메뉴 건너뛰기




Volumn 395, Issue 6698, 1998, Pages 199-202

Interactions controlling the assembly of nuclear-receptor heterodimers and co-activators

Author keywords

[No Author keywords available]

Indexed keywords

PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; RETINOIC ACID RECEPTOR; RETINOIC ACID RECEPTOR ALPHA; RETINOID X RECEPTOR; UNCLASSIFIED DRUG;

EID: 0032505066     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/26040     Document Type: Article
Times cited : (308)

References (28)
  • 1
    • 0012473279 scopus 로고
    • The nuclear receptor superfamily: The second decade
    • Mangelsdorf, D. J. et al. The nuclear receptor superfamily: the second decade. Cell 83, 835-839 (1995).
    • (1995) Cell , vol.83 , pp. 835-839
    • Mangelsdorf, D.J.1
  • 2
    • 0028332036 scopus 로고
    • Differential recognition of target genes by nuclear receptor monomers, dimers and heterodimers
    • Glass, C. K. Differential recognition of target genes by nuclear receptor monomers, dimers and heterodimers. Endocrinol. Rev. 15, 1503-1519 (1994).
    • (1994) Endocrinol. Rev. , vol.15 , pp. 1503-1519
    • Glass, C.K.1
  • 3
    • 0026705751 scopus 로고
    • Convergence of 9-cis retinoic acid and peroxisome proliferator signaling pathways through heterodimer formation of their receptors
    • Kliewer, S. A., Umesono, K., Noonan, D. J., Heyman, R. A. & Evans, R. M. Convergence of 9-cis retinoic acid and peroxisome proliferator signaling pathways through heterodimer formation of their receptors. Nature 358, 771-774 (1992).
    • (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
  • 4
    • 0028122988 scopus 로고
    • Regulation of retinoid signaling by receptor polarity and allosteric control of ligand binding
    • Kurokawa, R. et al. Regulation of retinoid signaling by receptor polarity and allosteric control of ligand binding. Nature 371, 528-531 (1994).
    • (1994) Nature , vol.371 , pp. 528-531
    • Kurokawa, R.1
  • 5
    • 0029002298 scopus 로고
    • Unique response pathways are established by allosteric interactions among nuclear hormone receptors
    • Forman, B. M., Umesono, K., Chen, J. & Evans, R. M. Unique response pathways are established by allosteric interactions among nuclear hormone receptors. Cell 81, 541-550 (1995).
    • (1995) Cell , vol.81 , pp. 541-550
    • Forman, B.M.1    Umesono, K.2    Chen, J.3    Evans, R.M.4
  • 6
    • 0029781068 scopus 로고    scopus 로고
    • Two distinct actions of retinoid-receptor ligands
    • Chen, J.-Y. et al. Two distinct actions of retinoid-receptor ligands. Nature 382, 819-822 (1996).
    • (1996) Nature , vol.382 , pp. 819-822
    • Chen, J.-Y.1
  • 7
    • 0027941792 scopus 로고
    • Activation function 2 (AF2) 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 AF2 activity
    • Durand, B. et al. Activation function 2 (AF2) 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 AF2 activity. EMBO J. 13, 5370-5382 (1994).
    • (1994) EMBO J. , vol.13 , pp. 5370-5382
    • Durand, B.1
  • 8
    • 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
  • 9
    • 0028233763 scopus 로고
    • Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor
    • Barettino, D., Vivanco Ruiz, M. 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
    • Barettino, D.1    Vivanco Ruiz, M.M.2    Stunnenberg, H.G.3
  • 10
    • 0029643769 scopus 로고
    • A structural role for hormone in the thyroid hormone receptor
    • Wagner, R. L. et al. A structural role for hormone in the thyroid hormone receptor. Nature 378, 690-697 (1995).
    • (1995) Nature , vol.378 , pp. 690-697
    • Wagner, R.L.1
  • 11
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet, W., Ruffr, M., Chambon, P., Gronemeyer, H. & Moras, D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 375, 377-382 (1995).
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruffr, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 12
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
    • Renaud, J.-P. et al. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378, 681-689 (1995).
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.-P.1
  • 13
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Oñate, S. A., Tsai, S. Y., Tsai, M.-J. & O'Malley, B. W. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270, 1354-1357 (1995).
    • (1995) Science , vol.270 , pp. 1354-1357
    • Oñate, S.A.1    Tsai, S.Y.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 14
    • 0242587820 scopus 로고    scopus 로고
    • A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors
    • Kamei, Y. et al. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85, 403-414 (1996).
    • (1996) Cell , vol.85 , pp. 403-414
    • Kamei, Y.1
  • 15
    • 0029858911 scopus 로고    scopus 로고
    • p300 is a component of an estrogen receptor coactivator complex
    • Hanstein, B. et al. p300 is a component of an estrogen receptor coactivator complex. Proc. Natl Acad. Sci. USA 93, 11540-11545 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11540-11545
    • Hanstein, B.1
  • 16
    • 0029817669 scopus 로고    scopus 로고
    • Role of CBP/p300 in nuclear receptor signaling
    • Chakravarti, D. et al. Role of CBP/p300 in nuclear receptor signaling. Nature 383, 99-103 (1996).
    • (1996) Nature , vol.383 , pp. 99-103
    • Chakravarti, D.1
  • 17
    • 0030912539 scopus 로고    scopus 로고
    • The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
    • Torchia, J. et al. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387, 677-684 (1997).
    • (1997) Nature , vol.387 , pp. 677-684
    • Torchia, J.1
  • 18
    • 0032579292 scopus 로고    scopus 로고
    • Transcription factor-specific requirements for coactivators and their acetyltransferase functions
    • Korzus, E. et al. Transcription factor-specific requirements for coactivators and their acetyltransferase functions. Science 279, 703-707 (1998).
    • (1998) Science , vol.279 , pp. 703-707
    • Korzus, E.1
  • 19
    • 0032579289 scopus 로고    scopus 로고
    • Differential use of CREB binding protein-coactivator complexes
    • Kurokawa, R. et al. Differential use of CREB binding protein-coactivator complexes. Science 279, 700-703 (1998).
    • (1998) Science , vol.279 , pp. 700-703
    • Kurokawa, R.1
  • 20
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional coactivators mediates binding to nuclear receptors
    • Heery, D. M., Kalkhoven, E., Hoare, S. & Parker, M. G. A signature motif in transcriptional coactivators mediates binding to nuclear receptors. Nature 387, 733-736 (1997).
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 21
    • 0032230231 scopus 로고    scopus 로고
    • Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): Multiple motifs with different binding specificities
    • Ding, X. F. et al. Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): multiple motifs with different binding specificities. Mol. Endocrinol. 12, 302-313 (1998).
    • (1998) Mol. Endocrinol. , vol.12 , pp. 302-313
    • Ding, X.F.1
  • 22
    • 0029841744 scopus 로고    scopus 로고
    • A possible involvement of TIF1α and TIF1β in the epigenetic control of transcription by nuclear recetors
    • Le Douarin, B. et al. A possible involvement of TIF1α and TIF1β in the epigenetic control of transcription by nuclear recetors. EMBO J. 15, 6701-6715 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6701-6715
    • Le Douarin, B.1
  • 23
    • 0032518944 scopus 로고    scopus 로고
    • The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways
    • Voegel, J. J. et al. The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. EMBO J. 17, 507-519 (1998).
    • (1998) EMBO J. , vol.17 , pp. 507-519
    • Voegel, J.J.1
  • 24
    • 0032472408 scopus 로고    scopus 로고
    • Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor
    • Kalkhoven, E., Valentine, J. E., Heery, D. M. & Parker, M. G. Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 17, 232-243 (1998).
    • (1998) EMBO J. , vol.17 , pp. 232-243
    • Kalkhoven, E.1    Valentine, J.E.2    Heery, D.M.3    Parker, M.G.4
  • 25
    • 0029773871 scopus 로고    scopus 로고
    • The nuclear hormone receptor coactivator SRC-1 is a specific target of p300
    • Yao, T.-P., Ku, G., Zhou, N., Scully, R. & Livingston, D. M. The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proc. Natl Acad. Sci. USA 93, 10626-10631 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10626-10631
    • Yao, T.-P.1    Ku, G.2    Zhou, N.3    Scully, R.4    Livingston, D.M.5
  • 26
    • 0032505096 scopus 로고    scopus 로고
    • Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ
    • in the press
    • Nolte, R. T. et al. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ. Nature (in the press).
    • Nature
    • Nolte, R.T.1
  • 27
    • 0017874586 scopus 로고
    • Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a 6a-diphrenylglycoluril
    • Fraker, P. J. & Speck, J. C. J. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a 6a-diphrenylglycoluril. Biochem. Biophys. Res. Commun. 80, 849-857 (1978).
    • (1978) Biochem. Biophys. Res. Commun. , vol.80 , pp. 849-857
    • Fraker, P.J.1    Speck, J.C.J.2
  • 28
    • 0023392945 scopus 로고
    • High efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C. & Okayama, H. High efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7, 2745-2752 (1987).
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.