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Volumn 112, Issue 4-5, 2008, Pages 205-212

Ligand induced interaction of thyroid hormone receptor beta with its coregulators

Author keywords

DAX1; GC 1; Kinetics; LBD; NH 3; SRC2; Surface plasmon resonance; Thyroid hormone receptor beta

Indexed keywords

THYROID HORMONE RECEPTOR BETA;

EID: 57449113796     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2008.10.006     Document Type: Article
Times cited : (15)

References (44)
  • 1
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans R.M. The steroid and thyroid hormone receptor superfamily. Science 240 4854 (1988) 889-895
    • (1988) Science , vol.240 , Issue.4854 , pp. 889-895
    • Evans, R.M.1
  • 2
  • 5
    • 1942453725 scopus 로고    scopus 로고
    • Selective activation of thyroid hormone signaling pathways by GC-1: a new approach to controlling cholesterol and body weight
    • Baxter J.D., Webb P., Grover G., and Scanlan T.S. Selective activation of thyroid hormone signaling pathways by GC-1: a new approach to controlling cholesterol and body weight. Trends Endocrinol. Metab. 15 4 (2004) 154-157
    • (2004) Trends Endocrinol. Metab. , vol.15 , Issue.4 , pp. 154-157
    • Baxter, J.D.1    Webb, P.2    Grover, G.3    Scanlan, T.S.4
  • 15
    • 0034615669 scopus 로고    scopus 로고
    • The SRC family of nuclear receptor coactivators
    • Leo C., and Chen J.D. The SRC family of nuclear receptor coactivators. Gene 245 1 (2000) 1-11
    • (2000) Gene , vol.245 , Issue.1 , pp. 1-11
    • Leo, C.1    Chen, J.D.2
  • 16
    • 0042334873 scopus 로고    scopus 로고
    • Review of the in vivo functions of the p160 steroid receptor coactivator family
    • Xu J., and Li Q. Review of the in vivo functions of the p160 steroid receptor coactivator family. Mol. Endocrinol. 17 9 (2003) 1681-1692
    • (2003) Mol. Endocrinol. , vol.17 , Issue.9 , pp. 1681-1692
    • Xu, J.1    Li, Q.2
  • 18
    • 0028558750 scopus 로고
    • An unusual member of the nuclear hormone receptor superfamily responsible for X-linked adrenal hypoplasia congenital
    • Zanaria E., Muscatelli F., Bardoni B., Strom T.M., Guioli S., Guo W., Lalli E., Moser C., Walker A.P., and McCabe E.R. An unusual member of the nuclear hormone receptor superfamily responsible for X-linked adrenal hypoplasia congenital. Nature 372 6507 (1994) 635-641
    • (1994) Nature , vol.372 , Issue.6507 , pp. 635-641
    • Zanaria, E.1    Muscatelli, F.2    Bardoni, B.3    Strom, T.M.4    Guioli, S.5    Guo, W.6    Lalli, E.7    Moser, C.8    Walker, A.P.9    McCabe, E.R.10
  • 19
    • 0029912474 scopus 로고    scopus 로고
    • Mouse Dax1 expression is consistent with a role in sex determination as well as in adrenal and hypothalamus function
    • Swain A., Zanaria E., Hacker A., Lovell-Badge R., and Camerino G. Mouse Dax1 expression is consistent with a role in sex determination as well as in adrenal and hypothalamus function. Nat. Genet. 12 4 (1996) 404-409
    • (1996) Nat. Genet. , vol.12 , Issue.4 , pp. 404-409
    • Swain, A.1    Zanaria, E.2    Hacker, A.3    Lovell-Badge, R.4    Camerino, G.5
  • 20
    • 0035079932 scopus 로고    scopus 로고
    • Comparative localization of Dax-1 and Ad4BP/SF-1 during development of the hypothalamic-pituitary-gonadal axis suggests their closely related and distinct functions
    • Ikeda Y., Takeda Y., Shikayama T., Mukai T., Hisano S., and Morohashi K.I. Comparative localization of Dax-1 and Ad4BP/SF-1 during development of the hypothalamic-pituitary-gonadal axis suggests their closely related and distinct functions. Dev. Dyn. 220 4 (2001) 363-376
    • (2001) Dev. Dyn. , vol.220 , Issue.4 , pp. 363-376
    • Ikeda, Y.1    Takeda, Y.2    Shikayama, T.3    Mukai, T.4    Hisano, S.5    Morohashi, K.I.6
  • 21
    • 4944263717 scopus 로고    scopus 로고
    • Molecular mechanisms of DAX1 action
    • Iyer A.K., and McCabe E.R. Molecular mechanisms of DAX1 action. Mol. Genet. Metab. 83 1-2 (2004) 60-73
    • (2004) Mol. Genet. Metab. , vol.83 , Issue.1-2 , pp. 60-73
    • Iyer, A.K.1    McCabe, E.R.2
  • 22
    • 33847053927 scopus 로고    scopus 로고
    • DAX1: Increasing complexity in the roles of this novel nuclear receptor
    • McCabe E.R. DAX1: Increasing complexity in the roles of this novel nuclear receptor. Mol. Cell. Endocrinol. 265-266 (2007) 179-182
    • (2007) Mol. Cell. Endocrinol. , vol.265-266 , pp. 179-182
    • McCabe, E.R.1
  • 23
    • 26244433172 scopus 로고    scopus 로고
    • DAX1 origin, function, and novel role
    • Niakan K.K., and McCabe E.R. DAX1 origin, function, and novel role. Mol. Genet. Metab. 86 1-2 (2005) 70-83
    • (2005) Mol. Genet. Metab. , vol.86 , Issue.1-2 , pp. 70-83
    • Niakan, K.K.1    McCabe, E.R.2
  • 24
  • 25
    • 0035849586 scopus 로고    scopus 로고
    • Structure-function evaluation of ER alpha and beta interplay with SRC family coactivators. ER selective ligands
    • Wong C.W., Komm B., and Cheskis B.J. Structure-function evaluation of ER alpha and beta interplay with SRC family coactivators. ER selective ligands. Biochemistry 40 23 (2001) 6756-6765
    • (2001) Biochemistry , vol.40 , Issue.23 , pp. 6756-6765
    • Wong, C.W.1    Komm, B.2    Cheskis, B.J.3
  • 26
    • 0035968333 scopus 로고    scopus 로고
    • Differential recruitment of the mammalian mediator subunit TRAP220 by estrogen receptors ERalpha and ERbeta
    • Wärnmark A., Almlöf T., Leers J., Gustafsson J.A., and Treuter E. Differential recruitment of the mammalian mediator subunit TRAP220 by estrogen receptors ERalpha and ERbeta. J. Biol. Chem. 276 26 (2001) 23397-23404
    • (2001) J. Biol. Chem. , vol.276 , Issue.26 , pp. 23397-23404
    • Wärnmark, A.1    Almlöf, T.2    Leers, J.3    Gustafsson, J.A.4    Treuter, E.5
  • 27
    • 0037077233 scopus 로고    scopus 로고
    • Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha
    • Wärnmark A., Treuter E., Gustafsson J.A., Hubbard R.E., Brzozowski A.M., and Pike A.C. Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha. J. Biol. Chem. 277 24 (2002) 21862-21868
    • (2002) J. Biol. Chem. , vol.277 , Issue.24 , pp. 21862-21868
    • Wärnmark, A.1    Treuter, E.2    Gustafsson, J.A.3    Hubbard, R.E.4    Brzozowski, A.M.5    Pike, A.C.6
  • 28
    • 19344376991 scopus 로고    scopus 로고
    • Recognition and accommodation at the androgen receptor coactivator binding interface
    • Hur E., Pfaff S.J., Payne E.S., Gron H., Buehrer B.M., and Fletterick R.J. Recognition and accommodation at the androgen receptor coactivator binding interface. PLoS Biol. 2 9 (2004) E274
    • (2004) PLoS Biol. , vol.2 , Issue.9
    • Hur, E.1    Pfaff, S.J.2    Payne, E.S.3    Gron, H.4    Buehrer, B.M.5    Fletterick, R.J.6
  • 29
    • 20344379442 scopus 로고    scopus 로고
    • Mouse estrogen receptor beta isoforms exhibit differences in ligand selectivity and coactivator recruitment
    • Zhao C., Toresson G., Xu L., Koehler K.F., Gustafsson J.A., and Dahlman-Wright K. Mouse estrogen receptor beta isoforms exhibit differences in ligand selectivity and coactivator recruitment. Biochemistry 44 22 (2005) 7936-7944
    • (2005) Biochemistry , vol.44 , Issue.22 , pp. 7936-7944
    • Zhao, C.1    Toresson, G.2    Xu, L.3    Koehler, K.F.4    Gustafsson, J.A.5    Dahlman-Wright, K.6
  • 31
    • 0037130243 scopus 로고    scopus 로고
    • Rational design and synthesis of a novel thyroid hormone antagonist that blocks coactivator recruitment
    • Nguyen N.H., Apriletti J.W., Cunha Lima S.T., Webb P., Baxter J.D., and Scanlan T.S. Rational design and synthesis of a novel thyroid hormone antagonist that blocks coactivator recruitment. J. Med. Chem. 45 15 (2002) 3310-3320
    • (2002) J. Med. Chem. , vol.45 , Issue.15 , pp. 3310-3320
    • Nguyen, N.H.1    Apriletti, J.W.2    Cunha Lima, S.T.3    Webb, P.4    Baxter, J.D.5    Scanlan, T.S.6
  • 32
    • 0031014046 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • Myszka D.G. Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Curr. Opin. Biotechnol 8 1 (1997) 50-57
    • (1997) Curr. Opin. Biotechnol , vol.8 , Issue.1 , pp. 50-57
    • Myszka, D.G.1
  • 33
    • 0037144443 scopus 로고    scopus 로고
    • A thyroid hormone antagonist that inhibits thyroid hormone action in vivo
    • Lim W., Nguyen N.H., Yang H.Y., Scanlan T.S., and Furlow J.D. A thyroid hormone antagonist that inhibits thyroid hormone action in vivo. J. Biol. Chem. 277 38 (2002) 35664-35670
    • (2002) J. Biol. Chem. , vol.277 , Issue.38 , pp. 35664-35670
    • Lim, W.1    Nguyen, N.H.2    Yang, H.Y.3    Scanlan, T.S.4    Furlow, J.D.5
  • 34
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • Myszka D.G. Improving biosensor analysis. J. Mol. Recognit. 12 5 (1999) 279-284
    • (1999) J. Mol. Recognit. , vol.12 , Issue.5 , pp. 279-284
    • Myszka, D.G.1
  • 35
    • 0034426852 scopus 로고    scopus 로고
    • Experimental design for analysis of complex kinetics using surface plasmon resonance
    • Lipschultz C.A., Li Y., and Smith-Gill S. Experimental design for analysis of complex kinetics using surface plasmon resonance. Methods 20 3 (2000) 310-318
    • (2000) Methods , vol.20 , Issue.3 , pp. 310-318
    • Lipschultz, C.A.1    Li, Y.2    Smith-Gill, S.3
  • 36
    • 0342813129 scopus 로고    scopus 로고
    • Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors
    • Karlsson R., and Fält A. Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 200 1-2 (1997) 121-133
    • (1997) J. Immunol. Methods , vol.200 , Issue.1-2 , pp. 121-133
    • Karlsson, R.1    Fält, A.2
  • 39
    • 33745966042 scopus 로고    scopus 로고
    • A functionally orthogonal ligand-receptor pair created by targeting the allosteric mechanism of the thyroid hormone receptor
    • Hassan A.Q., and Koh J.T. A functionally orthogonal ligand-receptor pair created by targeting the allosteric mechanism of the thyroid hormone receptor. J. Am. Chem. Soc. 128 27 (2006) 8868-8874
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.27 , pp. 8868-8874
    • Hassan, A.Q.1    Koh, J.T.2
  • 41
    • 34547107881 scopus 로고    scopus 로고
    • Ajulemic acid, a synthetic nonpsychoactive cannabinoid acid, bound to the ligand binding domain of the human peroxisome proliferator-activated receptor gamma
    • Ambrosio A.L., Dias S.M., Polikarpov I., Zurier R.B., Burstein S.H., and Garratt R.C. Ajulemic acid, a synthetic nonpsychoactive cannabinoid acid, bound to the ligand binding domain of the human peroxisome proliferator-activated receptor gamma. J. Biol. Chem. 282 25 (2007) 18625-18633
    • (2007) J. Biol. Chem. , vol.282 , Issue.25 , pp. 18625-18633
    • Ambrosio, A.L.1    Dias, S.M.2    Polikarpov, I.3    Zurier, R.B.4    Burstein, S.H.5    Garratt, R.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.