메뉴 건너뛰기




Volumn 3, Issue 1, 1996, Pages 87-94

A canonical structure for the ligandbinding domain of nuclear receptors

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; GLUCOCORTICOID RECEPTOR;

EID: 0030056997     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0196-87     Document Type: Article
Times cited : (695)

References (27)
  • 1
    • 0345208432 scopus 로고
    • Nuclear Receptors
    • Academic Press, in the press
    • Gronemeyer, H. & Laudet, V. Nuclear Receptors. Protein Profile 2, (Academic Press, 1995), in the press.
    • (1995) Protein Profile , vol.2
    • Gronemeyer, H.1    Laudet, V.2
  • 2
    • 0023797380 scopus 로고
    • Nuclear receptors enhance our understanding of transcription regulation
    • Green, S. & Chambon, P. Nuclear receptors enhance our understanding of transcription regulation. Trends Genet. 4, 309-314 (1983).
    • (1983) Trends Genet. , vol.4 , pp. 309-314
    • Green, S.1    Chambon, P.2
  • 3
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans, R.M. The steroid and thyroid hormone receptor superfamily. Science 240, 889-895 (1988).
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 4
    • 0026343481 scopus 로고
    • Transcription activation by estrogen and progesterone receptors
    • Gronemeyer, H. Transcription activation by estrogen and progesterone receptors. A Rev. Genet 25, 89-123 (1991).
    • (1991) A Rev. Genet , vol.25 , pp. 89-123
    • Gronemeyer, H.1
  • 5
    • 0026742534 scopus 로고
    • Multiplicity generates diversity in the retinoic acid signalling pathways
    • Leid, M., P. Kastner & P. Chambon. Multiplicity generates diversity in the retinoic acid signalling pathways. Trends Biochem. Sci. 17, 427-433 (1992).
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 427-433
    • Leid, M.1    Kastner, P.2    Chambon, P.3
  • 6
    • 0028419153 scopus 로고
    • The retinoid signalling pathway: Molecular and genetic analysis
    • Chambon, P. The retinoid signalling pathway: molecular and genetic analysis. Semin. Cell Biol. 5, 115-125 (1994).
    • (1994) Semin. Cell Biol. , vol.5 , pp. 115-125
    • Chambon, P.1
  • 7
    • 0028527272 scopus 로고
    • Negative transcriptional regulation by nuclear receptors
    • Saatcioglu, F., Claret, F.X. & Karin, M. Negative transcriptional regulation by nuclear receptors. Sem. Cancer Biol. 5, 347-359 (1994).
    • (1994) Sem. Cancer Biol. , vol.5 , pp. 347-359
    • Saatcioglu, F.1    Claret, F.X.2    Karin, M.3
  • 8
    • 0028072053 scopus 로고
    • Ligand-dependent occupancy of the retinoic acid receptor beta 2 promoter in vivo
    • Dey, A., Minucci, S. & Ozato, K. Ligand-dependent occupancy of the retinoic acid receptor beta 2 promoter in vivo. Mol. cell. Biol. 14, 8191-8201 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8191-8201
    • Dey, A.1    Minucci, S.2    Ozato, K.3
  • 9
    • 0028052137 scopus 로고
    • Antiprogestins prevent progesterone receptor binding to hormone responsive elements in vivo
    • Truss, M., Bartsch, J. & Beato, M. Antiprogestins prevent progesterone receptor binding to hormone responsive elements in vivo. Proc. natn. Acad. Sci. U.S.A. 91, 11333-11337 (1994).
    • (1994) Proc. Natn. Acad. Sci. U.S.A. , vol.91 , pp. 11333-11337
    • Truss, M.1    Bartsch, J.2    Beato, M.3
  • 10
    • 0025339079 scopus 로고
    • V-erba oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA
    • Zenke, M., Munoz, A., Sap, J., Vennström, B. & Beug, H. V-erba oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA. Cell 61, 1035-1049 (1990).
    • (1990) Cell , vol.61 , pp. 1035-1049
    • Zenke, M.1    Munoz, A.2    Sap, J.3    Vennström, B.4    Beug, H.5
  • 11
    • 0026600841 scopus 로고
    • Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors
    • Danielian, P.S., White, R., Lees, J.A. & Parker, M.G. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 11, 1025-1033 (1992).
    • (1992) EMBO J. , vol.11 , pp. 1025-1033
    • Danielian, P.S.1    White, R.2    Lees, J.A.3    Parker, M.G.4
  • 12
    • 0028233763 scopus 로고
    • Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor
    • Barretino, D., Vivanco-Ruiz, M.d.M. & Stunnenberg, H.G. Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor. EMBO J. 13, 3039-3049 (1994).
    • (1994) EMBO J. , vol.13 , pp. 3039-3049
    • Barretino, D.1    Vivanco-Ruiz, M.D.M.2    Stunnenberg, H.G.3
  • 13
    • 0027941792 scopus 로고
    • Activation function 2 (AF-2) of RAR and RXR: Presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity
    • Durand, B. et al. Activation function 2 (AF-2) of RAR and RXR: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity. EMBO J. 13, 5370-5382 (1994).
    • (1994) EMBO J. , vol.13 , pp. 5370-5382
    • Durand, B.1
  • 14
    • 0028961189 scopus 로고
    • Mouse retinoid X receptor contains a separable ligand-binding and transactivation domain in its E region
    • Leng, X. et al. Mouse retinoid X receptor contains a separable ligand-binding and transactivation domain in its E region. Mol. cell. Biol. 15, 255-263 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 255-263
    • Leng, X.1
  • 15
    • 0028233383 scopus 로고
    • Oestrogen receptor-associated proteins: Possible mediators of hormone-induced transcription
    • Halachmi, S. et al. Oestrogen receptor-associated proteins: possible mediators of hormone-induced transcription. Science 264, 1455-1458 (1994).
    • (1994) Science , vol.264 , pp. 1455-1458
    • Halachmi, S.1
  • 17
    • 0029121358 scopus 로고
    • Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor
    • Cavaillès, V. et al. Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor. EMBO J. 14, 3741-3751 (1995).
    • (1995) EMBO J. , vol.14 , pp. 3741-3751
    • Cavaillès, V.1
  • 18
    • 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
    • LeDouarin, B. et al. 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).
    • (1995) EMBO J. , vol.14 , pp. 2020-2033
    • LeDouarin, B.1
  • 19
    • 0028890361 scopus 로고
    • Interaction of thyroid-hormone receptor with a conserved transcriptional mediator
    • Lee, J.W., Ryan, F., Swaffield, J.C., Johnston, S.A., & Moore, D.A. Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. Nature 374, 91-94 (1995).
    • (1995) Nature , vol.374 , pp. 91-94
    • Lee, J.W.1    Ryan, F.2    Swaffield, J.C.3    Johnston, S.A.4    Moore, D.A.5
  • 20
    • 85088549149 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
    • in the press
    • Vom Baur, E. et al. Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1. EMBO J. in the press.
    • EMBO J.
    • Vom Baur, E.1
  • 21
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
    • Hörlein, A.J. et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 377, 397-403 (1995).
    • (1995) Nature , vol.377 , pp. 397-403
    • Hörlein, A.J.1
  • 22
    • 0029154931 scopus 로고
    • Polarity-specific activities of retinoic acid receptors determined by a co-repressor
    • Kurokawa, R. et al. Polarity-specific activities of retinoic acid receptors determined by a co-repressor. Nature 377, 451-454 (1995).
    • (1995) Nature , vol.377 , pp. 451-454
    • Kurokawa, R.1
  • 23
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen, J.D. & Evans, R.M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377, 454-457 (1995).
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 24
    • 0029046741 scopus 로고
    • How to finger DNA
    • Gronemeyer, H. & Moras, D. How to finger DNA. Nature 375, 190-191 (1995).
    • (1995) Nature , vol.375 , pp. 190-191
    • Gronemeyer, H.1    Moras, D.2
  • 25
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXRa
    • Bourguet, W., Ruff, M., Chambon, P., Gronemeyer, H. & Moras, D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXRa. Nature 375, 377-382 (1995).
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 26
    • 0029643780 scopus 로고    scopus 로고
    • D Crystal structure of the RARg ligand-binding domain bound to all-trans retinoic acid
    • in the press
    • Renaud, J.P. et al. D Crystal structure of the RARg ligand-binding domain bound to all-trans retinoic acid. Nature in the press.
    • Nature
    • Renaud, J.P.1
  • 27
    • 0026557977 scopus 로고
    • Evolution of the nuclear receptor gene superfamily
    • Laudet, V., Hanni, C., Coll, J., Catzeflis, F. & Stehelin, D. Evolution of the nuclear receptor gene superfamily. EMBO J. 11, 1003-1013 (1992).
    • (1992) EMBO J. , vol.11 , pp. 1003-1013
    • Laudet, V.1    Hanni, C.2    Coll, J.3    Catzeflis, F.4    Stehelin, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.