodimerization with NGFIB and NURR1
    • of special interest. A detailed analysis of the interaction of RXR with the orphan receptors NGFI-B and NURR1. Interestingly, canonical RAREs are shown to be activated by RXR/NGFI-B heterodimers and this activation is dependent on ligand binding to RXR.
    • Perlmann T, Jansson L. A novel pathway for Vitamin A signaling mediated by RXR heterodimerization with NGFIB and NURR1. of special interest Genes Dev. 9:1995;769-782 A detailed analysis of the interaction of RXR with the orphan receptors NGFI-B and NURR1. Interestingly, canonical RAREs are shown to be activated by RXR/NGFI-B heterodimers and this activation is dependent on ligand binding to RXR.
    • (1995) Genes Dev , vol.9 , pp. 769-782
    • Perlmann, T.1    Jansson, L.2
  • 38
    • 0029035278 scopus 로고
    • LXR, a nuclear receptor that defines a distinct retinoid response pathway
    • of special interest. Cloning of the gene for LXR, a novel orphan receptor that heterodimerizes with RXR and is activated by RXR-selective ligands. The DNA target for activated efficiently by RXR/TR heterodimers.
    • Willy PJ, Umesono K, Ong ES, Evans RM, Heyman RA, Mangelsdorf DJ. LXR, a nuclear receptor that defines a distinct retinoid response pathway. of special interest Genes Dev. 9:1995;1033-1045 Cloning of the gene for LXR, a novel orphan receptor that heterodimerizes with RXR and is activated by RXR-selective ligands. The DNA target for activated efficiently by RXR/TR heterodimers.
    • (1995) Genes Dev , vol.9 , pp. 1033-1045
    • Willy, P.J.1    Umesono, K.2    Ong, E.S.3    Evans, R.M.4    Heyman, R.A.5    Mangelsdorf, D.J.6
  • 39
    • 0029046931 scopus 로고
    • Identification of a nuclear receptor that is activated by farnesol metabolites
    • of special interest. Cloning of the gene for the farnesoid receptor, that binds to farnesol metabolites produced in the mevalonate pathway leading to the synthesis of cholesterol, steroids, and several key signalling molecules.
    • Forman B, Goode E, Chen J, Oro A, Bradley DJ, Perlmann T, Noonan D, Burka LT, McMorris T, Lamph WW, Evans RM. Identification of a nuclear receptor that is activated by farnesol metabolites. of special interest Cell. 81:1995;687-693 Cloning of the gene for the farnesoid receptor, that binds to farnesol metabolites produced in the mevalonate pathway leading to the synthesis of cholesterol, steroids, and several key signalling molecules.
    • (1995) Cell , vol.81 , pp. 687-693
    • Forman, B.1    Goode, E.2    Chen, J.3    Oro, A.4    Bradley, D.J.5    Perlmann, T.6    Noonan, D.7    Burka, L.T.8    McMorris, T.9    Lamph, W.W.10    Evans, R.M.11
  • 40
    • 0029085038 scopus 로고
    • Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation
    • Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM. Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation. Proc Natl Acad Sci USA. 92:1995;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
  • 42
    • 0029044001 scopus 로고
    • A 10-amino acid sequence in the N-terminal A/B/ domain of thyroid hormone receptor α is essential for transcriptional activation and interaction with the general transcription factor TFIIB
    • Hazdic E, Desai-Yajnik V, Helmer E, Guo S, Wu S, Koudinova N, Casanova J, Raaka BM, Samuels HH. A 10-amino acid sequence in the N-terminal A/B/ domain of thyroid hormone receptor α is essential for transcriptional activation and interaction with the general transcription factor TFIIB. Mol Cell Biol. 15:1995;4507-4517.
    • (1995) Mol Cell Biol , vol.15 , pp. 4507-4517
    • Hazdic, 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
  • 43
    • 0024564101 scopus 로고
    • Steroid hormone receptors compete for factors that mediate their enhancer function
    • Meyer ME, Gronemeyer H, Turcotte B, Bocquel MT, Tasset D, Chambon P. Steroid hormone receptors compete for factors that mediate their enhancer function. Cell. 57:1989;433-442.
    • (1989) Cell , vol.57 , pp. 433-442
    • Meyer, M.E.1    Gronemeyer, H.2    Turcotte, B.3    Bocquel, M.T.4    Tasset, D.5    Chambon, P.6
  • 44
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
    • of outstanding interest. Cloning of genes for NCoR, co-repressor for RAR, TR and potentially other receptors. In this report (and [45]) the association of NCoR (and SMRT, see below) with RAR and TR is shown to be critical for receptor-mediated repression in the absence of ligand.
    • Horlein AJ, Näär AM, Heinzel T, Torchia J, Gloss B, Kurokawa R, Ryan A, Kamei Y, Soderstrom M, Glass CK, Rosenfeld MG. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. of outstanding interest Nature. 377:1995;397-403 Cloning of genes for NCoR, co-repressor for RAR, TR and potentially other receptors. In this report (and [45]) the association of NCoR (and SMRT, see below) with RAR and TR is shown to be critical for receptor-mediated repression in the absence of ligand.
    • (1995) Nature , vol.377 , pp. 397-403
    • Horlein, A.J.1    Näär, A.M.2    Heinzel, T.3    Torchia, J.4    Gloss, B.5    Kurokawa, R.6    Ryan, A.7    Kamei, Y.8    Soderstrom, M.9    Glass, C.K.10    Rosenfeld, M.G.11
  • 45
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • of outstanding interest. This report details the cloning of the gene for another co-repressor, SMRT; the sequence homology with NCoR suggests the presence of families of co-repressors with possible distinct functions.
    • Chen D, Evans RM. A transcriptional co-repressor that interacts with nuclear hormone receptors. of outstanding interest Nature. 377:1995;454-457 This report details the cloning of the gene for another co-repressor, SMRT; the sequence homology with NCoR suggests the presence of families of co-repressors with possible distinct functions.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, D.1    Evans, R.M.2
  • 46
    • 0029154931 scopus 로고
    • Polarity-specific activities of retinoic acid receptors determined by a co-repressor
    • of special interest. NCoR is not released from RAR bound on a DR1 element, providing a possible mechanism of the lack of activation via this element.
    • Kurokawa R, Soderstrom M, Hörlein A, Halachmi S, Brown M, Rosenfeld MG, Glass CK. Polarity-specific activities of retinoic acid receptors determined by a co-repressor. of special interest Nature. 377:1995;451-454 NCoR is not released from RAR bound on a DR1 element, providing a possible mechanism of the lack of activation via this element.
    • (1995) Nature , vol.377 , pp. 451-454
    • Kurokawa, R.1    Soderstrom, M.2    Hörlein, A.3    Halachmi, S.4    Brown, M.5    Rosenfeld, M.G.6    Glass, C.K.7
  • 47
    • 0028527272 scopus 로고
    • Negative transcriptional regulation by nuclear receptors
    • Saatclogiu F, Claret FX, Karin M. Negative transcriptional regulation by nuclear receptors. Semin Cancer Biol. 5:1994;347-359.
    • (1994) Semin Cancer Biol , vol.5 , pp. 347-359
    • Saatclogiu, F.1    Claret, F.X.2    Karin, M.3
  • 48
    • 0029656208 scopus 로고    scopus 로고
    • Unliganded thyroid hormone receptor α can target TATA-binding protein for transcription repression
    • of special interest. Using biochemical approaches and in vitro transcription systems, the autors show that TBP might represent a direct target for the transcriptional repression mediated by TR in the absence of ligand.
    • Fondell JB, Brunel F, Hisatake K, Roeder RG. Unliganded thyroid hormone receptor α can target TATA-binding protein for transcription repression. of special interest Mol Cell Biol. 16:1996;281-287 Using biochemical approaches and in vitro transcription systems, the autors show that TBP might represent a direct target for the transcriptional repression mediated by TR in the absence of ligand.
    • (1996) Mol Cell Biol , vol.16 , pp. 281-287
    • Fondell, J.B.1    Brunel, F.2    Hisatake, K.3    Roeder, R.G.4
  • 50
    • 0029121358 scopus 로고
    • Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor
    • of special interest. The initial characterization of RIP140, a protein that binds to the estrogen receptor in a ligand-dependent fashion. RIP140 is shown to weakly modulate the transcriptional activity of ER by estrogen but not by anti-estrogens.
    • Cavailles V, Dauvois S, L'Horset F, Lopez G, Hoare S, Kushner PJ, Parker MG. Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor. of special interest EMBO J. 14:1995;3741-3751 The initial characterization of RIP140, a protein that binds to the estrogen receptor in a ligand-dependent fashion. RIP140 is shown to weakly modulate the transcriptional activity of ER by estrogen but not by anti-estrogens.
    • (1995) EMBO J , vol.14 , pp. 3741-3751
    • Cavailles, V.1    Dauvois, S.2    L'Horset, F.3    Lopez, G.4    Hoare, S.5    Kushner, P.J.6    Parker, M.G.7
  • 51
    • 0028233383 scopus 로고
    • Estrogen receptor-associated proteins: Possible mediators of hormone-induced transcription
    • Halachmi S, Marden E, Martin G, MacKay I, Abbondanza C, Brown M. Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription. Science. 264:1994;1455-1458.
    • (1994) Science , vol.264 , pp. 1455-1458
    • Halachmi, S.1    Marden, E.2    Martin, G.3    MacKay, I.4    Abbondanza, C.5    Brown, M.6
  • 52
    • 0029030016 scopus 로고
    • The N-terminal part of TIF-1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18
    • of special interest. A yeast genetic screen was used to clone TIF1, protein with 1017 residues. The amino-terminal region of TIF1 is fused to B-raf in the mouse oncoprotein T18.
    • Le Douarin B, Zechel C, Garnier JM, Lutz Y, Tora L, Pierrat B, Heery D, Gronemeyer H, Chambon P, Losson R. The N-terminal part of TIF-1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. of special interest EMBO J. 14:1995;2020-2033 A yeast genetic screen was used to clone TIF1, protein with 1017 residues. The amino-terminal region of TIF1 is fused to B-raf in the mouse oncoprotein T18.
    • (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, B.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
    • of special interest. The yeast two-hybrid system was used to isolate Trip 1, a human factor that interacts with TR and RXR in a ligand-dependent manner and that is homologous to the yeast factor SUG1.
    • Lee JW, Ryan F, Swaffield JC, Johnston SA, Moore DD. Interaction of thyroid hormone receptor with a conserved transcriptional mediator. of special interest Nature. 371:1995;91-94 The yeast two-hybrid system was used to isolate Trip 1, a human factor that interacts with TR and RXR in a ligand-dependent manner and that is homologous to the yeast factor SUG1.
    • (1995) Nature , vol.371 , pp. 91-94
    • Lee, J.W.1    Ryan, F.2    Swaffield, J.C.3    Johnston, S.A.4    Moore, D.D.5
  • 54
    • 0028846193 scopus 로고
    • Sequence and characterization of a coativator for the steroid hormone receptor superfamily
    • of special interest. Cloning of the gene for SRC-1, a co-activator for several classes of transcription factors, including nuclear receptors. The functional studies presented in this report show a clear increase in ligand-dependent transcriptional capacity to all the nuclear receptors tested and are the best example of a transcriptional coactivator for the members of the superfamily.
    • Oñate SA, Tsai M-J, O'Malley BW. Sequence and characterization of a coativator for the steroid hormone receptor superfamily. of special interest Science. 270:1995;1354-1357 Cloning of the gene for SRC-1, a co-activator for several classes of transcription factors, including nuclear receptors. The functional studies presented in this report show a clear increase in ligand-dependent transcriptional capacity to all the nuclear receptors tested and are the best example of a transcriptional coactivator for the members of the superfamily.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Oñate, S.A.1    Tsai M-J2    O'Malley, B.W.3
  • 55
    • 0012316186 scopus 로고    scopus 로고
    • Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1
    • of special interest. Analysis of the interaction of several nuclear receptors with two putative co-activators mSUG1 and TIF1. The receptors show marked differences in their interaction with these two factors, suggesting that differential receptor-co-activator interactions may take place in vivo.
    • Von Baur E, Zechel C, Heery D, Heine MJS, Garnier J-M, Vivat V, Le Douarin B, Gronemeyer H, Chambon P, Losson R. Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1. of special interest EMBO J. 15:1996;110-124 Analysis of the interaction of several nuclear receptors with two putative co-activators mSUG1 and TIF1. The receptors show marked differences in their interaction with these two factors, suggesting that differential receptor-co-activator interactions may take place in vivo.
    • (1996) EMBO J , vol.15 , pp. 110-124
    • Von Baur, E.1    Zechel, C.2    Heery, D.3    Heine, M.J.S.4    Garnier J-M5    Vivat, V.6    Le Douarin, B.7    Gronemeyer, H.8    Chambon, P.9    Losson, R.10
  • 56
    • 0242587820 scopus 로고    scopus 로고
    • A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors
    • of outstanding interest. CBP, originally defined as a co-activator for the CREB family of transcription factors, is shown to modulate activities of RXR and RAR.
    • Kamei Y, Xu L, Heinzel T, Torchia J, Kurokawa R, Gloss B, Lin S-C, Heyman RA, Rose DW, Glass CK, Rosenfeld MG. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. of outstanding interest Cell. 85:1996;403-414 CBP, originally defined as a co-activator for the CREB family of transcription factors, is shown to modulate activities of RXR and RAR.
    • (1996) Cell , vol.85 , pp. 403-414
    • Kamei, Y.1    Xu, L.2    Heinzel, T.3    Torchia, J.4    Kurokawa, R.5    Gloss, B.6    Lin S-C7    Heyman, R.A.8    Rose, D.W.9    Glass, C.K.10    Rosenfeld, M.G.11
  • 57
    • 0027521592 scopus 로고
    • Nuclear receptors/AP-1 interactions
    • Pfahl M. Nuclear receptors/AP-1 interactions. Endocr Rev. 14:1993;651-658.
    • (1993) Endocr Rev , vol.14 , pp. 651-658
    • Pfahl, M.1
  • 58
    • 0028246161 scopus 로고
    • E1A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators
    • Arany Z, Sellers WR, Livingston DM, Eckner R. E1A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators. Cell. 77:1994;799-800.
    • (1994) Cell , vol.77 , pp. 799-800
    • Arany, Z.1    Sellers, W.R.2    Livingston, D.M.3    Eckner, R.4
  • 59
    • 0030001371 scopus 로고    scopus 로고
    • An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizers with other receptors
    • of special interest. Cloning SHP, a natural dominant negative member of the nuclear receptor superfamily. The possibility of a negative control of the function of several receptors by SHP deserves to be carefully explored.
    • Seol W, Choi HS, Moore DD. An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizers with other receptors. of special interest Science. 272:1996;1336-1339 Cloning SHP, a natural dominant negative member of the nuclear receptor superfamily. The possibility of a negative control of the function of several receptors by SHP deserves to be carefully explored.
    • (1996) Science , vol.272 , pp. 1336-1339
    • Seol, W.1    Choi, H.S.2    Moore, D.D.3
  • 60
    • 0027434083 scopus 로고
    • A human homologue of Saccharomyces cerevisiae SNF2/SW12 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor
    • Muchardt C, Yaniv M. A human homologue of Saccharomyces cerevisiae SNF2/SW12 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor. EMBO J. 12:1993;4279-4290.
    • (1993) EMBO J , vol.12 , pp. 4279-4290
    • Muchardt, C.1    Yaniv, M.2
  • 61
    • 0027048595 scopus 로고
    • Roles of SWI1, SWI2, and SWI3 proteins for trancriptional enhancement by steroid receptors
    • Yoshinaga SK, Peterson C, Herskowitz I, Yamamoto KR. Roles of SWI1, SWI2, and SWI3 proteins for trancriptional enhancement by steroid receptors. Science. 258:1992;1598-1604.
    • (1992) Science , vol.258 , pp. 1598-1604
    • Yoshinaga, S.K.1    Peterson, C.2    Herskowitz, I.3    Yamamoto, K.R.4
  • 62
    • 0028031681 scopus 로고
    • Dominant negative retinoid X receptor β inhibits retinoic acid-responsive gene regulation in embryonal carcinoma cells
    • Minucci S, Zand DJ, Dey A, Marks MS, Nagata T, Grippo JF, Ozato K. Dominant negative retinoid X receptor β inhibits retinoic acid-responsive gene regulation in embryonal carcinoma cells. Mol Cell Biol. 14:1994;360-372.
    • (1994) Mol Cell Biol , vol.14 , pp. 360-372
    • Minucci, S.1    Zand, D.J.2    Dey, A.3    Marks, M.S.4    Nagata, T.5    Grippo, J.F.6    Ozato, K.7
  • 63
    • 0028072053 scopus 로고
    • Ligand-dependent occupancy of the retinoic acid receptor-β2 promoter in vivo
    • Dey A, Minucci S, Ozato K. Ligand-dependent occupancy of the retinoic acid receptor-β2 promoter in vivo. Mol Cell Biol. 12:1994;3590-3599.
    • (1994) Mol Cell Biol , vol.12 , pp. 3590-3599
    • Dey, A.1    Minucci, S.2    Ozato, K.3
  • 64
    • 0030072614 scopus 로고    scopus 로고
    • Inhibition of ligand-induced promoter occupancy in vivo by a dominant negative RXR
    • of special interest. In this report, stably transfected P19 cell clones expressing a mutated RXR that lacks the AF-2 region are shown to be defective in ligand-induced in vivo occupancy of the RARβ2 promoter, suggesting that the AF-2 region of RXR plays a role in receptor - DNA interactions in vivo.
    • Blanco JC, Dey A, Leid M, Minucci S, Park BK, Jurutka P, Haussler M, Ozato K. Inhibition of ligand-induced promoter occupancy in vivo by a dominant negative RXR. of special interest From Genes to Cell. 1:1996;209-221 In this report, stably transfected P19 cell clones expressing a mutated RXR that lacks the AF-2 region are shown to be defective in ligand-induced in vivo occupancy of the RARβ2 promoter, suggesting that the AF-2 region of RXR plays a role in receptor - DNA interactions in vivo.
    • (1996) From Genes to Cell , vol.1 , pp. 209-221
    • Blanco, J.C.1    Dey, A.2    Leid, M.3    Minucci, S.4    Park, B.K.5    Jurutka, P.6    Haussler, M.7    Ozato, K.8
  • 65
    • 0030059509 scopus 로고    scopus 로고
    • Retinoic acid-mediated down-regulation of in vivo
    • of special interest. Genomic footprinting analysis of the Oct3/4 promoter, that is downregulated by retinoids in embryonal carcinoma and embryonic stem cells. In the absence of RA, when the RA is expressed, several sites crucial for expression are occupied in vivo. Upon RA addition, factors are displaced from the promoter, coinciding with the transcriptional downregulation of the gene.
    • Minucci S, Botquin V, Yeom YI, Dey A, Sylvester I, Zand DJ, Ohbo K, Ozato K, Schöler HR. Retinoic acid-mediated down-regulation of in vivo. of special interest EMBO J. 15:1996;888-899 Genomic footprinting analysis of the Oct3/4 promoter, that is downregulated by retinoids in embryonal carcinoma and embryonic stem cells. In the absence of RA, when the RA is expressed, several sites crucial for expression are occupied in vivo. Upon RA addition, factors are displaced from the promoter, coinciding with the transcriptional downregulation of the gene.
    • (1996) EMBO J , vol.15 , pp. 888-899
    • Minucci, S.1    Botquin, V.2    Yeom, Y.I.3    Dey, A.4    Sylvester, I.5    Zand, D.J.6    Ohbo, K.7    Ozato, K.8    Schöler, H.R.9
  • 66
    • 0029044997 scopus 로고
    • Structural repeats
    • of outstanding interest. A report detailing the X-ray structure of the DBDs of RXR and TR bound to a DR4 response element. The DBDs are assembled in a polar way, with the RXR DBD occupying the 5' half-site.
    • Restinejad F, Perlmann T, Evans RM, Sigler PB. Structural repeats. of outstanding interest Nature. 375:1995;203-211 A report detailing the X-ray structure of the DBDs of RXR and TR bound to a DR4 response element. The DBDs are assembled in a polar way, with the RXR DBD occupying the 5' half-site.
    • (1995) Nature , vol.375 , pp. 203-211
    • Restinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.